data_26541 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Chemical Shift Assignment of the FimH lectin domain from Escherichia coli ; _BMRB_accession_number 26541 _BMRB_flat_file_name bmr26541.str _Entry_type original _Submission_date 2015-03-13 _Accession_date 2015-03-13 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone resonance assignment of the FimH lectin domain from Escherichia coli K12 obtained from solution NMR experiments' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fiege Brigitte . . 2 Ernst Beat . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 191 "13C chemical shifts" 510 "15N chemical shifts" 173 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-13 update BMRB 'update entry citation' 2015-05-11 original author 'original release' stop_ _Original_release_date 2015-05-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; he Tyrosine Gate of the Bacterial Lectin FimH: A Conformational Analysis by NMR Spectroscopy and X-ray Crystallography ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25940742 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fiege Brigitte . . 2 Rabbani Said . . 3 Preston Roland C. . 4 Jakob Roman P. . 5 Zihlmann Pascal . . 6 Schwardt Oliver . . 7 Jiang Xiaohua . . 8 Maier Timm . . 9 Ernst Beat . . stop_ _Journal_abbreviation Chembiochem _Journal_volume 16 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1235 _Page_last 1246 _Year 2015 _Details . loop_ _Keyword FimH ITC 'NMR spectroscopy' 'X-ray diffraction' 'urinary tract infections' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name FimH-CRD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label FimH-CRD $FimH-CRD stop_ _System_molecular_weight 18643.8386 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FimH-CRD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FimH-CRD _Molecular_mass 18643.8386 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'mannose-specific lectin on the tip of bacterial type 1 pili' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; FACKTANGTAIPIGGGSANV YVNLAPVVNVGQNLVVDLST QIFCHNDYPETITDYVTLQR GSAYGGVLSNFSGTVKYSGS SYPFPTTSETPRVVYNSRTD KPWPVALYLTPVSSAGGVAI KAGSLIAVLILRQTNNYNSD DFQFVWNIYANNDVVVPTGL VPRGSLEHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 PHE 2 2 ALA 3 3 CYS 4 4 LYS 5 5 THR 6 6 ALA 7 7 ASN 8 8 GLY 9 9 THR 10 10 ALA 11 11 ILE 12 12 PRO 13 13 ILE 14 14 GLY 15 15 GLY 16 16 GLY 17 17 SER 18 18 ALA 19 19 ASN 20 20 VAL 21 21 TYR 22 22 VAL 23 23 ASN 24 24 LEU 25 25 ALA 26 26 PRO 27 27 VAL 28 28 VAL 29 29 ASN 30 30 VAL 31 31 GLY 32 32 GLN 33 33 ASN 34 34 LEU 35 35 VAL 36 36 VAL 37 37 ASP 38 38 LEU 39 39 SER 40 40 THR 41 41 GLN 42 42 ILE 43 43 PHE 44 44 CYS 45 45 HIS 46 46 ASN 47 47 ASP 48 48 TYR 49 49 PRO 50 50 GLU 51 51 THR 52 52 ILE 53 53 THR 54 54 ASP 55 55 TYR 56 56 VAL 57 57 THR 58 58 LEU 59 59 GLN 60 60 ARG 61 61 GLY 62 62 SER 63 63 ALA 64 64 TYR 65 65 GLY 66 66 GLY 67 67 VAL 68 68 LEU 69 69 SER 70 70 ASN 71 71 PHE 72 72 SER 73 73 GLY 74 74 THR 75 75 VAL 76 76 LYS 77 77 TYR 78 78 SER 79 79 GLY 80 80 SER 81 81 SER 82 82 TYR 83 83 PRO 84 84 PHE 85 85 PRO 86 86 THR 87 87 THR 88 88 SER 89 89 GLU 90 90 THR 91 91 PRO 92 92 ARG 93 93 VAL 94 94 VAL 95 95 TYR 96 96 ASN 97 97 SER 98 98 ARG 99 99 THR 100 100 ASP 101 101 LYS 102 102 PRO 103 103 TRP 104 104 PRO 105 105 VAL 106 106 ALA 107 107 LEU 108 108 TYR 109 109 LEU 110 110 THR 111 111 PRO 112 112 VAL 113 113 SER 114 114 SER 115 115 ALA 116 116 GLY 117 117 GLY 118 118 VAL 119 119 ALA 120 120 ILE 121 121 LYS 122 122 ALA 123 123 GLY 124 124 SER 125 125 LEU 126 126 ILE 127 127 ALA 128 128 VAL 129 129 LEU 130 130 ILE 131 131 LEU 132 132 ARG 133 133 GLN 134 134 THR 135 135 ASN 136 136 ASN 137 137 TYR 138 138 ASN 139 139 SER 140 140 ASP 141 141 ASP 142 142 PHE 143 143 GLN 144 144 PHE 145 145 VAL 146 146 TRP 147 147 ASN 148 148 ILE 149 149 TYR 150 150 ALA 151 151 ASN 152 152 ASN 153 153 ASP 154 154 VAL 155 155 VAL 156 156 VAL 157 157 PRO 158 158 THR 159 159 GLY 160 160 LEU 161 161 VAL 162 162 PRO 163 163 ARG 164 164 GLY 165 165 SER 166 166 LEU 167 167 GLU 168 168 HIS 169 169 HIS 170 170 HIS 171 171 HIS 172 172 HIS 173 173 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 UniProt A2IC68_ECOLX A2IC68_ECOLX . . . . . PDB 4BUQ 'Crystal structure of wild type FimH lectin domain in complex with heptyl alpha-D-mannopyrannoside' . . . . . PDB 4CST "Crystal structure of FimH in complex with 3'-Chloro-4'-(alpha-D-mannopyranosyloxy)-biphenyl-4-carbonitrile" . . . . . PDB 1UWF '1.7 A RESOLUTION STRUCTURE OF THE RECEPTOR BINDING DOMAIN OF THE FIMH ADHESIN FROM UROPATHOGENIC E. COLI' . . . . . PDB 1TR7 'FimH adhesin receptor binding domain from uropathogenic E. coli' . . . . . PDB 3MCY 'Crystal structure of FimH lectin domain bound to biphenyl mannoside meta-methyl ester' . . . . . PDB 4CSS 'Crystal structure of FimH in complex with a sulfonamide biphenyl alpha D-mannoside' . . . . . PDB 4AV5 'Structure of a triclinic crystal of the FimH lectin domain in complex with a propynyl biphenyl alpha-D-mannoside' . . . . . PDB 4AV4 'FimH lectin domain co-crystal with a alpha-D-mannoside O-linked to a propynyl pyridine' . . . . . PDB 2VCO 'Crystal structure of the fimbrial adhesin FimH in complex with its high-mannose epitope' . . . . . PDB 1KLF 'FIMH ADHESIN-FIMC CHAPERONE COMPLEX WITH D-MANNOSE' . . . . . PDB 4AUU 'Crystal structure of apo FimH lectin domain at 1.5 A resolution' . . . . . PDB 1QUN 'X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI' . . . . . PDB 4CA4 'Crystal structure of FimH lectin domain with the Tyr48Ala mutation, in complex with heptyl alpha-D-mannopyrannoside' . . . . . PDB 4LOV 'Crystal structure of FimH in complex with Heptylmannoside' . . . . . PDB 3ZPD 'Solution structure of the FimH adhesin carbohydrate-binding domain' . . . . . BMRB 19066 'Solution structure of the FimH adhesin carbohydrate-binding domain' . . . . . GB CAM92099.1 'Type 1 fimbrial adhesin FimH [Escherichia coli]' . . . . . PDB 4X50 'Crystal structure of FimH in complex with biphenyl alpha-D-mannopyranoside' . . . . . PDB 4X5Q 'Crystal structure of FimH in complex with 5-nitro-indolinylphenyl alpha-D-mannopyranoside' . . . . . PDB 4X5R 'Crystal structure of FimH in complex with a squaryl-phenyl alpha-D-mannopyranoside derivative' . . . . . PDB 4X5P 'Crystal structure of FimH in complex with a benzoyl-amidophenyl alpha-D-mannopyranoside' . . . . . 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 _Gene_mnemonic $FimH-CRD 'E. coli' 562 Bacteria . Escherichia coli K12 fimH 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 $FimH-CRD 'recombinant technology' 'Escherichia coli' Escherichia coli HM125 pDsbA3 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.6 mM FimH-CRD, 25 mM sodium phosphate buffer pH 6.8' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FimH-CRD 0.6 mM '[U-100% 13C; U-100% 15N]' 'sodium phosphate' 25.0 mM 'natural abundance' TSP-d4 0.1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Saveframe_category software _Name CcpNmr_Analysis _Version 2.3 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_Sparta _Saveframe_category software _Name Sparta _Version any loop_ _Vendor _Address _Electronic_address 'Yang Shen, Ad Bax' 'National Institutes of Health, Bethesda, USA' http://spin.niddk.nih.gov/bax/software/SPARTA/ stop_ loop_ _Task 'chemical shift calculation' stop_ _Details . save_ save_Topspin _Saveframe_category software _Name Topspin _Version 3.2 loop_ _Vendor _Address _Electronic_address Bruker 'Bruker BioSpin, Faellanden, Switzerland' . stop_ loop_ _Task 'data acquisition' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details 'NMR buffering condition' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.025 . M pH 6.800 . pH pressure 1.000 . atm temperature 298.000 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 HDO C 13 H ppm 4.7 internal indirect . . . 0.25144953 HDO H 1 H ppm 4.7 internal direct . . . 1 HDO N 15 H ppm 4.7 internal 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_assigned_chem_shift_list _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CcpNmr_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HN(CO)CA' '3D HN(CA)CO' '3D HNCO' '3D HNCACB' '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name FimH-CRD _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 1 PHE C C 171.352 0.004 1 2 1 1 PHE CA C 56.088 0.016 1 3 1 1 PHE CB C 37.908 0.037 1 4 2 2 ALA H H 6.720 0.004 1 5 2 2 ALA C C 174.270 0.009 1 6 2 2 ALA CA C 51.456 0.016 1 7 2 2 ALA CB C 22.379 0.05 1 8 2 2 ALA N N 129.155 0.052 1 9 3 3 CYS H H 7.746 0.001 1 10 3 3 CYS C C 173.071 0.008 1 11 3 3 CYS CA C 56.064 0.024 1 12 3 3 CYS CB C 51.407 0.034 1 13 3 3 CYS N N 112.134 0.009 1 14 4 4 LYS H H 9.926 0.003 1 15 4 4 LYS C C 174.555 0.01 1 16 4 4 LYS CA C 55.032 0.015 1 17 4 4 LYS CB C 36.073 0.034 1 18 4 4 LYS N N 121.144 0.009 1 19 5 5 THR H H 8.718 0.002 1 20 5 5 THR C C 178.496 0.004 1 21 5 5 THR CA C 59.072 0.042 1 22 5 5 THR CB C 72.064 0.005 1 23 5 5 THR N N 109.346 0.008 1 24 6 6 ALA H H 8.600 0.001 1 25 6 6 ALA C C 178.205 0.006 1 26 6 6 ALA CA C 54.417 0.029 1 27 6 6 ALA CB C 18.808 0.015 1 28 6 6 ALA N N 123.362 0.017 1 29 7 7 ASN H H 8.052 0.002 1 30 7 7 ASN HD21 H 7.758 0.002 2 31 7 7 ASN HD22 H 7.024 0.003 2 32 7 7 ASN C C 175.963 0.003 1 33 7 7 ASN CA C 52.773 0.045 1 34 7 7 ASN CB C 38.521 0.069 1 35 7 7 ASN CG C 177.633 0.003 1 36 7 7 ASN N N 112.741 0.017 1 37 7 7 ASN ND2 N 112.521 0.006 1 38 8 8 GLY H H 8.003 0.001 1 39 8 8 GLY C C 174.582 0.006 1 40 8 8 GLY CA C 45.673 0.024 1 41 8 8 GLY N N 107.654 0.008 1 42 9 9 THR H H 7.693 0.001 1 43 9 9 THR C C 172.881 0.001 1 44 9 9 THR CA C 63.372 0.05 1 45 9 9 THR CB C 69.297 0.058 1 46 9 9 THR N N 118.164 0.034 1 47 10 10 ALA H H 8.667 0.002 1 48 10 10 ALA C C 177.412 0.003 1 49 10 10 ALA CA C 51.458 0.032 1 50 10 10 ALA CB C 21.979 0.039 1 51 10 10 ALA N N 127.939 0.022 1 52 11 11 ILE H H 8.375 0.001 1 53 11 11 ILE C C 173.678 . 1 54 11 11 ILE CA C 59.204 0.01 1 55 11 11 ILE CB C 40.041 . 1 56 11 11 ILE N N 120.571 0.011 1 57 12 12 PRO C C 174.159 0.006 1 58 12 12 PRO CA C 62.259 0.015 1 59 12 12 PRO CB C 34.156 0.0 1 60 13 13 ILE H H 7.689 0.001 1 61 13 13 ILE C C 177.981 0.01 1 62 13 13 ILE CA C 63.131 0.031 1 63 13 13 ILE CB C 39.207 0.018 1 64 13 13 ILE N N 115.570 0.022 1 65 14 14 GLY H H 8.182 0.002 1 66 14 14 GLY C C 174.778 0.006 1 67 14 14 GLY CA C 42.776 0.038 1 68 14 14 GLY N N 116.116 0.009 1 69 15 15 GLY H H 7.538 0.001 1 70 15 15 GLY C C 172.173 0.003 1 71 15 15 GLY CA C 42.766 0.065 1 72 15 15 GLY N N 108.654 0.027 1 73 16 16 GLY H H 7.476 0.003 1 74 16 16 GLY C C 171.187 0.003 1 75 16 16 GLY CA C 44.599 0.027 1 76 16 16 GLY N N 103.994 0.012 1 77 17 17 SER H H 8.267 0.001 1 78 17 17 SER C C 172.859 0.01 1 79 17 17 SER CA C 56.220 0.059 1 80 17 17 SER CB C 66.588 0.034 1 81 17 17 SER N N 115.468 0.019 1 82 18 18 ALA H H 8.460 0.002 1 83 18 18 ALA C C 175.041 0.007 1 84 18 18 ALA CA C 51.661 0.025 1 85 18 18 ALA CB C 22.644 0.075 1 86 18 18 ALA N N 122.070 0.035 1 87 19 19 ASN H H 8.614 0.001 1 88 19 19 ASN HD21 H 6.880 0.003 2 89 19 19 ASN HD22 H 7.323 0.002 2 90 19 19 ASN C C 174.467 0.001 1 91 19 19 ASN CA C 51.626 0.06 1 92 19 19 ASN CB C 39.702 0.046 1 93 19 19 ASN CG C 176.135 0.011 1 94 19 19 ASN N N 118.937 0.016 1 95 19 19 ASN ND2 N 112.408 0.008 1 96 20 20 VAL H H 9.431 0.003 1 97 20 20 VAL C C 173.366 0.005 1 98 20 20 VAL CA C 61.339 0.033 1 99 20 20 VAL CB C 34.537 0.095 1 100 20 20 VAL N N 124.114 0.037 1 101 21 21 TYR H H 8.789 0.002 1 102 21 21 TYR C C 176.239 0.009 1 103 21 21 TYR CA C 57.310 0.059 1 104 21 21 TYR CB C 38.546 0.035 1 105 21 21 TYR N N 128.367 0.037 1 106 22 22 VAL H H 8.662 0.002 1 107 22 22 VAL C C 174.668 0.002 1 108 22 22 VAL CA C 58.955 0.042 1 109 22 22 VAL CB C 34.127 0.03 1 110 22 22 VAL N N 115.991 0.027 1 111 23 23 ASN H H 8.824 0.001 1 112 23 23 ASN HD21 H 7.022 0.005 2 113 23 23 ASN HD22 H 7.576 0.001 2 114 23 23 ASN C C 174.486 0.012 1 115 23 23 ASN CA C 53.138 0.025 1 116 23 23 ASN CB C 38.477 0.049 1 117 23 23 ASN CG C 176.897 0.011 1 118 23 23 ASN N N 124.153 0.029 1 119 23 23 ASN ND2 N 114.326 0.002 1 120 24 24 LEU H H 9.024 0.002 1 121 24 24 LEU C C 176.703 0.02 1 122 24 24 LEU CA C 52.615 0.017 1 123 24 24 LEU CB C 45.736 0.039 1 124 24 24 LEU N N 124.471 0.023 1 125 25 25 ALA H H 7.817 0.001 1 126 25 25 ALA C C 175.122 . 1 127 25 25 ALA CA C 50.663 0.012 1 128 25 25 ALA CB C 17.804 . 1 129 25 25 ALA N N 128.756 0.014 1 130 26 26 PRO C C 177.386 0.009 1 131 26 26 PRO CA C 64.237 0.028 1 132 26 26 PRO CB C 32.285 0.042 1 133 27 27 VAL H H 7.274 0.002 1 134 27 27 VAL C C 175.195 0.005 1 135 27 27 VAL CA C 60.225 0.035 1 136 27 27 VAL CB C 35.696 0.033 1 137 27 27 VAL N N 118.046 0.008 1 138 28 28 VAL H H 8.547 0.001 1 139 28 28 VAL C C 172.118 0.006 1 140 28 28 VAL CA C 60.733 0.051 1 141 28 28 VAL CB C 34.480 0.046 1 142 28 28 VAL N N 126.492 0.013 1 143 29 29 ASN H H 8.063 0.001 1 144 29 29 ASN HD21 H 7.241 0.001 2 145 29 29 ASN HD22 H 6.779 0.004 2 146 29 29 ASN C C 175.895 0.004 1 147 29 29 ASN CA C 52.695 0.074 1 148 29 29 ASN CB C 40.339 0.043 1 149 29 29 ASN CG C 176.694 0.013 1 150 29 29 ASN N N 121.435 0.009 1 151 29 29 ASN ND2 N 111.824 0.002 1 152 30 30 VAL H H 8.413 0.001 1 153 30 30 VAL C C 177.566 0.006 1 154 30 30 VAL CA C 65.654 0.072 1 155 30 30 VAL CB C 31.329 0.048 1 156 30 30 VAL N N 119.133 0.019 1 157 31 31 GLY H H 8.763 0.001 1 158 31 31 GLY C C 173.605 0.007 1 159 31 31 GLY CA C 45.085 0.032 1 160 31 31 GLY N N 114.990 0.011 1 161 32 32 GLN H H 8.022 0.002 1 162 32 32 GLN HE21 H 6.866 0.002 2 163 32 32 GLN HE22 H 7.597 0.001 2 164 32 32 GLN C C 174.593 0.009 1 165 32 32 GLN CA C 54.043 0.022 1 166 32 32 GLN CB C 30.686 0.037 1 167 32 32 GLN CG C 33.948 0.06 1 168 32 32 GLN CD C 180.666 0.01 1 169 32 32 GLN N N 119.751 0.008 1 170 32 32 GLN NE2 N 113.092 0.006 1 171 33 33 ASN H H 8.455 0.002 1 172 33 33 ASN HD21 H 7.389 0.002 2 173 33 33 ASN HD22 H 6.822 0.003 2 174 33 33 ASN C C 174.883 0.004 1 175 33 33 ASN CA C 52.441 0.031 1 176 33 33 ASN CB C 40.354 0.051 1 177 33 33 ASN CG C 175.419 0.013 1 178 33 33 ASN N N 116.701 0.016 1 179 33 33 ASN ND2 N 111.891 0.006 1 180 34 34 LEU H H 9.764 0.003 1 181 34 34 LEU C C 174.245 0.001 1 182 34 34 LEU CA C 54.126 0.051 1 183 34 34 LEU CB C 43.521 0.006 1 184 34 34 LEU N N 126.227 0.011 1 185 35 35 VAL H H 8.554 0.002 1 186 35 35 VAL C C 176.223 0.001 1 187 35 35 VAL CA C 61.166 0.028 1 188 35 35 VAL CB C 32.676 0.006 1 189 35 35 VAL N N 127.439 0.031 1 190 36 36 VAL H H 8.865 0.002 1 191 36 36 VAL C C 174.229 0.003 1 192 36 36 VAL CA C 60.178 0.04 1 193 36 36 VAL CB C 31.321 0.037 1 194 36 36 VAL N N 129.056 0.017 1 195 37 37 ASP H H 8.907 0.003 1 196 37 37 ASP C C 176.388 0.003 1 197 37 37 ASP CA C 53.373 0.016 1 198 37 37 ASP CB C 39.954 0.015 1 199 37 37 ASP N N 126.471 0.011 1 200 38 38 LEU H H 8.435 0.003 1 201 38 38 LEU C C 177.766 0.006 1 202 38 38 LEU CA C 54.894 0.048 1 203 38 38 LEU CB C 39.495 0.019 1 204 38 38 LEU N N 125.237 0.043 1 205 39 39 SER H H 8.646 0.002 1 206 39 39 SER C C 174.054 0.012 1 207 39 39 SER CA C 61.091 0.027 1 208 39 39 SER CB C 63.240 0.043 1 209 39 39 SER N N 120.228 0.024 1 210 40 40 THR H H 6.581 0.003 1 211 40 40 THR C C 174.628 0.018 1 212 40 40 THR CA C 61.071 0.078 1 213 40 40 THR CB C 68.975 0.008 1 214 40 40 THR N N 105.445 0.019 1 215 41 41 GLN H H 7.499 0.001 1 216 41 41 GLN HE21 H 6.729 0.003 2 217 41 41 GLN HE22 H 7.380 0.001 2 218 41 41 GLN C C 173.931 0.005 1 219 41 41 GLN CA C 55.781 0.054 1 220 41 41 GLN CB C 32.584 0.056 1 221 41 41 GLN CG C 32.643 0.056 1 222 41 41 GLN CD C 178.206 0.004 1 223 41 41 GLN N N 117.168 0.025 1 224 41 41 GLN NE2 N 112.217 0.003 1 225 42 42 ILE H H 7.137 0.002 1 226 42 42 ILE C C 172.374 0.005 1 227 42 42 ILE CA C 61.340 0.055 1 228 42 42 ILE CB C 40.586 0.016 1 229 42 42 ILE N N 118.031 0.014 1 230 43 43 PHE H H 8.479 0.003 1 231 43 43 PHE C C 175.235 0.002 1 232 43 43 PHE CA C 55.294 0.038 1 233 43 43 PHE CB C 43.014 0.029 1 234 43 43 PHE N N 123.407 0.01 1 235 44 44 CYS H H 9.118 0.002 1 236 44 44 CYS C C 172.606 0.005 1 237 44 44 CYS CA C 55.797 0.023 1 238 44 44 CYS CB C 49.811 0.051 1 239 44 44 CYS N N 117.980 0.024 1 240 45 45 HIS H H 7.383 0.003 1 241 45 45 HIS C C 169.761 0.003 1 242 45 45 HIS CA C 55.322 0.028 1 243 45 45 HIS CB C 31.720 0.031 1 244 45 45 HIS N N 112.619 0.036 1 245 46 46 ASN H H 7.689 0.003 1 246 46 46 ASN C C 175.760 0.003 1 247 46 46 ASN CA C 51.771 0.081 1 248 46 46 ASN CB C 40.944 0.026 1 249 46 46 ASN N N 118.436 0.039 1 250 47 47 ASP H H 8.927 0.003 1 251 47 47 ASP C C 175.573 . 1 252 47 47 ASP CA C 56.988 0.037 1 253 47 47 ASP CB C 44.692 0.02 1 254 47 47 ASP N N 123.214 0.034 1 255 48 48 TYR H H 9.098 0.003 1 256 48 48 TYR C C 172.923 . 1 257 48 48 TYR CA C 55.457 0.007 1 258 48 48 TYR CB C 38.943 . 1 259 48 48 TYR N N 118.800 0.022 1 260 49 49 PRO C C 177.597 0.004 1 261 49 49 PRO CA C 64.661 0.053 1 262 49 49 PRO CB C 31.442 0.075 1 263 50 50 GLU H H 8.954 0.002 1 264 50 50 GLU C C 177.636 0.003 1 265 50 50 GLU CA C 59.549 0.047 1 266 50 50 GLU CB C 28.686 0.042 1 267 50 50 GLU N N 118.616 0.005 1 268 51 51 THR H H 7.447 0.002 1 269 51 51 THR C C 173.879 0.009 1 270 51 51 THR CA C 61.810 0.041 1 271 51 51 THR CB C 71.033 0.009 1 272 51 51 THR N N 105.965 0.009 1 273 52 52 ILE H H 8.210 0.002 1 274 52 52 ILE C C 175.460 0.007 1 275 52 52 ILE CA C 61.312 0.027 1 276 52 52 ILE CB C 41.182 0.014 1 277 52 52 ILE N N 123.923 0.023 1 278 53 53 THR H H 8.427 0.001 1 279 53 53 THR C C 170.875 0.01 1 280 53 53 THR CA C 63.201 0.025 1 281 53 53 THR CB C 69.986 0.003 1 282 53 53 THR N N 123.946 0.013 1 283 54 54 ASP H H 6.836 0.005 1 284 54 54 ASP C C 174.499 0.028 1 285 54 54 ASP CA C 54.073 0.049 1 286 54 54 ASP CB C 44.082 0.011 1 287 54 54 ASP N N 124.912 0.049 1 288 55 55 TYR H H 8.733 0.003 1 289 55 55 TYR C C 175.984 0.005 1 290 55 55 TYR CA C 54.766 0.057 1 291 55 55 TYR CB C 40.353 0.045 1 292 55 55 TYR N N 120.952 0.037 1 293 56 56 VAL H H 9.186 0.003 1 294 56 56 VAL C C 177.363 0.007 1 295 56 56 VAL CA C 60.979 0.027 1 296 56 56 VAL CB C 35.841 0.03 1 297 56 56 VAL N N 121.366 0.061 1 298 57 57 THR H H 9.572 0.003 1 299 57 57 THR C C 173.853 0.009 1 300 57 57 THR CA C 59.663 0.036 1 301 57 57 THR CB C 70.978 0.009 1 302 57 57 THR N N 123.562 0.04 1 303 58 58 LEU H H 7.346 0.002 1 304 58 58 LEU C C 175.175 0.002 1 305 58 58 LEU CA C 54.496 0.023 1 306 58 58 LEU CB C 40.791 0.05 1 307 58 58 LEU N N 120.246 0.022 1 308 59 59 GLN H H 9.143 0.002 1 309 59 59 GLN HE21 H 7.152 0.002 2 310 59 59 GLN HE22 H 6.529 0.003 2 311 59 59 GLN C C 175.195 0.011 1 312 59 59 GLN CA C 58.551 0.018 1 313 59 59 GLN CB C 29.633 0.069 1 314 59 59 GLN CG C 33.478 0.075 1 315 59 59 GLN CD C 177.454 0.01 1 316 59 59 GLN N N 130.874 0.044 1 317 59 59 GLN NE2 N 108.481 0.001 1 318 60 60 ARG H H 7.051 0.002 1 319 60 60 ARG C C 173.606 0.006 1 320 60 60 ARG CA C 55.676 0.049 1 321 60 60 ARG CB C 33.723 0.02 1 322 60 60 ARG N N 112.690 0.018 1 323 61 61 GLY H H 9.253 0.002 1 324 61 61 GLY C C 171.706 0.004 1 325 61 61 GLY CA C 45.823 0.039 1 326 61 61 GLY N N 112.630 0.022 1 327 62 62 SER H H 9.072 0.003 1 328 62 62 SER C C 171.379 0.008 1 329 62 62 SER CA C 57.663 0.02 1 330 62 62 SER CB C 65.777 0.022 1 331 62 62 SER N N 122.131 0.03 1 332 63 63 ALA H H 8.059 0.001 1 333 63 63 ALA C C 173.964 0.004 1 334 63 63 ALA CA C 50.522 0.042 1 335 63 63 ALA CB C 22.439 0.027 1 336 63 63 ALA N N 125.762 0.036 1 337 64 64 TYR H H 7.557 0.002 1 338 64 64 TYR C C 175.982 0.014 1 339 64 64 TYR CA C 57.529 0.023 1 340 64 64 TYR CB C 44.389 0.057 1 341 64 64 TYR N N 116.054 0.017 1 342 65 65 GLY H H 8.869 0.003 1 343 65 65 GLY C C 176.808 0.009 1 344 65 65 GLY CA C 47.088 0.04 1 345 65 65 GLY N N 108.217 0.009 1 346 66 66 GLY H H 9.571 0.001 1 347 66 66 GLY C C 176.947 0.015 1 348 66 66 GLY CA C 46.745 0.019 1 349 66 66 GLY N N 114.428 0.016 1 350 67 67 VAL H H 7.598 0.001 1 351 67 67 VAL C C 176.326 0.004 1 352 67 67 VAL CA C 66.613 0.059 1 353 67 67 VAL CB C 31.007 0.019 1 354 67 67 VAL N N 119.579 0.043 1 355 68 68 LEU H H 6.491 0.003 1 356 68 68 LEU C C 178.715 0.003 1 357 68 68 LEU CA C 56.610 0.016 1 358 68 68 LEU CB C 41.431 0.003 1 359 68 68 LEU N N 118.609 0.011 1 360 69 69 SER H H 7.797 0.001 1 361 69 69 SER C C 176.031 0.021 1 362 69 69 SER CA C 61.014 0.074 1 363 69 69 SER CB C 64.127 0.059 1 364 69 69 SER N N 109.098 0.017 1 365 70 70 ASN H H 8.023 0.002 1 366 70 70 ASN HD21 H 7.872 0.001 2 367 70 70 ASN HD22 H 7.281 0.004 2 368 70 70 ASN C C 174.160 0.012 1 369 70 70 ASN CA C 54.181 0.013 1 370 70 70 ASN CB C 41.374 0.071 1 371 70 70 ASN CG C 176.817 0.009 1 372 70 70 ASN N N 114.099 0.017 1 373 70 70 ASN ND2 N 117.138 0.002 1 374 71 71 PHE H H 7.782 0.002 1 375 71 71 PHE C C 174.579 0.002 1 376 71 71 PHE CA C 57.066 0.014 1 377 71 71 PHE CB C 43.087 0.035 1 378 71 71 PHE N N 116.912 0.01 1 379 72 72 SER H H 9.120 0.002 1 380 72 72 SER C C 174.672 0.007 1 381 72 72 SER CA C 56.889 0.042 1 382 72 72 SER CB C 65.350 0.013 1 383 72 72 SER N N 115.214 0.016 1 384 73 73 GLY H H 8.868 0.001 1 385 73 73 GLY C C 172.278 0.003 1 386 73 73 GLY CA C 46.664 0.02 1 387 73 73 GLY N N 109.593 0.017 1 388 74 74 THR H H 8.619 0.002 1 389 74 74 THR C C 172.631 0.004 1 390 74 74 THR CA C 60.576 0.045 1 391 74 74 THR CB C 73.562 0.009 1 392 74 74 THR N N 111.776 0.039 1 393 75 75 VAL H H 9.501 0.003 1 394 75 75 VAL C C 172.709 0.007 1 395 75 75 VAL CA C 58.126 0.035 1 396 75 75 VAL CB C 34.914 0.024 1 397 75 75 VAL N N 119.669 0.024 1 398 76 76 LYS H H 9.406 0.003 1 399 76 76 LYS C C 175.775 0.002 1 400 76 76 LYS CA C 54.395 0.036 1 401 76 76 LYS CB C 34.284 0.033 1 402 76 76 LYS N N 128.126 0.023 1 403 77 77 TYR H H 9.289 0.003 1 404 77 77 TYR C C 176.263 0.011 1 405 77 77 TYR CA C 55.908 0.041 1 406 77 77 TYR CB C 41.307 0.003 1 407 77 77 TYR N N 125.385 0.014 1 408 78 78 SER H H 8.800 0.003 1 409 78 78 SER CA C 58.025 0.008 1 410 78 78 SER CB C 62.707 . 1 411 78 78 SER N N 125.202 0.032 1 412 79 79 GLY C C 174.211 0.006 1 413 79 79 GLY CA C 45.592 0.022 1 414 80 80 SER H H 7.429 0.002 1 415 80 80 SER C C 171.523 0.004 1 416 80 80 SER CA C 58.188 0.027 1 417 80 80 SER CB C 65.763 0.048 1 418 80 80 SER N N 117.153 0.022 1 419 81 81 SER H H 8.250 0.001 1 420 81 81 SER C C 172.710 0.003 1 421 81 81 SER CA C 58.404 0.059 1 422 81 81 SER CB C 64.677 0.056 1 423 81 81 SER N N 117.966 0.021 1 424 82 82 TYR H H 9.140 0.003 1 425 82 82 TYR C C 172.301 . 1 426 82 82 TYR CA C 55.761 0.012 1 427 82 82 TYR CB C 39.931 . 1 428 82 82 TYR N N 123.636 0.023 1 429 83 83 PRO C C 173.657 0.011 1 430 83 83 PRO CA C 64.079 0.083 1 431 83 83 PRO CB C 32.264 0.026 1 432 84 84 PHE H H 7.424 0.002 1 433 84 84 PHE C C 173.155 . 1 434 84 84 PHE CA C 55.017 0.006 1 435 84 84 PHE CB C 43.115 . 1 436 84 84 PHE N N 119.228 0.019 1 437 85 85 PRO C C 175.862 0.007 1 438 85 85 PRO CA C 62.724 0.021 1 439 85 85 PRO CB C 34.824 0.023 1 440 86 86 THR H H 8.268 0.001 1 441 86 86 THR C C 176.303 0.01 1 442 86 86 THR CA C 61.955 0.038 1 443 86 86 THR CB C 70.755 0.048 1 444 86 86 THR N N 113.513 0.021 1 445 87 87 THR H H 8.706 0.004 1 446 87 87 THR C C 174.367 0.001 1 447 87 87 THR CA C 60.974 0.023 1 448 87 87 THR CB C 69.517 0.03 1 449 87 87 THR N N 110.066 0.033 1 450 88 88 SER H H 7.610 0.001 1 451 88 88 SER C C 172.383 0.004 1 452 88 88 SER CA C 57.565 0.049 1 453 88 88 SER CB C 64.829 0.016 1 454 88 88 SER N N 116.089 0.006 1 455 89 89 GLU H H 8.338 0.004 1 456 89 89 GLU C C 176.774 0.006 1 457 89 89 GLU CA C 56.060 0.08 1 458 89 89 GLU CB C 30.784 0.07 1 459 89 89 GLU N N 124.387 0.035 1 460 90 90 THR H H 7.500 0.002 1 461 90 90 THR C C 172.531 . 1 462 90 90 THR CA C 61.724 0.037 1 463 90 90 THR CB C 69.208 . 1 464 90 90 THR N N 116.842 0.026 1 465 91 91 PRO C C 175.965 0.002 1 466 91 91 PRO CA C 62.759 0.036 1 467 91 91 PRO CB C 32.553 0.012 1 468 92 92 ARG H H 8.147 0.001 1 469 92 92 ARG C C 176.962 0.009 1 470 92 92 ARG CA C 55.610 0.041 1 471 92 92 ARG CB C 32.149 0.041 1 472 92 92 ARG N N 117.423 0.022 1 473 93 93 VAL H H 9.153 0.003 1 474 93 93 VAL C C 175.482 0.003 1 475 93 93 VAL CA C 61.304 0.043 1 476 93 93 VAL CB C 34.813 0.023 1 477 93 93 VAL N N 121.163 0.009 1 478 94 94 VAL H H 8.422 0.002 1 479 94 94 VAL C C 176.171 0.001 1 480 94 94 VAL CA C 62.321 0.026 1 481 94 94 VAL CB C 33.264 0.015 1 482 94 94 VAL N N 125.334 0.023 1 483 95 95 TYR H H 9.070 0.003 1 484 95 95 TYR C C 176.261 . 1 485 95 95 TYR CA C 58.158 0.0 1 486 95 95 TYR CB C 40.325 . 1 487 95 95 TYR N N 126.315 0.028 1 488 96 96 ASN HD21 H 7.551 0.001 2 489 96 96 ASN HD22 H 6.799 0.003 2 490 96 96 ASN C C 173.019 0.01 1 491 96 96 ASN CA C 52.581 0.042 1 492 96 96 ASN CB C 38.728 0.053 1 493 96 96 ASN CG C 177.059 0.022 1 494 96 96 ASN ND2 N 110.409 0.01 1 495 97 97 SER H H 7.328 0.002 1 496 97 97 SER C C 174.387 . 1 497 97 97 SER CA C 56.472 0.05 1 498 97 97 SER CB C 64.864 . 1 499 97 97 SER N N 109.609 0.013 1 500 98 98 ARG C C 176.122 0.005 1 501 98 98 ARG CA C 57.646 0.028 1 502 98 98 ARG CB C 30.708 0.006 1 503 99 99 THR H H 8.267 0.001 1 504 99 99 THR C C 173.856 0.012 1 505 99 99 THR CA C 62.808 0.039 1 506 99 99 THR CB C 69.317 0.044 1 507 99 99 THR N N 117.049 0.028 1 508 100 100 ASP H H 8.392 0.001 1 509 100 100 ASP C C 175.723 0.014 1 510 100 100 ASP CA C 56.093 0.011 1 511 100 100 ASP CB C 41.318 0.027 1 512 100 100 ASP N N 126.184 0.013 1 513 101 101 LYS H H 9.309 0.003 1 514 101 101 LYS C C 173.802 . 1 515 101 101 LYS CA C 52.819 0.05 1 516 101 101 LYS CB C 35.027 . 1 517 101 101 LYS N N 124.488 0.017 1 518 102 102 PRO C C 177.234 0.0 1 519 102 102 PRO CA C 62.830 0.056 1 520 102 102 PRO CB C 33.202 0.038 1 521 103 103 TRP H H 8.265 0.001 1 522 103 103 TRP HE1 H 8.969 . 1 523 103 103 TRP C C 176.071 . 1 524 103 103 TRP CA C 52.745 0.049 1 525 103 103 TRP CB C 28.095 . 1 526 103 103 TRP N N 128.228 0.023 1 527 103 103 TRP NE1 N 127.951 . 1 528 104 104 PRO C C 173.024 0.006 1 529 104 104 PRO CA C 62.827 0.05 1 530 104 104 PRO CB C 28.857 0.057 1 531 105 105 VAL H H 8.017 0.001 1 532 105 105 VAL C C 173.493 0.002 1 533 105 105 VAL CA C 60.169 0.022 1 534 105 105 VAL CB C 35.058 0.063 1 535 105 105 VAL N N 125.652 0.008 1 536 106 106 ALA H H 8.294 0.002 1 537 106 106 ALA C C 175.167 0.012 1 538 106 106 ALA CA C 50.822 0.025 1 539 106 106 ALA CB C 22.800 0.076 1 540 106 106 ALA N N 125.856 0.031 1 541 107 107 LEU H H 8.567 0.001 1 542 107 107 LEU C C 174.576 0.002 1 543 107 107 LEU CA C 53.048 0.022 1 544 107 107 LEU CB C 42.511 0.037 1 545 107 107 LEU N N 119.996 0.015 1 546 108 108 TYR H H 8.871 0.003 1 547 108 108 TYR C C 175.028 0.002 1 548 108 108 TYR CA C 57.675 0.023 1 549 108 108 TYR CB C 38.961 0.003 1 550 108 108 TYR N N 123.117 0.01 1 551 109 109 LEU H H 8.947 0.002 1 552 109 109 LEU C C 175.531 0.012 1 553 109 109 LEU CA C 52.866 0.018 1 554 109 109 LEU CB C 44.804 0.051 1 555 109 109 LEU N N 124.850 0.026 1 556 110 110 THR H H 9.581 0.003 1 557 110 110 THR C C 172.172 . 1 558 110 110 THR CA C 58.077 0.035 1 559 110 110 THR CB C 72.402 . 1 560 110 110 THR N N 120.308 0.009 1 561 111 111 PRO C C 177.761 0.003 1 562 111 111 PRO CA C 62.870 0.036 1 563 111 111 PRO CB C 32.166 0.005 1 564 112 112 VAL H H 7.988 0.001 1 565 112 112 VAL C C 177.048 0.007 1 566 112 112 VAL CA C 61.215 0.022 1 567 112 112 VAL CB C 31.924 0.067 1 568 112 112 VAL N N 117.994 0.028 1 569 113 113 SER H H 8.285 0.003 1 570 113 113 SER C C 174.640 0.009 1 571 113 113 SER CA C 60.521 0.045 1 572 113 113 SER CB C 63.223 0.004 1 573 113 113 SER N N 114.957 0.035 1 574 114 114 SER H H 7.635 0.002 1 575 114 114 SER C C 174.237 0.004 1 576 114 114 SER CA C 57.651 0.02 1 577 114 114 SER CB C 63.596 0.06 1 578 114 114 SER N N 112.671 0.02 1 579 115 115 ALA H H 7.720 0.002 1 580 115 115 ALA C C 176.969 0.003 1 581 115 115 ALA CA C 52.464 0.028 1 582 115 115 ALA CB C 19.880 0.052 1 583 115 115 ALA N N 126.161 0.026 1 584 116 116 GLY H H 8.061 0.001 1 585 116 116 GLY C C 173.416 0.01 1 586 116 116 GLY CA C 45.911 0.052 1 587 116 116 GLY N N 106.324 0.027 1 588 117 117 GLY H H 8.612 0.002 1 589 117 117 GLY C C 173.996 0.008 1 590 117 117 GLY CA C 44.595 0.035 1 591 117 117 GLY N N 111.594 0.029 1 592 118 118 VAL H H 8.563 0.001 1 593 118 118 VAL C C 175.276 0.012 1 594 118 118 VAL CA C 64.363 0.038 1 595 118 118 VAL CB C 30.360 0.052 1 596 118 118 VAL N N 122.311 0.017 1 597 119 119 ALA H H 9.024 0.002 1 598 119 119 ALA C C 177.390 0.005 1 599 119 119 ALA CA C 52.464 0.03 1 600 119 119 ALA CB C 21.445 0.069 1 601 119 119 ALA N N 134.777 0.047 1 602 120 120 ILE H H 7.539 0.002 1 603 120 120 ILE C C 174.079 0.003 1 604 120 120 ILE CA C 60.904 0.087 1 605 120 120 ILE CB C 42.590 0.008 1 606 120 120 ILE N N 115.525 0.008 1 607 121 121 LYS H H 8.335 0.001 1 608 121 121 LYS C C 177.269 0.008 1 609 121 121 LYS CA C 54.429 0.018 1 610 121 121 LYS CB C 33.881 0.038 1 611 121 121 LYS N N 125.381 0.011 1 612 122 122 ALA H H 9.770 0.003 1 613 122 122 ALA C C 177.861 0.001 1 614 122 122 ALA CA C 54.164 0.022 1 615 122 122 ALA CB C 18.531 0.076 1 616 122 122 ALA N N 128.993 0.02 1 617 123 123 GLY H H 8.976 0.002 1 618 123 123 GLY C C 174.061 0.024 1 619 123 123 GLY CA C 45.468 0.051 1 620 123 123 GLY N N 111.804 0.02 1 621 124 124 SER H H 7.997 0.001 1 622 124 124 SER C C 172.816 0.003 1 623 124 124 SER CA C 57.954 0.075 1 624 124 124 SER CB C 65.389 0.011 1 625 124 124 SER N N 114.875 0.031 1 626 125 125 LEU H H 8.182 0.003 1 627 125 125 LEU C C 177.498 0.009 1 628 125 125 LEU CA C 55.193 0.081 1 629 125 125 LEU CB C 42.144 0.068 1 630 125 125 LEU N N 123.719 0.027 1 631 126 126 ILE H H 9.016 0.006 1 632 126 126 ILE C C 175.537 0.007 1 633 126 126 ILE CA C 60.955 0.107 1 634 126 126 ILE CB C 39.941 0.042 1 635 126 126 ILE N N 119.630 0.04 1 636 127 127 ALA H H 7.631 0.003 1 637 127 127 ALA C C 174.689 0.003 1 638 127 127 ALA CA C 51.887 0.013 1 639 127 127 ALA CB C 21.263 0.062 1 640 127 127 ALA N N 120.143 0.049 1 641 128 128 VAL H H 8.473 0.001 1 642 128 128 VAL C C 176.058 0.009 1 643 128 128 VAL CA C 62.413 0.087 1 644 128 128 VAL CB C 35.274 0.022 1 645 128 128 VAL N N 118.998 0.036 1 646 129 129 LEU H H 9.334 0.003 1 647 129 129 LEU C C 174.399 0.018 1 648 129 129 LEU CA C 53.347 0.046 1 649 129 129 LEU CB C 44.667 0.022 1 650 129 129 LEU N N 128.491 0.015 1 651 130 130 ILE H H 9.004 0.003 1 652 130 130 ILE C C 173.944 0.008 1 653 130 130 ILE CA C 61.503 0.092 1 654 130 130 ILE CB C 38.798 0.048 1 655 130 130 ILE N N 121.695 0.012 1 656 131 131 LEU H H 9.284 0.003 1 657 131 131 LEU C C 174.609 0.008 1 658 131 131 LEU CA C 54.421 0.019 1 659 131 131 LEU CB C 43.795 0.036 1 660 131 131 LEU N N 134.610 0.021 1 661 132 132 ARG H H 8.975 0.003 1 662 132 132 ARG C C 173.797 0.003 1 663 132 132 ARG CA C 54.595 0.058 1 664 132 132 ARG CB C 32.317 0.081 1 665 132 132 ARG N N 129.932 0.026 1 666 133 133 GLN H H 9.403 0.003 1 667 133 133 GLN HE21 H 6.010 0.002 2 668 133 133 GLN HE22 H 6.922 0.0 2 669 133 133 GLN C C 173.415 0.017 1 670 133 133 GLN CA C 54.470 0.026 1 671 133 133 GLN CB C 29.581 0.033 1 672 133 133 GLN CD C 178.286 0.011 1 673 133 133 GLN N N 132.708 0.018 1 674 133 133 GLN NE2 N 110.161 0.0 1 675 134 134 THR H H 8.795 0.003 1 676 134 134 THR C C 174.836 0.023 1 677 134 134 THR CA C 59.937 0.063 1 678 134 134 THR CB C 72.348 0.075 1 679 134 134 THR N N 117.756 0.013 1 680 135 135 ASN H H 9.716 0.006 1 681 135 135 ASN HD21 H 7.715 0.006 2 682 135 135 ASN HD22 H 7.559 0.004 2 683 135 135 ASN C C 175.370 0.001 1 684 135 135 ASN CA C 54.249 0.04 1 685 135 135 ASN CB C 41.810 0.056 1 686 135 135 ASN CG C 177.841 0.001 1 687 135 135 ASN N N 117.675 0.022 1 688 135 135 ASN ND2 N 116.713 0.0 1 689 136 136 ASN H H 8.263 0.001 1 690 136 136 ASN HD21 H 7.094 0.0 2 691 136 136 ASN HD22 H 7.701 0.001 2 692 136 136 ASN C C 175.309 0.017 1 693 136 136 ASN CA C 52.321 0.07 1 694 136 136 ASN CB C 38.424 0.028 1 695 136 136 ASN CG C 178.566 0.034 1 696 136 136 ASN N N 115.866 0.013 1 697 136 136 ASN ND2 N 112.158 0.004 1 698 137 137 TYR H H 9.152 0.003 1 699 137 137 TYR C C 174.313 0.024 1 700 137 137 TYR CA C 58.841 0.041 1 701 137 137 TYR CB C 43.994 0.072 1 702 137 137 TYR N N 122.996 0.06 1 703 138 138 ASN H H 9.352 0.004 1 704 138 138 ASN HD21 H 6.906 0.003 2 705 138 138 ASN HD22 H 7.625 0.004 2 706 138 138 ASN C C 175.719 0.016 1 707 138 138 ASN CA C 51.819 0.038 1 708 138 138 ASN CB C 38.992 0.063 1 709 138 138 ASN CG C 177.029 0.006 1 710 138 138 ASN N N 121.334 0.05 1 711 138 138 ASN ND2 N 111.295 0.004 1 712 139 139 SER H H 7.778 0.005 1 713 139 139 SER C C 174.388 0.011 1 714 139 139 SER CA C 57.805 0.09 1 715 139 139 SER CB C 63.558 0.081 1 716 139 139 SER N N 111.578 0.031 1 717 140 140 ASP H H 7.675 0.002 1 718 140 140 ASP C C 175.350 0.005 1 719 140 140 ASP CA C 55.816 0.057 1 720 140 140 ASP CB C 40.903 0.005 1 721 140 140 ASP N N 124.119 0.048 1 722 141 141 ASP H H 6.605 0.006 1 723 141 141 ASP C C 175.122 0.006 1 724 141 141 ASP CA C 53.177 0.082 1 725 141 141 ASP CB C 40.061 0.037 1 726 141 141 ASP N N 121.697 0.02 1 727 142 142 PHE H H 8.915 0.003 1 728 142 142 PHE C C 175.089 0.009 1 729 142 142 PHE CA C 54.673 0.016 1 730 142 142 PHE CB C 43.111 0.024 1 731 142 142 PHE N N 123.160 0.023 1 732 143 143 GLN H H 8.761 0.002 1 733 143 143 GLN HE21 H 6.534 0.005 2 734 143 143 GLN HE22 H 7.684 0.001 2 735 143 143 GLN C C 174.811 0.008 1 736 143 143 GLN CA C 54.752 0.07 1 737 143 143 GLN CB C 31.170 0.062 1 738 143 143 GLN CG C 34.215 0.031 1 739 143 143 GLN CD C 180.241 0.015 1 740 143 143 GLN N N 118.031 0.01 1 741 143 143 GLN NE2 N 112.170 0.001 1 742 144 144 PHE H H 9.863 0.004 1 743 144 144 PHE C C 172.375 0.003 1 744 144 144 PHE CA C 56.457 0.052 1 745 144 144 PHE CB C 39.723 0.022 1 746 144 144 PHE N N 127.270 0.03 1 747 145 145 VAL H H 8.708 0.003 1 748 145 145 VAL C C 173.158 0.002 1 749 145 145 VAL CA C 63.047 0.075 1 750 145 145 VAL CB C 32.162 0.005 1 751 145 145 VAL N N 125.147 0.028 1 752 146 146 TRP H H 8.701 0.002 1 753 146 146 TRP HE1 H 7.009 . 1 754 146 146 TRP C C 174.631 0.005 1 755 146 146 TRP CA C 53.991 0.02 1 756 146 146 TRP CB C 30.070 0.039 1 757 146 146 TRP N N 126.648 0.041 1 758 146 146 TRP NE1 N 122.557 . 1 759 147 147 ASN H H 8.935 0.003 1 760 147 147 ASN HD21 H 6.599 0.001 2 761 147 147 ASN HD22 H 6.226 0.001 2 762 147 147 ASN C C 172.928 0.005 1 763 147 147 ASN CA C 52.966 0.066 1 764 147 147 ASN CB C 39.920 0.064 1 765 147 147 ASN CG C 175.187 0.012 1 766 147 147 ASN N N 124.870 0.021 1 767 147 147 ASN ND2 N 110.551 0.01 1 768 148 148 ILE H H 9.156 0.002 1 769 148 148 ILE C C 173.669 0.009 1 770 148 148 ILE CA C 58.891 0.067 1 771 148 148 ILE CB C 35.730 0.048 1 772 148 148 ILE N N 124.491 0.017 1 773 149 149 TYR H H 9.248 0.004 1 774 149 149 TYR C C 175.362 0.006 1 775 149 149 TYR CA C 56.333 0.082 1 776 149 149 TYR CB C 42.296 0.024 1 777 149 149 TYR N N 127.266 0.027 1 778 150 150 ALA H H 8.496 0.002 1 779 150 150 ALA C C 179.237 0.002 1 780 150 150 ALA CA C 51.442 0.026 1 781 150 150 ALA CB C 21.022 0.079 1 782 150 150 ALA N N 122.228 0.024 1 783 151 151 ASN H H 9.051 0.002 1 784 151 151 ASN HD21 H 6.475 0.004 2 785 151 151 ASN HD22 H 7.318 0.002 2 786 151 151 ASN C C 174.782 0.004 1 787 151 151 ASN CA C 53.111 0.087 1 788 151 151 ASN CB C 39.447 0.045 1 789 151 151 ASN CG C 175.427 0.017 1 790 151 151 ASN N N 119.998 0.016 1 791 151 151 ASN ND2 N 109.287 0.001 1 792 152 152 ASN H H 7.313 0.002 1 793 152 152 ASN HD21 H 7.087 0.003 2 794 152 152 ASN HD22 H 7.158 0.002 2 795 152 152 ASN C C 170.990 0.009 1 796 152 152 ASN CA C 52.171 0.047 1 797 152 152 ASN CB C 41.840 0.032 1 798 152 152 ASN CG C 176.337 0.005 1 799 152 152 ASN N N 110.829 0.026 1 800 152 152 ASN ND2 N 114.866 0.002 1 801 153 153 ASP H H 8.409 0.001 1 802 153 153 ASP C C 177.780 0.005 1 803 153 153 ASP CA C 53.852 0.042 1 804 153 153 ASP CB C 42.077 0.035 1 805 153 153 ASP N N 117.123 0.033 1 806 154 154 VAL H H 8.749 0.002 1 807 154 154 VAL C C 175.226 0.0 1 808 154 154 VAL CA C 61.736 0.024 1 809 154 154 VAL CB C 35.169 0.028 1 810 154 154 VAL N N 121.095 0.027 1 811 155 155 VAL H H 8.630 0.002 1 812 155 155 VAL C C 174.380 0.009 1 813 155 155 VAL CA C 60.629 0.028 1 814 155 155 VAL CB C 34.683 0.057 1 815 155 155 VAL N N 128.403 0.03 1 816 156 156 VAL H H 8.426 0.001 1 817 156 156 VAL C C 175.106 . 1 818 156 156 VAL CA C 57.590 0.009 1 819 156 156 VAL CB C 33.808 . 1 820 156 156 VAL N N 126.838 0.025 1 821 157 157 PRO C C 176.613 0.008 1 822 157 157 PRO CA C 63.013 0.075 1 823 157 157 PRO CB C 32.415 0.074 1 824 158 158 THR H H 8.128 0.001 1 825 158 158 THR C C 175.057 0.007 1 826 158 158 THR CA C 61.582 0.06 1 827 158 158 THR CB C 70.006 0.006 1 828 158 158 THR N N 113.949 0.03 1 829 159 159 GLY H H 8.312 0.001 1 830 159 159 GLY C C 173.710 0.006 1 831 159 159 GLY CA C 45.186 0.022 1 832 159 159 GLY N N 110.766 0.012 1 833 160 160 LEU H H 8.108 0.0 1 834 160 160 LEU C C 177.095 0.004 1 835 160 160 LEU CA C 55.069 0.009 1 836 160 160 LEU CB C 42.420 0.024 1 837 160 160 LEU N N 121.722 0.008 1 838 161 161 VAL H H 8.043 0.001 1 839 161 161 VAL C C 174.311 . 1 840 161 161 VAL CA C 59.721 0.009 1 841 161 161 VAL CB C 32.539 . 1 842 161 161 VAL N N 122.669 0.038 1 843 162 162 PRO C C 176.908 . 1 844 162 162 PRO CA C 63.052 0.057 1 845 162 162 PRO CB C 31.950 0.099 1 846 163 163 ARG H H 8.416 0.001 1 847 163 163 ARG C C 177.006 0.017 1 848 163 163 ARG CA C 56.462 0.029 1 849 163 163 ARG CB C 30.747 0.07 1 850 163 163 ARG N N 121.995 0.006 1 851 164 164 GLY H H 8.438 0.007 1 852 164 164 GLY C C 174.142 0.003 1 853 164 164 GLY CA C 45.210 0.025 1 854 164 164 GLY N N 110.170 0.026 1 855 165 165 SER H H 8.125 0.003 1 856 165 165 SER C C 174.677 0.002 1 857 165 165 SER CA C 58.485 0.034 1 858 165 165 SER CB C 63.776 0.001 1 859 165 165 SER N N 115.492 0.01 1 860 166 166 LEU H H 8.246 0.001 1 861 166 166 LEU C C 177.336 0.012 1 862 166 166 LEU CA C 55.300 0.035 1 863 166 166 LEU CB C 42.073 0.016 1 864 166 166 LEU N N 123.667 0.008 1 865 167 167 GLU H H 8.189 0.0 1 866 167 167 GLU C C 176.124 0.01 1 867 167 167 GLU CA C 56.705 0.027 1 868 167 167 GLU CB C 30.200 0.035 1 869 167 167 GLU N N 120.619 0.014 1 870 168 168 HIS H H 8.089 0.003 1 871 168 168 HIS C C 175.119 . 1 872 168 168 HIS CA C 56.222 0.021 1 873 168 168 HIS CB C 30.637 . 1 874 168 168 HIS N N 119.758 0.01 1 stop_ save_