data_5618 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N and Side Chain 13C Chemical Shift Assignments for DFPase from Loligo vulgaris ; _BMRB_accession_number 5618 _BMRB_flat_file_name bmr5618.str _Entry_type original _Submission_date 2002-12-05 _Accession_date 2002-12-09 _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 Lohr Frank . . 2 Katsemi Vicky . . 3 Hartleib Judith . . 4 Ruterjans Heinz . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 634 "13C chemical shifts" 1230 "15N chemical shifts" 332 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-08-01 original BMRB . stop_ _Original_release_date 2002-12-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Strategy to Obtain Backbone Resonance Assignments of Deuterated Proteins in the Presence of Incomplete Amide (2)H/(1)H Back-exchange ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22651145 _PubMed_ID 12766392 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lohr Frank . . 2 Katsemi Vicky . . 3 Hartleib Judith . . 4 Gunther Ulrich . . 5 Ruterjans Heinz . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 25 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 291 _Page_last 311 _Year 2003 _Details . loop_ _Keyword DFPase TROSY 'fractional deuteration' 'multiple-quantum line narrowing' 'slow 2H/1H exchange' 'triple-resonance NMR' stop_ save_ ################################## # Molecular system description # ################################## save_system_DFPase _Saveframe_category molecular_system _Mol_system_name Diisopropylfluorophosphatase _Abbreviation_common DFPase _Enzyme_commission_number 3.1.8.2 loop_ _Mol_system_component_name _Mol_label Diisopropylfluorophosphatase $DFPase 'Calcium ion' $CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DFPase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Diisopropylfluorophosphatase _Abbreviation_common DFPase _Molecular_mass 35222 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 316 _Mol_residue_sequence ; GSMEIPVIEPLFTKVTEDIP GAEGPVFDKNGDFYIVAPEV EVNGKPAGEILRIDLKTGKK TVICKPEVNGYGGIPAGCQC DRDANQLFVADMRLGLLVVQ TDGTFEEIAKKDSEGRRMQG CNDCAFDYEGNLWITAPAGE VAPADYTRSMQEKFGSIYCF TTDGQMIQVDTAFQFPNGIA VRHMNDGRPYQLIVAETPTK KLWSYDIKGPAKIENKKVWG HIPGTHEGGADGMDFDEDNN LLVANWGSSHIEVFGPDGGQ PKMRIRCPFEKPSNLHFKPQ TKTIFVTEHENNAVWKFEWQ RNGKKQYCETLKFGIF ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 1 MET 4 2 GLU 5 3 ILE 6 4 PRO 7 5 VAL 8 6 ILE 9 7 GLU 10 8 PRO 11 9 LEU 12 10 PHE 13 11 THR 14 12 LYS 15 13 VAL 16 14 THR 17 15 GLU 18 16 ASP 19 17 ILE 20 18 PRO 21 19 GLY 22 20 ALA 23 21 GLU 24 22 GLY 25 23 PRO 26 24 VAL 27 25 PHE 28 26 ASP 29 27 LYS 30 28 ASN 31 29 GLY 32 30 ASP 33 31 PHE 34 32 TYR 35 33 ILE 36 34 VAL 37 35 ALA 38 36 PRO 39 37 GLU 40 38 VAL 41 39 GLU 42 40 VAL 43 41 ASN 44 42 GLY 45 43 LYS 46 44 PRO 47 45 ALA 48 46 GLY 49 47 GLU 50 48 ILE 51 49 LEU 52 50 ARG 53 51 ILE 54 52 ASP 55 53 LEU 56 54 LYS 57 55 THR 58 56 GLY 59 57 LYS 60 58 LYS 61 59 THR 62 60 VAL 63 61 ILE 64 62 CYS 65 63 LYS 66 64 PRO 67 65 GLU 68 66 VAL 69 67 ASN 70 68 GLY 71 69 TYR 72 70 GLY 73 71 GLY 74 72 ILE 75 73 PRO 76 74 ALA 77 75 GLY 78 76 CYS 79 77 GLN 80 78 CYS 81 79 ASP 82 80 ARG 83 81 ASP 84 82 ALA 85 83 ASN 86 84 GLN 87 85 LEU 88 86 PHE 89 87 VAL 90 88 ALA 91 89 ASP 92 90 MET 93 91 ARG 94 92 LEU 95 93 GLY 96 94 LEU 97 95 LEU 98 96 VAL 99 97 VAL 100 98 GLN 101 99 THR 102 100 ASP 103 101 GLY 104 102 THR 105 103 PHE 106 104 GLU 107 105 GLU 108 106 ILE 109 107 ALA 110 108 LYS 111 109 LYS 112 110 ASP 113 111 SER 114 112 GLU 115 113 GLY 116 114 ARG 117 115 ARG 118 116 MET 119 117 GLN 120 118 GLY 121 119 CYS 122 120 ASN 123 121 ASP 124 122 CYS 125 123 ALA 126 124 PHE 127 125 ASP 128 126 TYR 129 127 GLU 130 128 GLY 131 129 ASN 132 130 LEU 133 131 TRP 134 132 ILE 135 133 THR 136 134 ALA 137 135 PRO 138 136 ALA 139 137 GLY 140 138 GLU 141 139 VAL 142 140 ALA 143 141 PRO 144 142 ALA 145 143 ASP 146 144 TYR 147 145 THR 148 146 ARG 149 147 SER 150 148 MET 151 149 GLN 152 150 GLU 153 151 LYS 154 152 PHE 155 153 GLY 156 154 SER 157 155 ILE 158 156 TYR 159 157 CYS 160 158 PHE 161 159 THR 162 160 THR 163 161 ASP 164 162 GLY 165 163 GLN 166 164 MET 167 165 ILE 168 166 GLN 169 167 VAL 170 168 ASP 171 169 THR 172 170 ALA 173 171 PHE 174 172 GLN 175 173 PHE 176 174 PRO 177 175 ASN 178 176 GLY 179 177 ILE 180 178 ALA 181 179 VAL 182 180 ARG 183 181 HIS 184 182 MET 185 183 ASN 186 184 ASP 187 185 GLY 188 186 ARG 189 187 PRO 190 188 TYR 191 189 GLN 192 190 LEU 193 191 ILE 194 192 VAL 195 193 ALA 196 194 GLU 197 195 THR 198 196 PRO 199 197 THR 200 198 LYS 201 199 LYS 202 200 LEU 203 201 TRP 204 202 SER 205 203 TYR 206 204 ASP 207 205 ILE 208 206 LYS 209 207 GLY 210 208 PRO 211 209 ALA 212 210 LYS 213 211 ILE 214 212 GLU 215 213 ASN 216 214 LYS 217 215 LYS 218 216 VAL 219 217 TRP 220 218 GLY 221 219 HIS 222 220 ILE 223 221 PRO 224 222 GLY 225 223 THR 226 224 HIS 227 225 GLU 228 226 GLY 229 227 GLY 230 228 ALA 231 229 ASP 232 230 GLY 233 231 MET 234 232 ASP 235 233 PHE 236 234 ASP 237 235 GLU 238 236 ASP 239 237 ASN 240 238 ASN 241 239 LEU 242 240 LEU 243 241 VAL 244 242 ALA 245 243 ASN 246 244 TRP 247 245 GLY 248 246 SER 249 247 SER 250 248 HIS 251 249 ILE 252 250 GLU 253 251 VAL 254 252 PHE 255 253 GLY 256 254 PRO 257 255 ASP 258 256 GLY 259 257 GLY 260 258 GLN 261 259 PRO 262 260 LYS 263 261 MET 264 262 ARG 265 263 ILE 266 264 ARG 267 265 CYS 268 266 PRO 269 267 PHE 270 268 GLU 271 269 LYS 272 270 PRO 273 271 SER 274 272 ASN 275 273 LEU 276 274 HIS 277 275 PHE 278 276 LYS 279 277 PRO 280 278 GLN 281 279 THR 282 280 LYS 283 281 THR 284 282 ILE 285 283 PHE 286 284 VAL 287 285 THR 288 286 GLU 289 287 HIS 290 288 GLU 291 289 ASN 292 290 ASN 293 291 ALA 294 292 VAL 295 293 TRP 296 294 LYS 297 295 PHE 298 296 GLU 299 297 TRP 300 298 GLN 301 299 ARG 302 300 ASN 303 301 GLY 304 302 LYS 305 303 LYS 306 304 GLN 307 305 TYR 308 306 CYS 309 307 GLU 310 308 THR 311 309 LEU 312 310 LYS 313 311 PHE 314 312 GLY 315 313 ILE 316 314 PHE stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 1E1A 'Crystal Structure Of Dfpase From Loligo Vulgaris' 99.37 314 100.00 100.00 0.00e+00 PDB 1PJX '0.85 Angstrom Structure Of Squid Ganglion Dfpase' 99.37 314 100.00 100.00 0.00e+00 PDB 2GVU 'Crystal Structure Of Diisopropyl Fluorophosphatase (Dfpase), Mutant D229n N120D' 99.37 314 99.36 100.00 0.00e+00 PDB 2GVV 'Structure Of Diisopropyl Fluorophosphatase (Dfpase) In Complex With Dicyclopentylphosphoroamidate (Dcppa)' 99.37 314 100.00 100.00 0.00e+00 PDB 2GVW 'Structure Of Diisopropyl Fluorophosphatase (Dfpase) Holoenzyme (Rt)' 99.37 314 100.00 100.00 0.00e+00 PDB 2GVX 'Structure Of Diisopropyl Fluorophosphatase (Dfpase), Mutant D229n N175D' 99.37 314 99.36 100.00 0.00e+00 PDB 2IAO 'Crystal Structure Of Squid Ganglion Dfpase E37q Mutant' 98.73 312 99.68 100.00 0.00e+00 PDB 2IAP 'Crystal Structure Of Squid Ganglion Dfpase E21q Mutant' 98.73 312 99.68 100.00 0.00e+00 PDB 2IAQ 'Crystal Structure Of Squid Ganglion Dfpase S271a Mutant' 98.73 312 99.68 100.00 0.00e+00 PDB 2IAR 'Crystal Structure Of Squid Ganglion Dfpase W244h Mutant' 98.73 312 99.68 99.68 0.00e+00 PDB 2IAS 'Crystal Structure Of Squid Ganglion Dfpase W244f Mutant' 98.73 312 99.68 100.00 0.00e+00 PDB 2IAT 'Crystal Structure Of Squid Ganglion Dfpase W244l Mutant' 98.73 312 99.68 99.68 0.00e+00 PDB 2IAU 'Crystal Structure Of Squid Ganglion Dfpase W244y Mutant' 98.73 312 99.68 100.00 0.00e+00 PDB 2IAV 'Crystal Structure Of Squid Ganglion Dfpase H287a Mutant' 98.73 312 99.68 99.68 0.00e+00 PDB 2IAW 'Crystal Structure Of Squid Ganglion Dfpase N175d Mutant' 98.73 312 99.68 100.00 0.00e+00 PDB 2IAX 'Crystal Structure Of Squid Ganglion Dfpase D232s Mutant' 98.73 312 99.68 99.68 0.00e+00 SWISS-PROT Q7SIG4 'Diisopropyl-fluorophosphatase (DFPase)' 99.37 314 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type non-polymer _Name_common "CA (CALCIUM ION)" _BMRB_code . _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 9 15:51:10 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ _Tissue _Gene_mnemonic $DFPase Squid 6622 Eukaryota Metazoa Loligo vulgaris head ganglion DFPase 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 $DFPase 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pKKH 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 $DFPase 1.6 mM '[U-98% 13C; U-98% 15N]' Bis-Tris-propane 10 mM . 'calcium chloride' 5 mM . 'sodium azide' 0.03 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DFPase 0.9 mM '[U-98% 13C; U-98% 15N; U-95% 2H]' Bis-Tris-propane 10 mM . 'calcium chloride' 5 mM . 'sodium azide' 0.03 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DFPase 1.0 mM '[U-98% 15N]' Bis-Tris-propane 10 mM . 'calcium chloride' 5 mM . 'sodium azide' 0.03 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $DFPase 0.6 mM '[U-98% 13C; U-98% 15N; 20-95% 2H]' Bis-Tris-propane 10 mM . 'calcium chloride' 5 mM . 'sodium azide' 0.03 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_[15N,1H]-TROSY-HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-TROSY-HNCO _Sample_label . save_ save_[15N,1H]-TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-TROSY-HNCA _Sample_label . save_ save_[15N,1H]-TROSY-HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-TROSY-HNCACB _Sample_label . save_ save_[15N,1H]-TROSY-HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-TROSY-HN(CA)CO _Sample_label . save_ save_[15N,1H]-TROSY-HNCAN_5 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-TROSY-HNCAN _Sample_label . save_ save_(HCA)CO(CA)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name (HCA)CO(CA)NH _Sample_label . save_ save_H(CACO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CACO)NH _Sample_label . save_ save_H(CA)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name H(CA)NH _Sample_label . save_ save_HCACO_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCACO _Sample_label . save_ save_HCACB_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCACB _Sample_label . save_ save_CC(CO)NH-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH-TOCSY _Sample_label . save_ save_(H)CC(CO)NH-TOCSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name (H)CC(CO)NH-TOCSY _Sample_label . save_ save_CC(CA)NH_TOCSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name 'CC(CA)NH TOCSY' _Sample_label . save_ save_[15N,1H]-TROSY-(HNCAC)C(C)CANH_TOCSY_14 _Saveframe_category NMR_applied_experiment _Experiment_name '[15N,1H]-TROSY-(HNCAC)C(C)CANH TOCSY' _Sample_label . save_ save_[13C,1H]-TROSY-HCDCG_15 _Saveframe_category NMR_applied_experiment _Experiment_name [13C,1H]-TROSY-HCDCG _Sample_label . save_ save_[13C,1H]-TROSY-HCD(CG)CB_16 _Saveframe_category NMR_applied_experiment _Experiment_name [13C,1H]-TROSY-HCD(CG)CB _Sample_label . save_ save_[15N,1H]-TROSY-HN(CDCG)CB_17 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-TROSY-HN(CDCG)CB _Sample_label . save_ save_[13C,1H]-TROSY-HCN_18 _Saveframe_category NMR_applied_experiment _Experiment_name [13C,1H]-TROSY-HCN _Sample_label . save_ save_[15N,1H]-TROSY-H(N)C_19 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-TROSY-H(N)C _Sample_label . save_ save_[15N,1H]-HMBC_20 _Saveframe_category NMR_applied_experiment _Experiment_name [15N,1H]-HMBC _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 pH temperature 301 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; The effect of TROSY on 1HN and 15N chemical shifts has been corrected based on a uniform 1JNH coupling constant of 94 Hz. Chemical shifts of 13C resonances only observed in spectra of deuterated protein have been corrected for the 2H isotope effect. ; loop_ _Experiment_label [15N,1H]-TROSY-HNCO [15N,1H]-TROSY-HNCA [15N,1H]-TROSY-HNCACB [15N,1H]-TROSY-HN(CA)CO stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Diisopropylfluorophosphatase _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 1 3 MET H H 8.54 0.03 1 2 1 3 MET HA H 4.48 0.03 1 3 1 3 MET C C 176.05 0.1 1 4 1 3 MET CA C 55.55 0.1 1 5 1 3 MET CB C 33 0.1 1 6 1 3 MET CG C 32.05 0.1 1 7 1 3 MET N N 122.13 0.2 1 8 2 4 GLU H H 8.4 0.03 1 9 2 4 GLU HA H 4.29 0.03 1 10 2 4 GLU C C 176.05 0.1 1 11 2 4 GLU CA C 56.25 0.1 1 12 2 4 GLU CB C 30.07 0.1 1 13 2 4 GLU CG C 36.14 0.1 1 14 2 4 GLU N N 122.7 0.2 1 15 3 5 ILE H H 7.99 0.03 1 16 3 5 ILE HA H 4.31 0.03 1 17 3 5 ILE C C 174.24 0.1 1 18 3 5 ILE CA C 59.13 0.1 1 19 3 5 ILE CB C 39.51 0.1 1 20 3 5 ILE CG1 C 26.9 0.1 1 21 3 5 ILE CG2 C 17.45 0.1 1 22 3 5 ILE CD1 C 13.32 0.1 1 23 3 5 ILE N N 124.1 0.2 1 24 4 6 PRO HA H 4.39 0.03 1 25 4 6 PRO C C 175.08 0.1 1 26 4 6 PRO CA C 63.69 0.1 1 27 4 6 PRO CB C 32.9 0.1 1 28 4 6 PRO CG C 27.72 0.1 1 29 4 6 PRO CD C 51.06 0.1 1 30 4 6 PRO N N 140.01 0.2 1 31 5 7 VAL H H 8.17 0.03 1 32 5 7 VAL HA H 5.16 0.03 1 33 5 7 VAL C C 177.05 0.1 1 34 5 7 VAL CA C 60.38 0.1 1 35 5 7 VAL CB C 34.89 0.1 1 36 5 7 VAL CG1 C 21.94 0.1 2 37 5 7 VAL N N 120.95 0.2 1 38 6 8 ILE H H 8.98 0.03 1 39 6 8 ILE HA H 4.78 0.03 1 40 6 8 ILE C C 174.3 0.1 1 41 6 8 ILE CA C 59.8 0.1 1 42 6 8 ILE CB C 41.48 0.1 1 43 6 8 ILE CG1 C 27 0.1 1 44 6 8 ILE CG2 C 17.97 0.1 1 45 6 8 ILE CD1 C 14.1 0.1 1 46 6 8 ILE N N 122.6 0.2 1 47 7 9 GLU H H 8.74 0.03 1 48 7 9 GLU HA H 4.98 0.03 1 49 7 9 GLU C C 172.98 0.1 1 50 7 9 GLU CA C 53.31 0.1 1 51 7 9 GLU CB C 30.74 0.1 1 52 7 9 GLU CG C 36.8 0.1 1 53 7 9 GLU N N 122.83 0.2 1 54 8 10 PRO HA H 4.62 0.03 1 55 8 10 PRO C C 175.18 0.1 1 56 8 10 PRO CA C 62.29 0.1 1 57 8 10 PRO CB C 32.89 0.1 1 58 8 10 PRO CG C 27 0.1 1 59 8 10 PRO CD C 50.2 0.1 1 60 8 10 PRO N N 135.85 0.2 1 61 9 11 LEU H H 8.21 0.03 1 62 9 11 LEU HA H 4.54 0.03 1 63 9 11 LEU C C 177.55 0.1 1 64 9 11 LEU CA C 55.54 0.1 1 65 9 11 LEU CB C 42.23 0.1 1 66 9 11 LEU CG C 27.2 0.1 1 67 9 11 LEU CD1 C 24.88 0.1 2 68 9 11 LEU CD2 C 24.3 0.1 2 69 9 11 LEU N N 120.03 0.2 1 70 10 12 PHE H H 9.33 0.03 1 71 10 12 PHE HA H 5.42 0.03 1 72 10 12 PHE C C 176.23 0.1 1 73 10 12 PHE CA C 56.89 0.1 1 74 10 12 PHE CB C 41.94 0.1 1 75 10 12 PHE N N 129.24 0.2 1 76 11 13 THR H H 9.41 0.03 1 77 11 13 THR HA H 4.82 0.03 1 78 11 13 THR C C 173.81 0.1 1 79 11 13 THR CA C 61.81 0.1 1 80 11 13 THR CB C 71.28 0.1 1 81 11 13 THR CG2 C 21.14 0.1 1 82 11 13 THR N N 117.53 0.2 1 83 12 14 LYS H H 9.17 0.03 1 84 12 14 LYS HA H 3.52 0.03 1 85 12 14 LYS C C 176.02 0.1 1 86 12 14 LYS CA C 58.18 0.1 1 87 12 14 LYS CB C 31.32 0.1 1 88 12 14 LYS CG C 23.77 0.1 1 89 12 14 LYS CD C 28.8 0.1 1 90 12 14 LYS CE C 41.05 0.1 1 91 12 14 LYS N N 131.69 0.2 1 92 13 15 VAL H H 9.32 0.03 1 93 13 15 VAL HA H 4.02 0.03 1 94 13 15 VAL C C 175.53 0.1 1 95 13 15 VAL CA C 63.83 0.1 1 96 13 15 VAL CB C 33.73 0.1 1 97 13 15 VAL CG1 C 20.7 0.1 2 98 13 15 VAL CG2 C 19.9 0.1 2 99 13 15 VAL N N 126.91 0.2 1 100 14 16 THR H H 7.52 0.03 1 101 14 16 THR HA H 4.57 0.03 1 102 14 16 THR C C 171.49 0.1 1 103 14 16 THR CA C 61.52 0.1 1 104 14 16 THR CB C 67.17 0.1 1 105 14 16 THR CG2 C 20.02 0.1 1 106 14 16 THR N N 110.77 0.2 1 107 15 17 GLU H H 8.12 0.03 1 108 15 17 GLU HA H 4.92 0.03 1 109 15 17 GLU C C 173.48 0.1 1 110 15 17 GLU CA C 55.2 0.1 1 111 15 17 GLU CB C 33.24 0.1 1 112 15 17 GLU CG C 34.88 0.1 1 113 15 17 GLU N N 119.91 0.2 1 114 16 18 ASP H H 8.54 0.03 1 115 16 18 ASP HA H 4.37 0.03 1 116 16 18 ASP C C 174.67 0.1 1 117 16 18 ASP CA C 55.22 0.1 1 118 16 18 ASP CB C 39.02 0.1 1 119 16 18 ASP N N 117.42 0.2 1 120 17 19 ILE H H 8.42 0.03 1 121 17 19 ILE HA H 4.41 0.03 1 122 17 19 ILE C C 173.26 0.1 1 123 17 19 ILE CA C 58.17 0.1 1 124 17 19 ILE CB C 38.4 0.1 1 125 17 19 ILE CG1 C 26.9 0.1 1 126 17 19 ILE CG2 C 19.52 0.1 1 127 17 19 ILE CD1 C 14.85 0.1 1 128 17 19 ILE N N 118.35 0.2 1 129 18 20 PRO HA H 3.82 0.03 1 130 18 20 PRO C C 177.18 0.1 1 131 18 20 PRO CA C 64.76 0.1 1 132 18 20 PRO CB C 31.56 0.1 1 133 18 20 PRO CD C 50.65 0.1 1 134 18 20 PRO N N 138.94 0.2 1 135 19 21 GLY H H 8.22 0.03 1 136 19 21 GLY HA2 H 3.35 0.03 2 137 19 21 GLY C C 173.49 0.1 1 138 19 21 GLY CA C 46.7 0.1 1 139 19 21 GLY N N 115 0.2 1 140 20 22 ALA H H 7.61 0.03 1 141 20 22 ALA HA H 4.15 0.03 1 142 20 22 ALA C C 176.31 0.1 1 143 20 22 ALA CA C 54.77 0.1 1 144 20 22 ALA CB C 19.87 0.1 1 145 20 22 ALA N N 119.03 0.2 1 146 21 23 GLU H H 8.99 0.03 1 147 21 23 GLU HA H 5.06 0.03 1 148 21 23 GLU C C 177.21 0.1 1 149 21 23 GLU CA C 56.86 0.1 1 150 21 23 GLU CB C 36.12 0.1 1 151 21 23 GLU CG C 32.8 0.1 1 152 21 23 GLU N N 135.65 0.2 1 153 22 24 GLY H H 10.57 0.03 1 154 22 24 GLY HA2 H 3.8 0.03 2 155 22 24 GLY C C 169.5 0.1 1 156 22 24 GLY CA C 50.39 0.1 1 157 22 24 GLY N N 105.62 0.2 1 158 23 25 PRO C C 174.96 0.1 1 159 23 25 PRO N N 134.2 0.2 1 160 24 26 VAL H H 7.08 0.03 1 161 24 26 VAL HA H 3.52 0.03 1 162 24 26 VAL C C 171.62 0.1 1 163 24 26 VAL CA C 61.1 0.1 1 164 24 26 VAL CB C 34.38 0.1 1 165 24 26 VAL CG1 C 22.1 0.1 2 166 24 26 VAL CG2 C 20.3 0.1 2 167 24 26 VAL N N 110.3 0.2 1 168 25 27 PHE H H 6.3 0.03 1 169 25 27 PHE HA H 6.2 0.03 1 170 25 27 PHE C C 177.18 0.1 1 171 25 27 PHE CA C 56.27 0.1 1 172 25 27 PHE CB C 43.72 0.1 1 173 25 27 PHE N N 121.03 0.2 1 174 26 28 ASP H H 9.33 0.03 1 175 26 28 ASP HA H 5.51 0.03 1 176 26 28 ASP C C 179.06 0.1 1 177 26 28 ASP CA C 52.37 0.1 1 178 26 28 ASP CB C 42.4 0.1 1 179 26 28 ASP N N 122.48 0.2 1 180 27 29 LYS H H 8.51 0.03 1 181 27 29 LYS HA H 4.14 0.03 1 182 27 29 LYS C C 178.39 0.1 1 183 27 29 LYS CA C 59.58 0.1 1 184 27 29 LYS CB C 31.6 0.1 1 185 27 29 LYS CG C 25.71 0.1 1 186 27 29 LYS CD C 28.55 0.1 1 187 27 29 LYS CE C 41.12 0.1 1 188 27 29 LYS N N 116.86 0.2 1 189 28 30 ASN H H 8 0.03 1 190 28 30 ASN HA H 4.9 0.03 1 191 28 30 ASN C C 175.58 0.1 1 192 28 30 ASN CA C 52.75 0.1 1 193 28 30 ASN CB C 39.15 0.1 1 194 28 30 ASN N N 114.83 0.2 1 195 29 31 GLY H H 8.18 0.03 1 196 29 31 GLY HA2 H 4.42 0.03 2 197 29 31 GLY C C 174.62 0.1 1 198 29 31 GLY CA C 45.81 0.1 1 199 29 31 GLY N N 108.3 0.2 1 200 30 32 ASP H H 8.57 0.03 1 201 30 32 ASP HA H 4.9 0.03 1 202 30 32 ASP C C 173.9 0.1 1 203 30 32 ASP CA C 55.03 0.1 1 204 30 32 ASP CB C 41.62 0.1 1 205 30 32 ASP N N 122.59 0.2 1 206 31 33 PHE H H 8.79 0.03 1 207 31 33 PHE HA H 4.7 0.03 1 208 31 33 PHE C C 172.59 0.1 1 209 31 33 PHE CA C 55.16 0.1 1 210 31 33 PHE CB C 42.29 0.1 1 211 31 33 PHE N N 122.54 0.2 1 212 32 34 TYR H H 8.21 0.03 1 213 32 34 TYR HA H 5.19 0.03 1 214 32 34 TYR C C 173.15 0.1 1 215 32 34 TYR CA C 54.89 0.1 1 216 32 34 TYR CB C 40.29 0.1 1 217 32 34 TYR N N 124.36 0.2 1 218 33 35 ILE H H 8.25 0.03 1 219 33 35 ILE HA H 4.31 0.03 1 220 33 35 ILE C C 174.17 0.1 1 221 33 35 ILE CA C 57.95 0.1 1 222 33 35 ILE CB C 42.19 0.1 1 223 33 35 ILE CG1 C 26.16 0.1 1 224 33 35 ILE CG2 C 19.29 0.1 1 225 33 35 ILE CD1 C 14.75 0.1 1 226 33 35 ILE N N 113.33 0.2 1 227 34 36 VAL H H 8.14 0.03 1 228 34 36 VAL HA H 5 0.03 1 229 34 36 VAL C C 173.34 0.1 1 230 34 36 VAL CA C 58.84 0.1 1 231 34 36 VAL CB C 33.62 0.1 1 232 34 36 VAL N N 113.18 0.2 1 233 35 37 ALA H H 8.67 0.03 1 234 35 37 ALA HA H 4.88 0.03 1 235 35 37 ALA C C 175.15 0.1 1 236 35 37 ALA CA C 48 0.1 1 237 35 37 ALA CB C 21.33 0.1 1 238 35 37 ALA N N 122.8 0.2 1 239 37 39 GLU HA H 4.27 0.03 1 240 37 39 GLU C C 175.49 0.1 1 241 37 39 GLU CA C 55.85 0.1 1 242 37 39 GLU CB C 29.34 0.1 1 243 37 39 GLU CG C 37.13 0.1 1 244 38 40 VAL H H 6.58 0.03 1 245 38 40 VAL HA H 3.71 0.03 1 246 38 40 VAL C C 175.49 0.1 1 247 38 40 VAL CA C 64.27 0.1 1 248 38 40 VAL CB C 31.79 0.1 1 249 38 40 VAL CG1 C 22.41 0.1 2 250 38 40 VAL N N 120.22 0.2 1 251 39 41 GLU H H 8.56 0.03 1 252 39 41 GLU HA H 4.94 0.03 1 253 39 41 GLU C C 175.76 0.1 1 254 39 41 GLU CA C 54.82 0.1 1 255 39 41 GLU CB C 34.46 0.1 1 256 39 41 GLU CG C 35.85 0.1 1 257 39 41 GLU N N 128.29 0.2 1 258 40 42 VAL H H 8.61 0.03 1 259 40 42 VAL HA H 4.17 0.03 1 260 40 42 VAL C C 176.8 0.1 1 261 40 42 VAL CA C 61.81 0.1 1 262 40 42 VAL CB C 33.6 0.1 1 263 40 42 VAL CG1 C 21.41 0.1 2 264 40 42 VAL CG2 C 20.6 0.1 2 265 40 42 VAL N N 121.04 0.2 1 266 41 43 ASN HA H 4.38 0.03 1 267 41 43 ASN C C 175.4 0.1 1 268 41 43 ASN CA C 54.26 0.1 1 269 41 43 ASN CB C 37.34 0.1 1 270 42 44 GLY H H 8.73 0.03 1 271 42 44 GLY HA2 H 4.06 0.03 2 272 42 44 GLY HA3 H 3.72 0.03 2 273 42 44 GLY C C 173.82 0.1 1 274 42 44 GLY CA C 45.56 0.1 1 275 42 44 GLY N N 103.02 0.2 1 276 43 45 LYS H H 7.72 0.03 1 277 43 45 LYS HA H 4.92 0.03 1 278 43 45 LYS C C 173.61 0.1 1 279 43 45 LYS CA C 52.95 0.1 1 280 43 45 LYS CB C 33.42 0.1 1 281 43 45 LYS CG C 24.65 0.1 1 282 43 45 LYS CD C 28.9 0.1 1 283 43 45 LYS CE C 42.65 0.1 1 284 43 45 LYS N N 120.57 0.2 1 285 44 46 PRO HA H 4.19 0.03 1 286 44 46 PRO C C 177.01 0.1 1 287 44 46 PRO CA C 64.74 0.1 1 288 44 46 PRO CB C 32.45 0.1 1 289 44 46 PRO CG C 28.2 0.1 1 290 44 46 PRO CD C 51.4 0.1 1 291 44 46 PRO N N 133.07 0.2 1 292 45 47 ALA H H 8.21 0.03 1 293 45 47 ALA HA H 4.62 0.03 1 294 45 47 ALA C C 175.78 0.1 1 295 45 47 ALA CA C 51.3 0.1 1 296 45 47 ALA CB C 19.13 0.1 1 297 45 47 ALA N N 128.89 0.2 1 298 46 48 GLY H H 8.4 0.03 1 299 46 48 GLY HA2 H 3.71 0.03 2 300 46 48 GLY C C 172.87 0.1 1 301 46 48 GLY CA C 46.89 0.1 1 302 46 48 GLY N N 106.07 0.2 1 303 47 49 GLU H H 7.05 0.03 1 304 47 49 GLU HA H 5.03 0.03 1 305 47 49 GLU C C 174.5 0.1 1 306 47 49 GLU CA C 54.45 0.1 1 307 47 49 GLU CB C 35.35 0.1 1 308 47 49 GLU CG C 35.87 0.1 1 309 47 49 GLU N N 113.71 0.2 1 310 48 50 ILE H H 8.48 0.03 1 311 48 50 ILE HA H 4.36 0.03 1 312 48 50 ILE C C 174.65 0.1 1 313 48 50 ILE CA C 61.73 0.1 1 314 48 50 ILE CB C 38.77 0.1 1 315 48 50 ILE CG1 C 27.27 0.1 1 316 48 50 ILE CG2 C 15.73 0.1 1 317 48 50 ILE N N 119.63 0.2 1 318 49 51 LEU H H 9.23 0.03 1 319 49 51 LEU HA H 5.32 0.03 1 320 49 51 LEU C C 174.81 0.1 1 321 49 51 LEU CA C 54.36 0.1 1 322 49 51 LEU CB C 45.63 0.1 1 323 49 51 LEU CG C 26.99 0.1 2 324 49 51 LEU N N 127.85 0.2 1 325 50 52 ARG H H 8.98 0.03 1 326 50 52 ARG HA H 4.65 0.03 1 327 50 52 ARG HE H 6.85 0.03 1 328 50 52 ARG C C 175.51 0.1 1 329 50 52 ARG CA C 54.39 0.1 1 330 50 52 ARG CB C 33.89 0.1 1 331 50 52 ARG CG C 27.48 0.1 1 332 50 52 ARG CD C 43.57 0.1 1 333 50 52 ARG CZ C 159.8 0.1 1 334 50 52 ARG N N 120.8 0.2 1 335 50 52 ARG NE N 84.35 0.2 1 336 51 53 ILE H H 8.45 0.03 1 337 51 53 ILE HA H 4.63 0.03 1 338 51 53 ILE C C 175.41 0.1 1 339 51 53 ILE CA C 57.21 0.1 1 340 51 53 ILE CB C 38.8 0.1 1 341 51 53 ILE CG1 C 27.1 0.1 1 342 51 53 ILE CG2 C 16.51 0.1 1 343 51 53 ILE CD1 C 11.45 0.1 1 344 51 53 ILE N N 126.55 0.2 1 345 52 54 ASP H H 8.44 0.03 1 346 52 54 ASP HA H 4.65 0.03 1 347 52 54 ASP C C 177.06 0.1 1 348 52 54 ASP CA C 53.58 0.1 1 349 52 54 ASP CB C 42.17 0.1 1 350 52 54 ASP N N 126.73 0.2 1 351 53 55 LEU H H 8.86 0.03 1 352 53 55 LEU HA H 4 0.03 1 353 53 55 LEU C C 178.58 0.1 1 354 53 55 LEU CA C 56.94 0.1 1 355 53 55 LEU CB C 41.57 0.1 1 356 53 55 LEU CG C 25.55 0.1 1 357 53 55 LEU CD1 C 26.86 0.1 2 358 53 55 LEU CD2 C 23.6 0.1 2 359 53 55 LEU N N 127.68 0.2 1 360 54 56 LYS H H 8.6 0.03 1 361 54 56 LYS HA H 4.31 0.03 1 362 54 56 LYS C C 178.42 0.1 1 363 54 56 LYS CA C 58.72 0.1 1 364 54 56 LYS CB C 32.74 0.1 1 365 54 56 LYS CG C 25.32 0.1 1 366 54 56 LYS CD C 29 0.1 1 367 54 56 LYS CE C 42 0.1 1 368 54 56 LYS N N 118.13 0.2 1 369 55 57 THR H H 7.53 0.03 1 370 55 57 THR HA H 4.52 0.03 1 371 55 57 THR C C 176.59 0.1 1 372 55 57 THR CA C 61.51 0.1 1 373 55 57 THR CB C 71.77 0.1 1 374 55 57 THR CG2 C 21.14 0.1 1 375 55 57 THR N N 105.14 0.2 1 376 56 58 GLY H H 8.77 0.03 1 377 56 58 GLY HA2 H 4.37 0.03 2 378 56 58 GLY C C 173.81 0.1 1 379 56 58 GLY CA C 46.04 0.1 1 380 56 58 GLY N N 112.54 0.2 1 381 57 59 LYS H H 7.74 0.03 1 382 57 59 LYS HA H 4.19 0.03 1 383 57 59 LYS C C 176.37 0.1 1 384 57 59 LYS CA C 57.55 0.1 1 385 57 59 LYS CB C 33.24 0.1 1 386 57 59 LYS CG C 25.34 0.1 1 387 57 59 LYS CD C 29.06 0.1 1 388 57 59 LYS CE C 42.21 0.1 1 389 57 59 LYS N N 120.3 0.2 1 390 58 60 LYS H H 8.68 0.03 1 391 58 60 LYS HA H 4.94 0.03 1 392 58 60 LYS C C 176.23 0.1 1 393 58 60 LYS CA C 55.21 0.1 1 394 58 60 LYS CB C 34.84 0.1 1 395 58 60 LYS CG C 24.11 0.1 1 396 58 60 LYS CD C 29.51 0.1 1 397 58 60 LYS CE C 41.8 0.1 1 398 58 60 LYS N N 124.45 0.2 1 399 59 61 THR H H 8.95 0.03 1 400 59 61 THR HA H 4.47 0.03 1 401 59 61 THR C C 173.56 0.1 1 402 59 61 THR CA C 61.84 0.1 1 403 59 61 THR CB C 71.84 0.1 1 404 59 61 THR CG2 C 20.98 0.1 1 405 59 61 THR N N 119.42 0.2 1 406 60 62 VAL H H 9.09 0.03 1 407 60 62 VAL HA H 3.96 0.03 1 408 60 62 VAL C C 176.16 0.1 1 409 60 62 VAL CA C 63.74 0.1 1 410 60 62 VAL CB C 31.4 0.1 1 411 60 62 VAL CG1 C 21.4 0.1 2 412 60 62 VAL N N 128.27 0.2 1 413 61 63 ILE H H 9 0.03 1 414 61 63 ILE HA H 4.44 0.03 1 415 61 63 ILE C C 175.66 0.1 1 416 61 63 ILE CA C 60.31 0.1 1 417 61 63 ILE CB C 38.58 0.1 1 418 61 63 ILE CG1 C 26.76 0.1 1 419 61 63 ILE CG2 C 18.14 0.1 1 420 61 63 ILE CD1 C 11.95 0.1 1 421 61 63 ILE N N 125.74 0.2 1 422 62 64 CYS H H 7.49 0.03 1 423 62 64 CYS HA H 4.52 0.03 1 424 62 64 CYS C C 171.74 0.1 1 425 62 64 CYS CA C 58.39 0.1 1 426 62 64 CYS CB C 30.4 0.1 1 427 62 64 CYS N N 116.86 0.2 1 428 63 65 LYS H H 8.75 0.03 1 429 63 65 LYS HA H 5 0.03 1 430 63 65 LYS C C 173.04 0.1 1 431 63 65 LYS CA C 53 0.1 1 432 63 65 LYS CB C 32.8 0.1 1 433 63 65 LYS CG C 24.55 0.1 1 434 63 65 LYS CD C 30.05 0.1 1 435 63 65 LYS CE C 41.92 0.1 1 436 63 65 LYS N N 130.86 0.2 1 437 64 66 PRO HA H 3.15 0.03 1 438 64 66 PRO C C 175.97 0.1 1 439 64 66 PRO CA C 63.54 0.1 1 440 64 66 PRO CB C 32.26 0.1 1 441 64 66 PRO CG C 27.13 0.1 1 442 64 66 PRO CD C 49.22 0.1 1 443 64 66 PRO N N 133.86 0.2 1 444 65 67 GLU H H 6.91 0.03 1 445 65 67 GLU HA H 5.02 0.03 1 446 65 67 GLU C C 174.73 0.1 1 447 65 67 GLU CA C 55.59 0.1 1 448 65 67 GLU CB C 32.3 0.1 1 449 65 67 GLU CG C 35.2 0.1 1 450 65 67 GLU N N 120.72 0.2 1 451 66 68 VAL H H 8.5 0.03 1 452 66 68 VAL HA H 4.31 0.03 1 453 66 68 VAL C C 176.89 0.1 1 454 66 68 VAL CA C 62.08 0.1 1 455 66 68 VAL CB C 34.7 0.1 1 456 66 68 VAL CG1 C 20.92 0.1 2 457 66 68 VAL N N 123.01 0.2 1 458 67 69 ASN H H 9.71 0.03 1 459 67 69 ASN HA H 4.46 0.03 1 460 67 69 ASN C C 174.51 0.1 1 461 67 69 ASN CA C 54.26 0.1 1 462 67 69 ASN CB C 37.55 0.1 1 463 67 69 ASN N N 128.31 0.2 1 464 68 70 GLY H H 8.79 0.03 1 465 68 70 GLY HA2 H 4.49 0.03 2 466 68 70 GLY HA3 H 4.01 0.03 2 467 68 70 GLY C C 174.34 0.1 1 468 68 70 GLY CA C 45.21 0.1 1 469 68 70 GLY N N 102.82 0.2 1 470 69 71 TYR H H 8 0.03 1 471 69 71 TYR HA H 4.32 0.03 1 472 69 71 TYR C C 174.81 0.1 1 473 69 71 TYR CA C 58.21 0.1 1 474 69 71 TYR CB C 37.6 0.1 1 475 69 71 TYR N N 121.63 0.2 1 476 70 72 GLY H H 8.52 0.03 1 477 70 72 GLY HA2 H 3.85 0.03 2 478 70 72 GLY C C 173.03 0.1 1 479 70 72 GLY CA C 44.29 0.1 1 480 70 72 GLY N N 111.35 0.2 1 481 71 73 GLY H H 7.77 0.03 1 482 71 73 GLY HA2 H 3.74 0.03 2 483 71 73 GLY C C 172.48 0.1 1 484 71 73 GLY CA C 44.98 0.1 1 485 71 73 GLY N N 105.41 0.2 1 486 72 74 ILE H H 9.75 0.03 1 487 72 74 ILE HA H 4.32 0.03 1 488 72 74 ILE C C 171.61 0.1 1 489 72 74 ILE CA C 58.93 0.1 1 490 72 74 ILE CB C 41.62 0.1 1 491 72 74 ILE N N 118.03 0.2 1 492 73 75 PRO HA H 4.24 0.03 1 493 73 75 PRO C C 174.71 0.1 1 494 73 75 PRO CA C 63.34 0.1 1 495 73 75 PRO CB C 31.76 0.1 1 496 73 75 PRO CG C 27.69 0.1 1 497 73 75 PRO CD C 50.61 0.1 1 498 74 76 ALA H H 9.05 0.03 1 499 74 76 ALA HA H 4.54 0.03 1 500 74 76 ALA C C 175.51 0.1 1 501 74 76 ALA CA C 53.55 0.1 1 502 74 76 ALA CB C 23.09 0.1 1 503 74 76 ALA N N 122.17 0.2 1 504 75 77 GLY H H 7.53 0.03 1 505 75 77 GLY HA2 H 4.27 0.03 2 506 75 77 GLY C C 172.78 0.1 1 507 75 77 GLY CA C 46.05 0.1 1 508 75 77 GLY N N 103.42 0.2 1 509 76 78 CYS H H 8.11 0.03 1 510 76 78 CYS HA H 5.95 0.03 1 511 76 78 CYS C C 176.72 0.1 1 512 76 78 CYS CA C 56.65 0.1 1 513 76 78 CYS CB C 33.64 0.1 1 514 76 78 CYS N N 116.17 0.2 1 515 77 79 GLN H H 9.11 0.03 1 516 77 79 GLN HA H 4.98 0.03 1 517 77 79 GLN C C 174.31 0.1 1 518 77 79 GLN CA C 55.6 0.1 1 519 77 79 GLN CB C 37.53 0.1 1 520 77 79 GLN N N 119.29 0.2 1 521 78 80 CYS H H 8.91 0.03 1 522 78 80 CYS HA H 5.31 0.03 1 523 78 80 CYS C C 173.49 0.1 1 524 78 80 CYS CA C 59.07 0.1 1 525 78 80 CYS CB C 28.8 0.1 1 526 78 80 CYS N N 121.65 0.2 1 527 79 81 ASP H H 9.02 0.03 1 528 79 81 ASP HA H 4.89 0.03 1 529 79 81 ASP C C 173.11 0.1 1 530 79 81 ASP CA C 54.52 0.1 1 531 79 81 ASP CB C 42.68 0.1 1 532 79 81 ASP CG C 179.81 0.1 1 533 79 81 ASP N N 129.37 0.2 1 534 80 82 ARG H H 7.95 0.03 1 535 80 82 ARG HA H 4.06 0.03 1 536 80 82 ARG HE H 7.06 0.03 1 537 80 82 ARG C C 177.79 0.1 1 538 80 82 ARG CA C 57.81 0.1 1 539 80 82 ARG CB C 31.84 0.1 1 540 80 82 ARG CG C 25.7 0.1 1 541 80 82 ARG CD C 43.19 0.1 1 542 80 82 ARG CZ C 159.7 0.1 1 543 80 82 ARG N N 117.66 0.2 1 544 80 82 ARG NE N 84.85 0.2 1 545 81 83 ASP H H 8.09 0.03 1 546 81 83 ASP HA H 4.4 0.03 1 547 81 83 ASP C C 175.11 0.1 1 548 81 83 ASP CA C 56.54 0.1 1 549 81 83 ASP CB C 40.09 0.1 1 550 81 83 ASP N N 117.78 0.2 1 551 82 84 ALA H H 7.5 0.03 1 552 82 84 ALA HA H 4.4 0.03 1 553 82 84 ALA C C 175.13 0.1 1 554 82 84 ALA CA C 50.59 0.1 1 555 82 84 ALA CB C 21.36 0.1 1 556 82 84 ALA N N 120.13 0.2 1 557 83 85 ASN H H 8.78 0.03 1 558 83 85 ASN HA H 4.78 0.03 1 559 83 85 ASN C C 171.81 0.1 1 560 83 85 ASN CA C 53.17 0.1 1 561 83 85 ASN CB C 37.86 0.1 1 562 83 85 ASN N N 119.87 0.2 1 563 84 86 GLN H H 7.64 0.03 1 564 84 86 GLN HA H 4.68 0.03 1 565 84 86 GLN C C 172.37 0.1 1 566 84 86 GLN CA C 53.03 0.1 1 567 84 86 GLN CB C 28.68 0.1 1 568 84 86 GLN CG C 30.77 0.1 1 569 84 86 GLN N N 119.28 0.2 1 570 85 87 LEU H H 8.87 0.03 1 571 85 87 LEU HA H 5.07 0.03 1 572 85 87 LEU C C 175.77 0.1 1 573 85 87 LEU CA C 53.23 0.1 1 574 85 87 LEU CB C 43.95 0.1 1 575 85 87 LEU CG C 26.75 0.1 1 576 85 87 LEU CD1 C 23.17 0.1 2 577 85 87 LEU CD2 C 22.05 0.1 2 578 85 87 LEU N N 119.79 0.2 1 579 86 88 PHE H H 9.43 0.03 1 580 86 88 PHE HA H 5.01 0.03 1 581 86 88 PHE C C 174.94 0.1 1 582 86 88 PHE CA C 57.96 0.1 1 583 86 88 PHE CB C 40.57 0.1 1 584 86 88 PHE N N 123.64 0.2 1 585 87 89 VAL H H 9.17 0.03 1 586 87 89 VAL HA H 4.94 0.03 1 587 87 89 VAL C C 174.55 0.1 1 588 87 89 VAL CA C 60.2 0.1 1 589 87 89 VAL CB C 35.73 0.1 1 590 87 89 VAL CG1 C 21.4 0.1 2 591 87 89 VAL CG2 C 20.4 0.1 2 592 87 89 VAL N N 123.38 0.2 1 593 88 90 ALA H H 9.1 0.03 1 594 88 90 ALA HA H 4.23 0.03 1 595 88 90 ALA C C 173.32 0.1 1 596 88 90 ALA CA C 50.94 0.1 1 597 88 90 ALA CB C 18.71 0.1 1 598 88 90 ALA N N 131.54 0.2 1 599 89 91 ASP H H 9.22 0.03 1 600 89 91 ASP HA H 5.3 0.03 1 601 89 91 ASP C C 178.97 0.1 1 602 89 91 ASP CA C 53.64 0.1 1 603 89 91 ASP CB C 47.67 0.1 1 604 89 91 ASP N N 128.16 0.2 1 605 90 92 MET H H 9.16 0.03 1 606 90 92 MET HA H 4.28 0.03 1 607 90 92 MET C C 176.84 0.1 1 608 90 92 MET CA C 57.37 0.1 1 609 90 92 MET CB C 33.97 0.1 1 610 90 92 MET CG C 32.77 0.1 1 611 90 92 MET N N 130.21 0.2 1 612 91 93 ARG H H 9.48 0.03 1 613 91 93 ARG HA H 4.74 0.03 1 614 91 93 ARG HE H 7.96 0.03 1 615 91 93 ARG C C 176.95 0.1 1 616 91 93 ARG CA C 54.26 0.1 1 617 91 93 ARG CB C 31.97 0.1 1 618 91 93 ARG CG C 25.65 0.1 1 619 91 93 ARG CZ C 160.8 0.1 1 620 91 93 ARG N N 116.63 0.2 1 621 91 93 ARG NE N 84.75 0.2 1 622 92 94 LEU H H 9.21 0.03 1 623 92 94 LEU HA H 4.63 0.03 1 624 92 94 LEU C C 178.12 0.1 1 625 92 94 LEU CA C 53.88 0.1 1 626 92 94 LEU CB C 43.5 0.1 1 627 92 94 LEU CG C 27.2 0.1 1 628 92 94 LEU CD1 C 25.1 0.1 2 629 92 94 LEU N N 116.48 0.2 1 630 93 95 GLY H H 8.74 0.03 1 631 93 95 GLY HA2 H 4.22 0.03 2 632 93 95 GLY C C 170.14 0.1 1 633 93 95 GLY CA C 45.92 0.1 1 634 93 95 GLY N N 110.65 0.2 1 635 94 96 LEU H H 8.34 0.03 1 636 94 96 LEU HA H 5.07 0.03 1 637 94 96 LEU C C 174.18 0.1 1 638 94 96 LEU CA C 53.48 0.1 1 639 94 96 LEU CB C 44.49 0.1 1 640 94 96 LEU CG C 26.35 0.1 1 641 94 96 LEU CD1 C 22.48 0.1 1 642 94 96 LEU CD2 C 21.19 0.1 1 643 94 96 LEU N N 127.34 0.2 1 644 95 97 LEU H H 9.29 0.03 1 645 95 97 LEU HA H 5.22 0.03 1 646 95 97 LEU C C 176.1 0.1 1 647 95 97 LEU CA C 52.26 0.1 1 648 95 97 LEU CB C 45.83 0.1 1 649 95 97 LEU CG C 25.43 0.1 1 650 95 97 LEU CD1 C 20.9 0.1 2 651 95 97 LEU N N 126.76 0.2 1 652 96 98 VAL H H 8.55 0.03 1 653 96 98 VAL HA H 4.74 0.03 1 654 96 98 VAL C C 175.87 0.1 1 655 96 98 VAL CA C 60.26 0.1 1 656 96 98 VAL CB C 32.3 0.1 1 657 96 98 VAL CG1 C 21.08 0.1 2 658 96 98 VAL CG2 C 20.03 0.1 2 659 96 98 VAL N N 119.19 0.2 1 660 97 99 VAL H H 9.66 0.03 1 661 97 99 VAL HA H 4.58 0.03 1 662 97 99 VAL C C 175.05 0.1 1 663 97 99 VAL CA C 61.33 0.1 1 664 97 99 VAL CB C 35.14 0.1 1 665 97 99 VAL CG1 C 21.4 0.1 2 666 97 99 VAL CG2 C 20.19 0.1 2 667 97 99 VAL N N 132.01 0.2 1 668 98 100 GLN H H 9.05 0.03 1 669 98 100 GLN HA H 4.67 0.03 1 670 98 100 GLN C C 178.71 0.1 1 671 98 100 GLN CA C 52.8 0.1 1 672 98 100 GLN CB C 29.12 0.1 1 673 98 100 GLN CG C 33.4 0.1 1 674 98 100 GLN N N 122.94 0.2 1 675 99 101 THR H H 9.35 0.03 1 676 99 101 THR HA H 3.8 0.03 1 677 99 101 THR C C 175.1 0.1 1 678 99 101 THR CA C 65.12 0.1 1 679 99 101 THR CB C 68.02 0.1 1 680 99 101 THR CG2 C 22.09 0.1 1 681 99 101 THR N N 110.88 0.2 1 682 100 102 ASP H H 7.44 0.03 1 683 100 102 ASP HA H 4.63 0.03 1 684 100 102 ASP C C 177.55 0.1 1 685 100 102 ASP CA C 53.37 0.1 1 686 100 102 ASP CB C 40.06 0.1 1 687 100 102 ASP N N 117.41 0.2 1 688 101 103 GLY H H 8.28 0.03 1 689 101 103 GLY HA2 H 4.64 0.03 2 690 101 103 GLY C C 175.13 0.1 1 691 101 103 GLY CA C 46.36 0.1 1 692 101 103 GLY N N 108.66 0.2 1 693 102 104 THR H H 8.15 0.03 1 694 102 104 THR HA H 4.36 0.03 1 695 102 104 THR C C 173.02 0.1 1 696 102 104 THR CA C 63.18 0.1 1 697 102 104 THR CB C 69.86 0.1 1 698 102 104 THR CG2 C 21.88 0.1 1 699 102 104 THR N N 115.79 0.2 1 700 103 105 PHE H H 8.17 0.03 1 701 103 105 PHE HA H 5.85 0.03 1 702 103 105 PHE C C 173.19 0.1 1 703 103 105 PHE CA C 55.55 0.1 1 704 103 105 PHE CB C 43.88 0.1 1 705 103 105 PHE N N 116.97 0.2 1 706 104 106 GLU H H 8.47 0.03 1 707 104 106 GLU HA H 4.44 0.03 1 708 104 106 GLU C C 175.14 0.1 1 709 104 106 GLU CA C 54.61 0.1 1 710 104 106 GLU CB C 34.24 0.1 1 711 104 106 GLU CG C 35.8 0.1 1 712 104 106 GLU N N 117.42 0.2 1 713 105 107 GLU H H 8.96 0.03 1 714 105 107 GLU HA H 4.44 0.03 1 715 105 107 GLU C C 176.9 0.1 1 716 105 107 GLU CA C 55.91 0.1 1 717 105 107 GLU CB C 31.45 0.1 1 718 105 107 GLU CG C 36.44 0.1 1 719 105 107 GLU N N 123.24 0.2 1 720 106 108 ILE H H 8.42 0.03 1 721 106 108 ILE HA H 4.01 0.03 1 722 106 108 ILE C C 175.4 0.1 1 723 106 108 ILE CA C 61.11 0.1 1 724 106 108 ILE CB C 37.25 0.1 1 725 106 108 ILE CG1 C 27.58 0.1 1 726 106 108 ILE CG2 C 17.93 0.1 1 727 106 108 ILE CD1 C 10.84 0.1 1 728 106 108 ILE N N 125.24 0.2 1 729 107 109 ALA H H 7.83 0.03 1 730 107 109 ALA HA H 4.62 0.03 1 731 107 109 ALA C C 175.86 0.1 1 732 107 109 ALA CA C 51.93 0.1 1 733 107 109 ALA CB C 21.55 0.1 1 734 107 109 ALA N N 119.85 0.2 1 735 108 110 LYS H H 8.86 0.03 1 736 108 110 LYS HA H 4.27 0.03 1 737 108 110 LYS C C 176.99 0.1 1 738 108 110 LYS CA C 56.87 0.1 1 739 108 110 LYS CB C 33.37 0.1 1 740 108 110 LYS CG C 25.05 0.1 1 741 108 110 LYS CD C 28.66 0.1 1 742 108 110 LYS CE C 42.03 0.1 1 743 108 110 LYS N N 119.85 0.2 1 744 109 111 LYS H H 7.7 0.03 1 745 109 111 LYS HA H 4.93 0.03 1 746 109 111 LYS C C 175.08 0.1 1 747 109 111 LYS CA C 54.01 0.1 1 748 109 111 LYS CB C 37.07 0.1 1 749 109 111 LYS CG C 24.43 0.1 1 750 109 111 LYS CD C 29.7 0.1 1 751 109 111 LYS CE C 42.15 0.1 1 752 109 111 LYS N N 116.86 0.2 1 753 110 112 ASP H H 8.88 0.03 1 754 110 112 ASP HA H 4.78 0.03 1 755 110 112 ASP C C 179.44 0.1 1 756 110 112 ASP CA C 52.79 0.1 1 757 110 112 ASP CB C 42.47 0.1 1 758 110 112 ASP N N 119.52 0.2 1 759 111 113 SER H H 9.1 0.03 1 760 111 113 SER HA H 4.22 0.03 1 761 111 113 SER C C 176.07 0.1 1 762 111 113 SER CA C 61.54 0.1 1 763 111 113 SER CB C 62.75 0.1 1 764 111 113 SER N N 113.78 0.2 1 765 112 114 GLU H H 8.45 0.03 1 766 112 114 GLU HA H 4.59 0.03 1 767 112 114 GLU C C 176.88 0.1 1 768 112 114 GLU CA C 55.73 0.1 1 769 112 114 GLU CB C 29.72 0.1 1 770 112 114 GLU CG C 36.86 0.1 1 771 112 114 GLU N N 122.19 0.2 1 772 113 115 GLY H H 8.42 0.03 1 773 113 115 GLY HA2 H 4.26 0.03 2 774 113 115 GLY C C 174.35 0.1 1 775 113 115 GLY CA C 45.71 0.1 1 776 113 115 GLY N N 108.67 0.2 1 777 114 116 ARG H H 8.31 0.03 1 778 114 116 ARG HA H 4.36 0.03 1 779 114 116 ARG HE H 8.27 0.03 1 780 114 116 ARG C C 177.29 0.1 1 781 114 116 ARG CA C 55.42 0.1 1 782 114 116 ARG CB C 30.38 0.1 1 783 114 116 ARG CG C 28.17 0.1 1 784 114 116 ARG CD C 43.38 0.1 1 785 114 116 ARG CZ C 159.39 0.1 1 786 114 116 ARG N N 122.68 0.2 1 787 114 116 ARG NE N 86.9 0.2 1 788 115 117 ARG H H 8.67 0.03 1 789 115 117 ARG HA H 4.13 0.03 1 790 115 117 ARG C C 177.33 0.1 1 791 115 117 ARG CA C 57.6 0.1 1 792 115 117 ARG CB C 29.85 0.1 1 793 115 117 ARG CG C 28.7 0.1 1 794 115 117 ARG CD C 42.63 0.1 1 795 115 117 ARG N N 121.39 0.2 1 796 116 118 MET H H 8.14 0.03 1 797 116 118 MET HA H 4.36 0.03 1 798 116 118 MET C C 175.61 0.1 1 799 116 118 MET CA C 54.6 0.1 1 800 116 118 MET CB C 31.87 0.1 1 801 116 118 MET CG C 32.4 0.1 1 802 116 118 MET N N 122.89 0.2 1 803 117 119 GLN H H 7.07 0.03 1 804 117 119 GLN HA H 4.61 0.03 1 805 117 119 GLN C C 175.86 0.1 1 806 117 119 GLN CA C 54.94 0.1 1 807 117 119 GLN CB C 33.27 0.1 1 808 117 119 GLN CG C 36.78 0.1 1 809 117 119 GLN N N 116.93 0.2 1 810 118 120 GLY H H 8.44 0.03 1 811 118 120 GLY HA2 H 4.3 0.03 2 812 118 120 GLY C C 173.28 0.1 1 813 118 120 GLY CA C 46.35 0.1 1 814 118 120 GLY N N 103.41 0.2 1 815 119 121 CYS H H 7.55 0.03 1 816 119 121 CYS HA H 5.35 0.03 1 817 119 121 CYS C C 171.85 0.1 1 818 119 121 CYS CA C 59.27 0.1 1 819 119 121 CYS CB C 31.82 0.1 1 820 119 121 CYS N N 175.79 0.2 1 821 120 122 ASN H H 8.61 0.03 1 822 120 122 ASN HA H 4.79 0.03 1 823 120 122 ASN C C 172.76 0.1 1 824 120 122 ASN CA C 54.11 0.1 1 825 120 122 ASN CB C 44.26 0.1 1 826 120 122 ASN N N 116.81 0.2 1 827 121 123 ASP H H 7.86 0.03 1 828 121 123 ASP HA H 5.03 0.03 1 829 121 123 ASP C C 173.49 0.1 1 830 121 123 ASP CA C 51.55 0.1 1 831 121 123 ASP CB C 45.19 0.1 1 832 121 123 ASP N N 116.84 0.2 1 833 122 124 CYS H H 9.41 0.03 1 834 122 124 CYS HA H 5.8 0.03 1 835 122 124 CYS C C 172.21 0.1 1 836 122 124 CYS CA C 54.29 0.1 1 837 122 124 CYS CB C 30.73 0.1 1 838 122 124 CYS N N 111.61 0.2 1 839 123 125 ALA H H 9.31 0.03 1 840 123 125 ALA HA H 4.82 0.03 1 841 123 125 ALA C C 176.94 0.1 1 842 123 125 ALA CA C 51.11 0.1 1 843 123 125 ALA CB C 22.24 0.1 1 844 123 125 ALA N N 120.58 0.2 1 845 124 126 PHE H H 8.88 0.03 1 846 124 126 PHE HA H 5.45 0.03 1 847 124 126 PHE C C 178.95 0.1 1 848 124 126 PHE CA C 59.41 0.1 1 849 124 126 PHE CB C 41.48 0.1 1 850 124 126 PHE N N 124 0.2 1 851 125 127 ASP H H 9.2 0.03 1 852 125 127 ASP HA H 5.21 0.03 1 853 125 127 ASP C C 178.91 0.1 1 854 125 127 ASP CA C 51.94 0.1 1 855 125 127 ASP CB C 45.3 0.1 1 856 125 127 ASP N N 118.71 0.2 1 857 126 128 TYR H H 11.41 0.03 1 858 126 128 TYR HA H 4.85 0.03 1 859 126 128 TYR C C 178.5 0.1 1 860 126 128 TYR CA C 56.15 0.1 1 861 126 128 TYR CB C 35.81 0.1 1 862 126 128 TYR N N 118.96 0.2 1 863 127 129 GLU H H 8.73 0.03 1 864 127 129 GLU HA H 4.47 0.03 1 865 127 129 GLU C C 177.05 0.1 1 866 127 129 GLU CA C 56.49 0.1 1 867 127 129 GLU CB C 29.9 0.1 1 868 127 129 GLU CG C 36.9 0.1 1 869 127 129 GLU N N 118.69 0.2 1 870 128 130 GLY H H 7.96 0.03 1 871 128 130 GLY HA2 H 4.08 0.03 2 872 128 130 GLY C C 174.93 0.1 1 873 128 130 GLY CA C 44.75 0.1 1 874 128 130 GLY N N 107.83 0.2 1 875 129 131 ASN H H 8.44 0.03 1 876 129 131 ASN HA H 4.48 0.03 1 877 129 131 ASN C C 172.6 0.1 1 878 129 131 ASN CA C 53.67 0.1 1 879 129 131 ASN CB C 38.52 0.1 1 880 129 131 ASN N N 121.07 0.2 1 881 130 132 LEU H H 8.48 0.03 1 882 130 132 LEU HA H 4.38 0.03 1 883 130 132 LEU C C 173.43 0.1 1 884 130 132 LEU CA C 53.43 0.1 1 885 130 132 LEU CB C 44.09 0.1 1 886 130 132 LEU CG C 27.21 0.1 1 887 130 132 LEU CD1 C 20.7 0.1 2 888 130 132 LEU N N 125.13 0.2 1 889 131 133 TRP H H 8.75 0.03 1 890 131 133 TRP HA H 5.05 0.03 1 891 131 133 TRP HD1 H 7.37 0.03 1 892 131 133 TRP HE1 H 11.6 0.03 1 893 131 133 TRP C C 177 0.1 1 894 131 133 TRP CA C 56.24 0.1 1 895 131 133 TRP CB C 29.34 0.1 1 896 131 133 TRP CG C 110.6 0.1 1 897 131 133 TRP CD1 C 129.91 0.1 1 898 131 133 TRP CE2 C 139.47 0.1 1 899 131 133 TRP N N 131.66 0.2 1 900 131 133 TRP NE1 N 133.16 0.2 1 901 132 134 ILE H H 9.33 0.03 1 902 132 134 ILE HA H 4.91 0.03 1 903 132 134 ILE C C 176.13 0.1 1 904 132 134 ILE CA C 61.08 0.1 1 905 132 134 ILE CB C 44.66 0.1 1 906 132 134 ILE CG1 C 28.18 0.1 1 907 132 134 ILE CG2 C 19.61 0.1 1 908 132 134 ILE CD1 C 17.3 0.1 1 909 132 134 ILE N N 123.74 0.2 1 910 133 135 THR H H 9.09 0.03 1 911 133 135 THR HA H 4.45 0.03 1 912 133 135 THR C C 174.83 0.1 1 913 133 135 THR CA C 60.76 0.1 1 914 133 135 THR CB C 70.7 0.1 1 915 133 135 THR CG2 C 24.49 0.1 1 916 133 135 THR N N 115.92 0.2 1 917 134 136 ALA H H 8.68 0.03 1 918 134 136 ALA HA H 5.6 0.03 1 919 134 136 ALA C C 174.13 0.1 1 920 134 136 ALA CA C 49.71 0.1 1 921 134 136 ALA CB C 21.68 0.1 1 922 134 136 ALA N N 123.02 0.2 1 923 135 137 PRO HA H 4.34 0.03 1 924 135 137 PRO C C 177.67 0.1 1 925 135 137 PRO CA C 62.78 0.1 1 926 135 137 PRO CB C 31.17 0.1 1 927 135 137 PRO CG C 27.4 0.1 1 928 135 137 PRO CD C 48.24 0.1 1 929 135 137 PRO N N 131.09 0.2 1 930 136 138 ALA H H 7.31 0.03 1 931 136 138 ALA HA H 5.24 0.03 1 932 136 138 ALA C C 175.77 0.1 1 933 136 138 ALA CA C 51.21 0.1 1 934 136 138 ALA CB C 21.57 0.1 1 935 136 138 ALA N N 124.89 0.2 1 936 137 139 GLY H H 7.75 0.03 1 937 137 139 GLY HA2 H 3.73 0.03 2 938 137 139 GLY C C 172.75 0.1 1 939 137 139 GLY CA C 44.25 0.1 1 940 137 139 GLY N N 103.99 0.2 1 941 138 140 GLU H H 8.18 0.03 1 942 138 140 GLU HA H 4.3 0.03 1 943 138 140 GLU C C 176.74 0.1 1 944 138 140 GLU CA C 57.5 0.1 1 945 138 140 GLU CB C 30.78 0.1 1 946 138 140 GLU CG C 36.88 0.1 1 947 138 140 GLU N N 119.18 0.2 1 948 139 141 VAL H H 7.75 0.03 1 949 139 141 VAL HA H 4.05 0.03 1 950 139 141 VAL C C 176.54 0.1 1 951 139 141 VAL CA C 61.28 0.1 1 952 139 141 VAL CB C 33.86 0.1 1 953 139 141 VAL CG1 C 22 0.1 2 954 139 141 VAL CG2 C 16.5 0.1 2 955 139 141 VAL N N 112.9 0.2 1 956 140 142 ALA H H 8.47 0.03 1 957 140 142 ALA HA H 3.98 0.03 1 958 140 142 ALA C C 122.8 0.1 1 959 140 142 ALA CA C 51.6 0.1 1 960 140 142 ALA CB C 16.7 0.1 1 961 140 142 ALA N N 122.8 0.2 1 962 141 143 PRO HA H 3.22 0.03 1 963 141 143 PRO C C 175.72 0.1 1 964 141 143 PRO CA C 63.48 0.1 1 965 141 143 PRO CB C 34.02 0.1 1 966 141 143 PRO CG C 24.27 0.1 1 967 141 143 PRO CD C 50.07 0.1 1 968 141 143 PRO N N 132.53 0.2 1 969 142 144 ALA H H 8.15 0.03 1 970 142 144 ALA HA H 4.17 0.03 1 971 142 144 ALA C C 177.77 0.1 1 972 142 144 ALA CA C 53.34 0.1 1 973 142 144 ALA CB C 19.15 0.1 1 974 142 144 ALA N N 129.7 0.2 1 975 143 145 ASP H H 8.68 0.03 1 976 143 145 ASP HA H 4.53 0.03 1 977 143 145 ASP C C 176.93 0.1 1 978 143 145 ASP CA C 55.19 0.1 1 979 143 145 ASP CB C 40.47 0.1 1 980 143 145 ASP N N 122.44 0.2 1 981 144 146 TYR H H 9.03 0.03 1 982 144 146 TYR HA H 4.97 0.03 1 983 144 146 TYR C C 175.18 0.1 1 984 144 146 TYR CA C 56.71 0.1 1 985 144 146 TYR CB C 38.34 0.1 1 986 144 146 TYR N N 124.54 0.2 1 987 145 147 THR H H 8.43 0.03 1 988 145 147 THR HA H 4.53 0.03 1 989 145 147 THR C C 172.47 0.1 1 990 145 147 THR CA C 59.95 0.1 1 991 145 147 THR CB C 71.78 0.1 1 992 145 147 THR CG2 C 21.56 0.1 1 993 145 147 THR N N 123.03 0.2 1 994 146 148 ARG H H 8.61 0.03 1 995 146 148 ARG HA H 4.93 0.03 1 996 146 148 ARG HE H 7.33 0.03 1 997 146 148 ARG C C 177.18 0.1 1 998 146 148 ARG CA C 55.23 0.1 1 999 146 148 ARG CB C 35.43 0.1 1 1000 146 148 ARG CG C 26.99 0.1 1 1001 146 148 ARG CD C 43.58 0.1 1 1002 146 148 ARG CZ C 159.5 0.1 1 1003 146 148 ARG N N 117.2 0.2 1 1004 146 148 ARG NE N 83.4 0.2 1 1005 147 149 SER H H 7.95 0.03 1 1006 147 149 SER HA H 3.92 0.03 1 1007 147 149 SER C C 172.59 0.1 1 1008 147 149 SER CA C 58.96 0.1 1 1009 147 149 SER CB C 61.89 0.1 1 1010 147 149 SER N N 118.1 0.2 1 1011 148 150 MET HA H 4.42 0.03 1 1012 148 150 MET C C 177.25 0.1 1 1013 148 150 MET CA C 56.98 0.1 1 1014 148 150 MET CB C 32 0.1 1 1015 148 150 MET CG C 32.73 0.1 1 1016 149 151 GLN H H 8.64 0.03 1 1017 149 151 GLN HA H 4.47 0.03 1 1018 149 151 GLN C C 175.15 0.1 1 1019 149 151 GLN CA C 56.56 0.1 1 1020 149 151 GLN CB C 31.1 0.1 1 1021 149 151 GLN CG C 34.24 0.1 1 1022 149 151 GLN N N 115.23 0.2 1 1023 150 152 GLU H H 7.91 0.03 1 1024 150 152 GLU HA H 4.45 0.03 1 1025 150 152 GLU C C 175.58 0.1 1 1026 150 152 GLU CA C 55.09 0.1 1 1027 150 152 GLU CB C 32.3 0.1 1 1028 150 152 GLU CG C 36.65 0.1 1 1029 150 152 GLU N N 119.3 0.2 1 1030 151 153 LYS H H 8.39 0.03 1 1031 151 153 LYS HA H 4.06 0.03 1 1032 151 153 LYS C C 175.96 0.1 1 1033 151 153 LYS CA C 55.7 0.1 1 1034 151 153 LYS CB C 30.25 0.1 1 1035 151 153 LYS CG C 25.15 0.1 1 1036 151 153 LYS CD C 29.6 0.1 1 1037 151 153 LYS CE C 42.39 0.1 1 1038 151 153 LYS N N 120.57 0.2 1 1039 152 154 PHE H H 7.06 0.03 1 1040 152 154 PHE HA H 5.25 0.03 1 1041 152 154 PHE C C 175.19 0.1 1 1042 152 154 PHE CA C 55.78 0.1 1 1043 152 154 PHE CB C 38.47 0.1 1 1044 152 154 PHE N N 117.32 0.2 1 1045 153 155 GLY H H 9.44 0.03 1 1046 153 155 GLY HA2 H 4.31 0.03 2 1047 153 155 GLY C C 173.6 0.1 1 1048 153 155 GLY CA C 46.14 0.1 1 1049 153 155 GLY N N 112.83 0.2 1 1050 154 156 SER H H 8.67 0.03 1 1051 154 156 SER HA H 5.31 0.03 1 1052 154 156 SER C C 169.95 0.1 1 1053 154 156 SER CA C 57.18 0.1 1 1054 154 156 SER CB C 66.49 0.1 1 1055 154 156 SER N N 118.94 0.2 1 1056 155 157 ILE H H 7.95 0.03 1 1057 155 157 ILE HA H 4.84 0.03 1 1058 155 157 ILE C C 175.52 0.1 1 1059 155 157 ILE CA C 58.68 0.1 1 1060 155 157 ILE CB C 40.3 0.1 1 1061 155 157 ILE CG1 C 27.41 0.1 1 1062 155 157 ILE CG2 C 16.99 0.1 1 1063 155 157 ILE CD1 C 12.94 0.1 1 1064 155 157 ILE N N 118.85 0.2 1 1065 156 158 TYR H H 9.51 0.03 1 1066 156 158 TYR HA H 5.64 0.03 1 1067 156 158 TYR C C 174.83 0.1 1 1068 156 158 TYR CA C 56.35 0.1 1 1069 156 158 TYR CB C 44.93 0.1 1 1070 156 158 TYR N N 123.15 0.2 1 1071 157 159 CYS H H 9.45 0.03 1 1072 157 159 CYS HA H 4.8 0.03 1 1073 157 159 CYS C C 172.65 0.1 1 1074 157 159 CYS CA C 57.25 0.1 1 1075 157 159 CYS CB C 31.34 0.1 1 1076 157 159 CYS N N 120.49 0.2 1 1077 158 160 PHE H H 9.62 0.03 1 1078 158 160 PHE HA H 5.96 0.03 1 1079 158 160 PHE C C 176.7 0.1 1 1080 158 160 PHE CA C 55.09 0.1 1 1081 158 160 PHE CB C 39.84 0.1 1 1082 158 160 PHE N N 131.57 0.2 1 1083 159 161 THR H H 8.81 0.03 1 1084 159 161 THR HA H 4.63 0.03 1 1085 159 161 THR C C 177.35 0.1 1 1086 159 161 THR CA C 61.33 0.1 1 1087 159 161 THR CB C 71.26 0.1 1 1088 159 161 THR CG2 C 22.85 0.1 1 1089 159 161 THR N N 119.2 0.2 1 1090 160 162 THR H H 7.92 0.03 1 1091 160 162 THR HA H 4.01 0.03 1 1092 160 162 THR C C 175.8 0.1 1 1093 160 162 THR CA C 64.31 0.1 1 1094 160 162 THR CB C 68.71 0.1 1 1095 160 162 THR CG2 C 21.64 0.1 1 1096 160 162 THR N N 110.42 0.2 1 1097 161 163 ASP H H 7.7 0.03 1 1098 161 163 ASP HA H 4.69 0.03 1 1099 161 163 ASP C C 176.33 0.1 1 1100 161 163 ASP CA C 53.45 0.1 1 1101 161 163 ASP CB C 40 0.1 1 1102 161 163 ASP N N 116.81 0.2 1 1103 162 164 GLY H H 7.92 0.03 1 1104 162 164 GLY HA2 H 3.91 0.03 2 1105 162 164 GLY C C 174.49 0.1 1 1106 162 164 GLY CA C 46.49 0.1 1 1107 162 164 GLY N N 109 0.2 1 1108 163 165 GLN H H 7.16 0.03 1 1109 163 165 GLN HA H 4.5 0.03 1 1110 163 165 GLN C C 173.52 0.1 1 1111 163 165 GLN CA C 54.68 0.1 1 1112 163 165 GLN CB C 30.97 0.1 1 1113 163 165 GLN CG C 34.22 0.1 1 1114 163 165 GLN N N 118.03 0.2 1 1115 164 166 MET H H 8.99 0.03 1 1116 164 166 MET HA H 5.38 0.03 1 1117 164 166 MET C C 173.4 0.1 1 1118 164 166 MET CA C 53.51 0.1 1 1119 164 166 MET CB C 31.86 0.1 1 1120 164 166 MET CG C 33.51 0.1 1 1121 164 166 MET N N 123.59 0.2 1 1122 165 167 ILE H H 8.97 0.03 1 1123 165 167 ILE HA H 4.56 0.03 1 1124 165 167 ILE C C 176.31 0.1 1 1125 165 167 ILE CA C 60.12 0.1 1 1126 165 167 ILE CB C 40.66 0.1 1 1127 165 167 ILE CG1 C 26.96 0.1 1 1128 165 167 ILE CG2 C 17.2 0.1 1 1129 165 167 ILE CD1 C 12.75 0.1 1 1130 165 167 ILE N N 128.76 0.2 1 1131 166 168 GLN H H 9.85 0.03 1 1132 166 168 GLN HA H 4.26 0.03 1 1133 166 168 GLN C C 175.78 0.1 1 1134 166 168 GLN CA C 56.75 0.1 1 1135 166 168 GLN CB C 30.33 0.1 1 1136 166 168 GLN CG C 35.91 0.1 1 1137 166 168 GLN N N 130.39 0.2 1 1138 167 169 VAL H H 8.72 0.03 1 1139 167 169 VAL HA H 4.45 0.03 1 1140 167 169 VAL C C 175.67 0.1 1 1141 167 169 VAL CA C 61.97 0.1 1 1142 167 169 VAL CB C 32 0.1 1 1143 167 169 VAL CG1 C 21.1 0.1 2 1144 167 169 VAL CG2 C 19.89 0.1 2 1145 167 169 VAL N N 122.69 0.2 1 1146 168 170 ASP H H 7.69 0.03 1 1147 168 170 ASP HA H 4.84 0.03 1 1148 168 170 ASP C C 174.51 0.1 1 1149 168 170 ASP CA C 53.77 0.1 1 1150 168 170 ASP CB C 42.42 0.1 1 1151 168 170 ASP CG C 180.58 0.1 1 1152 168 170 ASP N N 115.42 0.2 1 1153 169 171 THR H H 8.78 0.03 1 1154 169 171 THR HA H 5.07 0.03 1 1155 169 171 THR C C 172.24 0.1 1 1156 169 171 THR CA C 60.13 0.1 1 1157 169 171 THR CB C 69.69 0.1 1 1158 169 171 THR CG2 C 17.86 0.1 1 1159 169 171 THR N N 113.42 0.2 1 1160 170 172 ALA H H 8.29 0.03 1 1161 170 172 ALA HA H 3.98 0.03 1 1162 170 172 ALA C C 176.61 0.1 1 1163 170 172 ALA CA C 53.04 0.1 1 1164 170 172 ALA CB C 16.53 0.1 1 1165 170 172 ALA N N 117.66 0.2 1 1166 171 173 PHE H H 8.61 0.03 1 1167 171 173 PHE HA H 4.3 0.03 1 1168 171 173 PHE C C 175.1 0.1 1 1169 171 173 PHE CA C 57.94 0.1 1 1170 171 173 PHE CB C 42.79 0.1 1 1171 171 173 PHE N N 116.39 0.2 1 1172 172 174 GLN H H 10.3 0.03 1 1173 172 174 GLN HA H 4.65 0.03 1 1174 172 174 GLN C C 172.71 0.1 1 1175 172 174 GLN CA C 54.22 0.1 1 1176 172 174 GLN CB C 28.48 0.1 1 1177 172 174 GLN CG C 34.25 0.1 1 1178 172 174 GLN N N 128.42 0.2 1 1179 173 175 PHE H H 7.39 0.03 1 1180 173 175 PHE HA H 3.51 0.03 1 1181 173 175 PHE C C 172.1 0.1 1 1182 173 175 PHE CA C 59.73 0.1 1 1183 173 175 PHE CB C 39.5 0.1 1 1184 173 175 PHE N N 120.11 0.2 1 1185 174 176 PRO HA H 5.28 0.03 1 1186 174 176 PRO C C 177.14 0.1 1 1187 174 176 PRO CA C 62.38 0.1 1 1188 174 176 PRO CB C 30.57 0.1 1 1189 174 176 PRO CG C 24.3 0.1 1 1190 174 176 PRO N N 134.54 0.2 1 1191 175 177 ASN H H 8.4 0.03 1 1192 175 177 ASN HA H 4.76 0.03 1 1193 175 177 ASN C C 173.88 0.1 1 1194 175 177 ASN CA C 52.3 0.1 1 1195 175 177 ASN CB C 40.12 0.1 1 1196 175 177 ASN N N 120.03 0.2 1 1197 176 178 GLY H H 7.2 0.03 1 1198 176 178 GLY HA2 H 4.48 0.03 2 1199 176 178 GLY C C 170.58 0.1 1 1200 176 178 GLY CA C 47.09 0.1 1 1201 176 178 GLY N N 106.63 0.2 1 1202 177 179 ILE H H 8.54 0.03 1 1203 177 179 ILE HA H 5.3 0.03 1 1204 177 179 ILE C C 172.23 0.1 1 1205 177 179 ILE CA C 59.04 0.1 1 1206 177 179 ILE CB C 40.4 0.1 1 1207 177 179 ILE CG1 C 28.05 0.1 1 1208 177 179 ILE CG2 C 13.8 0.1 1 1209 177 179 ILE N N 118.5 0.2 1 1210 178 180 ALA H H 8.75 0.03 1 1211 178 180 ALA HA H 4.46 0.03 1 1212 178 180 ALA C C 174.03 0.1 1 1213 178 180 ALA CA C 51.32 0.1 1 1214 178 180 ALA CB C 23.5 0.1 1 1215 178 180 ALA N N 126.06 0.2 1 1216 179 181 VAL H H 8.67 0.03 1 1217 179 181 VAL HA H 4.47 0.03 1 1218 179 181 VAL C C 173.96 0.1 1 1219 179 181 VAL CA C 60.57 0.1 1 1220 179 181 VAL CB C 34.32 0.1 1 1221 179 181 VAL CG1 C 20.85 0.1 2 1222 179 181 VAL N N 118.84 0.2 1 1223 180 182 ARG H H 9.23 0.03 1 1224 180 182 ARG HA H 4.02 0.03 1 1225 180 182 ARG C C 175.63 0.1 1 1226 180 182 ARG CA C 53.95 0.1 1 1227 180 182 ARG CB C 32.87 0.1 1 1228 180 182 ARG CG C 27.21 0.1 1 1229 180 182 ARG CD C 43.5 0.1 1 1230 180 182 ARG N N 127.92 0.2 1 1231 181 183 HIS H H 9.53 0.03 1 1232 181 183 HIS HA H 5.11 0.03 1 1233 181 183 HIS HD1 H 10.84 0.03 1 1234 181 183 HIS HD2 H 6.64 0.03 1 1235 181 183 HIS HE1 H 7.1 0.03 1 1236 181 183 HIS C C 177.06 0.1 1 1237 181 183 HIS CA C 57.08 0.1 1 1238 181 183 HIS CB C 32.04 0.1 1 1239 181 183 HIS CG C 128.25 0.1 1 1240 181 183 HIS CD2 C 127.4 0.1 1 1241 181 183 HIS CE1 C 138.25 0.1 1 1242 181 183 HIS N N 127.51 0.2 1 1243 181 183 HIS ND1 N 169.23 0.2 1 1244 181 183 HIS NE2 N 249.96 0.2 1 1245 182 184 MET H H 8.93 0.03 1 1246 182 184 MET HA H 4.54 0.03 1 1247 182 184 MET C C 178.84 0.1 1 1248 182 184 MET CA C 54.99 0.1 1 1249 182 184 MET CB C 33.65 0.1 1 1250 182 184 MET N N 120.36 0.2 1 1251 183 185 ASN HA H 4.49 0.03 1 1252 183 185 ASN C C 175.58 0.1 1 1253 183 185 ASN CA C 56.2 0.1 1 1254 183 185 ASN CB C 37.37 0.1 1 1255 183 185 ASN N N 122.7 0.2 1 1256 184 186 ASP H H 7.87 0.03 1 1257 184 186 ASP HA H 4.53 0.03 1 1258 184 186 ASP C C 177.03 0.1 1 1259 184 186 ASP CA C 53.51 0.1 1 1260 184 186 ASP CB C 39.86 0.1 1 1261 184 186 ASP N N 116.71 0.2 1 1262 185 187 GLY H H 8.14 0.03 1 1263 185 187 GLY HA2 H 4.5 0.03 2 1264 185 187 GLY C C 174.28 0.1 1 1265 185 187 GLY CA C 45.22 0.1 1 1266 185 187 GLY N N 107.93 0.2 1 1267 186 188 ARG H H 7.99 0.03 1 1268 186 188 ARG HE H 7.82 0.03 1 1269 186 188 ARG C C 175.96 0.1 1 1270 186 188 ARG CA C 55.24 0.1 1 1271 186 188 ARG CB C 30.99 0.1 1 1272 186 188 ARG CG C 27.12 0.1 1 1273 186 188 ARG CD C 43.75 0.1 1 1274 186 188 ARG CZ C 159.8 0.1 1 1275 186 188 ARG N N 121.98 0.2 1 1276 186 188 ARG NE N 85.7 0.2 1 1277 187 189 PRO HA H 4.14 0.03 1 1278 187 189 PRO C C 175.86 0.1 1 1279 187 189 PRO CA C 63.94 0.1 1 1280 187 189 PRO CB C 32.4 0.1 1 1281 187 189 PRO CG C 27.69 0.1 1 1282 187 189 PRO CD C 51.25 0.1 1 1283 187 189 PRO N N 140.21 0.2 1 1284 188 190 TYR H H 8.75 0.03 1 1285 188 190 TYR HA H 5.25 0.03 1 1286 188 190 TYR C C 175.1 0.1 1 1287 188 190 TYR CA C 57.85 0.1 1 1288 188 190 TYR CB C 41.86 0.1 1 1289 188 190 TYR N N 121.97 0.2 1 1290 189 191 GLN H H 7.69 0.03 1 1291 189 191 GLN HA H 5.29 0.03 1 1292 189 191 GLN C C 172.38 0.1 1 1293 189 191 GLN CA C 54.17 0.1 1 1294 189 191 GLN CB C 34.57 0.1 1 1295 189 191 GLN N N 119.65 0.2 1 1296 190 192 LEU H H 8.75 0.03 1 1297 190 192 LEU HA H 4.57 0.03 1 1298 190 192 LEU C C 174.27 0.1 1 1299 190 192 LEU CA C 52.75 0.1 1 1300 190 192 LEU CB C 45.62 0.1 1 1301 190 192 LEU CG C 25.69 0.1 1 1302 190 192 LEU CD1 C 22.35 0.1 2 1303 190 192 LEU N N 127.09 0.2 1 1304 191 193 ILE H H 8.81 0.03 1 1305 191 193 ILE HA H 4.98 0.03 1 1306 191 193 ILE C C 174.55 0.1 1 1307 191 193 ILE CA C 58.6 0.1 1 1308 191 193 ILE CB C 38.7 0.1 1 1309 191 193 ILE CG1 C 27.21 0.1 1 1310 191 193 ILE CG2 C 17.98 0.1 1 1311 191 193 ILE N N 126.3 0.2 1 1312 192 194 VAL H H 9.22 0.03 1 1313 192 194 VAL HA H 4.52 0.03 1 1314 192 194 VAL C C 175.62 0.1 1 1315 192 194 VAL CA C 60.57 0.1 1 1316 192 194 VAL CB C 36.65 0.1 1 1317 192 194 VAL CG1 C 20.91 0.1 1 1318 192 194 VAL N N 123.58 0.2 1 1319 193 195 ALA H H 8.76 0.03 1 1320 193 195 ALA HA H 4.57 0.03 1 1321 193 195 ALA C C 175.45 0.1 1 1322 193 195 ALA CA C 51.5 0.1 1 1323 193 195 ALA CB C 20.92 0.1 1 1324 193 195 ALA N N 129.6 0.2 1 1325 194 196 GLU H H 8.41 0.03 1 1326 194 196 GLU HA H 4.84 0.03 1 1327 194 196 GLU C C 176.69 0.1 1 1328 194 196 GLU CA C 55.07 0.1 1 1329 194 196 GLU CB C 32.47 0.1 1 1330 194 196 GLU CG C 40.19 0.1 1 1331 194 196 GLU N N 125.72 0.2 1 1332 195 197 THR H H 8.41 0.03 1 1333 195 197 THR C C 175 0.1 1 1334 195 197 THR CA C 71.15 0.1 1 1335 195 197 THR CB C 67.23 0.1 1 1336 195 197 THR N N 120.34 0.2 1 1337 196 198 PRO HA H 4.66 0.03 1 1338 196 198 PRO C C 178.1 0.1 1 1339 196 198 PRO CA C 65.52 0.1 1 1340 196 198 PRO CB C 31.37 0.1 1 1341 196 198 PRO CG C 29.1 0.1 1 1342 196 198 PRO CD C 50.58 0.1 1 1343 197 199 THR H H 6.95 0.03 1 1344 197 199 THR HA H 4.37 0.03 1 1345 197 199 THR C C 175.29 0.1 1 1346 197 199 THR CA C 61.62 0.1 1 1347 197 199 THR CB C 68.88 0.1 1 1348 197 199 THR CG2 C 22.34 0.1 1 1349 197 199 THR N N 106.46 0.2 1 1350 198 200 LYS H H 7.81 0.03 1 1351 198 200 LYS HA H 4.43 0.03 1 1352 198 200 LYS C C 176.13 0.1 1 1353 198 200 LYS CA C 56.84 0.1 1 1354 198 200 LYS CB C 27.87 0.1 1 1355 198 200 LYS CG C 24.43 0.1 1 1356 198 200 LYS CE C 43.15 0.1 1 1357 198 200 LYS N N 111.21 0.2 1 1358 199 201 LYS H H 7.38 0.03 1 1359 199 201 LYS HA H 4.83 0.03 1 1360 199 201 LYS C C 175.78 0.1 1 1361 199 201 LYS CA C 55.72 0.1 1 1362 199 201 LYS CB C 37.47 0.1 1 1363 199 201 LYS CG C 25.2 0.1 1 1364 199 201 LYS CD C 29.84 0.1 1 1365 199 201 LYS N N 116.95 0.2 1 1366 200 202 LEU H H 7.92 0.03 1 1367 200 202 LEU HA H 5.01 0.03 1 1368 200 202 LEU C C 175.98 0.1 1 1369 200 202 LEU CA C 53.44 0.1 1 1370 200 202 LEU CB C 44 0.1 1 1371 200 202 LEU CG C 26.92 0.1 1 1372 200 202 LEU N N 117.93 0.2 1 1373 201 203 TRP H H 9.71 0.03 1 1374 201 203 TRP HA H 5.09 0.03 1 1375 201 203 TRP HD1 H 6.93 0.03 1 1376 201 203 TRP HE1 H 10.04 0.03 1 1377 201 203 TRP C C 174.49 0.1 1 1378 201 203 TRP CA C 56.36 0.1 1 1379 201 203 TRP CB C 31.45 0.1 1 1380 201 203 TRP CG C 112.32 0.1 1 1381 201 203 TRP CD1 C 125.57 0.1 1 1382 201 203 TRP CE2 C 138.89 0.1 1 1383 201 203 TRP N N 126.55 0.2 1 1384 201 203 TRP NE1 N 128.95 0.2 1 1385 202 204 SER H H 9.82 0.03 1 1386 202 204 SER HA H 6.02 0.03 1 1387 202 204 SER C C 172.46 0.1 1 1388 202 204 SER CA C 56.19 0.1 1 1389 202 204 SER CB C 67.81 0.1 1 1390 202 204 SER N N 114.88 0.2 1 1391 203 205 TYR H H 8.58 0.03 1 1392 203 205 TYR HA H 4.66 0.03 1 1393 203 205 TYR C C 176.81 0.1 1 1394 203 205 TYR CA C 56.28 0.1 1 1395 203 205 TYR CB C 42.9 0.1 1 1396 203 205 TYR N N 113.33 0.2 1 1397 204 206 ASP H H 9.05 0.03 1 1398 204 206 ASP HA H 4.9 0.03 1 1399 204 206 ASP C C 176.03 0.1 1 1400 204 206 ASP CA C 54.08 0.1 1 1401 204 206 ASP CB C 41.05 0.1 1 1402 204 206 ASP N N 121.25 0.2 1 1403 205 207 ILE H H 7.77 0.03 1 1404 205 207 ILE HA H 4.25 0.03 1 1405 205 207 ILE C C 176.62 0.1 1 1406 205 207 ILE CA C 62.04 0.1 1 1407 205 207 ILE CB C 39.35 0.1 1 1408 205 207 ILE CG1 C 27.59 0.1 1 1409 205 207 ILE CG2 C 18.01 0.1 1 1410 205 207 ILE N N 122.66 0.2 1 1411 206 208 LYS H H 9.05 0.03 1 1412 206 208 LYS HA H 4.65 0.03 1 1413 206 208 LYS C C 176.17 0.1 1 1414 206 208 LYS CA C 53.88 0.1 1 1415 206 208 LYS CB C 32.14 0.1 1 1416 206 208 LYS CG C 23.51 0.1 1 1417 206 208 LYS CD C 27.35 0.1 1 1418 206 208 LYS CE C 41.83 0.1 1 1419 206 208 LYS N N 127.15 0.2 1 1420 207 209 GLY H H 8.06 0.03 1 1421 207 209 GLY HA2 H 4.24 0.03 2 1422 207 209 GLY HA3 H 4.16 0.03 2 1423 207 209 GLY C C 169.91 0.1 1 1424 207 209 GLY CA C 44.74 0.1 1 1425 207 209 GLY N N 109.61 0.2 1 1426 208 210 PRO HA H 4.09 0.03 1 1427 208 210 PRO C C 176.97 0.1 1 1428 208 210 PRO CA C 63.95 0.1 1 1429 208 210 PRO CB C 30.84 0.1 1 1430 208 210 PRO CG C 28.04 0.1 1 1431 208 210 PRO CD C 49.29 0.1 1 1432 208 210 PRO N N 136.09 0.2 1 1433 209 211 ALA H H 6.9 0.03 1 1434 209 211 ALA HA H 3.38 0.03 1 1435 209 211 ALA C C 174.27 0.1 1 1436 209 211 ALA CA C 53.41 0.1 1 1437 209 211 ALA CB C 18.75 0.1 1 1438 209 211 ALA N N 122.78 0.2 1 1439 210 212 LYS H H 8.15 0.03 1 1440 210 212 LYS HA H 4.8 0.03 1 1441 210 212 LYS C C 174.44 0.1 1 1442 210 212 LYS CA C 55.44 0.1 1 1443 210 212 LYS CB C 33.57 0.1 1 1444 210 212 LYS CG C 24.11 0.1 1 1445 210 212 LYS CD C 28.9 0.1 1 1446 210 212 LYS CE C 42.5 0.1 1 1447 210 212 LYS N N 120.48 0.2 1 1448 211 213 ILE H H 8.53 0.03 1 1449 211 213 ILE HA H 5.44 0.03 1 1450 211 213 ILE C C 175.56 0.1 1 1451 211 213 ILE CA C 58.28 0.1 1 1452 211 213 ILE CB C 41.65 0.1 1 1453 211 213 ILE CG1 C 24.59 0.1 1 1454 211 213 ILE CG2 C 20.57 0.1 1 1455 211 213 ILE CD1 C 12.15 0.1 1 1456 211 213 ILE N N 118.14 0.2 1 1457 212 214 GLU H H 8.7 0.03 1 1458 212 214 GLU HA H 4.92 0.03 1 1459 212 214 GLU C C 174.84 0.1 1 1460 212 214 GLU CA C 54.59 0.1 1 1461 212 214 GLU CB C 34.35 0.1 1 1462 212 214 GLU CG C 35.61 0.1 1 1463 212 214 GLU N N 118.1 0.2 1 1464 213 215 ASN H H 9.05 0.03 1 1465 213 215 ASN HA H 4.37 0.03 1 1466 213 215 ASN C C 173.15 0.1 1 1467 213 215 ASN CA C 53.61 0.1 1 1468 213 215 ASN CB C 36.58 0.1 1 1469 213 215 ASN CG C 178.31 0.1 1 1470 213 215 ASN N N 117.27 0.2 1 1471 214 216 LYS H H 7.98 0.03 1 1472 214 216 LYS HA H 4.37 0.03 1 1473 214 216 LYS C C 178.43 0.1 1 1474 214 216 LYS CA C 56.86 0.1 1 1475 214 216 LYS CB C 33.72 0.1 1 1476 214 216 LYS CG C 24.96 0.1 1 1477 214 216 LYS CD C 30.16 0.1 1 1478 214 216 LYS CE C 41.2 0.1 1 1479 214 216 LYS N N 120.2 0.2 1 1480 215 217 LYS H H 9.3 0.03 1 1481 215 217 LYS HA H 4.83 0.03 1 1482 215 217 LYS C C 174.81 0.1 1 1483 215 217 LYS CA C 55.32 0.1 1 1484 215 217 LYS CB C 36.05 0.1 1 1485 215 217 LYS CG C 23.36 0.1 1 1486 215 217 LYS CD C 29.57 0.1 1 1487 215 217 LYS CE C 42.77 0.1 1 1488 215 217 LYS N N 126.75 0.2 1 1489 216 218 VAL H H 8.51 0.03 1 1490 216 218 VAL HA H 3.18 0.03 1 1491 216 218 VAL C C 174.92 0.1 1 1492 216 218 VAL CA C 64.65 0.1 1 1493 216 218 VAL CB C 30.64 0.1 1 1494 216 218 VAL CG1 C 21.33 0.1 2 1495 216 218 VAL N N 122.3 0.2 1 1496 217 219 TRP H H 9.36 0.03 1 1497 217 219 TRP HA H 4.29 0.03 1 1498 217 219 TRP HD1 H 7.25 0.03 1 1499 217 219 TRP HE1 H 9.95 0.03 1 1500 217 219 TRP C C 176.25 0.1 1 1501 217 219 TRP CA C 59.31 0.1 1 1502 217 219 TRP CB C 32.01 0.1 1 1503 217 219 TRP CG C 109.92 0.1 1 1504 217 219 TRP CD1 C 127.45 0.1 1 1505 217 219 TRP CE2 C 138.5 0.1 1 1506 217 219 TRP N N 132.85 0.2 1 1507 217 219 TRP NE1 N 129.12 0.2 1 1508 218 220 GLY H H 7.95 0.03 1 1509 218 220 GLY HA2 H 2.96 0.03 2 1510 218 220 GLY C C 169.74 0.1 1 1511 218 220 GLY CA C 44.89 0.1 1 1512 218 220 GLY N N 103.48 0.2 1 1513 219 221 HIS H H 8.03 0.03 1 1514 219 221 HIS HA H 4.95 0.03 1 1515 219 221 HIS HD2 H 7.43 0.03 1 1516 219 221 HIS HE1 H 8.57 0.03 1 1517 219 221 HIS C C 174.39 0.1 1 1518 219 221 HIS CA C 55.22 0.1 1 1519 219 221 HIS CB C 32.77 0.1 1 1520 219 221 HIS CG C 134.41 0.1 1 1521 219 221 HIS CD2 C 120.06 0.1 1 1522 219 221 HIS CE1 C 138.14 0.1 1 1523 219 221 HIS N N 118.7 0.2 1 1524 219 221 HIS ND1 N 250.4 0.2 1 1525 219 221 HIS NE2 N 166.68 0.2 1 1526 220 222 ILE H H 8.31 0.03 1 1527 220 222 ILE HA H 4.62 0.03 1 1528 220 222 ILE C C 173.48 0.1 1 1529 220 222 ILE CA C 54.5 0.1 1 1530 220 222 ILE CB C 36.53 0.1 1 1531 220 222 ILE N N 125.05 0.2 1 1532 221 223 PRO HA H 4.48 0.03 1 1533 221 223 PRO C C 176.88 0.1 1 1534 221 223 PRO CA C 63.5 0.1 1 1535 221 223 PRO CB C 33.12 0.1 1 1536 221 223 PRO CG C 27.19 0.1 1 1537 221 223 PRO CD C 51.32 0.1 1 1538 221 223 PRO N N 137.75 0.2 1 1539 222 224 GLY H H 8.09 0.03 1 1540 222 224 GLY HA2 H 5.04 0.03 2 1541 222 224 GLY C C 175.18 0.1 1 1542 222 224 GLY CA C 44.9 0.1 1 1543 222 224 GLY N N 106.57 0.2 1 1544 223 225 THR H H 8.62 0.03 1 1545 223 225 THR HA H 4.57 0.03 1 1546 223 225 THR C C 174.65 0.1 1 1547 223 225 THR CA C 60.62 0.1 1 1548 223 225 THR CB C 68.53 0.1 1 1549 223 225 THR CG2 C 21.36 0.1 1 1550 223 225 THR N N 109.6 0.2 1 1551 224 226 HIS H H 8.68 0.03 1 1552 224 226 HIS HA H 4.5 0.03 1 1553 224 226 HIS HD2 H 6.83 0.03 1 1554 224 226 HIS HE1 H 7.81 0.03 1 1555 224 226 HIS C C 174.58 0.1 1 1556 224 226 HIS CA C 55.42 0.1 1 1557 224 226 HIS CB C 31.52 0.1 1 1558 224 226 HIS CG C 138.07 0.1 1 1559 224 226 HIS CD2 C 119.16 0.1 1 1560 224 226 HIS CE1 C 140.15 0.1 1 1561 224 226 HIS N N 121.08 0.2 1 1562 224 226 HIS ND1 N 215.41 0.2 1 1563 224 226 HIS NE2 N 183.88 0.2 1 1564 225 227 GLU H H 8.73 0.03 1 1565 225 227 GLU HA H 4.34 0.03 1 1566 225 227 GLU C C 175.91 0.1 1 1567 225 227 GLU CA C 56.9 0.1 1 1568 225 227 GLU CB C 29.1 0.1 1 1569 225 227 GLU CG C 36.22 0.1 1 1570 225 227 GLU N N 121.88 0.2 1 1571 226 228 GLY H H 8.28 0.03 1 1572 226 228 GLY HA2 H 5.52 0.03 2 1573 226 228 GLY C C 172.52 0.1 1 1574 226 228 GLY CA C 43.94 0.1 1 1575 226 228 GLY N N 114.15 0.2 1 1576 227 229 GLY H H 8.5 0.03 1 1577 227 229 GLY HA2 H 5.05 0.03 2 1578 227 229 GLY C C 172.31 0.1 1 1579 227 229 GLY CA C 44.13 0.1 1 1580 227 229 GLY N N 105.74 0.2 1 1581 228 230 ALA H H 8.4 0.03 1 1582 228 230 ALA HA H 4.6 0.03 1 1583 228 230 ALA C C 175.3 0.1 1 1584 228 230 ALA CA C 53.18 0.1 1 1585 228 230 ALA CB C 21.37 0.1 1 1586 228 230 ALA N N 120.23 0.2 1 1587 229 231 ASP H H 8.87 0.03 1 1588 229 231 ASP HA H 4.84 0.03 1 1589 229 231 ASP C C 176.1 0.1 1 1590 229 231 ASP CA C 53.71 0.1 1 1591 229 231 ASP CB C 41.86 0.1 1 1592 229 231 ASP N N 127.58 0.2 1 1593 230 232 GLY H H 8.95 0.03 1 1594 230 232 GLY HA2 H 4.13 0.03 2 1595 230 232 GLY C C 172.95 0.1 1 1596 230 232 GLY CA C 45.55 0.1 1 1597 230 232 GLY N N 106.65 0.2 1 1598 231 233 MET H H 8.67 0.03 1 1599 231 233 MET HA H 6 0.03 1 1600 231 233 MET C C 176.33 0.1 1 1601 231 233 MET CA C 54.84 0.1 1 1602 231 233 MET CB C 38.31 0.1 1 1603 231 233 MET CG C 30.65 0.1 1 1604 231 233 MET N N 113.47 0.2 1 1605 232 234 ASP H H 8.74 0.03 1 1606 232 234 ASP HA H 4.9 0.03 1 1607 232 234 ASP C C 174.81 0.1 1 1608 232 234 ASP CA C 55.44 0.1 1 1609 232 234 ASP CB C 48.53 0.1 1 1610 232 234 ASP N N 120.79 0.2 1 1611 233 235 PHE H H 9.21 0.03 1 1612 233 235 PHE HA H 5.75 0.03 1 1613 233 235 PHE C C 177.77 0.1 1 1614 233 235 PHE CA C 58.37 0.1 1 1615 233 235 PHE CB C 41.41 0.1 1 1616 233 235 PHE N N 116.95 0.2 1 1617 234 236 ASP H H 9.45 0.03 1 1618 234 236 ASP HA H 4.7 0.03 1 1619 234 236 ASP C C 179.54 0.1 1 1620 234 236 ASP CA C 52.12 0.1 1 1621 234 236 ASP CB C 42.44 0.1 1 1622 234 236 ASP N N 119.98 0.2 1 1623 235 237 GLU H H 8.67 0.03 1 1624 235 237 GLU HA H 3.88 0.03 1 1625 235 237 GLU C C 176.43 0.1 1 1626 235 237 GLU CA C 58.89 0.1 1 1627 235 237 GLU CB C 29.01 0.1 1 1628 235 237 GLU CG C 35.12 0.1 1 1629 235 237 GLU N N 114.61 0.2 1 1630 236 238 ASP H H 8.14 0.03 1 1631 236 238 ASP HA H 5.01 0.03 1 1632 236 238 ASP C C 175.75 0.1 1 1633 236 238 ASP CA C 53.75 0.1 1 1634 236 238 ASP CB C 40.87 0.1 1 1635 236 238 ASP N N 121.63 0.2 1 1636 237 239 ASN H H 8.68 0.03 1 1637 237 239 ASN HA H 4.37 0.03 1 1638 237 239 ASN C C 174.98 0.1 1 1639 237 239 ASN CA C 55.79 0.1 1 1640 237 239 ASN CB C 36.29 0.1 1 1641 237 239 ASN N N 112.19 0.2 1 1642 238 240 ASN H H 8.44 0.03 1 1643 238 240 ASN HA H 5.36 0.03 1 1644 238 240 ASN C C 174.81 0.1 1 1645 238 240 ASN CA C 53.86 0.1 1 1646 238 240 ASN CB C 38.37 0.1 1 1647 238 240 ASN N N 114.51 0.2 1 1648 239 241 LEU H H 9.47 0.03 1 1649 239 241 LEU HA H 4.38 0.03 1 1650 239 241 LEU C C 174.87 0.1 1 1651 239 241 LEU CA C 53.94 0.1 1 1652 239 241 LEU CB C 44.82 0.1 1 1653 239 241 LEU CG C 28.4 0.1 1 1654 239 241 LEU CD1 C 27.25 0.1 2 1655 239 241 LEU N N 127.15 0.2 1 1656 240 242 LEU H H 9.03 0.03 1 1657 240 242 LEU HA H 5.25 0.03 1 1658 240 242 LEU C C 176.34 0.1 1 1659 240 242 LEU CA C 56.1 0.1 1 1660 240 242 LEU CB C 42.92 0.1 1 1661 240 242 LEU N N 130.53 0.2 1 1662 241 243 VAL H H 9.18 0.03 1 1663 241 243 VAL HA H 4.74 0.03 1 1664 241 243 VAL C C 176.09 0.1 1 1665 241 243 VAL CA C 59.95 0.1 1 1666 241 243 VAL CB C 36.14 0.1 1 1667 241 243 VAL CG1 C 22.04 0.1 1 1668 241 243 VAL N N 119.99 0.2 1 1669 242 244 ALA H H 9.25 0.03 1 1670 242 244 ALA HA H 4.05 0.03 1 1671 242 244 ALA C C 174.64 0.1 1 1672 242 244 ALA CA C 53.41 0.1 1 1673 242 244 ALA CB C 18.01 0.1 1 1674 242 244 ALA N N 131.22 0.2 1 1675 243 245 ASN H H 8.01 0.03 1 1676 243 245 ASN HA H 5.12 0.03 1 1677 243 245 ASN C C 176.51 0.1 1 1678 243 245 ASN CA C 51.14 0.1 1 1679 243 245 ASN CB C 37.83 0.1 1 1680 243 245 ASN N N 124.75 0.2 1 1681 244 246 TRP H H 8.6 0.03 1 1682 244 246 TRP HA H 4.17 0.03 1 1683 244 246 TRP HD1 H 7.02 0.03 1 1684 244 246 TRP HE1 H 12.14 0.03 1 1685 244 246 TRP C C 177.81 0.1 1 1686 244 246 TRP CA C 62.29 0.1 1 1687 244 246 TRP CB C 32.05 0.1 1 1688 244 246 TRP CD1 C 130.27 0.1 1 1689 244 246 TRP CE2 C 139.31 0.1 1 1690 244 246 TRP N N 131.7 0.2 1 1691 244 246 TRP NE1 N 134.76 0.2 1 1692 245 247 GLY H H 7.3 0.03 1 1693 245 247 GLY HA2 H 4.91 0.03 2 1694 245 247 GLY C C 174.35 0.1 1 1695 245 247 GLY CA C 46.32 0.1 1 1696 245 247 GLY N N 114.84 0.2 1 1697 246 248 SER H H 8.05 0.03 1 1698 246 248 SER HA H 4.01 0.03 1 1699 246 248 SER C C 178.04 0.1 1 1700 246 248 SER CA C 59.27 0.1 1 1701 246 248 SER CB C 68.01 0.1 1 1702 246 248 SER N N 113.82 0.2 1 1703 247 249 SER H H 8.06 0.03 1 1704 247 249 SER HA H 4.51 0.03 1 1705 247 249 SER C C 171.21 0.1 1 1706 247 249 SER CA C 60 0.1 1 1707 247 249 SER CB C 61.65 0.1 1 1708 247 249 SER N N 113.18 0.2 1 1709 248 250 HIS H H 8.79 0.03 1 1710 248 250 HIS HA H 5.61 0.03 1 1711 248 250 HIS HD2 H 6.24 0.03 1 1712 248 250 HIS HE1 H 7.65 0.03 1 1713 248 250 HIS C C 174.39 0.1 1 1714 248 250 HIS CA C 55.95 0.1 1 1715 248 250 HIS CB C 31.99 0.1 1 1716 248 250 HIS CG C 130 0.1 1 1717 248 250 HIS CD2 C 126.32 0.1 1 1718 248 250 HIS CE1 C 138.55 0.1 1 1719 248 250 HIS N N 116.25 0.2 1 1720 248 250 HIS ND1 N 168.37 0.2 1 1721 248 250 HIS NE2 N 246.28 0.2 1 1722 249 251 ILE H H 8.81 0.03 1 1723 249 251 ILE HA H 4.54 0.03 1 1724 249 251 ILE C C 175.41 0.1 1 1725 249 251 ILE CA C 59.85 0.1 1 1726 249 251 ILE CB C 40.98 0.1 1 1727 249 251 ILE CG1 C 24.3 0.1 1 1728 249 251 ILE CG2 C 17.36 0.1 1 1729 249 251 ILE N N 119.53 0.2 1 1730 250 252 GLU H H 9.42 0.03 1 1731 250 252 GLU HA H 5.16 0.03 1 1732 250 252 GLU C C 176.71 0.1 1 1733 250 252 GLU CA C 54.06 0.1 1 1734 250 252 GLU CB C 31.72 0.1 1 1735 250 252 GLU CG C 33.74 0.1 1 1736 250 252 GLU N N 125.46 0.2 1 1737 251 253 VAL H H 8.19 0.03 1 1738 251 253 VAL HA H 5 0.03 1 1739 251 253 VAL C C 175.53 0.1 1 1740 251 253 VAL CA C 61.29 0.1 1 1741 251 253 VAL CB C 32.87 0.1 1 1742 251 253 VAL CG1 C 20.54 0.1 2 1743 251 253 VAL N N 119.76 0.2 1 1744 252 254 PHE H H 9.97 0.03 1 1745 252 254 PHE HA H 4.73 0.03 1 1746 252 254 PHE C C 177.75 0.1 1 1747 252 254 PHE CA C 57.47 0.1 1 1748 252 254 PHE CB C 43.15 0.1 1 1749 252 254 PHE N N 126.4 0.2 1 1750 253 255 GLY H H 9.33 0.03 1 1751 253 255 GLY HA2 H 4.06 0.03 2 1752 253 255 GLY C C 173.57 0.1 1 1753 253 255 GLY CA C 44.87 0.1 1 1754 253 255 GLY N N 108.41 0.2 1 1755 254 256 PRO HA H 4.88 0.03 1 1756 254 256 PRO C C 176.62 0.1 1 1757 254 256 PRO CA C 65.4 0.1 1 1758 254 256 PRO CB C 32.23 0.1 1 1759 254 256 PRO CG C 27.29 0.1 1 1760 254 256 PRO CD C 49.95 0.1 1 1761 254 256 PRO N N 132.15 0.2 1 1762 255 257 ASP H H 8.47 0.03 1 1763 255 257 ASP HA H 4.93 0.03 1 1764 255 257 ASP C C 177.19 0.1 1 1765 255 257 ASP CA C 53.68 0.1 1 1766 255 257 ASP CB C 41.01 0.1 1 1767 255 257 ASP N N 112.74 0.2 1 1768 256 258 GLY H H 7.87 0.03 1 1769 256 258 GLY HA2 H 5.78 0.03 2 1770 256 258 GLY C C 174.46 0.1 1 1771 256 258 GLY CA C 43.92 0.1 1 1772 256 258 GLY N N 110.67 0.2 1 1773 257 259 GLY H H 8.79 0.03 1 1774 257 259 GLY HA2 H 4.29 0.03 2 1775 257 259 GLY C C 173 0.1 1 1776 257 259 GLY CA C 46.15 0.1 1 1777 257 259 GLY N N 113.03 0.2 1 1778 258 260 GLN H H 8.25 0.03 1 1779 258 260 GLN HA H 4.97 0.03 1 1780 258 260 GLN C C 173.41 0.1 1 1781 258 260 GLN CA C 53.04 0.1 1 1782 258 260 GLN CB C 28.78 0.1 1 1783 258 260 GLN N N 124.91 0.2 1 1784 259 261 PRO HA H 3.36 0.03 1 1785 259 261 PRO C C 175.22 0.1 1 1786 259 261 PRO CA C 63.85 0.1 1 1787 259 261 PRO CB C 31.34 0.1 1 1788 259 261 PRO CG C 27.21 0.1 1 1789 259 261 PRO CD C 49.37 0.1 1 1790 259 261 PRO N N 135.14 0.2 1 1791 260 262 LYS H H 9.13 0.03 1 1792 260 262 LYS HA H 4.46 0.03 1 1793 260 262 LYS C C 176.67 0.1 1 1794 260 262 LYS CA C 55.76 0.1 1 1795 260 262 LYS CB C 33.66 0.1 1 1796 260 262 LYS CG C 24.2 0.1 1 1797 260 262 LYS CD C 29.38 0.1 1 1798 260 262 LYS N N 119.63 0.2 1 1799 261 263 MET H H 8.03 0.03 1 1800 261 263 MET HA H 4.86 0.03 1 1801 261 263 MET C C 172.34 0.1 1 1802 261 263 MET CA C 55.07 0.1 1 1803 261 263 MET CB C 36.95 0.1 1 1804 261 263 MET CG C 31.42 0.1 1 1805 261 263 MET N N 117.08 0.2 1 1806 262 264 ARG H H 8.87 0.03 1 1807 262 264 ARG HA H 5.24 0.03 1 1808 262 264 ARG HE H 10.42 0.03 1 1809 262 264 ARG C C 174.42 0.1 1 1810 262 264 ARG CA C 54.06 0.1 1 1811 262 264 ARG CB C 35.31 0.1 1 1812 262 264 ARG CG C 25.03 0.1 1 1813 262 264 ARG CD C 43.37 0.1 1 1814 262 264 ARG CZ C 160.2 0.1 1 1815 262 264 ARG N N 118.38 0.2 1 1816 262 264 ARG NE N 84.9 0.2 1 1817 263 265 ILE H H 9.63 0.03 1 1818 263 265 ILE HA H 4.57 0.03 1 1819 263 265 ILE C C 175.4 0.1 1 1820 263 265 ILE CA C 59.82 0.1 1 1821 263 265 ILE CB C 39.98 0.1 1 1822 263 265 ILE CG1 C 26.87 0.1 1 1823 263 265 ILE CG2 C 17.4 0.1 1 1824 263 265 ILE CD1 C 15.15 0.1 1 1825 263 265 ILE N N 122.47 0.2 1 1826 264 266 ARG H H 8.95 0.03 1 1827 264 266 ARG HA H 3.69 0.03 1 1828 264 266 ARG HE H 7.1 0.03 1 1829 264 266 ARG C C 174.82 0.1 1 1830 264 266 ARG CA C 56.32 0.1 1 1831 264 266 ARG CB C 30.35 0.1 1 1832 264 266 ARG CG C 26.9 0.1 1 1833 264 266 ARG CD C 43.01 0.1 1 1834 264 266 ARG CZ C 159.5 0.1 1 1835 264 266 ARG N N 128.66 0.2 1 1836 264 266 ARG NE N 85.1 0.2 1 1837 265 267 CYS H H 8.15 0.03 1 1838 265 267 CYS HA H 3.52 0.03 1 1839 265 267 CYS C C 173.58 0.1 1 1840 265 267 CYS CA C 54.67 0.1 1 1841 265 267 CYS CB C 27.92 0.1 1 1842 265 267 CYS N N 124.21 0.2 1 1843 266 268 PRO HA H 4.19 0.03 1 1844 266 268 PRO C C 173.3 0.1 1 1845 266 268 PRO CA C 62.05 0.1 1 1846 266 268 PRO CB C 28.5 0.1 1 1847 266 268 PRO CG C 25.25 0.1 1 1848 266 268 PRO CD C 48.23 0.1 1 1849 267 269 PHE H H 5.75 0.03 1 1850 267 269 PHE HA H 4.66 0.03 1 1851 267 269 PHE C C 176.47 0.1 1 1852 267 269 PHE CA C 53.1 0.1 1 1853 267 269 PHE CB C 40.65 0.1 1 1854 267 269 PHE N N 114.01 0.2 1 1855 268 270 GLU H H 9.17 0.03 1 1856 268 270 GLU HA H 4.44 0.03 1 1857 268 270 GLU C C 179.34 0.1 1 1858 268 270 GLU CA C 58 0.1 1 1859 268 270 GLU CB C 32.71 0.1 1 1860 268 270 GLU CG C 36.63 0.1 1 1861 268 270 GLU N N 114.24 0.2 1 1862 269 271 LYS H H 6.09 0.03 1 1863 269 271 LYS HA H 3.92 0.03 1 1864 269 271 LYS C C 171.45 0.1 1 1865 269 271 LYS CA C 54.49 0.1 1 1866 269 271 LYS CB C 34.54 0.1 1 1867 269 271 LYS N N 112.48 0.2 1 1868 271 273 SER HA H 5.26 0.03 1 1869 271 273 SER C C 172.55 0.1 1 1870 271 273 SER CA C 56.5 0.1 1 1871 271 273 SER CB C 64.96 0.1 1 1872 272 274 ASN H H 7.87 0.03 1 1873 272 274 ASN HA H 4.98 0.03 1 1874 272 274 ASN C C 173 0.1 1 1875 272 274 ASN CA C 50.79 0.1 1 1876 272 274 ASN CB C 42.11 0.1 1 1877 272 274 ASN N N 116.49 0.2 1 1878 273 275 LEU H H 9.91 0.03 1 1879 273 275 LEU HA H 6.4 0.03 1 1880 273 275 LEU C C 177.47 0.1 1 1881 273 275 LEU CA C 53.93 0.1 1 1882 273 275 LEU CB C 45.4 0.1 1 1883 273 275 LEU CG C 26.63 0.1 1 1884 273 275 LEU N N 115.55 0.2 1 1885 274 276 HIS H H 9.77 0.03 1 1886 274 276 HIS HA H 4.86 0.03 1 1887 274 276 HIS HD2 H 7.71 0.03 1 1888 274 276 HIS HE1 H 8.57 0.03 1 1889 274 276 HIS HE2 H 12.42 0.03 1 1890 274 276 HIS C C 174.3 0.1 1 1891 274 276 HIS CA C 57.86 0.1 1 1892 274 276 HIS CB C 37.1 0.1 1 1893 274 276 HIS CG C 139.68 0.1 1 1894 274 276 HIS CD2 C 117.32 0.1 1 1895 274 276 HIS CE1 C 140.7 0.1 1 1896 274 276 HIS N N 125.97 0.2 1 1897 274 276 HIS ND1 N 244.56 0.2 1 1898 274 276 HIS NE2 N 163.89 0.2 1 1899 275 277 PHE H H 9.19 0.03 1 1900 275 277 PHE HA H 5.27 0.03 1 1901 275 277 PHE C C 177.31 0.1 1 1902 275 277 PHE CA C 58.21 0.1 1 1903 275 277 PHE CB C 39.83 0.1 1 1904 275 277 PHE N N 125.17 0.2 1 1905 276 278 LYS H H 8.9 0.03 1 1906 276 278 LYS C C 175.64 0.1 1 1907 276 278 LYS CA C 53.92 0.1 1 1908 276 278 LYS CB C 32.57 0.1 1 1909 276 278 LYS N N 125.15 0.2 1 1910 277 279 PRO HA H 4.22 0.03 1 1911 277 279 PRO C C 175.93 0.1 1 1912 277 279 PRO CA C 64.08 0.1 1 1913 277 279 PRO CB C 32.34 0.1 1 1914 277 279 PRO CG C 27.57 0.1 1 1915 277 279 PRO CD C 51.45 0.1 1 1916 277 279 PRO N N 144.18 0.2 1 1917 278 280 GLN H H 9.38 0.03 1 1918 278 280 GLN HA H 3.78 0.03 1 1919 278 280 GLN C C 174.73 0.1 1 1920 278 280 GLN CA C 57.26 0.1 1 1921 278 280 GLN CB C 26.54 0.1 1 1922 278 280 GLN CG C 34.71 0.1 1 1923 278 280 GLN N N 115.76 0.2 1 1924 279 281 THR H H 7.89 0.03 1 1925 279 281 THR HA H 4.98 0.03 1 1926 279 281 THR C C 172.91 0.1 1 1927 279 281 THR CA C 60.62 0.1 1 1928 279 281 THR CB C 73.38 0.1 1 1929 279 281 THR CG2 C 21.35 0.1 1 1930 279 281 THR N N 108.65 0.2 1 1931 280 282 LYS H H 7.9 0.03 1 1932 280 282 LYS HA H 4.84 0.03 1 1933 280 282 LYS C C 175.72 0.1 1 1934 280 282 LYS CA C 55.29 0.1 1 1935 280 282 LYS CB C 32.61 0.1 1 1936 280 282 LYS CG C 24.89 0.1 1 1937 280 282 LYS CD C 29.14 0.1 1 1938 280 282 LYS CE C 42.47 0.1 1 1939 280 282 LYS N N 115.47 0.2 1 1940 281 283 THR H H 8.76 0.03 1 1941 281 283 THR HA H 4.21 0.03 1 1942 281 283 THR C C 172.99 0.1 1 1943 281 283 THR CA C 63.74 0.1 1 1944 281 283 THR CB C 69.36 0.1 1 1945 281 283 THR CG2 C 24 0.1 1 1946 281 283 THR N N 118.49 0.2 1 1947 282 284 ILE H H 8.67 0.03 1 1948 282 284 ILE HA H 4.01 0.03 1 1949 282 284 ILE C C 174.91 0.1 1 1950 282 284 ILE CA C 60.74 0.1 1 1951 282 284 ILE CB C 38.05 0.1 1 1952 282 284 ILE CG1 C 28.42 0.1 1 1953 282 284 ILE CG2 C 19.12 0.1 1 1954 282 284 ILE CD1 C 15.5 0.1 1 1955 282 284 ILE N N 126.79 0.2 1 1956 283 285 PHE H H 9.09 0.03 1 1957 283 285 PHE HA H 5.33 0.03 1 1958 283 285 PHE C C 175.8 0.1 1 1959 283 285 PHE CA C 56.82 0.1 1 1960 283 285 PHE CB C 41.37 0.1 1 1961 283 285 PHE N N 125.37 0.2 1 1962 284 286 VAL H H 9.85 0.03 1 1963 284 286 VAL HA H 5.49 0.03 1 1964 284 286 VAL C C 175.46 0.1 1 1965 284 286 VAL CA C 59.84 0.1 1 1966 284 286 VAL CB C 36.85 0.1 1 1967 284 286 VAL CG1 C 22.8 0.1 2 1968 284 286 VAL CG2 C 21.47 0.1 2 1969 284 286 VAL N N 121.99 0.2 1 1970 285 287 THR H H 9.28 0.03 1 1971 285 287 THR HA H 5.35 0.03 1 1972 285 287 THR C C 174.38 0.1 1 1973 285 287 THR CA C 59.62 0.1 1 1974 285 287 THR CB C 69.56 0.1 1 1975 285 287 THR CG2 C 23.34 0.1 1 1976 285 287 THR N N 117.43 0.2 1 1977 286 288 GLU H H 8.65 0.03 1 1978 286 288 GLU HA H 5.05 0.03 1 1979 286 288 GLU C C 177.65 0.1 1 1980 286 288 GLU CA C 55.37 0.1 1 1981 286 288 GLU CB C 32.77 0.1 1 1982 286 288 GLU CG C 37.85 0.1 1 1983 286 288 GLU N N 115.66 0.2 1 1984 287 289 HIS H H 7.95 0.03 1 1985 287 289 HIS HA H 5.04 0.03 1 1986 287 289 HIS HD2 H 6.86 0.03 1 1987 287 289 HIS HE1 H 8.4 0.03 1 1988 287 289 HIS C C 175.9 0.1 1 1989 287 289 HIS CA C 53.86 0.1 1 1990 287 289 HIS CB C 33.68 0.1 1 1991 287 289 HIS CG C 139.83 0.1 1 1992 287 289 HIS CD2 C 113.87 0.1 1 1993 287 289 HIS CE1 C 140.84 0.1 1 1994 287 289 HIS N N 118.36 0.2 1 1995 287 289 HIS ND1 N 247.1 0.2 1 1996 287 289 HIS NE2 N 166.73 0.2 1 1997 288 290 GLU H H 9.43 0.03 1 1998 288 290 GLU HA H 4.39 0.03 1 1999 288 290 GLU C C 177.58 0.1 1 2000 288 290 GLU CA C 59.09 0.1 1 2001 288 290 GLU CB C 30.29 0.1 1 2002 288 290 GLU CG C 35.9 0.1 1 2003 288 290 GLU N N 125.38 0.2 1 2004 289 291 ASN H H 10.75 0.03 1 2005 289 291 ASN HA H 4.96 0.03 1 2006 289 291 ASN C C 175.7 0.1 1 2007 289 291 ASN CA C 52.1 0.1 1 2008 289 291 ASN CB C 38.77 0.1 1 2009 289 291 ASN N N 114.84 0.2 1 2010 290 292 ASN H H 7.02 0.03 1 2011 290 292 ASN HA H 4.96 0.03 1 2012 290 292 ASN C C 172.85 0.1 1 2013 290 292 ASN CA C 55.03 0.1 1 2014 290 292 ASN CB C 36.33 0.1 1 2015 290 292 ASN N N 116.47 0.2 1 2016 291 293 ALA H H 7.63 0.03 1 2017 291 293 ALA HA H 4.95 0.03 1 2018 291 293 ALA C C 175.01 0.1 1 2019 291 293 ALA CA C 50.77 0.1 1 2020 291 293 ALA CB C 23.86 0.1 1 2021 291 293 ALA N N 117.89 0.2 1 2022 292 294 VAL H H 7.93 0.03 1 2023 292 294 VAL HA H 5.37 0.03 1 2024 292 294 VAL C C 174.38 0.1 1 2025 292 294 VAL CA C 60.06 0.1 1 2026 292 294 VAL CB C 34.88 0.1 1 2027 292 294 VAL CG1 C 22.45 0.1 2 2028 292 294 VAL CG2 C 20.91 0.1 2 2029 292 294 VAL N N 116.02 0.2 1 2030 293 295 TRP H H 9.77 0.03 1 2031 293 295 TRP HA H 5.62 0.03 1 2032 293 295 TRP HD1 H 6.71 0.03 1 2033 293 295 TRP HE1 H 12.61 0.03 1 2034 293 295 TRP C C 174.31 0.1 1 2035 293 295 TRP CA C 55.75 0.1 1 2036 293 295 TRP CB C 34.71 0.1 1 2037 293 295 TRP CG C 109.94 0.1 1 2038 293 295 TRP CD1 C 128.12 0.1 1 2039 293 295 TRP CE2 C 138.93 0.1 1 2040 293 295 TRP N N 128.43 0.2 1 2041 293 295 TRP NE1 N 139.38 0.2 1 2042 294 296 LYS H H 9.54 0.03 1 2043 294 296 LYS HA H 6 0.03 1 2044 294 296 LYS C C 174.7 0.1 1 2045 294 296 LYS CA C 54.03 0.1 1 2046 294 296 LYS CB C 35.27 0.1 1 2047 294 296 LYS CG C 23.47 0.1 1 2048 294 296 LYS CD C 29.9 0.1 1 2049 294 296 LYS N N 117.2 0.2 1 2050 295 297 PHE H H 8.76 0.03 1 2051 295 297 PHE HA H 4.76 0.03 1 2052 295 297 PHE C C 171.18 0.1 1 2053 295 297 PHE CA C 55.78 0.1 1 2054 295 297 PHE CB C 41.26 0.1 1 2055 295 297 PHE N N 118.08 0.2 1 2056 296 298 GLU H H 8.87 0.03 1 2057 296 298 GLU HA H 4.64 0.03 1 2058 296 298 GLU C C 176.14 0.1 1 2059 296 298 GLU CA C 55.06 0.1 1 2060 296 298 GLU CB C 31.07 0.1 1 2061 296 298 GLU CG C 36.28 0.1 1 2062 296 298 GLU N N 118.75 0.2 1 2063 297 299 TRP H H 9.35 0.03 1 2064 297 299 TRP HA H 5.49 0.03 1 2065 297 299 TRP HD1 H 8.06 0.03 1 2066 297 299 TRP HE1 H 13.13 0.03 1 2067 297 299 TRP C C 173.41 0.1 1 2068 297 299 TRP CA C 52.47 0.1 1 2069 297 299 TRP CB C 32.1 0.1 1 2070 297 299 TRP CG C 112.67 0.1 1 2071 297 299 TRP CD1 C 128.63 0.1 1 2072 297 299 TRP CE2 C 141.13 0.1 1 2073 297 299 TRP N N 126.44 0.2 1 2074 297 299 TRP NE1 N 135.94 0.2 1 2075 298 300 GLN H H 5.47 0.03 1 2076 298 300 GLN HA H 3.8 0.03 1 2077 298 300 GLN C C 175.29 0.1 1 2078 298 300 GLN CA C 56.17 0.1 1 2079 298 300 GLN CB C 29.51 0.1 1 2080 298 300 GLN N N 118.13 0.2 1 2081 299 301 ARG H H 7.12 0.03 1 2082 299 301 ARG HA H 4.46 0.03 1 2083 299 301 ARG C C 172.87 0.1 1 2084 299 301 ARG CA C 53.61 0.1 1 2085 299 301 ARG CB C 31.37 0.1 1 2086 299 301 ARG CG C 24.73 0.1 1 2087 299 301 ARG CD C 42.45 0.1 1 2088 299 301 ARG CZ C 159.3 0.1 1 2089 299 301 ARG N N 113.65 0.2 1 2090 299 301 ARG NE N 83.5 0.2 1 2091 300 302 ASN H H 8.21 0.03 1 2092 300 302 ASN HA H 4.82 0.03 1 2093 300 302 ASN C C 174.88 0.1 1 2094 300 302 ASN CA C 52.67 0.1 1 2095 300 302 ASN CB C 38.61 0.1 1 2096 300 302 ASN N N 115.35 0.2 1 2097 301 303 GLY H H 8.01 0.03 1 2098 301 303 GLY C C 173.66 0.1 1 2099 301 303 GLY CA C 43.13 0.1 1 2100 301 303 GLY N N 109.33 0.2 1 2101 302 304 LYS H H 7.35 0.03 1 2102 302 304 LYS HA H 4.22 0.03 1 2103 302 304 LYS C C 179.21 0.1 1 2104 302 304 LYS CA C 54.38 0.1 1 2105 302 304 LYS CB C 32.1 0.1 1 2106 302 304 LYS CG C 23.33 0.1 1 2107 302 304 LYS CD C 29.2 0.1 1 2108 302 304 LYS CE C 42.5 0.1 1 2109 302 304 LYS N N 120.92 0.2 1 2110 303 305 LYS H H 9.1 0.03 1 2111 303 305 LYS HA H 4.16 0.03 1 2112 303 305 LYS C C 179.42 0.1 1 2113 303 305 LYS CA C 59.02 0.1 1 2114 303 305 LYS CB C 32.27 0.1 1 2115 303 305 LYS CG C 26.24 0.1 1 2116 303 305 LYS CD C 29.8 0.1 1 2117 303 305 LYS CE C 42.29 0.1 1 2118 303 305 LYS N N 130.64 0.2 1 2119 304 306 GLN H H 9.16 0.03 1 2120 304 306 GLN HA H 4.89 0.03 1 2121 304 306 GLN C C 177.25 0.1 1 2122 304 306 GLN CA C 55.57 0.1 1 2123 304 306 GLN CB C 31.2 0.1 1 2124 304 306 GLN CG C 36.1 0.1 1 2125 304 306 GLN N N 126.09 0.2 1 2126 305 307 TYR H H 10.24 0.03 1 2127 305 307 TYR HA H 4.37 0.03 1 2128 305 307 TYR C C 179.23 0.1 1 2129 305 307 TYR CA C 60.9 0.1 1 2130 305 307 TYR CB C 39.27 0.1 1 2131 305 307 TYR N N 124.69 0.2 1 2132 306 308 CYS H H 9.67 0.03 1 2133 306 308 CYS HA H 3.74 0.03 1 2134 306 308 CYS C C 174.31 0.1 1 2135 306 308 CYS CA C 59.51 0.1 1 2136 306 308 CYS CB C 26.99 0.1 1 2137 306 308 CYS N N 115.48 0.2 1 2138 307 309 GLU H H 7.96 0.03 1 2139 307 309 GLU HA H 4.45 0.03 1 2140 307 309 GLU C C 177.1 0.1 1 2141 307 309 GLU CA C 56.7 0.1 1 2142 307 309 GLU CB C 32.63 0.1 1 2143 307 309 GLU CG C 38.96 0.1 1 2144 307 309 GLU N N 121.43 0.2 1 2145 308 310 THR H H 7.6 0.03 1 2146 308 310 THR HA H 4.2 0.03 1 2147 308 310 THR C C 173.21 0.1 1 2148 308 310 THR CA C 61.6 0.1 1 2149 308 310 THR CB C 71.42 0.1 1 2150 308 310 THR CG2 C 21.3 0.1 1 2151 308 310 THR N N 110.55 0.2 1 2152 309 311 LEU H H 7.98 0.03 1 2153 309 311 LEU HA H 4.36 0.03 1 2154 309 311 LEU C C 176.86 0.1 1 2155 309 311 LEU CA C 54.22 0.1 1 2156 309 311 LEU CB C 43.66 0.1 1 2157 309 311 LEU CG C 26.96 0.1 1 2158 309 311 LEU CD1 C 25 0.1 2 2159 309 311 LEU CD2 C 23.57 0.1 2 2160 309 311 LEU N N 120.1 0.2 1 2161 310 312 LYS H H 8.3 0.03 1 2162 310 312 LYS HA H 4.08 0.03 1 2163 310 312 LYS C C 176.06 0.1 1 2164 310 312 LYS CA C 56.86 0.1 1 2165 310 312 LYS CB C 33.5 0.1 1 2166 310 312 LYS CG C 24.75 0.1 1 2167 310 312 LYS CD C 29.14 0.1 1 2168 310 312 LYS CE C 42.6 0.1 1 2169 310 312 LYS N N 123.05 0.2 1 2170 311 313 PHE H H 8.37 0.03 1 2171 311 313 PHE HA H 4.66 0.03 1 2172 311 313 PHE C C 175.21 0.1 1 2173 311 313 PHE CA C 57.78 0.1 1 2174 311 313 PHE CB C 39.64 0.1 1 2175 311 313 PHE N N 122.89 0.2 1 2176 312 314 GLY H H 8.2 0.03 1 2177 312 314 GLY HA2 H 3.89 0.03 2 2178 312 314 GLY HA3 H 3.74 0.03 2 2179 312 314 GLY C C 172.97 0.1 1 2180 312 314 GLY CA C 45.44 0.1 1 2181 312 314 GLY N N 111.03 0.2 1 2182 313 315 ILE H H 7.74 0.03 1 2183 313 315 ILE HA H 4.06 0.03 1 2184 313 315 ILE C C 175.02 0.1 1 2185 313 315 ILE CA C 62.39 0.1 1 2186 313 315 ILE CB C 38.67 0.1 1 2187 313 315 ILE CG1 C 26.04 0.1 1 2188 313 315 ILE CG2 C 17.17 0.1 1 2189 313 315 ILE CD1 C 12.7 0.1 1 2190 313 315 ILE N N 118.51 0.2 1 2191 314 316 PHE H H 7.76 0.03 1 2192 314 316 PHE HA H 4.43 0.03 1 2193 314 316 PHE C C 180.42 0.1 1 2194 314 316 PHE CA C 59.07 0.1 1 2195 314 316 PHE CB C 39.72 0.1 1 2196 314 316 PHE N N 128.2 0.2 1 stop_ save_