data_7265 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone and Selected Sidechain 1H, 13C, and 15N Chemical Shift Assignments of the beta-1,4-glycosidase Cex from Cellulomonas fimi ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Poon David "K.Y." . 2 Ludwiczek Martin L. . 3 Schubert Mario . . 4 Kwan Emily M. . 5 Withers Stephen G. . 6 McIntosh Lawrence P. . stop_ _BMRB_accession_number 7265 _BMRB_flat_file_name bmr7265.str _Entry_type new _Submission_date 2006-08-15 _Accession_date 2006-08-16 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 631 "1H chemical shifts" 313 "15N chemical shifts" 308 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-17 update BMRB "complete entry citation" 2006-11-13 original author "original release" stop_ loop_ _Related_BMRB_accession_number _Relationship 7264 "Characterization of a beta-(1,4)-Glycosidase" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; NMR spectroscopic characterization of a beta-(1,4)-glycosidase along its reaction pathway: stabilization upon formation of the glycosyl-enzyme intermediate. ; _Citation_status published _Citation_type journal _PubMed_ID 17253772 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Poon David "K. Y." . 2 Ludwiczek Martin L. . 3 Schubert Mario . . 4 Kwan Emily M. . 5 Withers Stephen G. . 6 McIntosh Lawrence "K. Y." . stop_ _Journal_abbreviation Biochemistry _Journal_volume 46 _Journal_issue 7 _Page_first 1759 _Page_last 1770 _Year 2007 save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "Cex catalytic domain" _Abbreviation_common "Cex catalytic domain" _Enzyme_commission_number 3.2.1.91 loop_ _Mol_system_component_name _Mol_label "Cex catalytic domain" $2FCb-CexCD stop_ _System_molecular_weight 34569 _System_physical_state native _System_oligomer_state "protein-inhibitor complex" _System_paramagnetic no _System_thiol_state "all disulfide bound" loop_ _Biological_function Cellulase Xylanase stop_ _Details ; The family 10 catalytic domain of the beta-1,4-glycosidase Cex (or CfXyn10A) from Cellulomonas fimi with a covalently-bound 2-deoxy-2-fluorocellobioside ; save_ ######################## # Monomeric polymers # ######################## save_2FCb-CexCD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 2FCb-CexCD _Molecular_mass 34569 _Mol_thiol_state "all disulfide bound" ############################## # Polymer residue sequence # ############################## _Residue_count 315 _Mol_residue_sequence ; ATTLKEAADGAGRDFGFALD PNRLSEAQYKAIADSEFNLV VAENAMKWDATEPSQNSFSF GAGDRVASYAADTGKELYGH TLVWHSQLPDWAKNLNGSAF ESAMVNHVTKVADHFEGKVA SWDVVNEAFADGGGRRQDSA FQQKLGNGYIETAFRAARAA DPTAKLCINDYNVEGINAKS NSLYDLVKDFKARGVPLDCV GFQSHLIVGQVPGDFRQNLQ RFADLGVDVRITELDIRMRT PSDATKLATQAADYKKVVQA CMQVTRCQGVTVWGITDKYS WVPDVFPGEGAALVWDASYA KKPAYAAVMEAFGAS ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 THR 4 LEU 5 LYS 6 GLU 7 ALA 8 ALA 9 ASP 10 GLY 11 ALA 12 GLY 13 ARG 14 ASP 15 PHE 16 GLY 17 PHE 18 ALA 19 LEU 20 ASP 21 PRO 22 ASN 23 ARG 24 LEU 25 SER 26 GLU 27 ALA 28 GLN 29 TYR 30 LYS 31 ALA 32 ILE 33 ALA 34 ASP 35 SER 36 GLU 37 PHE 38 ASN 39 LEU 40 VAL 41 VAL 42 ALA 43 GLU 44 ASN 45 ALA 46 MET 47 LYS 48 TRP 49 ASP 50 ALA 51 THR 52 GLU 53 PRO 54 SER 55 GLN 56 ASN 57 SER 58 PHE 59 SER 60 PHE 61 GLY 62 ALA 63 GLY 64 ASP 65 ARG 66 VAL 67 ALA 68 SER 69 TYR 70 ALA 71 ALA 72 ASP 73 THR 74 GLY 75 LYS 76 GLU 77 LEU 78 TYR 79 GLY 80 HIS 81 THR 82 LEU 83 VAL 84 TRP 85 HIS 86 SER 87 GLN 88 LEU 89 PRO 90 ASP 91 TRP 92 ALA 93 LYS 94 ASN 95 LEU 96 ASN 97 GLY 98 SER 99 ALA 100 PHE 101 GLU 102 SER 103 ALA 104 MET 105 VAL 106 ASN 107 HIS 108 VAL 109 THR 110 LYS 111 VAL 112 ALA 113 ASP 114 HIS 115 PHE 116 GLU 117 GLY 118 LYS 119 VAL 120 ALA 121 SER 122 TRP 123 ASP 124 VAL 125 VAL 126 ASN 127 GLU 128 ALA 129 PHE 130 ALA 131 ASP 132 GLY 133 GLY 134 GLY 135 ARG 136 ARG 137 GLN 138 ASP 139 SER 140 ALA 141 PHE 142 GLN 143 GLN 144 LYS 145 LEU 146 GLY 147 ASN 148 GLY 149 TYR 150 ILE 151 GLU 152 THR 153 ALA 154 PHE 155 ARG 156 ALA 157 ALA 158 ARG 159 ALA 160 ALA 161 ASP 162 PRO 163 THR 164 ALA 165 LYS 166 LEU 167 CYS 168 ILE 169 ASN 170 ASP 171 TYR 172 ASN 173 VAL 174 GLU 175 GLY 176 ILE 177 ASN 178 ALA 179 LYS 180 SER 181 ASN 182 SER 183 LEU 184 TYR 185 ASP 186 LEU 187 VAL 188 LYS 189 ASP 190 PHE 191 LYS 192 ALA 193 ARG 194 GLY 195 VAL 196 PRO 197 LEU 198 ASP 199 CYS 200 VAL 201 GLY 202 PHE 203 GLN 204 SER 205 HIS 206 LEU 207 ILE 208 VAL 209 GLY 210 GLN 211 VAL 212 PRO 213 GLY 214 ASP 215 PHE 216 ARG 217 GLN 218 ASN 219 LEU 220 GLN 221 ARG 222 PHE 223 ALA 224 ASP 225 LEU 226 GLY 227 VAL 228 ASP 229 VAL 230 ARG 231 ILE 232 THR 233 GLU 234 LEU 235 ASP 236 ILE 237 ARG 238 MET 239 ARG 240 THR 241 PRO 242 SER 243 ASP 244 ALA 245 THR 246 LYS 247 LEU 248 ALA 249 THR 250 GLN 251 ALA 252 ALA 253 ASP 254 TYR 255 LYS 256 LYS 257 VAL 258 VAL 259 GLN 260 ALA 261 CYS 262 MET 263 GLN 264 VAL 265 THR 266 ARG 267 CYS 268 GLN 269 GLY 270 VAL 271 THR 272 VAL 273 TRP 274 GLY 275 ILE 276 THR 277 ASP 278 LYS 279 TYR 280 SER 281 TRP 282 VAL 283 PRO 284 ASP 285 VAL 286 PHE 287 PRO 288 GLY 289 GLU 290 GLY 291 ALA 292 ALA 293 LEU 294 VAL 295 TRP 296 ASP 297 ALA 298 SER 299 TYR 300 ALA 301 LYS 302 LYS 303 PRO 304 ALA 305 TYR 306 ALA 307 ALA 308 VAL 309 MET 310 GLU 311 ALA 312 PHE 313 GLY 314 ALA 315 SER 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 7264 apo-CexCD 100.00 315 100.00 100.00 0.00e+00 PDB 1EXP "Beta-1,4-Glycanase Cex-Cd" 99.05 312 100.00 100.00 0.00e+00 PDB 1FH7 "Crystal Structure Of The Xylanase Cex With Xylobiose- Derived Inhibitor Deoxynojirimycin" 99.05 312 100.00 100.00 0.00e+00 PDB 1FH8 "Crystal Structure Of The Xylanase Cex With Xylobiose- Derived Isofagomine Inhibitor" 99.05 312 100.00 100.00 0.00e+00 PDB 1FH9 "Crystal Structure Of The Xylanase Cex With Xylobiose- Derived Lactam Oxime Inhibitor" 99.05 312 100.00 100.00 0.00e+00 PDB 1FHD "Crystal Structure Of The Xylanase Cex With Xylobiose- Derived Imidazole Inhibitor" 99.05 312 100.00 100.00 0.00e+00 PDB 1J01 "Crystal Structure Of The Xylanase Cex With Xylobiose- Derived Inhibitor Isofagomine Lactam" 99.05 312 100.00 100.00 0.00e+00 PDB 2EXO "Crystal Structure Of The Catalytic Domain Of The Beta-1,4- Glycanase Cex From Cellulomonas Fimi" 99.05 312 100.00 100.00 0.00e+00 PDB 2HIS "Cellulomonas Fimi XylanaseCELLULASE DOUBLE MUTANT E127aH205N WITH COVALENT CELLOBIOSE" 99.05 312 99.36 99.68 0.00e+00 PDB 2XYL "Cellulomonas Fimi XylanaseCELLULASE COMPLEXED WITH 2-Deoxy- 2-Fluoro-Xylobiose" 99.05 312 100.00 100.00 0.00e+00 PDB 3CUF "Cellulomonas Fimi XylanaseCELLULASE CEX (CF XYN10A) IN Complex With Cellobiose-Like Isofagomine" 100.00 315 100.00 100.00 0.00e+00 PDB 3CUG "Cellulomonas Fimi XylanaseCELLULASE CEX (CF XYN10A) IN Complex With Cellotetraose-Like Isofagomine" 100.00 315 100.00 100.00 0.00e+00 PDB 3CUH "Cellulomonas Fimi XylanaseCELLULASE CEX (CF XYN10A) IN Complex With Cellotriose-Like Isofagomine" 100.00 315 100.00 100.00 0.00e+00 PDB 3CUI "Cellulomonas Fimi XylanaseCELLULASE CEX (CF XYN10A) IN Complex With Sulfur Substituted Beta-1,4 Xylotetraose" 100.00 315 100.00 100.00 0.00e+00 PDB 3CUJ "Cellulomonas Fimi XylanaseCELLULASE CEX (CF XYN10A) IN Complex With Sulfur Substituted Beta-1,4 Xylopentaose" 100.00 315 100.00 100.00 0.00e+00 GB AAA56791 "exoglucanase [Cellulomonas fimi]" 100.00 484 99.05 99.05 0.00e+00 GB AAA56792 "exo-beta-1,4-glucanase [Cellulomonas fimi]" 100.00 485 100.00 100.00 0.00e+00 GB AEA30147 "exoglucanase [Cellulomonas fimi ATCC 484]" 100.00 485 100.00 100.00 0.00e+00 GB AEE45406 "glycoside hydrolase family 10 [Cellulomonas fimi ATCC 484]" 100.00 510 100.00 100.00 0.00e+00 PRF 1211268A exoglucanase 100.00 484 99.05 99.05 0.00e+00 REF WP_013770432 "endo-1,4-beta-xylanase [Cellulomonas fimi]" 100.00 510 100.00 100.00 0.00e+00 REF YP_004452793 "glycoside hydrolase family 10 [Cellulomonas fimi ATCC 484]" 100.00 510 100.00 100.00 0.00e+00 SP P07986 "RecName: Full=Exoglucanase/xylanase; Includes: RecName: Full=Exoglucanase; AltName: Full=1,4-beta-cellobiohydrolase; AltName: F" 100.00 484 99.05 99.05 0.00e+00 stop_ save_ ############# # Ligands # ############# save_2FCb _Saveframe_category ligand _Mol_type complex _Name_common 2-fluoro-cellobioside _Mol_charge 0 _Mol_paramagnetic no _Mol_aromatic no save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "Cex catalytic domain" 167 CYS SG "Cex catalytic domain" 199 CYS SG single disulfide "Cex catalytic domain" 261 CYS SG "Cex catalytic domain" 267 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $2FCb-CexCD "Cellulomonas fimi" 1708 Bacteria Actinobacteria Cellulomonas fimi 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 $2FCb-CexCD "recombinant technology" "E. coli" Escherichia coli BL21 plasmid pUC12-1.1Cex(PTIS) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 2FCb-CexCD 0.4 mM "[70% 2H; U-99% 13C; U-99% 15N]" "potassium phosphate" 20 mM ? "sodium azide" 0.02 % ? stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRpipe save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_600MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_experiment_list _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N TROSY HSQC HNCA HN(CO)CA HN(CA)CB HN(COCA)CB ; save_ save_1H-15N_TROSY_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name "1H-15N TROSY HSQC" _Sample_label $sample1 save_ save_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample1 save_ save_HN(CO)CA _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample1 save_ save_HN(CA)CB _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CB _Sample_label $sample1 save_ save_HN(COCA)CB _Saveframe_category NMR_applied_experiment _Experiment_name HN(COCA)CB _Sample_label $sample1 save_ ####################### # Sample conditions # ####################### save_NMR_buffering_condition _Saveframe_category sample_conditions _Details ; 20mM potassium phosphate 0.02% sodium azide ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 pH temperature 303 ? K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference 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 direct external cylindrical "outside sample" parallel 1.0 DSS C 13 "methyl carbon" ppm 0 direct external cylindrical "outside sample" parallel 1.0 NH3 N 15 nitrogen ppm 0 indirect external cylindrical "outside sample" parallel 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details ; Chemical shifts not corrected for trosy (1HN, 15N) or deuterium-isotope shifts (13C) ; loop_ _Sample_label $sample1 stop_ _Sample_conditions_label $NMR_buffering_condition _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "Cex catalytic domain" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 THR CA C 62.641 0.2 1 2 2 THR CB C 69.82 0.2 1 3 3 THR H H 7.304 0.02 1 4 3 THR CA C 58.782 0.2 1 5 3 THR CB C 74.186 0.2 1 6 3 THR N N 110.805 0.2 1 7 4 LEU H H 9.688 0.02 1 8 4 LEU CA C 57.032 0.2 1 9 4 LEU CB C 39.31 0.2 1 10 4 LEU N N 122.468 0.2 1 11 5 LYS H H 6.491 0.02 1 12 5 LYS CA C 59.305 0.2 1 13 5 LYS CB C 32.146 0.2 1 14 5 LYS N N 119.342 0.2 1 15 6 GLU H H 7.616 0.02 1 16 6 GLU CA C 58.455 0.2 1 17 6 GLU CB C 29.975 0.2 1 18 6 GLU CD C 183.737 0.2 1 19 6 GLU N N 118.814 0.2 1 20 7 ALA H H 7.596 0.02 1 21 7 ALA CA C 54.018 0.2 1 22 7 ALA CB C 18.362 0.2 1 23 7 ALA N N 123.159 0.2 1 24 8 ALA H H 8.271 0.02 1 25 8 ALA CA C 55.208 0.2 1 26 8 ALA CB C 17.704 0.2 1 27 8 ALA N N 124.192 0.2 1 28 9 ASP H H 8.93 0.02 1 29 9 ASP CA C 56.923 0.2 1 30 9 ASP CB C 39.559 0.2 1 31 9 ASP CG C 178.694 0.2 1 32 9 ASP N N 119.572 0.2 1 33 10 GLY H H 7.984 0.02 1 34 10 GLY CA C 46.432 0.2 1 35 10 GLY N N 108.664 0.2 1 36 11 ALA H H 7.412 0.02 1 37 11 ALA CA C 51.522 0.2 1 38 11 ALA CB C 19.707 0.2 1 39 11 ALA N N 122.924 0.2 1 40 12 GLY H H 7.93 0.02 1 41 12 GLY CA C 46.269 0.2 1 42 12 GLY N N 110.129 0.2 1 43 13 ARG H H 7.94 0.02 1 44 13 ARG CA C 52.41 0.2 1 45 13 ARG CB C 34.637 0.2 1 46 13 ARG N N 117.447 0.2 1 47 14 ASP H H 8.887 0.02 1 48 14 ASP CA C 53.294 0.2 1 49 14 ASP CB C 42.532 0.2 1 50 14 ASP CG C 177.321 0.2 1 51 14 ASP N N 120.259 0.2 1 52 15 PHE H H 10.107 0.02 1 53 15 PHE CA C 56.681 0.2 1 54 15 PHE CB C 41.53 0.2 1 55 15 PHE N N 125.421 0.2 1 56 16 GLY H H 9.211 0.02 1 57 16 GLY CA C 44.979 0.2 1 58 16 GLY N N 114.772 0.2 1 59 17 PHE H H 7.138 0.02 1 60 17 PHE CA C 53.521 0.2 1 61 17 PHE CB C 41.919 0.2 1 62 17 PHE N N 113.51 0.2 1 63 18 ALA H H 5.609 0.02 1 64 18 ALA CA C 48.978 0.2 1 65 18 ALA CB C 14.94 0.2 1 66 18 ALA N N 119.679 0.2 1 67 19 LEU H H 8.562 0.02 1 68 19 LEU CA C 53.904 0.2 1 69 19 LEU CB C 43.472 0.2 1 70 19 LEU N N 125.163 0.2 1 71 20 ASP H H 7.132 0.02 1 72 20 ASP CA C 49.949 0.2 1 73 20 ASP CB C 41.763 0.2 1 74 20 ASP N N 127.358 0.2 1 75 21 PRO CA C 63.828 0.2 1 76 21 PRO CB C 30.962 0.2 1 77 22 ASN H H 8.102 0.02 1 78 22 ASN CA C 55.153 0.2 1 79 22 ASN CB C 37.523 0.2 1 80 22 ASN CG C 176.508 0.2 1 81 22 ASN N N 118.061 0.2 1 82 23 ARG H H 7.554 0.02 1 83 23 ARG CA C 54.051 0.2 1 84 23 ARG CB C 25.537 0.2 1 85 23 ARG N N 115.06 0.2 1 86 24 LEU H H 6.864 0.02 1 87 24 LEU CA C 56.48 0.2 1 88 24 LEU CB C 40.46 0.2 1 89 24 LEU N N 116.459 0.2 1 90 25 SER H H 6.989 0.02 1 91 25 SER CA C 58.654 0.2 1 92 25 SER CB C 63.011 0.2 1 93 25 SER N N 110.719 0.2 1 94 26 GLU H H 7.761 0.02 1 95 26 GLU CA C 55.27 0.2 1 96 26 GLU CB C 28.455 0.2 1 97 26 GLU CD C 184.425 0.2 1 98 26 GLU N N 126.043 0.2 1 99 27 ALA H H 8.752 0.02 1 100 27 ALA CA C 55.795 0.2 1 101 27 ALA CB C 18.03 0.2 1 102 27 ALA N N 131.262 0.2 1 103 28 GLN H H 8.902 0.02 1 104 28 GLN CA C 58.579 0.2 1 105 28 GLN CB C 28.376 0.2 1 106 28 GLN CD C 180.502 0.2 1 107 28 GLN N N 115.421 0.2 1 108 29 TYR H H 6.461 0.02 1 109 29 TYR CA C 60.951 0.2 1 110 29 TYR CB C 37.247 0.2 1 111 29 TYR N N 119.352 0.2 1 112 30 LYS H H 8.009 0.02 1 113 30 LYS CA C 59.094 0.2 1 114 30 LYS CB C 31.937 0.2 1 115 30 LYS N N 118.712 0.2 1 116 31 ALA H H 7.926 0.02 1 117 31 ALA CA C 54.731 0.2 1 118 31 ALA CB C 17.696 0.2 1 119 31 ALA N N 118.24 0.2 1 120 32 ILE H H 6.851 0.02 1 121 32 ILE CA C 64.464 0.2 1 122 32 ILE CB C 37.995 0.2 1 123 32 ILE N N 120.479 0.2 1 124 33 ALA H H 7.965 0.02 1 125 33 ALA CA C 54.566 0.2 1 126 33 ALA CB C 18.514 0.2 1 127 33 ALA N N 123.792 0.2 1 128 34 ASP H H 8.707 0.02 1 129 34 ASP CA C 57.115 0.2 1 130 34 ASP CB C 40.462 0.2 1 131 34 ASP CG C 178.819 0.2 1 132 34 ASP N N 112.479 0.2 1 133 35 SER H H 7.47 0.02 1 134 35 SER CA C 60.166 0.2 1 135 35 SER CB C 66.033 0.2 1 136 35 SER N N 111.827 0.2 1 137 36 GLU H H 8.272 0.02 1 138 36 GLU CA C 57.966 0.2 1 139 36 GLU CB C 28.827 0.2 1 140 36 GLU CD C 182.567 0.2 1 141 36 GLU N N 117.228 0.2 1 142 37 PHE H H 6.424 0.02 1 143 37 PHE CA C 56.194 0.2 1 144 37 PHE CB C 44.11 0.2 1 145 37 PHE N N 109.867 0.2 1 146 38 ASN H H 9.363 0.02 1 147 38 ASN CA C 52.005 0.2 1 148 38 ASN CB C 39.975 0.2 1 149 38 ASN CG C 176.809 0.2 1 150 38 ASN N N 118.723 0.2 1 151 39 LEU H H 7.604 0.02 1 152 39 LEU CA C 54.498 0.2 1 153 39 LEU CB C 43.086 0.2 1 154 39 LEU N N 122.445 0.2 1 155 40 VAL H H 8.947 0.02 1 156 40 VAL CA C 58.997 0.2 1 157 40 VAL CB C 35.472 0.2 1 158 40 VAL N N 124.064 0.2 1 159 41 VAL H H 7.721 0.02 1 160 41 VAL CA C 57.689 0.2 1 161 41 VAL CB C 35.851 0.2 1 162 41 VAL N N 125.554 0.2 1 163 42 ALA H H 8.959 0.02 1 164 42 ALA CA C 51.195 0.2 1 165 42 ALA CB C 19.396 0.2 1 166 42 ALA N N 128.602 0.2 1 167 43 GLU H H 7.848 0.02 1 168 43 GLU CA C 58.684 0.2 1 169 43 GLU CB C 29.548 0.2 1 170 43 GLU CD C 182.422 0.2 1 171 43 GLU N N 128.774 0.2 1 172 44 ASN H H 8.575 0.02 1 173 44 ASN CA C 54.608 0.2 1 174 44 ASN CB C 43.963 0.2 1 175 44 ASN CG C 176.467 0.2 1 176 44 ASN N N 108.895 0.2 1 177 45 ALA H H 7.212 0.02 1 178 45 ALA CA C 54.776 0.2 1 179 45 ALA CB C 19.581 0.2 1 180 45 ALA N N 118.578 0.2 1 181 46 MET H H 9.007 0.02 1 182 46 MET CA C 55.428 0.2 1 183 46 MET CB C 32.143 0.2 1 184 46 MET N N 113.603 0.2 1 185 47 LYS H H 6.974 0.02 1 186 47 LYS HZ H 7.979 0.02 1 187 47 LYS CA C 57.337 0.2 1 188 47 LYS CB C 34.845 0.2 1 189 47 LYS N N 118.527 0.2 1 190 47 LYS NZ N 35.607 0.2 2 191 48 TRP H H 10.179 0.02 1 192 48 TRP HE1 H 8.384 0.02 1 193 48 TRP CA C 59.93 0.2 1 194 48 TRP CB C 28.199 0.2 1 195 48 TRP N N 127.111 0.2 1 196 48 TRP NE1 N 125.5 0.2 1 197 49 ASP H H 8.855 0.02 1 198 49 ASP CA C 56.971 0.2 1 199 49 ASP CB C 38.135 0.2 1 200 49 ASP CG C 179.191 0.2 1 201 49 ASP N N 119.083 0.2 1 202 50 ALA H H 7.174 0.02 1 203 50 ALA CA C 52.935 0.2 1 204 50 ALA CB C 20.091 0.2 1 205 50 ALA N N 121.941 0.2 1 206 51 THR H H 7.812 0.02 1 207 51 THR CA C 61.764 0.2 1 208 51 THR CB C 72.664 0.2 1 209 51 THR N N 104.564 0.2 1 210 52 GLU H H 8.898 0.02 1 211 52 GLU CA C 52.855 0.2 1 212 52 GLU CB C 31.146 0.2 1 213 52 GLU N N 124.215 0.2 1 214 53 PRO CA C 64.569 0.2 1 215 53 PRO CB C 31.814 0.2 1 216 54 SER H H 7.305 0.02 1 217 54 SER CA C 56.204 0.2 1 218 54 SER CB C 64.794 0.2 1 219 54 SER N N 112.526 0.2 1 220 55 GLN H H 7.31 0.02 1 221 55 GLN CA C 57.741 0.2 1 222 55 GLN CB C 26.025 0.2 1 223 55 GLN CD C 179.154 0.2 1 224 55 GLN N N 123.608 0.2 1 225 56 ASN H H 10.621 0.02 1 226 56 ASN CA C 53.793 0.2 1 227 56 ASN CB C 38.507 0.2 1 228 56 ASN CG C 178.462 0.2 1 229 56 ASN N N 127.376 0.2 1 230 57 SER H H 7.354 0.02 1 231 57 SER CA C 56.031 0.2 1 232 57 SER CB C 63.149 0.2 1 233 57 SER N N 117.291 0.2 1 234 58 PHE H H 8.105 0.02 1 235 58 PHE CA C 56.83 0.2 1 236 58 PHE CB C 40.614 0.2 1 237 58 PHE N N 122.725 0.2 1 238 59 SER H H 8.588 0.02 1 239 59 SER CA C 55.05 0.2 1 240 59 SER CB C 64.151 0.2 1 241 59 SER N N 119.474 0.2 1 242 60 PHE H H 8.726 0.02 1 243 60 PHE CA C 57.083 0.2 1 244 60 PHE CB C 39.445 0.2 1 245 60 PHE N N 122.282 0.2 1 246 61 GLY H H 8.618 0.02 1 247 61 GLY CA C 48.196 0.2 1 248 61 GLY N N 110.045 0.2 1 249 62 ALA H H 8.751 0.02 1 250 62 ALA CA C 55.379 0.2 1 251 62 ALA CB C 17.743 0.2 1 252 62 ALA N N 125.263 0.2 1 253 63 GLY H H 9.102 0.02 1 254 63 GLY CA C 47.406 0.2 1 255 63 GLY N N 109.268 0.2 1 256 64 ASP H H 9.925 0.02 1 257 64 ASP CA C 57.375 0.2 1 258 64 ASP CB C 39.111 0.2 1 259 64 ASP N N 124.713 0.2 1 260 65 ARG H H 7.901 0.02 1 261 65 ARG CA C 59.203 0.2 1 262 65 ARG CB C 29.506 0.2 1 263 65 ARG N N 122.131 0.2 1 264 66 VAL H H 7.51 0.02 1 265 66 VAL CA C 66.349 0.2 1 266 66 VAL CB C 30.216 0.2 1 267 66 VAL N N 121.068 0.2 1 268 67 ALA H H 8.428 0.02 1 269 67 ALA CA C 55.138 0.2 1 270 67 ALA CB C 17.619 0.2 1 271 67 ALA N N 121.977 0.2 1 272 68 SER H H 8.966 0.02 1 273 68 SER CA C 61.694 0.2 1 274 68 SER CB C 62.783 0.2 1 275 68 SER N N 117.146 0.2 1 276 69 TYR H H 7.644 0.02 1 277 69 TYR CA C 61.94 0.2 1 278 69 TYR CB C 37.456 0.2 1 279 69 TYR N N 123.301 0.2 1 280 70 ALA H H 7.949 0.02 1 281 70 ALA CA C 55.237 0.2 1 282 70 ALA CB C 17.34 0.2 1 283 70 ALA N N 122.712 0.2 1 284 71 ALA H H 7.867 0.02 1 285 71 ALA CA C 54.483 0.2 1 286 71 ALA CB C 17.856 0.2 1 287 71 ALA N N 119.509 0.2 1 288 72 ASP H H 8.649 0.02 1 289 72 ASP CA C 56.621 0.2 1 290 72 ASP CB C 40.644 0.2 1 291 72 ASP CG C 179.17 0.2 1 292 72 ASP N N 119.174 0.2 1 293 73 THR H H 7.298 0.02 1 294 73 THR CA C 60.924 0.2 1 295 73 THR CB C 69.706 0.2 1 296 73 THR N N 105.416 0.2 1 297 74 GLY H H 7.591 0.02 1 298 74 GLY CA C 46.852 0.2 1 299 74 GLY N N 113.872 0.2 1 300 75 LYS H H 8.408 0.02 1 301 75 LYS CA C 55.019 0.2 1 302 75 LYS CB C 36.003 0.2 1 303 75 LYS N N 120.625 0.2 1 304 76 GLU H H 7.741 0.02 1 305 76 GLU CA C 56.093 0.2 1 306 76 GLU CB C 30.728 0.2 1 307 76 GLU CD C 183.286 0.2 1 308 76 GLU N N 121.735 0.2 1 309 77 LEU H H 8.763 0.02 1 310 77 LEU CA C 53.002 0.2 1 311 77 LEU CB C 42.908 0.2 1 312 77 LEU N N 125.049 0.2 1 313 78 TYR H H 8.939 0.02 1 314 78 TYR CA C 56.158 0.2 1 315 78 TYR CB C 41.792 0.2 1 316 78 TYR N N 132.08 0.2 1 317 79 GLY H H 8.686 0.02 1 318 79 GLY CA C 44.959 0.2 1 319 79 GLY N N 117.729 0.2 1 320 80 HIS H H 8.012 0.02 1 321 80 HIS HD1 H 13.8 0.02 1 322 80 HIS HD2 H 6.83 0.02 1 323 80 HIS HE1 H 6.64 0.02 1 324 80 HIS CA C 51.783 0.2 1 325 80 HIS CB C 32.425 0.2 1 326 80 HIS CD2 C 120.1 0.22 1 327 80 HIS CE1 C 138.6 0.2 1 328 80 HIS N N 129.096 0.2 1 329 80 HIS ND1 N 172.1 0.2 1 330 80 HIS NE2 N 246.9 0.2 1 331 81 THR H H 6.363 0.02 1 332 81 THR CA C 59.942 0.2 1 333 81 THR CB C 70.709 0.2 1 334 81 THR N N 120.177 0.2 1 335 82 LEU H H 7.716 0.02 1 336 82 LEU CA C 58.76 0.2 1 337 82 LEU CB C 40.731 0.2 1 338 82 LEU N N 129.33 0.2 1 339 83 VAL H H 7.492 0.02 1 340 83 VAL CA C 63.393 0.2 1 341 83 VAL CB C 32.582 0.2 1 342 83 VAL N N 115.74 0.2 1 343 84 TRP H H 6.764 0.02 1 344 84 TRP HE1 H 10.78 0.02 1 345 84 TRP CA C 53.341 0.2 1 346 84 TRP N N 124.262 0.2 1 347 84 TRP NE1 N 135.03 0.2 1 348 85 HIS HD2 H 6.88 0.02 1 349 85 HIS HE1 H 8.43 0.02 1 350 85 HIS HE2 H 11.8 0.02 1 351 85 HIS CD2 C 118.4 0.22 1 352 85 HIS CE1 C 139 0.2 1 353 85 HIS ND1 N 247.5 0.2 1 354 85 HIS NE2 N 167.5 0.2 1 355 89 PRO CA C 62.002 0.2 1 356 89 PRO CB C 32.778 0.2 1 357 90 ASP H H 8.627 0.02 1 358 90 ASP CA C 57.581 0.2 1 359 90 ASP CB C 39.749 0.2 1 360 90 ASP CG C 179.442 0.2 1 361 90 ASP N N 123.143 0.2 1 362 91 TRP H H 8.222 0.02 1 363 91 TRP HE1 H 9.532 0.02 1 364 91 TRP CA C 58.582 0.2 1 365 91 TRP CB C 27.336 0.2 1 366 91 TRP N N 115.731 0.2 1 367 91 TRP NE1 N 128.3 0.2 1 368 92 ALA H H 5.915 0.02 1 369 92 ALA CA C 53.666 0.2 1 370 92 ALA CB C 15.936 0.2 1 371 92 ALA N N 124.664 0.2 1 372 93 LYS H H 6.818 0.02 1 373 93 LYS CA C 58.869 0.2 1 374 93 LYS CB C 31.677 0.2 1 375 93 LYS N N 115.74 0.2 1 376 94 ASN H H 7.108 0.02 1 377 94 ASN CA C 52.99 0.2 1 378 94 ASN CB C 39.019 0.2 1 379 94 ASN CG C 176.769 0.2 1 380 94 ASN N N 113.579 0.2 1 381 95 LEU H H 7.041 0.02 1 382 95 LEU CA C 53.919 0.2 1 383 95 LEU CB C 43.463 0.2 1 384 95 LEU N N 120.41 0.2 1 385 96 ASN H H 8.592 0.02 1 386 96 ASN CA C 51.793 0.2 1 387 96 ASN CB C 42.715 0.2 1 388 96 ASN CG C 176.741 0.2 1 389 96 ASN N N 118.11 0.2 1 390 97 GLY H H 8.882 0.02 1 391 97 GLY CA C 46.873 0.2 1 392 97 GLY N N 108.82 0.2 1 393 98 SER CA C 61.034 0.2 1 394 98 SER CB C 62.688 0.2 1 395 99 ALA H H 8.297 0.02 1 396 99 ALA CA C 54.766 0.2 1 397 99 ALA CB C 18.192 0.2 1 398 99 ALA N N 125.842 0.2 1 399 100 PHE H H 7.53 0.02 1 400 100 PHE CA C 60.529 0.2 1 401 100 PHE CB C 37.547 0.2 1 402 100 PHE N N 121.838 0.2 1 403 101 GLU H H 8.456 0.02 1 404 101 GLU CA C 60.517 0.2 1 405 101 GLU CB C 29.773 0.2 1 406 101 GLU CD C 182.883 0.2 1 407 101 GLU N N 121.52 0.2 1 408 102 SER H H 8.76 0.02 1 409 102 SER CA C 61.448 0.2 1 410 102 SER CB C 62.715 0.2 1 411 102 SER N N 113.936 0.2 1 412 103 ALA H H 7.878 0.02 1 413 103 ALA CA C 54.771 0.2 1 414 103 ALA CB C 18.061 0.2 1 415 103 ALA N N 124.863 0.2 1 416 104 MET H H 8.31 0.02 1 417 104 MET CA C 59.481 0.2 1 418 104 MET CB C 31.959 0.2 1 419 104 MET N N 120.802 0.2 1 420 105 VAL H H 8.764 0.02 1 421 105 VAL CA C 67.611 0.2 1 422 105 VAL CB C 31.291 0.2 1 423 105 VAL N N 120.825 0.2 1 424 106 ASN H H 8.965 0.02 1 425 106 ASN CA C 57.003 0.2 1 426 106 ASN CB C 39.153 0.2 1 427 106 ASN CG C 176.128 0.2 1 428 106 ASN N N 121.644 0.2 1 429 107 HIS H H 8.344 0.02 1 430 107 HIS HD1 H 16.68 0.02 1 431 107 HIS HD2 H 6.36 0.02 1 432 107 HIS HE1 H 8.3 0.02 1 433 107 HIS HE2 H 13.5 0.02 1 434 107 HIS CA C 61.025 0.2 1 435 107 HIS CB C 28.377 0.2 1 436 107 HIS CD2 C 118.8 0.22 1 437 107 HIS CE1 C 136 0.2 1 438 107 HIS N N 118.605 0.2 1 439 107 HIS ND1 N 184.6 0.2 1 440 107 HIS NE2 N 170.6 0.2 1 441 108 VAL H H 8.161 0.02 1 442 108 VAL CA C 66.15 0.2 1 443 108 VAL CB C 31.49 0.2 1 444 108 VAL N N 116.333 0.2 1 445 109 THR H H 8.101 0.02 1 446 109 THR CA C 66.253 0.2 1 447 109 THR CB C 68.976 0.2 1 448 109 THR N N 112.581 0.2 1 449 110 LYS H H 8.23 0.02 1 450 110 LYS CA C 58.262 0.2 1 451 110 LYS CB C 31.197 0.2 1 452 110 LYS N N 118.728 0.2 1 453 111 VAL H H 7.732 0.02 1 454 111 VAL CB C 31.549 0.2 1 455 111 VAL N N 120.039 0.2 1 456 112 ALA H H 7.747 0.02 1 457 112 ALA CA C 54.987 0.2 1 458 112 ALA CB C 16.383 0.2 1 459 112 ALA N N 120.552 0.2 1 460 113 ASP H H 8.622 0.02 1 461 113 ASP CA C 57.245 0.2 1 462 113 ASP CB C 42.564 0.2 1 463 113 ASP CG C 179.159 0.2 1 464 113 ASP N N 117.02 0.2 1 465 114 HIS H H 7.418 0.02 1 466 114 HIS HE1 H 8.23 0.02 1 467 114 HIS CA C 59.267 0.2 1 468 114 HIS CB C 27.813 0.2 1 469 114 HIS CE1 C 135.7 0.2 1 470 114 HIS N N 116.327 0.2 1 471 114 HIS ND1 N 181.4 0.2 4 472 114 HIS NE2 N 177.4 0.2 4 473 115 PHE H H 7.142 0.02 1 474 115 PHE CA C 58.242 0.2 1 475 115 PHE CB C 39.915 0.2 1 476 115 PHE N N 112.452 0.2 1 477 116 GLU H H 7.219 0.02 1 478 116 GLU CA C 58.467 0.2 1 479 116 GLU CB C 27.968 0.2 1 480 116 GLU CD C 182.36 0.2 1 481 116 GLU N N 126.108 0.2 1 482 117 GLY H H 9.7 0.02 1 483 117 GLY CA C 45.083 0.2 1 484 117 GLY N N 118.606 0.2 1 485 118 LYS H H 8.242 0.02 1 486 118 LYS CA C 56.798 0.2 1 487 118 LYS CB C 33.049 0.2 1 488 118 LYS N N 119.301 0.2 1 489 119 VAL H H 7.34 0.02 1 490 119 VAL CA C 60.132 0.2 1 491 119 VAL CB C 36.237 0.2 1 492 119 VAL N N 117.624 0.2 1 493 120 ALA H H 8.354 0.02 1 494 120 ALA CA C 53.128 0.2 1 495 120 ALA CB C 19.807 0.2 1 496 120 ALA N N 128.628 0.2 1 497 121 SER H H 6.587 0.02 1 498 121 SER CA C 55.961 0.2 1 499 121 SER CB C 66.977 0.2 1 500 121 SER N N 111.313 0.2 1 501 122 TRP H H 8.944 0.02 1 502 122 TRP HE1 H 12.14 0.02 1 503 122 TRP CA C 55.579 0.2 1 504 122 TRP CB C 34.921 0.2 1 505 122 TRP N N 121.597 0.2 1 506 122 TRP NE1 N 134.83 0.2 1 507 123 ASP H H 8.723 0.02 1 508 123 ASP CA C 53.586 0.2 1 509 123 ASP CB C 40.362 0.2 1 510 123 ASP CG C 174.83 0.2 1 511 123 ASP N N 119.852 0.2 1 512 124 VAL H H 9.474 0.02 1 513 124 VAL CA C 65.464 0.2 1 514 124 VAL CB C 30.395 0.2 1 515 124 VAL N N 132.664 0.2 1 516 125 VAL H H 6.426 0.02 1 517 125 VAL CA C 60.326 0.2 1 518 125 VAL CB C 35.332 0.2 1 519 125 VAL N N 112.225 0.2 1 520 126 ASN H H 8.345 0.02 1 521 126 ASN CA C 50.412 0.2 1 522 126 ASN CB C 41.524 0.2 1 523 126 ASN CG C 174.258 0.2 1 524 126 ASN N N 126.422 0.2 1 525 127 GLU H H 8.819 0.02 1 526 127 GLU CA C 56.996 0.2 1 527 127 GLU CB C 26.522 0.2 1 528 127 GLU CD C 183.027 0.2 1 529 127 GLU N N 121.203 0.2 1 530 128 ALA H H 8.882 0.02 1 531 128 ALA CA C 52.954 0.2 1 532 128 ALA CB C 19.947 0.2 1 533 128 ALA N N 118.386 0.2 1 534 129 PHE H H 8.097 0.02 1 535 129 PHE CA C 59.218 0.2 1 536 129 PHE CB C 40.232 0.2 1 537 129 PHE N N 117.618 0.2 1 538 130 ALA H H 8.665 0.02 1 539 130 ALA CA C 49.882 0.2 1 540 130 ALA CB C 20.262 0.2 1 541 130 ALA N N 124.022 0.2 1 542 131 ASP H H 8.58 0.02 1 543 131 ASP CA C 57.148 0.2 1 544 131 ASP CB C 39.875 0.2 1 545 131 ASP N N 122.902 0.2 1 546 132 GLY CA C 44.719 0.2 1 547 133 GLY H H 7.931 0.02 1 548 133 GLY CA C 43.554 0.2 1 549 133 GLY N N 108.797 0.2 1 550 134 GLY H H 8.284 0.02 1 551 134 GLY CA C 43.957 0.2 1 552 134 GLY N N 106.694 0.2 1 553 135 ARG H H 8.683 0.02 1 554 135 ARG CA C 53.493 0.2 1 555 135 ARG CB C 30.349 0.2 1 556 135 ARG N N 116.493 0.2 1 557 136 ARG H H 7.998 0.02 1 558 136 ARG CA C 57.099 0.2 1 559 136 ARG CB C 29.392 0.2 1 560 136 ARG N N 122.599 0.2 1 561 137 GLN H H 8.636 0.02 1 562 137 GLN CA C 56.088 0.2 1 563 137 GLN CB C 28.582 0.2 1 564 137 GLN CD C 180.295 0.2 1 565 137 GLN N N 124.082 0.2 1 566 138 ASP H H 8.204 0.02 1 567 138 ASP CA C 52.275 0.2 1 568 138 ASP CB C 38.244 0.2 1 569 138 ASP CG C 180.658 0.2 1 570 138 ASP N N 118.667 0.2 1 571 139 SER H H 6.505 0.02 1 572 139 SER CA C 54.127 0.2 1 573 139 SER CB C 63.771 0.2 1 574 139 SER N N 111.821 0.2 1 575 140 ALA H H 8.983 0.02 1 576 140 ALA CA C 54.534 0.2 1 577 140 ALA CB C 17.788 0.2 1 578 140 ALA N N 132.262 0.2 1 579 141 PHE H H 6.973 0.02 1 580 141 PHE CA C 61.206 0.2 1 581 141 PHE CB C 36.718 0.2 1 582 141 PHE N N 113.404 0.2 1 583 142 GLN H H 6.799 0.02 1 584 142 GLN CA C 57.254 0.2 1 585 142 GLN CB C 29.334 0.2 1 586 142 GLN CD C 180.086 0.2 1 587 142 GLN N N 119.769 0.2 1 588 143 GLN H H 8.339 0.02 1 589 143 GLN CA C 58.4 0.2 1 590 143 GLN CB C 28.34 0.2 1 591 143 GLN CD C 180.027 0.2 1 592 143 GLN N N 116.576 0.2 1 593 144 LYS H H 7.817 0.02 1 594 144 LYS CA C 53.829 0.2 1 595 144 LYS N N 114.811 0.2 1 596 145 LEU H H 7.835 0.02 1 597 145 LEU N N 114.94 0.2 1 598 146 GLY H H 7.588 0.02 1 599 146 GLY N N 109.81 0.2 1 600 147 ASN H H 8.725 0.02 1 601 147 ASN N N 115.417 0.2 1 602 148 GLY CA C 46.564 0.2 1 603 149 TYR H H 7.141 0.02 1 604 149 TYR CA C 60.044 0.2 1 605 149 TYR CB C 38.598 0.2 1 606 149 TYR N N 117.529 0.2 1 607 150 ILE H H 5.872 0.02 1 608 150 ILE CA C 65.544 0.2 1 609 150 ILE CB C 36.287 0.2 1 610 150 ILE N N 120.239 0.2 1 611 151 GLU H H 8.736 0.02 1 612 151 GLU CA C 59.828 0.2 1 613 151 GLU CB C 27.863 0.2 1 614 151 GLU CD C 182.423 0.2 1 615 151 GLU N N 122.833 0.2 1 616 152 THR H H 7.839 0.02 1 617 152 THR CA C 66.012 0.2 1 618 152 THR CB C 67.683 0.2 1 619 152 THR N N 116.436 0.2 1 620 153 ALA H H 8.392 0.02 1 621 153 ALA CA C 55.975 0.2 1 622 153 ALA CB C 17.533 0.2 1 623 153 ALA N N 124.36 0.2 1 624 154 PHE H H 8.363 0.02 1 625 154 PHE CA C 63.954 0.2 1 626 154 PHE CB C 38.403 0.2 1 627 154 PHE N N 117.091 0.2 1 628 155 ARG H H 8.509 0.02 1 629 155 ARG CA C 60.421 0.2 1 630 155 ARG CB C 28.692 0.2 1 631 155 ARG N N 117.04 0.2 1 632 156 ALA H H 8.093 0.02 1 633 156 ALA CA C 54.127 0.2 1 634 156 ALA CB C 17.418 0.2 1 635 156 ALA N N 122.325 0.2 1 636 157 ALA H H 8.178 0.02 1 637 157 ALA CA C 55.063 0.2 1 638 157 ALA CB C 17.872 0.2 1 639 157 ALA N N 123.216 0.2 1 640 158 ARG H H 7.817 0.02 1 641 158 ARG CA C 55.874 0.2 1 642 158 ARG CB C 27.373 0.2 1 643 158 ARG N N 117.059 0.2 1 644 159 ALA H H 7.345 0.02 1 645 159 ALA CA C 53.596 0.2 1 646 159 ALA CB C 17.527 0.2 1 647 159 ALA N N 119.305 0.2 1 648 160 ALA H H 7.109 0.02 1 649 160 ALA CA C 52.704 0.2 1 650 160 ALA CB C 21.091 0.2 1 651 160 ALA N N 119.212 0.2 1 652 161 ASP H H 7.775 0.02 1 653 161 ASP CA C 50.552 0.2 1 654 161 ASP CB C 41.126 0.2 1 655 161 ASP N N 114.784 0.2 1 656 162 PRO CA C 63.673 0.2 1 657 162 PRO CB C 32.599 0.2 1 658 163 THR H H 8.247 0.02 1 659 163 THR CA C 62.251 0.2 1 660 163 THR CB C 70.073 0.2 1 661 163 THR N N 110.49 0.2 1 662 164 ALA H H 7.607 0.02 1 663 164 ALA CA C 52.092 0.2 1 664 164 ALA CB C 18.23 0.2 1 665 164 ALA N N 126.876 0.2 1 666 165 LYS H H 8.458 0.02 1 667 165 LYS CA C 54.935 0.2 1 668 165 LYS CB C 31.071 0.2 1 669 165 LYS N N 122.461 0.2 1 670 166 LEU H H 10.441 0.02 1 671 166 LEU CA C 54.17 0.2 1 672 166 LEU CB C 40.596 0.2 1 673 166 LEU N N 125.211 0.2 1 674 167 CYS H H 10.025 0.02 1 675 167 CYS CA C 52.131 0.2 1 676 167 CYS CB C 39.292 0.2 1 677 167 CYS N N 123.051 0.2 1 678 168 ILE H H 8.097 0.02 1 679 168 ILE CA C 58.677 0.2 1 680 168 ILE CB C 41.731 0.2 1 681 168 ILE N N 121.95 0.2 1 682 169 ASN H H 8.026 0.02 1 683 169 ASN CA C 52.03 0.2 1 684 169 ASN CB C 43.218 0.2 1 685 169 ASN N N 126.296 0.2 1 686 170 ASP H H 8.495 0.02 1 687 170 ASP CA C 53.891 0.2 1 688 170 ASP CB C 46.352 0.2 1 689 170 ASP CG C 180.482 0.2 1 690 170 ASP N N 127.532 0.2 1 691 171 TYR H H 10.116 0.02 1 692 171 TYR CA C 54.524 0.2 1 693 171 TYR CB C 40.511 0.2 1 694 171 TYR N N 118.157 0.2 1 695 172 ASN H H 9.168 0.02 1 696 172 ASN CA C 54.173 0.2 1 697 172 ASN CB C 36.056 0.2 1 698 172 ASN CG C 178.237 0.2 1 699 172 ASN N N 121.782 0.2 1 700 173 VAL H H 6.566 0.02 1 701 173 VAL CA C 58.875 0.2 1 702 173 VAL CB C 31.026 0.2 1 703 173 VAL N N 103.877 0.2 1 704 174 GLU H H 8.121 0.02 1 705 174 GLU CA C 61.707 0.2 1 706 174 GLU CB C 27.27 0.2 1 707 174 GLU CD C 183.838 0.2 1 708 174 GLU N N 121.058 0.2 1 709 175 GLY H H 7.429 0.02 1 710 175 GLY CA C 42.504 0.2 1 711 175 GLY N N 103.114 0.2 1 712 176 ILE H H 8.232 0.02 1 713 176 ILE CA C 63.073 0.2 1 714 176 ILE CB C 34.917 0.2 1 715 176 ILE N N 119.96 0.2 1 716 177 ASN H H 7.901 0.02 1 717 177 ASN CA C 51.631 0.2 1 718 177 ASN CB C 38.51 0.2 1 719 177 ASN N N 127.244 0.2 1 720 178 ALA CA C 55.338 0.2 1 721 178 ALA CB C 18.194 0.2 1 722 179 LYS H H 8.216 0.02 1 723 179 LYS CA C 60.538 0.2 1 724 179 LYS CB C 33.148 0.2 1 725 179 LYS N N 121.936 0.2 1 726 180 SER H H 9.513 0.02 1 727 180 SER CA C 60.818 0.2 1 728 180 SER CB C 63.048 0.2 1 729 180 SER N N 116.279 0.2 1 730 181 ASN H H 8.999 0.02 1 731 181 ASN CA C 55.533 0.2 1 732 181 ASN CB C 36.264 0.2 1 733 181 ASN CG C 175.824 0.2 1 734 181 ASN N N 123.689 0.2 1 735 182 SER H H 7.858 0.02 1 736 182 SER CA C 62.636 0.2 1 737 182 SER CB C 63.496 0.2 1 738 182 SER N N 119.804 0.2 1 739 183 LEU H H 7.405 0.02 1 740 183 LEU CA C 57.526 0.2 1 741 183 LEU CB C 41.181 0.2 1 742 183 LEU N N 126.364 0.2 1 743 184 TYR H H 8.922 0.02 1 744 184 TYR CA C 61.795 0.2 1 745 184 TYR CB C 37.526 0.2 1 746 184 TYR N N 122.281 0.2 1 747 185 ASP H H 7.97 0.02 1 748 185 ASP CA C 57.015 0.2 1 749 185 ASP CB C 40.091 0.2 1 750 185 ASP CG C 179.032 0.2 1 751 185 ASP N N 118.743 0.2 1 752 186 LEU H H 7.324 0.02 1 753 186 LEU CA C 58.339 0.2 1 754 186 LEU CB C 40.731 0.2 1 755 186 LEU N N 122.758 0.2 1 756 187 VAL H H 8.183 0.02 1 757 187 VAL CA C 66.637 0.2 1 758 187 VAL CB C 30.202 0.2 1 759 187 VAL N N 121.215 0.2 1 760 188 LYS H H 8.453 0.02 1 761 188 LYS CA C 59.907 0.2 1 762 188 LYS CB C 31.985 0.2 1 763 188 LYS N N 119.638 0.2 1 764 189 ASP H H 7.657 0.02 1 765 189 ASP CA C 57.01 0.2 1 766 189 ASP CB C 42.347 0.2 1 767 189 ASP CG C 180.282 0.2 1 768 189 ASP N N 120.32 0.2 1 769 190 PHE H H 9.199 0.02 1 770 190 PHE CA C 59.534 0.2 1 771 190 PHE CB C 36.855 0.2 1 772 190 PHE N N 120.991 0.2 1 773 191 LYS H H 8.651 0.02 1 774 191 LYS CA C 56.099 0.2 1 775 191 LYS CB C 28.55 0.2 1 776 191 LYS N N 116.578 0.2 1 777 192 ALA H H 8.092 0.02 1 778 192 ALA CA C 54.719 0.2 1 779 192 ALA CB C 17.96 0.2 1 780 192 ALA N N 123.757 0.2 1 781 193 ARG H H 7.805 0.02 1 782 193 ARG CA C 56.466 0.2 1 783 193 ARG CB C 30.963 0.2 1 784 193 ARG N N 114.182 0.2 1 785 194 GLY H H 7.645 0.02 1 786 194 GLY CA C 45.964 0.2 1 787 194 GLY N N 109.424 0.2 1 788 195 VAL H H 8.344 0.02 1 789 195 VAL CA C 60.31 0.2 1 790 195 VAL CB C 31.792 0.2 1 791 195 VAL N N 125.447 0.2 1 792 196 PRO CA C 63.602 0.2 1 793 196 PRO CB C 30.809 0.2 1 794 197 LEU H H 7.285 0.02 1 795 197 LEU CA C 56.949 0.2 1 796 197 LEU CB C 42.067 0.2 1 797 197 LEU N N 121.723 0.2 1 798 198 ASP H H 9.812 0.02 1 799 198 ASP CA C 54.705 0.2 1 800 198 ASP CB C 45.057 0.2 1 801 198 ASP N N 123.61 0.2 1 802 199 CYS H H 8.127 0.02 1 803 199 CYS CA C 53.375 0.2 1 804 199 CYS CB C 49.19 0.2 1 805 199 CYS N N 116.621 0.2 1 806 200 VAL H H 8.56 0.02 1 807 200 VAL CA C 60.561 0.2 1 808 200 VAL CB C 34.413 0.2 1 809 200 VAL N N 120.798 0.2 1 810 201 GLY H H 9.537 0.02 1 811 201 GLY CA C 44.359 0.2 1 812 201 GLY N N 115.582 0.2 1 813 202 PHE H H 8.46 0.02 1 814 202 PHE N N 122.402 0.2 1 815 203 GLN H H 9.009 0.02 1 816 203 GLN CA C 59.668 0.2 1 817 203 GLN CB C 27.728 0.2 1 818 203 GLN CD C 179.598 0.2 1 819 203 GLN N N 125.234 0.2 1 820 204 SER H H 8.701 0.02 1 821 204 SER CA C 58.401 0.2 1 822 204 SER CB C 61.752 0.2 1 823 204 SER N N 102.635 0.2 1 824 205 HIS H H 8.305 0.02 1 825 205 HIS HD1 H 17.64 0.02 1 826 205 HIS HD2 H 7.23 0.02 1 827 205 HIS HE1 H 7.75 0.02 1 828 205 HIS HE2 H 10.22 0.02 1 829 205 HIS CA C 54.538 0.2 1 830 205 HIS CB C 27.251 0.2 1 831 205 HIS CD2 C 119.5 0.22 1 832 205 HIS CE1 C 136.4 0.2 1 833 205 HIS N N 118.088 0.2 1 834 205 HIS ND1 N 188 0.2 1 835 205 HIS NE2 N 164.3 0.2 1 836 206 LEU H H 8.623 0.02 1 837 206 LEU CA C 52.604 0.2 1 838 206 LEU CB C 43.945 0.2 1 839 206 LEU N N 125.524 0.2 1 840 207 ILE H H 8.385 0.02 1 841 207 ILE CA C 60.01 0.2 1 842 207 ILE CB C 40.26 0.2 1 843 207 ILE N N 124.071 0.2 1 844 208 VAL H H 8.192 0.02 1 845 208 VAL CA C 62.434 0.2 1 846 208 VAL CB C 31.632 0.2 1 847 208 VAL N N 125.004 0.2 1 848 209 GLY H H 11.921 0.02 1 849 209 GLY CA C 44.551 0.2 1 850 209 GLY N N 119.755 0.2 1 851 210 GLN H H 8.374 0.02 1 852 210 GLN CA C 53.618 0.2 1 853 210 GLN CB C 27.943 0.2 1 854 210 GLN CD C 180.648 0.2 1 855 210 GLN N N 120.812 0.2 1 856 211 VAL H H 8.834 0.02 1 857 211 VAL CA C 61.688 0.2 1 858 211 VAL CB C 31.495 0.2 1 859 211 VAL N N 126.738 0.2 1 860 212 PRO CA C 63.419 0.2 1 861 212 PRO CB C 31.327 0.2 1 862 213 GLY H H 8.996 0.02 1 863 213 GLY CA C 46.272 0.2 1 864 213 GLY N N 113.716 0.2 1 865 214 ASP H H 8.983 0.02 1 866 214 ASP CA C 51.807 0.2 1 867 214 ASP CB C 38.09 0.2 1 868 214 ASP CG C 180.665 0.2 1 869 214 ASP N N 118.675 0.2 1 870 215 PHE H H 6.94 0.02 1 871 215 PHE CA C 58.043 0.2 1 872 215 PHE CB C 39.007 0.2 1 873 215 PHE N N 121.51 0.2 1 874 216 ARG H H 8.942 0.02 1 875 216 ARG CA C 60.328 0.2 1 876 216 ARG CB C 28.079 0.2 1 877 216 ARG N N 118.869 0.2 1 878 217 GLN H H 8.445 0.02 1 879 217 GLN CA C 59.153 0.2 1 880 217 GLN CB C 27.541 0.2 1 881 217 GLN CD C 180.07 0.2 1 882 217 GLN N N 118.894 0.2 1 883 218 ASN H H 8.548 0.02 1 884 218 ASN CA C 55.711 0.2 1 885 218 ASN CB C 38.982 0.2 1 886 218 ASN N N 120.22 0.2 1 887 219 LEU H H 8.605 0.02 1 888 219 LEU N N 119.008 0.2 1 889 220 GLN H H 8.694 0.02 1 890 220 GLN CA C 57.46 0.2 1 891 220 GLN CB C 28.679 0.2 1 892 220 GLN CD C 180.298 0.2 1 893 220 GLN N N 117.1 0.2 1 894 221 ARG H H 8.064 0.02 1 895 221 ARG CA C 58.648 0.2 1 896 221 ARG CB C 26.885 0.2 1 897 221 ARG N N 117.571 0.2 1 898 222 PHE H H 7.608 0.02 1 899 222 PHE CA C 63.053 0.2 1 900 222 PHE CB C 39.464 0.2 1 901 222 PHE N N 121.787 0.2 1 902 223 ALA H H 8.281 0.02 1 903 223 ALA CA C 54.147 0.2 1 904 223 ALA CB C 18.322 0.2 1 905 223 ALA N N 123.808 0.2 1 906 224 ASP H H 8.574 0.02 1 907 224 ASP CA C 56.301 0.2 1 908 224 ASP CB C 40.274 0.2 1 909 224 ASP CG C 179.26 0.2 1 910 224 ASP N N 118.701 0.2 1 911 225 LEU H H 7.878 0.02 1 912 225 LEU CA C 55.242 0.2 1 913 225 LEU CB C 41.795 0.2 1 914 225 LEU N N 120.169 0.2 1 915 226 GLY H H 8.406 0.02 1 916 226 GLY CA C 45.235 0.2 1 917 226 GLY N N 106.6 0.2 1 918 227 VAL H H 6.851 0.02 1 919 227 VAL CA C 57.963 0.2 1 920 227 VAL CB C 33.998 0.2 1 921 227 VAL N N 110.812 0.2 1 922 228 ASP H H 7.644 0.02 1 923 228 ASP CA C 53.554 0.2 1 924 228 ASP CB C 42.316 0.2 1 925 228 ASP CG C 178.796 0.2 1 926 228 ASP N N 117.58 0.2 1 927 229 VAL H H 8.131 0.02 1 928 229 VAL CA C 57.838 0.2 1 929 229 VAL CB C 35.111 0.2 1 930 229 VAL N N 110.17 0.2 1 931 230 ARG H H 8.669 0.02 1 932 230 ARG CA C 55.805 0.2 1 933 230 ARG CB C 34.352 0.2 1 934 230 ARG N N 120.935 0.2 1 935 231 ILE H H 8.026 0.02 1 936 231 ILE CA C 60.379 0.2 1 937 231 ILE CB C 38.065 0.2 1 938 231 ILE N N 128.342 0.2 1 939 232 THR H H 8.035 0.02 1 940 232 THR CA C 63.318 0.2 1 941 232 THR CB C 69.512 0.2 1 942 232 THR N N 117.528 0.2 1 943 233 GLU H H 7.71 0.02 1 944 233 GLU CA C 52.663 0.2 1 945 233 GLU CB C 30.735 0.2 1 946 233 GLU N N 123.704 0.2 1 947 234 LEU H H 7.918 0.02 1 948 234 LEU CA C 55.847 0.2 1 949 234 LEU CB C 41.532 0.2 1 950 234 LEU N N 115.773 0.2 1 951 235 ASP H H 8.299 0.02 1 952 235 ASP CA C 52.75 0.2 1 953 235 ASP CB C 41.376 0.2 1 954 235 ASP CG C 181.134 0.2 1 955 235 ASP N N 119.681 0.2 1 956 236 ILE H H 8.112 0.02 1 957 236 ILE CA C 60.111 0.2 1 958 236 ILE CB C 37.775 0.2 1 959 236 ILE N N 119.247 0.2 1 960 237 ARG H H 8.434 0.02 1 961 237 ARG CA C 54.77 0.2 1 962 237 ARG CB C 32.427 0.2 1 963 237 ARG N N 123.047 0.2 1 964 238 MET H H 8.355 0.02 1 965 238 MET CA C 52.462 0.2 1 966 238 MET CB C 37.146 0.2 1 967 238 MET N N 117.215 0.2 1 968 239 ARG H H 8.514 0.02 1 969 239 ARG CA C 55.766 0.2 1 970 239 ARG CB C 28.763 0.2 1 971 239 ARG N N 120.962 0.2 1 972 240 THR H H 8.004 0.02 1 973 240 THR N N 117.635 0.2 1 974 244 ALA CA C 55.692 0.2 1 975 244 ALA CB C 18.236 0.2 1 976 245 THR H H 8.207 0.02 1 977 245 THR CA C 66.121 0.2 1 978 245 THR CB C 68.192 0.2 1 979 245 THR N N 117.838 0.2 1 980 246 LYS H H 8.997 0.02 1 981 246 LYS CA C 60.122 0.2 1 982 246 LYS CB C 34.725 0.2 1 983 246 LYS N N 125.588 0.2 1 984 247 LEU H H 8.453 0.02 1 985 247 LEU CA C 57.631 0.2 1 986 247 LEU CB C 41.589 0.2 1 987 247 LEU N N 117.207 0.2 1 988 248 ALA H H 7.929 0.02 1 989 248 ALA CA C 54.809 0.2 1 990 248 ALA CB C 17.602 0.2 1 991 248 ALA N N 125.039 0.2 1 992 249 THR H H 8.432 0.02 1 993 249 THR CA C 66.389 0.2 1 994 249 THR CB C 68.207 0.2 1 995 249 THR N N 120.81 0.2 1 996 250 GLN H H 8.613 0.02 1 997 250 GLN CA C 58.862 0.2 1 998 250 GLN CB C 30.304 0.2 1 999 250 GLN N N 120.237 0.2 1 1000 251 ALA H H 7.911 0.02 1 1001 251 ALA CA C 55.785 0.2 1 1002 251 ALA CB C 17.451 0.2 1 1003 251 ALA N N 122.184 0.2 1 1004 252 ALA H H 7.526 0.02 1 1005 252 ALA CA C 54.624 0.2 1 1006 252 ALA CB C 17.449 0.2 1 1007 252 ALA N N 120.753 0.2 1 1008 253 ASP H H 8.522 0.02 1 1009 253 ASP CA C 57.619 0.2 1 1010 253 ASP CB C 41.256 0.2 1 1011 253 ASP CG C 175.787 0.2 1 1012 253 ASP N N 123.051 0.2 1 1013 254 TYR H H 8.593 0.02 1 1014 254 TYR CA C 63.802 0.2 1 1015 254 TYR CB C 38.207 0.2 1 1016 254 TYR N N 121.246 0.2 1 1017 256 LYS CA C 59.499 0.2 1 1018 256 LYS CB C 32.686 0.2 1 1019 257 VAL H H 7.947 0.02 1 1020 257 VAL CA C 66.548 0.2 1 1021 257 VAL CB C 31.267 0.2 1 1022 257 VAL N N 120.566 0.2 1 1023 258 VAL H H 7.867 0.02 1 1024 258 VAL CA C 66.811 0.2 1 1025 258 VAL CB C 29.809 0.2 1 1026 258 VAL N N 118.283 0.2 1 1027 259 GLN H H 8.838 0.02 1 1028 259 GLN CA C 59.372 0.2 1 1029 259 GLN CB C 28.359 0.2 1 1030 259 GLN CD C 180.282 0.2 1 1031 259 GLN N N 119.015 0.2 1 1032 260 ALA H H 7.571 0.02 1 1033 260 ALA CA C 55.256 0.2 1 1034 260 ALA CB C 16.349 0.2 1 1035 260 ALA N N 121.678 0.2 1 1036 261 CYS H H 6.914 0.02 1 1037 261 CYS CA C 57.553 0.2 1 1038 261 CYS CB C 41.361 0.2 1 1039 261 CYS N N 111.495 0.2 1 1040 262 MET H H 8.411 0.02 1 1041 262 MET CA C 55.751 0.2 1 1042 262 MET CB C 30.038 0.2 1 1043 262 MET N N 118.519 0.2 1 1044 263 GLN H H 7.581 0.02 1 1045 263 GLN CA C 56.11 0.2 1 1046 263 GLN CB C 28.917 0.2 1 1047 263 GLN CD C 180.34 0.2 1 1048 263 GLN N N 116.864 0.2 1 1049 264 VAL H H 7.642 0.02 1 1050 264 VAL CA C 61.14 0.2 1 1051 264 VAL CB C 32.683 0.2 1 1052 264 VAL N N 124.225 0.2 1 1053 265 THR H H 9.106 0.02 1 1054 265 THR CA C 66.016 0.2 1 1055 265 THR CB C 68.324 0.2 1 1056 265 THR N N 123.952 0.2 1 1057 266 ARG H H 7.275 0.02 1 1058 266 ARG CA C 55.949 0.2 1 1059 266 ARG CB C 29.219 0.2 1 1060 266 ARG N N 114.298 0.2 1 1061 267 CYS H H 8.183 0.02 1 1062 267 CYS CA C 55.515 0.2 1 1063 267 CYS CB C 44.692 0.2 1 1064 267 CYS N N 122.437 0.2 1 1065 268 GLN H H 9.261 0.02 1 1066 268 GLN CA C 56.102 0.2 1 1067 268 GLN CB C 30.069 0.2 1 1068 268 GLN CD C 178.413 0.2 1 1069 268 GLN N N 128.552 0.2 1 1070 269 GLY H H 7.333 0.02 1 1071 269 GLY CA C 45.6 0.2 1 1072 269 GLY N N 101.509 0.2 1 1073 270 VAL H H 8.343 0.02 1 1074 270 VAL CA C 60.275 0.2 1 1075 270 VAL CB C 36.709 0.2 1 1076 270 VAL N N 118.599 0.2 1 1077 271 THR H H 8.623 0.02 1 1078 271 THR CA C 59.845 0.2 1 1079 271 THR CB C 70.182 0.2 1 1080 271 THR N N 127.841 0.2 1 1081 272 VAL H H 8.361 0.02 1 1082 272 VAL CA C 58.537 0.2 1 1083 272 VAL CB C 33.38 0.2 1 1084 272 VAL N N 120.006 0.2 1 1085 273 TRP H H 9.053 0.02 1 1086 273 TRP HE1 H 10.2 0.02 1 1087 273 TRP CA C 55.71 0.2 1 1088 273 TRP CB C 27.154 0.2 1 1089 273 TRP N N 129.73 0.2 1 1090 273 TRP NE1 N 147.43 0.2 1 1091 274 GLY H H 8.213 0.02 1 1092 274 GLY CA C 42.804 0.2 1 1093 274 GLY N N 112.074 0.2 1 1094 275 ILE H H 8.813 0.02 1 1095 275 ILE CA C 63.443 0.2 1 1096 275 ILE CB C 40.55 0.2 1 1097 275 ILE N N 115.981 0.2 1 1098 276 THR H H 7.166 0.02 1 1099 276 THR CA C 56.079 0.2 1 1100 276 THR CB C 69.514 0.2 1 1101 276 THR N N 109.982 0.2 1 1102 277 ASP H H 8.376 0.02 1 1103 277 ASP CA C 56.941 0.2 1 1104 277 ASP CB C 41.956 0.2 1 1105 277 ASP CG C 175.935 0.2 1 1106 277 ASP N N 130.942 0.2 1 1107 278 LYS H H 7.765 0.02 1 1108 278 LYS CA C 58.895 0.2 1 1109 278 LYS CB C 33.343 0.2 1 1110 278 LYS N N 118.978 0.2 1 1111 279 TYR H H 7.238 0.02 1 1112 279 TYR CA C 54.39 0.2 1 1113 279 TYR CB C 38.626 0.2 1 1114 279 TYR N N 115.941 0.2 1 1115 280 SER H H 7.16 0.02 1 1116 280 SER CA C 57.013 0.2 1 1117 280 SER CB C 64.129 0.2 1 1118 280 SER N N 113.952 0.2 1 1119 281 TRP H H 8.296 0.02 1 1120 281 TRP HE1 H 12.15 0.02 1 1121 281 TRP CA C 58.45 0.2 1 1122 281 TRP CB C 28.101 0.2 1 1123 281 TRP N N 128.455 0.2 1 1124 281 TRP NE1 N 135.13 0.2 1 1125 282 VAL H H 6.758 0.02 1 1126 282 VAL N N 119.805 0.2 1 1127 283 PRO CA C 64.694 0.2 1 1128 283 PRO CB C 30.531 0.2 1 1129 284 ASP H H 7.249 0.02 1 1130 284 ASP CA C 55.879 0.2 1 1131 284 ASP CB C 40.605 0.2 1 1132 284 ASP CG C 179.764 0.2 1 1133 284 ASP N N 115.479 0.2 1 1134 285 VAL H H 7.227 0.02 1 1135 285 VAL CA C 63.496 0.2 1 1136 285 VAL CB C 33.667 0.2 1 1137 285 VAL N N 119.966 0.2 1 1138 286 PHE H H 8.393 0.02 1 1139 286 PHE CA C 54.239 0.2 1 1140 286 PHE CB C 38.984 0.2 1 1141 286 PHE N N 121.254 0.2 1 1142 287 PRO CA C 63.45 0.2 1 1143 287 PRO CB C 30.999 0.2 1 1144 288 GLY H H 8.789 0.02 1 1145 288 GLY CA C 44.794 0.2 1 1146 288 GLY N N 112.004 0.2 1 1147 289 GLU H H 8.286 0.02 1 1148 289 GLU CA C 53.938 0.2 1 1149 289 GLU CB C 33.05 0.2 1 1150 289 GLU CD C 182.563 0.2 1 1151 289 GLU N N 120.099 0.2 1 1152 290 GLY H H 8.712 0.02 1 1153 290 GLY CA C 46.242 0.2 1 1154 290 GLY N N 104.677 0.2 1 1155 291 ALA H H 8.222 0.02 1 1156 291 ALA CA C 52.039 0.2 1 1157 291 ALA CB C 17.722 0.2 1 1158 291 ALA N N 124.476 0.2 1 1159 292 ALA H H 8.762 0.02 1 1160 292 ALA CA C 53.73 0.2 1 1161 292 ALA CB C 22.518 0.2 1 1162 292 ALA N N 120.703 0.2 1 1163 293 LEU H H 9.454 0.02 1 1164 293 LEU CA C 54.315 0.2 1 1165 293 LEU CB C 41.602 0.2 1 1166 293 LEU N N 123.58 0.2 1 1167 294 VAL H H 8.021 0.02 1 1168 294 VAL CA C 65.442 0.2 1 1169 294 VAL CB C 30.316 0.2 1 1170 294 VAL N N 119.448 0.2 1 1171 295 TRP H H 7.343 0.02 1 1172 295 TRP HE1 H 10.09 0.02 1 1173 295 TRP CA C 58.062 0.2 1 1174 295 TRP CB C 32.533 0.2 1 1175 295 TRP N N 116.558 0.2 1 1176 295 TRP NE1 N 130.5 0.2 1 1177 296 ASP H H 8.736 0.02 1 1178 296 ASP N N 120.04 0.2 1 1179 297 ALA CA C 54.194 0.2 1 1180 297 ALA CB C 17.898 0.2 1 1181 298 SER H H 8.445 0.02 1 1182 298 SER CA C 57.336 0.2 1 1183 298 SER CB C 63.89 0.2 1 1184 298 SER N N 114.518 0.2 1 1185 299 TYR H H 7.938 0.02 1 1186 299 TYR CA C 61.905 0.2 1 1187 299 TYR CB C 33.413 0.2 1 1188 299 TYR N N 113.737 0.2 1 1189 300 ALA H H 8.479 0.02 1 1190 300 ALA CA C 50.882 0.2 1 1191 300 ALA CB C 18.83 0.2 1 1192 300 ALA N N 123.581 0.2 1 1193 301 LYS H H 8.436 0.02 1 1194 301 LYS CA C 57.255 0.2 1 1195 301 LYS CB C 32.747 0.2 1 1196 301 LYS N N 122.122 0.2 1 1197 302 LYS H H 7.695 0.02 1 1198 302 LYS HZ H 8.062 0.02 1 1199 302 LYS CA C 55.024 0.2 1 1200 302 LYS CB C 29.623 0.2 1 1201 302 LYS N N 125.694 0.2 1 1202 302 LYS NZ N 34.834 0.2 2 1203 303 PRO CA C 65.376 0.2 1 1204 303 PRO CB C 30.571 0.2 1 1205 304 ALA H H 7.621 0.02 1 1206 304 ALA CA C 54.393 0.2 1 1207 304 ALA CB C 19.382 0.2 1 1208 304 ALA N N 117.32 0.2 1 1209 305 TYR H H 7.894 0.02 1 1210 305 TYR CA C 62.44 0.2 1 1211 305 TYR CB C 37.682 0.2 1 1212 305 TYR N N 118.39 0.2 1 1213 306 ALA H H 7.616 0.02 1 1214 306 ALA CA C 53.907 0.2 1 1215 306 ALA CB C 17.919 0.2 1 1216 306 ALA N N 120.338 0.2 1 1217 307 ALA H H 6.97 0.02 1 1218 307 ALA CA C 54.483 0.2 1 1219 307 ALA CB C 20.294 0.2 1 1220 307 ALA N N 120.603 0.2 1 1221 308 VAL H H 7.819 0.02 1 1222 308 VAL CA C 66.713 0.2 1 1223 308 VAL CB C 30.421 0.2 1 1224 308 VAL N N 119.579 0.2 1 1225 309 MET H H 7.472 0.02 1 1226 309 MET CA C 59.166 0.2 1 1227 309 MET CB C 31.843 0.2 1 1228 309 MET N N 118.787 0.2 1 1229 310 GLU H H 8.056 0.02 1 1230 310 GLU CA C 58.179 0.2 1 1231 310 GLU CB C 29.426 0.2 1 1232 310 GLU CD C 183.39 0.2 1 1233 310 GLU N N 117.934 0.2 1 1234 311 ALA H H 8.116 0.02 1 1235 311 ALA CA C 54.338 0.2 1 1236 311 ALA CB C 19.732 0.2 1 1237 311 ALA N N 124.059 0.2 1 1238 312 PHE H H 7.578 0.02 1 1239 312 PHE CA C 59.293 0.2 1 1240 312 PHE CB C 39.524 0.2 1 1241 312 PHE N N 115.027 0.2 1 1242 313 GLY H H 7.839 0.02 1 1243 313 GLY CA C 45.087 0.2 1 1244 313 GLY N N 106.953 0.2 1 1245 314 ALA H H 7.475 0.02 1 1246 314 ALA CA C 51.118 0.2 1 1247 314 ALA CB C 19.807 0.2 1 1248 314 ALA N N 123.55 0.2 1 1249 315 SER H H 8.121 0.02 1 1250 315 SER CA C 55.891 0.2 1 1251 315 SER CB C 63.728 0.2 1 1252 315 SER N N 116.684 0.2 1 stop_ save_