data_6357 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone Resonance Assignments of Wild-Type TEM-1 Beta-lactamase from E. coli ; _BMRB_accession_number 6357 _BMRB_flat_file_name bmr6357.str _Entry_type original _Submission_date 2004-10-14 _Accession_date 2004-10-14 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; This backbone resonance assignments of Wild-Type TEM-1 Beta-lactamase follows the previous one of the mutant E28G. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Julien Olivier . . 2 Savard Pierre-Yves . . 3 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" 727 "15N chemical shifts" 248 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-07-20 update BMRB 'addition of relationship loop' 2004-11-01 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 6024 'TEM-1 beta-lactamase, mutant E28G' 7236 'TEM-1 beta-lactamase, mutant Y105W' 7237 'TEM-1 beta-lactamase, mutant Y105G' 7238 'TEM-1 beta-lactamase, mutant Y105N' 7239 'TEM-1 beta-lactamase, mutant Y105D' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone Resonance Assignments of Wild-Type TEM-1 Beta-lactamase from E. coli' _Citation_status published _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Julien Olivier . . 2 Savard Pierre-Yves . . 3 Gagne Stephane M. . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2004 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref1 _Saveframe_category citation _Citation_full ; 1H, 13C and 15N backbone resonance assignments for TEM-1, a 28.9 kDa beta-lactamase from E. coli. J Biomol NMR. 2004 Jul;29(3):433-4. ; _Citation_title '1H, 13C and 15N backbone resonance assignments for TEM-1, a 28.9 kDa beta-lactamase from E. coli.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15213455 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Savard Pierre-Yves Y. . 2 Sosa-Peinado Alejandro . . 3 Levesque 'Roger C' C. . 4 Makinen 'Marvin W' W. . 5 Gagne 'Stephane M' M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 29 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 433 _Page_last 434 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_TEM-1 _Saveframe_category molecular_system _Mol_system_name 'Beta-lactamase TEM' _Abbreviation_common TEM-1 _Enzyme_commission_number 3.5.2.6 loop_ _Mol_system_component_name _Mol_label TEM-1 $TEM-1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function Hydrolase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_TEM-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'TEM-1 beta-lactamase' _Abbreviation_common TEM-1 _Molecular_mass 28907 _Mol_thiol_state 'all disulfide bound' _Details ; The sequence numbering is sequential,from 26 to 288. This is not the same numbering scheme as in most publications that use a non-sequential numbering, where numbers 239 and 253 are not used in the coordinates. ; ############################## # Polymer residue sequence # ############################## _Residue_count 263 _Mol_residue_sequence ; HPETLVKVKDAEDQLGARVG YIELDLNSGKILESFRPEER FPMMSTFKVLLCGAVLSRVD AGQEQLGRRIHYSQNDLVEY 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 TYR 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 99.62 99.62 0.00e+00 BMRB 6024 "TEM-1 beta-lactamase" 100.00 263 99.62 99.62 0.00e+00 BMRB 7236 TEM-1_beta-lactamase 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 99.24 99.62 0.00e+00 PDB 1BT5 "Crystal Structure Of The Imipenem Inhibited Tem-1 Beta-Lactamase From Escherichia Coli" 100.00 263 99.24 99.62 0.00e+00 PDB 1BTL "Crystal Structure Of Escherichia Coli Tem1 Beta-Lactamase At 1.8 Angstroms Resolution" 100.00 263 99.24 99.62 0.00e+00 PDB 1CK3 "N276d Mutant Of Escherichia Coli Tem-1 Beta-Lactamase" 100.00 263 98.86 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 99.62 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-" 100.00 263 100.00 100.00 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" 100.00 263 100.00 100.00 0.00e+00 PDB 1ESU "S235a Mutant Of Tem1 Beta-Lactamase" 100.00 263 99.62 100.00 0.00e+00 PDB 1FQG "Molecular Structure Of The Acyl-Enzyme Intermediate In Tem- 1 Beta-Lactamase" 100.00 263 99.62 99.62 0.00e+00 PDB 1HTZ "Crystal Structure Of Tem52 Beta-Lactamase" 100.00 263 98.86 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 99.62 99.62 0.00e+00 PDB 1JTG "Crystal Structure Of Tem-1 Beta-lactamase / Beta-lactamase Inhibitor Protein Complex" 100.00 263 99.24 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 99.62 99.62 0.00e+00 PDB 1JWP "Structure Of M182t Mutant Of Tem-1 Beta-Lactamase" 100.00 263 99.62 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 99.62 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 98.86 99.24 0.00e+00 PDB 1LHY "Crystal Structure Of Tem-30 Beta-lactamase At 2.0 Angstrom" 100.00 263 99.62 99.62 0.00e+00 PDB 1LI0 "Crystal Structure Of Tem-32 Beta-Lactamase At 1.6 Angstrom" 100.00 263 99.24 99.62 0.00e+00 PDB 1LI9 "Crystal Structure Of Tem-34 Beta-lactamase At 1.5 Angstrom" 100.00 263 99.62 100.00 0.00e+00 PDB 1M40 "Ultra High Resolution Crystal Structure Of Tem-1" 100.00 263 99.62 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 99.62 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 99.62 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 99.62 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 99.62 99.62 0.00e+00 PDB 1PZO "Tem-1 Beta-lactamase In Complex With A Novel, Core- Disrupting, Allosteric Inhibitor" 100.00 263 99.62 99.62 0.00e+00 PDB 1PZP "Tem-1 Beta-Lactamase In Complex With A Novel, Core- Disrupting, Allosteric Inhibitor" 100.00 263 99.62 99.62 0.00e+00 PDB 1S0W "1b Lactamse B LACTAMASE INHIBITOR" 100.00 263 100.00 100.00 0.00e+00 PDB 1TEM "6 Alpha Hydroxymethyl Penicilloic Acid Acylated On The Tem- 1 Beta-Lactamase From Escherichia Coli" 100.00 263 99.24 99.62 0.00e+00 PDB 1XPB "Structure Of Beta-Lactamase Tem1" 100.00 263 100.00 100.00 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 99.62 99.62 0.00e+00 PDB 1ZG4 "Tem1 Beta Lactamase" 100.00 286 99.24 99.62 0.00e+00 PDB 1ZG6 "Tem1 Beta Lactamase Mutant S70g" 100.00 286 98.86 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 99.24 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 99.24 99.62 0.00e+00 PDB 3CMZ "Tem-1 Class-A Beta-Lactamase L201p Mutant Apo Structure" 100.00 263 99.62 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 99.62 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 99.62 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 98.48 99.24 0.00e+00 PDB 4GKU "Crystal Structure Of Beta Lactamase In Pet-15b" 100.00 263 100.00 100.00 0.00e+00 PDB 4IBX "Crystal Structure Of Stabilized Tem-1 Beta-lactamase Variant V.13" 100.00 263 97.34 97.34 0.00e+00 PDB 4MEZ "Crystal Structure Of M68l/m69t Double Mutant Tem-1" 100.00 263 99.24 99.62 0.00e+00 DBJ BAA00795 "ampicillin resistance protein [Shuttle vector pHY320PLK]" 100.00 286 100.00 100.00 0.00e+00 DBJ BAA03488 "beta-lactamase [Cloning vector pKF2]" 100.00 286 99.24 99.62 0.00e+00 DBJ BAA12825 "beta-lactamase [Cloning vector pBEN66]" 100.00 286 99.24 99.62 0.00e+00 DBJ BAA14388 "Ap resistance protein [synthetic construct]" 100.00 286 100.00 100.00 0.00e+00 DBJ BAA19239 "beta-lactamase [Cloning vector pBEN77]" 100.00 286 99.24 99.62 0.00e+00 EMBL CAA04868 "beta-lactamase [Escherichia coli]" 100.00 286 99.24 99.62 0.00e+00 EMBL CAA05682 "beta-lactamase [synthetic construct]" 100.00 286 99.24 99.62 0.00e+00 EMBL CAA05685 "beta-lactamase [synthetic construct]" 100.00 286 99.24 99.62 0.00e+00 EMBL CAA05686 "beta-lactamase [synthetic construct]" 100.00 286 99.24 99.62 0.00e+00 EMBL CAA05689 "beta-lactamase [synthetic construct]" 100.00 286 99.24 99.62 0.00e+00 GB AAA24057 "beta-lactamase [Escherichia coli]" 100.00 286 99.24 99.62 0.00e+00 GB AAA25053 "TEM-26B beta-lactamase [Klebsiella oxytoca]" 100.00 286 99.62 99.62 0.00e+00 GB AAA32208 "ampicillinase, partial [Enterobacteria phage f1]" 76.81 225 100.00 100.00 4.71e-144 GB AAA53119 "beta-lactamase [unidentified cloning vector]" 100.00 286 99.24 99.62 0.00e+00 GB AAA53121 "beta-lactamase [unidentified cloning vector]" 100.00 286 99.24 99.62 0.00e+00 PIR S60310 "extended spectrum beta-lactamase CAZ-2 - Klebsiella pneumoniae" 100.00 286 98.48 99.24 0.00e+00 PIR S60312 "extended spectrum beta-lactamase CAZ-7 - Klebsiella pneumoniae" 100.00 286 98.86 99.62 0.00e+00 PIR T51301 "beta-lactamase (EC 3.5.2.6) - fission yeast (Schizosaccharomyces pombe)" 100.00 286 99.24 99.62 0.00e+00 PRF 2018199A "beta lactamase IRT-4" 100.00 286 100.00 100.00 0.00e+00 REF NP_052173 "beta-lactamase [Neisseria gonorrhoeae]" 100.00 286 100.00 100.00 0.00e+00 REF NP_569411 "beta-lactamase [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 286 100.00 100.00 0.00e+00 REF NP_608310 "TEM beta-lactamase [Klebsiella pneumoniae]" 100.00 286 100.00 100.00 0.00e+00 REF NP_758767 "beta lactamase [Erwinia amylovora ATCC BAA-2158]" 98.48 283 98.07 98.07 0.00e+00 REF NP_775035 "BlaTEM1 [Citrobacter freundii]" 100.00 286 100.00 100.00 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" 100.00 286 100.00 100.00 0.00e+00 SP P62594 "RecName: Full=Beta-lactamase TEM; AltName: Full=Penicillinase; Flags: Precursor [Salmonella enterica subsp. enterica serovar Ty" 100.00 286 100.00 100.00 0.00e+00 SP Q48406 "RecName: Full=Beta-lactamase TEM-12; Flags: Precursor [Klebsiella oxytoca]" 100.00 286 99.62 99.62 0.00e+00 TPE CAJ85677 "TPA: beta lactamase [Birmingham IncP-alpha plasmid]" 100.00 286 99.62 100.00 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 _Fraction _Plasmid _Gene_mnemonic $TEM-1 'E. coli' 562 Eubacteria . Escherichia coli periplasm PBR322 bla stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $TEM-1 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pet24 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TEM-1 1.0 mM '[U-97.5% 13C; U-97.5% 15N]' 'sodium phosphate' 25 mM . Imidazole 4.0 mM . DSS 0.1 mM . 'sodium azide' 0.1 % . D2O 10 % . H2O 90 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TEM-1 1.0 mM '[U-97.5% 15N]' 'sodium phosphate' 25 mM . Imidazole 4.0 mM . DSS 0.1 mM . 'sodium azide' 0.1 % . D2O 10 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_Vnmr _Saveframe_category software _Name Vnmr _Version 6.1c loop_ _Task 'Acquisition of NMR experiments' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.2 loop_ _Task 'Processing of NMR spectra' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.2.2 loop_ _Task 'Sequential assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_Chemical_shifts_were_corrected_for_the_TROSY_experiment_by_adding_46.1Hz_to_the_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Chemical shifts were corrected for the TROSY experiment by adding 46.1Hz to the' _Sample_label . save_ save_1H_shifts_and_removing_46.1Hz_to_the_15N_shifts._2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H shifts and removing 46.1Hz to the 15N shifts.' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 0.02 na temperature 303 0.1 K 'ionic strength' 0.05 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; Chemical shifts were corrected for the TROSY experiment by adding 46.1Hz to the 1H shifts and removing 46.1Hz to the 15N shifts. ; loop_ _Experiment_label 'Chemical shifts were corrected for the TROSY experiment by adding 46.1Hz to the' '1H shifts and removing 46.1Hz to the 15N shifts.' stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name TEM-1 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 PRO CA C 65.520 0.2 1 2 . 2 PRO CB C 32.376 0.2 1 3 . 2 PRO C C 179.360 0.2 1 4 . 3 GLU N N 121.860 0.2 1 5 . 3 GLU H H 11.070 0.01 1 6 . 3 GLU CA C 59.711 0.2 1 7 . 3 GLU CB C 28.656 0.2 1 8 . 3 GLU C C 179.554 0.2 1 9 . 4 THR N N 119.042 0.2 1 10 . 4 THR H H 7.800 0.01 1 11 . 4 THR CA C 65.108 0.2 1 12 . 4 THR CB C 67.677 0.2 1 13 . 4 THR C C 176.056 0.2 1 14 . 5 LEU N N 120.333 0.2 1 15 . 5 LEU H H 7.044 0.01 1 16 . 5 LEU CA C 57.552 0.2 1 17 . 5 LEU CB C 40.847 0.2 1 18 . 5 LEU C C 179.016 0.2 1 19 . 6 VAL N N 119.907 0.2 1 20 . 6 VAL H H 7.509 0.01 1 21 . 6 VAL CA C 66.815 0.2 1 22 . 6 VAL CB C 31.256 0.2 1 23 . 6 VAL C C 178.416 0.2 1 24 . 7 LYS N N 119.576 0.2 1 25 . 7 LYS H H 7.297 0.01 1 26 . 7 LYS CA C 57.257 0.2 1 27 . 7 LYS CB C 30.325 0.2 1 28 . 7 LYS C C 178.385 0.2 1 29 . 8 VAL N N 123.065 0.2 1 30 . 8 VAL H H 8.317 0.01 1 31 . 8 VAL CA C 67.138 0.2 1 32 . 8 VAL CB C 31.049 0.2 1 33 . 8 VAL C C 176.772 0.2 1 34 . 9 LYS N N 118.700 0.2 1 35 . 9 LYS H H 7.701 0.01 1 36 . 9 LYS CA C 59.971 0.2 1 37 . 9 LYS CB C 31.909 0.2 1 38 . 9 LYS C C 179.309 0.2 1 39 . 10 ASP N N 120.620 0.2 1 40 . 10 ASP H H 8.334 0.01 1 41 . 10 ASP CA C 57.511 0.2 1 42 . 10 ASP CB C 41.932 0.2 1 43 . 10 ASP C C 178.127 0.2 1 44 . 11 ALA N N 122.342 0.2 1 45 . 11 ALA H H 8.529 0.01 1 46 . 11 ALA CA C 55.512 0.2 1 47 . 11 ALA CB C 18.322 0.2 1 48 . 11 ALA C C 179.571 0.2 1 49 . 12 GLU N N 117.822 0.2 1 50 . 12 GLU H H 7.960 0.01 1 51 . 12 GLU CA C 61.104 0.2 1 52 . 12 GLU CB C 29.255 0.2 1 53 . 12 GLU C C 180.467 0.2 1 54 . 13 ASP N N 120.089 0.2 1 55 . 13 ASP H H 7.934 0.01 1 56 . 13 ASP CA C 57.341 0.2 1 57 . 13 ASP CB C 40.910 0.2 1 58 . 13 ASP C C 179.149 0.2 1 59 . 14 GLN N N 118.632 0.2 1 60 . 14 GLN H H 8.873 0.01 1 61 . 14 GLN CA C 58.631 0.2 1 62 . 14 GLN CB C 28.588 0.2 1 63 . 14 GLN C C 179.168 0.2 1 64 . 15 LEU N N 114.476 0.2 1 65 . 15 LEU H H 8.750 0.01 1 66 . 15 LEU CA C 54.960 0.2 1 67 . 15 LEU CB C 42.792 0.2 1 68 . 15 LEU C C 178.973 0.2 1 69 . 16 GLY N N 113.119 0.2 1 70 . 16 GLY H H 8.103 0.01 1 71 . 16 GLY CA C 47.395 0.2 1 72 . 16 GLY C C 174.002 0.2 1 73 . 17 ALA N N 119.694 0.2 1 74 . 17 ALA H H 7.749 0.01 1 75 . 17 ALA CA C 50.954 0.2 1 76 . 17 ALA CB C 24.111 0.2 1 77 . 17 ALA C C 174.858 0.2 1 78 . 18 ARG N N 115.571 0.2 1 79 . 18 ARG H H 7.640 0.01 1 80 . 18 ARG CA C 55.899 0.2 1 81 . 18 ARG CB C 33.335 0.2 1 82 . 18 ARG C C 177.711 0.2 1 83 . 19 VAL N N 128.576 0.2 1 84 . 19 VAL H H 10.663 0.01 1 85 . 19 VAL CA C 61.416 0.2 1 86 . 19 VAL CB C 34.188 0.2 1 87 . 19 VAL C C 172.685 0.2 1 88 . 20 GLY N N 111.392 0.2 1 89 . 20 GLY H H 8.889 0.01 1 90 . 20 GLY CA C 44.049 0.2 1 91 . 20 GLY C C 172.483 0.2 1 92 . 21 TYR N N 124.210 0.2 1 93 . 21 TYR H H 9.429 0.01 1 94 . 21 TYR CA C 57.090 0.2 1 95 . 21 TYR CB C 45.207 0.2 1 96 . 21 TYR C C 174.030 0.2 1 97 . 22 ILE N N 125.578 0.2 1 98 . 22 ILE H H 8.049 0.01 1 99 . 22 ILE CA C 59.384 0.2 1 100 . 22 ILE CB C 41.962 0.2 1 101 . 22 ILE C C 171.466 0.2 1 102 . 23 GLU N N 123.602 0.2 1 103 . 23 GLU H H 7.821 0.01 1 104 . 23 GLU CA C 54.464 0.2 1 105 . 23 GLU CB C 34.640 0.2 1 106 . 23 GLU C C 175.004 0.2 1 107 . 24 LEU N N 126.956 0.2 1 108 . 24 LEU H H 9.705 0.01 1 109 . 24 LEU CA C 53.345 0.2 1 110 . 24 LEU CB C 47.189 0.2 1 111 . 24 LEU C C 175.622 0.2 1 112 . 25 ASP N N 126.780 0.2 1 113 . 25 ASP H H 9.058 0.01 1 114 . 25 ASP CA C 55.645 0.2 1 115 . 25 ASP CB C 43.160 0.2 1 116 . 25 ASP C C 176.783 0.2 1 117 . 26 LEU N N 129.015 0.2 1 118 . 26 LEU H H 8.244 0.01 1 119 . 26 LEU CA C 58.790 0.2 1 120 . 26 LEU CB C 43.222 0.2 1 121 . 26 LEU C C 177.563 0.2 1 122 . 27 ASN N N 116.717 0.2 1 123 . 27 ASN H H 8.695 0.01 1 124 . 27 ASN CA C 56.420 0.2 1 125 . 27 ASN CB C 38.778 0.2 1 126 . 27 ASN C C 176.977 0.2 1 127 . 28 SER N N 112.986 0.2 1 128 . 28 SER H H 8.566 0.01 1 129 . 28 SER CA C 59.100 0.2 1 130 . 28 SER CB C 65.800 0.2 1 131 . 28 SER C C 176.503 0.2 1 132 . 29 GLY N N 112.350 0.2 1 133 . 29 GLY H H 8.001 0.01 1 134 . 29 GLY CA C 45.709 0.2 1 135 . 29 GLY C C 172.352 0.2 1 136 . 30 LYS N N 119.520 0.2 1 137 . 30 LYS H H 7.689 0.01 1 138 . 30 LYS CA C 56.665 0.2 1 139 . 30 LYS CB C 33.708 0.2 1 140 . 30 LYS C C 176.113 0.2 1 141 . 31 ILE N N 125.021 0.2 1 142 . 31 ILE H H 8.676 0.01 1 143 . 31 ILE CA C 62.660 0.2 1 144 . 31 ILE CB C 37.737 0.2 1 145 . 31 ILE C C 176.122 0.2 1 146 . 32 LEU N N 130.506 0.2 1 147 . 32 LEU H H 8.943 0.01 1 148 . 32 LEU CA C 55.905 0.2 1 149 . 32 LEU CB C 42.216 0.2 1 150 . 32 LEU C C 177.054 0.2 1 151 . 33 GLU N N 116.026 0.2 1 152 . 33 GLU H H 7.550 0.01 1 153 . 33 GLU CA C 55.108 0.2 1 154 . 33 GLU CB C 34.233 0.2 1 155 . 33 GLU C C 174.635 0.2 1 156 . 34 SER N N 115.669 0.2 1 157 . 34 SER H H 9.010 0.01 1 158 . 34 SER CA C 58.050 0.2 1 159 . 34 SER CB C 67.230 0.2 1 160 . 34 SER C C 171.997 0.2 1 161 . 35 PHE N N 122.514 0.2 1 162 . 35 PHE H H 9.553 0.01 1 163 . 35 PHE CA C 59.973 0.2 1 164 . 35 PHE CB C 43.873 0.2 1 165 . 35 PHE C C 173.281 0.2 1 166 . 36 ARG N N 121.911 0.2 1 167 . 36 ARG H H 8.767 0.01 1 168 . 36 ARG CA C 57.928 0.2 1 169 . 37 PRO CA C 65.284 0.2 1 170 . 37 PRO CB C 32.704 0.2 1 171 . 37 PRO C C 177.508 0.2 1 172 . 38 GLU N N 116.590 0.2 1 173 . 38 GLU H H 8.494 0.01 1 174 . 38 GLU CA C 55.037 0.2 1 175 . 38 GLU CB C 29.188 0.2 1 176 . 38 GLU C C 175.056 0.2 1 177 . 39 GLU N N 117.402 0.2 1 178 . 39 GLU H H 6.856 0.01 1 179 . 39 GLU CA C 55.081 0.2 1 180 . 39 GLU CB C 32.311 0.2 1 181 . 39 GLU C C 174.856 0.2 1 182 . 40 ARG N N 117.328 0.2 1 183 . 40 ARG H H 8.309 0.01 1 184 . 40 ARG CA C 55.980 0.2 1 185 . 40 ARG CB C 31.976 0.2 1 186 . 40 ARG C C 177.224 0.2 1 187 . 41 PHE N N 117.824 0.2 1 188 . 41 PHE H H 8.725 0.01 1 189 . 42 PRO CA C 62.751 0.2 1 190 . 42 PRO CB C 32.419 0.2 1 191 . 42 PRO C C 176.164 0.2 1 192 . 43 MET N N 119.285 0.2 1 193 . 43 MET H H 7.771 0.01 1 194 . 43 MET CA C 58.561 0.2 1 195 . 43 MET CB C 35.666 0.2 1 196 . 43 MET C C 179.775 0.2 1 197 . 44 MET N N 120.436 0.2 1 198 . 44 MET H H 10.523 0.01 1 199 . 44 MET CA C 56.498 0.2 1 200 . 45 SER C C 176.083 0.2 1 201 . 46 THR N N 112.165 0.2 1 202 . 46 THR H H 7.913 0.01 1 203 . 46 THR CA C 65.942 0.2 1 204 . 46 THR CB C 69.063 0.2 1 205 . 46 THR C C 175.260 0.2 1 206 . 47 PHE N N 116.989 0.2 1 207 . 47 PHE H H 7.728 0.01 1 208 . 47 PHE CA C 59.499 0.2 1 209 . 47 PHE CB C 39.428 0.2 1 210 . 47 PHE C C 176.560 0.2 1 211 . 48 LYS N N 122.341 0.2 1 212 . 48 LYS H H 7.430 0.01 1 213 . 48 LYS CA C 60.071 0.2 1 214 . 48 LYS CB C 31.925 0.2 1 215 . 48 LYS C C 177.367 0.2 1 216 . 49 VAL N N 115.686 0.2 1 217 . 49 VAL H H 6.614 0.01 1 218 . 49 VAL CA C 66.405 0.2 1 219 . 49 VAL CB C 32.726 0.2 1 220 . 49 VAL C C 175.972 0.2 1 221 . 50 LEU N N 117.863 0.2 1 222 . 50 LEU H H 6.647 0.01 1 223 . 50 LEU CA C 57.443 0.2 1 224 . 50 LEU CB C 40.690 0.2 1 225 . 50 LEU C C 178.033 0.2 1 226 . 51 LEU N N 116.882 0.2 1 227 . 51 LEU H H 8.016 0.01 1 228 . 51 LEU CA C 57.537 0.2 1 229 . 51 LEU CB C 42.550 0.2 1 230 . 51 LEU C C 177.204 0.2 1 231 . 52 CYS N N 113.915 0.2 1 232 . 52 CYS H H 7.457 0.01 1 233 . 52 CYS CA C 63.882 0.2 1 234 . 52 CYS CB C 44.972 0.2 1 235 . 52 CYS C C 175.623 0.2 1 236 . 53 GLY N N 111.103 0.2 1 237 . 53 GLY H H 8.373 0.01 1 238 . 53 GLY CA C 47.968 0.2 1 239 . 53 GLY C C 173.101 0.2 1 240 . 54 ALA N N 124.736 0.2 1 241 . 54 ALA H H 7.811 0.01 1 242 . 54 ALA CA C 55.173 0.2 1 243 . 54 ALA CB C 16.745 0.2 1 244 . 54 ALA C C 180.980 0.2 1 245 . 55 VAL N N 119.522 0.2 1 246 . 55 VAL H H 7.998 0.01 1 247 . 55 VAL CA C 66.782 0.2 1 248 . 55 VAL CB C 32.127 0.2 1 249 . 55 VAL C C 177.984 0.2 1 250 . 56 LEU N N 119.525 0.2 1 251 . 56 LEU H H 8.494 0.01 1 252 . 56 LEU CA C 57.998 0.2 1 253 . 56 LEU CB C 40.669 0.2 1 254 . 56 LEU C C 178.222 0.2 1 255 . 57 SER N N 115.830 0.2 1 256 . 57 SER H H 8.166 0.01 1 257 . 57 SER CA C 61.892 0.2 1 258 . 57 SER CB C 62.722 0.2 1 259 . 57 SER C C 177.980 0.2 1 260 . 58 ARG N N 122.065 0.2 1 261 . 58 ARG H H 7.495 0.01 1 262 . 58 ARG CA C 59.452 0.2 1 263 . 58 ARG CB C 30.351 0.2 1 264 . 58 ARG C C 179.385 0.2 1 265 . 59 VAL N N 124.460 0.2 1 266 . 59 VAL H H 8.302 0.01 1 267 . 59 VAL CA C 65.120 0.2 1 268 . 59 VAL CB C 31.036 0.2 1 269 . 59 VAL C C 180.835 0.2 1 270 . 60 ASP N N 123.534 0.2 1 271 . 60 ASP H H 9.087 0.01 1 272 . 60 ASP CA C 57.367 0.2 1 273 . 60 ASP CB C 40.923 0.2 1 274 . 60 ASP C C 177.757 0.2 1 275 . 61 ALA N N 118.685 0.2 1 276 . 61 ALA H H 7.515 0.01 1 277 . 61 ALA CA C 52.454 0.2 1 278 . 61 ALA CB C 19.495 0.2 1 279 . 61 ALA C C 177.895 0.2 1 280 . 62 GLY N N 107.742 0.2 1 281 . 62 GLY H H 8.209 0.01 1 282 . 62 GLY CA C 45.822 0.2 1 283 . 62 GLY C C 174.929 0.2 1 284 . 63 GLN N N 117.371 0.2 1 285 . 63 GLN H H 8.396 0.01 1 286 . 63 GLN CA C 55.758 0.2 1 287 . 63 GLN CB C 30.201 0.2 1 288 . 63 GLN C C 173.504 0.2 1 289 . 64 GLU N N 118.181 0.2 1 290 . 64 GLU H H 7.360 0.01 1 291 . 64 GLU CA C 53.031 0.2 1 292 . 64 GLU CB C 33.868 0.2 1 293 . 64 GLU C C 172.691 0.2 1 294 . 65 GLN N N 125.281 0.2 1 295 . 65 GLN H H 10.071 0.01 1 296 . 65 GLN CA C 54.983 0.2 1 297 . 65 GLN CB C 31.483 0.2 1 298 . 65 GLN C C 176.035 0.2 1 299 . 66 LEU N N 123.178 0.2 1 300 . 66 LEU H H 9.070 0.01 1 301 . 66 LEU CA C 57.798 0.2 1 302 . 66 LEU CB C 41.587 0.2 1 303 . 66 LEU C C 177.346 0.2 1 304 . 67 GLY N N 102.157 0.2 1 305 . 67 GLY H H 8.399 0.01 1 306 . 67 GLY CA C 44.560 0.2 1 307 . 67 GLY C C 173.858 0.2 1 308 . 68 ARG N N 122.619 0.2 1 309 . 68 ARG H H 7.350 0.01 1 310 . 68 ARG CA C 58.117 0.2 1 311 . 68 ARG CB C 31.911 0.2 1 312 . 68 ARG C C 174.736 0.2 1 313 . 69 ARG N N 127.415 0.2 1 314 . 69 ARG H H 8.546 0.01 1 315 . 69 ARG CA C 56.656 0.2 1 316 . 69 ARG CB C 31.660 0.2 1 317 . 69 ARG C C 174.523 0.2 1 318 . 70 ILE N N 130.439 0.2 1 319 . 70 ILE H H 9.117 0.01 1 320 . 70 ILE CA C 60.459 0.2 1 321 . 70 ILE CB C 39.113 0.2 1 322 . 70 ILE C C 174.525 0.2 1 323 . 71 HIS N N 124.770 0.2 1 324 . 71 HIS H H 8.480 0.01 1 325 . 71 HIS CA C 55.511 0.2 1 326 . 71 HIS CB C 30.989 0.2 1 327 . 71 HIS C C 174.131 0.2 1 328 . 72 TYR N N 121.090 0.2 1 329 . 72 TYR H H 8.505 0.01 1 330 . 72 TYR CA C 56.109 0.2 1 331 . 72 TYR CB C 38.720 0.2 1 332 . 72 TYR C C 173.038 0.2 1 333 . 73 SER N N 114.770 0.2 1 334 . 73 SER H H 9.451 0.01 1 335 . 73 SER CA C 57.100 0.2 1 336 . 73 SER CB C 67.395 0.2 1 337 . 73 SER C C 175.662 0.2 1 338 . 74 GLN N N 122.062 0.2 1 339 . 74 GLN H H 9.086 0.01 1 340 . 74 GLN CA C 59.172 0.2 1 341 . 74 GLN CB C 28.239 0.2 1 342 . 74 GLN C C 177.989 0.2 1 343 . 75 ASN N N 115.299 0.2 1 344 . 75 ASN H H 8.215 0.01 1 345 . 75 ASN CA C 55.151 0.2 1 346 . 75 ASN CB C 38.190 0.2 1 347 . 75 ASN C C 175.588 0.2 1 348 . 76 ASP N N 116.726 0.2 1 349 . 76 ASP H H 7.891 0.01 1 350 . 76 ASP CA C 55.832 0.2 1 351 . 76 ASP CB C 42.627 0.2 1 352 . 76 ASP C C 175.505 0.2 1 353 . 77 LEU N N 116.810 0.2 1 354 . 77 LEU H H 7.121 0.01 1 355 . 77 LEU CA C 55.432 0.2 1 356 . 77 LEU CB C 41.889 0.2 1 357 . 77 LEU C C 178.020 0.2 1 358 . 78 VAL N N 117.333 0.2 1 359 . 78 VAL H H 7.755 0.01 1 360 . 78 VAL CA C 58.974 0.2 1 361 . 78 VAL CB C 34.499 0.2 1 362 . 78 VAL C C 176.588 0.2 1 363 . 79 GLU N N 123.413 0.2 1 364 . 79 GLU H H 8.570 0.01 1 365 . 79 GLU CA C 58.010 0.2 1 366 . 79 GLU CB C 30.193 0.2 1 367 . 79 GLU C C 174.919 0.2 1 368 . 80 TYR N N 121.280 0.2 1 369 . 80 TYR H H 8.696 0.01 1 370 . 80 TYR CA C 60.540 0.2 1 371 . 80 TYR CB C 36.092 0.2 1 372 . 80 TYR C C 172.124 0.2 1 373 . 81 SER N N 119.925 0.2 1 374 . 81 SER H H 8.366 0.01 1 375 . 81 SER CA C 55.797 0.2 1 376 . 82 PRO CA C 64.207 0.2 1 377 . 82 PRO CB C 31.954 0.2 1 378 . 82 PRO C C 177.759 0.2 1 379 . 83 VAL N N 118.449 0.2 1 380 . 83 VAL H H 8.673 0.01 1 381 . 83 VAL CA C 64.526 0.2 1 382 . 83 VAL CB C 33.347 0.2 1 383 . 83 VAL C C 179.093 0.2 1 384 . 84 THR N N 113.704 0.2 1 385 . 84 THR H H 9.643 0.01 1 386 . 84 THR CA C 63.991 0.2 1 387 . 84 THR CB C 69.390 0.2 1 388 . 84 THR C C 181.956 0.2 1 389 . 85 GLU N N 120.042 0.2 1 390 . 85 GLU H H 8.192 0.01 1 391 . 85 GLU CA C 58.912 0.2 1 392 . 85 GLU CB C 28.545 0.2 1 393 . 85 GLU C C 176.435 0.2 1 394 . 86 LYS N N 116.396 0.2 1 395 . 86 LYS H H 7.444 0.01 1 396 . 86 LYS CA C 56.011 0.2 1 397 . 86 LYS CB C 32.617 0.2 1 398 . 86 LYS C C 177.256 0.2 1 399 . 87 HIS N N 116.378 0.2 1 400 . 87 HIS H H 7.138 0.01 1 401 . 87 HIS CA C 55.352 0.2 1 402 . 87 HIS CB C 28.688 0.2 1 403 . 87 HIS C C 174.524 0.2 1 404 . 88 LEU N N 120.367 0.2 1 405 . 88 LEU H H 7.864 0.01 1 406 . 88 LEU CA C 58.255 0.2 1 407 . 88 LEU CB C 42.053 0.2 1 408 . 88 LEU C C 179.136 0.2 1 409 . 89 THR N N 109.487 0.2 1 410 . 89 THR H H 8.316 0.01 1 411 . 89 THR CA C 64.397 0.2 1 412 . 89 THR CB C 68.859 0.2 1 413 . 89 THR C C 175.616 0.2 1 414 . 90 ASP N N 117.295 0.2 1 415 . 90 ASP H H 8.818 0.01 1 416 . 90 ASP CA C 54.068 0.2 1 417 . 90 ASP CB C 40.434 0.2 1 418 . 90 ASP C C 177.664 0.2 1 419 . 91 GLY N N 110.884 0.2 1 420 . 91 GLY H H 7.907 0.01 1 421 . 91 GLY CA C 45.100 0.2 1 422 . 91 GLY C C 171.626 0.2 1 423 . 92 MET N N 113.520 0.2 1 424 . 92 MET H H 8.301 0.01 1 425 . 92 MET CA C 55.068 0.2 1 426 . 92 MET CB C 40.407 0.2 1 427 . 92 MET C C 175.125 0.2 1 428 . 93 THR N N 112.303 0.2 1 429 . 93 THR H H 8.926 0.01 1 430 . 93 THR CA C 60.220 0.2 1 431 . 93 THR CB C 71.074 0.2 1 432 . 93 THR C C 175.850 0.2 1 433 . 94 VAL N N 122.139 0.2 1 434 . 94 VAL H H 8.117 0.01 1 435 . 94 VAL CA C 67.988 0.2 1 436 . 94 VAL CB C 31.692 0.2 1 437 . 94 VAL C C 177.959 0.2 1 438 . 95 ARG N N 118.446 0.2 1 439 . 95 ARG H H 9.079 0.01 1 440 . 95 ARG CA C 60.244 0.2 1 441 . 95 ARG CB C 31.271 0.2 1 442 . 95 ARG C C 177.550 0.2 1 443 . 96 GLU N N 118.628 0.2 1 444 . 96 GLU H H 7.632 0.01 1 445 . 96 GLU CA C 58.497 0.2 1 446 . 96 GLU CB C 30.062 0.2 1 447 . 96 GLU C C 180.572 0.2 1 448 . 97 LEU N N 122.985 0.2 1 449 . 97 LEU H H 9.112 0.01 1 450 . 97 LEU CA C 58.122 0.2 1 451 . 97 LEU CB C 41.031 0.2 1 452 . 97 LEU C C 179.070 0.2 1 453 . 98 CYS N N 119.150 0.2 1 454 . 98 CYS H H 8.163 0.01 1 455 . 98 CYS CA C 62.340 0.2 1 456 . 98 CYS CB C 42.470 0.2 1 457 . 98 CYS C C 176.013 0.2 1 458 . 99 SER N N 113.414 0.2 1 459 . 99 SER H H 7.734 0.01 1 460 . 99 SER CA C 61.441 0.2 1 461 . 99 SER CB C 62.553 0.2 1 462 . 99 SER C C 179.042 0.2 1 463 . 100 ALA N N 124.775 0.2 1 464 . 100 ALA H H 8.517 0.01 1 465 . 100 ALA CA C 55.685 0.2 1 466 . 100 ALA CB C 17.546 0.2 1 467 . 100 ALA C C 180.246 0.2 1 468 . 101 ALA N N 121.017 0.2 1 469 . 101 ALA H H 8.675 0.01 1 470 . 101 ALA CA C 55.273 0.2 1 471 . 101 ALA CB C 17.553 0.2 1 472 . 101 ALA C C 178.464 0.2 1 473 . 102 ILE N N 113.757 0.2 1 474 . 102 ILE H H 8.231 0.01 1 475 . 102 ILE CA C 65.050 0.2 1 476 . 102 ILE C C 176.482 0.2 1 477 . 103 THR N N 109.590 0.2 1 478 . 103 THR H H 8.966 0.01 1 479 . 103 THR CA C 65.249 0.2 1 480 . 103 THR CB C 70.367 0.2 1 481 . 103 THR C C 175.943 0.2 1 482 . 104 MET N N 114.331 0.2 1 483 . 104 MET H H 6.733 0.01 1 484 . 104 MET CA C 53.150 0.2 1 485 . 104 MET CB C 33.521 0.2 1 486 . 104 MET C C 176.202 0.2 1 487 . 105 SER N N 115.196 0.2 1 488 . 105 SER H H 7.142 0.01 1 489 . 105 SER CA C 59.201 0.2 1 490 . 105 SER CB C 63.929 0.2 1 491 . 105 SER C C 174.125 0.2 1 492 . 106 ASP N N 120.726 0.2 1 493 . 106 ASP H H 7.365 0.01 1 494 . 106 ASP CA C 56.190 0.2 1 495 . 106 ASP CB C 44.319 0.2 1 496 . 106 ASP C C 176.528 0.2 1 497 . 107 ASN N N 127.327 0.2 1 498 . 107 ASN H H 8.807 0.01 1 499 . 107 ASN CA C 56.339 0.2 1 500 . 107 ASN CB C 38.980 0.2 1 501 . 107 ASN C C 178.079 0.2 1 502 . 108 THR N N 120.167 0.2 1 503 . 108 THR H H 7.668 0.01 1 504 . 108 THR CA C 68.144 0.2 1 505 . 108 THR CB C 67.218 0.2 1 506 . 108 THR C C 176.580 0.2 1 507 . 109 ALA N N 122.744 0.2 1 508 . 109 ALA H H 8.953 0.01 1 509 . 109 ALA CA C 55.364 0.2 1 510 . 109 ALA CB C 18.721 0.2 1 511 . 109 ALA C C 178.415 0.2 1 512 . 110 ALA N N 115.349 0.2 1 513 . 110 ALA H H 7.098 0.01 1 514 . 110 ALA CA C 54.852 0.2 1 515 . 110 ALA CB C 19.468 0.2 1 516 . 110 ALA C C 178.177 0.2 1 517 . 111 ASN N N 119.800 0.2 1 518 . 111 ASN H H 7.922 0.01 1 519 . 111 ASN CA C 56.297 0.2 1 520 . 111 ASN CB C 37.250 0.2 1 521 . 111 ASN C C 178.697 0.2 1 522 . 112 LEU N N 121.585 0.2 1 523 . 112 LEU H H 9.071 0.01 1 524 . 112 LEU CA C 58.258 0.2 1 525 . 112 LEU CB C 41.982 0.2 1 526 . 112 LEU C C 181.158 0.2 1 527 . 113 LEU N N 119.492 0.2 1 528 . 113 LEU H H 8.127 0.01 1 529 . 113 LEU CA C 57.539 0.2 1 530 . 113 LEU CB C 42.812 0.2 1 531 . 113 LEU C C 180.734 0.2 1 532 . 114 LEU N N 124.258 0.2 1 533 . 114 LEU H H 9.174 0.01 1 534 . 114 LEU CA C 57.978 0.2 1 535 . 114 LEU CB C 43.769 0.2 1 536 . 114 LEU C C 180.097 0.2 1 537 . 115 THR N N 118.038 0.2 1 538 . 115 THR H H 8.709 0.01 1 539 . 115 THR CA C 67.986 0.2 1 540 . 115 THR CB C 68.614 0.2 1 541 . 115 THR C C 177.777 0.2 1 542 . 116 THR N N 112.754 0.2 1 543 . 116 THR H H 7.628 0.01 1 544 . 116 THR CA C 65.353 0.2 1 545 . 116 THR CB C 68.864 0.2 1 546 . 116 THR C C 175.726 0.2 1 547 . 117 ILE N N 110.944 0.2 1 548 . 117 ILE H H 6.892 0.01 1 549 . 117 ILE CA C 61.075 0.2 1 550 . 117 ILE CB C 38.780 0.2 1 551 . 117 ILE C C 175.426 0.2 1 552 . 118 GLY N N 106.532 0.2 1 553 . 118 GLY H H 7.484 0.01 1 554 . 118 GLY CA C 45.045 0.2 1 555 . 118 GLY C C 175.141 0.2 1 556 . 119 GLY N N 108.294 0.2 1 557 . 119 GLY H H 8.201 0.01 1 558 . 120 PRO CA C 66.312 0.2 1 559 . 120 PRO CB C 31.989 0.2 1 560 . 120 PRO C C 177.854 0.2 1 561 . 121 LYS N N 116.162 0.2 1 562 . 121 LYS H H 8.675 0.01 1 563 . 121 LYS CA C 59.526 0.2 1 564 . 121 LYS CB C 31.939 0.2 1 565 . 121 LYS C C 179.817 0.2 1 566 . 122 GLU N N 118.679 0.2 1 567 . 122 GLU H H 7.338 0.01 1 568 . 122 GLU CA C 57.155 0.2 1 569 . 122 GLU CB C 29.372 0.2 1 570 . 122 GLU C C 180.351 0.2 1 571 . 123 LEU N N 123.447 0.2 1 572 . 123 LEU H H 7.653 0.01 1 573 . 123 LEU CA C 57.571 0.2 1 574 . 123 LEU CB C 40.341 0.2 1 575 . 123 LEU C C 178.091 0.2 1 576 . 124 THR N N 117.166 0.2 1 577 . 124 THR H H 8.174 0.01 1 578 . 124 THR CA C 67.850 0.2 1 579 . 124 THR C C 175.062 0.2 1 580 . 125 ALA N N 123.323 0.2 1 581 . 125 ALA H H 7.898 0.01 1 582 . 125 ALA CA C 55.877 0.2 1 583 . 125 ALA CB C 18.061 0.2 1 584 . 125 ALA C C 179.476 0.2 1 585 . 126 PHE N N 120.570 0.2 1 586 . 126 PHE H H 7.793 0.01 1 587 . 126 PHE CA C 61.170 0.2 1 588 . 126 PHE CB C 38.256 0.2 1 589 . 126 PHE C C 177.702 0.2 1 590 . 127 LEU N N 121.703 0.2 1 591 . 127 LEU H H 8.055 0.01 1 592 . 127 LEU CA C 57.778 0.2 1 593 . 127 LEU CB C 39.940 0.2 1 594 . 127 LEU C C 179.045 0.2 1 595 . 128 HIS N N 120.867 0.2 1 596 . 128 HIS H H 8.905 0.01 1 597 . 128 HIS CA C 59.289 0.2 1 598 . 128 HIS CB C 28.928 0.2 1 599 . 128 HIS C C 179.793 0.2 1 600 . 129 ASN N N 118.327 0.2 1 601 . 129 ASN H H 8.390 0.01 1 602 . 129 ASN CA C 55.703 0.2 1 603 . 129 ASN CB C 38.202 0.2 1 604 . 129 ASN C C 176.469 0.2 1 605 . 130 MET N N 115.637 0.2 1 606 . 130 MET H H 7.501 0.01 1 607 . 130 MET CA C 55.449 0.2 1 608 . 130 MET CB C 32.020 0.2 1 609 . 130 MET C C 175.820 0.2 1 610 . 131 GLY N N 107.845 0.2 1 611 . 131 GLY H H 7.728 0.01 1 612 . 131 GLY CA C 45.274 0.2 1 613 . 131 GLY C C 172.691 0.2 1 614 . 132 ASP N N 121.767 0.2 1 615 . 132 ASP H H 8.005 0.01 1 616 . 132 ASP CA C 52.459 0.2 1 617 . 132 ASP CB C 39.856 0.2 1 618 . 132 ASP C C 174.720 0.2 1 619 . 133 HIS N N 121.332 0.2 1 620 . 133 HIS H H 8.337 0.01 1 621 . 133 HIS CA C 54.540 0.2 1 622 . 133 HIS CB C 29.428 0.2 1 623 . 133 HIS C C 174.990 0.2 1 624 . 134 VAL N N 121.396 0.2 1 625 . 134 VAL H H 8.805 0.01 1 626 . 134 VAL CA C 63.826 0.2 1 627 . 134 VAL CB C 34.850 0.2 1 628 . 134 VAL C C 176.010 0.2 1 629 . 135 THR N N 125.777 0.2 1 630 . 135 THR H H 9.373 0.01 1 631 . 135 THR CA C 64.830 0.2 1 632 . 135 THR CB C 66.931 0.2 1 633 . 135 THR C C 172.770 0.2 1 634 . 136 ARG N N 119.907 0.2 1 635 . 136 ARG H H 8.460 0.01 1 636 . 136 ARG CA C 54.210 0.2 1 637 . 136 ARG CB C 32.593 0.2 1 638 . 136 ARG C C 171.629 0.2 1 639 . 137 LEU N N 121.237 0.2 1 640 . 137 LEU H H 7.731 0.01 1 641 . 137 LEU CA C 53.334 0.2 1 642 . 137 LEU CB C 45.995 0.2 1 643 . 137 LEU C C 174.259 0.2 1 644 . 138 ASP N N 126.890 0.2 1 645 . 138 ASP H H 10.008 0.01 1 646 . 138 ASP CA C 55.489 0.2 1 647 . 138 ASP CB C 45.745 0.2 1 648 . 138 ASP C C 175.637 0.2 1 649 . 139 ARG N N 125.195 0.2 1 650 . 139 ARG H H 9.231 0.01 1 651 . 139 ARG CA C 55.376 0.2 1 652 . 139 ARG CB C 34.558 0.2 1 653 . 139 ARG C C 170.545 0.2 1 654 . 140 TRP N N 114.588 0.2 1 655 . 140 TRP H H 7.705 0.01 1 656 . 140 TRP CA C 55.174 0.2 1 657 . 140 TRP CB C 29.161 0.2 1 658 . 140 TRP C C 177.911 0.2 1 659 . 141 GLU N N 117.481 0.2 1 660 . 141 GLU H H 9.532 0.01 1 661 . 142 PRO CA C 63.863 0.2 1 662 . 142 PRO CB C 34.229 0.2 1 663 . 142 PRO C C 177.786 0.2 1 664 . 143 GLU N N 128.362 0.2 1 665 . 143 GLU H H 8.668 0.01 1 666 . 143 GLU CA C 60.891 0.2 1 667 . 143 GLU CB C 29.452 0.2 1 668 . 143 GLU C C 176.637 0.2 1 669 . 144 LEU N N 113.109 0.2 1 670 . 144 LEU H H 7.671 0.01 1 671 . 144 LEU CA C 57.314 0.2 1 672 . 144 LEU CB C 40.671 0.2 1 673 . 144 LEU C C 176.857 0.2 1 674 . 145 ASN N N 119.956 0.2 1 675 . 145 ASN H H 7.550 0.01 1 676 . 145 ASN CA C 54.037 0.2 1 677 . 145 ASN CB C 40.818 0.2 1 678 . 145 ASN C C 174.765 0.2 1 679 . 146 GLU N N 120.822 0.2 1 680 . 146 GLU H H 7.463 0.01 1 681 . 146 GLU CA C 60.824 0.2 1 682 . 146 GLU CB C 30.920 0.2 1 683 . 146 GLU C C 175.723 0.2 1 684 . 147 ALA N N 118.355 0.2 1 685 . 147 ALA H H 9.509 0.01 1 686 . 147 ALA CA C 52.160 0.2 1 687 . 147 ALA CB C 18.070 0.2 1 688 . 147 ALA C C 176.476 0.2 1 689 . 148 ILE N N 120.878 0.2 1 690 . 148 ILE H H 8.660 0.01 1 691 . 148 ILE CA C 60.250 0.2 1 692 . 149 PRO CA C 64.275 0.2 1 693 . 149 PRO CB C 31.551 0.2 1 694 . 149 PRO C C 177.498 0.2 1 695 . 150 ASN N N 116.053 0.2 1 696 . 150 ASN H H 8.908 0.01 1 697 . 150 ASN CA C 55.369 0.2 1 698 . 150 ASN CB C 37.501 0.2 1 699 . 150 ASN C C 173.229 0.2 1 700 . 151 ASP N N 120.911 0.2 1 701 . 151 ASP H H 7.599 0.01 1 702 . 151 ASP CA C 53.449 0.2 1 703 . 151 ASP CB C 42.066 0.2 1 704 . 151 ASP C C 177.313 0.2 1 705 . 152 GLU N N 126.549 0.2 1 706 . 152 GLU H H 8.990 0.01 1 707 . 152 GLU CA C 56.994 0.2 1 708 . 152 GLU CB C 29.845 0.2 1 709 . 152 GLU C C 177.603 0.2 1 710 . 153 ARG N N 122.428 0.2 1 711 . 153 ARG H H 8.103 0.01 1 712 . 153 ARG CA C 57.372 0.2 1 713 . 153 ARG CB C 30.785 0.2 1 714 . 153 ARG C C 177.153 0.2 1 715 . 154 ASP N N 115.693 0.2 1 716 . 154 ASP H H 8.777 0.01 1 717 . 154 ASP CA C 55.982 0.2 1 718 . 154 ASP CB C 42.409 0.2 1 719 . 154 ASP C C 177.909 0.2 1 720 . 155 THR N N 104.920 0.2 1 721 . 155 THR H H 7.275 0.01 1 722 . 155 THR CA C 59.777 0.2 1 723 . 155 THR CB C 75.098 0.2 1 724 . 155 THR C C 173.092 0.2 1 725 . 156 THR N N 111.812 0.2 1 726 . 156 THR H H 8.216 0.01 1 727 . 156 THR CA C 59.765 0.2 1 728 . 156 THR CB C 69.066 0.2 1 729 . 156 THR C C 173.561 0.2 1 730 . 157 MET N N 117.972 0.2 1 731 . 157 MET H H 8.513 0.01 1 732 . 157 MET CA C 53.310 0.2 1 733 . 158 PRO CA C 67.568 0.2 1 734 . 158 PRO CB C 32.565 0.2 1 735 . 158 PRO C C 176.865 0.2 1 736 . 159 ALA N N 114.855 0.2 1 737 . 159 ALA H H 8.672 0.01 1 738 . 159 ALA CA C 56.284 0.2 1 739 . 159 ALA CB C 18.517 0.2 1 740 . 159 ALA C C 179.051 0.2 1 741 . 160 ALA N N 121.213 0.2 1 742 . 160 ALA H H 6.859 0.01 1 743 . 160 ALA CA C 54.892 0.2 1 744 . 160 ALA CB C 18.984 0.2 1 745 . 160 ALA C C 177.965 0.2 1 746 . 161 MET N N 116.178 0.2 1 747 . 161 MET H H 8.331 0.01 1 748 . 161 MET CA C 57.394 0.2 1 749 . 161 MET CB C 31.309 0.2 1 750 . 161 MET C C 177.862 0.2 1 751 . 162 ALA N N 117.937 0.2 1 752 . 162 ALA H H 8.281 0.01 1 753 . 162 ALA CA C 55.890 0.2 1 754 . 162 ALA CB C 19.336 0.2 1 755 . 162 ALA C C 178.416 0.2 1 756 . 163 THR N N 112.405 0.2 1 757 . 163 THR H H 7.705 0.01 1 758 . 163 THR CA C 66.421 0.2 1 759 . 163 THR CB C 68.878 0.2 1 760 . 163 THR C C 177.373 0.2 1 761 . 164 THR N N 124.712 0.2 1 762 . 164 THR H H 9.058 0.01 1 763 . 164 THR CA C 67.273 0.2 1 764 . 164 THR CB C 67.892 0.2 1 765 . 164 THR C C 175.737 0.2 1 766 . 165 LEU N N 121.426 0.2 1 767 . 165 LEU H H 8.853 0.01 1 768 . 165 LEU CA C 58.178 0.2 1 769 . 165 LEU CB C 41.637 0.2 1 770 . 165 LEU C C 178.214 0.2 1 771 . 166 ARG N N 118.455 0.2 1 772 . 166 ARG H H 8.127 0.01 1 773 . 166 ARG CA C 60.928 0.2 1 774 . 166 ARG CB C 28.945 0.2 1 775 . 166 ARG C C 178.708 0.2 1 776 . 167 LYS N N 121.028 0.2 1 777 . 167 LYS H H 8.094 0.01 1 778 . 167 LYS CA C 60.167 0.2 1 779 . 167 LYS CB C 32.828 0.2 1 780 . 167 LYS C C 178.599 0.2 1 781 . 168 LEU N N 117.504 0.2 1 782 . 168 LEU H H 8.049 0.01 1 783 . 168 LEU CA C 57.999 0.2 1 784 . 168 LEU CB C 42.875 0.2 1 785 . 168 LEU C C 177.441 0.2 1 786 . 169 LEU N N 111.534 0.2 1 787 . 169 LEU H H 8.042 0.01 1 788 . 169 LEU CA C 56.756 0.2 1 789 . 169 LEU CB C 43.119 0.2 1 790 . 169 LEU C C 178.282 0.2 1 791 . 170 THR N N 105.453 0.2 1 792 . 170 THR H H 7.969 0.01 1 793 . 170 THR CA C 61.015 0.2 1 794 . 170 THR CB C 72.210 0.2 1 795 . 170 THR C C 174.638 0.2 1 796 . 171 GLY N N 110.564 0.2 1 797 . 171 GLY H H 7.901 0.01 1 798 . 171 GLY CA C 45.051 0.2 1 799 . 171 GLY C C 174.014 0.2 1 800 . 172 GLU N N 116.800 0.2 1 801 . 172 GLU H H 8.392 0.01 1 802 . 172 GLU CA C 56.079 0.2 1 803 . 172 GLU CB C 29.620 0.2 1 804 . 172 GLU C C 176.409 0.2 1 805 . 173 LEU N N 122.783 0.2 1 806 . 173 LEU H H 7.475 0.01 1 807 . 173 LEU CA C 58.270 0.2 1 808 . 173 LEU CB C 42.775 0.2 1 809 . 173 LEU C C 177.394 0.2 1 810 . 174 LEU N N 118.297 0.2 1 811 . 174 LEU H H 8.697 0.01 1 812 . 174 LEU CA C 52.808 0.2 1 813 . 174 LEU CB C 44.332 0.2 1 814 . 174 LEU C C 177.569 0.2 1 815 . 175 THR N N 112.642 0.2 1 816 . 175 THR H H 8.964 0.01 1 817 . 175 THR CA C 62.169 0.2 1 818 . 175 THR CB C 71.603 0.2 1 819 . 175 THR C C 175.365 0.2 1 820 . 176 LEU N N 123.086 0.2 1 821 . 176 LEU H H 8.699 0.01 1 822 . 176 LEU CA C 58.971 0.2 1 823 . 176 LEU CB C 41.646 0.2 1 824 . 176 LEU C C 179.074 0.2 1 825 . 177 ALA N N 118.771 0.2 1 826 . 177 ALA H H 8.453 0.01 1 827 . 177 ALA CA C 55.091 0.2 1 828 . 177 ALA CB C 18.171 0.2 1 829 . 177 ALA C C 181.483 0.2 1 830 . 178 SER N N 118.640 0.2 1 831 . 178 SER H H 7.748 0.01 1 832 . 178 SER CA C 62.875 0.2 1 833 . 178 SER CB C 64.788 0.2 1 834 . 178 SER C C 175.065 0.2 1 835 . 179 ARG N N 123.777 0.2 1 836 . 179 ARG H H 9.072 0.01 1 837 . 179 ARG CA C 60.471 0.2 1 838 . 179 ARG CB C 31.106 0.2 1 839 . 179 ARG C C 178.519 0.2 1 840 . 180 GLN N N 117.749 0.2 1 841 . 180 GLN H H 8.226 0.01 1 842 . 180 GLN CA C 57.696 0.2 1 843 . 180 GLN CB C 28.404 0.2 1 844 . 180 GLN C C 177.109 0.2 1 845 . 181 GLN N N 118.220 0.2 1 846 . 181 GLN H H 7.602 0.01 1 847 . 181 GLN CA C 57.092 0.2 1 848 . 181 GLN CB C 28.630 0.2 1 849 . 181 GLN C C 177.862 0.2 1 850 . 182 LEU N N 121.240 0.2 1 851 . 182 LEU H H 7.985 0.01 1 852 . 182 LEU CA C 58.300 0.2 1 853 . 182 LEU CB C 41.711 0.2 1 854 . 182 LEU C C 178.265 0.2 1 855 . 183 ILE N N 118.270 0.2 1 856 . 183 ILE H H 7.812 0.01 1 857 . 183 ILE CA C 65.566 0.2 1 858 . 183 ILE CB C 38.249 0.2 1 859 . 183 ILE C C 177.262 0.2 1 860 . 184 ASP N N 122.512 0.2 1 861 . 184 ASP H H 8.689 0.01 1 862 . 184 ASP CA C 57.710 0.2 1 863 . 184 ASP CB C 39.950 0.2 1 864 . 184 ASP C C 181.415 0.2 1 865 . 185 TRP N N 120.526 0.2 1 866 . 185 TRP H H 8.034 0.01 1 867 . 185 TRP CA C 59.866 0.2 1 868 . 185 TRP CB C 28.867 0.2 1 869 . 185 TRP C C 177.112 0.2 1 870 . 186 MET N N 116.102 0.2 1 871 . 186 MET H H 7.733 0.01 1 872 . 186 MET CA C 59.494 0.2 1 873 . 186 MET C C 180.252 0.2 1 874 . 187 GLU N N 124.846 0.2 1 875 . 187 GLU H H 9.647 0.01 1 876 . 187 GLU CA C 59.774 0.2 1 877 . 187 GLU CB C 29.888 0.2 1 878 . 187 GLU C C 178.125 0.2 1 879 . 188 ALA N N 119.728 0.2 1 880 . 188 ALA H H 7.332 0.01 1 881 . 188 ALA CA C 51.935 0.2 1 882 . 188 ALA CB C 19.067 0.2 1 883 . 188 ALA C C 175.495 0.2 1 884 . 189 ASP N N 115.894 0.2 1 885 . 189 ASP H H 6.983 0.01 1 886 . 189 ASP CA C 55.067 0.2 1 887 . 189 ASP CB C 39.226 0.2 1 888 . 189 ASP C C 177.410 0.2 1 889 . 190 LYS N N 127.440 0.2 1 890 . 190 LYS H H 9.491 0.01 1 891 . 190 LYS CA C 56.479 0.2 1 892 . 190 LYS CB C 35.131 0.2 1 893 . 190 LYS C C 179.571 0.2 1 894 . 191 VAL N N 110.491 0.2 1 895 . 191 VAL H H 7.223 0.01 1 896 . 191 VAL CA C 60.717 0.2 1 897 . 191 VAL CB C 31.620 0.2 1 898 . 191 VAL C C 175.044 0.2 1 899 . 192 ALA N N 125.596 0.2 1 900 . 192 ALA H H 8.927 0.01 1 901 . 192 ALA CA C 50.614 0.2 1 902 . 192 ALA CB C 20.753 0.2 1 903 . 192 ALA C C 178.313 0.2 1 904 . 193 GLY N N 114.393 0.2 1 905 . 193 GLY H H 8.937 0.01 1 906 . 194 PRO CA C 64.010 0.2 1 907 . 194 PRO CB C 32.608 0.2 1 908 . 194 PRO C C 175.150 0.2 1 909 . 195 LEU N N 114.135 0.2 1 910 . 195 LEU H H 6.804 0.01 1 911 . 195 LEU CA C 52.002 0.2 1 912 . 195 LEU CB C 39.888 0.2 1 913 . 195 LEU C C 176.368 0.2 1 914 . 196 LEU N N 123.561 0.2 1 915 . 196 LEU H H 6.898 0.01 1 916 . 196 LEU CA C 58.121 0.2 1 917 . 196 LEU CB C 42.272 0.2 1 918 . 196 LEU C C 178.523 0.2 1 919 . 197 ARG N N 116.113 0.2 1 920 . 197 ARG H H 8.944 0.01 1 921 . 197 ARG CA C 59.919 0.2 1 922 . 197 ARG CB C 30.038 0.2 1 923 . 197 ARG C C 177.446 0.2 1 924 . 198 SER N N 113.506 0.2 1 925 . 198 SER H H 7.012 0.01 1 926 . 198 SER CA C 61.076 0.2 1 927 . 198 SER CB C 63.335 0.2 1 928 . 198 SER C C 174.020 0.2 1 929 . 199 ALA N N 122.972 0.2 1 930 . 199 ALA H H 7.271 0.01 1 931 . 199 ALA CA C 50.822 0.2 1 932 . 199 ALA CB C 19.574 0.2 1 933 . 199 ALA C C 176.273 0.2 1 934 . 200 LEU N N 121.036 0.2 1 935 . 200 LEU H H 6.705 0.01 1 936 . 200 LEU CA C 53.233 0.2 1 937 . 201 PRO CA C 61.558 0.2 1 938 . 201 PRO CB C 32.059 0.2 1 939 . 201 PRO C C 175.783 0.2 1 940 . 202 ALA N N 122.887 0.2 1 941 . 202 ALA H H 8.242 0.01 1 942 . 202 ALA CA C 53.574 0.2 1 943 . 202 ALA CB C 18.288 0.2 1 944 . 202 ALA C C 179.420 0.2 1 945 . 203 GLY N N 110.228 0.2 1 946 . 203 GLY H H 8.827 0.01 1 947 . 203 GLY CA C 45.434 0.2 1 948 . 203 GLY C C 175.340 0.2 1 949 . 204 TRP N N 120.696 0.2 1 950 . 204 TRP H H 7.622 0.01 1 951 . 204 TRP CA C 59.148 0.2 1 952 . 204 TRP CB C 28.846 0.2 1 953 . 204 TRP C C 175.366 0.2 1 954 . 205 PHE N N 123.047 0.2 1 955 . 205 PHE H H 9.377 0.01 1 956 . 205 PHE CA C 56.873 0.2 1 957 . 205 PHE CB C 42.311 0.2 1 958 . 205 PHE C C 174.789 0.2 1 959 . 206 ILE N N 123.469 0.2 1 960 . 206 ILE H H 7.518 0.01 1 961 . 206 ILE CA C 60.555 0.2 1 962 . 206 ILE CB C 40.264 0.2 1 963 . 206 ILE C C 169.475 0.2 1 964 . 207 ALA N N 128.170 0.2 1 965 . 207 ALA H H 8.449 0.01 1 966 . 207 ALA CA C 50.861 0.2 1 967 . 207 ALA CB C 21.589 0.2 1 968 . 207 ALA C C 174.899 0.2 1 969 . 208 ASP N N 124.058 0.2 1 970 . 208 ASP H H 8.236 0.01 1 971 . 208 ASP CA C 53.137 0.2 1 972 . 208 ASP CB C 45.214 0.2 1 973 . 208 ASP C C 172.690 0.2 1 974 . 209 LYS N N 109.667 0.2 1 975 . 209 LYS H H 8.036 0.01 1 976 . 209 LYS CA C 55.747 0.2 1 977 . 210 SER N N 115.641 0.2 1 978 . 210 SER H H 8.239 0.01 1 979 . 210 SER CA C 57.244 0.2 1 980 . 210 SER CB C 68.091 0.2 1 981 . 210 SER C C 174.033 0.2 1 982 . 211 GLY N N 102.916 0.2 1 983 . 211 GLY H H 8.602 0.01 1 984 . 212 ALA CA C 53.169 0.2 1 985 . 212 ALA CB C 23.117 0.2 1 986 . 212 ALA C C 175.489 0.2 1 987 . 213 GLY N N 107.642 0.2 1 988 . 213 GLY H H 7.726 0.01 1 989 . 213 GLY CA C 45.527 0.2 1 990 . 213 GLY C C 172.718 0.2 1 991 . 214 GLU N N 117.220 0.2 1 992 . 214 GLU H H 7.860 0.01 1 993 . 214 GLU CA C 56.264 0.2 1 994 . 214 GLU CB C 30.079 0.2 1 995 . 214 GLU C C 176.018 0.2 1 996 . 215 ARG N N 118.256 0.2 1 997 . 215 ARG H H 9.471 0.01 1 998 . 215 ARG CA C 57.370 0.2 1 999 . 215 ARG CB C 27.634 0.2 1 1000 . 215 ARG C C 176.020 0.2 1 1001 . 216 GLY N N 102.908 0.2 1 1002 . 216 GLY H H 8.797 0.01 1 1003 . 216 GLY CA C 46.621 0.2 1 1004 . 216 GLY C C 177.321 0.2 1 1005 . 217 SER N N 119.501 0.2 1 1006 . 217 SER H H 7.542 0.01 1 1007 . 217 SER CA C 60.135 0.2 1 1008 . 217 SER CB C 64.445 0.2 1 1009 . 217 SER C C 174.939 0.2 1 1010 . 218 ARG N N 126.380 0.2 1 1011 . 218 ARG H H 9.047 0.01 1 1012 . 218 ARG CA C 54.509 0.2 1 1013 . 218 ARG CB C 34.859 0.2 1 1014 . 218 ARG C C 174.210 0.2 1 1015 . 219 GLY N N 111.745 0.2 1 1016 . 219 GLY H H 8.521 0.01 1 1017 . 219 GLY CA C 46.714 0.2 1 1018 . 219 GLY C C 170.313 0.2 1 1019 . 220 ILE N N 116.966 0.2 1 1020 . 220 ILE H H 9.177 0.01 1 1021 . 220 ILE CA C 59.706 0.2 1 1022 . 220 ILE C C 170.440 0.2 1 1023 . 221 ILE N N 118.224 0.2 1 1024 . 221 ILE H H 8.104 0.01 1 1025 . 221 ILE CA C 58.550 0.2 1 1026 . 221 ILE CB C 39.992 0.2 1 1027 . 221 ILE C C 174.738 0.2 1 1028 . 222 ALA N N 122.940 0.2 1 1029 . 222 ALA H H 8.986 0.01 1 1030 . 222 ALA CA C 51.605 0.2 1 1031 . 222 ALA CB C 24.548 0.2 1 1032 . 222 ALA C C 174.594 0.2 1 1033 . 223 ALA N N 122.994 0.2 1 1034 . 223 ALA H H 9.339 0.01 1 1035 . 223 ALA CA C 50.618 0.2 1 1036 . 223 ALA CB C 20.450 0.2 1 1037 . 223 ALA C C 175.586 0.2 1 1038 . 224 LEU N N 121.313 0.2 1 1039 . 224 LEU H H 9.323 0.01 1 1040 . 224 LEU CA C 55.183 0.2 1 1041 . 224 LEU CB C 46.635 0.2 1 1042 . 224 LEU C C 176.667 0.2 1 1043 . 225 GLY N N 110.565 0.2 1 1044 . 225 GLY H H 8.813 0.01 1 1045 . 226 PRO CA C 60.827 0.2 1 1046 . 226 PRO CB C 31.609 0.2 1 1047 . 226 PRO C C 176.013 0.2 1 1048 . 227 ASP N N 114.401 0.2 1 1049 . 227 ASP H H 7.937 0.01 1 1050 . 227 ASP CA C 55.063 0.2 1 1051 . 227 ASP CB C 39.325 0.2 1 1052 . 227 ASP C C 177.139 0.2 1 1053 . 228 GLY N N 100.253 0.2 1 1054 . 228 GLY H H 7.721 0.01 1 1055 . 228 GLY CA C 46.889 0.2 1 1056 . 228 GLY C C 173.389 0.2 1 1057 . 229 LYS N N 119.497 0.2 1 1058 . 229 LYS H H 7.181 0.01 1 1059 . 229 LYS CA C 52.522 0.2 1 1060 . 230 PRO CA C 62.151 0.2 1 1061 . 230 PRO CB C 31.579 0.2 1 1062 . 230 PRO C C 176.073 0.2 1 1063 . 231 SER N N 112.643 0.2 1 1064 . 231 SER H H 8.543 0.01 1 1065 . 231 SER CA C 59.074 0.2 1 1066 . 231 SER CB C 65.749 0.2 1 1067 . 231 SER C C 174.520 0.2 1 1068 . 232 ARG N N 123.085 0.2 1 1069 . 232 ARG H H 8.840 0.01 1 1070 . 232 ARG CA C 55.948 0.2 1 1071 . 232 ARG CB C 36.100 0.2 1 1072 . 232 ARG C C 174.499 0.2 1 1073 . 233 ILE N N 122.778 0.2 1 1074 . 233 ILE H H 9.243 0.01 1 1075 . 233 ILE CA C 58.807 0.2 1 1076 . 233 ILE CB C 40.835 0.2 1 1077 . 233 ILE C C 174.554 0.2 1 1078 . 234 VAL N N 126.416 0.2 1 1079 . 234 VAL H H 9.202 0.01 1 1080 . 234 VAL CA C 59.683 0.2 1 1081 . 234 VAL CB C 36.148 0.2 1 1082 . 234 VAL C C 173.547 0.2 1 1083 . 235 VAL N N 125.525 0.2 1 1084 . 235 VAL H H 8.237 0.01 1 1085 . 235 VAL CA C 60.638 0.2 1 1086 . 235 VAL CB C 35.782 0.2 1 1087 . 235 VAL C C 173.787 0.2 1 1088 . 236 ILE N N 123.209 0.2 1 1089 . 236 ILE H H 8.340 0.01 1 1090 . 236 ILE CA C 60.106 0.2 1 1091 . 236 ILE CB C 41.823 0.2 1 1092 . 236 ILE C C 174.323 0.2 1 1093 . 237 TYR N N 122.337 0.2 1 1094 . 237 TYR H H 8.736 0.01 1 1095 . 237 TYR CA C 57.228 0.2 1 1096 . 237 TYR CB C 45.422 0.2 1 1097 . 237 TYR C C 173.953 0.2 1 1098 . 238 THR N N 111.481 0.2 1 1099 . 238 THR H H 8.946 0.01 1 1100 . 238 THR CA C 59.675 0.2 1 1101 . 238 THR CB C 70.318 0.2 1 1102 . 238 THR C C 172.478 0.2 1 1103 . 239 THR N N 122.025 0.2 1 1104 . 239 THR H H 8.019 0.01 1 1105 . 239 THR CA C 63.587 0.2 1 1106 . 239 THR CB C 69.338 0.2 1 1107 . 239 THR C C 171.631 0.2 1 1108 . 240 GLY N N 114.116 0.2 1 1109 . 240 GLY H H 8.679 0.01 1 1110 . 240 GLY CA C 45.728 0.2 1 1111 . 240 GLY C C 174.889 0.2 1 1112 . 241 SER N N 114.702 0.2 1 1113 . 241 SER H H 8.363 0.01 1 1114 . 241 SER CA C 59.119 0.2 1 1115 . 241 SER CB C 65.739 0.2 1 1116 . 241 SER C C 175.992 0.2 1 1117 . 242 GLN N N 123.485 0.2 1 1118 . 242 GLN H H 8.845 0.01 1 1119 . 242 GLN CA C 55.872 0.2 1 1120 . 242 GLN CB C 29.037 0.2 1 1121 . 242 GLN C C 175.956 0.2 1 1122 . 243 ALA N N 123.444 0.2 1 1123 . 243 ALA H H 8.711 0.01 1 1124 . 243 ALA CA C 52.410 0.2 1 1125 . 243 ALA CB C 20.583 0.2 1 1126 . 243 ALA C C 178.724 0.2 1 1127 . 244 THR N N 112.909 0.2 1 1128 . 244 THR H H 8.655 0.01 1 1129 . 244 THR CA C 61.701 0.2 1 1130 . 244 THR CB C 71.004 0.2 1 1131 . 244 THR C C 175.978 0.2 1 1132 . 245 MET N N 122.533 0.2 1 1133 . 245 MET H H 9.144 0.01 1 1134 . 245 MET CA C 58.205 0.2 1 1135 . 245 MET CB C 30.995 0.2 1 1136 . 245 MET C C 177.815 0.2 1 1137 . 246 ASP N N 116.657 0.2 1 1138 . 246 ASP H H 8.452 0.01 1 1139 . 246 ASP CA C 57.847 0.2 1 1140 . 246 ASP CB C 40.649 0.2 1 1141 . 246 ASP C C 178.689 0.2 1 1142 . 247 GLU N N 120.361 0.2 1 1143 . 247 GLU H H 7.637 0.01 1 1144 . 247 GLU CA C 59.004 0.2 1 1145 . 247 GLU CB C 30.090 0.2 1 1146 . 247 GLU C C 179.327 0.2 1 1147 . 248 ARG N N 118.863 0.2 1 1148 . 248 ARG H H 8.116 0.01 1 1149 . 248 ARG CA C 60.867 0.2 1 1150 . 248 ARG CB C 31.182 0.2 1 1151 . 248 ARG C C 177.500 0.2 1 1152 . 249 ASN N N 117.029 0.2 1 1153 . 249 ASN H H 8.777 0.01 1 1154 . 249 ASN CA C 55.427 0.2 1 1155 . 249 ASN CB C 37.261 0.2 1 1156 . 249 ASN C C 176.568 0.2 1 1157 . 250 ARG N N 118.803 0.2 1 1158 . 250 ARG H H 8.026 0.01 1 1159 . 250 ARG CA C 59.310 0.2 1 1160 . 250 ARG CB C 30.151 0.2 1 1161 . 250 ARG C C 178.852 0.2 1 1162 . 251 GLN N N 114.993 0.2 1 1163 . 251 GLN H H 7.801 0.01 1 1164 . 251 GLN CA C 58.385 0.2 1 1165 . 251 GLN CB C 27.583 0.2 1 1166 . 251 GLN C C 178.488 0.2 1 1167 . 252 ILE N N 117.762 0.2 1 1168 . 252 ILE H H 7.417 0.01 1 1169 . 252 ILE CA C 65.823 0.2 1 1170 . 252 ILE CB C 36.414 0.2 1 1171 . 252 ILE C C 177.204 0.2 1 1172 . 253 ALA N N 123.423 0.2 1 1173 . 253 ALA H H 8.710 0.01 1 1174 . 253 ALA CA C 56.171 0.2 1 1175 . 253 ALA CB C 17.813 0.2 1 1176 . 253 ALA C C 180.445 0.2 1 1177 . 254 GLU N N 118.328 0.2 1 1178 . 254 GLU H H 8.428 0.01 1 1179 . 254 GLU CA C 59.762 0.2 1 1180 . 254 GLU CB C 29.796 0.2 1 1181 . 254 GLU C C 180.729 0.2 1 1182 . 255 ILE N N 123.554 0.2 1 1183 . 255 ILE H H 8.035 0.01 1 1184 . 255 ILE CA C 66.601 0.2 1 1185 . 255 ILE CB C 38.068 0.2 1 1186 . 255 ILE C C 177.968 0.2 1 1187 . 256 GLY N N 106.155 0.2 1 1188 . 256 GLY H H 8.360 0.01 1 1189 . 256 GLY CA C 47.708 0.2 1 1190 . 256 GLY C C 173.952 0.2 1 1191 . 257 ALA N N 122.405 0.2 1 1192 . 257 ALA H H 8.633 0.01 1 1193 . 257 ALA CA C 55.321 0.2 1 1194 . 257 ALA CB C 17.806 0.2 1 1195 . 257 ALA C C 180.171 0.2 1 1196 . 258 SER N N 113.514 0.2 1 1197 . 258 SER H H 7.493 0.01 1 1198 . 258 SER CA C 61.810 0.2 1 1199 . 258 SER CB C 63.091 0.2 1 1200 . 258 SER C C 176.257 0.2 1 1201 . 259 LEU N N 122.971 0.2 1 1202 . 259 LEU H H 8.211 0.01 1 1203 . 259 LEU CA C 58.144 0.2 1 1204 . 259 LEU CB C 40.964 0.2 1 1205 . 259 LEU C C 178.866 0.2 1 1206 . 260 ILE N N 118.290 0.2 1 1207 . 260 ILE H H 7.969 0.01 1 1208 . 260 ILE CA C 63.764 0.2 1 1209 . 260 ILE CB C 37.524 0.2 1 1210 . 260 ILE C C 178.489 0.2 1 1211 . 261 LYS N N 121.285 0.2 1 1212 . 261 LYS H H 8.117 0.01 1 1213 . 261 LYS CA C 59.087 0.2 1 1214 . 261 LYS CB C 32.587 0.2 1 1215 . 261 LYS C C 177.968 0.2 1 1216 . 262 HIS N N 114.378 0.2 1 1217 . 262 HIS H H 7.618 0.01 1 1218 . 262 HIS CA C 55.030 0.2 1 1219 . 262 HIS CB C 28.055 0.2 1 1220 . 262 HIS C C 173.667 0.2 1 1221 . 263 TRP N N 128.921 0.2 1 1222 . 263 TRP H H 7.254 0.01 1 1223 . 263 TRP CA C 62.405 0.2 1 stop_ save_