data_5854 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N backbone assignments for the 60.8 kD dimer of the NAD+ synthetase from Bacillus subtilis ; _BMRB_accession_number 5854 _BMRB_flat_file_name bmr5854.str _Entry_type original _Submission_date 2003-06-26 _Accession_date 2003-07-01 _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 Markus Michelle A. . 2 Doliveira Lisa . . 3 Malakian Karl . . 4 Keeney David . . 5 Severin Anatoly . . 6 Underwood Kathryn W. . 7 Tsao Desiree 'H. H.' . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 250 "13C chemical shifts" 759 "15N chemical shifts" 250 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-10 original author . stop_ _Original_release_date 2004-02-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H , 13C, and 15N backbone assignments and secondary structure for the 60.8 kD dimer of the NAD+ synthetase from Bacillus subtilis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14752265 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Markus Michelle A. . 2 Doliveira Lisa . . 3 Malakian Karl . . 4 Keeney David . . 5 Severin Anatoly . . 6 Underwood Kathryn W. . 7 Tsao Desiree H.H. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 301 _Page_last 302 _Year 2004 _Details . loop_ _Keyword 'antibiotic target' 'NAD synthesis pathway' 'resonance assignments' TROSY stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR, 6, 277-293. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister 'G. W.' W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_reference_2 _Saveframe_category citation _Citation_full ; Garrett, D.S., Powers, R., Gronenborn A., and Clore, G.M. (1991) J. Magn. Reson., 95, 214-220. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _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 . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_NADS_nadE _Saveframe_category molecular_system _Mol_system_name 'NAD+ synthetase' _Abbreviation_common 'NADS, nadE' _Enzyme_commission_number 6.3.5.1 loop_ _Mol_system_component_name _Mol_label 'NAD+ synthetase subunit 1' $NAD+_synthetase 'NAD+ synthetase subunit 2' $NAD+_synthetase stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'NAD+ synthetase subunit 1' 1 'NAD+ synthetase subunit 2' stop_ loop_ _Biological_function 'converts nicotinic acid adenine dinucleotide into NAD+' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NAD+_synthetase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'NAD+ synthetase' _Abbreviation_common 'NADS, nadE' _Molecular_mass 30395 _Mol_thiol_state 'not present' _Details ; The initator methionine is present and is numbered "0" for consistency with the numbering used in the previously published crystal structures. ; ############################## # Polymer residue sequence # ############################## _Residue_count 272 _Mol_residue_sequence ; MSMQEKIMRELHVKPSIDPK QEIEDRVNFLKQYVKKTGAK GFVLGISGGQDSTLAGRLAQ LAVESIREEGGDAQFIAVRL PHGTQQDEDDAQLALKFIKP DKSWKFDIKSTVSAFSDQYQ QETGDQLTDFNKGNVKARTR MIAQYAIGGQEGLLVLGTDH AAEAVTGFFTKYGDGGADLL PLTGLTKRQGRTLLKELGAP ERLYLKEPTADLLDEKPQQS DETELGISYDEIDDYLEGKE VSAKVSEALEKRYSMTEHKR QVPASMFDDWWK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 SER 3 2 MET 4 3 GLN 5 4 GLU 6 5 LYS 7 6 ILE 8 7 MET 9 8 ARG 10 9 GLU 11 10 LEU 12 11 HIS 13 12 VAL 14 13 LYS 15 14 PRO 16 15 SER 17 16 ILE 18 17 ASP 19 18 PRO 20 19 LYS 21 20 GLN 22 21 GLU 23 22 ILE 24 23 GLU 25 24 ASP 26 25 ARG 27 26 VAL 28 27 ASN 29 28 PHE 30 29 LEU 31 30 LYS 32 31 GLN 33 32 TYR 34 33 VAL 35 34 LYS 36 35 LYS 37 36 THR 38 37 GLY 39 38 ALA 40 39 LYS 41 40 GLY 42 41 PHE 43 42 VAL 44 43 LEU 45 44 GLY 46 45 ILE 47 46 SER 48 47 GLY 49 48 GLY 50 49 GLN 51 50 ASP 52 51 SER 53 52 THR 54 53 LEU 55 54 ALA 56 55 GLY 57 56 ARG 58 57 LEU 59 58 ALA 60 59 GLN 61 60 LEU 62 61 ALA 63 62 VAL 64 63 GLU 65 64 SER 66 65 ILE 67 66 ARG 68 67 GLU 69 68 GLU 70 69 GLY 71 70 GLY 72 71 ASP 73 72 ALA 74 73 GLN 75 74 PHE 76 75 ILE 77 76 ALA 78 77 VAL 79 78 ARG 80 79 LEU 81 80 PRO 82 81 HIS 83 82 GLY 84 83 THR 85 84 GLN 86 85 GLN 87 86 ASP 88 87 GLU 89 88 ASP 90 89 ASP 91 90 ALA 92 91 GLN 93 92 LEU 94 93 ALA 95 94 LEU 96 95 LYS 97 96 PHE 98 97 ILE 99 98 LYS 100 99 PRO 101 100 ASP 102 101 LYS 103 102 SER 104 103 TRP 105 104 LYS 106 105 PHE 107 106 ASP 108 107 ILE 109 108 LYS 110 109 SER 111 110 THR 112 111 VAL 113 112 SER 114 113 ALA 115 114 PHE 116 115 SER 117 116 ASP 118 117 GLN 119 118 TYR 120 119 GLN 121 120 GLN 122 121 GLU 123 122 THR 124 123 GLY 125 124 ASP 126 125 GLN 127 126 LEU 128 127 THR 129 128 ASP 130 129 PHE 131 130 ASN 132 131 LYS 133 132 GLY 134 133 ASN 135 134 VAL 136 135 LYS 137 136 ALA 138 137 ARG 139 138 THR 140 139 ARG 141 140 MET 142 141 ILE 143 142 ALA 144 143 GLN 145 144 TYR 146 145 ALA 147 146 ILE 148 147 GLY 149 148 GLY 150 149 GLN 151 150 GLU 152 151 GLY 153 152 LEU 154 153 LEU 155 154 VAL 156 155 LEU 157 156 GLY 158 157 THR 159 158 ASP 160 159 HIS 161 160 ALA 162 161 ALA 163 162 GLU 164 163 ALA 165 164 VAL 166 165 THR 167 166 GLY 168 167 PHE 169 168 PHE 170 169 THR 171 170 LYS 172 171 TYR 173 172 GLY 174 173 ASP 175 174 GLY 176 175 GLY 177 176 ALA 178 177 ASP 179 178 LEU 180 179 LEU 181 180 PRO 182 181 LEU 183 182 THR 184 183 GLY 185 184 LEU 186 185 THR 187 186 LYS 188 187 ARG 189 188 GLN 190 189 GLY 191 190 ARG 192 191 THR 193 192 LEU 194 193 LEU 195 194 LYS 196 195 GLU 197 196 LEU 198 197 GLY 199 198 ALA 200 199 PRO 201 200 GLU 202 201 ARG 203 202 LEU 204 203 TYR 205 204 LEU 206 205 LYS 207 206 GLU 208 207 PRO 209 208 THR 210 209 ALA 211 210 ASP 212 211 LEU 213 212 LEU 214 213 ASP 215 214 GLU 216 215 LYS 217 216 PRO 218 217 GLN 219 218 GLN 220 219 SER 221 220 ASP 222 221 GLU 223 222 THR 224 223 GLU 225 224 LEU 226 225 GLY 227 226 ILE 228 227 SER 229 228 TYR 230 229 ASP 231 230 GLU 232 231 ILE 233 232 ASP 234 233 ASP 235 234 TYR 236 235 LEU 237 236 GLU 238 237 GLY 239 238 LYS 240 239 GLU 241 240 VAL 242 241 SER 243 242 ALA 244 243 LYS 245 244 VAL 246 245 SER 247 246 GLU 248 247 ALA 249 248 LEU 250 249 GLU 251 250 LYS 252 251 ARG 253 252 TYR 254 253 SER 255 254 MET 256 255 THR 257 256 GLU 258 257 HIS 259 258 LYS 260 259 ARG 261 260 GLN 262 261 VAL 263 262 PRO 264 263 ALA 265 264 SER 266 265 MET 267 266 PHE 268 267 ASP 269 268 ASP 270 269 TRP 271 270 TRP 272 271 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-12-21 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 PDB 1EE1 "Crystal Structure Of Nh3-Dependent Nad+ Synthetase From Bacillus Subtilis Complexed With One Molecule Atp, Two Molecules Deamid" 99.63 271 100.00 100.00 0.00e+00 PDB 1FYD "Crystal Structure Of Nh3-Dependent Nad+ Synthetase From Bacillus Subtilis Complexed With One Molecule Amp, One Pyrophosphate Io" 99.63 271 100.00 100.00 0.00e+00 PDB 1IFX "Crystal Structure Of Nh3-Dependent Nad+ Synthetase From Bacillus Subtilis Complexed With Two Molecules Deamido-Nad" 99.63 271 100.00 100.00 0.00e+00 PDB 1IH8 "Nh3-Dependent Nad+ Synthetase From Bacillus Subtilis Complexed With Amp-Cpp And Mg2+ Ions." 99.63 271 100.00 100.00 0.00e+00 PDB 1KQP "Nh3-Dependent Nad+ Synthetase From Bacillus Subtilis At 1 A Resolution" 99.63 271 100.00 100.00 0.00e+00 PDB 1NSY "Crystal Structure Of Nh3-dependent Nad+ Synthetase From Bacillus Subtilis" 99.63 271 100.00 100.00 0.00e+00 PDB 2NSY "Crystal Structure Of Nh3-Dependent Nad+ Synthetase From Bacillus Subtilis In Complex With Nad-Adenylate" 99.63 271 100.00 100.00 0.00e+00 DBJ BAA08947 "spore outgrowth factor B [Bacillus subtilis]" 100.00 272 100.00 100.00 0.00e+00 DBJ BAI83777 "NAD synthetase [Bacillus subtilis subsp. natto BEST195]" 100.00 286 100.00 100.00 0.00e+00 DBJ BAM49243 "NAD synthetase [Bacillus subtilis BEST7613]" 100.00 272 100.00 100.00 0.00e+00 DBJ BAM56513 "NAD synthetase [Bacillus subtilis BEST7003]" 100.00 272 100.00 100.00 0.00e+00 DBJ GAK81413 "NAD synthetase [Bacillus subtilis Miyagi-4]" 100.00 272 100.00 100.00 0.00e+00 EMBL CAB12107 "ammonium-dependent NAD+ synthetase [Bacillus subtilis subsp. subtilis str. 168]" 100.00 272 100.00 100.00 0.00e+00 EMBL CCU56768 "NAD synthetase [Bacillus subtilis E1]" 100.00 272 100.00 100.00 0.00e+00 EMBL CEI55431 "NH(3)-dependent NAD(+) synthetase [Bacillus subtilis]" 100.00 272 100.00 100.00 0.00e+00 EMBL CEJ75856 "NH(3)-dependent NAD(+) synthetase [Bacillus sp.]" 100.00 272 100.00 100.00 0.00e+00 GB AAA22635 "outB [Bacillus subtilis]" 100.00 272 100.00 100.00 0.00e+00 GB ADV95243 "NAD synthetase [Bacillus subtilis BSn5]" 100.00 272 100.00 100.00 0.00e+00 GB AEP89377 "NAD+ synthetase [Bacillus subtilis subsp. subtilis str. RO-NN-1]" 100.00 272 100.00 100.00 0.00e+00 GB AFI26860 "NAD synthetase [Bacillus sp. JS]" 100.00 272 98.16 99.63 0.00e+00 GB AFQ56248 "Ammonium-dependent NAD+ synthetase [Bacillus subtilis QB928]" 100.00 272 100.00 100.00 0.00e+00 REF NP_388195 "NH(3)-dependent NAD(+) synthetase [Bacillus subtilis subsp. subtilis str. 168]" 100.00 272 100.00 100.00 0.00e+00 REF WP_003241188 "NAD synthetase [Bacillus subtilis]" 100.00 272 97.43 100.00 0.00e+00 REF WP_003246440 "MULTISPECIES: NAD synthetase [Bacillales]" 100.00 272 100.00 100.00 0.00e+00 REF WP_010332951 "NAD synthetase [Bacillus mojavensis]" 100.00 272 97.43 99.26 0.00e+00 REF WP_014662699 "NAD synthetase [Bacillus sp. JS]" 100.00 272 98.16 99.63 0.00e+00 SP P08164 "RecName: Full=NH(3)-dependent NAD(+) synthetase; AltName: Full=General stress protein 38; Short=GSP38; AltName: Full=Spore outg" 100.00 272 100.00 100.00 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 $NAD+_synthetase 'Bacillus subtilis' 1423 Eubacteria . Bacillus subtilis 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 $NAD+_synthetase 'recombinant technology' 'E. coli' Escherichia coli 'BL21 (lambda DE3)' plasmid pET28a 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 $NAD+_synthetase 1.0 mM '[U-2H; U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $NAD+_synthetase . uM 210 270 '[U-2H; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version 2.1 loop_ _Task processing 'inital visualization with nmrDraw' stop_ _Details . _Citation_label $reference_1 save_ save_PIPP _Saveframe_category software _Name PIPP _Version 4.2.2 loop_ _Task 'analysis of spectra' 'specifically peak-picking' stop_ _Details . _Citation_label $reference_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_The_spectrometer_was_equipped_with_a_triple_resonance_probe_with_x,_y,_and_z_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'The spectrometer was equipped with a triple resonance probe with x, y, and z' _Sample_label . save_ save_gradients._2 _Saveframe_category NMR_applied_experiment _Experiment_name gradients. _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_ save_NMR_spec_expt__4_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__6_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__6_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__7_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__7_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.1 na temperature 308 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details 'The reference is described in Cavanagh et al. (1996) page 176.' 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 TSP H 1 'methyl protons' ppm 0.00 external direct cylindrical external . 1.00000000 TSP C 13 'methyl protons' ppm 0.00 external indirect . . . 0.25144954 TSP N 15 'methyl protons' ppm 0.00 external indirect . . . 0.10132900 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'NAD+ synthetase subunit 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 3 MET CA C 56.100 0.200 1 2 2 3 MET CB C 30.630 0.200 1 3 2 3 MET C C 176.220 0.200 1 4 3 4 GLN N N 123.380 0.050 1 5 3 4 GLN H H 8.000 0.010 1 6 3 4 GLN CA C 59.440 0.200 1 7 3 4 GLN CB C 27.510 0.200 1 8 3 4 GLN C C 177.510 0.200 1 9 4 5 GLU N N 118.270 0.050 1 10 4 5 GLU H H 7.570 0.010 1 11 4 5 GLU CA C 58.910 0.200 1 12 4 5 GLU CB C 28.720 0.200 1 13 4 5 GLU C C 178.630 0.200 1 14 5 6 LYS N N 122.870 0.050 1 15 5 6 LYS H H 7.330 0.010 1 16 5 6 LYS CA C 59.190 0.200 1 17 5 6 LYS CB C 31.990 0.200 1 18 5 6 LYS C C 178.000 0.200 1 19 6 7 ILE N N 122.330 0.050 1 20 6 7 ILE H H 8.310 0.010 1 21 6 7 ILE CA C 66.110 0.200 1 22 6 7 ILE CB C 36.340 0.200 1 23 6 7 ILE C C 181.040 0.200 1 24 7 8 MET N N 119.310 0.050 1 25 7 8 MET H H 8.080 0.010 1 26 7 8 MET CA C 59.900 0.200 1 27 7 8 MET CB C 32.970 0.200 1 28 7 8 MET C C 178.320 0.200 1 29 8 9 ARG N N 118.160 0.050 1 30 8 9 ARG H H 7.500 0.010 1 31 8 9 ARG CA C 58.410 0.200 1 32 8 9 ARG CB C 29.310 0.200 1 33 8 9 ARG C C 180.390 0.200 1 34 9 10 GLU N N 122.660 0.050 1 35 9 10 GLU H H 8.590 0.010 1 36 9 10 GLU CA C 58.560 0.200 1 37 9 10 GLU CB C 28.420 0.200 1 38 9 10 GLU C C 178.040 0.200 1 39 10 11 LEU N N 115.320 0.050 1 40 10 11 LEU H H 7.890 0.010 1 41 10 11 LEU CA C 53.600 0.200 1 42 10 11 LEU CB C 40.300 0.200 1 43 10 11 LEU C C 176.040 0.200 1 44 11 12 HIS N N 113.400 0.050 1 45 11 12 HIS H H 7.000 0.010 1 46 11 12 HIS CA C 55.940 0.200 1 47 11 12 HIS CB C 23.540 0.200 1 48 11 12 HIS C C 172.800 0.200 1 49 12 13 VAL N N 121.480 0.050 1 50 12 13 VAL H H 7.970 0.010 1 51 12 13 VAL CA C 61.810 0.200 1 52 12 13 VAL CB C 32.200 0.200 1 53 12 13 VAL C C 176.350 0.200 1 54 13 14 LYS N N 129.640 0.050 1 55 13 14 LYS H H 9.090 0.010 1 56 13 14 LYS CA C 52.600 0.200 1 57 13 14 LYS CB C 33.140 0.200 1 58 13 14 LYS C C 174.740 0.200 1 59 14 15 PRO CA C 64.230 0.200 1 60 14 15 PRO CB C 31.480 0.200 1 61 14 15 PRO C C 176.460 0.200 1 62 15 16 SER N N 110.900 0.050 1 63 15 16 SER H H 7.060 0.010 1 64 15 16 SER CA C 55.900 0.200 1 65 15 16 SER CB C 63.900 0.200 1 66 15 16 SER C C 173.120 0.200 1 67 16 17 ILE N N 116.610 0.050 1 68 16 17 ILE H H 8.150 0.010 1 69 16 17 ILE CA C 58.390 0.200 1 70 16 17 ILE CB C 41.800 0.200 1 71 16 17 ILE C C 174.670 0.200 1 72 17 18 ASP N N 125.030 0.050 1 73 17 18 ASP H H 9.080 0.010 1 74 17 18 ASP CA C 49.740 0.200 1 75 17 18 ASP CB C 41.350 0.200 1 76 17 18 ASP C C 175.260 0.200 1 77 18 19 PRO CA C 65.320 0.200 1 78 18 19 PRO CB C 31.890 0.200 1 79 18 19 PRO C C 177.410 0.200 1 80 19 20 LYS N N 116.650 0.050 1 81 19 20 LYS H H 7.660 0.010 1 82 19 20 LYS CA C 59.710 0.200 1 83 19 20 LYS CB C 31.370 0.200 1 84 19 20 LYS C C 179.040 0.200 1 85 20 21 GLN N N 122.580 0.050 1 86 20 21 GLN H H 7.330 0.010 1 87 20 21 GLN CA C 57.260 0.200 1 88 20 21 GLN CB C 28.220 0.200 1 89 20 21 GLN C C 177.760 0.200 1 90 21 22 GLU N N 118.660 0.050 1 91 21 22 GLU H H 8.320 0.010 1 92 21 22 GLU CA C 58.590 0.200 1 93 21 22 GLU CB C 29.920 0.200 1 94 21 22 GLU C C 179.540 0.200 1 95 22 23 ILE N N 119.860 0.050 1 96 22 23 ILE H H 7.780 0.010 1 97 22 23 ILE CA C 65.890 0.200 1 98 22 23 ILE CB C 37.560 0.200 1 99 22 23 ILE C C 176.630 0.200 1 100 23 24 GLU N N 120.200 0.050 1 101 23 24 GLU H H 7.520 0.010 1 102 23 24 GLU CA C 59.300 0.200 1 103 23 24 GLU CB C 28.640 0.200 1 104 23 24 GLU C C 179.430 0.200 1 105 24 25 ASP N N 120.210 0.050 1 106 24 25 ASP H H 8.960 0.010 1 107 24 25 ASP CA C 57.020 0.200 1 108 24 25 ASP CB C 39.240 0.200 1 109 24 25 ASP C C 179.960 0.200 1 110 25 26 ARG N N 124.200 0.050 1 111 25 26 ARG H H 8.300 0.010 1 112 25 26 ARG CA C 60.090 0.200 1 113 25 26 ARG CB C 28.980 0.200 1 114 25 26 ARG C C 178.330 0.200 1 115 26 27 VAL N N 123.100 0.050 1 116 26 27 VAL H H 8.630 0.010 1 117 26 27 VAL CA C 67.410 0.200 1 118 26 27 VAL CB C 30.800 0.200 1 119 26 27 VAL C C 178.160 0.200 1 120 27 28 ASN N N 118.990 0.050 1 121 27 28 ASN H H 8.360 0.010 1 122 27 28 ASN CA C 56.170 0.200 1 123 27 28 ASN CB C 37.210 0.200 1 124 27 28 ASN C C 177.630 0.200 1 125 28 29 PHE N N 122.840 0.050 1 126 28 29 PHE H H 7.950 0.010 1 127 28 29 PHE CA C 58.960 0.200 1 128 28 29 PHE CB C 37.760 0.200 1 129 28 29 PHE C C 175.270 0.200 1 130 29 30 LEU N N 120.290 0.050 1 131 29 30 LEU H H 7.170 0.010 1 132 29 30 LEU CA C 57.740 0.200 1 133 29 30 LEU CB C 39.640 0.200 1 134 29 30 LEU C C 178.850 0.200 1 135 30 31 LYS N N 117.420 0.050 1 136 30 31 LYS H H 8.030 0.010 1 137 30 31 LYS CA C 59.660 0.200 1 138 30 31 LYS CB C 31.570 0.200 1 139 30 31 LYS C C 178.500 0.200 1 140 31 32 GLN N N 120.080 0.050 1 141 31 32 GLN H H 8.680 0.010 1 142 31 32 GLN CA C 58.120 0.200 1 143 31 32 GLN CB C 27.930 0.200 1 144 31 32 GLN C C 179.350 0.200 1 145 32 33 TYR N N 123.330 0.050 1 146 32 33 TYR H H 8.520 0.010 1 147 32 33 TYR CA C 61.980 0.200 1 148 32 33 TYR CB C 37.570 0.200 1 149 32 33 TYR C C 179.230 0.200 1 150 33 34 VAL N N 121.210 0.050 1 151 33 34 VAL H H 7.690 0.010 1 152 33 34 VAL CA C 65.680 0.200 1 153 33 34 VAL CB C 30.280 0.200 1 154 33 34 VAL C C 177.500 0.200 1 155 34 35 LYS N N 122.500 0.050 1 156 34 35 LYS H H 7.580 0.010 1 157 34 35 LYS CA C 58.900 0.200 1 158 34 35 LYS CB C 31.270 0.200 1 159 34 35 LYS C C 179.290 0.200 1 160 35 36 LYS N N 120.570 0.050 1 161 35 36 LYS H H 7.900 0.010 1 162 35 36 LYS CA C 57.480 0.200 1 163 35 36 LYS CB C 31.160 0.200 1 164 35 36 LYS C C 178.460 0.200 1 165 36 37 THR N N 107.690 0.050 1 166 36 37 THR H H 7.370 0.010 1 167 36 37 THR CA C 62.640 0.200 1 168 36 37 THR CB C 70.780 0.200 1 169 36 37 THR C C 176.690 0.200 1 170 37 38 GLY N N 112.490 0.050 1 171 37 38 GLY H H 7.790 0.010 1 172 37 38 GLY CA C 45.540 0.200 1 173 37 38 GLY C C 174.260 0.200 1 174 38 39 ALA N N 122.740 0.050 1 175 38 39 ALA H H 7.230 0.010 1 176 38 39 ALA CA C 51.230 0.200 1 177 38 39 ALA CB C 19.010 0.200 1 178 38 39 ALA C C 176.340 0.200 1 179 39 40 LYS N N 115.500 0.050 1 180 39 40 LYS H H 8.270 0.010 1 181 39 40 LYS CA C 55.090 0.200 1 182 39 40 LYS CB C 30.570 0.200 1 183 39 40 LYS C C 175.550 0.200 1 184 40 41 GLY N N 103.970 0.050 1 185 40 41 GLY H H 6.550 0.010 1 186 40 41 GLY CA C 43.160 0.200 1 187 40 41 GLY C C 171.920 0.200 1 188 41 42 PHE N N 118.810 0.050 1 189 41 42 PHE H H 8.160 0.010 1 190 41 42 PHE CA C 54.820 0.200 1 191 41 42 PHE CB C 44.460 0.200 1 192 41 42 PHE C C 172.760 0.200 1 193 42 43 VAL N N 122.070 0.050 1 194 42 43 VAL H H 8.940 0.010 1 195 42 43 VAL CA C 58.250 0.200 1 196 42 43 VAL CB C 34.320 0.200 1 197 42 43 VAL C C 171.980 0.200 1 198 43 44 LEU N N 126.530 0.050 1 199 43 44 LEU H H 7.670 0.010 1 200 43 44 LEU CA C 54.010 0.200 1 201 43 44 LEU CB C 46.270 0.200 1 202 43 44 LEU C C 175.230 0.200 1 203 44 45 GLY N N 115.160 0.050 1 204 44 45 GLY H H 8.100 0.010 1 205 44 45 GLY CA C 44.410 0.200 1 206 44 45 GLY C C 173.300 0.200 1 207 45 46 ILE N N 128.120 0.050 1 208 45 46 ILE H H 8.610 0.010 1 209 45 46 ILE CA C 57.380 0.200 1 210 45 46 ILE CB C 37.090 0.200 1 211 45 46 ILE C C 175.760 0.200 1 212 47 48 GLY CA C 44.270 0.200 1 213 47 48 GLY C C 173.280 0.200 1 214 48 49 GLY N N 108.980 0.050 1 215 48 49 GLY H H 7.970 0.010 1 216 48 49 GLY CA C 43.920 0.200 1 217 48 49 GLY C C 174.670 0.200 1 218 49 50 GLN CA C 59.420 0.200 1 219 49 50 GLN CB C 28.660 0.200 1 220 49 50 GLN C C 177.010 0.200 1 221 50 51 ASP N N 120.530 0.050 1 222 50 51 ASP H H 8.330 0.010 1 223 50 51 ASP CA C 57.040 0.200 1 224 50 51 ASP CB C 39.040 0.200 1 225 50 51 ASP C C 178.020 0.200 1 226 51 52 SER N N 115.350 0.050 1 227 51 52 SER H H 8.650 0.010 1 228 51 52 SER CA C 60.930 0.200 1 229 51 52 SER CB C 62.640 0.200 1 230 52 53 THR N N 123.140 0.050 1 231 52 53 THR H H 7.930 0.010 1 232 52 53 THR CA C 59.000 0.200 1 233 52 53 THR CB C 66.790 0.200 1 234 52 53 THR C C 175.270 0.200 1 235 53 54 LEU N N 122.730 0.050 1 236 53 54 LEU H H 8.120 0.010 1 237 53 54 LEU CA C 57.880 0.200 1 238 53 54 LEU CB C 39.590 0.200 1 239 53 54 LEU C C 177.310 0.200 1 240 54 55 ALA N N 119.710 0.050 1 241 54 55 ALA H H 8.370 0.010 1 242 54 55 ALA CA C 55.100 0.200 1 243 54 55 ALA CB C 16.980 0.200 1 244 54 55 ALA C C 177.890 0.200 1 245 55 56 GLY N N 105.390 0.050 1 246 55 56 GLY H H 8.270 0.010 1 247 55 56 GLY CA C 46.460 0.200 1 248 55 56 GLY C C 173.830 0.200 1 249 56 57 ARG N N 122.870 0.050 1 250 56 57 ARG H H 8.050 0.010 1 251 56 57 ARG CA C 56.930 0.200 1 252 56 57 ARG CB C 27.960 0.200 1 253 56 57 ARG C C 177.630 0.200 1 254 57 58 LEU N N 117.240 0.050 1 255 57 58 LEU H H 7.700 0.010 1 256 57 58 LEU CA C 57.530 0.200 1 257 57 58 LEU CB C 39.610 0.200 1 258 57 58 LEU C C 177.600 0.200 1 259 58 59 ALA N N 121.740 0.050 1 260 58 59 ALA H H 7.400 0.010 1 261 58 59 ALA CA C 54.270 0.200 1 262 58 59 ALA CB C 16.470 0.200 1 263 58 59 ALA C C 178.360 0.200 1 264 59 60 GLN N N 120.640 0.050 1 265 59 60 GLN H H 7.500 0.010 1 266 59 60 GLN CA C 56.970 0.200 1 267 59 60 GLN CB C 26.880 0.200 1 268 59 60 GLN C C 178.460 0.200 1 269 60 61 LEU N N 119.900 0.050 1 270 60 61 LEU H H 8.020 0.010 1 271 60 61 LEU CA C 57.400 0.200 1 272 60 61 LEU CB C 40.530 0.200 1 273 60 61 LEU C C 181.130 0.200 1 274 61 62 ALA N N 123.330 0.050 1 275 61 62 ALA H H 8.230 0.010 1 276 61 62 ALA CA C 55.340 0.200 1 277 61 62 ALA CB C 18.270 0.200 1 278 61 62 ALA C C 179.790 0.200 1 279 62 63 VAL N N 114.150 0.050 1 280 62 63 VAL H H 8.310 0.010 1 281 62 63 VAL CA C 65.670 0.200 1 282 62 63 VAL CB C 29.800 0.200 1 283 62 63 VAL C C 178.410 0.200 1 284 63 64 GLU N N 123.180 0.050 1 285 63 64 GLU H H 8.130 0.010 1 286 63 64 GLU CA C 59.700 0.200 1 287 63 64 GLU CB C 28.150 0.200 1 288 63 64 GLU C C 179.720 0.200 1 289 64 65 SER N N 116.320 0.050 1 290 64 65 SER H H 7.700 0.010 1 291 64 65 SER CA C 60.470 0.200 1 292 64 65 SER CB C 62.040 0.200 1 293 64 65 SER C C 177.500 0.200 1 294 65 66 ILE N N 121.930 0.050 1 295 65 66 ILE H H 8.110 0.010 1 296 65 66 ILE CA C 64.670 0.200 1 297 65 66 ILE CB C 36.770 0.200 1 298 65 66 ILE C C 179.500 0.200 1 299 66 67 ARG N N 120.650 0.050 1 300 66 67 ARG H H 8.100 0.010 1 301 66 67 ARG CA C 59.720 0.200 1 302 66 67 ARG CB C 29.920 0.200 1 303 66 67 ARG C C 181.290 0.200 1 304 67 68 GLU N N 124.930 0.050 1 305 67 68 GLU H H 8.250 0.010 1 306 67 68 GLU CA C 58.820 0.200 1 307 67 68 GLU CB C 28.500 0.200 1 308 67 68 GLU C C 178.260 0.200 1 309 68 69 GLU N N 118.060 0.050 1 310 68 69 GLU H H 7.440 0.010 1 311 68 69 GLU CA C 55.710 0.200 1 312 68 69 GLU CB C 28.760 0.200 1 313 68 69 GLU C C 176.700 0.200 1 314 69 70 GLY N N 109.050 0.050 1 315 69 70 GLY H H 7.770 0.010 1 316 69 70 GLY CA C 44.720 0.200 1 317 69 70 GLY C C 174.990 0.200 1 318 70 71 GLY N N 111.070 0.050 1 319 70 71 GLY H H 8.100 0.010 1 320 70 71 GLY CA C 43.430 0.200 1 321 70 71 GLY C C 171.580 0.200 1 322 71 72 ASP N N 119.840 0.050 1 323 71 72 ASP H H 8.060 0.010 1 324 71 72 ASP CA C 52.800 0.200 1 325 71 72 ASP CB C 41.950 0.200 1 326 71 72 ASP C C 174.480 0.200 1 327 72 73 ALA N N 124.900 0.050 1 328 72 73 ALA H H 7.270 0.010 1 329 72 73 ALA CA C 50.950 0.200 1 330 72 73 ALA CB C 21.230 0.200 1 331 72 73 ALA C C 175.330 0.200 1 332 73 74 GLN N N 117.940 0.050 1 333 73 74 GLN H H 8.240 0.010 1 334 73 74 GLN CA C 53.840 0.200 1 335 73 74 GLN CB C 32.930 0.200 1 336 73 74 GLN C C 173.400 0.200 1 337 74 75 PHE N N 125.300 0.050 1 338 74 75 PHE H H 9.380 0.010 1 339 74 75 PHE CA C 53.750 0.200 1 340 74 75 PHE CB C 39.320 0.200 1 341 74 75 PHE C C 172.940 0.200 1 342 75 76 ILE N N 127.440 0.050 1 343 75 76 ILE H H 8.060 0.010 1 344 75 76 ILE CA C 60.150 0.200 1 345 75 76 ILE CB C 37.650 0.200 1 346 75 76 ILE C C 172.700 0.200 1 347 76 77 ALA N N 130.180 0.050 1 348 76 77 ALA H H 7.480 0.010 1 349 76 77 ALA CA C 48.890 0.200 1 350 76 77 ALA CB C 19.080 0.200 1 351 76 77 ALA C C 176.050 0.200 1 352 77 78 VAL N N 122.600 0.050 1 353 77 78 VAL H H 8.620 0.010 1 354 77 78 VAL CA C 57.220 0.200 1 355 77 78 VAL CB C 35.100 0.200 1 356 77 78 VAL C C 174.880 0.200 1 357 78 79 ARG N N 130.860 0.050 1 358 78 79 ARG H H 8.480 0.010 1 359 78 79 ARG CA C 55.520 0.200 1 360 78 79 ARG CB C 30.470 0.200 1 361 78 79 ARG C C 175.170 0.200 1 362 79 80 LEU N N 125.850 0.050 1 363 79 80 LEU H H 8.720 0.010 1 364 79 80 LEU CA C 51.510 0.200 1 365 79 80 LEU CB C 42.220 0.200 1 366 79 80 LEU C C 173.800 0.200 1 367 80 81 PRO CA C 62.750 0.200 1 368 80 81 PRO CB C 31.310 0.200 1 369 80 81 PRO C C 174.200 0.200 1 370 81 82 HIS N N 121.990 0.050 1 371 81 82 HIS H H 8.410 0.010 1 372 81 82 HIS CA C 55.420 0.200 1 373 81 82 HIS CB C 28.540 0.200 1 374 81 82 HIS C C 174.200 0.200 1 375 82 83 GLY N N 117.540 0.050 1 376 82 83 GLY H H 9.030 0.010 1 377 82 83 GLY CA C 44.650 0.200 1 378 82 83 GLY C C 173.970 0.200 1 379 83 84 THR N N 115.060 0.050 1 380 83 84 THR H H 7.900 0.010 1 381 83 84 THR CA C 61.830 0.200 1 382 83 84 THR CB C 69.080 0.200 1 383 83 84 THR C C 175.180 0.200 1 384 84 85 GLN N N 125.060 0.050 1 385 84 85 GLN H H 8.450 0.010 1 386 84 85 GLN CA C 55.360 0.200 1 387 84 85 GLN CB C 28.980 0.200 1 388 84 85 GLN C C 175.990 0.200 1 389 85 86 GLN N N 123.170 0.050 1 390 85 86 GLN H H 8.300 0.010 1 391 85 86 GLN CA C 56.150 0.200 1 392 85 86 GLN CB C 29.260 0.200 1 393 85 86 GLN C C 176.150 0.200 1 394 86 87 ASP N N 121.120 0.050 1 395 86 87 ASP H H 8.490 0.010 1 396 86 87 ASP CA C 53.890 0.200 1 397 86 87 ASP CB C 40.260 0.200 1 398 86 87 ASP C C 176.470 0.200 1 399 87 88 GLU N N 123.550 0.050 1 400 87 88 GLU H H 8.170 0.010 1 401 87 88 GLU CA C 56.940 0.200 1 402 87 88 GLU CB C 29.610 0.200 1 403 87 88 GLU C C 175.430 0.200 1 404 88 89 ASP N N 122.310 0.050 1 405 88 89 ASP H H 8.340 0.010 1 406 88 89 ASP CA C 56.690 0.200 1 407 88 89 ASP CB C 39.860 0.200 1 408 88 89 ASP C C 178.590 0.200 1 409 89 90 ASP N N 121.850 0.050 1 410 89 90 ASP H H 8.350 0.010 1 411 89 90 ASP CA C 56.740 0.200 1 412 89 90 ASP CB C 39.270 0.200 1 413 89 90 ASP C C 178.090 0.200 1 414 90 91 ALA N N 124.880 0.050 1 415 90 91 ALA H H 8.090 0.010 1 416 90 91 ALA CA C 54.810 0.200 1 417 90 91 ALA CB C 16.750 0.200 1 418 90 91 ALA C C 179.020 0.200 1 419 91 92 GLN N N 117.290 0.050 1 420 91 92 GLN H H 8.130 0.010 1 421 91 92 GLN CA C 58.510 0.200 1 422 91 92 GLN CB C 27.050 0.200 1 423 91 92 GLN C C 179.260 0.200 1 424 92 93 LEU N N 123.750 0.050 1 425 92 93 LEU H H 7.880 0.010 1 426 92 93 LEU CA C 57.450 0.200 1 427 92 93 LEU CB C 40.520 0.200 1 428 92 93 LEU C C 179.340 0.200 1 429 93 94 ALA N N 123.180 0.050 1 430 93 94 ALA H H 8.200 0.010 1 431 93 94 ALA CA C 55.230 0.200 1 432 93 94 ALA CB C 17.530 0.200 1 433 93 94 ALA C C 180.520 0.200 1 434 94 95 LEU N N 120.180 0.050 1 435 94 95 LEU H H 8.240 0.010 1 436 94 95 LEU CA C 58.370 0.200 1 437 94 95 LEU CB C 40.600 0.200 1 438 94 95 LEU C C 179.790 0.200 1 439 95 96 LYS N N 121.990 0.050 1 440 95 96 LYS H H 7.760 0.010 1 441 95 96 LYS CA C 58.570 0.200 1 442 95 96 LYS CB C 31.530 0.200 1 443 95 96 LYS C C 177.110 0.200 1 444 96 97 PHE N N 119.830 0.050 1 445 96 97 PHE H H 7.380 0.010 1 446 96 97 PHE CA C 58.130 0.200 1 447 96 97 PHE CB C 39.230 0.200 1 448 96 97 PHE C C 175.570 0.200 1 449 97 98 ILE N N 121.050 0.050 1 450 97 98 ILE H H 8.850 0.010 1 451 97 98 ILE CA C 65.430 0.200 1 452 97 98 ILE CB C 39.190 0.200 1 453 97 98 ILE C C 174.890 0.200 1 454 98 99 LYS N N 110.990 0.050 1 455 98 99 LYS H H 7.870 0.010 1 456 98 99 LYS CA C 56.160 0.200 1 457 98 99 LYS CB C 29.140 0.200 1 458 98 99 LYS C C 173.530 0.200 1 459 99 100 PRO CA C 60.810 0.200 1 460 99 100 PRO CB C 32.060 0.200 1 461 99 100 PRO C C 178.650 0.200 1 462 100 101 ASP N N 120.850 0.050 1 463 100 101 ASP H H 7.860 0.010 1 464 100 101 ASP CA C 57.880 0.200 1 465 100 101 ASP CB C 40.490 0.200 1 466 100 101 ASP C C 177.210 0.200 1 467 101 102 LYS N N 115.630 0.050 1 468 101 102 LYS H H 7.490 0.010 1 469 101 102 LYS CA C 54.500 0.200 1 470 101 102 LYS CB C 36.600 0.200 1 471 101 102 LYS C C 173.860 0.200 1 472 102 103 SER N N 117.420 0.050 1 473 102 103 SER H H 8.450 0.010 1 474 102 103 SER CA C 54.960 0.200 1 475 102 103 SER CB C 62.950 0.200 1 476 102 103 SER C C 173.620 0.200 1 477 103 104 TRP N N 130.180 0.050 1 478 103 104 TRP H H 9.140 0.010 1 479 103 104 TRP CA C 53.900 0.200 1 480 103 104 TRP CB C 33.050 0.200 1 481 103 104 TRP C C 175.590 0.200 1 482 104 105 LYS N N 126.590 0.050 1 483 104 105 LYS H H 8.750 0.010 1 484 104 105 LYS CA C 55.460 0.200 1 485 104 105 LYS CB C 33.130 0.200 1 486 104 105 LYS C C 172.850 0.200 1 487 105 106 PHE N N 124.670 0.050 1 488 105 106 PHE H H 8.710 0.010 1 489 105 106 PHE CA C 57.300 0.200 1 490 105 106 PHE CB C 39.980 0.200 1 491 105 106 PHE C C 172.660 0.200 1 492 106 107 ASP N N 129.010 0.050 1 493 106 107 ASP H H 7.910 0.010 1 494 106 107 ASP CA C 52.460 0.200 1 495 106 107 ASP CB C 40.640 0.200 1 496 106 107 ASP C C 177.890 0.200 1 497 107 108 ILE N N 121.440 0.050 1 498 107 108 ILE H H 8.450 0.010 1 499 107 108 ILE CA C 62.500 0.200 1 500 107 108 ILE CB C 38.500 0.200 1 501 107 108 ILE C C 176.530 0.200 1 502 108 109 LYS N N 126.830 0.050 1 503 108 109 LYS H H 8.950 0.010 1 504 108 109 LYS CA C 60.670 0.200 1 505 108 109 LYS CB C 31.540 0.200 1 506 108 109 LYS C C 178.850 0.200 1 507 109 110 SER N N 117.890 0.050 1 508 109 110 SER H H 9.470 0.010 1 509 109 110 SER CA C 60.720 0.200 1 510 110 111 THR C C 175.930 0.200 1 511 111 112 VAL N N 123.010 0.050 1 512 111 112 VAL H H 8.130 0.010 1 513 111 112 VAL CA C 66.550 0.200 1 514 111 112 VAL CB C 30.980 0.200 1 515 111 112 VAL C C 179.130 0.200 1 516 112 113 SER N N 119.850 0.050 1 517 112 113 SER H H 9.290 0.010 1 518 112 113 SER CA C 61.700 0.200 1 519 112 113 SER CB C 66.150 0.200 1 520 112 113 SER C C 175.560 0.200 1 521 113 114 ALA N N 125.790 0.050 1 522 113 114 ALA H H 7.780 0.010 1 523 113 114 ALA CA C 54.930 0.200 1 524 113 114 ALA CB C 17.110 0.200 1 525 113 114 ALA C C 180.500 0.200 1 526 114 115 PHE N N 122.440 0.050 1 527 114 115 PHE H H 8.350 0.010 1 528 114 115 PHE CA C 62.200 0.200 1 529 114 115 PHE CB C 38.250 0.200 1 530 114 115 PHE C C 177.630 0.200 1 531 115 116 SER N N 117.790 0.050 1 532 115 116 SER H H 8.950 0.010 1 533 115 116 SER CA C 62.180 0.200 1 534 115 116 SER C C 177.740 0.200 1 535 116 117 ASP N N 124.800 0.050 1 536 116 117 ASP H H 8.680 0.010 1 537 116 117 ASP CA C 56.810 0.200 1 538 116 117 ASP CB C 39.380 0.200 1 539 116 117 ASP C C 178.880 0.200 1 540 117 118 GLN N N 124.140 0.050 1 541 117 118 GLN H H 8.050 0.010 1 542 117 118 GLN CA C 57.990 0.200 1 543 117 118 GLN CB C 25.710 0.200 1 544 117 118 GLN C C 177.900 0.200 1 545 118 119 TYR N N 122.290 0.050 1 546 118 119 TYR H H 8.880 0.010 1 547 118 119 TYR CA C 63.440 0.200 1 548 118 119 TYR CB C 38.020 0.200 1 549 118 119 TYR C C 178.920 0.200 1 550 119 120 GLN N N 122.250 0.050 1 551 119 120 GLN H H 7.760 0.010 1 552 119 120 GLN CA C 58.150 0.200 1 553 119 120 GLN CB C 27.330 0.200 1 554 119 120 GLN C C 179.340 0.200 1 555 120 121 GLN N N 122.600 0.050 1 556 120 121 GLN H H 7.980 0.010 1 557 120 121 GLN CA C 58.510 0.200 1 558 120 121 GLN CB C 27.990 0.200 1 559 120 121 GLN C C 178.360 0.200 1 560 121 122 GLU N N 116.610 0.050 1 561 121 122 GLU H H 8.280 0.010 1 562 121 122 GLU CA C 57.060 0.200 1 563 121 122 GLU CB C 28.920 0.200 1 564 121 122 GLU C C 179.290 0.200 1 565 122 123 THR N N 106.660 0.050 1 566 122 123 THR H H 7.530 0.010 1 567 122 123 THR CA C 61.540 0.200 1 568 122 123 THR CB C 71.380 0.200 1 569 122 123 THR C C 176.290 0.200 1 570 123 124 GLY N N 113.760 0.050 1 571 123 124 GLY H H 7.890 0.010 1 572 123 124 GLY CA C 45.170 0.200 1 573 123 124 GLY C C 172.960 0.200 1 574 124 125 ASP N N 124.070 0.050 1 575 124 125 ASP H H 8.470 0.010 1 576 124 125 ASP CA C 52.630 0.200 1 577 124 125 ASP CB C 42.690 0.200 1 578 124 125 ASP C C 174.150 0.200 1 579 125 126 GLN N N 118.340 0.050 1 580 125 126 GLN H H 7.990 0.010 1 581 125 126 GLN CA C 54.040 0.200 1 582 125 126 GLN CB C 29.600 0.200 1 583 125 126 GLN C C 177.040 0.200 1 584 126 127 LEU N N 125.990 0.050 1 585 126 127 LEU H H 8.520 0.010 1 586 126 127 LEU CA C 54.250 0.200 1 587 126 127 LEU CB C 42.630 0.200 1 588 126 127 LEU C C 178.330 0.200 1 589 127 128 THR N N 116.820 0.050 1 590 127 128 THR H H 8.900 0.010 1 591 127 128 THR CA C 60.660 0.200 1 592 127 128 THR CB C 70.440 0.200 1 593 127 128 THR C C 175.140 0.200 1 594 128 129 ASP N N 123.880 0.050 1 595 128 129 ASP H H 8.960 0.010 1 596 128 129 ASP CA C 57.950 0.200 1 597 128 129 ASP CB C 39.350 0.200 1 598 128 129 ASP C C 179.560 0.200 1 599 129 130 PHE N N 122.110 0.050 1 600 129 130 PHE H H 8.680 0.010 1 601 129 130 PHE CA C 60.500 0.200 1 602 129 130 PHE CB C 38.640 0.200 1 603 129 130 PHE C C 178.110 0.200 1 604 130 131 ASN N N 119.340 0.050 1 605 130 131 ASN H H 7.690 0.010 1 606 130 131 ASN CA C 56.180 0.200 1 607 130 131 ASN CB C 36.910 0.200 1 608 130 131 ASN C C 179.660 0.200 1 609 131 132 LYS N N 127.120 0.050 1 610 131 132 LYS H H 9.440 0.010 1 611 131 132 LYS CA C 60.250 0.200 1 612 131 132 LYS CB C 31.010 0.200 1 613 131 132 LYS C C 178.680 0.200 1 614 132 133 GLY N N 111.120 0.050 1 615 132 133 GLY H H 8.300 0.010 1 616 132 133 GLY CA C 47.100 0.200 1 617 132 133 GLY C C 177.050 0.200 1 618 133 134 ASN N N 122.190 0.050 1 619 133 134 ASN H H 7.240 0.010 1 620 133 134 ASN CA C 55.110 0.200 1 621 133 134 ASN CB C 36.910 0.200 1 622 133 134 ASN C C 178.040 0.200 1 623 134 135 VAL N N 124.060 0.050 1 624 134 135 VAL H H 7.700 0.010 1 625 134 135 VAL CA C 66.780 0.200 1 626 134 135 VAL CB C 30.050 0.200 1 627 134 135 VAL C C 179.850 0.200 1 628 135 136 LYS N N 124.160 0.050 1 629 135 136 LYS H H 8.350 0.010 1 630 135 136 LYS CA C 60.640 0.200 1 631 135 136 LYS CB C 31.460 0.200 1 632 135 136 LYS C C 177.920 0.200 1 633 136 137 ALA N N 121.910 0.050 1 634 136 137 ALA H H 7.650 0.010 1 635 136 137 ALA CA C 54.930 0.200 1 636 136 137 ALA CB C 17.890 0.200 1 637 136 137 ALA C C 180.950 0.200 1 638 137 138 ARG N N 118.420 0.050 1 639 137 138 ARG H H 8.130 0.010 1 640 137 138 ARG CA C 58.870 0.200 1 641 137 138 ARG CB C 30.740 0.200 1 642 137 138 ARG C C 177.810 0.200 1 643 138 139 THR N N 122.520 0.050 1 644 138 139 THR H H 8.720 0.010 1 645 138 139 THR CA C 67.810 0.200 1 646 138 139 THR CB C 66.480 0.200 1 647 138 139 THR C C 176.680 0.200 1 648 139 140 ARG N N 123.200 0.050 1 649 139 140 ARG H H 8.100 0.010 1 650 139 140 ARG CA C 61.160 0.200 1 651 139 140 ARG CB C 28.400 0.200 1 652 139 140 ARG C C 179.160 0.200 1 653 140 141 MET N N 125.150 0.050 1 654 140 141 MET H H 7.210 0.010 1 655 140 141 MET CA C 59.980 0.200 1 656 140 141 MET CB C 28.290 0.200 1 657 140 141 MET C C 178.130 0.200 1 658 141 142 ILE N N 121.800 0.050 1 659 141 142 ILE H H 7.990 0.010 1 660 141 142 ILE CA C 66.780 0.200 1 661 141 142 ILE CB C 35.960 0.200 1 662 141 142 ILE C C 175.970 0.200 1 663 142 143 ALA N N 122.970 0.050 1 664 142 143 ALA H H 8.510 0.010 1 665 142 143 ALA CA C 55.450 0.200 1 666 142 143 ALA CB C 17.900 0.200 1 667 142 143 ALA C C 179.230 0.200 1 668 143 144 GLN N N 117.280 0.050 1 669 143 144 GLN H H 7.890 0.010 1 670 143 144 GLN CA C 60.120 0.200 1 671 143 144 GLN CB C 29.710 0.200 1 672 143 144 GLN C C 177.720 0.200 1 673 144 145 TYR N N 118.150 0.050 1 674 144 145 TYR H H 8.780 0.010 1 675 144 145 TYR CA C 63.290 0.200 1 676 144 145 TYR CB C 37.450 0.200 1 677 144 145 TYR C C 179.700 0.200 1 678 145 146 ALA N N 130.060 0.050 1 679 145 146 ALA H H 8.800 0.010 1 680 145 146 ALA CA C 54.810 0.200 1 681 145 146 ALA CB C 17.010 0.200 1 682 145 146 ALA C C 178.440 0.200 1 683 146 147 ILE N N 120.590 0.050 1 684 146 147 ILE H H 7.740 0.010 1 685 146 147 ILE CA C 64.890 0.200 1 686 146 147 ILE CB C 37.900 0.200 1 687 146 147 ILE C C 178.990 0.200 1 688 147 148 GLY N N 106.930 0.050 1 689 147 148 GLY H H 8.780 0.010 1 690 147 148 GLY CA C 47.230 0.200 1 691 147 148 GLY C C 176.430 0.200 1 692 148 149 GLY N N 111.770 0.050 1 693 148 149 GLY H H 8.730 0.010 1 694 148 149 GLY CA C 46.160 0.200 1 695 148 149 GLY C C 177.040 0.200 1 696 149 150 GLN N N 124.050 0.050 1 697 149 150 GLN H H 8.430 0.010 1 698 149 150 GLN CA C 58.430 0.200 1 699 149 150 GLN CB C 30.540 0.200 1 700 149 150 GLN C C 178.160 0.200 1 701 150 151 GLU N N 114.870 0.050 1 702 150 151 GLU H H 8.100 0.010 1 703 150 151 GLU CA C 54.700 0.200 1 704 150 151 GLU CB C 29.760 0.200 1 705 150 151 GLU C C 176.050 0.200 1 706 151 152 GLY N N 112.470 0.050 1 707 151 152 GLY H H 7.640 0.010 1 708 151 152 GLY CA C 46.840 0.200 1 709 151 152 GLY C C 174.030 0.200 1 710 152 153 LEU N N 119.350 0.050 1 711 152 153 LEU H H 8.650 0.010 1 712 152 153 LEU CA C 51.910 0.200 1 713 152 153 LEU CB C 43.200 0.200 1 714 152 153 LEU C C 176.110 0.200 1 715 153 154 LEU N N 122.220 0.050 1 716 153 154 LEU H H 8.370 0.010 1 717 153 154 LEU CA C 53.060 0.200 1 718 153 154 LEU CB C 43.210 0.200 1 719 153 154 LEU C C 176.110 0.200 1 720 154 155 VAL N N 125.620 0.050 1 721 154 155 VAL H H 9.500 0.010 1 722 154 155 VAL CA C 62.010 0.200 1 723 154 155 VAL CB C 31.600 0.200 1 724 154 155 VAL C C 177.650 0.200 1 725 155 156 LEU N N 131.870 0.050 1 726 155 156 LEU H H 8.410 0.010 1 727 155 156 LEU CA C 53.750 0.200 1 728 155 156 LEU CB C 43.570 0.200 1 729 155 156 LEU C C 174.810 0.200 1 730 156 157 GLY N N 107.030 0.050 1 731 156 157 GLY H H 8.040 0.010 1 732 156 157 GLY CA C 42.870 0.200 1 733 156 157 GLY C C 175.460 0.200 1 734 157 158 THR N N 111.910 0.050 1 735 157 158 THR H H 8.390 0.010 1 736 157 158 THR CA C 61.180 0.200 1 737 157 158 THR CB C 67.260 0.200 1 738 157 158 THR C C 175.450 0.200 1 739 162 163 GLU CA C 55.840 0.200 1 740 162 163 GLU CB C 31.980 0.200 1 741 162 163 GLU C C 177.740 0.200 1 742 163 164 ALA N N 125.120 0.050 1 743 163 164 ALA H H 8.570 0.010 1 744 163 164 ALA CA C 55.160 0.200 1 745 163 164 ALA C C 180.620 0.200 1 746 164 165 VAL N N 116.000 0.050 1 747 164 165 VAL H H 7.890 0.010 1 748 164 165 VAL CA C 63.450 0.200 1 749 164 165 VAL CB C 30.190 0.200 1 750 164 165 VAL C C 172.440 0.200 1 751 165 166 THR N N 104.330 0.050 1 752 165 166 THR H H 6.490 0.010 1 753 165 166 THR CA C 60.550 0.200 1 754 165 166 THR CB C 68.310 0.200 1 755 165 166 THR C C 176.800 0.200 1 756 166 167 GLY N N 110.340 0.050 1 757 166 167 GLY H H 7.730 0.010 1 758 166 167 GLY CA C 46.840 0.200 1 759 166 167 GLY C C 174.290 0.200 1 760 167 168 PHE N N 122.890 0.050 1 761 167 168 PHE H H 8.480 0.010 1 762 167 168 PHE CA C 57.070 0.200 1 763 167 168 PHE CB C 37.270 0.200 1 764 167 168 PHE C C 175.430 0.200 1 765 168 169 PHE N N 118.540 0.050 1 766 168 169 PHE H H 7.560 0.010 1 767 168 169 PHE CA C 55.490 0.200 1 768 168 169 PHE CB C 37.980 0.200 1 769 168 169 PHE C C 173.800 0.200 1 770 169 170 THR N N 121.110 0.050 1 771 169 170 THR H H 9.740 0.010 1 772 169 170 THR CA C 62.740 0.200 1 773 169 170 THR CB C 68.960 0.200 1 774 169 170 THR C C 175.840 0.200 1 775 170 171 LYS N N 136.660 0.050 1 776 170 171 LYS H H 9.400 0.010 1 777 170 171 LYS CA C 57.470 0.200 1 778 170 171 LYS CB C 31.880 0.200 1 779 170 171 LYS C C 176.690 0.200 1 780 171 172 TYR N N 126.060 0.050 1 781 171 172 TYR H H 9.520 0.010 1 782 171 172 TYR CA C 57.400 0.200 1 783 171 172 TYR CB C 34.550 0.200 1 784 171 172 TYR C C 171.660 0.200 1 785 172 173 GLY N N 103.980 0.050 1 786 172 173 GLY H H 7.680 0.010 1 787 172 173 GLY CA C 44.510 0.200 1 788 172 173 GLY C C 173.700 0.200 1 789 173 174 ASP N N 129.900 0.050 1 790 173 174 ASP H H 9.180 0.010 1 791 173 174 ASP CA C 55.320 0.200 1 792 173 174 ASP CB C 36.890 0.200 1 793 173 174 ASP C C 177.310 0.200 1 794 174 175 GLY N N 103.490 0.050 1 795 174 175 GLY H H 7.650 0.010 1 796 174 175 GLY CA C 44.990 0.200 1 797 174 175 GLY C C 175.150 0.200 1 798 175 176 GLY N N 111.010 0.050 1 799 175 176 GLY H H 7.690 0.010 1 800 175 176 GLY CA C 45.640 0.200 1 801 175 176 GLY C C 169.600 0.200 1 802 176 177 ALA N N 126.580 0.050 1 803 176 177 ALA H H 7.300 0.010 1 804 176 177 ALA CA C 51.210 0.200 1 805 176 177 ALA CB C 20.830 0.200 1 806 176 177 ALA C C 176.610 0.200 1 807 177 178 ASP N N 118.290 0.050 1 808 177 178 ASP H H 9.180 0.010 1 809 177 178 ASP CA C 55.730 0.200 1 810 177 178 ASP CB C 41.840 0.200 1 811 177 178 ASP C C 176.590 0.200 1 812 178 179 LEU N N 118.990 0.050 1 813 178 179 LEU H H 7.490 0.010 1 814 178 179 LEU CA C 55.380 0.200 1 815 178 179 LEU CB C 41.590 0.200 1 816 178 179 LEU C C 175.140 0.200 1 817 179 180 LEU N N 120.220 0.050 1 818 179 180 LEU H H 8.410 0.010 1 819 179 180 LEU CA C 51.990 0.200 1 820 179 180 LEU CB C 41.670 0.200 1 821 179 180 LEU C C 175.810 0.200 1 822 180 181 PRO CA C 63.500 0.200 1 823 180 181 PRO C C 176.510 0.200 1 824 181 182 LEU N N 118.830 0.050 1 825 181 182 LEU H H 9.890 0.010 1 826 181 182 LEU CA C 53.920 0.200 1 827 181 182 LEU CB C 38.990 0.200 1 828 181 182 LEU C C 175.330 0.200 1 829 182 183 THR N N 116.210 0.050 1 830 182 183 THR H H 6.820 0.010 1 831 182 183 THR CA C 66.380 0.200 1 832 182 183 THR CB C 68.940 0.200 1 833 182 183 THR C C 175.230 0.200 1 834 183 184 GLY N N 118.410 0.050 1 835 183 184 GLY H H 9.370 0.010 1 836 183 184 GLY CA C 44.790 0.200 1 837 183 184 GLY C C 174.840 0.200 1 838 184 185 LEU N N 120.710 0.050 1 839 184 185 LEU H H 7.780 0.010 1 840 184 185 LEU CA C 54.940 0.200 1 841 184 185 LEU CB C 41.950 0.200 1 842 184 185 LEU C C 178.110 0.200 1 843 185 186 THR N N 112.250 0.050 1 844 185 186 THR H H 7.610 0.010 1 845 185 186 THR CA C 60.550 0.200 1 846 185 186 THR CB C 67.040 0.200 1 847 186 187 LYS CA C 60.250 0.200 1 848 186 187 LYS CB C 30.650 0.200 1 849 186 187 LYS C C 181.660 0.200 1 850 187 188 ARG N N 123.700 0.050 1 851 187 188 ARG H H 10.080 0.010 1 852 187 188 ARG CA C 58.620 0.200 1 853 187 188 ARG CB C 29.130 0.200 1 854 187 188 ARG C C 179.670 0.200 1 855 188 189 GLN N N 121.960 0.050 1 856 188 189 GLN H H 7.070 0.010 1 857 188 189 GLN CA C 58.260 0.200 1 858 188 189 GLN CB C 27.350 0.200 1 859 188 189 GLN C C 179.190 0.200 1 860 189 190 GLY N N 109.090 0.050 1 861 189 190 GLY H H 7.980 0.010 1 862 189 190 GLY CA C 46.610 0.200 1 863 189 190 GLY C C 175.520 0.200 1 864 190 191 ARG N N 122.380 0.050 1 865 190 191 ARG H H 7.560 0.010 1 866 190 191 ARG CA C 60.150 0.200 1 867 190 191 ARG CB C 28.930 0.200 1 868 190 191 ARG C C 178.020 0.200 1 869 191 192 THR N N 118.220 0.050 1 870 191 192 THR H H 7.850 0.010 1 871 191 192 THR CA C 66.210 0.200 1 872 191 192 THR CB C 67.430 0.200 1 873 191 192 THR C C 177.100 0.200 1 874 192 193 LEU N N 123.510 0.050 1 875 192 193 LEU H H 7.850 0.010 1 876 192 193 LEU CA C 59.050 0.200 1 877 192 193 LEU CB C 40.200 0.200 1 878 192 193 LEU C C 178.440 0.200 1 879 193 194 LEU N N 120.550 0.050 1 880 193 194 LEU H H 7.810 0.010 1 881 193 194 LEU CA C 57.880 0.200 1 882 193 194 LEU CB C 40.300 0.200 1 883 193 194 LEU C C 178.140 0.200 1 884 194 195 LYS N N 121.840 0.050 1 885 194 195 LYS H H 7.820 0.010 1 886 194 195 LYS CA C 59.210 0.200 1 887 194 195 LYS CB C 31.090 0.200 1 888 194 195 LYS C C 180.830 0.200 1 889 195 196 GLU N N 124.660 0.050 1 890 195 196 GLU H H 7.750 0.010 1 891 195 196 GLU CA C 58.010 0.200 1 892 195 196 GLU CB C 27.950 0.200 1 893 195 196 GLU C C 178.020 0.200 1 894 196 197 LEU N N 118.440 0.050 1 895 196 197 LEU H H 7.790 0.010 1 896 196 197 LEU CA C 54.850 0.200 1 897 196 197 LEU CB C 42.800 0.200 1 898 196 197 LEU C C 177.040 0.200 1 899 197 198 GLY N N 109.690 0.050 1 900 197 198 GLY H H 7.850 0.010 1 901 197 198 GLY CA C 45.210 0.200 1 902 197 198 GLY C C 175.010 0.200 1 903 198 199 ALA N N 124.340 0.050 1 904 198 199 ALA H H 7.650 0.010 1 905 198 199 ALA CA C 50.260 0.200 1 906 198 199 ALA CB C 16.940 0.200 1 907 198 199 ALA C C 174.360 0.200 1 908 199 200 PRO CA C 62.210 0.200 1 909 199 200 PRO CB C 31.110 0.200 1 910 199 200 PRO C C 177.340 0.200 1 911 200 201 GLU N N 125.490 0.050 1 912 200 201 GLU H H 8.430 0.010 1 913 200 201 GLU CA C 58.940 0.200 1 914 200 201 GLU CB C 28.460 0.200 1 915 200 201 GLU C C 177.360 0.200 1 916 201 202 ARG N N 117.920 0.050 1 917 201 202 ARG H H 8.110 0.010 1 918 201 202 ARG CA C 57.330 0.200 1 919 201 202 ARG CB C 29.260 0.200 1 920 201 202 ARG C C 176.870 0.200 1 921 202 203 LEU N N 115.070 0.050 1 922 202 203 LEU H H 7.450 0.010 1 923 202 203 LEU CA C 55.050 0.200 1 924 202 203 LEU CB C 40.510 0.200 1 925 202 203 LEU C C 176.640 0.200 1 926 203 204 TYR N N 113.180 0.050 1 927 203 204 TYR H H 7.100 0.010 1 928 203 204 TYR CA C 56.550 0.200 1 929 203 204 TYR CB C 38.580 0.200 1 930 203 204 TYR C C 174.230 0.200 1 931 204 205 LEU N N 125.520 0.050 1 932 204 205 LEU H H 7.590 0.010 1 933 204 205 LEU CA C 54.520 0.200 1 934 204 205 LEU CB C 41.260 0.200 1 935 204 205 LEU C C 176.750 0.200 1 936 205 206 LYS N N 123.230 0.050 1 937 205 206 LYS H H 7.690 0.010 1 938 205 206 LYS CA C 55.720 0.200 1 939 205 206 LYS CB C 32.360 0.200 1 940 205 206 LYS C C 176.050 0.200 1 941 206 207 GLU N N 125.980 0.050 1 942 206 207 GLU H H 8.360 0.010 1 943 206 207 GLU CA C 54.040 0.200 1 944 206 207 GLU CB C 28.870 0.200 1 945 206 207 GLU C C 174.810 0.200 1 946 207 208 PRO CA C 63.050 0.200 1 947 207 208 PRO CB C 31.180 0.200 1 948 207 208 PRO C C 177.110 0.200 1 949 208 209 THR N N 115.190 0.050 1 950 208 209 THR H H 7.980 0.010 1 951 208 209 THR CA C 61.430 0.200 1 952 208 209 THR CB C 69.280 0.200 1 953 208 209 THR C C 174.460 0.200 1 954 209 210 ALA N N 127.480 0.050 1 955 209 210 ALA H H 8.140 0.010 1 956 209 210 ALA CA C 52.330 0.200 1 957 209 210 ALA CB C 18.520 0.200 1 958 209 210 ALA C C 177.350 0.200 1 959 210 211 ASP N N 120.960 0.050 1 960 210 211 ASP H H 8.110 0.010 1 961 210 211 ASP CA C 54.130 0.200 1 962 210 211 ASP CB C 40.470 0.200 1 963 210 211 ASP C C 176.180 0.200 1 964 211 212 LEU N N 123.330 0.050 1 965 211 212 LEU H H 7.930 0.010 1 966 211 212 LEU CA C 55.080 0.200 1 967 211 212 LEU CB C 41.080 0.200 1 968 211 212 LEU C C 177.470 0.200 1 969 212 213 LEU N N 123.110 0.050 1 970 212 213 LEU H H 8.050 0.010 1 971 212 213 LEU CA C 55.080 0.200 1 972 212 213 LEU CB C 41.070 0.200 1 973 212 213 LEU C C 177.120 0.200 1 974 213 214 ASP N N 120.130 0.050 1 975 213 214 ASP H H 8.190 0.010 1 976 213 214 ASP CA C 54.150 0.200 1 977 213 214 ASP CB C 40.630 0.200 1 978 213 214 ASP C C 175.960 0.200 1 979 214 215 GLU N N 121.540 0.050 1 980 214 215 GLU H H 8.040 0.010 1 981 214 215 GLU CA C 56.120 0.200 1 982 214 215 GLU CB C 29.540 0.200 1 983 215 216 LYS N N 122.700 0.050 1 984 215 216 LYS H H 8.250 0.010 1 985 215 216 LYS CA C 53.760 0.200 1 986 215 216 LYS CB C 31.570 0.200 1 987 216 217 PRO CA C 62.870 0.200 1 988 216 217 PRO CB C 31.150 0.200 1 989 216 217 PRO C C 177.010 0.200 1 990 217 218 GLN N N 121.900 0.050 1 991 217 218 GLN H H 8.350 0.010 1 992 217 218 GLN CA C 55.630 0.200 1 993 217 218 GLN CB C 28.780 0.200 1 994 217 218 GLN C C 175.980 0.200 1 995 218 219 GLN N N 121.120 0.050 1 996 218 219 GLN H H 8.410 0.010 1 997 218 219 GLN CA C 55.580 0.200 1 998 218 219 GLN CB C 28.730 0.200 1 999 218 219 GLN C C 175.910 0.200 1 1000 219 220 SER N N 118.410 0.050 1 1001 219 220 SER H H 8.180 0.010 1 1002 219 220 SER CA C 58.140 0.200 1 1003 219 220 SER CB C 63.170 0.200 1 1004 219 220 SER C C 174.360 0.200 1 1005 220 221 ASP N N 123.600 0.050 1 1006 220 221 ASP H H 8.240 0.010 1 1007 220 221 ASP CA C 54.510 0.200 1 1008 220 221 ASP CB C 40.260 0.200 1 1009 220 221 ASP C C 176.530 0.200 1 1010 221 222 GLU N N 121.370 0.050 1 1011 221 222 GLU H H 8.140 0.010 1 1012 221 222 GLU CA C 57.150 0.200 1 1013 221 222 GLU CB C 29.370 0.200 1 1014 221 222 GLU C C 177.110 0.200 1 1015 222 223 THR N N 113.880 0.050 1 1016 222 223 THR H H 7.760 0.010 1 1017 222 223 THR CA C 61.990 0.200 1 1018 222 223 THR CB C 69.810 0.200 1 1019 222 223 THR C C 175.410 0.200 1 1020 223 224 GLU N N 123.630 0.050 1 1021 223 224 GLU H H 8.200 0.010 1 1022 223 224 GLU CA C 56.800 0.200 1 1023 223 224 GLU CB C 29.040 0.200 1 1024 223 224 GLU C C 176.720 0.200 1 1025 224 225 LEU N N 122.270 0.050 1 1026 224 225 LEU H H 7.950 0.010 1 1027 224 225 LEU CA C 55.330 0.200 1 1028 224 225 LEU CB C 42.060 0.200 1 1029 224 225 LEU C C 177.710 0.200 1 1030 225 226 GLY N N 108.830 0.050 1 1031 225 226 GLY H H 8.170 0.010 1 1032 225 226 GLY CA C 45.500 0.200 1 1033 225 226 GLY C C 173.520 0.200 1 1034 226 227 ILE N N 117.780 0.050 1 1035 226 227 ILE H H 6.910 0.010 1 1036 226 227 ILE CA C 59.020 0.200 1 1037 226 227 ILE CB C 39.560 0.200 1 1038 226 227 ILE C C 174.690 0.200 1 1039 227 228 SER N N 123.910 0.050 1 1040 227 228 SER H H 9.010 0.010 1 1041 227 228 SER CA C 56.980 0.200 1 1042 227 228 SER CB C 65.140 0.200 1 1043 227 228 SER C C 175.670 0.200 1 1044 228 229 TYR N N 120.790 0.050 1 1045 228 229 TYR H H 8.630 0.010 1 1046 228 229 TYR CA C 61.700 0.200 1 1047 228 229 TYR CB C 36.670 0.200 1 1048 228 229 TYR C C 178.640 0.200 1 1049 229 230 ASP N N 120.640 0.050 1 1050 229 230 ASP H H 8.240 0.010 1 1051 229 230 ASP CA C 57.480 0.200 1 1052 229 230 ASP CB C 39.940 0.200 1 1053 229 230 ASP C C 177.630 0.200 1 1054 230 231 GLU N N 121.200 0.050 1 1055 230 231 GLU H H 7.450 0.010 1 1056 230 231 GLU CA C 59.170 0.200 1 1057 230 231 GLU CB C 29.360 0.200 1 1058 230 231 GLU C C 178.300 0.200 1 1059 231 232 ILE N N 121.410 0.050 1 1060 231 232 ILE H H 7.630 0.010 1 1061 231 232 ILE CA C 65.670 0.200 1 1062 231 232 ILE CB C 37.570 0.200 1 1063 231 232 ILE C C 177.480 0.200 1 1064 232 233 ASP N N 121.770 0.050 1 1065 232 233 ASP H H 8.270 0.010 1 1066 232 233 ASP CA C 57.730 0.200 1 1067 232 233 ASP CB C 39.230 0.200 1 1068 232 233 ASP C C 178.560 0.200 1 1069 233 234 ASP N N 120.520 0.050 1 1070 233 234 ASP H H 8.210 0.010 1 1071 233 234 ASP CA C 57.540 0.200 1 1072 233 234 ASP CB C 39.400 0.200 1 1073 233 234 ASP C C 177.110 0.200 1 1074 234 235 TYR N N 121.590 0.050 1 1075 234 235 TYR H H 7.930 0.010 1 1076 234 235 TYR CA C 60.620 0.200 1 1077 234 235 TYR CB C 37.630 0.200 1 1078 234 235 TYR C C 179.480 0.200 1 1079 235 236 LEU N N 120.900 0.050 1 1080 235 236 LEU H H 8.390 0.010 1 1081 235 236 LEU CA C 56.630 0.200 1 1082 235 236 LEU CB C 41.830 0.200 1 1083 235 236 LEU C C 175.140 0.200 1 1084 236 237 GLU N N 112.860 0.050 1 1085 236 237 GLU H H 7.830 0.010 1 1086 236 237 GLU CA C 55.470 0.200 1 1087 236 237 GLU CB C 28.760 0.200 1 1088 236 237 GLU C C 176.920 0.200 1 1089 237 238 GLY N N 108.750 0.050 1 1090 237 238 GLY H H 7.500 0.010 1 1091 237 238 GLY CA C 45.610 0.200 1 1092 237 238 GLY C C 175.130 0.200 1 1093 238 239 LYS N N 122.140 0.050 1 1094 238 239 LYS H H 8.010 0.010 1 1095 238 239 LYS CA C 55.140 0.200 1 1096 238 239 LYS CB C 32.180 0.200 1 1097 238 239 LYS C C 175.340 0.200 1 1098 239 240 GLU N N 121.410 0.050 1 1099 239 240 GLU H H 8.000 0.010 1 1100 239 240 GLU CA C 56.530 0.200 1 1101 239 240 GLU CB C 28.810 0.200 1 1102 239 240 GLU C C 176.810 0.200 1 1103 240 241 VAL N N 120.160 0.050 1 1104 240 241 VAL H H 8.170 0.010 1 1105 240 241 VAL CA C 58.500 0.200 1 1106 240 241 VAL CB C 35.110 0.200 1 1107 240 241 VAL C C 175.960 0.200 1 1108 241 242 SER N N 119.530 0.050 1 1109 241 242 SER H H 8.560 0.010 1 1110 241 242 SER CA C 57.500 0.200 1 1111 241 242 SER CB C 63.620 0.200 1 1112 241 242 SER C C 175.160 0.200 1 1113 242 243 ALA N N 127.680 0.050 1 1114 242 243 ALA H H 8.730 0.010 1 1115 242 243 ALA CA C 54.340 0.200 1 1116 242 243 ALA CB C 17.200 0.200 1 1117 242 243 ALA C C 179.570 0.200 1 1118 243 244 LYS N N 117.490 0.050 1 1119 243 244 LYS H H 7.860 0.010 1 1120 243 244 LYS CA C 58.490 0.200 1 1121 243 244 LYS CB C 31.500 0.200 1 1122 243 244 LYS C C 179.300 0.200 1 1123 244 245 VAL N N 121.660 0.050 1 1124 244 245 VAL H H 7.290 0.010 1 1125 244 245 VAL CA C 65.550 0.200 1 1126 244 245 VAL CB C 31.420 0.200 1 1127 244 245 VAL C C 177.110 0.200 1 1128 245 246 SER N N 115.580 0.050 1 1129 245 246 SER H H 8.020 0.010 1 1130 245 246 SER CA C 65.550 0.200 1 1131 245 246 SER C C 176.240 0.200 1 1132 246 247 GLU N N 121.710 0.050 1 1133 246 247 GLU H H 8.270 0.010 1 1134 246 247 GLU CA C 59.120 0.200 1 1135 246 247 GLU CB C 28.790 0.200 1 1136 246 247 GLU C C 179.240 0.200 1 1137 247 248 ALA N N 121.600 0.050 1 1138 247 248 ALA H H 7.260 0.010 1 1139 247 248 ALA CA C 54.430 0.200 1 1140 247 248 ALA CB C 17.890 0.200 1 1141 247 248 ALA C C 177.220 0.200 1 1142 248 249 LEU N N 119.440 0.050 1 1143 248 249 LEU H H 8.080 0.010 1 1144 248 249 LEU CA C 57.110 0.200 1 1145 248 249 LEU CB C 40.220 0.200 1 1146 248 249 LEU C C 178.670 0.200 1 1147 249 250 GLU N N 120.680 0.050 1 1148 249 250 GLU H H 8.330 0.010 1 1149 249 250 GLU CA C 59.620 0.200 1 1150 249 250 GLU CB C 27.450 0.200 1 1151 249 250 GLU C C 179.790 0.200 1 1152 250 251 LYS N N 121.740 0.050 1 1153 250 251 LYS H H 7.660 0.010 1 1154 250 251 LYS CA C 59.010 0.200 1 1155 250 251 LYS CB C 31.350 0.200 1 1156 250 251 LYS C C 179.210 0.200 1 1157 251 252 ARG N N 120.330 0.050 1 1158 251 252 ARG H H 7.770 0.010 1 1159 251 252 ARG CA C 56.940 0.200 1 1160 251 252 ARG CB C 27.800 0.200 1 1161 251 252 ARG C C 179.140 0.200 1 1162 252 253 TYR N N 125.150 0.050 1 1163 252 253 TYR H H 9.010 0.010 1 1164 252 253 TYR CA C 61.990 0.200 1 1165 252 253 TYR CB C 37.820 0.200 1 1166 252 253 TYR C C 179.470 0.200 1 1167 253 254 SER N N 115.770 0.050 1 1168 253 254 SER H H 7.900 0.010 1 1169 253 254 SER CA C 61.290 0.200 1 1170 253 254 SER CB C 62.300 0.200 1 1171 253 254 SER C C 177.480 0.200 1 1172 254 255 MET N N 119.900 0.050 1 1173 254 255 MET H H 7.990 0.010 1 1174 254 255 MET CA C 57.460 0.200 1 1175 254 255 MET CB C 33.030 0.200 1 1176 254 255 MET C C 177.890 0.200 1 1177 255 256 THR N N 107.930 0.050 1 1178 255 256 THR H H 7.460 0.010 1 1179 255 256 THR CA C 60.960 0.200 1 1180 255 256 THR CB C 68.730 0.200 1 1181 255 256 THR C C 173.900 0.200 1 1182 256 257 GLU N N 128.240 0.050 1 1183 256 257 GLU H H 7.020 0.010 1 1184 256 257 GLU CA C 59.190 0.200 1 1185 256 257 GLU CB C 28.320 0.200 1 1186 256 257 GLU C C 177.900 0.200 1 1187 257 258 HIS N N 115.940 0.050 1 1188 257 258 HIS H H 8.540 0.010 1 1189 257 258 HIS CA C 57.230 0.200 1 1190 257 258 HIS CB C 30.020 0.200 1 1191 257 258 HIS C C 176.950 0.200 1 1192 258 259 LYS N N 118.070 0.050 1 1193 258 259 LYS H H 7.070 0.010 1 1194 258 259 LYS CA C 57.300 0.200 1 1195 258 259 LYS CB C 31.960 0.200 1 1196 258 259 LYS C C 177.080 0.200 1 1197 259 260 ARG N N 120.410 0.050 1 1198 259 260 ARG H H 7.650 0.010 1 1199 259 260 ARG CA C 55.200 0.200 1 1200 259 260 ARG CB C 30.070 0.200 1 1201 259 260 ARG C C 173.170 0.200 1 1202 260 261 GLN N N 118.030 0.050 1 1203 260 261 GLN H H 6.540 0.010 1 1204 260 261 GLN CA C 52.680 0.200 1 1205 260 261 GLN CB C 30.970 0.200 1 1206 260 261 GLN C C 176.340 0.200 1 1207 261 262 VAL N N 116.040 0.050 1 1208 261 262 VAL H H 8.110 0.010 1 1209 261 262 VAL CA C 61.580 0.200 1 1210 261 262 VAL CB C 27.940 0.200 1 1211 261 262 VAL C C 175.220 0.200 1 1212 262 263 PRO CA C 64.320 0.200 1 1213 262 263 PRO CB C 30.100 0.200 1 1214 262 263 PRO C C 174.780 0.200 1 1215 263 264 ALA N N 125.070 0.050 1 1216 263 264 ALA H H 7.060 0.010 1 1217 263 264 ALA CA C 52.980 0.200 1 1218 263 264 ALA CB C 19.700 0.200 1 1219 263 264 ALA C C 175.820 0.200 1 1220 264 265 SER N N 118.810 0.050 1 1221 264 265 SER H H 9.240 0.010 1 1222 264 265 SER CA C 56.650 0.200 1 1223 264 265 SER CB C 67.970 0.200 1 1224 264 265 SER C C 175.310 0.200 1 1225 265 266 MET N N 118.470 0.050 1 1226 265 266 MET H H 7.420 0.010 1 1227 265 266 MET CA C 56.680 0.200 1 1228 265 266 MET CB C 31.100 0.200 1 1229 265 266 MET C C 174.430 0.200 1 1230 266 267 PHE N N 120.260 0.050 1 1231 266 267 PHE H H 7.410 0.010 1 1232 266 267 PHE CA C 57.330 0.200 1 1233 266 267 PHE CB C 37.570 0.200 1 1234 266 267 PHE C C 174.980 0.200 1 1235 267 268 ASP N N 121.660 0.050 1 1236 267 268 ASP H H 7.200 0.010 1 1237 267 268 ASP CA C 54.050 0.200 1 1238 267 268 ASP CB C 43.170 0.200 1 1239 267 268 ASP C C 174.750 0.200 1 1240 268 269 ASP N N 117.750 0.050 1 1241 268 269 ASP H H 8.570 0.010 1 1242 268 269 ASP CA C 53.980 0.200 1 1243 268 269 ASP CB C 41.690 0.200 1 1244 268 269 ASP C C 179.660 0.200 1 1245 269 270 TRP N N 119.560 0.050 1 1246 269 270 TRP H H 7.370 0.010 1 1247 269 270 TRP CA C 58.400 0.200 1 1248 269 270 TRP CB C 27.960 0.200 1 1249 269 270 TRP C C 176.280 0.200 1 1250 270 271 TRP N N 118.020 0.050 1 1251 270 271 TRP H H 5.670 0.010 1 1252 270 271 TRP CA C 54.000 0.200 1 1253 270 271 TRP CB C 28.010 0.200 1 1254 270 271 TRP C C 175.270 0.200 1 1255 271 272 LYS N N 127.950 0.050 1 1256 271 272 LYS H H 6.200 0.010 1 1257 271 272 LYS CA C 58.910 0.200 1 1258 271 272 LYS CB C 32.310 0.200 1 1259 271 272 LYS C C 181.920 0.200 1 stop_ save_