data_6451 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C resonance assigment of the chaperone CesT from enteropathogenic Escherichia coli ; _BMRB_accession_number 6451 _BMRB_flat_file_name bmr6451.str _Entry_type original _Submission_date 2004-12-31 _Accession_date 2004-12-31 _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 Rumpel Sigrun . . 2 Kim Hai-Young . . 3 Vijayan Vinesh . . 4 Becker Stefan . . 5 Zweckstetter Markus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 148 "13C chemical shifts" 452 "15N chemical shifts" 148 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-26 original author . stop_ _Original_release_date 2005-07-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone resonance assigment of the homodimeric, 35 kDa chaperone CesT from enteropathogenic Escherichia coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15929012 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rumpel Sigrun . . 2 Kim Hai-Young . . 3 Vijayan Vinesh . . 4 Becker Stefan . . 5 Zweckstetter Markus . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 377 _Page_last 378 _Year 2005 _Details . loop_ _Keyword chaperone Mars 'NMR assignment' 'type three secretion system' stop_ save_ ################################## # Molecular system description # ################################## save_system_CesT _Saveframe_category molecular_system _Mol_system_name 'CesT dimer' _Abbreviation_common CesT _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CesT subunit 1' $CesT 'CesT subunit 2' $CesT stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'CesT subunit 1' 1 'CesT subunit 2' stop_ loop_ _Biological_function 'chaperone for the type III secretion of Map' 'chaperone for the type III secretion of Tir' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CesT _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'chaperone for the enteropathogenic E. coli secreted protein Tir' _Abbreviation_common CesT _Molecular_mass 15431 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 158 _Mol_residue_sequence ; GHMSSRSELLLDRFAEKIGV GSISFNENRLCSFAIDEIYY ISLSDANDEYMMIYGVCGKF PTDNPNFALEILNANLWFAE NGGPYLCYESGAQSLLLALR FPLDDATPEKLENEIEVVVK SMENLYLVLHNQGITLENEH MKIEEISSSDNKHYYAGR ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 SER 5 SER 6 ARG 7 SER 8 GLU 9 LEU 10 LEU 11 LEU 12 ASP 13 ARG 14 PHE 15 ALA 16 GLU 17 LYS 18 ILE 19 GLY 20 VAL 21 GLY 22 SER 23 ILE 24 SER 25 PHE 26 ASN 27 GLU 28 ASN 29 ARG 30 LEU 31 CYS 32 SER 33 PHE 34 ALA 35 ILE 36 ASP 37 GLU 38 ILE 39 TYR 40 TYR 41 ILE 42 SER 43 LEU 44 SER 45 ASP 46 ALA 47 ASN 48 ASP 49 GLU 50 TYR 51 MET 52 MET 53 ILE 54 TYR 55 GLY 56 VAL 57 CYS 58 GLY 59 LYS 60 PHE 61 PRO 62 THR 63 ASP 64 ASN 65 PRO 66 ASN 67 PHE 68 ALA 69 LEU 70 GLU 71 ILE 72 LEU 73 ASN 74 ALA 75 ASN 76 LEU 77 TRP 78 PHE 79 ALA 80 GLU 81 ASN 82 GLY 83 GLY 84 PRO 85 TYR 86 LEU 87 CYS 88 TYR 89 GLU 90 SER 91 GLY 92 ALA 93 GLN 94 SER 95 LEU 96 LEU 97 LEU 98 ALA 99 LEU 100 ARG 101 PHE 102 PRO 103 LEU 104 ASP 105 ASP 106 ALA 107 THR 108 PRO 109 GLU 110 LYS 111 LEU 112 GLU 113 ASN 114 GLU 115 ILE 116 GLU 117 VAL 118 VAL 119 VAL 120 LYS 121 SER 122 MET 123 GLU 124 ASN 125 LEU 126 TYR 127 LEU 128 VAL 129 LEU 130 HIS 131 ASN 132 GLN 133 GLY 134 ILE 135 THR 136 LEU 137 GLU 138 ASN 139 GLU 140 HIS 141 MET 142 LYS 143 ILE 144 GLU 145 GLU 146 ILE 147 SER 148 SER 149 SER 150 ASP 151 ASN 152 LYS 153 HIS 154 TYR 155 TYR 156 ALA 157 GLY 158 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 DBJ BAE80445 "CesT [Escherichia coli O127:H6]" 98.73 156 100.00 100.00 4.91e-109 DBJ BAE80446 "CesT [Escherichia coli O119:UT]" 98.73 156 100.00 100.00 4.91e-109 DBJ BAE80447 "CesT [Escherichia coli O157:H45]" 98.73 156 99.36 99.36 3.62e-108 DBJ BAE80448 "CesT [Escherichia coli O55:H6]" 98.73 156 99.36 99.36 3.62e-108 DBJ BAE80449 "CesT [Escherichia coli O153:H21]" 98.73 156 99.36 100.00 2.12e-108 EMBL CAA11066 "Hypothetical protein [Escherichia coli]" 98.73 156 99.36 100.00 8.02e-109 EMBL CAC81870 "CesT protein [Escherichia coli]" 98.73 156 99.36 100.00 8.02e-109 EMBL CAG17537 "CesT protein [Escherichia coli]" 98.73 156 100.00 100.00 4.91e-109 EMBL CAI43866 "CesT protein [Escherichia coli]" 98.73 156 99.36 100.00 8.02e-109 EMBL CAR47989 "CesT protein [Escherichia coli]" 98.73 156 99.36 100.00 8.02e-109 GB AAA62774 "ORF; putative [Escherichia coli]" 98.73 156 100.00 100.00 4.91e-109 GB AAB02942 "hypothetical 17.7kDa protein; similar to the hypothetical 17.7kDa proteins of EPEC and REPEC (84/110/1) and the hypothetical 17" 98.73 156 99.36 100.00 8.02e-109 GB AAB36673 "OrfU [Escherichia coli]" 98.73 156 99.36 100.00 8.02e-109 GB AAB39867 "unknown [Escherichia coli]" 98.73 156 99.36 100.00 8.02e-109 GB AAC32029 "unknown [Escherichia coli]" 98.73 156 98.72 100.00 7.29e-108 REF WP_000098785 "Tir chaperone [Escherichia coli]" 98.73 156 98.72 99.36 1.81e-107 REF WP_000098786 "MULTISPECIES: Tir chaperone [Escherichia]" 98.73 156 99.36 100.00 8.02e-109 REF WP_000098787 "Tir chaperone [Escherichia coli]" 98.73 156 98.72 99.36 1.13e-107 REF WP_000098788 "Tir chaperone [Escherichia coli]" 98.73 156 98.72 100.00 7.29e-108 REF WP_000098789 "Tir chaperone [Escherichia coli]" 98.73 156 98.72 100.00 7.29e-108 SP O30999 "RecName: Full=Tir chaperone [Escherichia coli O111:H-]" 98.73 156 99.36 100.00 2.12e-108 SP P21244 "RecName: Full=Tir chaperone [Escherichia coli O127:H6 str. E2348/69]" 98.73 156 100.00 100.00 4.91e-109 SP Q47015 "RecName: Full=Tir chaperone [Escherichia coli]" 98.73 156 98.72 100.00 7.29e-108 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Details $CesT 'E. coli' 562 Eubacteria . Escherichia coli 0181-6/86 'enteropathogenic E. 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_type _Vector_name $CesT 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET16b 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 $CesT . mM 0.5 1.5 '[U-95% 13C; U-90% 15N; 75% 2H]' K3PO4 50 mM . . . NaCl 100 mM . . . d-DTT 1 mM . . . EDTA 0.5 mM . . . D20 10 % . . . H20 90 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CesT . mM 0.5 1.5 '[U-95% 13C; U-90% 15N]' K3PO4 50 mM . . . NaCl 100 mM . . . d-DTT 1 mM . . . EDTA 0.5 mM . . . D20 10 % . . . H20 90 % . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 700 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 900 _Details . save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.15 0.02 M pH 6.8 0.2 n/a temperature 303 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 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_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CesT subunit 1' _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 . 3 MET CA C 54.70 0.2 1 2 . 3 MET C C 175.9 0.2 1 3 . 3 MET CB C 31.88 0.2 1 4 . 4 SER H H 8.363 0.02 1 5 . 4 SER N N 118.8 0.2 1 6 . 4 SER CA C 58.40 0.2 1 7 . 4 SER C C 174.1 0.2 1 8 . 4 SER CB C 63.33 0.2 1 9 . 5 SER H H 8.661 0.02 1 10 . 5 SER N N 120.0 0.2 1 11 . 5 SER CA C 57.25 0.2 1 12 . 5 SER C C 175.1 0.2 1 13 . 5 SER CB C 63.94 0.2 1 14 . 6 ARG H H 8.774 0.02 1 15 . 6 ARG N N 121.9 0.2 1 16 . 6 ARG CA C 59.42 0.2 1 17 . 6 ARG C C 179.5 0.2 1 18 . 6 ARG CB C 29.53 0.2 1 19 . 7 SER H H 8.514 0.02 1 20 . 7 SER N N 116.3 0.2 1 21 . 7 SER CA C 61.16 0.2 1 22 . 7 SER C C 176.0 0.2 1 23 . 7 SER CB C 61.98 0.2 1 24 . 8 GLU H H 7.654 0.02 1 25 . 8 GLU N N 123.3 0.2 1 26 . 8 GLU CA C 59.31 0.2 1 27 . 8 GLU C C 179.0 0.2 1 28 . 8 GLU CB C 28.54 0.2 1 29 . 9 LEU H H 8.017 0.02 1 30 . 9 LEU N N 119.9 0.2 1 31 . 9 LEU CA C 57.31 0.2 1 32 . 9 LEU C C 179.6 0.2 1 33 . 9 LEU CB C 40.94 0.2 1 34 . 10 LEU H H 7.586 0.02 1 35 . 10 LEU N N 119.7 0.2 1 36 . 10 LEU CA C 57.39 0.2 1 37 . 10 LEU C C 178.4 0.2 1 38 . 10 LEU CB C 40.79 0.2 1 39 . 11 LEU H H 8.120 0.02 1 40 . 11 LEU N N 119.6 0.2 1 41 . 11 LEU CA C 57.52 0.2 1 42 . 11 LEU C C 178.3 0.2 1 43 . 11 LEU CB C 40.48 0.2 1 44 . 12 ASP H H 7.925 0.02 1 45 . 12 ASP N N 118.7 0.2 1 46 . 12 ASP CA C 57.20 0.2 1 47 . 12 ASP C C 179.3 0.2 1 48 . 12 ASP CB C 40.15 0.2 1 49 . 13 ARG H H 7.749 0.02 1 50 . 13 ARG N N 118.0 0.2 1 51 . 13 ARG CA C 57.84 0.2 1 52 . 13 ARG C C 179.6 0.2 1 53 . 13 ARG CB C 29.62 0.2 1 54 . 14 PHE H H 8.676 0.02 1 55 . 14 PHE N N 122.9 0.2 1 56 . 14 PHE CA C 60.65 0.2 1 57 . 14 PHE C C 175.5 0.2 1 58 . 14 PHE CB C 39.05 0.2 1 59 . 15 ALA H H 8.753 0.02 1 60 . 15 ALA N N 121.6 0.2 1 61 . 15 ALA CA C 54.45 0.2 1 62 . 15 ALA C C 180.0 0.2 1 63 . 15 ALA CB C 17.24 0.2 1 64 . 16 GLU H H 7.333 0.02 1 65 . 16 GLU N N 116.2 0.2 1 66 . 16 GLU CA C 58.10 0.2 1 67 . 16 GLU C C 178.7 0.2 1 68 . 16 GLU CB C 28.48 0.2 1 69 . 17 LYS H H 7.476 0.02 1 70 . 17 LYS N N 120.2 0.2 1 71 . 17 LYS CA C 58.27 0.2 1 72 . 17 LYS C C 178.8 0.2 1 73 . 17 LYS CB C 31.17 0.2 1 74 . 18 ILE H H 7.372 0.02 1 75 . 18 ILE N N 110.7 0.2 1 76 . 18 ILE CA C 61.24 0.2 1 77 . 18 ILE C C 177.0 0.2 1 78 . 18 ILE CB C 37.12 0.2 1 79 . 19 GLY H H 7.455 0.02 1 80 . 19 GLY N N 110.1 0.2 1 81 . 19 GLY CA C 46.32 0.2 1 82 . 19 GLY C C 175.2 0.2 1 83 . 20 VAL H H 7.315 0.02 1 84 . 20 VAL N N 114.9 0.2 1 85 . 20 VAL CA C 60.52 0.2 1 86 . 20 VAL C C 175.5 0.2 1 87 . 20 VAL CB C 31.68 0.2 1 88 . 21 GLY H H 8.019 0.02 1 89 . 21 GLY N N 110.8 0.2 1 90 . 21 GLY CA C 44.66 0.2 1 91 . 21 GLY C C 173.3 0.2 1 92 . 22 SER H H 7.836 0.02 1 93 . 22 SER N N 114.2 0.2 1 94 . 22 SER CA C 57.77 0.2 1 95 . 22 SER C C 174.1 0.2 1 96 . 22 SER CB C 62.69 0.2 1 97 . 23 ILE H H 8.006 0.02 1 98 . 23 ILE N N 122.9 0.2 1 99 . 23 ILE CA C 60.05 0.2 1 100 . 23 ILE C C 173.9 0.2 1 101 . 23 ILE CB C 39.32 0.2 1 102 . 24 SER H H 7.931 0.02 1 103 . 24 SER N N 116.1 0.2 1 104 . 24 SER CA C 56.54 0.2 1 105 . 24 SER C C 173.7 0.2 1 106 . 24 SER CB C 64.79 0.2 1 107 . 25 PHE H H 8.700 0.02 1 108 . 25 PHE N N 120.8 0.2 1 109 . 25 PHE CA C 58.74 0.2 1 110 . 25 PHE C C 176.6 0.2 1 111 . 25 PHE CB C 39.40 0.2 1 112 . 26 ASN H H 8.714 0.02 1 113 . 26 ASN N N 121.6 0.2 1 114 . 26 ASN CA C 50.94 0.2 1 115 . 26 ASN C C 177.6 0.2 1 116 . 26 ASN CB C 38.34 0.2 1 117 . 27 GLU H H 9.217 0.02 1 118 . 27 GLU N N 118.9 0.2 1 119 . 27 GLU CA C 58.73 0.2 1 120 . 27 GLU C C 177.0 0.2 1 121 . 27 GLU CB C 27.87 0.2 1 122 . 28 ASN H H 7.806 0.02 1 123 . 28 ASN N N 117.5 0.2 1 124 . 28 ASN CA C 52.48 0.2 1 125 . 28 ASN C C 173.7 0.2 1 126 . 28 ASN CB C 38.30 0.2 1 127 . 29 ARG H H 8.385 0.02 1 128 . 29 ARG N N 112.8 0.2 1 129 . 29 ARG CA C 55.31 0.2 1 130 . 29 ARG C C 173.5 0.2 1 131 . 29 ARG CB C 23.42 0.2 1 132 . 30 LEU H H 7.779 0.02 1 133 . 30 LEU N N 118.3 0.2 1 134 . 30 LEU CA C 53.49 0.2 1 135 . 30 LEU C C 177.3 0.2 1 136 . 30 LEU CB C 45.43 0.2 1 137 . 31 CYS H H 9.147 0.02 1 138 . 31 CYS N N 123.0 0.2 1 139 . 31 CYS CA C 57.27 0.2 1 140 . 31 CYS C C 173.3 0.2 1 141 . 31 CYS CB C 29.62 0.2 1 142 . 32 SER H H 8.513 0.02 1 143 . 32 SER N N 120.4 0.2 1 144 . 32 SER CA C 57.23 0.2 1 145 . 32 SER C C 172.7 0.2 1 146 . 32 SER CB C 65.27 0.2 1 147 . 33 PHE H H 8.716 0.02 1 148 . 33 PHE N N 120.4 0.2 1 149 . 33 PHE CA C 55.83 0.2 1 150 . 33 PHE C C 171.7 0.2 1 151 . 33 PHE CB C 39.41 0.2 1 152 . 34 ALA H H 8.342 0.02 1 153 . 34 ALA N N 120.8 0.2 1 154 . 34 ALA CA C 49.70 0.2 1 155 . 34 ALA C C 177.3 0.2 1 156 . 34 ALA CB C 19.63 0.2 1 157 . 35 ILE H H 9.163 0.02 1 158 . 35 ILE N N 124.7 0.2 1 159 . 35 ILE CA C 58.62 0.2 1 160 . 35 ILE C C 175.4 0.2 1 161 . 35 ILE CB C 37.52 0.2 1 162 . 36 ASP H H 9.136 0.02 1 163 . 36 ASP N N 126.4 0.2 1 164 . 36 ASP CA C 55.20 0.2 1 165 . 36 ASP C C 175.7 0.2 1 166 . 36 ASP CB C 38.91 0.2 1 167 . 37 GLU H H 8.355 0.02 1 168 . 37 GLU N N 109.6 0.2 1 169 . 37 GLU CA C 60.05 0.2 1 170 . 37 GLU C C 177.3 0.2 1 171 . 37 GLU CB C 28.40 0.2 1 172 . 38 ILE H H 7.951 0.02 1 173 . 38 ILE N N 114.6 0.2 1 174 . 38 ILE CA C 61.60 0.2 1 175 . 38 ILE C C 174.7 0.2 1 176 . 38 ILE CB C 39.61 0.2 1 177 . 39 TYR H H 7.766 0.02 1 178 . 39 TYR N N 120.6 0.2 1 179 . 39 TYR CA C 56.71 0.2 1 180 . 39 TYR C C 174.3 0.2 1 181 . 39 TYR CB C 37.26 0.2 1 182 . 40 TYR H H 9.053 0.02 1 183 . 40 TYR N N 126.8 0.2 1 184 . 40 TYR CA C 58.61 0.2 1 185 . 40 TYR C C 173.8 0.2 1 186 . 40 TYR CB C 37.20 0.2 1 187 . 41 ILE H H 8.472 0.02 1 188 . 41 ILE N N 126.9 0.2 1 189 . 41 ILE CA C 56.33 0.2 1 190 . 41 ILE C C 175.3 0.2 1 191 . 41 ILE CB C 37.57 0.2 1 192 . 42 SER H H 9.231 0.02 1 193 . 42 SER N N 120.1 0.2 1 194 . 42 SER CA C 56.90 0.2 1 195 . 42 SER C C 172.5 0.2 1 196 . 42 SER CB C 66.39 0.2 1 197 . 43 LEU H H 9.019 0.02 1 198 . 43 LEU N N 123.1 0.2 1 199 . 43 LEU CA C 52.31 0.2 1 200 . 43 LEU C C 176.4 0.2 1 201 . 43 LEU CB C 43.33 0.2 1 202 . 44 SER H H 9.047 0.02 1 203 . 44 SER N N 114.6 0.2 1 204 . 44 SER CA C 54.59 0.2 1 205 . 44 SER C C 175.8 0.2 1 206 . 44 SER CB C 65.24 0.2 1 207 . 45 ASP H H 8.356 0.02 1 208 . 45 ASP N N 129.8 0.2 1 209 . 45 ASP CA C 52.03 0.2 1 210 . 45 ASP C C 175.6 0.2 1 211 . 45 ASP CB C 38.91 0.2 1 212 . 46 ALA H H 7.454 0.02 1 213 . 46 ALA N N 124.8 0.2 1 214 . 46 ALA CA C 53.94 0.2 1 215 . 46 ALA C C 177.1 0.2 1 216 . 46 ALA CB C 18.69 0.2 1 217 . 47 ASN H H 7.956 0.02 1 218 . 47 ASN N N 115.5 0.2 1 219 . 47 ASN CA C 52.43 0.2 1 220 . 47 ASN C C 173.5 0.2 1 221 . 47 ASN CB C 39.24 0.2 1 222 . 48 ASP H H 8.378 0.02 1 223 . 48 ASP N N 119.6 0.2 1 224 . 48 ASP CA C 56.23 0.2 1 225 . 48 ASP C C 176.5 0.2 1 226 . 48 ASP CB C 40.36 0.2 1 227 . 49 GLU H H 8.767 0.02 1 228 . 49 GLU N N 115.5 0.2 1 229 . 49 GLU CA C 56.62 0.2 1 230 . 49 GLU C C 176.8 0.2 1 231 . 49 GLU CB C 30.50 0.2 1 232 . 50 TYR H H 7.359 0.02 1 233 . 50 TYR N N 116.7 0.2 1 234 . 50 TYR CA C 56.49 0.2 1 235 . 50 TYR C C 172.4 0.2 1 236 . 50 TYR CB C 38.83 0.2 1 237 . 51 MET H H 8.969 0.02 1 238 . 51 MET N N 118.4 0.2 1 239 . 51 MET CA C 53.97 0.2 1 240 . 51 MET C C 176.0 0.2 1 241 . 51 MET CB C 36.75 0.2 1 242 . 52 MET H H 8.338 0.02 1 243 . 52 MET N N 118.8 0.2 1 244 . 52 MET CA C 51.99 0.2 1 245 . 52 MET C C 174.6 0.2 1 246 . 52 MET CB C 31.74 0.2 1 247 . 53 ILE H H 8.716 0.02 1 248 . 53 ILE N N 122.1 0.2 1 249 . 53 ILE CA C 60.11 0.2 1 250 . 53 ILE C C 174.1 0.2 1 251 . 53 ILE CB C 38.04 0.2 1 252 . 54 TYR H H 9.138 0.02 1 253 . 54 TYR N N 122.9 0.2 1 254 . 54 TYR CA C 54.03 0.2 1 255 . 54 TYR C C 175.7 0.2 1 256 . 54 TYR CB C 39.21 0.2 1 257 . 55 GLY H H 9.722 0.02 1 258 . 55 GLY N N 111.2 0.2 1 259 . 55 GLY CA C 45.80 0.2 1 260 . 55 GLY C C 173.5 0.2 1 261 . 56 VAL H H 8.895 0.02 1 262 . 56 VAL N N 128.6 0.2 1 263 . 56 VAL CA C 62.20 0.2 1 264 . 56 VAL C C 175.2 0.2 1 265 . 56 VAL CB C 29.35 0.2 1 266 . 57 CYS H H 8.572 0.02 1 267 . 57 CYS N N 125.1 0.2 1 268 . 57 CYS CA C 61.01 0.2 1 269 . 57 CYS C C 175.5 0.2 1 270 . 57 CYS CB C 27.45 0.2 1 271 . 58 GLY H H 7.095 0.02 1 272 . 58 GLY N N 102.7 0.2 1 273 . 58 GLY CA C 43.63 0.2 1 274 . 58 GLY C C 171.2 0.2 1 275 . 59 LYS H H 8.556 0.02 1 276 . 59 LYS N N 121.1 0.2 1 277 . 59 LYS CA C 55.85 0.2 1 278 . 59 LYS C C 176.3 0.2 1 279 . 59 LYS CB C 31.99 0.2 1 280 . 60 PHE H H 9.229 0.02 1 281 . 60 PHE N N 128.6 0.2 1 282 . 60 PHE CA C 56.02 0.2 1 283 . 60 PHE C C 173.9 0.2 1 284 . 60 PHE CB C 40.02 0.2 1 285 . 61 PRO CA C 61.95 0.2 1 286 . 61 PRO C C 176.4 0.2 1 287 . 61 PRO CB C 29.91 0.2 1 288 . 62 THR H H 8.199 0.02 1 289 . 62 THR N N 115.4 0.2 1 290 . 62 THR CA C 62.31 0.2 1 291 . 62 THR C C 174.9 0.2 1 292 . 62 THR CB C 68.50 0.2 1 293 . 63 ASP H H 8.394 0.02 1 294 . 63 ASP N N 119.8 0.2 1 295 . 63 ASP CA C 53.80 0.2 1 296 . 63 ASP C C 175.2 0.2 1 297 . 63 ASP CB C 39.62 0.2 1 298 . 64 ASN H H 7.779 0.02 1 299 . 64 ASN N N 116.6 0.2 1 300 . 64 ASN CA C 49.71 0.2 1 301 . 64 ASN C C 174.0 0.2 1 302 . 64 ASN CB C 38.28 0.2 1 303 . 65 PRO CA C 64.40 0.2 1 304 . 65 PRO C C 178.0 0.2 1 305 . 65 PRO CB C 31.21 0.2 1 306 . 66 ASN H H 8.144 0.02 1 307 . 66 ASN N N 115.6 0.2 1 308 . 66 ASN CA C 54.89 0.2 1 309 . 66 ASN C C 177.1 0.2 1 310 . 66 ASN CB C 37.76 0.2 1 311 . 67 PHE H H 7.672 0.02 1 312 . 67 PHE N N 121.9 0.2 1 313 . 67 PHE CA C 60.35 0.2 1 314 . 67 PHE C C 176.8 0.2 1 315 . 67 PHE CB C 37.85 0.2 1 316 . 68 ALA H H 7.975 0.02 1 317 . 68 ALA N N 118.9 0.2 1 318 . 68 ALA CA C 55.23 0.2 1 319 . 68 ALA C C 178.8 0.2 1 320 . 68 ALA CB C 17.61 0.2 1 321 . 69 LEU H H 7.094 0.02 1 322 . 69 LEU N N 115.4 0.2 1 323 . 69 LEU CA C 57.21 0.2 1 324 . 69 LEU C C 179.1 0.2 1 325 . 69 LEU CB C 39.09 0.2 1 326 . 70 GLU H H 7.491 0.02 1 327 . 70 GLU N N 120.0 0.2 1 328 . 70 GLU CA C 58.57 0.2 1 329 . 70 GLU C C 180.0 0.2 1 330 . 70 GLU CB C 27.63 0.2 1 331 . 71 ILE H H 7.732 0.02 1 332 . 71 ILE N N 120.6 0.2 1 333 . 71 ILE CA C 61.11 0.2 1 334 . 71 ILE C C 177.8 0.2 1 335 . 71 ILE CB C 34.01 0.2 1 336 . 72 LEU H H 8.097 0.02 1 337 . 72 LEU N N 119.5 0.2 1 338 . 72 LEU CA C 57.71 0.2 1 339 . 72 LEU C C 180.3 0.2 1 340 . 72 LEU CB C 42.24 0.2 1 341 . 73 ASN H H 8.420 0.02 1 342 . 73 ASN N N 120.9 0.2 1 343 . 73 ASN CA C 56.11 0.2 1 344 . 73 ASN C C 178.1 0.2 1 345 . 73 ASN CB C 40.21 0.2 1 346 . 74 ALA H H 8.236 0.02 1 347 . 74 ALA N N 124.6 0.2 1 348 . 74 ALA CA C 54.55 0.2 1 349 . 74 ALA C C 179.7 0.2 1 350 . 74 ALA CB C 17.38 0.2 1 351 . 75 ASN H H 7.585 0.02 1 352 . 75 ASN N N 116.0 0.2 1 353 . 75 ASN CA C 55.37 0.2 1 354 . 75 ASN C C 179.4 0.2 1 355 . 75 ASN CB C 32.0 0.2 1 356 . 76 LEU H H 7.869 0.02 1 357 . 76 LEU N N 123.5 0.2 1 358 . 76 LEU CA C 60.36 0.2 1 359 . 76 LEU C C 175.8 0.2 1 360 . 76 LEU CB C 37.16 0.2 1 361 . 77 TRP H H 8.640 0.02 1 362 . 77 TRP N N 124.6 0.2 1 363 . 77 TRP CA C 56.18 0.2 1 364 . 77 TRP C C 175.9 0.2 1 365 . 77 TRP CB C 30.15 0.2 1 366 . 78 PHE H H 8.230 0.02 1 367 . 78 PHE N N 119.3 0.2 1 368 . 78 PHE CA C 61.31 0.2 1 369 . 78 PHE C C 178.4 0.2 1 370 . 78 PHE CB C 38.06 0.2 1 371 . 79 ALA H H 7.973 0.02 1 372 . 79 ALA N N 122.5 0.2 1 373 . 79 ALA CA C 53.45 0.2 1 374 . 79 ALA C C 180.3 0.2 1 375 . 79 ALA CB C 18.15 0.2 1 376 . 80 GLU H H 7.082 0.02 1 377 . 80 GLU N N 116.3 0.2 1 378 . 80 GLU CA C 57.79 0.2 1 379 . 80 GLU C C 176.2 0.2 1 380 . 80 GLU CB C 28.78 0.2 1 381 . 81 ASN H H 6.980 0.02 1 382 . 81 ASN N N 112.9 0.2 1 383 . 81 ASN CA C 52.69 0.2 1 384 . 81 ASN C C 175.3 0.2 1 385 . 81 ASN CB C 39.00 0.2 1 386 . 82 GLY H H 7.352 0.02 1 387 . 82 GLY N N 110.6 0.2 1 388 . 82 GLY CA C 46.31 0.2 1 389 . 82 GLY C C 175.3 0.2 1 390 . 83 GLY H H 8.366 0.02 1 391 . 83 GLY N N 105.5 0.2 1 392 . 83 GLY CA C 43.76 0.2 1 393 . 83 GLY C C 180.7 0.2 1 394 . 86 LEU CA C 56.29 0.2 1 395 . 86 LEU C C 177.9 0.2 1 396 . 87 CYS H H 8.739 0.02 1 397 . 87 CYS N N 125.2 0.2 1 398 . 87 CYS CA C 55.63 0.2 1 399 . 87 CYS C C 172.1 0.2 1 400 . 87 CYS CB C 32.13 0.2 1 401 . 88 TYR H H 6.581 0.02 1 402 . 88 TYR N N 121.2 0.2 1 403 . 88 TYR CA C 54.53 0.2 1 404 . 88 TYR C C 172.2 0.2 1 405 . 88 TYR CB C 42.43 0.2 1 406 . 89 GLU H H 8.105 0.02 1 407 . 89 GLU N N 129.9 0.2 1 408 . 89 GLU CA C 54.84 0.2 1 409 . 89 GLU C C 175.4 0.2 1 410 . 89 GLU CB C 31.08 0.2 1 411 . 90 SER H H 7.543 0.02 1 412 . 90 SER N N 119.6 0.2 1 413 . 90 SER CA C 60.09 0.2 1 414 . 90 SER C C 175.4 0.2 1 415 . 90 SER CB C 62.69 0.2 1 416 . 91 GLY H H 8.833 0.02 1 417 . 91 GLY N N 115.1 0.2 1 418 . 91 GLY CA C 46.65 0.2 1 419 . 91 GLY C C 175.3 0.2 1 420 . 92 ALA H H 8.734 0.02 1 421 . 92 ALA N N 123.1 0.2 1 422 . 92 ALA CA C 50.81 0.2 1 423 . 92 ALA C C 177.4 0.2 1 424 . 92 ALA CB C 17.94 0.2 1 425 . 93 GLN H H 7.465 0.02 1 426 . 93 GLN N N 116.8 0.2 1 427 . 93 GLN CA C 56.48 0.2 1 428 . 93 GLN C C 175.2 0.2 1 429 . 93 GLN CB C 25.16 0.2 1 430 . 94 SER H H 7.460 0.02 1 431 . 94 SER N N 111.6 0.2 1 432 . 94 SER CA C 57.48 0.2 1 433 . 94 SER C C 173.4 0.2 1 434 . 94 SER CB C 65.83 0.2 1 435 . 95 LEU H H 8.796 0.02 1 436 . 95 LEU N N 124.0 0.2 1 437 . 95 LEU CA C 54.03 0.2 1 438 . 95 LEU C C 174.4 0.2 1 439 . 95 LEU CB C 42.05 0.2 1 440 . 96 LEU H H 8.748 0.02 1 441 . 96 LEU N N 126.8 0.2 1 442 . 96 LEU CA C 52.76 0.2 1 443 . 96 LEU C C 175.4 0.2 1 444 . 96 LEU CB C 45.52 0.2 1 445 . 97 LEU H H 8.948 0.02 1 446 . 97 LEU N N 122.0 0.2 1 447 . 97 LEU CA C 53.37 0.2 1 448 . 97 LEU C C 175.9 0.2 1 449 . 97 LEU CB C 43.47 0.2 1 450 . 98 ALA H H 9.182 0.02 1 451 . 98 ALA N N 125.3 0.2 1 452 . 98 ALA CA C 50.36 0.2 1 453 . 98 ALA C C 175.5 0.2 1 454 . 98 ALA CB C 23.21 0.2 1 455 . 99 LEU H H 8.889 0.02 1 456 . 99 LEU N N 123.9 0.2 1 457 . 99 LEU CA C 53.81 0.2 1 458 . 99 LEU C C 173.8 0.2 1 459 . 99 LEU CB C 47.04 0.2 1 460 . 100 ARG H H 9.104 0.02 1 461 . 100 ARG N N 128.3 0.2 1 462 . 100 ARG CA C 55.71 0.2 1 463 . 100 ARG C C 175.2 0.2 1 464 . 100 ARG CB C 30.65 0.2 1 465 . 101 PHE H H 9.180 0.02 1 466 . 101 PHE N N 128.1 0.2 1 467 . 101 PHE CA C 53.85 0.2 1 468 . 101 PHE C C 171.5 0.2 1 469 . 101 PHE CB C 39.89 0.2 1 470 . 102 PRO CA C 62.15 0.2 1 471 . 102 PRO C C 176.0 0.2 1 472 . 102 PRO CB C 31.16 0.2 1 473 . 103 LEU H H 7.532 0.02 1 474 . 103 LEU N N 119.0 0.2 1 475 . 103 LEU CA C 54.91 0.2 1 476 . 103 LEU C C 178.8 0.2 1 477 . 103 LEU CB C 41.26 0.2 1 478 . 104 ASP H H 8.171 0.02 1 479 . 104 ASP N N 121.7 0.2 1 480 . 104 ASP CA C 56.19 0.2 1 481 . 104 ASP C C 176.6 0.2 1 482 . 104 ASP CB C 39.18 0.2 1 483 . 105 ASP H H 8.665 0.02 1 484 . 105 ASP N N 120.6 0.2 1 485 . 105 ASP CA C 54.20 0.2 1 486 . 105 ASP C C 175.3 0.2 1 487 . 105 ASP CB C 39.37 0.2 1 488 . 106 ALA H H 7.329 0.2 1 489 . 106 ALA N N 120.5 0.2 1 490 . 106 ALA CA C 53.43 0.2 1 491 . 106 ALA C C 177.4 0.2 1 492 . 106 ALA CB C 20.44 0.2 1 493 . 107 THR H H 6.713 0.03 1 494 . 107 THR N N 108.9 0.2 1 495 . 107 THR CA C 57.81 0.2 1 496 . 107 THR C C 177.3 0.2 1 497 . 107 THR CB C 69.86 0.2 1 498 . 108 PRO CA C 65.26 0.2 1 499 . 108 PRO C C 177.5 0.2 1 500 . 108 PRO CB C 30.68 0.2 1 501 . 109 GLU H H 8.638 0.02 1 502 . 109 GLU N N 118.0 0.2 1 503 . 109 GLU CA C 60.01 0.2 1 504 . 109 GLU C C 178.7 0.2 1 505 . 109 GLU CB C 27.62 0.2 1 506 . 110 LYS H H 7.876 0.02 1 507 . 110 LYS N N 121.0 0.2 1 508 . 110 LYS CA C 59.35 0.2 1 509 . 110 LYS C C 178.9 0.2 1 510 . 110 LYS CB C 32.45 0.2 1 511 . 111 LEU H H 7.744 0.02 1 512 . 111 LEU N N 120.2 0.2 1 513 . 111 LEU CA C 57.34 0.2 1 514 . 111 LEU C C 177.5 0.2 1 515 . 111 LEU CB C 39.00 0.2 1 516 . 112 GLU H H 8.235 0.02 1 517 . 112 GLU N N 119.0 0.2 1 518 . 112 GLU CA C 59.70 0.2 1 519 . 112 GLU C C 178.3 0.2 1 520 . 112 GLU CB C 29.12 0.2 1 521 . 113 ASN H H 7.945 0.02 1 522 . 113 ASN N N 117.3 0.2 1 523 . 113 ASN CA C 56.11 0.2 1 524 . 113 ASN C C 177.7 0.2 1 525 . 113 ASN CB C 37.98 0.2 1 526 . 114 GLU H H 8.080 0.02 1 527 . 114 GLU N N 120.4 0.2 1 528 . 114 GLU CA C 58.02 0.2 1 529 . 114 GLU C C 179.0 0.2 1 530 . 114 GLU CB C 27.80 0.2 1 531 . 115 ILE H H 8.354 0.02 1 532 . 115 ILE N N 120.3 0.2 1 533 . 115 ILE CA C 65.57 0.2 1 534 . 115 ILE C C 178.1 0.2 1 535 . 115 ILE CB C 36.08 0.2 1 536 . 116 GLU H H 8.011 0.02 1 537 . 116 GLU N N 119.9 0.2 1 538 . 116 GLU CA C 59.35 0.2 1 539 . 116 GLU C C 178.4 0.2 1 540 . 116 GLU CB C 27.92 0.2 1 541 . 117 VAL H H 7.549 0.02 1 542 . 117 VAL N N 120.4 0.2 1 543 . 117 VAL CA C 66.30 0.2 1 544 . 117 VAL C C 180.0 0.2 1 545 . 117 VAL CB C 30.21 0.2 1 546 . 118 VAL H H 7.613 0.02 1 547 . 118 VAL N N 123.6 0.2 1 548 . 118 VAL CA C 67.72 0.2 1 549 . 118 VAL C C 177.4 0.2 1 550 . 118 VAL CB C 30.02 0.2 1 551 . 119 VAL H H 8.761 0.02 1 552 . 119 VAL N N 122.2 0.2 1 553 . 119 VAL CA C 66.70 0.2 1 554 . 119 VAL C C 177.8 0.2 1 555 . 119 VAL CB C 30.26 0.2 1 556 . 120 LYS H H 8.647 0.02 1 557 . 120 LYS N N 118.9 0.2 1 558 . 120 LYS CA C 58.19 0.2 1 559 . 120 LYS C C 180.2 0.2 1 560 . 120 LYS CB C 30.35 0.2 1 561 . 121 SER H H 7.857 0.02 1 562 . 121 SER N N 116.4 0.2 1 563 . 121 SER CA C 62.48 0.2 1 564 . 121 SER C C 176.2 0.2 1 565 . 121 SER CB C 63.25 0.2 1 566 . 122 MET H H 8.395 0.02 1 567 . 122 MET N N 124.3 0.2 1 568 . 122 MET CA C 59.82 0.2 1 569 . 122 MET C C 176.7 0.2 1 570 . 122 MET CB C 32.88 0.2 1 571 . 123 GLU H H 8.503 0.02 1 572 . 123 GLU N N 120.0 0.2 1 573 . 123 GLU CA C 59.51 0.2 1 574 . 123 GLU C C 179.3 0.2 1 575 . 123 GLU CB C 28.94 0.2 1 576 . 124 ASN H H 7.971 0.02 1 577 . 124 ASN N N 117.3 0.2 1 578 . 124 ASN CA C 56.11 0.2 1 579 . 124 ASN C C 177.1 0.2 1 580 . 124 ASN CB C 37.66 0.2 1 581 . 125 LEU H H 8.305 0.02 1 582 . 125 LEU N N 122.1 0.2 1 583 . 125 LEU CA C 57.79 0.2 1 584 . 125 LEU C C 178.6 0.2 1 585 . 125 LEU CB C 38.42 0.2 1 586 . 126 TYR H H 8.936 0.02 1 587 . 126 TYR N N 117.7 0.2 1 588 . 126 TYR CA C 59.29 0.2 1 589 . 126 TYR C C 179.2 0.2 1 590 . 126 TYR CB C 35.83 0.2 1 591 . 127 LEU H H 7.771 0.02 1 592 . 127 LEU N N 121.8 0.2 1 593 . 127 LEU CA C 58.15 0.2 1 594 . 127 LEU C C 179.0 0.2 1 595 . 127 LEU CB C 40.77 0.2 1 596 . 128 VAL H H 8.014 0.02 1 597 . 128 VAL N N 120.8 0.2 1 598 . 128 VAL CA C 65.95 0.2 1 599 . 128 VAL C C 179.8 0.2 1 600 . 128 VAL CB C 30.97 0.2 1 601 . 129 LEU H H 8.557 0.02 1 602 . 129 LEU N N 119.4 0.2 1 603 . 129 LEU CA C 57.72 0.2 1 604 . 129 LEU C C 179.8 0.2 1 605 . 129 LEU CB C 38.62 0.2 1 606 . 130 HIS H H 8.678 0.02 1 607 . 130 HIS N N 120.9 0.2 1 608 . 130 HIS CA C 59.09 0.2 1 609 . 130 HIS C C 179.7 0.2 1 610 . 130 HIS CB C 28.76 0.2 1 611 . 131 ASN H H 8.297 0.02 1 612 . 131 ASN N N 119.5 0.2 1 613 . 131 ASN CA C 55.12 0.2 1 614 . 131 ASN C C 176.3 0.2 1 615 . 131 ASN CB C 37.44 0.2 1 616 . 132 GLN H H 7.588 0.02 1 617 . 132 GLN N N 117.2 0.2 1 618 . 132 GLN CA C 54.93 0.2 1 619 . 132 GLN C C 175.8 0.2 1 620 . 132 GLN CB C 28.70 0.2 1 621 . 133 GLY H H 7.813 0.02 1 622 . 133 GLY N N 108.6 0.2 1 623 . 133 GLY CA C 45.32 0.2 1 624 . 133 GLY C C 174.3 0.2 1 625 . 134 ILE H H 8.024 0.02 1 626 . 134 ILE N N 122.8 0.2 1 627 . 134 ILE CA C 60.12 0.2 1 628 . 134 ILE C C 174.5 0.2 1 629 . 134 ILE CB C 38.42 0.2 1 630 . 135 THR H H 8.149 0.02 1 631 . 135 THR N N 122.2 0.2 1 632 . 135 THR CA C 60.52 0.2 1 633 . 135 THR C C 174.3 0.2 1 634 . 135 THR CB C 69.86 0.2 1 635 . 136 LEU H H 9.018 0.02 1 636 . 136 LEU N N 126.7 0.2 1 637 . 136 LEU CA C 53.62 0.2 1 638 . 136 LEU C C 177.0 0.2 1 639 . 136 LEU CB C 40.60 0.2 1 640 . 137 GLU H H 8.856 0.02 1 641 . 137 GLU N N 123.5 0.2 1 642 . 137 GLU CA C 56.24 0.2 1 643 . 137 GLU C C 176.0 0.2 1 644 . 137 GLU CB C 29.32 0.2 1 645 . 138 ASN H H 8.251 0.02 1 646 . 138 ASN N N 119.3 0.2 1 647 . 138 ASN CA C 52.95 0.2 1 648 . 138 ASN C C 175.4 0.2 1 649 . 138 ASN CB C 38.30 0.2 1 650 . 139 GLU H H 8.299 0.02 1 651 . 139 GLU N N 121.3 0.2 1 652 . 139 GLU CA C 56.67 0.2 1 653 . 139 GLU C C 176.4 0.2 1 654 . 139 GLU CB C 29.14 0.2 1 655 . 140 HIS H H 8.212 0.02 1 656 . 140 HIS N N 119.3 0.2 1 657 . 140 HIS CA C 55.72 0.2 1 658 . 140 HIS C C 175.1 0.2 1 659 . 140 HIS CB C 29.05 0.2 1 660 . 141 MET H H 8.023 0.02 1 661 . 141 MET N N 121.2 0.2 1 662 . 141 MET CA C 55.29 0.2 1 663 . 141 MET C C 175.8 0.2 1 664 . 141 MET CB C 32.03 0.2 1 665 . 142 LYS H H 8.155 0.02 1 666 . 142 LYS N N 123.3 0.2 1 667 . 142 LYS CA C 55.76 0.2 1 668 . 142 LYS C C 176.4 0.2 1 669 . 142 LYS CB C 31.94 0.2 1 670 . 143 ILE H H 8.112 0.02 1 671 . 143 ILE N N 123.3 0.2 1 672 . 143 ILE CA C 60.77 0.2 1 673 . 143 ILE C C 176.3 0.2 1 674 . 143 ILE CB C 37.59 0.2 1 675 . 144 GLU H H 8.410 0.02 1 676 . 144 GLU N N 125.0 0.2 1 677 . 144 GLU CA C 56.18 0.2 1 678 . 144 GLU C C 176.2 0.2 1 679 . 144 GLU CB C 29.16 0.2 1 680 . 145 GLU H H 8.255 0.02 1 681 . 145 GLU N N 122.5 0.2 1 682 . 145 GLU CA C 56.21 0.2 1 683 . 145 GLU C C 176.4 0.2 1 684 . 145 GLU CB C 29.01 0.2 1 685 . 146 ILE H H 8.074 0.02 1 686 . 146 ILE N N 122.3 0.2 1 687 . 146 ILE CA C 60.81 0.2 1 688 . 146 ILE C C 176.4 0.2 1 689 . 146 ILE CB C 37.65 0.2 1 690 . 147 SER H H 8.319 0.02 1 691 . 147 SER N N 119.9 0.2 1 692 . 147 SER CA C 57.82 0.2 1 693 . 147 SER C C 174.7 0.2 1 694 . 147 SER CB C 63.22 0.2 1 695 . 148 SER H H 8.394 0.02 1 696 . 148 SER N N 118.8 0.2 1 697 . 148 SER CA C 57.98 0.2 1 698 . 148 SER C C 174.8 0.2 1 699 . 148 SER CB C 63.02 0.2 1 700 . 149 SER H H 8.267 0.02 1 701 . 149 SER N N 117.9 0.2 1 702 . 149 SER CA C 58.17 0.2 1 703 . 149 SER C C 174.3 0.2 1 704 . 149 SER CB C 63.19 0.2 1 705 . 150 ASP H H 8.163 0.02 1 706 . 150 ASP N N 122.2 0.2 1 707 . 150 ASP CA C 54.14 0.2 1 708 . 150 ASP C C 175.9 0.2 1 709 . 150 ASP CB C 40.42 0.2 1 710 . 151 ASN H H 8.158 0.02 1 711 . 151 ASN N N 119.1 0.2 1 712 . 151 ASN CA C 53.03 0.2 1 713 . 151 ASN C C 175.3 0.2 1 714 . 151 ASN CB C 38.03 0.2 1 715 . 152 LYS H H 8.083 0.02 1 716 . 152 LYS N N 121.1 0.2 1 717 . 152 LYS CA C 56.24 0.2 1 718 . 152 LYS C C 176.4 0.2 1 719 . 152 LYS CB C 31.65 0.2 1 720 . 153 HIS H H 8.286 0.02 1 721 . 153 HIS N N 119.0 0.2 1 722 . 153 HIS CA C 55.42 0.2 1 723 . 153 HIS C C 174.6 0.2 1 724 . 153 HIS CB C 28.26 0.2 1 725 . 154 TYR H H 7.700 0.02 1 726 . 154 TYR N N 120.0 0.2 1 727 . 154 TYR CA C 54.95 0.2 1 728 . 154 TYR C C 175.1 0.2 1 729 . 154 TYR CB C 32.12 0.2 1 730 . 155 TYR H H 7.914 0.02 1 731 . 155 TYR N N 121.9 0.2 1 732 . 155 TYR CA C 57.11 0.2 1 733 . 155 TYR C C 175.2 0.2 1 734 . 155 TYR CB C 38.82 0.2 1 735 . 156 ALA H H 8.026 0.02 1 736 . 156 ALA N N 126.2 0.2 1 737 . 156 ALA CA C 51.99 0.2 1 738 . 156 ALA C C 177.7 0.2 1 739 . 156 ALA CB C 18.43 0.2 1 740 . 157 GLY H H 7.659 0.02 1 741 . 157 GLY N N 108.2 0.2 1 742 . 157 GLY CA C 44.98 0.2 1 743 . 157 GLY C C 173.0 0.2 1 744 . 158 ARG H H 7.648 0.02 1 745 . 158 ARG N N 125.6 0.2 1 746 . 158 ARG CA C 56.87 0.2 1 747 . 158 ARG C C 171.1 0.2 1 748 . 158 ARG CB C 30.35 0.2 1 stop_ save_