data_7237 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Investigation of Tyr105 Mutants in TEM-1 beta-lactamase Suggests Active-Site Dynamical Coupling ; _BMRB_accession_number 7237 _BMRB_flat_file_name bmr7237.str _Entry_type original _Submission_date 2006-07-18 _Accession_date 2006-07-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Doucet Nicolas . . 2 Savard Pierre-Yves . . 3 Pelletier Joelle N. . 4 Gagne Stephane M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 248 "13C chemical shifts" 248 "15N chemical shifts" 248 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-01-09 original author . stop_ _Original_release_date 2007-01-09 save_ ############################# # Citation for this entry # ############################# save_Citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16981701 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Savard Pierre-Yves . . 2 Gagne Stephane M. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 45 _Journal_issue 38 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11414 _Page_last 11424 _Year 2006 _Details 'The first and second authors contributed equally to this work.' loop_ _Keyword '15N relaxation' 'Enzyme dynamics' NMR 'TEM-1 beta-lactamase' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Mutants Y105G of TEM-1 beta-lactamase' _Enzyme_commission_number 3.5.2.6 loop_ _Mol_system_component_name _Mol_label 'TEM-1 Y105G' $TEM-1_beta-lactamase stop_ _System_molecular_weight 29000 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Cyclic amide hydrolase (beta-lactamase) (E.C. 3.5.2.6)' stop_ _Database_query_date . _Details 'Four different mutants of the protein TEM-1 in four entries.' save_ ######################## # Monomeric polymers # ######################## save_TEM-1_beta-lactamase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common TEM-1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function beta-lactamase stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 263 _Mol_residue_sequence ; HPETLVKVKDAEDQLGARVG YIELDLNSGKILESFRPEER FPMMSTFKVLLCGAVLSRVD AGQEQLGRRIHYSQNDLVEG SPVTEKHLTDGMTVRELCSA AITMSDNTAANLLLTTIGGP KELTAFLHNMGDHVTRLDRW EPELNEAIPNDERDTTMPAA MATTLRKLLTGELLTLASRQ QLIDWMEADKVAGPLLRSAL PAGWFIADKSGAGERGSRGI IAALGPDGKPSRIVVIYTTG SQATMDERNRQIAEIGASLI KHW ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 26 HIS 2 27 PRO 3 28 GLU 4 29 THR 5 30 LEU 6 31 VAL 7 32 LYS 8 33 VAL 9 34 LYS 10 35 ASP 11 36 ALA 12 37 GLU 13 38 ASP 14 39 GLN 15 40 LEU 16 41 GLY 17 42 ALA 18 43 ARG 19 44 VAL 20 45 GLY 21 46 TYR 22 47 ILE 23 48 GLU 24 49 LEU 25 50 ASP 26 51 LEU 27 52 ASN 28 53 SER 29 54 GLY 30 55 LYS 31 56 ILE 32 57 LEU 33 58 GLU 34 59 SER 35 60 PHE 36 61 ARG 37 62 PRO 38 63 GLU 39 64 GLU 40 65 ARG 41 66 PHE 42 67 PRO 43 68 MET 44 69 MET 45 70 SER 46 71 THR 47 72 PHE 48 73 LYS 49 74 VAL 50 75 LEU 51 76 LEU 52 77 CYS 53 78 GLY 54 79 ALA 55 80 VAL 56 81 LEU 57 82 SER 58 83 ARG 59 84 VAL 60 85 ASP 61 86 ALA 62 87 GLY 63 88 GLN 64 89 GLU 65 90 GLN 66 91 LEU 67 92 GLY 68 93 ARG 69 94 ARG 70 95 ILE 71 96 HIS 72 97 TYR 73 98 SER 74 99 GLN 75 100 ASN 76 101 ASP 77 102 LEU 78 103 VAL 79 104 GLU 80 105 GLY 81 106 SER 82 107 PRO 83 108 VAL 84 109 THR 85 110 GLU 86 111 LYS 87 112 HIS 88 113 LEU 89 114 THR 90 115 ASP 91 116 GLY 92 117 MET 93 118 THR 94 119 VAL 95 120 ARG 96 121 GLU 97 122 LEU 98 123 CYS 99 124 SER 100 125 ALA 101 126 ALA 102 127 ILE 103 128 THR 104 129 MET 105 130 SER 106 131 ASP 107 132 ASN 108 133 THR 109 134 ALA 110 135 ALA 111 136 ASN 112 137 LEU 113 138 LEU 114 139 LEU 115 140 THR 116 141 THR 117 142 ILE 118 143 GLY 119 144 GLY 120 145 PRO 121 146 LYS 122 147 GLU 123 148 LEU 124 149 THR 125 150 ALA 126 151 PHE 127 152 LEU 128 153 HIS 129 154 ASN 130 155 MET 131 156 GLY 132 157 ASP 133 158 HIS 134 159 VAL 135 160 THR 136 161 ARG 137 162 LEU 138 163 ASP 139 164 ARG 140 165 TRP 141 166 GLU 142 167 PRO 143 168 GLU 144 169 LEU 145 170 ASN 146 171 GLU 147 172 ALA 148 173 ILE 149 174 PRO 150 175 ASN 151 176 ASP 152 177 GLU 153 178 ARG 154 179 ASP 155 180 THR 156 181 THR 157 182 MET 158 183 PRO 159 184 ALA 160 185 ALA 161 186 MET 162 187 ALA 163 188 THR 164 189 THR 165 190 LEU 166 191 ARG 167 192 LYS 168 193 LEU 169 194 LEU 170 195 THR 171 196 GLY 172 197 GLU 173 198 LEU 174 199 LEU 175 200 THR 176 201 LEU 177 202 ALA 178 203 SER 179 204 ARG 180 205 GLN 181 206 GLN 182 207 LEU 183 208 ILE 184 209 ASP 185 210 TRP 186 211 MET 187 212 GLU 188 213 ALA 189 214 ASP 190 215 LYS 191 216 VAL 192 217 ALA 193 218 GLY 194 219 PRO 195 220 LEU 196 221 LEU 197 222 ARG 198 223 SER 199 224 ALA 200 225 LEU 201 226 PRO 202 227 ALA 203 228 GLY 204 229 TRP 205 230 PHE 206 231 ILE 207 232 ALA 208 233 ASP 209 234 LYS 210 235 SER 211 236 GLY 212 237 ALA 213 238 GLY 214 239 GLU 215 240 ARG 216 241 GLY 217 242 SER 218 243 ARG 219 244 GLY 220 245 ILE 221 246 ILE 222 247 ALA 223 248 ALA 224 249 LEU 225 250 GLY 226 251 PRO 227 252 ASP 228 253 GLY 229 254 LYS 230 255 PRO 231 256 SER 232 257 ARG 233 258 ILE 234 259 VAL 235 260 VAL 236 261 ILE 237 262 TYR 238 263 THR 239 264 THR 240 265 GLY 241 266 SER 242 267 GLN 243 268 ALA 244 269 THR 245 270 MET 246 271 ASP 247 272 GLU 248 273 ARG 249 274 ASN 250 275 ARG 251 276 GLN 252 277 ILE 253 278 ALA 254 279 GLU 255 280 ILE 256 281 GLY 257 282 ALA 258 283 SER 259 284 LEU 260 285 ILE 261 286 LYS 262 287 HIS 263 288 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16392 TEM-1 100.00 286 99.24 99.24 0.00e+00 BMRB 6024 "TEM-1 beta-lactamase" 100.00 263 99.24 99.24 0.00e+00 BMRB 6357 TEM-1 100.00 263 99.62 99.62 0.00e+00 BMRB 7236 TEM-1_beta-lactamase 100.00 263 99.62 99.62 0.00e+00 BMRB 7238 TEM-1_beta-lactamase 100.00 263 99.62 99.62 0.00e+00 BMRB 7239 TEM-1_beta-lactamase 100.00 263 99.62 99.62 0.00e+00 PDB 1AXB "Tem-1 Beta-Lactamase From Escherichia Coli Inhibited With An Acylation Transition State Analog" 100.00 263 98.86 99.24 0.00e+00 PDB 1BT5 "Crystal Structure Of The Imipenem Inhibited Tem-1 Beta-Lactamase From Escherichia Coli" 100.00 263 98.86 99.24 0.00e+00 PDB 1BTL "Crystal Structure Of Escherichia Coli Tem1 Beta-Lactamase At 1.8 Angstroms Resolution" 100.00 263 98.86 99.24 0.00e+00 PDB 1CK3 "N276d Mutant Of Escherichia Coli Tem-1 Beta-Lactamase" 100.00 263 98.48 99.24 0.00e+00 PDB 1ERM "X-Ray Crystal Structure Of Tem-1 Beta Lactamase In Complex With A Designed Boronic Acid Inhibitor (1r)-1-Acetamido-2-(3-Carboxy" 100.00 263 99.24 99.24 0.00e+00 PDB 1ERO "X-Ray Crystal Structure Of Tem-1 Beta Lactamase In Complex With A Designed Boronic Acid Inhibitor (1r)-2- Phenylacetamido-2-(3-" 100.00 263 99.62 99.62 0.00e+00 PDB 1ERQ "X-Ray Crystal Structure Of Tem-1 Beta Lactamase In Complex With A Designed Boronic Acid Inhibitor (1r)-1-Acetamido-2- (3-Carbox" 100.00 263 99.62 99.62 0.00e+00 PDB 1ESU "S235a Mutant Of Tem1 Beta-Lactamase" 100.00 263 99.24 99.62 0.00e+00 PDB 1FQG "Molecular Structure Of The Acyl-Enzyme Intermediate In Tem- 1 Beta-Lactamase" 100.00 263 99.24 99.24 0.00e+00 PDB 1HTZ "Crystal Structure Of Tem52 Beta-Lactamase" 100.00 263 98.48 98.86 0.00e+00 PDB 1JTD "Crystal Structure Of Beta-Lactamase Inhibitor Protein-Ii In Complex With Tem-1 Beta-Lactamase" 100.00 263 99.24 99.24 0.00e+00 PDB 1JTG "Crystal Structure Of Tem-1 Beta-lactamase / Beta-lactamase Inhibitor Protein Complex" 100.00 263 98.86 99.24 0.00e+00 PDB 1JVJ "Crystal Structure Of N132a Mutant Of Tem-1 Beta-Lactamase In Complex With A N-Formimidoyl-Thienamycine" 100.00 263 99.24 99.24 0.00e+00 PDB 1JWP "Structure Of M182t Mutant Of Tem-1 Beta-Lactamase" 100.00 263 99.24 99.24 0.00e+00 PDB 1JWV "Crystal Structure Of G238a Mutant Of Tem-1 Beta-Lactamase In Complex With A Boronic Acid Inhibitor (Sefb4)" 100.00 263 99.24 99.24 0.00e+00 PDB 1JWZ "Crystal Structure Of Tem-64 Beta-Lactamase In Complex With A Boronic Acid Inhibitor (105)" 100.00 263 98.48 98.86 0.00e+00 PDB 1LHY "Crystal Structure Of Tem-30 Beta-lactamase At 2.0 Angstrom" 100.00 263 99.24 99.24 0.00e+00 PDB 1LI0 "Crystal Structure Of Tem-32 Beta-Lactamase At 1.6 Angstrom" 100.00 263 98.86 99.24 0.00e+00 PDB 1LI9 "Crystal Structure Of Tem-34 Beta-lactamase At 1.5 Angstrom" 100.00 263 99.24 99.62 0.00e+00 PDB 1M40 "Ultra High Resolution Crystal Structure Of Tem-1" 100.00 263 99.24 99.24 0.00e+00 PDB 1NXY "Crystal Structure Of The Complex Between M182t Mutant Of Tem-1 And A Boronic Acid Inhibitor (Sm2)" 100.00 263 99.24 99.24 0.00e+00 PDB 1NY0 "Crystal Structure Of The Complex Between M182t Mutant Of Tem-1 And A Boronic Acid Inhibitor (Nbf)" 100.00 263 99.24 99.24 0.00e+00 PDB 1NYM "Crystal Structure Of The Complex Between M182t Mutant Of Tem-1 And A Boronic Acid Inhibitor (Cxb)" 100.00 263 99.24 99.24 0.00e+00 PDB 1NYY "Crystal Structure Of The Complex Between M182t Mutant Of Tem-1 And A Boronic Acid Inhibitor (105)" 100.00 263 99.24 99.24 0.00e+00 PDB 1PZO "Tem-1 Beta-lactamase In Complex With A Novel, Core- Disrupting, Allosteric Inhibitor" 100.00 263 99.24 99.24 0.00e+00 PDB 1PZP "Tem-1 Beta-Lactamase In Complex With A Novel, Core- Disrupting, Allosteric Inhibitor" 100.00 263 99.24 99.24 0.00e+00 PDB 1S0W "1b Lactamse B LACTAMASE INHIBITOR" 100.00 263 99.62 99.62 0.00e+00 PDB 1TEM "6 Alpha Hydroxymethyl Penicilloic Acid Acylated On The Tem- 1 Beta-Lactamase From Escherichia Coli" 100.00 263 98.86 99.24 0.00e+00 PDB 1XPB "Structure Of Beta-Lactamase Tem1" 100.00 263 99.62 99.62 0.00e+00 PDB 1XXM "The Modular Architecture Of Protein-Protein Binding Site" 100.00 263 98.86 99.24 0.00e+00 PDB 1YT4 "Crystal Structure Of Tem-76 Beta-Lactamase At 1.4 Angstrom Resolution" 100.00 263 99.24 99.24 0.00e+00 PDB 1ZG4 "Tem1 Beta Lactamase" 100.00 286 98.86 99.24 0.00e+00 PDB 1ZG6 "Tem1 Beta Lactamase Mutant S70g" 100.00 286 98.48 98.86 0.00e+00 PDB 2B5R "1b Lactamase B LACTAMASE INHIBITOR" 100.00 263 98.86 99.24 0.00e+00 PDB 3C7U "Structural Insight Into The Kinetics And Cp Of Interactions Between Tem-1-Lactamase And Blip" 100.00 263 98.86 99.24 0.00e+00 PDB 3C7V "Structural Insight Into The Kinetics And Delta-Cp Of Interactions Between Tem-1 Beta-Lactamase And Blip" 100.00 263 98.86 99.24 0.00e+00 PDB 3CMZ "Tem-1 Class-A Beta-Lactamase L201p Mutant Apo Structure" 100.00 263 99.24 99.24 0.00e+00 PDB 3GMW "Crystal Structure Of Beta-Lactamse Inhibitory Protein-I (Blip-I) In Complex With Tem-1 Beta-Lactamase" 99.24 261 99.23 99.23 0.00e+00 PDB 3JYI "Structural And Biochemical Evidence That A Tem-1 {beta}- Lactamase Asn170gly Active Site Mutant Acts Via Substrate- Assisted Ca" 100.00 263 99.24 99.24 0.00e+00 PDB 3P98 "The Crystal Structure Of The Extended Spectrum Beta-Lactamase Tem-72 Reveals Inhibition By Citrate" 100.00 286 98.10 98.86 0.00e+00 PDB 4GKU "Crystal Structure Of Beta Lactamase In Pet-15b" 100.00 263 99.62 99.62 0.00e+00 PDB 4IBX "Crystal Structure Of Stabilized Tem-1 Beta-lactamase Variant V.13" 100.00 263 96.96 96.96 0.00e+00 PDB 4MEZ "Crystal Structure Of M68l/m69t Double Mutant Tem-1" 100.00 263 98.86 99.24 0.00e+00 DBJ BAA00795 "ampicillin resistance protein [Shuttle vector pHY320PLK]" 100.00 286 99.62 99.62 0.00e+00 DBJ BAA03488 "beta-lactamase [Cloning vector pKF2]" 100.00 286 98.86 99.24 0.00e+00 DBJ BAA12825 "beta-lactamase [Cloning vector pBEN66]" 100.00 286 98.86 99.24 0.00e+00 DBJ BAA14388 "Ap resistance protein [synthetic construct]" 100.00 286 99.62 99.62 0.00e+00 DBJ BAA19239 "beta-lactamase [Cloning vector pBEN77]" 100.00 286 98.86 99.24 0.00e+00 EMBL CAA04868 "beta-lactamase [Escherichia coli]" 100.00 286 98.86 99.24 0.00e+00 EMBL CAA05682 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.24 0.00e+00 EMBL CAA05685 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.24 0.00e+00 EMBL CAA05686 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.24 0.00e+00 EMBL CAA05689 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.24 0.00e+00 GB AAA24057 "beta-lactamase [Escherichia coli]" 100.00 286 98.86 99.24 0.00e+00 GB AAA25053 "TEM-26B beta-lactamase [Klebsiella oxytoca]" 100.00 286 99.24 99.24 0.00e+00 GB AAA32208 "ampicillinase, partial [Enterobacteria phage f1]" 76.81 225 99.50 99.50 1.72e-142 GB AAA53119 "beta-lactamase [unidentified cloning vector]" 100.00 286 98.86 99.24 0.00e+00 GB AAA53121 "beta-lactamase [unidentified cloning vector]" 100.00 286 98.86 99.24 0.00e+00 PIR S60310 "extended spectrum beta-lactamase CAZ-2 - Klebsiella pneumoniae" 100.00 286 98.10 98.86 0.00e+00 PIR S60312 "extended spectrum beta-lactamase CAZ-7 - Klebsiella pneumoniae" 100.00 286 98.48 99.24 0.00e+00 PIR T51301 "beta-lactamase (EC 3.5.2.6) - fission yeast (Schizosaccharomyces pombe)" 100.00 286 98.86 99.24 0.00e+00 PRF 2018199A "beta lactamase IRT-4" 100.00 286 99.62 99.62 0.00e+00 REF NP_052173 "beta-lactamase [Neisseria gonorrhoeae]" 100.00 286 99.62 99.62 0.00e+00 REF NP_569411 "beta-lactamase [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 286 99.62 99.62 0.00e+00 REF NP_608310 "TEM beta-lactamase [Klebsiella pneumoniae]" 100.00 286 99.62 99.62 0.00e+00 REF NP_758767 "beta lactamase [Erwinia amylovora ATCC BAA-2158]" 98.48 283 97.68 97.68 0.00e+00 REF NP_775035 "BlaTEM1 [Citrobacter freundii]" 100.00 286 99.62 99.62 0.00e+00 SP P62593 "RecName: Full=Beta-lactamase TEM; AltName: Full=IRT-4; AltName: Full=Penicillinase; AltName: Full=TEM-1; AltName: Full=TEM-16/C" 100.00 286 99.62 99.62 0.00e+00 SP P62594 "RecName: Full=Beta-lactamase TEM; AltName: Full=Penicillinase; Flags: Precursor [Salmonella enterica subsp. enterica serovar Ty" 100.00 286 99.62 99.62 0.00e+00 SP Q48406 "RecName: Full=Beta-lactamase TEM-12; Flags: Precursor [Klebsiella oxytoca]" 100.00 286 99.24 99.24 0.00e+00 TPE CAJ85677 "TPA: beta lactamase [Birmingham IncP-alpha plasmid]" 100.00 286 99.24 99.62 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TEM-1_beta-lactamase 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $TEM-1_beta-lactamase 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '0.8 mM, pH 6.6 for all Y105X mutants' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TEM-1_beta-lactamase 0.8 mM '[U-13C; U-15N]' imidazole 4 mM . DSS 0.1 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name VNMR _Version 6.1c loop_ _Vendor _Address _Electronic_address Varian ; Varian Inc. 3120 Hansen Way Palo Alto, CA 94304-1030 USA ; http://www.varianinc.com stop_ loop_ _Task 'spectra acquisition' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Vendor _Address _Electronic_address 'Frank Delaglio (Ad Bax)' http://spin.niddk.nih.gov/NMRPipe/ http://spin.niddk.nih.gov/bax/people/delaglio.html stop_ loop_ _Task 'Transform/process data' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name NMRView _Version 5.2.2 loop_ _Vendor _Address _Electronic_address 'One moon scientific' http://www.onemoonscientific.com/index.html http://www.onemoonscientific.com/index.html stop_ loop_ _Task 'analyze data' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details 'with cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _Sample_label $sample_1 save_ save_3D-HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCO _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-CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-CBCA(CO)NH _Sample_label $sample_1 save_ save_15N-HSQC _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D-HNCO _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D-HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D-CBCA(CO)NH _Saveframe_category NMR_applied_experiment _Experiment_name 3D-CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details ; The enzymes were dissolved to a concentration of 0.8 mM in a 90 % H2O:10 % D2O solution containing 4 mM imidazole and 0.1 mM DSS (pH = 6.6). All NMR experiments were performed at 30?C on a Varian INOVA 600 spectrometer operating at a proton frequency of 599.739 MHz equipped with a z-axis gradient and a triple resonance cryoprobe. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.2 pH temperature 303 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0 internal indirect . . . 0.25144953 $Citation_1 $Citation_1 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 $Citation_1 $Citation_1 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 $Citation_1 $Citation_1 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details 'same for all Y105X mutants' loop_ _Software_label $software_1 stop_ loop_ _Experiment_label 15N-HSQC 3D-HNCO 3D-HN(CO)CA 3D-CBCA(CO)NH stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'TEM-1 Y105G' _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 27 2 PRO C C 179.325 0.2 1 2 28 3 GLU H H 11.052 0.02 1 3 28 3 GLU C C 179.542 0.2 1 4 28 3 GLU N N 121.725 0.15 1 5 29 4 THR H H 7.793 0.02 1 6 29 4 THR C C 176.039 0.2 1 7 29 4 THR N N 118.873 0.15 1 8 30 5 LEU H H 7.043 0.02 1 9 30 5 LEU C C 179.005 0.2 1 10 30 5 LEU N N 120.141 0.15 1 11 31 6 VAL H H 7.508 0.02 1 12 31 6 VAL C C 178.402 0.2 1 13 31 6 VAL N N 119.787 0.15 1 14 32 7 LYS H H 7.294 0.02 1 15 32 7 LYS C C 178.396 0.2 1 16 32 7 LYS N N 119.458 0.15 1 17 33 8 VAL H H 8.305 0.02 1 18 33 8 VAL C C 176.749 0.2 1 19 33 8 VAL N N 122.928 0.15 1 20 34 9 LYS H H 7.692 0.02 1 21 34 9 LYS C C 179.300 0.2 1 22 34 9 LYS N N 118.624 0.15 1 23 35 10 ASP H H 8.333 0.02 1 24 35 10 ASP C C 178.128 0.2 1 25 35 10 ASP N N 120.490 0.15 1 26 36 11 ALA H H 8.518 0.02 1 27 36 11 ALA C C 179.555 0.2 1 28 36 11 ALA N N 122.226 0.15 1 29 37 12 GLU H H 7.961 0.02 1 30 37 12 GLU C C 180.451 0.2 1 31 37 12 GLU N N 117.715 0.15 1 32 38 13 ASP H H 7.937 0.02 1 33 38 13 ASP C C 179.136 0.2 1 34 38 13 ASP N N 119.972 0.15 1 35 39 14 GLN H H 8.865 0.02 1 36 39 14 GLN C C 179.150 0.2 1 37 39 14 GLN N N 118.495 0.15 1 38 40 15 LEU H H 8.747 0.02 1 39 40 15 LEU C C 178.982 0.2 1 40 40 15 LEU N N 114.389 0.15 1 41 41 16 GLY H H 8.107 0.02 1 42 41 16 GLY C C 173.995 0.2 1 43 41 16 GLY N N 113.052 0.15 1 44 42 17 ALA H H 7.748 0.02 1 45 42 17 ALA C C 174.870 0.2 1 46 42 17 ALA N N 119.601 0.15 1 47 43 18 ARG H H 7.634 0.02 1 48 43 18 ARG C C 177.718 0.2 1 49 43 18 ARG N N 115.435 0.15 1 50 44 19 VAL H H 10.665 0.02 1 51 44 19 VAL C C 172.672 0.2 1 52 44 19 VAL N N 128.475 0.15 1 53 45 20 GLY H H 8.879 0.02 1 54 45 20 GLY C C 172.496 0.2 1 55 45 20 GLY N N 111.327 0.15 1 56 46 21 TYR H H 9.424 0.02 1 57 46 21 TYR C C 174.020 0.2 1 58 46 21 TYR N N 124.093 0.15 1 59 47 22 ILE H H 8.037 0.02 1 60 47 22 ILE C C 171.476 0.2 1 61 47 22 ILE N N 125.470 0.15 1 62 48 23 GLU H H 7.817 0.02 1 63 48 23 GLU C C 175.012 0.2 1 64 48 23 GLU N N 123.525 0.15 1 65 49 24 LEU H H 9.698 0.02 1 66 49 24 LEU C C 175.597 0.2 1 67 49 24 LEU N N 126.881 0.15 1 68 50 25 ASP H H 9.055 0.02 1 69 50 25 ASP C C 176.778 0.2 1 70 50 25 ASP N N 126.646 0.15 1 71 51 26 LEU H H 8.242 0.02 1 72 51 26 LEU C C 177.552 0.2 1 73 51 26 LEU N N 128.923 0.15 1 74 52 27 ASN H H 8.689 0.02 1 75 52 27 ASN C C 176.949 0.2 1 76 52 27 ASN N N 116.616 0.15 1 77 53 28 SER H H 8.552 0.02 1 78 53 28 SER C C 176.486 0.2 1 79 53 28 SER N N 112.840 0.15 1 80 54 29 GLY H H 7.996 0.02 1 81 54 29 GLY C C 172.347 0.2 1 82 54 29 GLY N N 112.237 0.15 1 83 55 30 LYS H H 7.681 0.02 1 84 55 30 LYS C C 176.121 0.2 1 85 55 30 LYS N N 119.413 0.15 1 86 56 31 ILE H H 8.664 0.02 1 87 56 31 ILE C C 176.111 0.2 1 88 56 31 ILE N N 124.917 0.15 1 89 57 32 LEU H H 8.930 0.02 1 90 57 32 LEU C C 177.049 0.2 1 91 57 32 LEU N N 130.445 0.15 1 92 58 33 GLU H H 7.541 0.02 1 93 58 33 GLU C C 174.653 0.2 1 94 58 33 GLU N N 115.927 0.15 1 95 59 34 SER H H 9.002 0.02 1 96 59 34 SER C C 171.966 0.2 1 97 59 34 SER N N 115.534 0.15 1 98 60 35 PHE H H 9.545 0.02 1 99 60 35 PHE C C 173.299 0.2 1 100 60 35 PHE N N 122.366 0.15 1 101 61 36 ARG H H 8.763 0.02 1 102 61 36 ARG N N 121.809 0.15 1 103 62 37 PRO C C 177.507 0.2 1 104 63 38 GLU H H 8.484 0.02 1 105 63 38 GLU C C 175.034 0.2 1 106 63 38 GLU N N 116.514 0.15 1 107 64 39 GLU H H 6.850 0.02 1 108 64 39 GLU C C 174.880 0.2 1 109 64 39 GLU N N 117.315 0.15 1 110 65 40 ARG H H 8.301 0.02 1 111 65 40 ARG C C 177.201 0.2 1 112 65 40 ARG N N 117.190 0.15 1 113 66 41 PHE H H 8.723 0.02 1 114 66 41 PHE N N 117.798 0.15 1 115 67 42 PRO C C 176.151 0.2 1 116 68 43 MET H H 7.772 0.02 1 117 68 43 MET C C 179.764 0.2 1 118 68 43 MET N N 119.230 0.15 1 119 69 44 MET H H 10.509 0.02 1 120 69 44 MET N N 120.317 0.15 1 121 70 45 SER C C 176.066 0.2 1 122 71 46 THR H H 7.899 0.02 1 123 71 46 THR C C 175.166 0.2 1 124 71 46 THR N N 111.841 0.15 1 125 72 47 PHE H H 7.689 0.02 1 126 72 47 PHE C C 176.594 0.2 1 127 72 47 PHE N N 116.763 0.15 1 128 73 48 LYS H H 7.423 0.02 1 129 73 48 LYS C C 177.403 0.2 1 130 73 48 LYS N N 122.329 0.15 1 131 74 49 VAL H H 6.607 0.02 1 132 74 49 VAL C C 175.937 0.2 1 133 74 49 VAL N N 115.594 0.15 1 134 75 50 LEU H H 6.666 0.02 1 135 75 50 LEU C C 178.068 0.2 1 136 75 50 LEU N N 117.752 0.15 1 137 76 51 LEU H H 7.964 0.02 1 138 76 51 LEU C C 177.228 0.2 1 139 76 51 LEU N N 116.706 0.15 1 140 77 52 CYS H H 7.506 0.02 1 141 77 52 CYS C C 175.618 0.2 1 142 77 52 CYS N N 113.790 0.15 1 143 78 53 GLY H H 8.355 0.02 1 144 78 53 GLY C C 173.095 0.2 1 145 78 53 GLY N N 110.985 0.15 1 146 79 54 ALA H H 7.794 0.02 1 147 79 54 ALA C C 180.992 0.2 1 148 79 54 ALA N N 124.658 0.15 1 149 80 55 VAL H H 8.020 0.02 1 150 80 55 VAL C C 177.986 0.2 1 151 80 55 VAL N N 119.426 0.15 1 152 81 56 LEU H H 8.491 0.02 1 153 81 56 LEU C C 178.206 0.2 1 154 81 56 LEU N N 119.412 0.15 1 155 82 57 SER H H 8.162 0.02 1 156 82 57 SER C C 177.944 0.2 1 157 82 57 SER N N 115.801 0.15 1 158 83 58 ARG H H 7.487 0.02 1 159 83 58 ARG C C 179.408 0.2 1 160 83 58 ARG N N 121.954 0.15 1 161 84 59 VAL H H 8.290 0.02 1 162 84 59 VAL C C 180.808 0.2 1 163 84 59 VAL N N 124.421 0.15 1 164 85 60 ASP H H 9.084 0.02 1 165 85 60 ASP C C 177.734 0.2 1 166 85 60 ASP N N 123.441 0.15 1 167 86 61 ALA H H 7.500 0.02 1 168 86 61 ALA C C 177.869 0.2 1 169 86 61 ALA N N 118.582 0.15 1 170 87 62 GLY H H 8.200 0.02 1 171 87 62 GLY C C 174.910 0.2 1 172 87 62 GLY N N 107.648 0.15 1 173 88 63 GLN H H 8.387 0.02 1 174 88 63 GLN C C 173.529 0.2 1 175 88 63 GLN N N 117.296 0.15 1 176 89 64 GLU H H 7.351 0.02 1 177 89 64 GLU C C 172.709 0.2 1 178 89 64 GLU N N 118.013 0.15 1 179 90 65 GLN H H 10.077 0.02 1 180 90 65 GLN C C 176.036 0.2 1 181 90 65 GLN N N 125.216 0.15 1 182 91 66 LEU H H 9.054 0.02 1 183 91 66 LEU C C 177.360 0.2 1 184 91 66 LEU N N 122.979 0.15 1 185 92 67 GLY H H 8.384 0.02 1 186 92 67 GLY C C 173.842 0.2 1 187 92 67 GLY N N 102.070 0.15 1 188 93 68 ARG H H 7.336 0.02 1 189 93 68 ARG C C 174.701 0.2 1 190 93 68 ARG N N 122.490 0.15 1 191 94 69 ARG H H 8.539 0.02 1 192 94 69 ARG C C 174.509 0.2 1 193 94 69 ARG N N 127.324 0.15 1 194 95 70 ILE H H 9.091 0.02 1 195 95 70 ILE C C 174.537 0.2 1 196 95 70 ILE N N 130.336 0.15 1 197 96 71 HIS H H 8.461 0.02 1 198 96 71 HIS C C 174.122 0.2 1 199 96 71 HIS N N 124.845 0.15 1 200 97 72 TYR H H 8.503 0.02 1 201 97 72 TYR C C 173.002 0.2 1 202 97 72 TYR N N 121.001 0.15 1 203 98 73 SER H H 9.437 0.02 1 204 98 73 SER C C 175.695 0.2 1 205 98 73 SER N N 114.603 0.15 1 206 99 74 GLN H H 9.080 0.02 1 207 99 74 GLN C C 177.971 0.2 1 208 99 74 GLN N N 121.886 0.15 1 209 100 75 ASN H H 8.208 0.02 1 210 100 75 ASN C C 175.610 0.2 1 211 100 75 ASN N N 115.213 0.15 1 212 101 76 ASP H H 7.882 0.02 1 213 101 76 ASP C C 175.764 0.2 1 214 101 76 ASP N N 116.431 0.15 1 215 102 77 LEU H H 7.182 0.02 1 216 102 77 LEU C C 177.491 0.2 1 217 102 77 LEU N N 117.698 0.15 1 218 103 78 VAL H H 7.785 0.02 1 219 103 78 VAL C C 176.965 0.2 1 220 103 78 VAL N N 117.366 0.15 1 221 104 79 GLU H H 8.721 0.02 1 222 104 79 GLU C C 175.584 0.2 1 223 104 79 GLU N N 123.330 0.15 1 224 105 80 GLY H H 8.477 0.02 1 225 105 80 GLY C C 176.165 0.2 1 226 105 80 GLY N N 117.525 0.15 1 227 106 81 SER H H 8.754 0.02 1 228 106 81 SER N N 110.956 0.15 1 229 107 82 PRO C C 177.837 0.2 1 230 108 83 VAL H H 8.755 0.02 1 231 108 83 VAL C C 179.226 0.2 1 232 108 83 VAL N N 118.978 0.15 1 233 109 84 THR H H 9.854 0.02 1 234 109 84 THR C C 182.037 0.2 1 235 109 84 THR N N 114.158 0.15 1 236 110 85 GLU H H 7.891 0.02 1 237 110 85 GLU C C 176.492 0.2 1 238 110 85 GLU N N 119.675 0.15 1 239 111 86 LYS H H 7.470 0.02 1 240 111 86 LYS C C 177.298 0.2 1 241 111 86 LYS N N 116.019 0.15 1 242 112 87 HIS H H 7.141 0.02 1 243 112 87 HIS C C 174.437 0.2 1 244 112 87 HIS N N 116.283 0.15 1 245 113 88 LEU H H 7.863 0.02 1 246 113 88 LEU C C 179.173 0.2 1 247 113 88 LEU N N 120.223 0.15 1 248 114 89 THR H H 8.299 0.02 1 249 114 89 THR C C 175.590 0.2 1 250 114 89 THR N N 109.291 0.15 1 251 115 90 ASP H H 8.780 0.02 1 252 115 90 ASP C C 177.717 0.2 1 253 115 90 ASP N N 117.127 0.15 1 254 116 91 GLY H H 7.913 0.02 1 255 116 91 GLY C C 171.623 0.2 1 256 116 91 GLY N N 110.739 0.15 1 257 117 92 MET H H 8.286 0.02 1 258 117 92 MET C C 175.126 0.2 1 259 117 92 MET N N 113.458 0.15 1 260 118 93 THR H H 8.918 0.02 1 261 118 93 THR C C 175.825 0.2 1 262 118 93 THR N N 112.220 0.15 1 263 119 94 VAL H H 8.134 0.02 1 264 119 94 VAL C C 177.956 0.2 1 265 119 94 VAL N N 122.032 0.15 1 266 120 95 ARG H H 9.074 0.02 1 267 120 95 ARG C C 177.525 0.2 1 268 120 95 ARG N N 118.297 0.15 1 269 121 96 GLU H H 7.612 0.02 1 270 121 96 GLU C C 180.470 0.2 1 271 121 96 GLU N N 118.444 0.15 1 272 122 97 LEU H H 9.121 0.02 1 273 122 97 LEU C C 179.055 0.2 1 274 122 97 LEU N N 122.858 0.15 1 275 123 98 CYS H H 8.149 0.02 1 276 123 98 CYS C C 176.002 0.2 1 277 123 98 CYS N N 118.969 0.15 1 278 124 99 SER H H 7.712 0.02 1 279 124 99 SER C C 178.981 0.2 1 280 124 99 SER N N 113.185 0.15 1 281 125 100 ALA H H 8.517 0.02 1 282 125 100 ALA C C 180.179 0.2 1 283 125 100 ALA N N 124.786 0.15 1 284 126 101 ALA H H 8.676 0.02 1 285 126 101 ALA C C 178.404 0.2 1 286 126 101 ALA N N 121.011 0.15 1 287 127 102 ILE H H 8.167 0.02 1 288 127 102 ILE C C 176.593 0.2 1 289 127 102 ILE N N 113.448 0.15 1 290 128 103 THR H H 8.943 0.02 1 291 128 103 THR C C 175.915 0.2 1 292 128 103 THR N N 109.317 0.15 1 293 129 104 MET H H 6.799 0.02 1 294 129 104 MET C C 175.807 0.2 1 295 129 104 MET N N 114.627 0.15 1 296 130 105 SER H H 7.068 0.02 1 297 130 105 SER C C 173.549 0.2 1 298 130 105 SER N N 114.087 0.15 1 299 131 106 ASP H H 7.368 0.02 1 300 131 106 ASP C C 176.602 0.2 1 301 131 106 ASP N N 120.154 0.15 1 302 132 107 ASN H H 8.608 0.02 1 303 132 107 ASN C C 177.724 0.2 1 304 132 107 ASN N N 127.849 0.15 1 305 133 108 THR H H 8.047 0.02 1 306 133 108 THR C C 176.369 0.2 1 307 133 108 THR N N 120.335 0.15 1 308 134 109 ALA H H 9.055 0.02 1 309 134 109 ALA C C 178.530 0.2 1 310 134 109 ALA N N 122.967 0.15 1 311 135 110 ALA H H 7.221 0.02 1 312 135 110 ALA C C 178.294 0.2 1 313 135 110 ALA N N 115.620 0.15 1 314 136 111 ASN H H 7.979 0.02 1 315 136 111 ASN C C 178.728 0.2 1 316 136 111 ASN N N 119.727 0.15 1 317 137 112 LEU H H 9.070 0.02 1 318 137 112 LEU C C 181.132 0.2 1 319 137 112 LEU N N 121.569 0.15 1 320 138 113 LEU H H 8.191 0.02 1 321 138 113 LEU C C 180.760 0.2 1 322 138 113 LEU N N 119.462 0.15 1 323 139 114 LEU H H 9.227 0.02 1 324 139 114 LEU C C 180.119 0.2 1 325 139 114 LEU N N 124.160 0.15 1 326 140 115 THR H H 8.692 0.02 1 327 140 115 THR C C 177.729 0.2 1 328 140 115 THR N N 118.058 0.15 1 329 141 116 THR H H 7.612 0.02 1 330 141 116 THR C C 175.693 0.2 1 331 141 116 THR N N 112.665 0.15 1 332 142 117 ILE H H 6.890 0.02 1 333 142 117 ILE C C 175.405 0.2 1 334 142 117 ILE N N 110.906 0.15 1 335 143 118 GLY H H 7.476 0.02 1 336 143 118 GLY C C 175.127 0.2 1 337 143 118 GLY N N 106.411 0.15 1 338 144 119 GLY H H 8.194 0.02 1 339 144 119 GLY N N 108.215 0.15 1 340 145 120 PRO C C 177.850 0.2 1 341 146 121 LYS H H 8.656 0.02 1 342 146 121 LYS C C 179.771 0.2 1 343 146 121 LYS N N 116.116 0.15 1 344 147 122 GLU H H 7.331 0.02 1 345 147 122 GLU C C 180.335 0.2 1 346 147 122 GLU N N 118.600 0.15 1 347 148 123 LEU H H 7.647 0.02 1 348 148 123 LEU C C 178.091 0.2 1 349 148 123 LEU N N 123.272 0.15 1 350 149 124 THR H H 8.168 0.02 1 351 149 124 THR C C 175.081 0.2 1 352 149 124 THR N N 117.043 0.15 1 353 150 125 ALA H H 7.887 0.02 1 354 150 125 ALA C C 179.437 0.2 1 355 150 125 ALA N N 123.221 0.15 1 356 151 126 PHE H H 7.795 0.02 1 357 151 126 PHE C C 177.729 0.2 1 358 151 126 PHE N N 120.500 0.15 1 359 152 127 LEU H H 8.048 0.02 1 360 152 127 LEU C C 179.082 0.2 1 361 152 127 LEU N N 121.537 0.15 1 362 153 128 HIS H H 8.893 0.02 1 363 153 128 HIS C C 179.780 0.2 1 364 153 128 HIS N N 120.788 0.15 1 365 154 129 ASN H H 8.384 0.02 1 366 154 129 ASN C C 176.479 0.2 1 367 154 129 ASN N N 118.301 0.15 1 368 155 130 MET H H 7.492 0.02 1 369 155 130 MET C C 175.813 0.2 1 370 155 130 MET N N 115.562 0.15 1 371 156 131 GLY H H 7.729 0.02 1 372 156 131 GLY C C 172.666 0.2 1 373 156 131 GLY N N 107.731 0.15 1 374 157 132 ASP H H 7.992 0.02 1 375 157 132 ASP C C 174.695 0.2 1 376 157 132 ASP N N 121.676 0.15 1 377 158 133 HIS H H 8.320 0.02 1 378 158 133 HIS C C 175.007 0.2 1 379 158 133 HIS N N 121.261 0.15 1 380 159 134 VAL H H 8.803 0.02 1 381 159 134 VAL C C 176.017 0.2 1 382 159 134 VAL N N 121.342 0.15 1 383 160 135 THR H H 9.371 0.02 1 384 160 135 THR C C 172.762 0.2 1 385 160 135 THR N N 125.666 0.15 1 386 161 136 ARG H H 8.453 0.02 1 387 161 136 ARG C C 171.611 0.2 1 388 161 136 ARG N N 119.806 0.15 1 389 162 137 LEU H H 7.714 0.02 1 390 162 137 LEU C C 174.257 0.2 1 391 162 137 LEU N N 121.179 0.15 1 392 163 138 ASP H H 9.987 0.02 1 393 163 138 ASP C C 175.614 0.2 1 394 163 138 ASP N N 126.796 0.15 1 395 164 139 ARG H H 9.227 0.02 1 396 164 139 ARG C C 170.521 0.2 1 397 164 139 ARG N N 125.142 0.15 1 398 165 140 TRP H H 7.662 0.02 1 399 165 140 TRP C C 177.851 0.2 1 400 165 140 TRP N N 114.432 0.15 1 401 166 141 GLU H H 9.546 0.02 1 402 166 141 GLU N N 117.448 0.15 1 403 167 142 PRO C C 177.737 0.2 1 404 168 143 GLU H H 8.659 0.02 1 405 168 143 GLU C C 176.617 0.2 1 406 168 143 GLU N N 128.187 0.15 1 407 169 144 LEU H H 7.666 0.02 1 408 169 144 LEU C C 176.834 0.2 1 409 169 144 LEU N N 113.088 0.15 1 410 170 145 ASN H H 7.543 0.02 1 411 170 145 ASN C C 174.781 0.2 1 412 170 145 ASN N N 119.778 0.15 1 413 171 146 GLU H H 7.476 0.02 1 414 171 146 GLU C C 175.697 0.2 1 415 171 146 GLU N N 120.698 0.15 1 416 172 147 ALA H H 9.489 0.02 1 417 172 147 ALA C C 176.475 0.2 1 418 172 147 ALA N N 118.373 0.15 1 419 173 148 ILE H H 8.654 0.02 1 420 173 148 ILE N N 120.809 0.15 1 421 174 149 PRO C C 177.492 0.2 1 422 175 150 ASN H H 8.887 0.02 1 423 175 150 ASN C C 173.221 0.2 1 424 175 150 ASN N N 115.859 0.15 1 425 176 151 ASP H H 7.591 0.02 1 426 176 151 ASP C C 177.284 0.2 1 427 176 151 ASP N N 120.809 0.15 1 428 177 152 GLU H H 8.968 0.02 1 429 177 152 GLU C C 177.604 0.2 1 430 177 152 GLU N N 126.395 0.15 1 431 178 153 ARG H H 8.094 0.02 1 432 178 153 ARG C C 177.153 0.2 1 433 178 153 ARG N N 122.317 0.15 1 434 179 154 ASP H H 8.776 0.02 1 435 179 154 ASP C C 177.902 0.2 1 436 179 154 ASP N N 115.625 0.15 1 437 180 155 THR H H 7.268 0.02 1 438 180 155 THR C C 173.092 0.2 1 439 180 155 THR N N 104.774 0.15 1 440 181 156 THR H H 8.208 0.02 1 441 181 156 THR C C 173.551 0.2 1 442 181 156 THR N N 111.766 0.15 1 443 182 157 MET H H 8.503 0.02 1 444 182 157 MET N N 117.882 0.15 1 445 183 158 PRO C C 176.837 0.2 1 446 184 159 ALA H H 8.667 0.02 1 447 184 159 ALA C C 179.061 0.2 1 448 184 159 ALA N N 114.751 0.15 1 449 185 160 ALA H H 6.857 0.02 1 450 185 160 ALA C C 177.960 0.2 1 451 185 160 ALA N N 121.085 0.15 1 452 186 161 MET H H 8.319 0.02 1 453 186 161 MET C C 177.849 0.2 1 454 186 161 MET N N 116.121 0.15 1 455 187 162 ALA H H 8.270 0.02 1 456 187 162 ALA C C 178.410 0.2 1 457 187 162 ALA N N 117.826 0.15 1 458 188 163 THR H H 7.695 0.02 1 459 188 163 THR C C 177.383 0.2 1 460 188 163 THR N N 112.282 0.15 1 461 189 164 THR H H 9.053 0.02 1 462 189 164 THR C C 175.727 0.2 1 463 189 164 THR N N 124.628 0.15 1 464 190 165 LEU H H 8.838 0.02 1 465 190 165 LEU C C 178.193 0.2 1 466 190 165 LEU N N 121.382 0.15 1 467 191 166 ARG H H 8.115 0.02 1 468 191 166 ARG C C 178.725 0.2 1 469 191 166 ARG N N 118.265 0.15 1 470 192 167 LYS H H 8.089 0.02 1 471 192 167 LYS C C 178.630 0.2 1 472 192 167 LYS N N 120.999 0.15 1 473 193 168 LEU H H 8.049 0.02 1 474 193 168 LEU C C 177.464 0.2 1 475 193 168 LEU N N 117.502 0.15 1 476 194 169 LEU H H 8.039 0.02 1 477 194 169 LEU C C 178.292 0.2 1 478 194 169 LEU N N 111.466 0.15 1 479 195 170 THR H H 7.959 0.02 1 480 195 170 THR C C 174.667 0.2 1 481 195 170 THR N N 105.265 0.15 1 482 196 171 GLY H H 7.882 0.02 1 483 196 171 GLY C C 173.999 0.2 1 484 196 171 GLY N N 110.539 0.15 1 485 197 172 GLU H H 8.381 0.02 1 486 197 172 GLU C C 176.378 0.2 1 487 197 172 GLU N N 116.703 0.15 1 488 198 173 LEU H H 7.464 0.02 1 489 198 173 LEU C C 177.381 0.2 1 490 198 173 LEU N N 122.639 0.15 1 491 199 174 LEU H H 8.657 0.02 1 492 199 174 LEU C C 177.600 0.2 1 493 199 174 LEU N N 118.189 0.15 1 494 200 175 THR H H 8.951 0.02 1 495 200 175 THR C C 175.362 0.2 1 496 200 175 THR N N 112.528 0.15 1 497 201 176 LEU H H 8.692 0.02 1 498 201 176 LEU C C 179.079 0.2 1 499 201 176 LEU N N 123.015 0.15 1 500 202 177 ALA H H 8.436 0.02 1 501 202 177 ALA C C 181.467 0.2 1 502 202 177 ALA N N 118.700 0.15 1 503 203 178 SER H H 7.748 0.02 1 504 203 178 SER C C 175.102 0.2 1 505 203 178 SER N N 118.512 0.15 1 506 204 179 ARG H H 9.059 0.02 1 507 204 179 ARG C C 178.515 0.2 1 508 204 179 ARG N N 123.646 0.15 1 509 205 180 GLN H H 8.218 0.02 1 510 205 180 GLN C C 177.139 0.2 1 511 205 180 GLN N N 117.522 0.15 1 512 206 181 GLN H H 7.605 0.02 1 513 206 181 GLN C C 177.848 0.2 1 514 206 181 GLN N N 118.120 0.15 1 515 207 182 LEU H H 7.978 0.02 1 516 207 182 LEU C C 178.280 0.2 1 517 207 182 LEU N N 121.121 0.15 1 518 208 183 ILE H H 7.803 0.02 1 519 208 183 ILE C C 177.266 0.2 1 520 208 183 ILE N N 118.170 0.15 1 521 209 184 ASP H H 8.687 0.02 1 522 209 184 ASP C C 181.381 0.2 1 523 209 184 ASP N N 122.358 0.15 1 524 210 185 TRP H H 8.028 0.02 1 525 210 185 TRP C C 177.059 0.2 1 526 210 185 TRP N N 120.436 0.15 1 527 211 186 MET H H 7.722 0.02 1 528 211 186 MET C C 180.277 0.2 1 529 211 186 MET N N 115.951 0.15 1 530 212 187 GLU H H 9.645 0.02 1 531 212 187 GLU C C 178.118 0.2 1 532 212 187 GLU N N 124.795 0.15 1 533 213 188 ALA H H 7.331 0.02 1 534 213 188 ALA C C 175.474 0.2 1 535 213 188 ALA N N 119.609 0.15 1 536 214 189 ASP H H 6.968 0.02 1 537 214 189 ASP C C 177.376 0.2 1 538 214 189 ASP N N 115.769 0.15 1 539 215 190 LYS H H 9.438 0.02 1 540 215 190 LYS C C 179.619 0.2 1 541 215 190 LYS N N 127.280 0.15 1 542 216 191 VAL H H 7.183 0.02 1 543 216 191 VAL C C 175.075 0.2 1 544 216 191 VAL N N 109.992 0.15 1 545 217 192 ALA H H 8.941 0.02 1 546 217 192 ALA C C 178.295 0.2 1 547 217 192 ALA N N 125.662 0.15 1 548 218 193 GLY H H 8.930 0.02 1 549 218 193 GLY N N 114.383 0.15 1 550 219 194 PRO C C 175.117 0.2 1 551 220 195 LEU H H 6.790 0.02 1 552 220 195 LEU C C 176.343 0.2 1 553 220 195 LEU N N 114.038 0.15 1 554 221 196 LEU H H 6.895 0.02 1 555 221 196 LEU C C 178.518 0.2 1 556 221 196 LEU N N 123.455 0.15 1 557 222 197 ARG H H 8.933 0.02 1 558 222 197 ARG C C 177.410 0.2 1 559 222 197 ARG N N 115.968 0.15 1 560 223 198 SER H H 7.002 0.02 1 561 223 198 SER C C 174.001 0.2 1 562 223 198 SER N N 113.352 0.15 1 563 224 199 ALA H H 7.265 0.02 1 564 224 199 ALA C C 176.258 0.2 1 565 224 199 ALA N N 122.844 0.15 1 566 225 200 LEU H H 6.699 0.02 1 567 225 200 LEU N N 120.923 0.15 1 568 226 201 PRO C C 175.797 0.2 1 569 227 202 ALA H H 8.227 0.02 1 570 227 202 ALA C C 179.403 0.2 1 571 227 202 ALA N N 122.731 0.15 1 572 228 203 GLY H H 8.810 0.02 1 573 228 203 GLY C C 175.343 0.2 1 574 228 203 GLY N N 110.142 0.15 1 575 229 204 TRP H H 7.616 0.02 1 576 229 204 TRP C C 175.356 0.2 1 577 229 204 TRP N N 120.585 0.15 1 578 230 205 PHE H H 9.366 0.02 1 579 230 205 PHE C C 174.785 0.2 1 580 230 205 PHE N N 122.964 0.15 1 581 231 206 ILE H H 7.508 0.02 1 582 231 206 ILE C C 169.472 0.2 1 583 231 206 ILE N N 123.370 0.15 1 584 232 207 ALA H H 8.442 0.02 1 585 232 207 ALA C C 174.906 0.2 1 586 232 207 ALA N N 128.072 0.15 1 587 233 208 ASP H H 8.232 0.02 1 588 233 208 ASP C C 172.640 0.2 1 589 233 208 ASP N N 123.966 0.15 1 590 234 209 LYS H H 8.030 0.02 1 591 234 209 LYS C C 178.300 0.2 1 592 234 209 LYS N N 109.562 0.15 1 593 235 210 SER H H 8.230 0.02 1 594 235 210 SER C C 173.981 0.2 1 595 235 210 SER N N 115.665 0.15 1 596 236 211 GLY H H 8.616 0.02 1 597 236 211 GLY N N 102.594 0.15 1 598 237 212 ALA C C 175.482 0.2 1 599 238 213 GLY H H 7.783 0.02 1 600 238 213 GLY C C 172.736 0.2 1 601 238 213 GLY N N 108.084 0.15 1 602 239 214 GLU H H 7.868 0.02 1 603 239 214 GLU C C 176.044 0.2 1 604 239 214 GLU N N 117.159 0.15 1 605 240 215 ARG H H 9.465 0.02 1 606 240 215 ARG C C 176.025 0.2 1 607 240 215 ARG N N 118.143 0.15 1 608 241 216 GLY H H 8.785 0.02 1 609 241 216 GLY C C 177.304 0.2 1 610 241 216 GLY N N 102.832 0.15 1 611 242 217 SER H H 7.560 0.02 1 612 242 217 SER C C 174.982 0.2 1 613 242 217 SER N N 119.418 0.15 1 614 243 218 ARG H H 9.051 0.02 1 615 243 218 ARG C C 174.223 0.2 1 616 243 218 ARG N N 126.287 0.15 1 617 244 219 GLY H H 8.470 0.02 1 618 244 219 GLY C C 170.348 0.2 1 619 244 219 GLY N N 111.496 0.15 1 620 245 220 ILE H H 9.185 0.02 1 621 245 220 ILE C C 170.418 0.2 1 622 245 220 ILE N N 117.000 0.15 1 623 246 221 ILE H H 8.113 0.02 1 624 246 221 ILE C C 174.731 0.2 1 625 246 221 ILE N N 118.142 0.15 1 626 247 222 ALA H H 8.991 0.02 1 627 247 222 ALA C C 174.578 0.2 1 628 247 222 ALA N N 122.845 0.15 1 629 248 223 ALA H H 9.334 0.02 1 630 248 223 ALA C C 175.581 0.2 1 631 248 223 ALA N N 122.880 0.15 1 632 249 224 LEU H H 9.317 0.02 1 633 249 224 LEU C C 176.692 0.2 1 634 249 224 LEU N N 121.209 0.15 1 635 250 225 GLY H H 8.808 0.02 1 636 250 225 GLY N N 110.506 0.15 1 637 251 226 PRO C C 176.017 0.2 1 638 252 227 ASP H H 7.928 0.02 1 639 252 227 ASP C C 177.134 0.2 1 640 252 227 ASP N N 114.304 0.15 1 641 253 228 GLY H H 7.708 0.02 1 642 253 228 GLY C C 173.397 0.2 1 643 253 228 GLY N N 100.202 0.15 1 644 254 229 LYS H H 7.175 0.02 1 645 254 229 LYS N N 119.360 0.15 1 646 255 230 PRO C C 176.054 0.2 1 647 256 231 SER H H 8.534 0.02 1 648 256 231 SER C C 174.525 0.2 1 649 256 231 SER N N 112.522 0.15 1 650 257 232 ARG H H 8.833 0.02 1 651 257 232 ARG C C 174.483 0.2 1 652 257 232 ARG N N 123.110 0.15 1 653 258 233 ILE H H 9.240 0.02 1 654 258 233 ILE C C 174.560 0.2 1 655 258 233 ILE N N 122.703 0.15 1 656 259 234 VAL H H 9.200 0.02 1 657 259 234 VAL C C 173.552 0.2 1 658 259 234 VAL N N 126.298 0.15 1 659 260 235 VAL H H 8.230 0.02 1 660 260 235 VAL C C 173.778 0.2 1 661 260 235 VAL N N 125.400 0.15 1 662 261 236 ILE H H 8.343 0.02 1 663 261 236 ILE C C 174.333 0.2 1 664 261 236 ILE N N 123.124 0.15 1 665 262 237 TYR H H 8.734 0.02 1 666 262 237 TYR C C 173.974 0.2 1 667 262 237 TYR N N 122.345 0.15 1 668 263 238 THR H H 8.934 0.02 1 669 263 238 THR C C 172.490 0.2 1 670 263 238 THR N N 111.381 0.15 1 671 264 239 THR H H 8.022 0.02 1 672 264 239 THR C C 171.632 0.2 1 673 264 239 THR N N 121.857 0.15 1 674 265 240 GLY H H 8.672 0.02 1 675 265 240 GLY C C 174.897 0.2 1 676 265 240 GLY N N 114.062 0.15 1 677 266 241 SER H H 8.362 0.02 1 678 266 241 SER C C 176.014 0.2 1 679 266 241 SER N N 114.544 0.15 1 680 267 242 GLN H H 8.846 0.02 1 681 267 242 GLN C C 175.934 0.2 1 682 267 242 GLN N N 123.601 0.15 1 683 268 243 ALA H H 8.712 0.02 1 684 268 243 ALA C C 178.726 0.2 1 685 268 243 ALA N N 123.354 0.15 1 686 269 244 THR H H 8.648 0.02 1 687 269 244 THR C C 175.960 0.2 1 688 269 244 THR N N 112.781 0.15 1 689 270 245 MET H H 9.138 0.02 1 690 270 245 MET C C 177.830 0.2 1 691 270 245 MET N N 122.378 0.15 1 692 271 246 ASP H H 8.438 0.02 1 693 271 246 ASP C C 178.663 0.2 1 694 271 246 ASP N N 116.640 0.15 1 695 272 247 GLU H H 7.639 0.02 1 696 272 247 GLU C C 179.310 0.2 1 697 272 247 GLU N N 120.291 0.15 1 698 273 248 ARG H H 8.112 0.02 1 699 273 248 ARG C C 177.506 0.2 1 700 273 248 ARG N N 118.733 0.15 1 701 274 249 ASN H H 8.769 0.02 1 702 274 249 ASN C C 176.514 0.2 1 703 274 249 ASN N N 116.881 0.15 1 704 275 250 ARG H H 8.027 0.02 1 705 275 250 ARG C C 178.845 0.2 1 706 275 250 ARG N N 118.746 0.15 1 707 276 251 GLN H H 7.813 0.02 1 708 276 251 GLN C C 178.503 0.2 1 709 276 251 GLN N N 114.903 0.15 1 710 277 252 ILE H H 7.413 0.02 1 711 277 252 ILE C C 177.172 0.2 1 712 277 252 ILE N N 117.547 0.15 1 713 278 253 ALA H H 8.707 0.02 1 714 278 253 ALA C C 180.437 0.2 1 715 278 253 ALA N N 123.339 0.15 1 716 279 254 GLU H H 8.432 0.02 1 717 279 254 GLU C C 180.700 0.2 1 718 279 254 GLU N N 118.242 0.15 1 719 280 255 ILE H H 8.027 0.02 1 720 280 255 ILE C C 177.963 0.2 1 721 280 255 ILE N N 123.433 0.15 1 722 281 256 GLY H H 8.353 0.02 1 723 281 256 GLY C C 173.962 0.2 1 724 281 256 GLY N N 106.007 0.15 1 725 282 257 ALA H H 8.631 0.02 1 726 282 257 ALA C C 180.136 0.2 1 727 282 257 ALA N N 122.316 0.15 1 728 283 258 SER H H 7.498 0.02 1 729 283 258 SER C C 176.263 0.2 1 730 283 258 SER N N 113.365 0.15 1 731 284 259 LEU H H 8.204 0.02 1 732 284 259 LEU C C 178.859 0.2 1 733 284 259 LEU N N 122.892 0.15 1 734 285 260 ILE H H 7.965 0.02 1 735 285 260 ILE C C 178.503 0.2 1 736 285 260 ILE N N 118.218 0.15 1 737 286 261 LYS H H 8.111 0.02 1 738 286 261 LYS C C 177.951 0.2 1 739 286 261 LYS N N 121.097 0.15 1 740 287 262 HIS H H 7.609 0.02 1 741 287 262 HIS C C 173.654 0.2 1 742 287 262 HIS N N 114.241 0.15 1 743 288 263 TRP H H 7.249 0.02 1 744 288 263 TRP N N 128.741 0.15 1 stop_ save_