data_25080 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The backbone chemical shift assignments of [FeZn]-IMP-1 metallo-beta-lactamase ; _BMRB_accession_number 25080 _BMRB_flat_file_name bmr25080.str _Entry_type original _Submission_date 2014-07-08 _Accession_date 2014-07-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'The chemical shift assignments of [FeZn]-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" 156 "13C chemical shifts" 162 "15N chemical shifts" 156 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-01-27 update author 'update entry citation' 2014-07-16 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25063 'The chemical shift assignments of [ZnZn]-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 [FeZn]IMP-1 _Enzyme_commission_number 3.5.2.6 loop_ _Mol_system_component_name _Mol_label IMP-1 $IMP-1 'FE (III) ION' $entity_FE 'ZINC ION' $entity_ZN stop_ _System_molecular_weight 25741 _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _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 25063 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_FE _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'FE (III) ION' _BMRB_code FE _PDB_code FE _Molecular_mass 55.845 _Mol_charge 3 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE FE FE . 3 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ 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' Escherichia coli BL21(DE3) pETMCSIII stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_FeZN-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_ ############################ # 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 $FeZN-IMP-1_in_vivo save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $FeZN-IMP-1_in_vivo save_ ####################### # Sample conditions # ####################### save_IMP1 _Saveframe_category sample_conditions _Details '20 mM MES (pH 6.5), 100 mM NaCl, in a standard 5 mm tube' 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 . 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 indirect . . . 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' '2D 1H-15N HSQC' stop_ loop_ _Sample_label $FeZN-IMP-1_in_vivo 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 CA C 56.022 0.5 1 2 0 5 THR H H 8.088 0.01 1 3 0 5 THR CA C 62.104 0.5 1 4 0 5 THR N N 113.680 0.1 1 5 1 6 GLY H H 8.262 0.01 1 6 1 6 GLY CA C 45.507 0.5 1 7 1 6 GLY N N 111.031 0.1 1 8 2 7 GLU H H 8.114 0.01 1 9 2 7 GLU CA C 56.598 0.5 1 10 2 7 GLU N N 120.495 0.1 1 11 3 8 SER H H 8.189 0.01 1 12 3 8 SER CA C 58.222 0.5 1 13 3 8 SER N N 116.579 0.1 1 14 4 9 LEU H H 8.055 0.01 1 15 4 9 LEU CA C 53.061 0.5 1 16 4 9 LEU N N 125.135 0.1 1 17 5 10 PRO CA C 62.556 0.5 1 18 6 11 ASP H H 7.722 0.01 1 19 6 11 ASP CA C 53.673 0.5 1 20 6 11 ASP N N 119.569 0.1 1 21 7 12 LEU H H 7.996 0.01 1 22 7 12 LEU CA C 56.194 0.5 1 23 7 12 LEU N N 120.182 0.1 1 24 8 13 LYS H H 9.091 0.01 1 25 8 13 LYS CA C 54.878 0.5 1 26 8 13 LYS N N 128.067 0.1 1 27 9 14 ILE H H 8.180 0.01 1 28 9 14 ILE CA C 61.169 0.5 1 29 9 14 ILE N N 123.674 0.1 1 30 10 15 GLU H H 8.762 0.01 1 31 10 15 GLU CA C 54.523 0.5 1 32 10 15 GLU N N 124.927 0.1 1 33 11 16 LYS H H 9.043 0.01 1 34 11 16 LYS CA C 58.374 0.5 1 35 11 16 LYS N N 126.761 0.1 1 36 12 17 LEU H H 8.935 0.01 1 37 12 17 LEU CA C 55.239 0.5 1 38 12 17 LEU N N 129.963 0.1 1 39 13 18 ASP H H 8.266 0.01 1 40 13 18 ASP CA C 51.405 0.5 1 41 13 18 ASP N N 116.385 0.1 1 42 14 19 GLU H H 9.195 0.01 1 43 14 19 GLU CA C 58.241 0.5 1 44 14 19 GLU N N 122.226 0.1 1 45 15 20 GLY H H 8.659 0.01 1 46 15 20 GLY CA C 46.588 0.5 1 47 15 20 GLY N N 113.998 0.1 1 48 16 21 VAL H H 8.013 0.01 1 49 16 21 VAL CA C 62.109 0.5 1 50 16 21 VAL N N 117.862 0.1 1 51 17 22 TYR H H 9.496 0.01 1 52 17 22 TYR CA C 56.656 0.5 1 53 17 22 TYR N N 127.122 0.1 1 54 18 23 VAL H H 9.588 0.01 1 55 18 23 VAL CA C 60.250 0.5 1 56 18 23 VAL N N 121.313 0.1 1 57 19 24 HIS H H 8.378 0.01 1 58 19 24 HIS CA C 52.617 0.5 1 59 19 24 HIS N N 126.136 0.1 1 60 20 25 THR H H 9.428 0.01 1 61 20 25 THR CA C 62.000 0.5 1 62 20 25 THR N N 120.433 0.1 1 63 28 33 TRP H H 8.222 0.01 1 64 28 33 TRP CA C 57.132 0.5 1 65 28 33 TRP N N 120.296 0.1 1 66 29 34 GLY H H 8.243 0.01 1 67 29 34 GLY CA C 44.587 0.5 1 68 29 34 GLY N N 108.647 0.1 1 69 36 41 LEU CA C 53.086 0.5 1 70 37 42 VAL H H 9.198 0.01 1 71 37 42 VAL CA C 63.183 0.5 1 72 37 42 VAL N N 121.439 0.1 1 73 38 43 VAL H H 8.966 0.01 1 74 38 43 VAL CA C 60.600 0.5 1 75 38 43 VAL N N 126.814 0.1 1 76 39 44 LEU H H 8.988 0.01 1 77 39 44 LEU CA C 53.320 0.5 1 78 39 44 LEU N N 126.645 0.1 1 79 40 45 VAL H H 9.301 0.01 1 80 40 45 VAL CA C 61.711 0.5 1 81 40 45 VAL N N 125.344 0.1 1 82 41 46 ASN CA C 56.110 0.5 1 83 42 47 ALA H H 8.348 0.01 1 84 42 47 ALA CA C 52.882 0.5 1 85 42 47 ALA N N 123.384 0.1 1 86 43 48 GLU H H 8.197 0.01 1 87 43 48 GLU CA C 55.288 0.5 1 88 43 48 GLU N N 119.233 0.1 1 89 44 49 ALA H H 8.814 0.01 1 90 44 49 ALA CA C 50.178 0.5 1 91 44 49 ALA N N 122.275 0.1 1 92 45 50 TYR H H 8.904 0.01 1 93 45 50 TYR CA C 56.662 0.5 1 94 45 50 TYR N N 119.116 0.1 1 95 46 51 LEU H H 8.750 0.01 1 96 46 51 LEU CA C 55.450 0.5 1 97 46 51 LEU N N 123.051 0.1 1 98 54 59 LYS H H 8.197 0.01 1 99 54 59 LYS CA C 59.561 0.5 1 100 54 59 LYS N N 117.947 0.1 1 101 55 60 ASP H H 7.762 0.01 1 102 55 60 ASP CA C 57.023 0.5 1 103 55 60 ASP N N 118.344 0.1 1 104 56 61 THR H H 7.736 0.01 1 105 56 61 THR CA C 68.953 0.5 1 106 56 61 THR N N 120.051 0.1 1 107 57 62 GLU H H 7.758 0.01 1 108 57 62 GLU CA C 59.071 0.5 1 109 57 62 GLU N N 122.277 0.1 1 110 58 63 LYS H H 7.683 0.01 1 111 58 63 LYS CA C 60.055 0.5 1 112 58 63 LYS N N 121.457 0.1 1 113 59 64 LEU H H 7.924 0.01 1 114 59 64 LEU CA C 58.201 0.5 1 115 59 64 LEU N N 121.101 0.1 1 116 60 65 VAL H H 8.266 0.01 1 117 60 65 VAL CA C 67.699 0.5 1 118 60 65 VAL N N 116.712 0.1 1 119 61 66 THR H H 8.550 0.01 1 120 61 66 THR CA C 67.330 0.5 1 121 61 66 THR N N 115.268 0.1 1 122 62 67 TRP H H 7.875 0.01 1 123 62 67 TRP CA C 62.629 0.5 1 124 62 67 TRP N N 122.206 0.1 1 125 63 68 PHE H H 7.391 0.01 1 126 63 68 PHE CA C 63.860 0.5 1 127 63 68 PHE N N 112.943 0.1 1 128 64 69 VAL H H 8.999 0.01 1 129 64 69 VAL CA C 66.613 0.5 1 130 64 69 VAL N N 124.187 0.1 1 131 65 70 GLU H H 8.737 0.01 1 132 65 70 GLU CA C 58.979 0.5 1 133 65 70 GLU N N 120.416 0.1 1 134 66 71 ARG H H 6.818 0.01 1 135 66 71 ARG CA C 56.112 0.5 1 136 66 71 ARG N N 117.240 0.1 1 137 67 72 GLY H H 7.675 0.01 1 138 67 72 GLY CA C 45.367 0.5 1 139 67 72 GLY N N 105.824 0.1 1 140 68 73 TYR H H 7.706 0.01 1 141 68 73 TYR CA C 57.705 0.5 1 142 68 73 TYR N N 119.484 0.1 1 143 69 74 LYS H H 8.165 0.01 1 144 69 74 LYS CA C 54.748 0.5 1 145 69 74 LYS N N 119.956 0.1 1 146 70 75 ILE H H 8.654 0.01 1 147 70 75 ILE CA C 59.372 0.5 1 148 70 75 ILE N N 124.095 0.1 1 149 71 76 LYS H H 8.745 0.01 1 150 71 76 LYS CA C 54.217 0.5 1 151 71 76 LYS N N 128.075 0.1 1 152 72 77 GLY H H 6.797 0.01 1 153 72 77 GLY CA C 45.690 0.5 1 154 72 77 GLY N N 102.151 0.1 1 155 73 78 SER H H 8.379 0.01 1 156 73 78 SER CA C 56.312 0.5 1 157 73 78 SER N N 113.241 0.1 1 158 74 79 ILE H H 9.270 0.01 1 159 74 79 ILE N N 124.837 0.1 1 160 75 80 SER H H 7.930 0.01 1 161 75 80 SER CA C 58.870 0.5 1 162 75 80 SER N N 121.892 0.1 1 163 86 91 ILE H H 7.879 0.01 1 164 86 91 ILE CA C 67.607 0.5 1 165 86 91 ILE N N 121.320 0.1 1 166 87 92 GLU H H 8.829 0.01 1 167 87 92 GLU CA C 60.859 0.5 1 168 87 92 GLU N N 120.342 0.1 1 169 88 93 TRP H H 8.785 0.01 1 170 88 93 TRP CA C 63.180 0.5 1 171 88 93 TRP N N 121.972 0.1 1 172 89 94 LEU H H 8.500 0.01 1 173 89 94 LEU CA C 59.130 0.5 1 174 89 94 LEU N N 120.945 0.1 1 175 90 95 ASN H H 9.156 0.01 1 176 90 95 ASN CA C 55.432 0.5 1 177 90 95 ASN N N 119.434 0.1 1 178 91 96 SER H H 8.087 0.01 1 179 91 96 SER CA C 61.316 0.5 1 180 91 96 SER N N 119.011 0.1 1 181 92 97 ARG H H 7.108 0.01 1 182 92 97 ARG CA C 54.165 0.5 1 183 92 97 ARG N N 122.366 0.1 1 184 93 98 SER H H 7.792 0.01 1 185 93 98 SER CA C 59.208 0.5 1 186 93 98 SER N N 111.038 0.1 1 187 94 99 ILE H H 7.734 0.01 1 188 94 99 ILE CA C 58.587 0.5 1 189 94 99 ILE N N 123.285 0.1 1 190 95 100 PRO CA C 64.517 0.5 1 191 96 101 THR H H 7.114 0.01 1 192 96 101 THR CA C 58.472 0.5 1 193 96 101 THR N N 112.167 0.1 1 194 97 102 TYR H H 9.179 0.01 1 195 97 102 TYR CA C 56.912 0.5 1 196 97 102 TYR N N 120.226 0.1 1 197 98 103 ALA H H 8.291 0.01 1 198 98 103 ALA CA C 51.215 0.5 1 199 98 103 ALA N N 121.696 0.1 1 200 99 104 SER H H 9.343 0.01 1 201 99 104 SER CA C 57.220 0.5 1 202 99 104 SER N N 117.149 0.1 1 203 100 105 GLU H H 7.989 0.01 1 204 100 105 GLU CA C 60.176 0.5 1 205 100 105 GLU N N 120.431 0.1 1 206 101 106 LEU H H 7.959 0.01 1 207 101 106 LEU CA C 57.800 0.5 1 208 101 106 LEU N N 119.795 0.1 1 209 102 107 THR H H 8.141 0.01 1 210 102 107 THR CA C 66.790 0.5 1 211 102 107 THR N N 119.227 0.1 1 212 103 108 ASN H H 8.222 0.01 1 213 103 108 ASN CA C 54.922 0.5 1 214 103 108 ASN N N 119.166 0.1 1 215 104 109 GLU H H 7.974 0.01 1 216 104 109 GLU CA C 59.497 0.5 1 217 104 109 GLU N N 122.767 0.1 1 218 105 110 LEU H H 7.923 0.01 1 219 105 110 LEU CA C 58.188 0.5 1 220 105 110 LEU N N 121.554 0.1 1 221 106 111 LEU H H 8.367 0.01 1 222 106 111 LEU CA C 58.489 0.5 1 223 106 111 LEU N N 120.923 0.1 1 224 107 112 LYS H H 7.840 0.01 1 225 107 112 LYS CA C 59.662 0.5 1 226 107 112 LYS N N 119.797 0.1 1 227 108 113 LYS H H 8.079 0.01 1 228 108 113 LYS CA C 59.553 0.5 1 229 108 113 LYS N N 121.188 0.1 1 230 109 114 ASP H H 7.320 0.01 1 231 109 114 ASP CA C 54.147 0.5 1 232 109 114 ASP N N 117.852 0.1 1 233 110 115 GLY H H 7.951 0.01 1 234 110 115 GLY CA C 46.243 0.5 1 235 110 115 GLY N N 108.329 0.1 1 236 111 116 LYS H H 8.007 0.01 1 237 111 116 LYS CA C 53.535 0.5 1 238 111 116 LYS N N 119.352 0.1 1 239 112 117 VAL H H 7.864 0.01 1 240 112 117 VAL CA C 63.696 0.5 1 241 112 117 VAL N N 120.069 0.1 1 242 113 118 GLN H H 7.764 0.01 1 243 113 118 GLN CA C 55.776 0.5 1 244 113 118 GLN N N 121.844 0.1 1 245 114 119 ALA H H 8.375 0.01 1 246 114 119 ALA CA C 51.831 0.5 1 247 114 119 ALA N N 122.919 0.1 1 248 115 120 THR H H 8.756 0.01 1 249 115 120 THR CA C 63.953 0.5 1 250 115 120 THR N N 114.392 0.1 1 251 116 121 ASN H H 8.398 0.01 1 252 116 121 ASN CA C 52.666 0.5 1 253 116 121 ASN N N 119.387 0.1 1 254 117 122 SER H H 8.403 0.01 1 255 117 122 SER CA C 55.954 0.5 1 256 117 122 SER N N 115.109 0.1 1 257 118 123 PHE H H 6.789 0.01 1 258 118 123 PHE CA C 55.291 0.5 1 259 118 123 PHE N N 115.916 0.1 1 260 119 124 SER H H 8.401 0.01 1 261 119 124 SER CA C 57.086 0.5 1 262 119 124 SER N N 115.730 0.1 1 263 120 125 GLY H H 8.154 0.01 1 264 120 125 GLY CA C 44.353 0.5 1 265 120 125 GLY N N 108.631 0.1 1 266 121 126 VAL H H 8.213 0.01 1 267 121 126 VAL CA C 64.812 0.5 1 268 121 126 VAL N N 117.640 0.1 1 269 122 127 ASN H H 7.664 0.01 1 270 122 127 ASN CA C 52.118 0.5 1 271 122 127 ASN N N 114.869 0.1 1 272 123 128 TYR H H 8.578 0.01 1 273 123 128 TYR CA C 57.134 0.5 1 274 123 128 TYR N N 123.029 0.1 1 275 124 129 TRP H H 8.182 0.01 1 276 124 129 TRP CA C 55.314 0.5 1 277 124 129 TRP N N 127.623 0.1 1 278 125 130 LEU H H 7.243 0.01 1 279 125 130 LEU CA C 56.900 0.5 1 280 125 130 LEU N N 127.025 0.1 1 281 126 131 VAL H H 6.959 0.01 1 282 126 131 VAL CA C 61.588 0.5 1 283 126 131 VAL N N 112.873 0.1 1 284 127 132 LYS CA C 59.383 0.5 1 285 128 133 ASN H H 5.860 0.01 1 286 128 133 ASN CA C 56.263 0.5 1 287 128 133 ASN N N 116.338 0.1 1 288 129 134 LYS H H 7.717 0.01 1 289 129 134 LYS CA C 57.130 0.5 1 290 129 134 LYS N N 115.612 0.1 1 291 130 135 ILE H H 8.500 0.01 1 292 130 135 ILE CA C 62.243 0.5 1 293 130 135 ILE N N 116.765 0.1 1 294 131 136 GLU H H 9.232 0.01 1 295 131 136 GLU CA C 54.731 0.5 1 296 131 136 GLU N N 131.877 0.1 1 297 132 137 VAL H H 9.168 0.01 1 298 132 137 VAL CA C 61.210 0.5 1 299 132 137 VAL N N 126.895 0.1 1 300 133 138 PHE H H 8.728 0.01 1 301 133 138 PHE CA C 55.446 0.5 1 302 133 138 PHE N N 126.965 0.1 1 303 134 139 TYR H H 8.361 0.01 1 304 134 139 TYR CA C 52.480 0.5 1 305 134 139 TYR N N 129.707 0.1 1 306 145 150 VAL H H 8.981 0.01 1 307 145 150 VAL CA C 58.717 0.5 1 308 145 150 VAL N N 111.843 0.1 1 309 146 151 VAL CA C 60.725 0.5 1 310 147 152 TRP H H 9.822 0.01 1 311 147 152 TRP CA C 54.226 0.5 1 312 147 152 TRP N N 131.337 0.1 1 313 148 153 LEU H H 7.940 0.01 1 314 148 153 LEU CA C 50.301 0.5 1 315 148 153 LEU N N 126.233 0.1 1 316 149 154 PRO CA C 64.357 0.5 1 317 150 155 GLU H H 8.617 0.01 1 318 150 155 GLU CA C 59.292 0.5 1 319 150 155 GLU N N 114.364 0.1 1 320 151 156 ARG H H 6.523 0.01 1 321 151 156 ARG CA C 52.944 0.5 1 322 151 156 ARG N N 111.387 0.1 1 323 152 157 LYS H H 7.570 0.01 1 324 152 157 LYS CA C 57.179 0.5 1 325 152 157 LYS N N 114.062 0.1 1 326 153 158 ILE H H 6.320 0.01 1 327 153 158 ILE CA C 60.176 0.5 1 328 153 158 ILE N N 116.178 0.1 1 329 154 159 LEU H H 8.823 0.01 1 330 154 159 LEU CA C 52.332 0.5 1 331 154 159 LEU N N 127.543 0.1 1 332 155 160 PHE H H 10.234 0.01 1 333 155 160 PHE CA C 57.559 0.5 1 334 155 160 PHE N N 127.956 0.1 1 335 160 165 ILE CA C 57.866 0.5 1 336 161 166 LYS H H 6.810 0.01 1 337 161 166 LYS CA C 59.740 0.5 1 338 161 166 LYS N N 122.031 0.1 1 339 172 177 ASN H H 8.260 0.01 1 340 172 177 ASN N N 118.413 0.1 1 341 173 178 ILE H H 8.370 0.01 1 342 173 178 ILE N N 121.992 0.1 1 343 174 179 GLU H H 8.006 0.01 1 344 174 179 GLU CA C 59.273 0.5 1 345 174 179 GLU N N 117.574 0.1 1 346 175 180 ALA H H 7.436 0.01 1 347 175 180 ALA CA C 52.966 0.5 1 348 175 180 ALA N N 118.574 0.1 1 349 176 181 TRP H H 7.812 0.01 1 350 176 181 TRP N N 119.747 0.1 1 351 177 182 PRO CA C 67.256 0.5 1 352 178 183 LYS H H 7.327 0.01 1 353 178 183 LYS CA C 60.228 0.5 1 354 178 183 LYS N N 118.456 0.1 1 355 179 184 SER H H 8.745 0.01 1 356 179 184 SER CA C 60.638 0.5 1 357 179 184 SER N N 119.199 0.1 1 358 180 185 ALA H H 9.538 0.01 1 359 180 185 ALA CA C 55.165 0.5 1 360 180 185 ALA N N 123.598 0.1 1 361 181 186 LYS H H 8.328 0.01 1 362 181 186 LYS CA C 60.391 0.5 1 363 181 186 LYS N N 122.287 0.1 1 364 183 188 LEU H H 8.156 0.01 1 365 183 188 LEU CA C 58.215 0.5 1 366 183 188 LEU N N 118.609 0.1 1 367 184 189 LYS H H 7.948 0.01 1 368 184 189 LYS CA C 59.233 0.5 1 369 184 189 LYS N N 117.523 0.1 1 370 185 190 SER H H 7.789 0.01 1 371 185 190 SER CA C 61.075 0.5 1 372 185 190 SER N N 113.343 0.1 1 373 186 191 LYS H H 7.677 0.01 1 374 186 191 LYS CA C 58.140 0.5 1 375 186 191 LYS N N 120.861 0.1 1 376 187 192 TYR H H 7.624 0.01 1 377 187 192 TYR CA C 56.874 0.5 1 378 187 192 TYR N N 114.286 0.1 1 379 188 193 GLY H H 7.083 0.01 1 380 188 193 GLY CA C 47.217 0.5 1 381 188 193 GLY N N 106.073 0.1 1 382 189 194 LYS H H 7.491 0.01 1 383 189 194 LYS CA C 55.121 0.5 1 384 189 194 LYS N N 115.425 0.1 1 385 190 195 ALA H H 7.693 0.01 1 386 190 195 ALA CA C 54.009 0.5 1 387 190 195 ALA N N 122.312 0.1 1 388 191 196 LYS H H 9.243 0.01 1 389 191 196 LYS CA C 58.166 0.5 1 390 191 196 LYS N N 122.978 0.1 1 391 192 197 LEU H H 7.224 0.01 1 392 192 197 LEU CA C 53.143 0.5 1 393 192 197 LEU N N 114.408 0.1 1 394 193 198 VAL H H 9.110 0.01 1 395 193 198 VAL CA C 60.720 0.5 1 396 193 198 VAL N N 122.071 0.1 1 397 194 199 VAL H H 9.031 0.01 1 398 194 199 VAL CA C 59.296 0.5 1 399 194 199 VAL N N 126.050 0.1 1 400 199 204 GLU H H 8.424 0.01 1 401 199 204 GLU CA C 57.230 0.5 1 402 199 204 GLU N N 117.664 0.1 1 403 200 205 VAL H H 7.989 0.01 1 404 200 205 VAL CA C 64.336 0.5 1 405 200 205 VAL N N 118.434 0.1 1 406 201 206 GLY H H 8.074 0.01 1 407 201 206 GLY CA C 45.057 0.5 1 408 201 206 GLY N N 114.684 0.1 1 409 202 207 ASP H H 8.007 0.01 1 410 202 207 ASP CA C 52.256 0.5 1 411 202 207 ASP N N 120.629 0.1 1 412 203 208 ALA H H 8.227 0.01 1 413 203 208 ALA CA C 55.255 0.5 1 414 203 208 ALA N N 116.322 0.1 1 415 204 209 SER H H 9.182 0.01 1 416 204 209 SER CA C 62.635 0.5 1 417 204 209 SER N N 119.655 0.1 1 418 205 210 LEU H H 8.108 0.01 1 419 205 210 LEU CA C 58.302 0.5 1 420 205 210 LEU N N 119.727 0.1 1 421 209 214 THR H H 7.277 0.01 1 422 209 214 THR CA C 67.686 0.5 1 423 209 214 THR N N 113.837 0.1 1 424 210 215 LEU H H 7.005 0.01 1 425 210 215 LEU CA C 59.005 0.5 1 426 210 215 LEU N N 121.500 0.1 1 427 211 216 GLU H H 7.978 0.01 1 428 211 216 GLU N N 116.640 0.1 1 429 212 217 GLN H H 8.160 0.01 1 430 212 217 GLN N N 117.978 0.1 1 431 213 218 ALA H H 8.387 0.01 1 432 213 218 ALA CA C 55.231 0.5 1 433 213 218 ALA N N 124.473 0.1 1 434 214 219 VAL H H 8.317 0.01 1 435 214 219 VAL CA C 67.226 0.5 1 436 214 219 VAL N N 119.593 0.1 1 437 215 220 LYS H H 7.849 0.01 1 438 215 220 LYS CA C 60.111 0.5 1 439 215 220 LYS N N 120.532 0.1 1 440 216 221 GLY H H 8.226 0.01 1 441 216 221 GLY CA C 46.680 0.5 1 442 216 221 GLY N N 105.935 0.1 1 443 217 222 LEU H H 8.069 0.01 1 444 217 222 LEU CA C 58.198 0.5 1 445 217 222 LEU N N 123.878 0.1 1 446 218 223 ASN H H 8.243 0.01 1 447 218 223 ASN CA C 56.098 0.5 1 448 218 223 ASN N N 118.804 0.1 1 449 219 224 GLU H H 8.306 0.01 1 450 219 224 GLU CA C 58.220 0.5 1 451 219 224 GLU N N 118.795 0.1 1 452 220 225 SER H H 7.758 0.01 1 453 220 225 SER CA C 60.201 0.5 1 454 220 225 SER N N 114.829 0.1 1 455 221 226 LYS H H 7.590 0.01 1 456 221 226 LYS CA C 56.152 0.5 1 457 221 226 LYS N N 121.016 0.1 1 458 222 227 LYS H H 7.814 0.01 1 459 222 227 LYS CA C 54.677 0.5 1 460 222 227 LYS N N 122.627 0.1 1 461 223 228 PRO CA C 63.366 0.5 1 462 224 229 SER H H 8.325 0.01 1 463 224 229 SER CA C 58.459 0.5 1 464 224 229 SER N N 116.594 0.1 1 465 225 230 LYS H H 8.135 0.01 1 466 225 230 LYS CA C 54.211 0.5 1 467 225 230 LYS N N 123.724 0.1 1 468 226 231 PRO CA C 63.437 0.5 1 469 227 232 SER H H 8.300 0.01 1 470 227 232 SER CA C 58.423 0.5 1 471 227 232 SER N N 116.332 0.1 1 472 228 233 ASN H H 7.926 0.01 1 473 228 233 ASN CA C 55.061 0.5 1 474 228 233 ASN N N 125.632 0.1 1 stop_ save_