data_4765 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H,13C, and 15N resonance assignments of an 18.2kDa protein, E.Coli peptidyl-prolyl cis-trans isomerase b (EPPIb) ; _BMRB_accession_number 4765 _BMRB_flat_file_name bmr4765.str _Entry_type original _Submission_date 2000-06-19 _Accession_date 2000-06-19 _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 Kainosho Masatsune . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 160 "13C chemical shifts" 474 "15N chemical shifts" 159 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-09-27 original author . stop_ _Original_release_date 2000-09-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments of an 18.2 kDa protein, E. coli peptidyl-prolyl cis-trans isomerase b (EPPIb) ; _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 Kariya Eri . . 2 Ohki Shin-ya . . 3 Hayano Toshiya . . 4 Kainosho Masatsune . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 18 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 75 _Page_last 76 _Year 2000 _Details . loop_ _Keyword 'cell-free protein synthesis' 'chemical shifts' 'peptidyl-prolyl cis-trans isomerase' stop_ save_ ################################## # Molecular system description # ################################## save_system_EPPIb _Saveframe_category molecular_system _Mol_system_name 'E.Coli peptidyl-prolyl cis-trans isomerase b' _Abbreviation_common EPPIb _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EPPIb $EPPIb stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EPPIb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E.Coli peptidyl-prolyl cis-trans isomerase b' _Abbreviation_common EPPIb _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 164 _Mol_residue_sequence ; MVTFHTNHGDIVIKTFDDKA PETVKNFLDYCREGFYNNTI FHRVINGFMIQGGGFEPGMK QKATKEPIKNEANNGLKNTR GTLAMARTQAPHSATAQFFI NVVDNDFLNFSGESLQGWGY CVFAEVVDGMDVVDKIKGVA TGRSGMHQDVPKEDVIIESV TVSE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 VAL 3 THR 4 PHE 5 HIS 6 THR 7 ASN 8 HIS 9 GLY 10 ASP 11 ILE 12 VAL 13 ILE 14 LYS 15 THR 16 PHE 17 ASP 18 ASP 19 LYS 20 ALA 21 PRO 22 GLU 23 THR 24 VAL 25 LYS 26 ASN 27 PHE 28 LEU 29 ASP 30 TYR 31 CYS 32 ARG 33 GLU 34 GLY 35 PHE 36 TYR 37 ASN 38 ASN 39 THR 40 ILE 41 PHE 42 HIS 43 ARG 44 VAL 45 ILE 46 ASN 47 GLY 48 PHE 49 MET 50 ILE 51 GLN 52 GLY 53 GLY 54 GLY 55 PHE 56 GLU 57 PRO 58 GLY 59 MET 60 LYS 61 GLN 62 LYS 63 ALA 64 THR 65 LYS 66 GLU 67 PRO 68 ILE 69 LYS 70 ASN 71 GLU 72 ALA 73 ASN 74 ASN 75 GLY 76 LEU 77 LYS 78 ASN 79 THR 80 ARG 81 GLY 82 THR 83 LEU 84 ALA 85 MET 86 ALA 87 ARG 88 THR 89 GLN 90 ALA 91 PRO 92 HIS 93 SER 94 ALA 95 THR 96 ALA 97 GLN 98 PHE 99 PHE 100 ILE 101 ASN 102 VAL 103 VAL 104 ASP 105 ASN 106 ASP 107 PHE 108 LEU 109 ASN 110 PHE 111 SER 112 GLY 113 GLU 114 SER 115 LEU 116 GLN 117 GLY 118 TRP 119 GLY 120 TYR 121 CYS 122 VAL 123 PHE 124 ALA 125 GLU 126 VAL 127 VAL 128 ASP 129 GLY 130 MET 131 ASP 132 VAL 133 VAL 134 ASP 135 LYS 136 ILE 137 LYS 138 GLY 139 VAL 140 ALA 141 THR 142 GLY 143 ARG 144 SER 145 GLY 146 MET 147 HIS 148 GLN 149 ASP 150 VAL 151 PRO 152 LYS 153 GLU 154 ASP 155 VAL 156 ILE 157 ILE 158 GLU 159 SER 160 VAL 161 THR 162 VAL 163 SER 164 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1LOP "Cyclophilin A Complexed With Succinyl-Ala-Pro-Ala-P-Nitroanilide" 100.00 164 99.39 99.39 3.06e-116 PDB 2NUL "Peptidylprolyl Isomerase From E. Coli" 100.00 164 100.00 100.00 2.79e-117 PDB 2RS4 "Nmr Strucure Of Stereo-array Isotope Labelled (sail) Peptidyl-prolyl Cis-trans Isomerase From E. Coli (eppib)" 100.00 164 100.00 100.00 2.79e-117 DBJ BAB34010 "peptidyl-prolyl cis-trans isomerase B [Escherichia coli O157:H7 str. Sakai]" 100.00 164 99.39 100.00 1.21e-116 DBJ BAE76302 "peptidyl-prolyl cis-trans isomerase B [Escherichia coli str. K-12 substr. W3110]" 100.00 164 100.00 100.00 2.79e-117 DBJ BAG76074 "peptidyl-prolyl cis-trans isomerase B [Escherichia coli SE11]" 100.00 164 100.00 100.00 2.79e-117 DBJ BAI23892 "peptidyl-prolyl cis-trans isomerase B [Escherichia coli O26:H11 str. 11368]" 100.00 164 99.39 100.00 1.21e-116 DBJ BAI29364 "peptidyl-prolyl cis-trans isomerase B [Escherichia coli O103:H2 str. 12009]" 100.00 164 99.39 100.00 1.21e-116 EMBL CAD05020 "peptidyl-prolyl cis-trans isomerase B [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 164 97.56 98.78 1.93e-114 EMBL CAP75055 "Peptidyl-prolyl cis-trans isomerase B [Escherichia coli LF82]" 100.00 164 99.39 100.00 1.21e-116 EMBL CAQ30997 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Escherichia coli BL21(DE3)]" 100.00 164 100.00 100.00 2.79e-117 EMBL CAQ88114 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Escherichia fergusonii ATCC 35469]" 100.00 164 99.39 100.00 1.21e-116 EMBL CAQ97399 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Escherichia coli IAI1]" 100.00 164 99.39 100.00 1.21e-116 GB AAA23453 "peptidyl-prolyl cis-trans isomerase b [Escherichia coli]" 100.00 164 99.39 99.39 3.06e-116 GB AAC73627 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Escherichia coli str. K-12 substr. MG1655]" 100.00 164 100.00 100.00 2.79e-117 GB AAG54882 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Escherichia coli O157:H7 str. EDL933]" 100.00 164 99.39 100.00 1.21e-116 GB AAL19490 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 164 97.56 98.78 1.93e-114 GB AAN42110 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Shigella flexneri 2a str. 301]" 100.00 164 99.39 100.00 1.68e-116 PIR AB0569 "peptidyl-prolyl cis-trans isomerase B [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 164 97.56 98.78 1.93e-114 REF NP_286274 "peptidyl-prolyl cis-trans isomerase B [Escherichia coli O157:H7 str. EDL933]" 100.00 164 99.39 100.00 1.21e-116 REF NP_308614 "peptidyl-prolyl cis-trans isomerase B [Escherichia coli O157:H7 str. Sakai]" 100.00 164 99.39 100.00 1.21e-116 REF NP_415058 "peptidyl-prolyl cis-trans isomerase B (rotamase B) [Escherichia coli str. K-12 substr. MG1655]" 100.00 164 100.00 100.00 2.79e-117 REF NP_455128 "peptidyl-prolyl cis-trans isomerase B [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 164 97.56 98.78 1.93e-114 REF NP_459531 "peptidyl-prolyl cis-trans isomerase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 164 97.56 98.78 1.93e-114 SP P23869 "RecName: Full=Peptidyl-prolyl cis-trans isomerase B; Short=PPIase B; AltName: Full=Rotamase B [Escherichia coli K-12]" 100.00 164 100.00 100.00 2.79e-117 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EPPIb 'E. coli' 562 Eubacteria . Escherichia coli 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 $EPPIb 'cell free synthesis' . . . . . 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 _Isotopic_labeling $EPPIb 1.6 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EPPIb 1.6 mM [U-15N] stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EPPIb 1.6 mM '[U-13C; U-15N]' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details 'selectively labeled' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EPPIb 1.6 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500.13 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600.13 _Details . save_ save_NMR_spectrometer3s _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800.13 _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 0.1 n/a temperature 308 0.1 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 H 1 'methyl protons' ppm 0.0 . direct . . . . DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name EPPIb _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET C C 170.79 . 1 2 . 1 MET CA C 53.54 . 1 3 . 1 MET CB C 32.55 . 1 4 . 2 VAL N N 124.91 . 1 5 . 2 VAL H H 9.09 . 1 6 . 2 VAL C C 172.51 . 1 7 . 2 VAL CA C 59.78 . 1 8 . 2 VAL CB C 34.12 . 1 9 . 3 THR N N 123.12 . 1 10 . 3 THR H H 9.04 . 1 11 . 3 THR C C 172.98 . 1 12 . 3 THR CA C 59.88 . 1 13 . 3 THR CB C 69.09 . 1 14 . 4 PHE N N 127.17 . 1 15 . 4 PHE H H 9.59 . 1 16 . 4 PHE C C 172.92 . 1 17 . 4 PHE CA C 52.70 . 1 18 . 4 PHE CB C 37.79 . 1 19 . 5 HIS N N 126.30 . 1 20 . 5 HIS H H 9.05 . 1 21 . 5 HIS C C 173.28 . 1 22 . 5 HIS CA C 52.91 . 1 23 . 5 HIS CB C 25.52 . 1 24 . 6 THR N N 117.15 . 1 25 . 6 THR H H 8.03 . 1 26 . 6 THR C C 174.99 . 1 27 . 6 THR CA C 58.89 . 1 28 . 6 THR CB C 71.22 . 1 29 . 7 ASN N N 120.60 . 1 30 . 7 ASN H H 9.43 . 1 31 . 7 ASN C C 173.54 . 1 32 . 7 ASN CA C 53.18 . 1 33 . 7 ASN CB C 34.24 . 1 34 . 8 HIS N N 119.44 . 1 35 . 8 HIS H H 8.80 . 1 36 . 8 HIS C C 172.03 . 1 37 . 8 HIS CA C 55.39 . 1 38 . 8 HIS CB C 31.04 . 1 39 . 9 GLY N N 109.80 . 1 40 . 9 GLY H H 7.44 . 1 41 . 9 GLY C C 173.83 . 1 42 . 9 GLY CA C 42.47 . 1 43 . 10 ASP N N 125.02 . 1 44 . 10 ASP H H 8.96 . 1 45 . 10 ASP C C 174.24 . 1 46 . 10 ASP CA C 53.02 . 1 47 . 10 ASP CB C 40.43 . 1 48 . 11 ILE N N 122.12 . 1 49 . 11 ILE H H 8.75 . 1 50 . 11 ILE C C 172.62 . 1 51 . 11 ILE CA C 59.95 . 1 52 . 11 ILE CB C 40.39 . 1 53 . 12 VAL N N 130.74 . 1 54 . 12 VAL H H 8.90 . 1 55 . 12 VAL C C 174.36 . 1 56 . 12 VAL CA C 60.99 . 1 57 . 12 VAL CB C 31.27 . 1 58 . 13 ILE N N 128.92 . 1 59 . 13 ILE H H 9.64 . 1 60 . 13 ILE C C 172.39 . 1 61 . 13 ILE CA C 58.40 . 1 62 . 13 ILE CB C 40.38 . 1 63 . 14 LYS N N 127.77 . 1 64 . 14 LYS H H 8.81 . 1 65 . 14 LYS C C 174.05 . 1 66 . 14 LYS CA C 52.60 . 1 67 . 14 LYS CB C 34.65 . 1 68 . 15 THR N N 114.94 . 1 69 . 15 THR H H 8.43 . 1 70 . 15 THR C C 173.80 . 1 71 . 15 THR CA C 58.48 . 1 72 . 15 THR CB C 68.16 . 1 73 . 16 PHE N N 123.77 . 1 74 . 16 PHE H H 8.42 . 1 75 . 16 PHE C C 175.37 . 1 76 . 16 PHE CA C 51.99 . 1 77 . 16 PHE CB C 35.31 . 1 78 . 17 ASP N N 121.41 . 1 79 . 17 ASP H H 9.23 . 1 80 . 17 ASP C C 174.98 . 1 81 . 17 ASP CA C 56.69 . 1 82 . 17 ASP CB C 37.86 . 1 83 . 18 ASP N N 112.73 . 1 84 . 18 ASP H H 8.73 . 1 85 . 18 ASP C C 176.01 . 1 86 . 18 ASP CA C 53.51 . 1 87 . 18 ASP CB C 38.44 . 1 88 . 19 LYS N N 119.12 . 1 89 . 19 LYS H H 7.45 . 1 90 . 19 LYS C C 175.63 . 1 91 . 19 LYS CA C 54.00 . 1 92 . 19 LYS CB C 32.91 . 1 93 . 20 ALA N N 124.84 . 1 94 . 20 ALA H H 7.67 . 1 95 . 20 ALA CA C 48.89 . 1 96 . 20 ALA CB C 17.33 . 1 97 . 21 PRO C C 179.91 . 1 98 . 21 PRO CA C 65.02 . 1 99 . 21 PRO CB C 30.46 . 1 100 . 22 GLU N N 123.72 . 1 101 . 22 GLU H H 9.97 . 1 102 . 22 GLU C C 178.66 . 1 103 . 22 GLU CA C 58.18 . 1 104 . 22 GLU CB C 27.36 . 1 105 . 23 THR N N 123.31 . 1 106 . 23 THR H H 9.55 . 1 107 . 23 THR C C 177.13 . 1 108 . 23 THR CA C 65.25 . 1 109 . 24 VAL N N 126.16 . 1 110 . 24 VAL H H 9.47 . 1 111 . 24 VAL C C 175.35 . 1 112 . 24 VAL CA C 67.00 . 1 113 . 24 VAL CB C 29.76 . 1 114 . 25 LYS N N 122.22 . 1 115 . 25 LYS H H 7.81 . 1 116 . 25 LYS C C 176.36 . 1 117 . 25 LYS CA C 58.97 . 1 118 . 25 LYS CB C 30.65 . 1 119 . 26 ASN N N 117.61 . 1 120 . 26 ASN H H 7.67 . 1 121 . 26 ASN C C 174.35 . 1 122 . 26 ASN CA C 55.26 . 1 123 . 26 ASN CB C 39.59 . 1 124 . 27 PHE N N 120.97 . 1 125 . 27 PHE H H 8.01 . 1 126 . 27 PHE C C 176.87 . 1 127 . 27 PHE CA C 59.64 . 1 128 . 27 PHE CB C 38.98 . 1 129 . 28 LEU N N 121.93 . 1 130 . 28 LEU H H 9.49 . 1 131 . 28 LEU C C 178.01 . 1 132 . 28 LEU CA C 56.64 . 1 133 . 28 LEU CB C 40.32 . 1 134 . 29 ASP N N 122.80 . 1 135 . 29 ASP H H 8.50 . 1 136 . 29 ASP C C 177.29 . 1 137 . 29 ASP CA C 56.53 . 1 138 . 29 ASP CB C 37.74 . 1 139 . 30 TYR N N 120.24 . 1 140 . 30 TYR H H 7.43 . 1 141 . 30 TYR C C 178.02 . 1 142 . 30 TYR CA C 60.48 . 1 143 . 30 TYR CB C 36.72 . 1 144 . 31 CYS N N 117.44 . 1 145 . 31 CYS H H 8.45 . 1 146 . 31 CYS C C 178.60 . 1 147 . 31 CYS CA C 63.11 . 1 148 . 31 CYS CB C 26.11 . 1 149 . 32 ARG N N 123.00 . 1 150 . 32 ARG H H 9.19 . 1 151 . 32 ARG C C 176.78 . 1 152 . 32 ARG CA C 58.41 . 1 153 . 32 ARG CB C 29.44 . 1 154 . 33 GLU N N 117.86 . 1 155 . 33 GLU H H 8.03 . 1 156 . 33 GLU C C 175.73 . 1 157 . 33 GLU CA C 55.16 . 1 158 . 33 GLU CB C 28.27 . 1 159 . 34 GLY N N 108.54 . 1 160 . 34 GLY H H 7.66 . 1 161 . 34 GLY C C 174.80 . 1 162 . 34 GLY CA C 44.27 . 1 163 . 35 PHE N N 123.35 . 1 164 . 35 PHE H H 8.23 . 1 165 . 35 PHE C C 174.81 . 1 166 . 35 PHE CA C 60.29 . 1 167 . 35 PHE CB C 39.24 . 1 168 . 36 TYR N N 112.46 . 1 169 . 36 TYR H H 7.46 . 1 170 . 36 TYR C C 174.89 . 1 171 . 36 TYR CA C 56.35 . 1 172 . 36 TYR CB C 36.53 . 1 173 . 37 ASN N N 123.04 . 1 174 . 37 ASN H H 7.23 . 1 175 . 37 ASN C C 174.58 . 1 176 . 37 ASN CA C 52.87 . 1 177 . 37 ASN CB C 34.75 . 1 178 . 38 ASN N N 122.57 . 1 179 . 38 ASN H H 9.33 . 1 180 . 38 ASN C C 172.74 . 1 181 . 38 ASN CA C 53.14 . 1 182 . 38 ASN CB C 37.17 . 1 183 . 39 THR N N 105.74 . 1 184 . 39 THR H H 7.45 . 1 185 . 39 THR C C 173.28 . 1 186 . 39 THR CA C 58.66 . 1 187 . 39 THR CB C 71.56 . 1 188 . 40 ILE N N 109.99 . 1 189 . 40 ILE H H 8.07 . 1 190 . 40 ILE C C 178.66 . 1 191 . 40 ILE CA C 57.54 . 1 192 . 40 ILE CB C 38.73 . 1 193 . 41 PHE N N 123.22 . 1 194 . 41 PHE H H 8.39 . 1 195 . 41 PHE C C 173.93 . 1 196 . 41 PHE CA C 57.55 . 1 197 . 41 PHE CB C 36.38 . 1 198 . 42 HIS N N 122.78 . 1 199 . 42 HIS H H 7.99 . 1 200 . 42 HIS C C 171.81 . 1 201 . 42 HIS CA C 55.36 . 1 202 . 42 HIS CB C 30.59 . 1 203 . 43 ARG N N 124.39 . 1 204 . 43 ARG H H 7.07 . 1 205 . 43 ARG C C 172.10 . 1 206 . 43 ARG CA C 53.92 . 1 207 . 43 ARG CB C 31.03 . 1 208 . 44 VAL N N 130.48 . 1 209 . 44 VAL H H 9.13 . 1 210 . 44 VAL C C 171.84 . 1 211 . 44 VAL CA C 61.07 . 1 212 . 44 VAL CB C 33.99 . 1 213 . 45 ILE N N 127.63 . 1 214 . 45 ILE H H 8.37 . 1 215 . 45 ILE C C 173.57 . 1 216 . 45 ILE CA C 59.15 . 1 217 . 45 ILE CB C 38.81 . 1 218 . 46 ASN N N 129.21 . 1 219 . 46 ASN H H 9.24 . 1 220 . 46 ASN C C 176.30 . 1 221 . 46 ASN CA C 53.06 . 1 222 . 46 ASN CB C 35.63 . 1 223 . 47 GLY N N 111.53 . 1 224 . 47 GLY H H 7.64 . 1 225 . 47 GLY C C 171.78 . 1 226 . 47 GLY CA C 44.51 . 1 227 . 48 PHE N N 117.75 . 1 228 . 48 PHE H H 7.92 . 1 229 . 48 PHE C C 172.61 . 1 230 . 48 PHE CA C 56.21 . 1 231 . 48 PHE CB C 37.39 . 1 232 . 49 MET N N 118.83 . 1 233 . 49 MET H H 8.47 . 1 234 . 49 MET C C 171.61 . 1 235 . 49 MET CA C 53.73 . 1 236 . 49 MET CB C 34.04 . 1 237 . 50 ILE N N 112.19 . 1 238 . 50 ILE H H 7.87 . 1 239 . 50 ILE C C 171.59 . 1 240 . 50 ILE CA C 58.53 . 1 241 . 50 ILE CB C 39.33 . 1 242 . 51 GLN N N 129.21 . 1 243 . 51 GLN H H 9.34 . 1 244 . 51 GLN C C 173.16 . 1 245 . 51 GLN CA C 52.83 . 1 246 . 51 GLN CB C 30.72 . 1 247 . 52 GLY N N 112.71 . 1 248 . 52 GLY H H 8.17 . 1 249 . 52 GLY C C 171.29 . 1 250 . 52 GLY CA C 44.21 . 1 251 . 53 GLY N N 107.44 . 1 252 . 53 GLY H H 8.49 . 1 253 . 53 GLY C C 170.35 . 1 254 . 53 GLY CA C 45.01 . 1 255 . 54 GLY N N 102.31 . 1 256 . 54 GLY H H 9.21 . 1 257 . 54 GLY C C 171.57 . 1 258 . 54 GLY CA C 43.35 . 1 259 . 55 PHE N N 122.41 . 1 260 . 55 PHE H H 9.43 . 1 261 . 55 PHE C C 173.45 . 1 262 . 55 PHE CA C 55.37 . 1 263 . 55 PHE CB C 40.86 . 1 264 . 56 GLU N N 121.41 . 1 265 . 56 GLU H H 8.67 . 1 266 . 56 GLU CA C 52.90 . 1 267 . 56 GLU CB C 28.35 . 1 268 . 57 PRO C C 174.99 . 1 269 . 57 PRO CA C 63.59 . 1 270 . 57 PRO CB C 29.96 . 1 271 . 58 GLY N N 114.59 . 1 272 . 58 GLY H H 9.54 . 1 273 . 58 GLY C C 173.87 . 1 274 . 58 GLY CA C 43.25 . 1 275 . 59 MET N N 115.24 . 1 276 . 59 MET H H 8.16 . 1 277 . 59 MET C C 173.82 . 1 278 . 59 MET CA C 53.41 . 1 279 . 59 MET CB C 24.86 . 1 280 . 60 LYS N N 121.74 . 1 281 . 60 LYS H H 7.11 . 1 282 . 60 LYS C C 174.41 . 1 283 . 60 LYS CA C 53.75 . 1 284 . 60 LYS CB C 31.40 . 1 285 . 61 GLN N N 131.23 . 1 286 . 61 GLN H H 9.04 . 1 287 . 61 GLN C C 174.61 . 1 288 . 61 GLN CA C 55.52 . 1 289 . 61 GLN CB C 27.51 . 1 290 . 62 LYS N N 127.33 . 1 291 . 62 LYS H H 7.44 . 1 292 . 62 LYS C C 175.27 . 1 293 . 62 LYS CA C 55.42 . 1 294 . 62 LYS CB C 31.96 . 1 295 . 63 ALA N N 128.87 . 1 296 . 63 ALA H H 8.56 . 1 297 . 63 ALA C C 176.36 . 1 298 . 63 ALA CA C 51.39 . 1 299 . 63 ALA CB C 17.42 . 1 300 . 64 THR N N 112.40 . 1 301 . 64 THR H H 8.20 . 1 302 . 64 THR C C 173.96 . 1 303 . 64 THR CA C 59.22 . 1 304 . 64 THR CB C 70.32 . 1 305 . 65 LYS N N 119.65 . 1 306 . 65 LYS H H 7.99 . 1 307 . 65 LYS C C 174.62 . 1 308 . 65 LYS CA C 54.07 . 1 309 . 65 LYS CB C 31.31 . 1 310 . 66 GLU N N 120.02 . 1 311 . 66 GLU H H 7.97 . 1 312 . 66 GLU CA C 54.45 . 1 313 . 66 GLU CB C 27.29 . 1 314 . 67 PRO C C 175.72 . 1 315 . 67 PRO CA C 60.82 . 1 316 . 67 PRO CB C 31.77 . 1 317 . 68 ILE N N 113.76 . 1 318 . 68 ILE H H 8.33 . 1 319 . 68 ILE C C 174.29 . 1 320 . 68 ILE CA C 57.67 . 1 321 . 68 ILE CB C 40.30 . 1 322 . 69 LYS N N 122.43 . 1 323 . 69 LYS H H 7.96 . 1 324 . 69 LYS C C 174.84 . 1 325 . 69 LYS CA C 53.79 . 1 326 . 69 LYS CB C 31.21 . 1 327 . 70 ASN N N 127.50 . 1 328 . 70 ASN H H 10.88 . 1 329 . 70 ASN C C 175.01 . 1 330 . 70 ASN CA C 51.98 . 1 331 . 70 ASN CB C 36.01 . 1 332 . 71 GLU N N 127.44 . 1 333 . 71 GLU H H 8.31 . 1 334 . 71 GLU C C 175.68 . 1 335 . 71 GLU CA C 54.20 . 1 336 . 71 GLU CB C 28.79 . 1 337 . 72 ALA N N 121.87 . 1 338 . 72 ALA H H 9.23 . 1 339 . 72 ALA C C 175.81 . 1 340 . 72 ALA CA C 53.92 . 1 341 . 72 ALA CB C 17.50 . 1 342 . 73 ASN N N 115.88 . 1 343 . 73 ASN H H 8.03 . 1 344 . 73 ASN C C 173.54 . 1 345 . 73 ASN CA C 51.03 . 1 346 . 73 ASN CB C 33.39 . 1 347 . 74 ASN N N 120.86 . 1 348 . 74 ASN H H 8.51 . 1 349 . 74 ASN C C 175.22 . 1 350 . 74 ASN CA C 51.39 . 1 351 . 74 ASN CB C 37.29 . 1 352 . 75 GLY N N 110.00 . 1 353 . 75 GLY H H 8.11 . 1 354 . 75 GLY C C 173.28 . 1 355 . 75 GLY CA C 44.48 . 1 356 . 76 LEU N N 121.78 . 1 357 . 76 LEU H H 7.84 . 1 358 . 76 LEU C C 175.97 . 1 359 . 76 LEU CA C 53.22 . 1 360 . 76 LEU CB C 40.13 . 1 361 . 77 LYS N N 123.01 . 1 362 . 77 LYS H H 8.25 . 1 363 . 77 LYS C C 175.42 . 1 364 . 77 LYS CA C 53.74 . 1 365 . 77 LYS CB C 33.78 . 1 366 . 78 ASN N N 125.87 . 1 367 . 78 ASN H H 9.66 . 1 368 . 78 ASN C C 174.41 . 1 369 . 78 ASN CA C 52.98 . 1 370 . 78 ASN CB C 35.94 . 1 371 . 79 THR N N 116.19 . 1 372 . 79 THR H H 8.31 . 1 373 . 79 THR C C 174.46 . 1 374 . 79 THR CA C 59.46 . 1 375 . 79 THR CB C 69.07 . 1 376 . 80 ARG N N 125.30 . 1 377 . 80 ARG H H 9.32 . 1 378 . 80 ARG C C 175.32 . 1 379 . 80 ARG CA C 56.95 . 1 380 . 80 ARG CB C 28.03 . 1 381 . 81 GLY N N 116.80 . 1 382 . 81 GLY H H 9.09 . 1 383 . 81 GLY C C 172.23 . 1 384 . 81 GLY CA C 43.91 . 1 385 . 82 THR N N 111.50 . 1 386 . 82 THR H H 8.19 . 1 387 . 82 THR C C 172.15 . 1 388 . 82 THR CA C 60.35 . 1 389 . 82 THR CB C 71.03 . 1 390 . 83 LEU N N 122.47 . 1 391 . 83 LEU H H 8.03 . 1 392 . 83 LEU C C 172.82 . 1 393 . 83 LEU CA C 53.02 . 1 394 . 83 LEU CB C 42.60 . 1 395 . 84 ALA N N 123.02 . 1 396 . 84 ALA H H 8.18 . 1 397 . 84 ALA C C 176.30 . 1 398 . 84 ALA CA C 47.84 . 1 399 . 84 ALA CB C 23.08 . 1 400 . 85 MET N N 116.61 . 1 401 . 85 MET H H 7.67 . 1 402 . 85 MET C C 176.88 . 1 403 . 85 MET CA C 51.33 . 1 404 . 85 MET CB C 28.73 . 1 405 . 86 ALA N N 127.70 . 1 406 . 86 ALA H H 8.41 . 1 407 . 86 ALA C C 174.68 . 1 408 . 86 ALA CA C 50.04 . 1 409 . 86 ALA CB C 18.41 . 1 410 . 87 ARG N N 114.74 . 1 411 . 87 ARG H H 8.11 . 1 412 . 87 ARG C C 174.88 . 1 413 . 87 ARG CA C 54.38 . 1 414 . 87 ARG CB C 28.68 . 1 415 . 88 THR N N 112.76 . 1 416 . 88 THR H H 8.03 . 1 417 . 88 THR C C 172.16 . 1 418 . 88 THR CA C 59.28 . 1 419 . 88 THR CB C 67.11 . 1 420 . 89 GLN N N 118.58 . 1 421 . 89 GLN H H 8.30 . 1 422 . 89 GLN C C 175.43 . 1 423 . 89 GLN CA C 57.55 . 1 424 . 89 GLN CB C 27.21 . 1 425 . 90 ALA N N 124.13 . 1 426 . 90 ALA H H 8.04 . 1 427 . 90 ALA CA C 48.25 . 1 428 . 90 ALA CB C 16.08 . 1 429 . 91 PRO C C 176.21 . 1 430 . 91 PRO CA C 64.02 . 1 431 . 91 PRO CB C 28.86 . 1 432 . 92 HIS N N 119.61 . 1 433 . 92 HIS H H 8.07 . 1 434 . 92 HIS C C 173.78 . 1 435 . 92 HIS CA C 52.96 . 1 436 . 92 HIS CB C 27.27 . 1 437 . 93 SER N N 109.56 . 1 438 . 93 SER H H 6.50 . 1 439 . 93 SER C C 174.22 . 1 440 . 93 SER CA C 56.41 . 1 441 . 93 SER CB C 64.95 . 1 442 . 94 ALA N N 131.23 . 1 443 . 94 ALA H H 8.65 . 1 444 . 94 ALA C C 174.76 . 1 445 . 94 ALA CA C 52.90 . 1 446 . 94 ALA CB C 19.41 . 1 447 . 95 THR N N 111.93 . 1 448 . 95 THR H H 9.02 . 1 449 . 95 THR C C 171.07 . 1 450 . 95 THR CA C 58.44 . 1 451 . 95 THR CB C 68.76 . 1 452 . 96 ALA N N 122.81 . 1 453 . 96 ALA H H 8.06 . 1 454 . 96 ALA C C 177.72 . 1 455 . 96 ALA CA C 50.16 . 1 456 . 96 ALA CB C 22.30 . 1 457 . 97 GLN N N 116.69 . 1 458 . 97 GLN H H 7.96 . 1 459 . 97 GLN C C 173.90 . 1 460 . 97 GLN CA C 56.17 . 1 461 . 97 GLN CB C 29.76 . 1 462 . 98 PHE N N 118.96 . 1 463 . 98 PHE H H 7.76 . 1 464 . 98 PHE C C 171.06 . 1 465 . 98 PHE CA C 53.34 . 1 466 . 98 PHE CB C 42.27 . 1 467 . 99 PHE N N 117.55 . 1 468 . 99 PHE H H 9.64 . 1 469 . 99 PHE C C 171.47 . 1 470 . 99 PHE CA C 53.71 . 1 471 . 99 PHE CB C 42.87 . 1 472 . 100 ILE N N 118.98 . 1 473 . 100 ILE H H 9.25 . 1 474 . 100 ILE C C 175.89 . 1 475 . 100 ILE CA C 58.03 . 1 476 . 100 ILE CB C 38.54 . 1 477 . 101 ASN N N 127.73 . 1 478 . 101 ASN H H 9.00 . 1 479 . 101 ASN C C 175.47 . 1 480 . 101 ASN CA C 54.39 . 1 481 . 101 ASN CB C 38.60 . 1 482 . 102 VAL N N 118.93 . 1 483 . 102 VAL H H 7.80 . 1 484 . 102 VAL C C 172.79 . 1 485 . 102 VAL CA C 60.65 . 1 486 . 102 VAL CB C 29.56 . 1 487 . 103 VAL N N 117.64 . 1 488 . 103 VAL H H 7.87 . 1 489 . 103 VAL C C 171.80 . 1 490 . 103 VAL CA C 58.06 . 1 491 . 103 VAL CB C 34.43 . 1 492 . 104 ASP N N 119.79 . 1 493 . 104 ASP H H 8.27 . 1 494 . 104 ASP C C 173.78 . 1 495 . 104 ASP CA C 53.69 . 1 496 . 104 ASP CB C 38.05 . 1 497 . 105 ASN N N 129.37 . 1 498 . 105 ASN H H 8.47 . 1 499 . 105 ASN C C 173.75 . 1 500 . 105 ASN CA C 50.18 . 1 501 . 105 ASN CB C 37.99 . 1 502 . 106 ASP N N 122.74 . 1 503 . 106 ASP H H 8.31 . 1 504 . 106 ASP C C 176.67 . 1 505 . 106 ASP CA C 55.51 . 1 506 . 106 ASP CB C 38.64 . 1 507 . 107 PHE N N 115.71 . 1 508 . 107 PHE H H 7.49 . 1 509 . 107 PHE C C 174.58 . 1 510 . 107 PHE CA C 55.96 . 1 511 . 107 PHE CB C 35.76 . 1 512 . 108 LEU N N 122.67 . 1 513 . 108 LEU H H 7.30 . 1 514 . 108 LEU C C 174.31 . 1 515 . 108 LEU CA C 53.20 . 1 516 . 108 LEU CB C 41.11 . 1 517 . 109 ASN N N 117.30 . 1 518 . 109 ASN H H 7.43 . 1 519 . 109 ASN C C 175.32 . 1 520 . 109 ASN CA C 51.46 . 1 521 . 109 ASN CB C 37.11 . 1 522 . 110 PHE N N 125.19 . 1 523 . 110 PHE H H 8.91 . 1 524 . 110 PHE C C 174.77 . 1 525 . 110 PHE CA C 57.79 . 1 526 . 110 PHE CB C 38.86 . 1 527 . 111 SER N N 123.33 . 1 528 . 111 SER H H 9.51 . 1 529 . 111 SER C C 172.14 . 1 530 . 111 SER CA C 56.19 . 1 531 . 111 SER CB C 63.62 . 1 532 . 112 GLY N N 111.63 . 1 533 . 112 GLY H H 5.66 . 1 534 . 112 GLY C C 169.60 . 1 535 . 112 GLY CA C 44.24 . 1 536 . 113 GLU N N 120.08 . 1 537 . 113 GLU H H 7.97 . 1 538 . 113 GLU C C 173.75 . 1 539 . 113 GLU CA C 53.82 . 1 540 . 113 GLU CB C 25.72 . 1 541 . 114 SER N N 120.31 . 1 542 . 114 SER H H 7.76 . 1 543 . 114 SER C C 172.89 . 1 544 . 114 SER CA C 55.02 . 1 545 . 114 SER CB C 64.35 . 1 546 . 115 LEU N N 123.44 . 1 547 . 115 LEU H H 8.85 . 1 548 . 115 LEU C C 178.12 . 1 549 . 115 LEU CA C 57.60 . 1 550 . 115 LEU CB C 40.20 . 1 551 . 116 GLN N N 115.76 . 1 552 . 116 GLN H H 8.40 . 1 553 . 116 GLN C C 176.08 . 1 554 . 116 GLN CA C 55.85 . 1 555 . 116 GLN CB C 27.11 . 1 556 . 117 GLY N N 110.82 . 1 557 . 117 GLY H H 7.95 . 1 558 . 117 GLY C C 174.76 . 1 559 . 117 GLY CA C 44.44 . 1 560 . 118 TRP N N 124.78 . 1 561 . 118 TRP H H 7.90 . 1 562 . 118 TRP C C 175.47 . 1 563 . 118 TRP CA C 60.90 . 1 564 . 118 TRP CB C 29.22 . 1 565 . 119 GLY H H 7.56 . 1 566 . 119 GLY C C 173.04 . 1 567 . 119 GLY CA C 44.20 . 1 568 . 120 TYR N N 120.95 . 1 569 . 120 TYR H H 8.39 . 1 570 . 120 TYR C C 174.21 . 1 571 . 120 TYR CA C 56.07 . 1 572 . 120 TYR CB C 38.81 . 1 573 . 121 CYS N N 127.18 . 1 574 . 121 CYS H H 9.91 . 1 575 . 121 CYS C C 172.40 . 1 576 . 121 CYS CA C 58.27 . 1 577 . 121 CYS CB C 26.97 . 1 578 . 122 VAL N N 136.29 . 1 579 . 122 VAL H H 9.49 . 1 580 . 122 VAL C C 174.36 . 1 581 . 122 VAL CA C 61.34 . 1 582 . 122 VAL CB C 30.43 . 1 583 . 123 PHE N N 119.65 . 1 584 . 123 PHE H H 7.96 . 1 585 . 123 PHE C C 171.06 . 1 586 . 123 PHE CA C 53.74 . 1 587 . 123 PHE CB C 40.80 . 1 588 . 124 ALA N N 125.71 . 1 589 . 124 ALA H H 7.46 . 1 590 . 124 ALA C C 173.10 . 1 591 . 124 ALA CA C 49.40 . 1 592 . 124 ALA CB C 21.76 . 1 593 . 125 GLU N N 116.45 . 1 594 . 125 GLU H H 8.35 . 1 595 . 125 GLU C C 172.48 . 1 596 . 125 GLU CA C 53.35 . 1 597 . 125 GLU CB C 31.72 . 1 598 . 126 VAL N N 124.54 . 1 599 . 126 VAL H H 8.89 . 1 600 . 126 VAL C C 175.29 . 1 601 . 126 VAL CA C 61.96 . 1 602 . 126 VAL CB C 30.72 . 1 603 . 127 VAL N N 124.76 . 1 604 . 127 VAL H H 9.20 . 1 605 . 127 VAL C C 174.30 . 1 606 . 127 VAL CA C 60.20 . 1 607 . 127 VAL CB C 31.43 . 1 608 . 128 ASP N N 122.31 . 1 609 . 128 ASP H H 7.85 . 1 610 . 128 ASP C C 173.70 . 1 611 . 128 ASP CA C 53.08 . 1 612 . 128 ASP CB C 41.98 . 1 613 . 129 GLY N N 112.10 . 1 614 . 129 GLY H H 8.42 . 1 615 . 129 GLY C C 175.95 . 1 616 . 129 GLY CA C 44.64 . 1 617 . 130 MET N N 124.14 . 1 618 . 130 MET H H 9.04 . 1 619 . 130 MET C C 176.76 . 1 620 . 130 MET CA C 54.88 . 1 621 . 130 MET CB C 27.67 . 1 622 . 131 ASP N N 118.41 . 1 623 . 131 ASP H H 9.04 . 1 624 . 131 ASP C C 177.44 . 1 625 . 131 ASP CA C 55.35 . 1 626 . 131 ASP CB C 37.61 . 1 627 . 132 VAL N N 125.28 . 1 628 . 132 VAL H H 7.35 . 1 629 . 132 VAL C C 177.08 . 1 630 . 132 VAL CA C 64.74 . 1 631 . 132 VAL CB C 29.84 . 1 632 . 133 VAL N N 123.03 . 1 633 . 133 VAL H H 7.49 . 1 634 . 133 VAL C C 175.78 . 1 635 . 133 VAL CA C 65.81 . 1 636 . 133 VAL CB C 29.70 . 1 637 . 134 ASP N N 118.78 . 1 638 . 134 ASP H H 8.53 . 1 639 . 134 ASP C C 176.60 . 1 640 . 134 ASP CA C 55.00 . 1 641 . 134 ASP CB C 38.81 . 1 642 . 135 LYS N N 123.79 . 1 643 . 135 LYS H H 7.56 . 1 644 . 135 LYS C C 178.04 . 1 645 . 135 LYS CA C 57.65 . 1 646 . 135 LYS CB C 31.09 . 1 647 . 136 ILE N N 122.79 . 1 648 . 136 ILE H H 8.20 . 1 649 . 136 ILE C C 175.70 . 1 650 . 136 ILE CA C 63.91 . 1 651 . 136 ILE CB C 36.16 . 1 652 . 137 LYS N N 114.81 . 1 653 . 137 LYS H H 8.09 . 1 654 . 137 LYS C C 173.52 . 1 655 . 137 LYS CA C 56.58 . 1 656 . 137 LYS CB C 30.45 . 1 657 . 138 GLY N N 106.02 . 1 658 . 138 GLY H H 6.99 . 1 659 . 138 GLY C C 174.21 . 1 660 . 138 GLY CA C 43.08 . 1 661 . 139 VAL N N 117.27 . 1 662 . 139 VAL H H 7.35 . 1 663 . 139 VAL C C 174.18 . 1 664 . 139 VAL CA C 60.48 . 1 665 . 139 VAL CB C 31.70 . 1 666 . 140 ALA N N 124.46 . 1 667 . 140 ALA H H 8.36 . 1 668 . 140 ALA C C 178.21 . 1 669 . 140 ALA CA C 51.60 . 1 670 . 140 ALA CB C 17.45 . 1 671 . 141 THR N N 114.31 . 1 672 . 141 THR H H 8.39 . 1 673 . 141 THR C C 172.91 . 1 674 . 141 THR CA C 57.91 . 1 675 . 141 THR CB C 72.12 . 1 676 . 142 GLY N N 108.60 . 1 677 . 142 GLY H H 8.61 . 1 678 . 142 GLY C C 170.10 . 1 679 . 142 GLY CA C 44.06 . 1 680 . 143 ARG N N 121.25 . 1 681 . 143 ARG H H 8.27 . 1 682 . 143 ARG C C 175.99 . 1 683 . 143 ARG CA C 53.91 . 1 684 . 143 ARG CB C 30.35 . 1 685 . 144 SER N N 120.62 . 1 686 . 144 SER H H 8.52 . 1 687 . 144 SER C C 173.35 . 1 688 . 144 SER CA C 55.56 . 1 689 . 144 SER CB C 62.20 . 1 690 . 145 GLY N N 118.90 . 1 691 . 145 GLY H H 8.98 . 1 692 . 145 GLY C C 173.83 . 1 693 . 145 GLY CA C 45.57 . 1 694 . 146 MET N N 126.74 . 1 695 . 146 MET H H 8.89 . 1 696 . 146 MET C C 174.30 . 1 697 . 146 MET CA C 54.17 . 1 698 . 146 MET CB C 30.50 . 1 699 . 147 HIS N N 122.48 . 1 700 . 147 HIS H H 8.11 . 1 701 . 147 HIS C C 173.22 . 1 702 . 147 HIS CA C 54.74 . 1 703 . 147 HIS CB C 30.42 . 1 704 . 148 GLN N N 122.57 . 1 705 . 148 GLN H H 8.77 . 1 706 . 148 GLN C C 173.70 . 1 707 . 148 GLN CA C 53.16 . 1 708 . 148 GLN CB C 30.31 . 1 709 . 149 ASP N N 118.38 . 1 710 . 149 ASP H H 8.73 . 1 711 . 149 ASP C C 172.07 . 1 712 . 149 ASP CA C 54.85 . 1 713 . 149 ASP CB C 38.65 . 1 714 . 150 VAL N N 121.49 . 1 715 . 150 VAL H H 8.56 . 1 716 . 150 VAL CA C 57.88 . 1 717 . 150 VAL CB C 32.03 . 1 718 . 151 PRO C C 175.43 . 1 719 . 151 PRO CA C 62.65 . 1 720 . 151 PRO CB C 31.29 . 1 721 . 152 LYS N N 126.76 . 1 722 . 152 LYS H H 8.30 . 1 723 . 152 LYS C C 175.62 . 1 724 . 152 LYS CA C 57.38 . 1 725 . 152 LYS CB C 30.97 . 1 726 . 153 GLU N N 120.23 . 1 727 . 153 GLU H H 8.04 . 1 728 . 153 GLU C C 174.00 . 1 729 . 153 GLU CA C 52.94 . 1 730 . 153 GLU CB C 29.71 . 1 731 . 154 ASP N N 123.00 . 1 732 . 154 ASP H H 8.28 . 1 733 . 154 ASP C C 175.47 . 1 734 . 154 ASP CA C 54.77 . 1 735 . 154 ASP CB C 39.79 . 1 736 . 155 VAL N N 130.79 . 1 737 . 155 VAL H H 10.14 . 1 738 . 155 VAL C C 173.55 . 1 739 . 155 VAL CA C 61.00 . 1 740 . 155 VAL CB C 30.68 . 1 741 . 156 ILE N N 126.90 . 1 742 . 156 ILE H H 8.37 . 1 743 . 156 ILE C C 175.26 . 1 744 . 156 ILE CA C 59.35 . 1 745 . 156 ILE CB C 41.84 . 1 746 . 157 ILE N N 127.70 . 1 747 . 157 ILE H H 9.29 . 1 748 . 157 ILE C C 173.10 . 1 749 . 157 ILE CA C 61.19 . 1 750 . 157 ILE CB C 34.99 . 1 751 . 158 GLU N N 131.26 . 1 752 . 158 GLU H H 9.07 . 1 753 . 158 GLU C C 176.06 . 1 754 . 158 GLU CA C 57.55 . 1 755 . 158 GLU CB C 28.93 . 1 756 . 159 SER N N 109.17 . 1 757 . 159 SER H H 7.88 . 1 758 . 159 SER C C 170.74 . 1 759 . 159 SER CA C 56.21 . 1 760 . 159 SER CB C 63.48 . 1 761 . 160 VAL N N 121.12 . 1 762 . 160 VAL H H 7.81 . 1 763 . 160 VAL C C 174.53 . 1 764 . 160 VAL CA C 59.28 . 1 765 . 160 VAL CB C 33.89 . 1 766 . 161 THR N N 123.57 . 1 767 . 161 THR H H 8.92 . 1 768 . 161 THR C C 172.19 . 1 769 . 161 THR CA C 59.97 . 1 770 . 161 THR CB C 69.95 . 1 771 . 162 VAL N N 130.25 . 1 772 . 162 VAL H H 9.17 . 1 773 . 162 VAL C C 173.83 . 1 774 . 162 VAL CA C 60.40 . 1 775 . 162 VAL CB C 31.56 . 1 776 . 163 SER N N 125.16 . 1 777 . 163 SER H H 8.83 . 1 778 . 163 SER C C 171.92 . 1 779 . 163 SER CA C 56.21 . 1 780 . 163 SER CB C 63.45 . 1 781 . 164 GLU N N 130.21 . 1 782 . 164 GLU H H 8.33 . 1 783 . 164 GLU CA C 56.89 . 1 784 . 164 GLU CB C 29.49 . 1 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details 'potential minor peaks' loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name EPPIb _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 . 163 SER N N 125.50 . . 2 . 163 SER H H 8.75 . . 3 . 163 SER C C 171.92 . . 4 . 163 SER CA C 57.12 . . 5 . 163 SER CB C 62.41 . . 6 . 164 GLU N N 130.32 . . 7 . 164 GLU H H 8.14 . . 8 . 164 GLU CA C 56.54 . . 9 . 164 GLU CB C 29.66 . . stop_ save_