data_25063 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The backbone chemical shift assignments of [ZnZn]-IMP-1 metallo-beta-lactamase ; _BMRB_accession_number 25063 _BMRB_flat_file_name bmr25063.str _Entry_type original _Submission_date 2014-07-02 _Accession_date 2014-07-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The chemical shift assignments of [ZnZn]-IMP-1 metallo-beta-lactamase.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Carruthers Thomas J. . 2 Otting Gottfried . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 196 "13C chemical shifts" 555 "15N chemical shifts" 196 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-01-27 update author 'update entry citation' 2014-08-26 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25080 'The chemical shift assignments of [FeZn]-IMP-1 metallo-beta-lactamase.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Iron(III) Located in the Dinuclear Metallo-beta-Lactamase IMP-1 by Pseudocontact Shifts.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25320022 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Carruthers Thomas J. . 2 Carr Paul D. . 3 Loh Choy-Theng . . 4 Jackson Colin J . 5 Otting Gottfried . . stop_ _Journal_abbreviation 'Angew. Chem. Int. Ed.' _Journal_name_full 'Angewandte Chemie International Edition' _Journal_volume 53 _Journal_issue 51 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14269 _Page_last 14272 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name [ZnZn]-IMP-1 _Enzyme_commission_number 3.5.2.6 loop_ _Mol_system_component_name _Mol_label IMP-1 $IMP-1 Zn1 $entity_ZN Zn2 $entity_ZN stop_ _System_molecular_weight 25747 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'Catalytic break-down of beta-lactam antibiotics' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IMP-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IMP-1 _Molecular_mass 25628.3184 _Mol_thiol_state 'all other bound' loop_ _Biological_function 'beta-lactam hydrolysis' stop_ _Details 'Sample included an N-terminal expression tag (MASMTG) without the transport peptide' ############################## # Polymer residue sequence # ############################## _Residue_count 233 _Mol_residue_sequence ; MASMTGESLPDLKIEKLDEG VYVHTSFEEVNGWGVVPKHG LVVLVNAEAYLIDTPFTAKD TEKLVTWFVERGYKIKGSIS SHFHSDSTGGIEWLNSRSIP TYASELTNELLKKDGKVQAT NSFSGVNYWLVKNKIEVFYP GPGHTPDNVVVWLPERKILF GGCFIKPYGLGNLGDANIEA WPKSAKLLKSKYGKAKLVVP SHSEVGDASLLKLTLEQAVK GLNESKKPSKPSN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -4 MET 2 -3 ALA 3 -2 SER 4 -1 MET 5 0 THR 6 1 GLY 7 2 GLU 8 3 SER 9 4 LEU 10 5 PRO 11 6 ASP 12 7 LEU 13 8 LYS 14 9 ILE 15 10 GLU 16 11 LYS 17 12 LEU 18 13 ASP 19 14 GLU 20 15 GLY 21 16 VAL 22 17 TYR 23 18 VAL 24 19 HIS 25 20 THR 26 21 SER 27 22 PHE 28 23 GLU 29 24 GLU 30 25 VAL 31 26 ASN 32 27 GLY 33 28 TRP 34 29 GLY 35 30 VAL 36 31 VAL 37 32 PRO 38 33 LYS 39 34 HIS 40 35 GLY 41 36 LEU 42 37 VAL 43 38 VAL 44 39 LEU 45 40 VAL 46 41 ASN 47 42 ALA 48 43 GLU 49 44 ALA 50 45 TYR 51 46 LEU 52 47 ILE 53 48 ASP 54 49 THR 55 50 PRO 56 51 PHE 57 52 THR 58 53 ALA 59 54 LYS 60 55 ASP 61 56 THR 62 57 GLU 63 58 LYS 64 59 LEU 65 60 VAL 66 61 THR 67 62 TRP 68 63 PHE 69 64 VAL 70 65 GLU 71 66 ARG 72 67 GLY 73 68 TYR 74 69 LYS 75 70 ILE 76 71 LYS 77 72 GLY 78 73 SER 79 74 ILE 80 75 SER 81 76 SER 82 77 HIS 83 78 PHE 84 79 HIS 85 80 SER 86 81 ASP 87 82 SER 88 83 THR 89 84 GLY 90 85 GLY 91 86 ILE 92 87 GLU 93 88 TRP 94 89 LEU 95 90 ASN 96 91 SER 97 92 ARG 98 93 SER 99 94 ILE 100 95 PRO 101 96 THR 102 97 TYR 103 98 ALA 104 99 SER 105 100 GLU 106 101 LEU 107 102 THR 108 103 ASN 109 104 GLU 110 105 LEU 111 106 LEU 112 107 LYS 113 108 LYS 114 109 ASP 115 110 GLY 116 111 LYS 117 112 VAL 118 113 GLN 119 114 ALA 120 115 THR 121 116 ASN 122 117 SER 123 118 PHE 124 119 SER 125 120 GLY 126 121 VAL 127 122 ASN 128 123 TYR 129 124 TRP 130 125 LEU 131 126 VAL 132 127 LYS 133 128 ASN 134 129 LYS 135 130 ILE 136 131 GLU 137 132 VAL 138 133 PHE 139 134 TYR 140 135 PRO 141 136 GLY 142 137 PRO 143 138 GLY 144 139 HIS 145 140 THR 146 141 PRO 147 142 ASP 148 143 ASN 149 144 VAL 150 145 VAL 151 146 VAL 152 147 TRP 153 148 LEU 154 149 PRO 155 150 GLU 156 151 ARG 157 152 LYS 158 153 ILE 159 154 LEU 160 155 PHE 161 156 GLY 162 157 GLY 163 158 CYS 164 159 PHE 165 160 ILE 166 161 LYS 167 162 PRO 168 163 TYR 169 164 GLY 170 165 LEU 171 166 GLY 172 167 ASN 173 168 LEU 174 169 GLY 175 170 ASP 176 171 ALA 177 172 ASN 178 173 ILE 179 174 GLU 180 175 ALA 181 176 TRP 182 177 PRO 183 178 LYS 184 179 SER 185 180 ALA 186 181 LYS 187 182 LEU 188 183 LEU 189 184 LYS 190 185 SER 191 186 LYS 192 187 TYR 193 188 GLY 194 189 LYS 195 190 ALA 196 191 LYS 197 192 LEU 198 193 VAL 199 194 VAL 200 195 PRO 201 196 SER 202 197 HIS 203 198 SER 204 199 GLU 205 200 VAL 206 201 GLY 207 202 ASP 208 203 ALA 209 204 SER 210 205 LEU 211 206 LEU 212 207 LYS 213 208 LEU 214 209 THR 215 210 LEU 216 211 GLU 217 212 GLN 218 213 ALA 219 214 VAL 220 215 LYS 221 216 GLY 222 217 LEU 223 218 ASN 224 219 GLU 225 220 SER 226 221 LYS 227 222 LYS 228 223 PRO 229 224 SER 230 225 LYS 231 226 PRO 232 227 SER 233 228 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 BMRB 25080 IMP-1 100.00 233 100.00 100.00 7.67e-166 PDB 1DD6 "Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa In Complex With A Mercaptocarboxylate Inhibitor" 97.85 228 99.56 99.56 5.59e-161 PDB 1DDK "Crystal Structure Of Imp-1 Metallo Beta-lactamase From Pseudomonas Aeruginosa" 94.42 220 100.00 100.00 1.47e-155 PDB 1JJE "Imp-1 Metallo Beta-Lactamase From Pseudomonas Aeruginosa In Complex With A Biaryl Succinic Acid Inhibitor (11)" 95.28 222 99.55 99.55 2.40e-156 PDB 1JJT "Imp-1 Metallo Beta-lactamase From Pseudomonas Aeruginosa In Complex With A Biaryl Succinic Acid Inhibitor (1)" 97.85 228 99.56 99.56 5.59e-161 PDB 1VGN "Structure-Based Design Of The Irreversible Inhibitors To Metallo--Lactamase (Imp-1)" 97.85 228 99.56 99.56 5.59e-161 PDB 1WUO "Crystal Structure Of Metallo-beta-lactamase Imp-1 Mutant (d81a)" 97.85 228 98.68 98.68 3.55e-158 PDB 1WUP "Crystal Structure Of Metallo-Beta-Lactamase Imp-1 Mutant (D81e)" 97.85 228 99.12 99.56 2.85e-160 PDB 2DOO "The Structure Of Imp-1 Complexed With The Detecting Reagent (Dansylc4sh) By A Fluorescent Probe" 97.85 228 99.56 99.56 5.59e-161 PDB 3WXC "Crystal Structure Of Imp-1 Metallo-beta-lactamase Complexed With A 3- Aminophtalic Acid Inhibitor" 95.28 222 99.55 99.55 2.40e-156 PDB 4C1F "Crystal Structure Of The Metallo-beta-lactamase Imp-1 With L-captopril" 97.85 228 99.56 99.56 5.59e-161 PDB 4C1G "Crystal Structure Of The Metallo-beta-lactamase Imp-1 With D-captopril" 97.85 228 99.56 99.56 5.59e-161 PDB 4F6H "Mutagenesis Of Zinc Ligand Residue Cys221 Reveals Plasticity In The Imp-1 Metallo-b-lactamase Active Site" 97.85 236 99.12 99.12 1.21e-158 PDB 4F6Z "Mutagenesis Of Zinc Ligand Residue Cys221 Reveals Plasticity In The Imp-1 Metallo-b-lactamase Active Site" 97.85 236 99.12 99.12 1.21e-158 PDB 4UAM "1.8 Angstrom Crystal Structure Of Imp-1 Metallo-beta-lactamase With A Mixed Iron-zinc Center In The Active Site" 94.85 221 99.55 99.55 1.38e-153 DBJ BAA06111 "metallo beta-lactamase [Klebsiella pneumoniae]" 99.14 246 98.27 98.70 1.20e-161 DBJ BAA08930 "metallo-beta-lactamase [Serratia marcescens]" 99.14 246 98.27 98.70 1.20e-161 DBJ BAA23768 "extended-spectrum B-lactamase [Pseudomonas aeruginosa]" 99.14 246 98.27 98.70 1.20e-161 DBJ BAA77393 "bate-Lactamase [Shigella flexneri]" 99.14 246 97.40 97.84 1.32e-159 DBJ BAB15941 "metallo-beta lactamase [Serratia marcescens]" 99.14 246 97.84 98.27 9.99e-161 EMBL CAA11471 "bla-imp [Pseudomonas aeruginosa]" 99.14 246 98.27 98.70 1.20e-161 EMBL CAA67040 "beta-lactamase [Pseudomonas aeruginosa]" 99.14 246 98.27 98.70 1.20e-161 EMBL CAG26809 "metallo-beta-lactamase IMP-1 [Acinetobacter baumannii]" 99.14 246 98.27 98.70 1.20e-161 EMBL CAK55556 "metallo-beta-lactamase IMP-1 [Pseudomonas putida]" 99.14 246 98.27 98.70 1.20e-161 EMBL CAK55562 "metallo-beta-lactamase IMP-1 [Acinetobacter baumannii]" 99.14 246 97.40 98.27 1.41e-159 GB AAB30289 "metallo beta-lactamase [Serratia marcescens]" 99.14 246 98.27 98.70 1.20e-161 GB AAL10407 "IMP-1 metallo-beta-lactamase [Serratia marcescens]" 99.14 246 98.27 98.70 1.20e-161 GB AAL17637 "beta-lactamase IMP-1 [Acinetobacter sp. A1411]" 99.14 246 98.27 98.70 1.20e-161 GB AAN87168 "metallo-beta-lactamase IMP-1 [Pseudomonas aeruginosa]" 99.14 246 98.27 98.70 1.20e-161 GB AAP04478 "metallo-beta-lactamase IMP-1 [Pseudomonas putida]" 99.14 246 98.27 98.70 1.20e-161 REF WP_003159548 "MULTISPECIES: carbapenem-hydrolyzing metallo-beta-lactamase IMP-1 [Proteobacteria]" 99.14 246 98.27 98.70 1.20e-161 REF WP_032490175 "carbapenem-hydrolyzing metallo-beta-lactamase IMP-10 [Pseudomonas aeruginosa]" 99.14 246 97.84 98.27 9.88e-161 REF WP_032492096 "MULTISPECIES: carbapenem-hydrolyzing metallo-beta-lactamase IMP-6 [Gammaproteobacteria]" 99.14 246 97.84 98.27 9.99e-161 REF WP_032492622 "carbapenem-hydrolyzing metallo-beta-lactamase IMP-34 [Klebsiella oxytoca]" 99.14 246 97.84 98.27 2.59e-160 REF WP_057694208 "subclass B1 metallo-beta-lactamase, partial [Acinetobacter baumannii]" 85.84 200 100.00 100.00 6.89e-140 SP P52699 "RecName: Full=Beta-lactamase IMP-1; AltName: Full=BLAIMP; AltName: Full=Beta-lactamase type II; AltName: Full=Penicillinase; Fl" 99.14 246 98.27 98.70 1.20e-161 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'ZINC ION' _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $IMP-1 'Pseudomonas aeruginosa' 287 Bacteria . Pseudomonas aeruginosa blaIMP-1 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 $IMP-1 'recombinant technology' 'E. coli' . . BL21(DE3) pETMCSIII $IMP-1 'cell free synthesis' . . . BL21(DE3) pETMCSIII stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_ZnZN-IMP-1_in_vivo _Saveframe_category sample _Sample_type solution _Details 'Recombinant uniformly 13C/15N-labelled protein expressed in vivo' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $IMP-1 0.4 mM '[U-13C; U-15N]' MES 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_ZnZn-IMP-1_cell_free _Saveframe_category sample _Sample_type solution _Details 'Recombinant uniformly 2H/13C/15N-labelled protein produced using cell-free protein synthesis' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $IMP-1 0.4 mM '[U-13C; U-15N; U-2H]' MES 20 mM 'natural abundance' 'sodium chloride' 100 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 'Spectrum display' 'Spectrum analysis' stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_Topspin _Saveframe_category software _Name Topspin _Version 2.1 loop_ _Vendor _Address _Electronic_address Bruker 'Bruker Pty. Ltd., Billerica, Massachusetts, USA' http://www.bruker.com stop_ loop_ _Task 'Data Acquisition' stop_ _Details 'Bruker Topspin NMR acquistion and analysis application' save_ save_nmrDraw _Saveframe_category software _Name nmrDraw _Version any loop_ _Vendor _Address _Electronic_address 'F. Delaglio/NIH' . http://spin.niddk.nih.gov/NMRPipe/ stop_ loop_ _Task 'Spectrum display' stop_ _Details 'NMRPipe Spectral Processing and Analysis System' save_ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version any loop_ _Vendor _Address _Electronic_address 'F. Delaglio/NIH' . http://spin.niddk.nih.gov/NMRPipe/ stop_ loop_ _Task 'Spectrum processing' stop_ _Details 'NMRPipe Spectral Processing and Analysis System' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'Bruker Avance II' save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $ZnZN-IMP-1_in_vivo save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $ZnZN-IMP-1_in_vivo save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $ZnZN-IMP-1_in_vivo save_ save_3D_TROSY-HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label $ZnZn-IMP-1_cell_free save_ save_3D_TROSY-HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCO' _Sample_label $ZnZn-IMP-1_cell_free save_ save_3D_TROSY-HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _Sample_label $ZnZn-IMP-1_cell_free save_ save_3D_TROSY-HNCACO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACO' _Sample_label $ZnZn-IMP-1_cell_free save_ save_2D_TROSY-[1H-15N]_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TROSY-[1H-15N]' _Sample_label $ZnZn-IMP-1_cell_free save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $ZnZN-IMP-1_in_vivo save_ ####################### # Sample conditions # ####################### save_IMP1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.120 . M pH 6.500 . pH pressure 1.000 . atm temperature 310.000 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details 'TROSY-type data was corrected to reference non-trosy shifts (approximately H:+0.048, N:-0.428, C:+0.372 ppm)' 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 H 1 H ppm 4.615 internal direct . . . 1 HDO C 13 H ppm 4.615 internal indirect . . . 0.25144953 HDO N 15 H ppm 4.615 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 '3D HNCA' '3D CBCA(CO)NH' '3D HNCACB' '3D TROSY-HNCA' '3D TROSY-HNCO' '3D TROSY-HNCACB' '3D TROSY-HNCACO' '2D TROSY-[1H-15N]' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $ZnZN-IMP-1_in_vivo $ZnZn-IMP-1_cell_free stop_ _Sample_conditions_label $IMP1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name IMP-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 -1 4 MET H H 8.569 0.01 1 2 -1 4 MET C C 176.865 0.1 1 3 -1 4 MET N N 122.524 0.2 1 4 0 5 THR H H 8.073 0.01 1 5 0 5 THR C C 175.555 0.1 1 6 0 5 THR N N 113.731 0.2 1 7 1 6 GLY H H 8.241 0.01 1 8 1 6 GLY C C 174.486 0.1 1 9 1 6 GLY CA C 45.396 0.1 1 10 1 6 GLY N N 110.966 0.2 1 11 2 7 GLU H H 8.075 0.01 1 12 2 7 GLU C C 176.799 0.1 1 13 2 7 GLU CA C 56.368 0.1 1 14 2 7 GLU CB C 30.072 0.4 1 15 2 7 GLU N N 120.311 0.2 1 16 3 8 SER H H 8.158 0.01 1 17 3 8 SER C C 174.285 0.1 1 18 3 8 SER CA C 58.121 0.1 1 19 3 8 SER CB C 63.655 0.4 1 20 3 8 SER N N 116.393 0.2 1 21 4 9 LEU H H 8.028 0.01 1 22 4 9 LEU C C 175.127 0.1 1 23 4 9 LEU CA C 52.928 0.1 1 24 4 9 LEU CB C 41.471 0.4 1 25 4 9 LEU N N 125.085 0.2 1 26 5 10 PRO C C 175.472 0.1 1 27 5 10 PRO CA C 62.349 0.1 1 28 5 10 PRO CB C 30.493 0.4 1 29 6 11 ASP H H 7.661 0.01 1 30 6 11 ASP C C 175.656 0.1 1 31 6 11 ASP CA C 53.640 0.1 1 32 6 11 ASP CB C 42.243 0.4 1 33 6 11 ASP N N 119.415 0.2 1 34 7 12 LEU H H 7.946 0.01 1 35 7 12 LEU C C 176.778 0.1 1 36 7 12 LEU CA C 55.860 0.1 1 37 7 12 LEU CB C 42.569 0.4 1 38 7 12 LEU N N 120.175 0.2 1 39 8 13 LYS H H 9.009 0.01 1 40 8 13 LYS C C 175.654 0.1 1 41 8 13 LYS CA C 54.725 0.1 1 42 8 13 LYS CB C 35.336 0.4 1 43 8 13 LYS N N 127.879 0.2 1 44 9 14 ILE H H 8.125 0.01 1 45 9 14 ILE C C 175.647 0.1 1 46 9 14 ILE CA C 61.035 0.1 1 47 9 14 ILE CB C 40.121 0.4 1 48 9 14 ILE N N 123.465 0.2 1 49 10 15 GLU H H 8.728 0.01 1 50 10 15 GLU C C 175.002 0.1 1 51 10 15 GLU CA C 54.381 0.1 1 52 10 15 GLU CB C 34.122 0.4 1 53 10 15 GLU N N 124.678 0.2 1 54 11 16 LYS H H 8.995 0.01 1 55 11 16 LYS C C 175.454 0.1 1 56 11 16 LYS CA C 58.133 0.1 1 57 11 16 LYS CB C 32.511 0.4 1 58 11 16 LYS N N 126.603 0.2 1 59 12 17 LEU H H 8.892 0.01 1 60 12 17 LEU C C 175.226 0.1 1 61 12 17 LEU CA C 55.288 0.1 1 62 12 17 LEU CB C 44.537 0.4 1 63 12 17 LEU N N 129.821 0.2 1 64 13 18 ASP H H 8.235 0.01 1 65 13 18 ASP C C 175.375 0.1 1 66 13 18 ASP CA C 51.385 0.1 1 67 13 18 ASP CB C 43.607 0.4 1 68 13 18 ASP N N 116.316 0.2 1 69 14 19 GLU H H 9.164 0.01 1 70 14 19 GLU C C 177.703 0.1 1 71 14 19 GLU CA C 58.032 0.1 1 72 14 19 GLU CB C 28.277 0.4 1 73 14 19 GLU N N 122.088 0.2 1 74 15 20 GLY H H 8.628 0.01 1 75 15 20 GLY C C 173.579 0.1 1 76 15 20 GLY CA C 46.477 0.1 1 77 15 20 GLY N N 113.746 0.2 1 78 16 21 VAL H H 7.989 0.01 1 79 16 21 VAL C C 173.951 0.1 1 80 16 21 VAL CA C 61.882 0.1 1 81 16 21 VAL CB C 34.656 0.4 1 82 16 21 VAL N N 117.926 0.2 1 83 17 22 TYR H H 9.457 0.01 1 84 17 22 TYR C C 174.962 0.1 1 85 17 22 TYR CA C 56.465 0.1 1 86 17 22 TYR CB C 41.068 0.4 1 87 17 22 TYR N N 126.923 0.2 1 88 18 23 VAL H H 9.536 0.01 1 89 18 23 VAL C C 176.762 0.1 1 90 18 23 VAL CA C 60.004 0.1 1 91 18 23 VAL CB C 33.772 0.4 1 92 18 23 VAL N N 121.105 0.2 1 93 19 24 HIS H H 8.323 0.01 1 94 19 24 HIS C C 174.514 0.1 1 95 19 24 HIS CA C 52.532 0.1 1 96 19 24 HIS CB C 34.874 0.4 1 97 19 24 HIS N N 126.041 0.2 1 98 20 25 THR H H 9.318 0.01 1 99 20 25 THR C C 172.382 0.1 1 100 20 25 THR CA C 61.573 0.1 1 101 20 25 THR CB C 70.467 0.4 1 102 20 25 THR N N 120.096 0.2 1 103 21 26 SER H H 8.443 0.01 1 104 21 26 SER C C 173.023 0.1 1 105 21 26 SER CA C 56.044 0.1 1 106 21 26 SER CB C 67.502 0.4 1 107 21 26 SER N N 119.967 0.2 1 108 22 27 PHE H H 8.670 0.01 1 109 22 27 PHE C C 174.553 0.1 1 110 22 27 PHE CA C 57.562 0.1 1 111 22 27 PHE CB C 43.570 0.4 1 112 22 27 PHE N N 116.181 0.2 1 113 23 28 GLU H H 7.907 0.01 1 114 23 28 GLU CA C 54.555 0.1 1 115 23 28 GLU CB C 31.324 0.4 1 116 23 28 GLU N N 119.993 0.2 1 117 24 29 GLU H H 8.689 0.01 1 118 24 29 GLU C C 175.865 0.1 1 119 24 29 GLU CA C 55.880 0.1 1 120 24 29 GLU CB C 29.801 0.4 1 121 24 29 GLU N N 124.661 0.2 1 122 25 30 VAL H H 8.568 0.01 1 123 25 30 VAL C C 176.657 0.1 1 124 25 30 VAL CA C 61.268 0.1 1 125 25 30 VAL CB C 33.188 0.4 1 126 25 30 VAL N N 127.875 0.2 1 127 27 32 GLY C C 174.398 0.1 1 128 27 32 GLY CA C 45.512 0.1 1 129 28 33 TRP H H 8.213 0.01 1 130 28 33 TRP C C 176.341 0.1 1 131 28 33 TRP CA C 57.719 0.1 1 132 28 33 TRP CB C 31.449 0.4 1 133 28 33 TRP N N 120.283 0.2 1 134 29 34 GLY H H 8.241 0.01 1 135 29 34 GLY C C 173.233 0.1 1 136 29 34 GLY CA C 44.673 0.1 1 137 29 34 GLY N N 108.411 0.2 1 138 30 35 VAL H H 8.331 0.01 1 139 30 35 VAL C C 176.614 0.1 1 140 30 35 VAL CA C 63.074 0.1 1 141 30 35 VAL CB C 31.408 0.4 1 142 30 35 VAL N N 122.128 0.2 1 143 31 36 VAL H H 9.065 0.01 1 144 31 36 VAL CA C 58.799 0.1 1 145 31 36 VAL CB C 34.332 0.4 1 146 31 36 VAL N N 130.002 0.2 1 147 32 37 PRO C C 176.933 0.1 1 148 32 37 PRO CA C 61.199 0.1 1 149 32 37 PRO CB C 32.634 0.4 1 150 33 38 LYS H H 8.740 0.01 1 151 33 38 LYS C C 175.722 0.1 1 152 33 38 LYS CA C 53.290 0.1 1 153 33 38 LYS CB C 35.105 0.4 1 154 33 38 LYS N N 119.816 0.2 1 155 34 39 HIS H H 9.830 0.01 1 156 34 39 HIS C C 176.187 0.1 1 157 34 39 HIS CA C 53.716 0.1 1 158 34 39 HIS CB C 29.394 0.4 1 159 34 39 HIS N N 128.747 0.2 1 160 35 40 GLY H H 8.788 0.01 1 161 35 40 GLY C C 172.937 0.1 1 162 35 40 GLY CA C 43.033 0.1 1 163 35 40 GLY N N 112.742 0.2 1 164 36 41 LEU H H 8.775 0.01 1 165 36 41 LEU C C 178.323 0.1 1 166 36 41 LEU CA C 52.952 0.1 1 167 36 41 LEU CB C 46.206 0.4 1 168 36 41 LEU N N 115.101 0.2 1 169 37 42 VAL H H 9.147 0.01 1 170 37 42 VAL C C 174.888 0.1 1 171 37 42 VAL CA C 62.979 0.1 1 172 37 42 VAL CB C 33.966 0.4 1 173 37 42 VAL N N 121.179 0.2 1 174 38 43 VAL H H 8.936 0.01 1 175 38 43 VAL C C 174.733 0.1 1 176 38 43 VAL CA C 60.381 0.1 1 177 38 43 VAL CB C 34.190 0.4 1 178 38 43 VAL N N 126.508 0.2 1 179 39 44 LEU H H 8.957 0.01 1 180 39 44 LEU C C 177.561 0.1 1 181 39 44 LEU CA C 53.268 0.1 1 182 39 44 LEU CB C 41.240 0.4 1 183 39 44 LEU N N 126.434 0.2 1 184 40 45 VAL H H 9.284 0.01 1 185 40 45 VAL C C 176.298 0.1 1 186 40 45 VAL CA C 61.467 0.1 1 187 40 45 VAL CB C 32.566 0.4 1 188 40 45 VAL N N 125.269 0.2 1 189 41 46 ASN C C 174.544 0.1 1 190 41 46 ASN CA C 55.961 0.1 1 191 41 46 ASN CB C 37.102 0.4 1 192 42 47 ALA H H 8.325 0.01 1 193 42 47 ALA C C 176.153 0.1 1 194 42 47 ALA CA C 52.793 0.1 1 195 42 47 ALA CB C 17.806 0.4 1 196 42 47 ALA N N 123.356 0.2 1 197 43 48 GLU H H 8.183 0.01 1 198 43 48 GLU C C 174.460 0.1 1 199 43 48 GLU CA C 55.225 0.1 1 200 43 48 GLU CB C 31.546 0.4 1 201 43 48 GLU N N 119.227 0.2 1 202 44 49 ALA H H 8.777 0.01 1 203 44 49 ALA C C 176.206 0.1 1 204 44 49 ALA CA C 50.092 0.1 1 205 44 49 ALA CB C 21.427 0.4 1 206 44 49 ALA N N 122.077 0.2 1 207 45 50 TYR H H 8.895 0.01 1 208 45 50 TYR C C 175.492 0.1 1 209 45 50 TYR CA C 56.610 0.1 1 210 45 50 TYR CB C 40.483 0.4 1 211 45 50 TYR N N 119.031 0.2 1 212 46 51 LEU H H 8.718 0.01 1 213 46 51 LEU C C 175.166 0.1 1 214 46 51 LEU CA C 55.258 0.1 1 215 46 51 LEU CB C 41.321 0.4 1 216 46 51 LEU N N 122.857 0.2 1 217 47 52 ILE H H 9.246 0.01 1 218 47 52 ILE C C 175.168 0.1 1 219 47 52 ILE CA C 60.531 0.1 1 220 47 52 ILE CB C 33.946 0.4 1 221 47 52 ILE N N 125.835 0.2 1 222 48 53 ASP H H 8.913 0.01 1 223 48 53 ASP C C 175.086 0.1 1 224 48 53 ASP CA C 57.129 0.1 1 225 48 53 ASP CB C 38.805 0.4 1 226 48 53 ASP N N 117.934 0.2 1 227 49 54 THR H H 6.869 0.01 1 228 49 54 THR C C 173.548 0.1 1 229 49 54 THR CA C 58.311 0.1 1 230 49 54 THR CB C 67.886 0.4 1 231 49 54 THR N N 104.472 0.2 1 232 50 55 PRO C C 173.619 0.1 1 233 50 55 PRO CA C 62.499 0.1 1 234 50 55 PRO CB C 33.207 0.4 1 235 51 56 PHE H H 6.855 0.01 1 236 51 56 PHE C C 177.637 0.1 1 237 51 56 PHE CA C 61.240 0.1 1 238 51 56 PHE CB C 41.018 0.4 1 239 51 56 PHE N N 111.860 0.2 1 240 52 57 THR H H 7.136 0.01 1 241 52 57 THR CA C 58.630 0.1 1 242 52 57 THR CB C 73.804 0.4 1 243 52 57 THR N N 99.520 0.2 1 244 53 58 ALA C C 179.857 0.1 1 245 53 58 ALA CA C 55.557 0.1 1 246 53 58 ALA CB C 17.947 0.4 1 247 54 59 LYS H H 8.150 0.01 1 248 54 59 LYS C C 179.628 0.1 1 249 54 59 LYS CA C 59.229 0.1 1 250 54 59 LYS CB C 31.228 0.4 1 251 54 59 LYS N N 117.870 0.2 1 252 55 60 ASP H H 7.688 0.01 1 253 55 60 ASP C C 178.845 0.1 1 254 55 60 ASP CA C 56.810 0.1 1 255 55 60 ASP CB C 40.617 0.4 1 256 55 60 ASP N N 118.105 0.2 1 257 56 61 THR H H 7.647 0.01 1 258 56 61 THR C C 174.617 0.1 1 259 56 61 THR CA C 68.569 0.1 1 260 56 61 THR CB C 66.909 0.4 1 261 56 61 THR N N 119.954 0.2 1 262 57 62 GLU H H 7.694 0.01 1 263 57 62 GLU C C 179.520 0.1 1 264 57 62 GLU CA C 58.794 0.1 1 265 57 62 GLU CB C 27.762 0.4 1 266 57 62 GLU N N 122.115 0.2 1 267 58 63 LYS H H 7.598 0.01 1 268 58 63 LYS C C 178.806 0.1 1 269 58 63 LYS CA C 60.119 0.1 1 270 58 63 LYS CB C 32.322 0.4 1 271 58 63 LYS N N 121.182 0.2 1 272 59 64 LEU H H 7.869 0.01 1 273 59 64 LEU C C 177.606 0.1 1 274 59 64 LEU CA C 58.039 0.1 1 275 59 64 LEU CB C 42.204 0.4 1 276 59 64 LEU N N 120.948 0.2 1 277 60 65 VAL H H 8.226 0.01 1 278 60 65 VAL C C 178.548 0.1 1 279 60 65 VAL CA C 67.379 0.1 1 280 60 65 VAL CB C 31.359 0.4 1 281 60 65 VAL N N 116.507 0.2 1 282 61 66 THR H H 8.495 0.01 1 283 61 66 THR C C 175.071 0.1 1 284 61 66 THR CA C 67.116 0.1 1 285 61 66 THR CB C 68.877 0.4 1 286 61 66 THR N N 115.180 0.2 1 287 62 67 TRP H H 7.816 0.01 1 288 62 67 TRP C C 179.618 0.1 1 289 62 67 TRP CA C 62.242 0.1 1 290 62 67 TRP CB C 29.527 0.4 1 291 62 67 TRP N N 122.106 0.2 1 292 63 68 PHE H H 7.360 0.01 1 293 63 68 PHE C C 178.998 0.1 1 294 63 68 PHE CA C 63.566 0.1 1 295 63 68 PHE CB C 39.017 0.4 1 296 63 68 PHE N N 112.826 0.2 1 297 64 69 VAL H H 8.980 0.01 1 298 64 69 VAL C C 182.136 0.1 1 299 64 69 VAL CA C 66.237 0.1 1 300 64 69 VAL CB C 31.378 0.4 1 301 64 69 VAL N N 124.083 0.2 1 302 65 70 GLU H H 8.691 0.01 1 303 65 70 GLU C C 178.086 0.1 1 304 65 70 GLU CA C 58.710 0.1 1 305 65 70 GLU CB C 28.563 0.4 1 306 65 70 GLU N N 120.289 0.2 1 307 66 71 ARG H H 6.785 0.01 1 308 66 71 ARG C C 175.485 0.1 1 309 66 71 ARG CA C 55.989 0.1 1 310 66 71 ARG CB C 29.356 0.4 1 311 66 71 ARG N N 117.126 0.2 1 312 67 72 GLY H H 7.640 0.01 1 313 67 72 GLY C C 174.477 0.1 1 314 67 72 GLY CA C 45.258 0.1 1 315 67 72 GLY N N 105.754 0.2 1 316 68 73 TYR H H 7.686 0.01 1 317 68 73 TYR C C 175.150 0.1 1 318 68 73 TYR CA C 57.540 0.1 1 319 68 73 TYR CB C 39.048 0.4 1 320 68 73 TYR N N 119.462 0.2 1 321 69 74 LYS H H 8.146 0.01 1 322 69 74 LYS C C 176.345 0.1 1 323 69 74 LYS CA C 54.634 0.1 1 324 69 74 LYS CB C 33.527 0.4 1 325 69 74 LYS N N 119.852 0.2 1 326 70 75 ILE H H 8.604 0.01 1 327 70 75 ILE C C 176.058 0.1 1 328 70 75 ILE CA C 59.170 0.1 1 329 70 75 ILE CB C 33.769 0.4 1 330 70 75 ILE N N 123.968 0.2 1 331 71 76 LYS H H 8.712 0.01 1 332 71 76 LYS C C 176.874 0.1 1 333 71 76 LYS CA C 54.162 0.1 1 334 71 76 LYS CB C 32.890 0.4 1 335 71 76 LYS N N 127.787 0.2 1 336 72 77 GLY H H 6.747 0.01 1 337 72 77 GLY C C 171.528 0.1 1 338 72 77 GLY CA C 45.554 0.1 1 339 72 77 GLY N N 102.115 0.2 1 340 73 78 SER H H 8.377 0.01 1 341 73 78 SER C C 173.584 0.1 1 342 73 78 SER CA C 56.242 0.1 1 343 73 78 SER CB C 66.622 0.4 1 344 73 78 SER N N 113.252 0.2 1 345 74 79 ILE H H 9.213 0.01 1 346 74 79 ILE C C 173.827 0.1 1 347 74 79 ILE CA C 57.828 0.1 1 348 74 79 ILE CB C 40.334 0.4 1 349 74 79 ILE N N 124.273 0.2 1 350 75 80 SER H H 7.866 0.01 1 351 75 80 SER C C 174.309 0.1 1 352 75 80 SER CA C 58.804 0.1 1 353 75 80 SER CB C 65.213 0.4 1 354 75 80 SER N N 121.769 0.2 1 355 76 81 SER H H 10.783 0.01 1 356 76 81 SER C C 173.820 0.1 1 357 76 81 SER CA C 60.179 0.1 1 358 76 81 SER CB C 63.737 0.4 1 359 76 81 SER N N 120.642 0.2 1 360 77 82 HIS H H 7.679 0.01 1 361 77 82 HIS C C 175.928 0.1 1 362 77 82 HIS CA C 55.347 0.1 1 363 77 82 HIS CB C 27.250 0.4 1 364 77 82 HIS N N 110.340 0.2 1 365 78 83 PHE H H 9.154 0.01 1 366 78 83 PHE C C 175.042 0.1 1 367 78 83 PHE CA C 59.929 0.1 1 368 78 83 PHE CB C 39.171 0.4 1 369 78 83 PHE N N 115.729 0.2 1 370 81 86 ASP C C 173.847 0.1 1 371 81 86 ASP CA C 54.938 0.1 1 372 81 86 ASP CB C 38.058 0.4 1 373 82 87 SER H H 7.461 0.01 1 374 82 87 SER C C 177.959 0.1 1 375 82 87 SER CA C 60.679 0.1 1 376 82 87 SER CB C 66.902 0.4 1 377 82 87 SER N N 108.436 0.2 1 378 83 88 THR H H 7.478 0.01 1 379 83 88 THR C C 176.731 0.1 1 380 83 88 THR CA C 61.339 0.1 1 381 83 88 THR CB C 71.699 0.4 1 382 83 88 THR N N 109.631 0.2 1 383 84 89 GLY H H 8.369 0.01 1 384 84 89 GLY C C 176.083 0.1 1 385 84 89 GLY CA C 47.678 0.1 1 386 84 89 GLY N N 113.004 0.2 1 387 85 90 GLY H H 8.616 0.01 1 388 85 90 GLY C C 174.576 0.1 1 389 85 90 GLY CA C 45.466 0.1 1 390 85 90 GLY N N 106.309 0.2 1 391 86 91 ILE H H 7.867 0.01 1 392 86 91 ILE C C 177.052 0.1 1 393 86 91 ILE CA C 67.201 0.1 1 394 86 91 ILE CB C 36.844 0.4 1 395 86 91 ILE N N 121.416 0.2 1 396 87 92 GLU H H 8.803 0.01 1 397 87 92 GLU C C 178.949 0.1 1 398 87 92 GLU CA C 60.565 0.1 1 399 87 92 GLU CB C 28.595 0.4 1 400 87 92 GLU N N 120.254 0.2 1 401 88 93 TRP H H 8.743 0.01 1 402 88 93 TRP C C 180.627 0.1 1 403 88 93 TRP CA C 62.904 0.1 1 404 88 93 TRP CB C 28.371 0.4 1 405 88 93 TRP N N 121.967 0.2 1 406 89 94 LEU H H 8.463 0.01 1 407 89 94 LEU C C 179.864 0.1 1 408 89 94 LEU CA C 58.849 0.1 1 409 89 94 LEU CB C 40.156 0.4 1 410 89 94 LEU N N 120.756 0.2 1 411 90 95 ASN H H 9.169 0.01 1 412 90 95 ASN C C 180.800 0.1 1 413 90 95 ASN CA C 55.371 0.1 1 414 90 95 ASN CB C 36.418 0.4 1 415 90 95 ASN N N 119.349 0.2 1 416 91 96 SER H H 8.072 0.01 1 417 91 96 SER C C 174.919 0.1 1 418 91 96 SER CA C 61.128 0.1 1 419 91 96 SER CB C 62.552 0.4 1 420 91 96 SER N N 118.764 0.2 1 421 92 97 ARG H H 7.087 0.01 1 422 92 97 ARG C C 175.523 0.1 1 423 92 97 ARG CA C 54.156 0.1 1 424 92 97 ARG CB C 28.825 0.4 1 425 92 97 ARG N N 122.263 0.2 1 426 93 98 SER H H 7.763 0.01 1 427 93 98 SER C C 174.303 0.1 1 428 93 98 SER CA C 59.078 0.1 1 429 93 98 SER CB C 60.953 0.4 1 430 93 98 SER N N 110.989 0.2 1 431 94 99 ILE H H 7.719 0.01 1 432 94 99 ILE C C 174.860 0.1 1 433 94 99 ILE CA C 58.358 0.1 1 434 94 99 ILE CB C 38.132 0.4 1 435 94 99 ILE N N 123.257 0.2 1 436 95 100 PRO C C 174.935 0.1 1 437 95 100 PRO CA C 64.261 0.1 1 438 95 100 PRO CB C 32.991 0.4 1 439 96 101 THR H H 7.055 0.01 1 440 96 101 THR C C 174.868 0.1 1 441 96 101 THR CA C 58.337 0.1 1 442 96 101 THR CB C 71.979 0.4 1 443 96 101 THR N N 111.945 0.2 1 444 97 102 TYR H H 9.111 0.01 1 445 97 102 TYR C C 176.463 0.1 1 446 97 102 TYR CA C 56.826 0.1 1 447 97 102 TYR CB C 41.666 0.4 1 448 97 102 TYR N N 120.043 0.2 1 449 98 103 ALA H H 8.290 0.01 1 450 98 103 ALA C C 174.283 0.1 1 451 98 103 ALA CA C 51.304 0.1 1 452 98 103 ALA CB C 20.958 0.4 1 453 98 103 ALA N N 121.515 0.2 1 454 99 104 SER H H 9.443 0.01 1 455 99 104 SER C C 174.809 0.1 1 456 99 104 SER CA C 57.227 0.1 1 457 99 104 SER CB C 64.104 0.4 1 458 99 104 SER N N 117.057 0.2 1 459 100 105 GLU H H 7.932 0.01 1 460 100 105 GLU C C 179.432 0.1 1 461 100 105 GLU CA C 59.923 0.1 1 462 100 105 GLU CB C 29.075 0.4 1 463 100 105 GLU N N 120.303 0.2 1 464 101 106 LEU H H 7.959 0.01 1 465 101 106 LEU C C 178.793 0.1 1 466 101 106 LEU CA C 57.544 0.1 1 467 101 106 LEU CB C 40.544 0.4 1 468 101 106 LEU N N 119.665 0.2 1 469 102 107 THR H H 8.146 0.01 1 470 102 107 THR C C 176.645 0.1 1 471 102 107 THR CA C 66.639 0.1 1 472 102 107 THR CB C 67.215 0.4 1 473 102 107 THR N N 119.133 0.2 1 474 103 108 ASN H H 8.211 0.01 1 475 103 108 ASN C C 178.997 0.1 1 476 103 108 ASN CA C 54.907 0.1 1 477 103 108 ASN CB C 36.998 0.4 1 478 103 108 ASN N N 119.033 0.2 1 479 104 109 GLU H H 7.975 0.01 1 480 104 109 GLU C C 179.423 0.1 1 481 104 109 GLU CA C 59.378 0.1 1 482 104 109 GLU CB C 28.803 0.4 1 483 104 109 GLU N N 122.616 0.2 1 484 105 110 LEU H H 7.929 0.01 1 485 105 110 LEU C C 180.415 0.1 1 486 105 110 LEU CA C 57.796 0.1 1 487 105 110 LEU CB C 38.946 0.4 1 488 105 110 LEU N N 121.509 0.2 1 489 106 111 LEU H H 8.358 0.01 1 490 106 111 LEU C C 179.086 0.1 1 491 106 111 LEU CA C 58.341 0.1 1 492 106 111 LEU CB C 40.923 0.4 1 493 106 111 LEU N N 120.695 0.2 1 494 107 112 LYS H H 7.844 0.01 1 495 107 112 LYS C C 181.482 0.1 1 496 107 112 LYS CA C 59.372 0.1 1 497 107 112 LYS CB C 31.690 0.4 1 498 107 112 LYS N N 119.796 0.2 1 499 108 113 LYS H H 8.065 0.01 1 500 108 113 LYS C C 177.765 0.1 1 501 108 113 LYS CA C 59.249 0.1 1 502 108 113 LYS CB C 31.584 0.4 1 503 108 113 LYS N N 121.035 0.2 1 504 109 114 ASP H H 7.286 0.01 1 505 109 114 ASP C C 176.760 0.1 1 506 109 114 ASP CA C 54.147 0.1 1 507 109 114 ASP CB C 42.085 0.4 1 508 109 114 ASP N N 117.731 0.2 1 509 110 115 GLY H H 7.939 0.01 1 510 110 115 GLY C C 175.233 0.1 1 511 110 115 GLY CA C 46.234 0.1 1 512 110 115 GLY N N 108.425 0.2 1 513 111 116 LYS H H 8.017 0.01 1 514 111 116 LYS C C 176.041 0.1 1 515 111 116 LYS CA C 53.333 0.1 1 516 111 116 LYS CB C 33.769 0.4 1 517 111 116 LYS N N 119.264 0.2 1 518 112 117 VAL H H 7.843 0.01 1 519 112 117 VAL C C 175.931 0.1 1 520 112 117 VAL CA C 63.455 0.1 1 521 112 117 VAL CB C 31.605 0.4 1 522 112 117 VAL N N 120.101 0.2 1 523 113 118 GLN H H 7.748 0.01 1 524 113 118 GLN C C 177.881 0.1 1 525 113 118 GLN CA C 55.676 0.1 1 526 113 118 GLN CB C 30.980 0.4 1 527 113 118 GLN N N 121.759 0.2 1 528 114 119 ALA H H 8.355 0.01 1 529 114 119 ALA C C 179.097 0.1 1 530 114 119 ALA CA C 51.696 0.1 1 531 114 119 ALA CB C 18.453 0.4 1 532 114 119 ALA N N 122.696 0.2 1 533 115 120 THR H H 8.743 0.01 1 534 115 120 THR C C 174.823 0.1 1 535 115 120 THR CA C 63.780 0.1 1 536 115 120 THR CB C 69.451 0.4 1 537 115 120 THR N N 114.535 0.2 1 538 116 121 ASN H H 8.382 0.01 1 539 116 121 ASN C C 173.404 0.1 1 540 116 121 ASN CA C 52.648 0.1 1 541 116 121 ASN CB C 41.560 0.4 1 542 116 121 ASN N N 119.269 0.2 1 543 117 122 SER H H 8.379 0.01 1 544 117 122 SER C C 174.213 0.1 1 545 117 122 SER CA C 55.908 0.1 1 546 117 122 SER CB C 65.889 0.4 1 547 117 122 SER N N 114.998 0.2 1 548 118 123 PHE H H 6.808 0.01 1 549 118 123 PHE C C 173.967 0.1 1 550 118 123 PHE CA C 55.132 0.1 1 551 118 123 PHE CB C 40.425 0.4 1 552 118 123 PHE N N 115.969 0.2 1 553 119 124 SER H H 8.431 0.01 1 554 119 124 SER C C 174.346 0.1 1 555 119 124 SER CA C 57.020 0.1 1 556 119 124 SER CB C 65.168 0.4 1 557 119 124 SER N N 115.824 0.2 1 558 120 125 GLY H H 8.174 0.01 1 559 120 125 GLY C C 174.347 0.1 1 560 120 125 GLY CA C 44.368 0.1 1 561 120 125 GLY N N 108.766 0.2 1 562 121 126 VAL H H 8.200 0.01 1 563 121 126 VAL C C 175.078 0.1 1 564 121 126 VAL CA C 64.431 0.1 1 565 121 126 VAL CB C 32.090 0.4 1 566 121 126 VAL N N 117.165 0.2 1 567 122 127 ASN H H 7.676 0.01 1 568 122 127 ASN C C 173.955 0.1 1 569 122 127 ASN CA C 52.106 0.1 1 570 122 127 ASN CB C 42.023 0.4 1 571 122 127 ASN N N 114.863 0.2 1 572 123 128 TYR H H 8.584 0.01 1 573 123 128 TYR C C 174.130 0.1 1 574 123 128 TYR CA C 57.050 0.1 1 575 123 128 TYR CB C 41.663 0.4 1 576 123 128 TYR N N 122.924 0.2 1 577 124 129 TRP H H 8.211 0.01 1 578 124 129 TRP C C 174.369 0.1 1 579 124 129 TRP CA C 55.328 0.1 1 580 124 129 TRP CB C 27.977 0.4 1 581 124 129 TRP N N 127.525 0.2 1 582 125 130 LEU H H 7.228 0.01 1 583 125 130 LEU C C 177.121 0.1 1 584 125 130 LEU CA C 56.737 0.1 1 585 125 130 LEU CB C 41.956 0.4 1 586 125 130 LEU N N 127.078 0.2 1 587 126 131 VAL H H 6.962 0.01 1 588 126 131 VAL C C 176.921 0.1 1 589 126 131 VAL CA C 61.316 0.1 1 590 126 131 VAL CB C 34.469 0.4 1 591 126 131 VAL N N 112.765 0.2 1 592 127 132 LYS C C 175.918 0.1 1 593 127 132 LYS CA C 59.152 0.1 1 594 127 132 LYS CB C 30.868 0.4 1 595 128 133 ASN H H 5.891 0.01 1 596 128 133 ASN C C 173.888 0.1 1 597 128 133 ASN CA C 56.113 0.1 1 598 128 133 ASN CB C 37.570 0.4 1 599 128 133 ASN N N 116.218 0.2 1 600 129 134 LYS H H 7.732 0.01 1 601 129 134 LYS C C 176.423 0.1 1 602 129 134 LYS CA C 56.914 0.1 1 603 129 134 LYS CB C 35.788 0.4 1 604 129 134 LYS N N 115.497 0.2 1 605 130 135 ILE H H 8.493 0.01 1 606 130 135 ILE C C 173.546 0.1 1 607 130 135 ILE CA C 62.116 0.1 1 608 130 135 ILE CB C 40.931 0.4 1 609 130 135 ILE N N 116.659 0.2 1 610 131 136 GLU H H 9.222 0.01 1 611 131 136 GLU C C 173.970 0.1 1 612 131 136 GLU CA C 54.586 0.1 1 613 131 136 GLU CB C 32.134 0.4 1 614 131 136 GLU N N 131.748 0.2 1 615 132 137 VAL H H 9.158 0.01 1 616 132 137 VAL C C 175.098 0.1 1 617 132 137 VAL CA C 60.876 0.1 1 618 132 137 VAL CB C 32.007 0.4 1 619 132 137 VAL N N 126.862 0.2 1 620 133 138 PHE H H 8.758 0.01 1 621 133 138 PHE C C 173.176 0.1 1 622 133 138 PHE CA C 55.442 0.1 1 623 133 138 PHE CB C 43.128 0.4 1 624 133 138 PHE N N 126.864 0.2 1 625 134 139 TYR H H 8.447 0.01 1 626 134 139 TYR C C 171.845 0.1 1 627 134 139 TYR CA C 52.497 0.1 1 628 134 139 TYR CB C 38.885 0.4 1 629 134 139 TYR N N 129.526 0.2 1 630 139 144 HIS CA C 59.076 0.5 1 631 140 145 THR H H 7.497 0.01 1 632 140 145 THR CA C 59.592 0.5 1 633 140 145 THR N N 103.791 0.2 1 634 141 146 PRO CA C 65.171 0.5 1 635 142 147 ASP H H 9.543 0.01 1 636 142 147 ASP CA C 53.152 0.5 1 637 142 147 ASP N N 108.382 0.2 1 638 143 148 ASN H H 6.575 0.01 1 639 143 148 ASN C C 175.634 0.1 1 640 143 148 ASN CA C 54.767 0.1 1 641 143 148 ASN CB C 39.351 0.4 1 642 143 148 ASN N N 116.682 0.2 1 643 144 149 VAL H H 9.024 0.01 1 644 144 149 VAL C C 176.143 0.1 1 645 144 149 VAL CA C 59.140 0.1 1 646 144 149 VAL CB C 34.343 0.4 1 647 144 149 VAL N N 115.271 0.2 1 648 145 150 VAL H H 9.015 0.01 1 649 145 150 VAL C C 174.973 0.1 1 650 145 150 VAL CA C 58.385 0.1 1 651 145 150 VAL CB C 32.325 0.4 1 652 145 150 VAL N N 111.657 0.2 1 653 146 151 VAL H H 8.266 0.01 1 654 146 151 VAL C C 173.034 0.1 1 655 146 151 VAL CA C 60.710 0.1 1 656 146 151 VAL CB C 34.686 0.4 1 657 146 151 VAL N N 118.147 0.2 1 658 147 152 TRP H H 9.811 0.01 1 659 147 152 TRP C C 173.877 0.1 1 660 147 152 TRP CA C 54.266 0.1 1 661 147 152 TRP CB C 33.580 0.4 1 662 147 152 TRP N N 131.136 0.2 1 663 148 153 LEU H H 7.902 0.01 1 664 148 153 LEU C C 175.325 0.1 1 665 148 153 LEU CA C 50.225 0.1 1 666 148 153 LEU CB C 39.602 0.4 1 667 148 153 LEU N N 125.927 0.2 1 668 149 154 PRO C C 179.132 0.1 1 669 149 154 PRO CA C 64.187 0.1 1 670 149 154 PRO CB C 32.120 0.4 1 671 150 155 GLU H H 8.614 0.01 1 672 150 155 GLU C C 178.398 0.1 1 673 150 155 GLU CA C 59.091 0.1 1 674 150 155 GLU CB C 29.221 0.4 1 675 150 155 GLU N N 114.436 0.2 1 676 151 156 ARG H H 6.550 0.01 1 677 151 156 ARG C C 175.108 0.1 1 678 151 156 ARG CA C 52.922 0.1 1 679 151 156 ARG CB C 30.403 0.4 1 680 151 156 ARG N N 111.341 0.2 1 681 152 157 LYS H H 7.526 0.01 1 682 152 157 LYS C C 175.633 0.1 1 683 152 157 LYS CA C 57.087 0.1 1 684 152 157 LYS CB C 28.876 0.4 1 685 152 157 LYS N N 114.067 0.2 1 686 153 158 ILE H H 6.368 0.01 1 687 153 158 ILE C C 173.006 0.1 1 688 153 158 ILE CA C 59.992 0.1 1 689 153 158 ILE CB C 41.110 0.4 1 690 153 158 ILE N N 116.219 0.2 1 691 154 159 LEU H H 8.824 0.01 1 692 154 159 LEU C C 175.858 0.1 1 693 154 159 LEU CA C 52.382 0.1 1 694 154 159 LEU CB C 45.707 0.4 1 695 154 159 LEU N N 127.241 0.2 1 696 155 160 PHE H H 10.290 0.01 1 697 155 160 PHE C C 174.380 0.1 1 698 155 160 PHE CA C 57.077 0.1 1 699 155 160 PHE CB C 38.160 0.4 1 700 155 160 PHE N N 128.349 0.2 1 701 156 161 GLY H H 7.857 0.01 1 702 156 161 GLY CA C 43.967 0.1 1 703 156 161 GLY N N 113.438 0.2 1 704 157 162 GLY H H 5.732 0.01 1 705 157 162 GLY C C 176.542 0.1 1 706 157 162 GLY CA C 47.367 0.1 1 707 157 162 GLY N N 104.867 0.2 1 708 158 163 CYS H H 9.315 0.01 1 709 158 163 CYS C C 173.970 0.1 1 710 158 163 CYS CA C 60.103 0.1 1 711 158 163 CYS CB C 27.027 0.4 1 712 158 163 CYS N N 128.742 0.2 1 713 159 164 PHE H H 6.975 0.01 1 714 159 164 PHE C C 174.701 0.1 1 715 159 164 PHE CA C 60.394 0.1 1 716 159 164 PHE CB C 40.526 0.4 1 717 159 164 PHE N N 116.465 0.2 1 718 160 165 ILE H H 6.175 0.01 1 719 160 165 ILE C C 179.309 0.1 1 720 160 165 ILE CA C 57.922 0.1 1 721 160 165 ILE CB C 35.309 0.4 1 722 160 165 ILE N N 111.649 0.2 1 723 161 166 LYS H H 6.799 0.01 1 724 161 166 LYS CA C 59.410 0.1 1 725 161 166 LYS N N 121.934 0.2 1 726 162 167 PRO CA C 63.279 0.5 1 727 163 168 TYR H H 7.774 0.01 1 728 163 168 TYR CA C 55.933 0.5 1 729 163 168 TYR N N 114.148 0.2 1 730 168 173 LEU CA C 55.033 0.5 1 731 169 174 GLY H H 8.543 0.01 1 732 169 174 GLY CA C 48.070 0.1 1 733 169 174 GLY N N 109.114 0.2 1 734 170 175 ASP H H 7.960 0.01 1 735 170 175 ASP CA C 54.001 0.5 1 736 170 175 ASP N N 117.101 0.2 1 737 171 176 ALA H H 7.242 0.01 1 738 171 176 ALA CA C 52.204 0.1 1 739 171 176 ALA CB C 20.801 0.4 1 740 171 176 ALA N N 122.119 0.2 1 741 172 177 ASN H H 8.251 0.01 1 742 172 177 ASN CA C 51.628 0.1 1 743 172 177 ASN CB C 38.110 0.4 1 744 172 177 ASN N N 118.427 0.2 1 745 173 178 ILE H H 8.353 0.01 1 746 173 178 ILE CA C 62.834 0.5 1 747 173 178 ILE N N 121.833 0.2 1 748 174 179 GLU H H 7.954 0.01 1 749 174 179 GLU C C 178.592 0.1 1 750 174 179 GLU CA C 59.063 0.5 1 751 174 179 GLU CB C 29.673 0.4 1 752 174 179 GLU N N 117.680 0.2 1 753 175 180 ALA H H 7.474 0.01 1 754 175 180 ALA C C 179.066 0.1 1 755 175 180 ALA CA C 52.990 0.1 1 756 175 180 ALA CB C 20.252 0.4 1 757 175 180 ALA N N 118.554 0.2 1 758 176 181 TRP H H 7.805 0.01 1 759 176 181 TRP CA C 61.319 0.1 1 760 176 181 TRP CB C 26.897 0.4 1 761 176 181 TRP N N 119.808 0.2 1 762 177 182 PRO C C 179.951 0.1 1 763 177 182 PRO CA C 66.841 0.1 1 764 177 182 PRO CB C 30.520 0.4 1 765 178 183 LYS H H 7.263 0.01 1 766 178 183 LYS C C 180.280 0.1 1 767 178 183 LYS CA C 59.943 0.1 1 768 178 183 LYS CB C 31.464 0.4 1 769 178 183 LYS N N 118.913 0.2 1 770 179 184 SER H H 8.742 0.01 1 771 179 184 SER CA C 60.404 0.5 1 772 179 184 SER N N 118.900 0.2 1 773 180 185 ALA H H 9.428 0.01 1 774 180 185 ALA CA C 55.025 0.5 1 775 180 185 ALA CB C 18.188 0.4 1 776 180 185 ALA N N 123.213 0.2 1 777 181 186 LYS H H 8.259 0.01 1 778 181 186 LYS CA C 60.148 0.5 1 779 181 186 LYS N N 122.343 0.2 1 780 182 187 LEU H H 7.736 0.01 1 781 182 187 LEU CA C 58.104 0.1 1 782 182 187 LEU N N 121.879 0.2 1 783 183 188 LEU H H 8.181 0.01 1 784 183 188 LEU C C 178.181 0.1 1 785 183 188 LEU CA C 58.251 0.1 1 786 183 188 LEU CB C 41.365 0.4 1 787 183 188 LEU N N 118.612 0.2 1 788 184 189 LYS H H 7.940 0.01 1 789 184 189 LYS C C 177.902 0.1 1 790 184 189 LYS CA C 59.209 0.1 1 791 184 189 LYS CB C 31.947 0.4 1 792 184 189 LYS N N 117.415 0.2 1 793 185 190 SER H H 7.736 0.01 1 794 185 190 SER C C 176.162 0.1 1 795 185 190 SER CA C 60.828 0.1 1 796 185 190 SER CB C 62.930 0.4 1 797 185 190 SER N N 113.128 0.2 1 798 186 191 LYS H H 7.524 0.01 1 799 186 191 LYS C C 178.227 0.1 1 800 186 191 LYS CA C 57.875 0.1 1 801 186 191 LYS CB C 32.605 0.4 1 802 186 191 LYS N N 120.651 0.2 1 803 187 192 TYR H H 7.546 0.01 1 804 187 192 TYR C C 175.454 0.1 1 805 187 192 TYR CA C 56.721 0.1 1 806 187 192 TYR CB C 37.426 0.4 1 807 187 192 TYR N N 114.111 0.2 1 808 188 193 GLY H H 7.115 0.01 1 809 188 193 GLY C C 174.633 0.1 1 810 188 193 GLY CA C 47.088 0.1 1 811 188 193 GLY N N 105.869 0.2 1 812 189 194 LYS H H 7.482 0.01 1 813 189 194 LYS C C 176.156 0.1 1 814 189 194 LYS CA C 55.214 0.1 1 815 189 194 LYS CB C 30.703 0.4 1 816 189 194 LYS N N 115.410 0.2 1 817 190 195 ALA H H 7.663 0.01 1 818 190 195 ALA C C 176.595 0.1 1 819 190 195 ALA CA C 53.784 0.1 1 820 190 195 ALA CB C 18.767 0.4 1 821 190 195 ALA N N 122.118 0.2 1 822 191 196 LYS H H 9.266 0.01 1 823 191 196 LYS C C 176.880 0.1 1 824 191 196 LYS CA C 57.884 0.1 1 825 191 196 LYS CB C 33.292 0.4 1 826 191 196 LYS N N 122.686 0.2 1 827 192 197 LEU H H 7.213 0.01 1 828 192 197 LEU C C 175.445 0.1 1 829 192 197 LEU CA C 53.107 0.1 1 830 192 197 LEU CB C 46.835 0.4 1 831 192 197 LEU N N 114.458 0.2 1 832 193 198 VAL H H 9.065 0.01 1 833 193 198 VAL C C 174.213 0.1 1 834 193 198 VAL CA C 60.588 0.1 1 835 193 198 VAL CB C 32.684 0.4 1 836 193 198 VAL N N 122.023 0.2 1 837 194 199 VAL H H 9.130 0.01 1 838 194 199 VAL C C 174.741 0.1 1 839 194 199 VAL CA C 59.084 0.1 1 840 194 199 VAL CB C 33.085 0.4 1 841 194 199 VAL N N 126.033 0.2 1 842 197 202 HIS CA C 54.800 0.5 1 843 198 203 SER H H 7.119 0.01 1 844 198 203 SER CA C 57.648 0.1 1 845 198 203 SER CB C 63.172 0.4 1 846 198 203 SER N N 111.514 0.2 1 847 199 204 GLU H H 8.265 0.01 1 848 199 204 GLU C C 176.551 0.1 1 849 199 204 GLU CA C 56.954 0.1 1 850 199 204 GLU CB C 29.870 0.4 1 851 199 204 GLU N N 117.304 0.2 1 852 200 205 VAL H H 7.965 0.01 1 853 200 205 VAL C C 176.516 0.1 1 854 200 205 VAL CA C 63.979 0.1 1 855 200 205 VAL CB C 31.402 0.4 1 856 200 205 VAL N N 118.323 0.2 1 857 201 206 GLY H H 8.125 0.01 1 858 201 206 GLY C C 172.132 0.1 1 859 201 206 GLY CA C 45.136 0.1 1 860 201 206 GLY N N 114.183 0.2 1 861 202 207 ASP H H 7.992 0.01 1 862 202 207 ASP CA C 52.271 0.1 1 863 202 207 ASP CB C 41.542 0.4 1 864 202 207 ASP N N 120.615 0.2 1 865 203 208 ALA H H 8.204 0.01 1 866 203 208 ALA CA C 55.104 0.1 1 867 203 208 ALA CB C 17.489 0.4 1 868 203 208 ALA N N 116.208 0.2 1 869 204 209 SER H H 9.183 0.01 1 870 204 209 SER CA C 62.262 0.1 1 871 204 209 SER N N 119.531 0.2 1 872 205 210 LEU H H 8.110 0.01 1 873 205 210 LEU CA C 58.291 0.1 1 874 205 210 LEU CB C 40.895 0.4 1 875 205 210 LEU N N 119.733 0.2 1 876 208 213 LEU CA C 58.102 0.5 1 877 209 214 THR H H 7.321 0.01 1 878 209 214 THR CA C 67.551 0.5 1 879 209 214 THR CB C 69.419 0.4 1 880 209 214 THR N N 113.854 0.2 1 881 210 215 LEU H H 7.019 0.01 1 882 210 215 LEU CA C 58.671 0.1 1 883 210 215 LEU N N 121.331 0.2 1 884 211 216 GLU H H 8.029 0.01 1 885 211 216 GLU CA C 59.503 0.1 1 886 211 216 GLU CB C 29.384 0.4 1 887 211 216 GLU N N 116.827 0.2 1 888 212 217 GLN H H 8.181 0.01 1 889 212 217 GLN CA C 58.001 0.1 1 890 212 217 GLN CB C 31.375 0.4 1 891 212 217 GLN N N 118.049 0.2 1 892 213 218 ALA H H 8.248 0.01 1 893 213 218 ALA CA C 54.982 0.5 1 894 213 218 ALA N N 124.051 0.2 1 895 214 219 VAL H H 8.272 0.01 1 896 214 219 VAL CA C 67.044 0.5 1 897 214 219 VAL N N 119.679 0.2 1 898 215 220 LYS H H 7.788 0.01 1 899 215 220 LYS CA C 59.706 0.5 1 900 215 220 LYS CB C 32.310 0.4 1 901 215 220 LYS N N 120.355 0.2 1 902 216 221 GLY H H 8.166 0.01 1 903 216 221 GLY CA C 46.372 0.1 1 904 216 221 GLY N N 105.866 0.2 1 905 217 222 LEU H H 7.895 0.01 1 906 217 222 LEU CA C 57.711 0.5 1 907 217 222 LEU N N 123.267 0.2 1 908 218 223 ASN H H 8.228 0.01 1 909 218 223 ASN CA C 55.884 0.5 1 910 218 223 ASN CB C 38.305 0.4 1 911 218 223 ASN N N 118.733 0.2 1 912 219 224 GLU H H 8.256 0.01 1 913 219 224 GLU CA C 58.039 0.5 1 914 219 224 GLU CB C 29.737 0.4 1 915 219 224 GLU N N 118.667 0.2 1 916 220 225 SER H H 7.706 0.01 1 917 220 225 SER CA C 60.054 0.5 1 918 220 225 SER CB C 63.842 0.4 1 919 220 225 SER N N 114.729 0.2 1 920 221 226 LYS H H 7.560 0.01 1 921 221 226 LYS CA C 55.901 0.1 1 922 221 226 LYS CB C 32.546 0.4 1 923 221 226 LYS N N 120.970 0.2 1 924 222 227 LYS H H 7.788 0.01 1 925 222 227 LYS N N 122.568 0.2 1 926 223 228 PRO CA C 63.218 0.5 1 927 223 228 PRO CB C 32.088 0.4 1 928 224 229 SER H H 8.299 0.01 1 929 224 229 SER CA C 58.293 0.5 1 930 224 229 SER CB C 64.073 0.4 1 931 224 229 SER N N 116.468 0.2 1 932 225 230 LYS H H 8.105 0.01 1 933 225 230 LYS CA C 54.070 0.5 1 934 225 230 LYS CB C 32.853 0.4 1 935 225 230 LYS N N 123.653 0.2 1 936 226 231 PRO CA C 63.377 0.5 1 937 226 231 PRO CB C 32.068 0.4 1 938 227 232 SER H H 8.269 0.01 1 939 227 232 SER C C 173.851 0.1 1 940 227 232 SER CA C 58.273 0.1 1 941 227 232 SER CB C 63.873 0.4 1 942 227 232 SER N N 116.175 0.2 1 943 228 233 ASN H H 7.896 0.01 1 944 228 233 ASN C C 179.741 0.1 1 945 228 233 ASN CA C 54.956 0.1 1 946 228 233 ASN CB C 40.242 0.4 1 947 228 233 ASN N N 125.442 0.2 1 stop_ save_