data_7236 ####################### # 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 7236 _BMRB_flat_file_name bmr7236.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" 247 "13C chemical shifts" 668 "15N chemical shifts" 247 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 Y105W of TEM-1 beta-lactamase' _Enzyme_commission_number 3.5.2.6 loop_ _Mol_system_component_name _Mol_label 'TEM-1 Y105W' $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 AGQEQLGRRIHYSQNDLVEW 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 TRP 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 99.62 0.00e+00 BMRB 6024 "TEM-1 beta-lactamase" 100.00 263 99.24 99.62 0.00e+00 BMRB 6357 TEM-1 100.00 263 99.62 100.00 0.00e+00 BMRB 7237 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 99.62 0.00e+00 PDB 1BT5 "Crystal Structure Of The Imipenem Inhibited Tem-1 Beta-Lactamase From Escherichia Coli" 100.00 263 98.86 99.62 0.00e+00 PDB 1BTL "Crystal Structure Of Escherichia Coli Tem1 Beta-Lactamase At 1.8 Angstroms Resolution" 100.00 263 98.86 99.62 0.00e+00 PDB 1CK3 "N276d Mutant Of Escherichia Coli Tem-1 Beta-Lactamase" 100.00 263 98.48 99.62 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 99.62 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 99.62 100.00 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 99.62 100.00 0.00e+00 PDB 1ESU "S235a Mutant Of Tem1 Beta-Lactamase" 100.00 263 99.24 100.00 0.00e+00 PDB 1FQG "Molecular Structure Of The Acyl-Enzyme Intermediate In Tem- 1 Beta-Lactamase" 100.00 263 99.24 99.62 0.00e+00 PDB 1HTZ "Crystal Structure Of Tem52 Beta-Lactamase" 100.00 263 98.48 99.24 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 99.62 0.00e+00 PDB 1JTG "Crystal Structure Of Tem-1 Beta-lactamase / Beta-lactamase Inhibitor Protein Complex" 100.00 263 98.86 99.62 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 99.62 0.00e+00 PDB 1JWP "Structure Of M182t Mutant Of Tem-1 Beta-Lactamase" 100.00 263 99.24 99.62 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 99.62 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 99.24 0.00e+00 PDB 1LHY "Crystal Structure Of Tem-30 Beta-lactamase At 2.0 Angstrom" 100.00 263 99.24 99.62 0.00e+00 PDB 1LI0 "Crystal Structure Of Tem-32 Beta-Lactamase At 1.6 Angstrom" 100.00 263 98.86 99.62 0.00e+00 PDB 1LI9 "Crystal Structure Of Tem-34 Beta-lactamase At 1.5 Angstrom" 100.00 263 99.24 100.00 0.00e+00 PDB 1M40 "Ultra High Resolution Crystal Structure Of Tem-1" 100.00 263 99.24 99.62 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 99.62 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 99.62 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 99.62 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 99.62 0.00e+00 PDB 1PZO "Tem-1 Beta-lactamase In Complex With A Novel, Core- Disrupting, Allosteric Inhibitor" 100.00 263 99.24 99.62 0.00e+00 PDB 1PZP "Tem-1 Beta-Lactamase In Complex With A Novel, Core- Disrupting, Allosteric Inhibitor" 100.00 263 99.24 99.62 0.00e+00 PDB 1S0W "1b Lactamse B LACTAMASE INHIBITOR" 100.00 263 99.62 100.00 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 99.62 0.00e+00 PDB 1XPB "Structure Of Beta-Lactamase Tem1" 100.00 263 99.62 100.00 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 99.62 0.00e+00 PDB 1ZG4 "Tem1 Beta Lactamase" 100.00 286 98.86 99.62 0.00e+00 PDB 1ZG6 "Tem1 Beta Lactamase Mutant S70g" 100.00 286 98.48 99.24 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 99.62 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 99.62 0.00e+00 PDB 3CMZ "Tem-1 Class-A Beta-Lactamase L201p Mutant Apo Structure" 100.00 263 99.24 99.62 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 99.62 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 99.62 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 99.24 0.00e+00 PDB 4GKU "Crystal Structure Of Beta Lactamase In Pet-15b" 100.00 263 99.62 100.00 0.00e+00 PDB 4IBX "Crystal Structure Of Stabilized Tem-1 Beta-lactamase Variant V.13" 100.00 263 96.96 97.34 0.00e+00 PDB 4MEZ "Crystal Structure Of M68l/m69t Double Mutant Tem-1" 100.00 263 98.86 99.62 0.00e+00 DBJ BAA00795 "ampicillin resistance protein [Shuttle vector pHY320PLK]" 100.00 286 99.62 100.00 0.00e+00 DBJ BAA03488 "beta-lactamase [Cloning vector pKF2]" 100.00 286 98.86 99.62 0.00e+00 DBJ BAA12825 "beta-lactamase [Cloning vector pBEN66]" 100.00 286 98.86 99.62 0.00e+00 DBJ BAA14388 "Ap resistance protein [synthetic construct]" 100.00 286 99.62 100.00 0.00e+00 DBJ BAA19239 "beta-lactamase [Cloning vector pBEN77]" 100.00 286 98.86 99.62 0.00e+00 EMBL CAA04868 "beta-lactamase [Escherichia coli]" 100.00 286 98.86 99.62 0.00e+00 EMBL CAA05682 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.62 0.00e+00 EMBL CAA05685 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.62 0.00e+00 EMBL CAA05686 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.62 0.00e+00 EMBL CAA05689 "beta-lactamase [synthetic construct]" 100.00 286 98.86 99.62 0.00e+00 GB AAA24057 "beta-lactamase [Escherichia coli]" 100.00 286 98.86 99.62 0.00e+00 GB AAA25053 "TEM-26B beta-lactamase [Klebsiella oxytoca]" 100.00 286 99.24 99.62 0.00e+00 GB AAA32208 "ampicillinase, partial [Enterobacteria phage f1]" 76.81 225 99.50 100.00 2.27e-143 GB AAA53119 "beta-lactamase [unidentified cloning vector]" 100.00 286 98.86 99.62 0.00e+00 GB AAA53121 "beta-lactamase [unidentified cloning vector]" 100.00 286 98.86 99.62 0.00e+00 PIR S60310 "extended spectrum beta-lactamase CAZ-2 - Klebsiella pneumoniae" 100.00 286 98.10 99.24 0.00e+00 PIR S60312 "extended spectrum beta-lactamase CAZ-7 - Klebsiella pneumoniae" 100.00 286 98.48 99.62 0.00e+00 PIR T51301 "beta-lactamase (EC 3.5.2.6) - fission yeast (Schizosaccharomyces pombe)" 100.00 286 98.86 99.62 0.00e+00 PRF 2018199A "beta lactamase IRT-4" 100.00 286 99.62 100.00 0.00e+00 REF NP_052173 "beta-lactamase [Neisseria gonorrhoeae]" 100.00 286 99.62 100.00 0.00e+00 REF NP_569411 "beta-lactamase [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 286 99.62 100.00 0.00e+00 REF NP_608310 "TEM beta-lactamase [Klebsiella pneumoniae]" 100.00 286 99.62 100.00 0.00e+00 REF NP_758767 "beta lactamase [Erwinia amylovora ATCC BAA-2158]" 98.48 283 97.68 98.07 0.00e+00 REF NP_775035 "BlaTEM1 [Citrobacter freundii]" 100.00 286 99.62 100.00 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 99.62 100.00 0.00e+00 SP P62594 "RecName: Full=Beta-lactamase TEM; AltName: Full=Penicillinase; Flags: Precursor [Salmonella enterica subsp. enterica serovar Ty" 100.00 286 99.62 100.00 0.00e+00 SP Q48406 "RecName: Full=Beta-lactamase TEM-12; Flags: Precursor [Klebsiella oxytoca]" 100.00 286 99.24 99.62 0.00e+00 TPE CAJ85677 "TPA: beta lactamase [Birmingham IncP-alpha plasmid]" 100.00 286 99.24 100.00 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 Y105W' _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 179.381 0.2 1 2 27 2 PRO CA C 65.608 0.2 1 3 27 2 PRO CB C 32.396 0.2 1 4 28 3 GLU H H 11.095 0.02 1 5 28 3 GLU C C 179.594 0.2 1 6 28 3 GLU CA C 59.644 0.2 1 7 28 3 GLU CB C 28.608 0.2 1 8 28 3 GLU N N 121.778 0.15 1 9 29 4 THR H H 7.814 0.02 1 10 29 4 THR C C 176.084 0.2 1 11 29 4 THR CA C 65.170 0.2 1 12 29 4 THR CB C 67.665 0.2 1 13 29 4 THR N N 118.936 0.15 1 14 30 5 LEU H H 7.068 0.02 1 15 30 5 LEU C C 179.015 0.2 1 16 30 5 LEU CA C 57.488 0.2 1 17 30 5 LEU CB C 40.807 0.2 1 18 30 5 LEU N N 120.229 0.15 1 19 31 6 VAL H H 7.535 0.02 1 20 31 6 VAL C C 178.454 0.2 1 21 31 6 VAL CA C 66.872 0.2 1 22 31 6 VAL CB C 31.426 0.2 1 23 31 6 VAL N N 119.756 0.15 1 24 32 7 LYS H H 7.315 0.02 1 25 32 7 LYS C C 178.398 0.2 1 26 32 7 LYS CA C 57.139 0.2 1 27 32 7 LYS CB C 30.413 0.2 1 28 32 7 LYS N N 119.503 0.15 1 29 33 8 VAL H H 8.338 0.02 1 30 33 8 VAL C C 176.813 0.2 1 31 33 8 VAL CA C 67.264 0.2 1 32 33 8 VAL CB C 31.013 0.2 1 33 33 8 VAL N N 123.033 0.15 1 34 34 9 LYS H H 7.726 0.02 1 35 34 9 LYS C C 179.359 0.2 1 36 34 9 LYS CA C 59.935 0.2 1 37 34 9 LYS CB C 31.935 0.2 1 38 34 9 LYS N N 118.586 0.15 1 39 35 10 ASP H H 8.353 0.02 1 40 35 10 ASP C C 178.148 0.2 1 41 35 10 ASP CA C 57.463 0.2 1 42 35 10 ASP CB C 42.013 0.2 1 43 35 10 ASP N N 120.569 0.15 1 44 36 11 ALA H H 8.549 0.02 1 45 36 11 ALA C C 179.599 0.2 1 46 36 11 ALA CA C 55.484 0.2 1 47 36 11 ALA CB C 18.393 0.2 1 48 36 11 ALA N N 122.292 0.15 1 49 37 12 GLU H H 7.974 0.02 1 50 37 12 GLU C C 180.485 0.2 1 51 37 12 GLU CA C 61.085 0.2 1 52 37 12 GLU CB C 29.175 0.2 1 53 37 12 GLU N N 117.685 0.15 1 54 38 13 ASP H H 7.938 0.02 1 55 38 13 ASP C C 179.151 0.2 1 56 38 13 ASP CA C 57.249 0.2 1 57 38 13 ASP CB C 41.010 0.2 1 58 38 13 ASP N N 119.968 0.15 1 59 39 14 GLN H H 8.888 0.02 1 60 39 14 GLN C C 179.180 0.2 1 61 39 14 GLN CA C 58.544 0.2 1 62 39 14 GLN CB C 28.594 0.2 1 63 39 14 GLN N N 118.490 0.15 1 64 40 15 LEU H H 8.760 0.02 1 65 40 15 LEU C C 178.972 0.2 1 66 40 15 LEU CA C 54.920 0.2 1 67 40 15 LEU CB C 42.659 0.2 1 68 40 15 LEU N N 114.392 0.15 1 69 41 16 GLY H H 8.119 0.02 1 70 41 16 GLY C C 174.016 0.2 1 71 41 16 GLY CA C 47.375 0.2 1 72 41 16 GLY N N 112.995 0.15 1 73 42 17 ALA H H 7.759 0.02 1 74 42 17 ALA C C 174.899 0.2 1 75 42 17 ALA CA C 50.774 0.2 1 76 42 17 ALA CB C 24.214 0.2 1 77 42 17 ALA N N 119.621 0.15 1 78 43 18 ARG H H 7.652 0.02 1 79 43 18 ARG C C 177.727 0.2 1 80 43 18 ARG CA C 55.768 0.2 1 81 43 18 ARG CB C 33.385 0.2 1 82 43 18 ARG N N 115.474 0.15 1 83 44 19 VAL H H 10.695 0.02 1 84 44 19 VAL C C 172.692 0.2 1 85 44 19 VAL CA C 61.381 0.2 1 86 44 19 VAL CB C 34.300 0.2 1 87 44 19 VAL N N 128.510 0.15 1 88 45 20 GLY H H 8.908 0.02 1 89 45 20 GLY C C 172.498 0.2 1 90 45 20 GLY CA C 44.020 0.2 1 91 45 20 GLY N N 111.371 0.15 1 92 46 21 TYR H H 9.437 0.02 1 93 46 21 TYR C C 174.052 0.2 1 94 46 21 TYR CA C 57.040 0.2 1 95 46 21 TYR CB C 45.253 0.2 1 96 46 21 TYR N N 124.075 0.15 1 97 47 22 ILE H H 8.063 0.02 1 98 47 22 ILE C C 171.492 0.2 1 99 47 22 ILE CA C 59.373 0.2 1 100 47 22 ILE CB C 41.717 0.2 1 101 47 22 ILE N N 125.490 0.15 1 102 48 23 GLU H H 7.840 0.02 1 103 48 23 GLU C C 175.036 0.2 1 104 48 23 GLU CA C 54.397 0.2 1 105 48 23 GLU CB C 34.770 0.2 1 106 48 23 GLU N N 123.566 0.15 1 107 49 24 LEU H H 9.719 0.02 1 108 49 24 LEU C C 175.649 0.2 1 109 49 24 LEU CA C 53.223 0.2 1 110 49 24 LEU CB C 47.249 0.2 1 111 49 24 LEU N N 126.866 0.15 1 112 50 25 ASP H H 9.075 0.02 1 113 50 25 ASP C C 176.799 0.2 1 114 50 25 ASP CA C 55.578 0.2 1 115 50 25 ASP CB C 43.132 0.2 1 116 50 25 ASP N N 126.600 0.15 1 117 51 26 LEU H H 8.263 0.02 1 118 51 26 LEU C C 177.586 0.2 1 119 51 26 LEU CA C 58.774 0.2 1 120 51 26 LEU CB C 43.125 0.2 1 121 51 26 LEU N N 128.916 0.15 1 122 52 27 ASN H H 8.710 0.02 1 123 52 27 ASN C C 176.986 0.2 1 124 52 27 ASN CA C 56.399 0.2 1 125 52 27 ASN CB C 38.764 0.2 1 126 52 27 ASN N N 116.621 0.15 1 127 53 28 SER H H 8.581 0.02 1 128 53 28 SER C C 176.516 0.2 1 129 53 28 SER CA C 59.049 0.2 1 130 53 28 SER CB C 65.777 0.2 1 131 53 28 SER N N 112.876 0.15 1 132 54 29 GLY H H 8.020 0.02 1 133 54 29 GLY C C 172.377 0.2 1 134 54 29 GLY CA C 45.642 0.2 1 135 54 29 GLY N N 112.261 0.15 1 136 55 30 LYS H H 7.707 0.02 1 137 55 30 LYS C C 176.136 0.2 1 138 55 30 LYS CA C 56.585 0.2 1 139 55 30 LYS CB C 33.788 0.2 1 140 55 30 LYS N N 119.419 0.15 1 141 56 31 ILE H H 8.689 0.02 1 142 56 31 ILE C C 176.141 0.2 1 143 56 31 ILE CA C 62.693 0.2 1 144 56 31 ILE CB C 37.731 0.2 1 145 56 31 ILE N N 124.912 0.15 1 146 57 32 LEU H H 8.960 0.02 1 147 57 32 LEU C C 177.080 0.2 1 148 57 32 LEU CA C 55.878 0.2 1 149 57 32 LEU CB C 42.167 0.2 1 150 57 32 LEU N N 130.475 0.15 1 151 58 33 GLU H H 7.567 0.02 1 152 58 33 GLU C C 174.650 0.2 1 153 58 33 GLU CA C 55.051 0.2 1 154 58 33 GLU CB C 34.336 0.2 1 155 58 33 GLU N N 115.970 0.15 1 156 59 34 SER H H 9.027 0.02 1 157 59 34 SER C C 172.030 0.2 1 158 59 34 SER CA C 57.983 0.2 1 159 59 34 SER CB C 67.162 0.2 1 160 59 34 SER N N 115.565 0.15 1 161 60 35 PHE H H 9.572 0.02 1 162 60 35 PHE C C 173.300 0.2 1 163 60 35 PHE CA C 59.918 0.2 1 164 60 35 PHE CB C 43.759 0.2 1 165 60 35 PHE N N 122.397 0.15 1 166 61 36 ARG H H 8.781 0.02 1 167 61 36 ARG N N 121.803 0.15 1 168 62 37 PRO C C 177.533 0.2 1 169 62 37 PRO CA C 65.290 0.2 1 170 62 37 PRO CB C 32.684 0.2 1 171 63 38 GLU H H 8.507 0.02 1 172 63 38 GLU C C 175.080 0.2 1 173 63 38 GLU CA C 55.007 0.2 1 174 63 38 GLU CB C 29.136 0.2 1 175 63 38 GLU N N 116.534 0.15 1 176 64 39 GLU H H 6.874 0.02 1 177 64 39 GLU C C 174.892 0.2 1 178 64 39 GLU CA C 55.025 0.2 1 179 64 39 GLU CB C 32.350 0.2 1 180 64 39 GLU N N 117.324 0.15 1 181 65 40 ARG H H 8.327 0.02 1 182 65 40 ARG C C 177.258 0.2 1 183 65 40 ARG CA C 55.961 0.2 1 184 65 40 ARG CB C 31.965 0.2 1 185 65 40 ARG N N 117.215 0.15 1 186 66 41 PHE H H 8.750 0.02 1 187 66 41 PHE N N 117.877 0.15 1 188 67 42 PRO C C 176.153 0.2 1 189 67 42 PRO CA C 62.761 0.2 1 190 68 43 MET H H 7.813 0.02 1 191 68 43 MET C C 179.670 0.2 1 192 68 43 MET CA C 58.426 0.2 1 193 68 43 MET N N 119.380 0.15 1 194 69 44 MET H H 10.537 0.02 1 195 69 44 MET N N 120.459 0.15 1 196 70 45 SER C C 176.091 0.2 1 197 71 46 THR H H 7.917 0.02 1 198 71 46 THR C C 175.240 0.2 1 199 71 46 THR CA C 65.961 0.2 1 200 71 46 THR N N 112.132 0.15 1 201 72 47 PHE H H 7.746 0.02 1 202 72 47 PHE C C 176.612 0.2 1 203 72 47 PHE CA C 59.473 0.2 1 204 72 47 PHE CB C 39.574 0.2 1 205 72 47 PHE N N 116.844 0.15 1 206 73 48 LYS H H 7.438 0.02 1 207 73 48 LYS C C 177.381 0.2 1 208 73 48 LYS CA C 60.042 0.2 1 209 73 48 LYS N N 122.317 0.15 1 210 74 49 VAL H H 6.639 0.02 1 211 74 49 VAL C C 176.005 0.2 1 212 74 49 VAL CA C 66.573 0.2 1 213 74 49 VAL N N 115.567 0.15 1 214 75 50 LEU H H 6.678 0.02 1 215 75 50 LEU C C 178.065 0.2 1 216 75 50 LEU CA C 57.449 0.2 1 217 75 50 LEU CB C 40.625 0.2 1 218 75 50 LEU N N 117.809 0.15 1 219 76 51 LEU H H 8.044 0.02 1 220 76 51 LEU C C 177.229 0.2 1 221 76 51 LEU CA C 57.514 0.2 1 222 76 51 LEU CB C 42.531 0.2 1 223 76 51 LEU N N 116.798 0.15 1 224 77 52 CYS H H 7.504 0.02 1 225 77 52 CYS C C 175.661 0.2 1 226 77 52 CYS CA C 63.857 0.2 1 227 77 52 CYS CB C 44.875 0.2 1 228 77 52 CYS N N 113.811 0.15 1 229 78 53 GLY H H 8.401 0.02 1 230 78 53 GLY C C 173.134 0.2 1 231 78 53 GLY CA C 47.891 0.2 1 232 78 53 GLY N N 111.027 0.15 1 233 79 54 ALA H H 7.848 0.02 1 234 79 54 ALA C C 181.006 0.2 1 235 79 54 ALA CA C 55.083 0.2 1 236 79 54 ALA CB C 16.656 0.2 1 237 79 54 ALA N N 124.666 0.15 1 238 80 55 VAL H H 8.034 0.02 1 239 80 55 VAL C C 178.007 0.2 1 240 80 55 VAL CA C 66.849 0.2 1 241 80 55 VAL N N 119.426 0.15 1 242 81 56 LEU H H 8.507 0.02 1 243 81 56 LEU C C 178.244 0.2 1 244 81 56 LEU CA C 57.947 0.2 1 245 81 56 LEU CB C 40.644 0.2 1 246 81 56 LEU N N 119.356 0.15 1 247 82 57 SER H H 8.196 0.02 1 248 82 57 SER C C 178.003 0.2 1 249 82 57 SER CA C 61.923 0.2 1 250 82 57 SER N N 115.742 0.15 1 251 83 58 ARG H H 7.521 0.02 1 252 83 58 ARG C C 179.412 0.2 1 253 83 58 ARG CA C 59.427 0.2 1 254 83 58 ARG CB C 30.512 0.2 1 255 83 58 ARG N N 121.945 0.15 1 256 84 59 VAL H H 8.322 0.02 1 257 84 59 VAL C C 180.851 0.2 1 258 84 59 VAL CA C 65.211 0.2 1 259 84 59 VAL CB C 31.083 0.2 1 260 84 59 VAL N N 124.449 0.15 1 261 85 60 ASP H H 9.114 0.02 1 262 85 60 ASP C C 177.780 0.2 1 263 85 60 ASP CA C 57.355 0.2 1 264 85 60 ASP CB C 40.986 0.2 1 265 85 60 ASP N N 123.447 0.15 1 266 86 61 ALA H H 7.535 0.02 1 267 86 61 ALA C C 177.929 0.2 1 268 86 61 ALA CA C 52.288 0.2 1 269 86 61 ALA N N 118.586 0.15 1 270 87 62 GLY H H 8.228 0.02 1 271 87 62 GLY C C 174.937 0.2 1 272 87 62 GLY CA C 45.900 0.2 1 273 87 62 GLY N N 107.709 0.15 1 274 88 63 GLN H H 8.419 0.02 1 275 88 63 GLN C C 173.524 0.2 1 276 88 63 GLN CA C 55.658 0.2 1 277 88 63 GLN CB C 30.111 0.2 1 278 88 63 GLN N N 117.322 0.15 1 279 89 64 GLU H H 7.379 0.02 1 280 89 64 GLU C C 172.700 0.2 1 281 89 64 GLU CA C 52.886 0.2 1 282 89 64 GLU CB C 33.854 0.2 1 283 89 64 GLU N N 118.050 0.15 1 284 90 65 GLN H H 10.085 0.02 1 285 90 65 GLN C C 176.055 0.2 1 286 90 65 GLN CA C 54.945 0.2 1 287 90 65 GLN CB C 31.473 0.2 1 288 90 65 GLN N N 125.233 0.15 1 289 91 66 LEU H H 9.078 0.02 1 290 91 66 LEU C C 177.339 0.2 1 291 91 66 LEU CA C 57.699 0.2 1 292 91 66 LEU CB C 41.619 0.2 1 293 91 66 LEU N N 123.124 0.15 1 294 92 67 GLY H H 8.390 0.02 1 295 92 67 GLY C C 173.880 0.2 1 296 92 67 GLY CA C 44.519 0.2 1 297 92 67 GLY N N 102.098 0.15 1 298 93 68 ARG H H 7.359 0.02 1 299 93 68 ARG C C 174.724 0.2 1 300 93 68 ARG CA C 58.030 0.2 1 301 93 68 ARG CB C 31.896 0.2 1 302 93 68 ARG N N 122.546 0.15 1 303 94 69 ARG H H 8.539 0.02 1 304 94 69 ARG C C 174.562 0.2 1 305 94 69 ARG CA C 56.563 0.2 1 306 94 69 ARG CB C 31.606 0.2 1 307 94 69 ARG N N 127.330 0.15 1 308 95 70 ILE H H 9.140 0.02 1 309 95 70 ILE C C 174.484 0.2 1 310 95 70 ILE CA C 60.464 0.2 1 311 95 70 ILE CB C 39.224 0.2 1 312 95 70 ILE N N 130.317 0.15 1 313 96 71 HIS H H 8.470 0.02 1 314 96 71 HIS C C 174.194 0.2 1 315 96 71 HIS CA C 55.509 0.2 1 316 96 71 HIS CB C 31.108 0.2 1 317 96 71 HIS N N 124.633 0.15 1 318 97 72 TYR H H 8.530 0.02 1 319 97 72 TYR C C 173.038 0.2 1 320 97 72 TYR CA C 56.092 0.2 1 321 97 72 TYR CB C 38.671 0.2 1 322 97 72 TYR N N 120.865 0.15 1 323 98 73 SER H H 9.442 0.02 1 324 98 73 SER C C 175.661 0.2 1 325 98 73 SER CA C 57.050 0.2 1 326 98 73 SER CB C 67.319 0.2 1 327 98 73 SER N N 114.528 0.15 1 328 99 74 GLN H H 9.102 0.02 1 329 99 74 GLN C C 178.011 0.2 1 330 99 74 GLN CA C 59.079 0.2 1 331 99 74 GLN CB C 28.152 0.2 1 332 99 74 GLN N N 122.016 0.15 1 333 100 75 ASN H H 8.236 0.02 1 334 100 75 ASN C C 175.622 0.2 1 335 100 75 ASN CA C 55.074 0.2 1 336 100 75 ASN CB C 38.226 0.2 1 337 100 75 ASN N N 115.322 0.15 1 338 101 76 ASP H H 7.910 0.02 1 339 101 76 ASP C C 175.572 0.2 1 340 101 76 ASP CA C 55.650 0.2 1 341 101 76 ASP CB C 42.566 0.2 1 342 101 76 ASP N N 116.691 0.15 1 343 102 77 LEU H H 7.135 0.02 1 344 102 77 LEU C C 178.079 0.2 1 345 102 77 LEU CA C 55.382 0.2 1 346 102 77 LEU CB C 41.913 0.2 1 347 102 77 LEU N N 116.592 0.15 1 348 103 78 VAL H H 7.631 0.02 1 349 103 78 VAL C C 176.552 0.2 1 350 103 78 VAL CA C 58.962 0.2 1 351 103 78 VAL CB C 34.567 0.2 1 352 103 78 VAL N N 117.136 0.15 1 353 104 79 GLU H H 8.615 0.02 1 354 104 79 GLU C C 175.020 0.2 1 355 104 79 GLU CA C 58.104 0.2 1 356 104 79 GLU CB C 30.222 0.2 1 357 104 79 GLU N N 123.857 0.15 1 358 105 80 TRP H H 8.786 0.02 1 359 105 80 TRP C C 171.588 0.2 1 360 105 80 TRP CA C 58.463 0.2 1 361 105 80 TRP CB C 27.481 0.2 1 362 105 80 TRP N N 121.660 0.15 1 363 106 81 SER H H 8.268 0.02 1 364 106 81 SER N N 120.448 0.15 1 365 107 82 PRO C C 177.592 0.2 1 366 108 83 VAL H H 8.508 0.02 1 367 108 83 VAL C C 179.063 0.2 1 368 108 83 VAL CA C 64.400 0.2 1 369 108 83 VAL N N 118.050 0.15 1 370 109 84 THR H H 9.633 0.02 1 371 109 84 THR C C 181.973 0.2 1 372 109 84 THR CA C 63.958 0.2 1 373 109 84 THR CB C 69.301 0.2 1 374 109 84 THR N N 113.723 0.15 1 375 110 85 GLU H H 8.208 0.02 1 376 110 85 GLU C C 176.471 0.2 1 377 110 85 GLU CA C 58.895 0.2 1 378 110 85 GLU CB C 28.568 0.2 1 379 110 85 GLU N N 119.951 0.15 1 380 111 86 LYS H H 7.457 0.02 1 381 111 86 LYS C C 177.265 0.2 1 382 111 86 LYS CA C 56.019 0.2 1 383 111 86 LYS CB C 32.514 0.2 1 384 111 86 LYS N N 116.265 0.15 1 385 112 87 HIS H H 7.137 0.02 1 386 112 87 HIS C C 174.538 0.2 1 387 112 87 HIS CA C 55.216 0.2 1 388 112 87 HIS CB C 28.615 0.2 1 389 112 87 HIS N N 116.254 0.15 1 390 113 88 LEU H H 7.866 0.02 1 391 113 88 LEU C C 179.200 0.2 1 392 113 88 LEU CA C 58.170 0.2 1 393 113 88 LEU CB C 42.067 0.2 1 394 113 88 LEU N N 120.210 0.15 1 395 114 89 THR H H 8.327 0.02 1 396 114 89 THR C C 175.616 0.2 1 397 114 89 THR CA C 64.393 0.2 1 398 114 89 THR CB C 68.958 0.2 1 399 114 89 THR N N 109.412 0.15 1 400 115 90 ASP H H 8.817 0.02 1 401 115 90 ASP C C 177.673 0.2 1 402 115 90 ASP CA C 54.016 0.2 1 403 115 90 ASP CB C 40.538 0.2 1 404 115 90 ASP N N 117.149 0.15 1 405 116 91 GLY H H 7.925 0.02 1 406 116 91 GLY C C 171.625 0.2 1 407 116 91 GLY CA C 45.032 0.2 1 408 116 91 GLY N N 110.719 0.15 1 409 117 92 MET H H 8.330 0.02 1 410 117 92 MET C C 175.135 0.2 1 411 117 92 MET CA C 54.988 0.2 1 412 117 92 MET CB C 40.438 0.2 1 413 117 92 MET N N 113.493 0.15 1 414 118 93 THR H H 8.933 0.02 1 415 118 93 THR C C 175.871 0.2 1 416 118 93 THR CA C 60.201 0.2 1 417 118 93 THR CB C 71.047 0.2 1 418 118 93 THR N N 112.214 0.15 1 419 119 94 VAL H H 8.125 0.02 1 420 119 94 VAL C C 177.948 0.2 1 421 119 94 VAL CA C 68.154 0.2 1 422 119 94 VAL N N 122.042 0.15 1 423 120 95 ARG H H 9.086 0.02 1 424 120 95 ARG C C 177.548 0.2 1 425 120 95 ARG CA C 60.219 0.2 1 426 120 95 ARG CB C 31.326 0.2 1 427 120 95 ARG N N 118.383 0.15 1 428 121 96 GLU H H 7.638 0.02 1 429 121 96 GLU C C 180.568 0.2 1 430 121 96 GLU CA C 58.462 0.2 1 431 121 96 GLU CB C 30.049 0.2 1 432 121 96 GLU N N 118.410 0.15 1 433 122 97 LEU H H 9.135 0.02 1 434 122 97 LEU C C 179.069 0.2 1 435 122 97 LEU CA C 58.006 0.2 1 436 122 97 LEU CB C 41.100 0.2 1 437 122 97 LEU N N 122.732 0.15 1 438 123 98 CYS H H 8.169 0.02 1 439 123 98 CYS C C 175.962 0.2 1 440 123 98 CYS CA C 62.348 0.2 1 441 123 98 CYS CB C 42.497 0.2 1 442 123 98 CYS N N 119.019 0.15 1 443 124 99 SER H H 7.719 0.02 1 444 124 99 SER C C 179.019 0.2 1 445 124 99 SER CA C 61.422 0.2 1 446 124 99 SER CB C 62.556 0.2 1 447 124 99 SER N N 113.189 0.15 1 448 125 100 ALA H H 8.492 0.02 1 449 125 100 ALA C C 180.265 0.2 1 450 125 100 ALA CA C 55.667 0.2 1 451 125 100 ALA CB C 17.592 0.2 1 452 125 100 ALA N N 124.606 0.15 1 453 126 101 ALA H H 8.700 0.02 1 454 126 101 ALA C C 178.401 0.2 1 455 126 101 ALA CA C 55.061 0.2 1 456 126 101 ALA CB C 17.513 0.2 1 457 126 101 ALA N N 121.003 0.15 1 458 127 102 ILE H H 8.186 0.02 1 459 127 102 ILE C C 176.544 0.2 1 460 127 102 ILE N N 113.493 0.15 1 461 128 103 THR H H 8.958 0.02 1 462 128 103 THR C C 176.028 0.2 1 463 128 103 THR N N 109.205 0.15 1 464 129 104 MET H H 6.870 0.02 1 465 129 104 MET C C 176.011 0.2 1 466 129 104 MET CA C 53.010 0.2 1 467 129 104 MET N N 114.653 0.15 1 468 130 105 SER H H 7.196 0.02 1 469 130 105 SER C C 174.440 0.2 1 470 130 105 SER CA C 58.926 0.2 1 471 130 105 SER N N 114.909 0.15 1 472 131 106 ASP H H 7.465 0.02 1 473 131 106 ASP N N 120.320 0.15 1 474 132 107 ASN C C 178.091 0.2 1 475 132 107 ASN CA C 56.338 0.2 1 476 132 107 ASN CB C 39.173 0.2 1 477 133 108 THR H H 7.634 0.02 1 478 133 108 THR C C 176.682 0.2 1 479 133 108 THR CA C 67.953 0.2 1 480 133 108 THR CB C 67.127 0.2 1 481 133 108 THR N N 120.199 0.15 1 482 134 109 ALA H H 8.900 0.02 1 483 134 109 ALA C C 178.473 0.2 1 484 134 109 ALA CB C 18.661 0.2 1 485 134 109 ALA N N 122.638 0.15 1 486 135 110 ALA H H 7.219 0.02 1 487 135 110 ALA C C 178.185 0.2 1 488 135 110 ALA CB C 19.438 0.2 1 489 135 110 ALA N N 115.487 0.15 1 490 136 111 ASN H H 8.029 0.02 1 491 136 111 ASN C C 178.791 0.2 1 492 136 111 ASN CA C 56.179 0.2 1 493 136 111 ASN CB C 37.257 0.2 1 494 136 111 ASN N N 119.654 0.15 1 495 137 112 LEU H H 9.084 0.02 1 496 137 112 LEU C C 181.196 0.2 1 497 137 112 LEU CA C 58.268 0.2 1 498 137 112 LEU N N 121.646 0.15 1 499 138 113 LEU H H 8.204 0.02 1 500 138 113 LEU C C 180.765 0.2 1 501 138 113 LEU CA C 57.487 0.2 1 502 138 113 LEU CB C 42.775 0.2 1 503 138 113 LEU N N 119.492 0.15 1 504 139 114 LEU H H 9.205 0.02 1 505 139 114 LEU C C 180.098 0.2 1 506 139 114 LEU N N 124.105 0.15 1 507 140 115 THR H H 8.709 0.02 1 508 140 115 THR C C 177.814 0.2 1 509 140 115 THR CA C 68.106 0.2 1 510 140 115 THR N N 118.128 0.15 1 511 141 116 THR H H 7.669 0.02 1 512 141 116 THR C C 175.762 0.2 1 513 141 116 THR CA C 65.434 0.2 1 514 141 116 THR CB C 68.984 0.2 1 515 141 116 THR N N 112.867 0.15 1 516 142 117 ILE H H 6.920 0.02 1 517 142 117 ILE C C 175.442 0.2 1 518 142 117 ILE CA C 61.054 0.2 1 519 142 117 ILE CB C 38.778 0.2 1 520 142 117 ILE N N 110.935 0.15 1 521 143 118 GLY H H 7.510 0.02 1 522 143 118 GLY C C 175.150 0.2 1 523 143 118 GLY CA C 45.000 0.2 1 524 143 118 GLY N N 106.445 0.15 1 525 144 119 GLY H H 8.227 0.02 1 526 144 119 GLY N N 108.279 0.15 1 527 145 120 PRO C C 177.889 0.2 1 528 145 120 PRO CA C 66.268 0.2 1 529 145 120 PRO CB C 31.964 0.2 1 530 146 121 LYS H H 8.683 0.02 1 531 146 121 LYS C C 179.838 0.2 1 532 146 121 LYS CA C 59.480 0.2 1 533 146 121 LYS CB C 31.935 0.2 1 534 146 121 LYS N N 116.085 0.15 1 535 147 122 GLU H H 7.365 0.02 1 536 147 122 GLU C C 180.378 0.2 1 537 147 122 GLU CA C 57.102 0.2 1 538 147 122 GLU CB C 29.252 0.2 1 539 147 122 GLU N N 118.599 0.15 1 540 148 123 LEU H H 7.670 0.02 1 541 148 123 LEU C C 178.131 0.2 1 542 148 123 LEU CA C 57.506 0.2 1 543 148 123 LEU CB C 40.319 0.2 1 544 148 123 LEU N N 123.395 0.15 1 545 149 124 THR H H 8.187 0.02 1 546 149 124 THR C C 175.077 0.2 1 547 149 124 THR CA C 68.013 0.2 1 548 149 124 THR N N 117.068 0.15 1 549 150 125 ALA H H 7.909 0.02 1 550 150 125 ALA C C 179.507 0.2 1 551 150 125 ALA CA C 55.775 0.2 1 552 150 125 ALA CB C 18.017 0.2 1 553 150 125 ALA N N 123.155 0.15 1 554 151 126 PHE H H 7.808 0.02 1 555 151 126 PHE C C 177.711 0.2 1 556 151 126 PHE CA C 61.095 0.2 1 557 151 126 PHE CB C 38.244 0.2 1 558 151 126 PHE N N 120.486 0.15 1 559 152 127 LEU H H 8.072 0.02 1 560 152 127 LEU C C 179.075 0.2 1 561 152 127 LEU CA C 57.692 0.2 1 562 152 127 LEU CB C 39.927 0.2 1 563 152 127 LEU N N 121.632 0.15 1 564 153 128 HIS H H 8.915 0.02 1 565 153 128 HIS C C 179.840 0.2 1 566 153 128 HIS CA C 59.314 0.2 1 567 153 128 HIS CB C 29.060 0.2 1 568 153 128 HIS N N 120.785 0.15 1 569 154 129 ASN H H 8.395 0.02 1 570 154 129 ASN C C 176.483 0.2 1 571 154 129 ASN CA C 55.621 0.2 1 572 154 129 ASN CB C 38.226 0.2 1 573 154 129 ASN N N 118.241 0.15 1 574 155 130 MET H H 7.522 0.02 1 575 155 130 MET C C 175.838 0.2 1 576 155 130 MET CA C 55.440 0.2 1 577 155 130 MET CB C 31.972 0.2 1 578 155 130 MET N N 115.550 0.15 1 579 156 131 GLY H H 7.748 0.02 1 580 156 131 GLY C C 172.695 0.2 1 581 156 131 GLY CA C 45.332 0.2 1 582 156 131 GLY N N 107.746 0.15 1 583 157 132 ASP H H 8.022 0.02 1 584 157 132 ASP C C 174.728 0.2 1 585 157 132 ASP CA C 52.303 0.2 1 586 157 132 ASP CB C 39.751 0.2 1 587 157 132 ASP N N 121.703 0.15 1 588 158 133 HIS H H 8.336 0.02 1 589 158 133 HIS C C 175.028 0.2 1 590 158 133 HIS CA C 54.528 0.2 1 591 158 133 HIS CB C 29.537 0.2 1 592 158 133 HIS N N 121.262 0.15 1 593 159 134 VAL H H 8.819 0.02 1 594 159 134 VAL C C 176.028 0.2 1 595 159 134 VAL CA C 63.823 0.2 1 596 159 134 VAL CB C 34.867 0.2 1 597 159 134 VAL N N 121.373 0.15 1 598 160 135 THR H H 9.386 0.02 1 599 160 135 THR C C 172.791 0.2 1 600 160 135 THR CA C 64.846 0.2 1 601 160 135 THR N N 125.682 0.15 1 602 161 136 ARG H H 8.480 0.02 1 603 161 136 ARG C C 171.646 0.2 1 604 161 136 ARG CA C 54.111 0.2 1 605 161 136 ARG CB C 32.591 0.2 1 606 161 136 ARG N N 119.768 0.15 1 607 162 137 LEU H H 7.750 0.02 1 608 162 137 LEU C C 174.291 0.2 1 609 162 137 LEU CA C 53.181 0.2 1 610 162 137 LEU CB C 45.955 0.2 1 611 162 137 LEU N N 121.131 0.15 1 612 163 138 ASP H H 10.031 0.02 1 613 163 138 ASP C C 175.663 0.2 1 614 163 138 ASP CA C 55.493 0.2 1 615 163 138 ASP CB C 45.902 0.2 1 616 163 138 ASP N N 126.784 0.15 1 617 164 139 ARG H H 9.243 0.02 1 618 164 139 ARG C C 170.522 0.2 1 619 164 139 ARG CA C 55.402 0.2 1 620 164 139 ARG CB C 34.580 0.2 1 621 164 139 ARG N N 125.228 0.15 1 622 165 140 TRP H H 7.707 0.02 1 623 165 140 TRP C C 177.906 0.2 1 624 165 140 TRP CA C 55.113 0.2 1 625 165 140 TRP CB C 29.100 0.2 1 626 165 140 TRP N N 114.623 0.15 1 627 166 141 GLU H H 9.510 0.02 1 628 166 141 GLU N N 117.711 0.15 1 629 167 142 PRO C C 177.857 0.2 1 630 167 142 PRO CA C 63.849 0.2 1 631 167 142 PRO CB C 34.236 0.2 1 632 168 143 GLU H H 8.674 0.02 1 633 168 143 GLU C C 176.660 0.2 1 634 168 143 GLU CA C 60.863 0.2 1 635 168 143 GLU CB C 29.472 0.2 1 636 168 143 GLU N N 128.351 0.15 1 637 169 144 LEU H H 7.717 0.02 1 638 169 144 LEU C C 176.824 0.2 1 639 169 144 LEU CA C 57.213 0.2 1 640 169 144 LEU CB C 40.684 0.2 1 641 169 144 LEU N N 113.121 0.15 1 642 170 145 ASN H H 7.585 0.02 1 643 170 145 ASN C C 174.776 0.2 1 644 170 145 ASN CA C 53.992 0.2 1 645 170 145 ASN CB C 40.683 0.2 1 646 170 145 ASN N N 119.935 0.15 1 647 171 146 GLU H H 7.462 0.02 1 648 171 146 GLU C C 175.726 0.2 1 649 171 146 GLU CA C 60.801 0.2 1 650 171 146 GLU CB C 30.938 0.2 1 651 171 146 GLU N N 120.739 0.15 1 652 172 147 ALA H H 9.514 0.02 1 653 172 147 ALA C C 176.510 0.2 1 654 172 147 ALA CA C 52.067 0.2 1 655 172 147 ALA CB C 18.053 0.2 1 656 172 147 ALA N N 118.304 0.15 1 657 173 148 ILE H H 8.669 0.02 1 658 173 148 ILE N N 120.822 0.15 1 659 174 149 PRO C C 177.515 0.2 1 660 174 149 PRO CA C 64.316 0.2 1 661 174 149 PRO CB C 31.501 0.2 1 662 175 150 ASN H H 8.915 0.02 1 663 175 150 ASN C C 173.249 0.2 1 664 175 150 ASN CA C 55.244 0.2 1 665 175 150 ASN CB C 37.459 0.2 1 666 175 150 ASN N N 115.888 0.15 1 667 176 151 ASP H H 7.613 0.02 1 668 176 151 ASP C C 177.324 0.2 1 669 176 151 ASP CA C 53.292 0.2 1 670 176 151 ASP CB C 42.074 0.2 1 671 176 151 ASP N N 120.832 0.15 1 672 177 152 GLU H H 9.000 0.02 1 673 177 152 GLU C C 177.613 0.2 1 674 177 152 GLU CA C 56.917 0.2 1 675 177 152 GLU CB C 29.958 0.2 1 676 177 152 GLU N N 126.443 0.15 1 677 178 153 ARG H H 8.118 0.02 1 678 178 153 ARG C C 177.172 0.2 1 679 178 153 ARG CA C 57.386 0.2 1 680 178 153 ARG N N 122.315 0.15 1 681 179 154 ASP H H 8.806 0.02 1 682 179 154 ASP C C 177.937 0.2 1 683 179 154 ASP CA C 55.927 0.2 1 684 179 154 ASP CB C 42.513 0.2 1 685 179 154 ASP N N 115.582 0.15 1 686 180 155 THR H H 7.292 0.02 1 687 180 155 THR C C 173.102 0.2 1 688 180 155 THR CA C 59.847 0.2 1 689 180 155 THR N N 104.795 0.15 1 690 181 156 THR H H 8.238 0.02 1 691 181 156 THR C C 173.581 0.2 1 692 181 156 THR CA C 59.804 0.2 1 693 181 156 THR CB C 69.066 0.2 1 694 181 156 THR N N 111.758 0.15 1 695 182 157 MET H H 8.540 0.02 1 696 182 157 MET N N 117.892 0.15 1 697 183 158 PRO C C 176.881 0.2 1 698 183 158 PRO CA C 67.492 0.2 1 699 183 158 PRO CB C 32.525 0.2 1 700 184 159 ALA H H 8.695 0.02 1 701 184 159 ALA C C 179.081 0.2 1 702 184 159 ALA CA C 56.178 0.2 1 703 184 159 ALA CB C 18.509 0.2 1 704 184 159 ALA N N 114.766 0.15 1 705 185 160 ALA H H 6.878 0.02 1 706 185 160 ALA C C 177.990 0.2 1 707 185 160 ALA CA C 54.762 0.2 1 708 185 160 ALA CB C 18.957 0.2 1 709 185 160 ALA N N 121.088 0.15 1 710 186 161 MET H H 8.344 0.02 1 711 186 161 MET C C 177.887 0.2 1 712 186 161 MET CA C 57.369 0.2 1 713 186 161 MET CB C 31.092 0.2 1 714 186 161 MET N N 116.123 0.15 1 715 187 162 ALA H H 8.293 0.02 1 716 187 162 ALA C C 178.438 0.2 1 717 187 162 ALA CA C 55.810 0.2 1 718 187 162 ALA CB C 19.413 0.2 1 719 187 162 ALA N N 117.822 0.15 1 720 188 163 THR H H 7.719 0.02 1 721 188 163 THR C C 177.374 0.2 1 722 188 163 THR CA C 66.591 0.2 1 723 188 163 THR CB C 68.957 0.2 1 724 188 163 THR N N 112.303 0.15 1 725 189 164 THR H H 9.069 0.02 1 726 189 164 THR C C 175.759 0.2 1 727 189 164 THR CA C 67.192 0.2 1 728 189 164 THR N N 124.624 0.15 1 729 190 165 LEU H H 8.869 0.02 1 730 190 165 LEU C C 178.229 0.2 1 731 190 165 LEU CA C 58.081 0.2 1 732 190 165 LEU CB C 41.633 0.2 1 733 190 165 LEU N N 121.364 0.15 1 734 191 166 ARG H H 8.152 0.02 1 735 191 166 ARG C C 178.752 0.2 1 736 191 166 ARG CA C 60.921 0.2 1 737 191 166 ARG CB C 28.989 0.2 1 738 191 166 ARG N N 118.353 0.15 1 739 192 167 LYS H H 8.124 0.02 1 740 192 167 LYS C C 178.638 0.2 1 741 192 167 LYS CA C 60.126 0.2 1 742 192 167 LYS CB C 32.907 0.2 1 743 192 167 LYS N N 120.975 0.15 1 744 193 168 LEU H H 8.067 0.02 1 745 193 168 LEU C C 177.470 0.2 1 746 193 168 LEU CA C 57.961 0.2 1 747 193 168 LEU CB C 42.997 0.2 1 748 193 168 LEU N N 117.436 0.15 1 749 194 169 LEU H H 8.066 0.02 1 750 194 169 LEU C C 178.325 0.2 1 751 194 169 LEU CA C 56.673 0.2 1 752 194 169 LEU CB C 43.080 0.2 1 753 194 169 LEU N N 111.458 0.15 1 754 195 170 THR H H 7.993 0.02 1 755 195 170 THR C C 174.662 0.2 1 756 195 170 THR CA C 60.978 0.2 1 757 195 170 THR CB C 72.073 0.2 1 758 195 170 THR N N 105.391 0.15 1 759 196 171 GLY H H 7.913 0.02 1 760 196 171 GLY C C 174.038 0.2 1 761 196 171 GLY CA C 45.014 0.2 1 762 196 171 GLY N N 110.535 0.15 1 763 197 172 GLU H H 8.404 0.02 1 764 197 172 GLU C C 176.434 0.2 1 765 197 172 GLU CA C 56.027 0.2 1 766 197 172 GLU CB C 29.581 0.2 1 767 197 172 GLU N N 116.766 0.15 1 768 198 173 LEU H H 7.490 0.02 1 769 198 173 LEU C C 177.429 0.2 1 770 198 173 LEU CB C 42.742 0.2 1 771 198 173 LEU N N 122.668 0.15 1 772 199 174 LEU H H 8.714 0.02 1 773 199 174 LEU C C 177.597 0.2 1 774 199 174 LEU CA C 52.685 0.2 1 775 199 174 LEU CB C 44.389 0.2 1 776 199 174 LEU N N 118.270 0.15 1 777 200 175 THR H H 8.980 0.02 1 778 200 175 THR C C 175.382 0.2 1 779 200 175 THR CA C 62.202 0.2 1 780 200 175 THR CB C 71.830 0.2 1 781 200 175 THR N N 112.524 0.15 1 782 201 176 LEU H H 8.713 0.02 1 783 201 176 LEU C C 179.087 0.2 1 784 201 176 LEU CA C 58.935 0.2 1 785 201 176 LEU CB C 41.611 0.2 1 786 201 176 LEU N N 123.040 0.15 1 787 202 177 ALA H H 8.466 0.02 1 788 202 177 ALA C C 181.502 0.2 1 789 202 177 ALA CA C 55.042 0.2 1 790 202 177 ALA CB C 18.110 0.2 1 791 202 177 ALA N N 118.701 0.15 1 792 203 178 SER H H 7.763 0.02 1 793 203 178 SER C C 175.076 0.2 1 794 203 178 SER CA C 62.867 0.2 1 795 203 178 SER N N 118.468 0.15 1 796 204 179 ARG H H 9.082 0.02 1 797 204 179 ARG C C 178.547 0.2 1 798 204 179 ARG CA C 60.423 0.2 1 799 204 179 ARG CB C 31.023 0.2 1 800 204 179 ARG N N 123.581 0.15 1 801 205 180 GLN H H 8.239 0.02 1 802 205 180 GLN C C 177.122 0.2 1 803 205 180 GLN CA C 57.621 0.2 1 804 205 180 GLN CB C 28.364 0.2 1 805 205 180 GLN N N 117.607 0.15 1 806 206 181 GLN H H 7.621 0.02 1 807 206 181 GLN C C 177.878 0.2 1 808 206 181 GLN CA C 57.033 0.2 1 809 206 181 GLN CB C 28.615 0.2 1 810 206 181 GLN N N 118.109 0.15 1 811 207 182 LEU H H 7.994 0.02 1 812 207 182 LEU C C 178.284 0.2 1 813 207 182 LEU CA C 58.223 0.2 1 814 207 182 LEU CB C 41.711 0.2 1 815 207 182 LEU N N 121.044 0.15 1 816 208 183 ILE H H 7.811 0.02 1 817 208 183 ILE C C 177.265 0.2 1 818 208 183 ILE CA C 65.629 0.2 1 819 208 183 ILE CB C 38.245 0.2 1 820 208 183 ILE N N 118.154 0.15 1 821 209 184 ASP H H 8.694 0.02 1 822 209 184 ASP C C 181.442 0.2 1 823 209 184 ASP CA C 57.600 0.2 1 824 209 184 ASP CB C 40.082 0.2 1 825 209 184 ASP N N 122.382 0.15 1 826 210 185 TRP H H 8.058 0.02 1 827 210 185 TRP C C 177.133 0.2 1 828 210 185 TRP CA C 59.830 0.2 1 829 210 185 TRP CB C 29.012 0.2 1 830 210 185 TRP N N 120.495 0.15 1 831 211 186 MET H H 7.757 0.02 1 832 211 186 MET C C 180.270 0.2 1 833 211 186 MET CA C 59.467 0.2 1 834 211 186 MET N N 115.996 0.15 1 835 212 187 GLU H H 9.642 0.02 1 836 212 187 GLU C C 178.127 0.2 1 837 212 187 GLU CA C 59.717 0.2 1 838 212 187 GLU CB C 29.966 0.2 1 839 212 187 GLU N N 124.658 0.15 1 840 213 188 ALA H H 7.348 0.02 1 841 213 188 ALA C C 175.511 0.2 1 842 213 188 ALA CA C 51.744 0.2 1 843 213 188 ALA N N 119.722 0.15 1 844 214 189 ASP H H 7.014 0.02 1 845 214 189 ASP C C 176.738 0.2 1 846 214 189 ASP CA C 56.303 0.2 1 847 214 189 ASP CB C 44.110 0.2 1 848 214 189 ASP N N 115.899 0.15 1 849 215 190 LYS H H 9.218 0.02 1 850 215 190 LYS C C 179.636 0.2 1 851 215 190 LYS CA C 56.720 0.2 1 852 215 190 LYS N N 128.075 0.15 1 853 216 191 VAL H H 7.267 0.02 1 854 216 191 VAL C C 174.959 0.2 1 855 216 191 VAL CA C 60.782 0.2 1 856 216 191 VAL N N 110.289 0.15 1 857 217 192 ALA H H 8.891 0.02 1 858 217 192 ALA C C 178.357 0.2 1 859 217 192 ALA CB C 20.845 0.2 1 860 217 192 ALA N N 125.406 0.15 1 861 218 193 GLY H H 8.943 0.02 1 862 218 193 GLY N N 114.293 0.15 1 863 219 194 PRO C C 175.178 0.2 1 864 219 194 PRO CA C 64.065 0.2 1 865 220 195 LEU H H 6.819 0.02 1 866 220 195 LEU C C 176.419 0.2 1 867 220 195 LEU CA C 51.935 0.2 1 868 220 195 LEU N N 114.022 0.15 1 869 221 196 LEU H H 6.902 0.02 1 870 221 196 LEU C C 178.553 0.2 1 871 221 196 LEU CA C 58.049 0.2 1 872 221 196 LEU N N 123.417 0.15 1 873 222 197 ARG H H 8.969 0.02 1 874 222 197 ARG C C 177.483 0.2 1 875 222 197 ARG CA C 59.914 0.2 1 876 222 197 ARG CB C 30.019 0.2 1 877 222 197 ARG N N 116.061 0.15 1 878 223 198 SER H H 7.036 0.02 1 879 223 198 SER C C 174.043 0.2 1 880 223 198 SER CA C 60.999 0.2 1 881 223 198 SER CB C 63.345 0.2 1 882 223 198 SER N N 113.404 0.15 1 883 224 199 ALA H H 7.288 0.02 1 884 224 199 ALA C C 176.295 0.2 1 885 224 199 ALA CA C 50.682 0.2 1 886 224 199 ALA CB C 19.522 0.2 1 887 224 199 ALA N N 122.881 0.15 1 888 225 200 LEU H H 6.724 0.02 1 889 225 200 LEU N N 120.958 0.15 1 890 226 201 PRO C C 175.817 0.2 1 891 226 201 PRO CA C 61.442 0.2 1 892 226 201 PRO CB C 32.006 0.2 1 893 227 202 ALA H H 8.258 0.02 1 894 227 202 ALA C C 179.431 0.2 1 895 227 202 ALA CA C 53.506 0.2 1 896 227 202 ALA CB C 18.377 0.2 1 897 227 202 ALA N N 122.766 0.15 1 898 228 203 GLY H H 8.838 0.02 1 899 228 203 GLY C C 175.360 0.2 1 900 228 203 GLY CA C 45.444 0.2 1 901 228 203 GLY N N 110.165 0.15 1 902 229 204 TRP H H 7.642 0.02 1 903 229 204 TRP C C 175.383 0.2 1 904 229 204 TRP CA C 59.072 0.2 1 905 229 204 TRP N N 120.601 0.15 1 906 230 205 PHE H H 9.395 0.02 1 907 230 205 PHE C C 174.818 0.2 1 908 230 205 PHE CA C 56.839 0.2 1 909 230 205 PHE CB C 42.158 0.2 1 910 230 205 PHE N N 122.983 0.15 1 911 231 206 ILE H H 7.534 0.02 1 912 231 206 ILE C C 169.507 0.2 1 913 231 206 ILE CA C 60.508 0.2 1 914 231 206 ILE N N 123.407 0.15 1 915 232 207 ALA H H 8.466 0.02 1 916 232 207 ALA C C 174.921 0.2 1 917 232 207 ALA CA C 50.713 0.2 1 918 232 207 ALA CB C 21.461 0.2 1 919 232 207 ALA N N 128.105 0.15 1 920 233 208 ASP H H 8.261 0.02 1 921 233 208 ASP C C 172.706 0.2 1 922 233 208 ASP N N 124.005 0.15 1 923 234 209 LYS H H 8.049 0.02 1 924 234 209 LYS C C 178.328 0.2 1 925 234 209 LYS N N 109.620 0.15 1 926 235 210 SER H H 8.277 0.02 1 927 235 210 SER C C 174.046 0.2 1 928 235 210 SER N N 115.560 0.15 1 929 236 211 GLY H H 8.590 0.02 1 930 236 211 GLY N N 102.953 0.15 1 931 237 212 ALA C C 175.434 0.2 1 932 238 213 GLY H H 7.720 0.02 1 933 238 213 GLY C C 172.748 0.2 1 934 238 213 GLY CA C 45.483 0.2 1 935 238 213 GLY N N 107.422 0.15 1 936 239 214 GLU H H 7.867 0.02 1 937 239 214 GLU C C 176.008 0.2 1 938 239 214 GLU CA C 56.193 0.2 1 939 239 214 GLU CB C 30.050 0.2 1 940 239 214 GLU N N 117.102 0.15 1 941 240 215 ARG H H 9.479 0.02 1 942 240 215 ARG C C 176.065 0.2 1 943 240 215 ARG CA C 57.358 0.2 1 944 240 215 ARG CB C 27.618 0.2 1 945 240 215 ARG N N 118.133 0.15 1 946 241 216 GLY H H 8.804 0.02 1 947 241 216 GLY C C 177.323 0.2 1 948 241 216 GLY CA C 46.523 0.2 1 949 241 216 GLY N N 102.899 0.15 1 950 242 217 SER H H 7.537 0.02 1 951 242 217 SER C C 174.938 0.2 1 952 242 217 SER CA C 60.049 0.2 1 953 242 217 SER CB C 64.389 0.2 1 954 242 217 SER N N 119.299 0.15 1 955 243 218 ARG H H 9.057 0.02 1 956 243 218 ARG C C 174.228 0.2 1 957 243 218 ARG CA C 54.483 0.2 1 958 243 218 ARG CB C 34.850 0.2 1 959 243 218 ARG N N 126.291 0.15 1 960 244 219 GLY H H 8.519 0.02 1 961 244 219 GLY C C 170.303 0.2 1 962 244 219 GLY CA C 46.779 0.2 1 963 244 219 GLY N N 111.676 0.15 1 964 245 220 ILE H H 9.179 0.02 1 965 245 220 ILE C C 170.468 0.2 1 966 245 220 ILE CA C 59.678 0.2 1 967 245 220 ILE N N 116.814 0.15 1 968 246 221 ILE H H 8.130 0.02 1 969 246 221 ILE C C 174.761 0.2 1 970 246 221 ILE CA C 58.489 0.2 1 971 246 221 ILE CB C 40.107 0.2 1 972 246 221 ILE N N 118.092 0.15 1 973 247 222 ALA H H 9.006 0.02 1 974 247 222 ALA C C 174.625 0.2 1 975 247 222 ALA CA C 51.374 0.2 1 976 247 222 ALA CB C 24.507 0.2 1 977 247 222 ALA N N 122.770 0.15 1 978 248 223 ALA H H 9.361 0.02 1 979 248 223 ALA C C 175.618 0.2 1 980 248 223 ALA CA C 50.337 0.2 1 981 248 223 ALA CB C 20.430 0.2 1 982 248 223 ALA N N 122.898 0.15 1 983 249 224 LEU H H 9.342 0.02 1 984 249 224 LEU C C 176.701 0.2 1 985 249 224 LEU CA C 55.110 0.2 1 986 249 224 LEU CB C 46.598 0.2 1 987 249 224 LEU N N 121.244 0.15 1 988 250 225 GLY H H 8.830 0.02 1 989 250 225 GLY N N 110.506 0.15 1 990 251 226 PRO C C 176.035 0.2 1 991 251 226 PRO CA C 60.851 0.2 1 992 251 226 PRO CB C 31.599 0.2 1 993 252 227 ASP H H 7.953 0.02 1 994 252 227 ASP C C 177.157 0.2 1 995 252 227 ASP CA C 55.003 0.2 1 996 252 227 ASP CB C 39.253 0.2 1 997 252 227 ASP N N 114.370 0.15 1 998 253 228 GLY H H 7.734 0.02 1 999 253 228 GLY C C 173.402 0.2 1 1000 253 228 GLY CA C 46.900 0.2 1 1001 253 228 GLY N N 100.239 0.15 1 1002 254 229 LYS H H 7.199 0.02 1 1003 254 229 LYS N N 119.397 0.15 1 1004 255 230 PRO C C 176.094 0.2 1 1005 255 230 PRO CA C 62.196 0.2 1 1006 255 230 PRO CB C 31.490 0.2 1 1007 256 231 SER H H 8.561 0.02 1 1008 256 231 SER C C 174.537 0.2 1 1009 256 231 SER CA C 59.016 0.2 1 1010 256 231 SER CB C 65.735 0.2 1 1011 256 231 SER N N 112.550 0.15 1 1012 257 232 ARG H H 8.853 0.02 1 1013 257 232 ARG C C 174.533 0.2 1 1014 257 232 ARG CA C 55.940 0.2 1 1015 257 232 ARG CB C 36.192 0.2 1 1016 257 232 ARG N N 123.133 0.15 1 1017 258 233 ILE H H 9.257 0.02 1 1018 258 233 ILE C C 174.569 0.2 1 1019 258 233 ILE CA C 58.835 0.2 1 1020 258 233 ILE CB C 40.721 0.2 1 1021 258 233 ILE N N 122.695 0.15 1 1022 259 234 VAL H H 9.226 0.02 1 1023 259 234 VAL C C 173.552 0.2 1 1024 259 234 VAL CA C 59.591 0.2 1 1025 259 234 VAL CB C 36.253 0.2 1 1026 259 234 VAL N N 126.292 0.15 1 1027 260 235 VAL H H 8.255 0.02 1 1028 260 235 VAL C C 173.804 0.2 1 1029 260 235 VAL CA C 60.568 0.2 1 1030 260 235 VAL CB C 35.794 0.2 1 1031 260 235 VAL N N 125.369 0.15 1 1032 261 236 ILE H H 8.356 0.02 1 1033 261 236 ILE C C 174.331 0.2 1 1034 261 236 ILE CA C 60.070 0.2 1 1035 261 236 ILE CB C 41.784 0.2 1 1036 261 236 ILE N N 123.142 0.15 1 1037 262 237 TYR H H 8.747 0.02 1 1038 262 237 TYR C C 173.979 0.2 1 1039 262 237 TYR CA C 57.114 0.2 1 1040 262 237 TYR CB C 45.415 0.2 1 1041 262 237 TYR N N 122.286 0.15 1 1042 263 238 THR H H 8.958 0.02 1 1043 263 238 THR C C 172.502 0.2 1 1044 263 238 THR CA C 59.615 0.2 1 1045 263 238 THR CB C 70.410 0.2 1 1046 263 238 THR N N 111.424 0.15 1 1047 264 239 THR H H 8.043 0.02 1 1048 264 239 THR C C 171.627 0.2 1 1049 264 239 THR CA C 63.531 0.2 1 1050 264 239 THR N N 121.861 0.15 1 1051 265 240 GLY H H 8.693 0.02 1 1052 265 240 GLY C C 174.888 0.2 1 1053 265 240 GLY CA C 45.657 0.2 1 1054 265 240 GLY N N 114.092 0.15 1 1055 266 241 SER H H 8.363 0.02 1 1056 266 241 SER C C 175.966 0.2 1 1057 266 241 SER CA C 59.041 0.2 1 1058 266 241 SER N N 114.612 0.15 1 1059 267 242 GLN H H 8.842 0.02 1 1060 267 242 GLN C C 175.975 0.2 1 1061 267 242 GLN CA C 55.670 0.2 1 1062 267 242 GLN CB C 29.049 0.2 1 1063 267 242 GLN N N 123.398 0.15 1 1064 268 243 ALA H H 8.706 0.02 1 1065 268 243 ALA C C 178.738 0.2 1 1066 268 243 ALA CA C 52.263 0.2 1 1067 268 243 ALA CB C 20.455 0.2 1 1068 268 243 ALA N N 123.379 0.15 1 1069 269 244 THR H H 8.664 0.02 1 1070 269 244 THR C C 175.985 0.2 1 1071 269 244 THR CA C 61.682 0.2 1 1072 269 244 THR N N 112.867 0.15 1 1073 270 245 MET H H 9.145 0.02 1 1074 270 245 MET C C 177.810 0.2 1 1075 270 245 MET CA C 58.116 0.2 1 1076 270 245 MET CB C 31.016 0.2 1 1077 270 245 MET N N 122.456 0.15 1 1078 271 246 ASP H H 8.463 0.02 1 1079 271 246 ASP C C 178.686 0.2 1 1080 271 246 ASP CA C 57.799 0.2 1 1081 271 246 ASP CB C 40.662 0.2 1 1082 271 246 ASP N N 116.644 0.15 1 1083 272 247 GLU H H 7.636 0.02 1 1084 272 247 GLU C C 179.359 0.2 1 1085 272 247 GLU CA C 58.980 0.2 1 1086 272 247 GLU CB C 30.074 0.2 1 1087 272 247 GLU N N 120.142 0.15 1 1088 273 248 ARG H H 8.126 0.02 1 1089 273 248 ARG C C 177.502 0.2 1 1090 273 248 ARG CA C 60.836 0.2 1 1091 273 248 ARG CB C 31.072 0.2 1 1092 273 248 ARG N N 118.723 0.15 1 1093 274 249 ASN H H 8.784 0.02 1 1094 274 249 ASN C C 176.593 0.2 1 1095 274 249 ASN CA C 55.300 0.2 1 1096 274 249 ASN CB C 37.237 0.2 1 1097 274 249 ASN N N 116.963 0.15 1 1098 275 250 ARG H H 8.035 0.02 1 1099 275 250 ARG C C 178.881 0.2 1 1100 275 250 ARG CA C 59.307 0.2 1 1101 275 250 ARG CB C 30.114 0.2 1 1102 275 250 ARG N N 118.652 0.15 1 1103 276 251 GLN H H 7.810 0.02 1 1104 276 251 GLN C C 178.503 0.2 1 1105 276 251 GLN CA C 58.375 0.2 1 1106 276 251 GLN CB C 27.599 0.2 1 1107 276 251 GLN N N 114.885 0.15 1 1108 277 252 ILE H H 7.432 0.02 1 1109 277 252 ILE C C 177.224 0.2 1 1110 277 252 ILE CA C 65.862 0.2 1 1111 277 252 ILE CB C 36.405 0.2 1 1112 277 252 ILE N N 117.588 0.15 1 1113 278 253 ALA H H 8.717 0.02 1 1114 278 253 ALA C C 180.446 0.2 1 1115 278 253 ALA CA C 56.090 0.2 1 1116 278 253 ALA CB C 17.934 0.2 1 1117 278 253 ALA N N 123.308 0.15 1 1118 279 254 GLU H H 8.445 0.02 1 1119 279 254 GLU C C 180.745 0.2 1 1120 279 254 GLU CA C 59.756 0.2 1 1121 279 254 GLU CB C 29.670 0.2 1 1122 279 254 GLU N N 118.235 0.15 1 1123 280 255 ILE H H 8.046 0.02 1 1124 280 255 ILE C C 177.990 0.2 1 1125 280 255 ILE CA C 66.670 0.2 1 1126 280 255 ILE N N 123.462 0.15 1 1127 281 256 GLY H H 8.373 0.02 1 1128 281 256 GLY C C 173.972 0.2 1 1129 281 256 GLY CA C 47.752 0.2 1 1130 281 256 GLY N N 106.031 0.15 1 1131 282 257 ALA H H 8.649 0.02 1 1132 282 257 ALA C C 180.196 0.2 1 1133 282 257 ALA CA C 55.191 0.2 1 1134 282 257 ALA CB C 17.842 0.2 1 1135 282 257 ALA N N 122.294 0.15 1 1136 283 258 SER H H 7.521 0.02 1 1137 283 258 SER C C 176.238 0.2 1 1138 283 258 SER CA C 61.855 0.2 1 1139 283 258 SER CB C 62.973 0.2 1 1140 283 258 SER N N 113.444 0.15 1 1141 284 259 LEU H H 8.226 0.02 1 1142 284 259 LEU C C 178.873 0.2 1 1143 284 259 LEU CA C 58.090 0.2 1 1144 284 259 LEU CB C 41.026 0.2 1 1145 284 259 LEU N N 122.884 0.15 1 1146 285 260 ILE H H 7.980 0.02 1 1147 285 260 ILE C C 178.496 0.2 1 1148 285 260 ILE CA C 63.796 0.2 1 1149 285 260 ILE CB C 37.416 0.2 1 1150 285 260 ILE N N 118.180 0.15 1 1151 286 261 LYS H H 8.132 0.02 1 1152 286 261 LYS C C 178.008 0.2 1 1153 286 261 LYS CA C 59.047 0.2 1 1154 286 261 LYS CB C 32.517 0.2 1 1155 286 261 LYS N N 121.208 0.15 1 1156 287 262 HIS H H 7.636 0.02 1 1157 287 262 HIS C C 173.745 0.2 1 1158 287 262 HIS CA C 55.035 0.2 1 1159 287 262 HIS CB C 28.103 0.2 1 1160 287 262 HIS N N 114.370 0.15 1 1161 288 263 TRP H H 7.271 0.02 1 1162 288 263 TRP N N 128.768 0.15 1 stop_ save_