data_5208 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N resonance assignments for the perdeuterated 22 kD palm-thumb domain of DNA polymerase B ; _BMRB_accession_number 5208 _BMRB_flat_file_name bmr5208.str _Entry_type original _Submission_date 2001-11-14 _Accession_date 2001-11-14 _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 Gryk Michael R. . 2 Maciejewski Mark W. . 3 Robertson Anthony . . 4 Mullen Mary A. . 5 Wilson Samuel H. . 6 Mullen Gregory P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 230 "13C chemical shifts" 621 "15N chemical shifts" 168 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-07 original author . stop_ _Original_release_date 2002-05-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N Resonance Assignments for the Perdeuterated 22 kD Palm-thumb Domain of DNA Polymerase Beta ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21880671 _PubMed_ID 11883786 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gryk Michael R. . 2 Maciejewski Mark W. . 3 Robertson Anthony . . 4 Mullen Mary A. . 5 Wilson Samuel H. . 6 Mullen Gregory P. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 197 _Page_last 198 _Year 2002 _Details . loop_ _Keyword 'Rattus norvegicus' 'DNA polymerase B' TROSY deuteration 'DNA repair' stop_ save_ ################################## # Molecular system description # ################################## save_system_B-pol _Saveframe_category molecular_system _Mol_system_name 'Palm-Thumb Domain of DNA Polymerase B' _Abbreviation_common B-pol _Enzyme_commission_number 2.7.7.7 loop_ _Mol_system_component_name _Mol_label 'B-Pol palm-thumb' $B-Pol stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'DNA polmerization (C-terminal domain)' 'DNA binding (N-terminal domain)' 'deoxyribose 5'-phosphate excision at incised abasic sites (N-terminal domain)' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_B-Pol _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DNA Polymerase B' _Abbreviation_common B-Pol _Molecular_mass 22022 _Mol_thiol_state 'all free' _Details 'First 3 residues: MGK are not native to full length B-Pol.' ############################## # Polymer residue sequence # ############################## _Residue_count 190 _Mol_residue_sequence ; MGKRIPREEMLQMQDIVLNE VKKLDPEYIATVCGSFRRGA ESSGDMDVLLTHPNFTSESS KQPKLLHRVVEQLQKVRFIT DTLSKGETKFMGVCQLPSEN DENEYPHRRIDIRLIPKDQY YCGVLYFTGSDIFNKNMRAH ALEKGFTINEYTIRPLGVTG VAGEPLPVDSEQDIFDYIQW RYREPKDRSE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 MET 2 -2 GLY 3 -1 LYS 4 149 ARG 5 150 ILE 6 151 PRO 7 152 ARG 8 153 GLU 9 154 GLU 10 155 MET 11 156 LEU 12 157 GLN 13 158 MET 14 159 GLN 15 160 ASP 16 161 ILE 17 162 VAL 18 163 LEU 19 164 ASN 20 165 GLU 21 166 VAL 22 167 LYS 23 168 LYS 24 169 LEU 25 170 ASP 26 171 PRO 27 172 GLU 28 173 TYR 29 174 ILE 30 175 ALA 31 176 THR 32 177 VAL 33 178 CYS 34 179 GLY 35 180 SER 36 181 PHE 37 182 ARG 38 183 ARG 39 184 GLY 40 185 ALA 41 186 GLU 42 187 SER 43 188 SER 44 189 GLY 45 190 ASP 46 191 MET 47 192 ASP 48 193 VAL 49 194 LEU 50 195 LEU 51 196 THR 52 197 HIS 53 198 PRO 54 199 ASN 55 200 PHE 56 201 THR 57 202 SER 58 203 GLU 59 204 SER 60 205 SER 61 206 LYS 62 207 GLN 63 208 PRO 64 209 LYS 65 210 LEU 66 211 LEU 67 212 HIS 68 213 ARG 69 214 VAL 70 215 VAL 71 216 GLU 72 217 GLN 73 218 LEU 74 219 GLN 75 220 LYS 76 221 VAL 77 222 ARG 78 223 PHE 79 224 ILE 80 225 THR 81 226 ASP 82 227 THR 83 228 LEU 84 229 SER 85 230 LYS 86 231 GLY 87 232 GLU 88 233 THR 89 234 LYS 90 235 PHE 91 236 MET 92 237 GLY 93 238 VAL 94 239 CYS 95 240 GLN 96 241 LEU 97 242 PRO 98 243 SER 99 244 GLU 100 245 ASN 101 246 ASP 102 247 GLU 103 248 ASN 104 249 GLU 105 250 TYR 106 251 PRO 107 252 HIS 108 253 ARG 109 254 ARG 110 255 ILE 111 256 ASP 112 257 ILE 113 258 ARG 114 259 LEU 115 260 ILE 116 261 PRO 117 262 LYS 118 263 ASP 119 264 GLN 120 265 TYR 121 266 TYR 122 267 CYS 123 268 GLY 124 269 VAL 125 270 LEU 126 271 TYR 127 272 PHE 128 273 THR 129 274 GLY 130 275 SER 131 276 ASP 132 277 ILE 133 278 PHE 134 279 ASN 135 280 LYS 136 281 ASN 137 282 MET 138 283 ARG 139 284 ALA 140 285 HIS 141 286 ALA 142 287 LEU 143 288 GLU 144 289 LYS 145 290 GLY 146 291 PHE 147 292 THR 148 293 ILE 149 294 ASN 150 295 GLU 151 296 TYR 152 297 THR 153 298 ILE 154 299 ARG 155 300 PRO 156 301 LEU 157 302 GLY 158 303 VAL 159 304 THR 160 305 GLY 161 306 VAL 162 307 ALA 163 308 GLY 164 309 GLU 165 310 PRO 166 311 LEU 167 312 PRO 168 313 VAL 169 314 ASP 170 315 SER 171 316 GLU 172 317 GLN 173 318 ASP 174 319 ILE 175 320 PHE 176 321 ASP 177 322 TYR 178 323 ILE 179 324 GLN 180 325 TRP 181 326 ARG 182 327 TYR 183 328 ARG 184 329 GLU 185 330 PRO 186 331 LYS 187 332 ASP 188 333 ARG 189 334 SER 190 335 GLU 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 18267 DNA_Polymerase_beta_polypeptide 98.95 335 100.00 100.00 1.13e-136 BMRB 7319 "pol beta" 98.95 335 100.00 100.00 1.13e-136 PDB 1BPB "Crystal Structure Of Rat Dna Polymerase Beta: Evidence For A Common Polymerase Mechanism" 98.95 248 100.00 100.00 1.97e-136 PDB 1BPD "Crystal Structure Of Rat Dna Polymerase Beta: Evidence For A Common Polymerase Mechanism" 98.95 335 100.00 100.00 1.13e-136 PDB 1BPE "Crystal Structure Of Rat Dna Polymerase Beta; Evidence For A Common Polymerase Mechanism" 98.95 335 100.00 100.00 1.34e-136 PDB 1HUO "Crystal Structure Of Dna Polymerase Beta Complexed With Dna And Cr-Tmppcp" 98.95 335 100.00 100.00 1.13e-136 PDB 1HUZ "Crystal Structure Of Dna Polymerase Complexed With Dna And Cr-Pcp" 98.95 335 100.00 100.00 1.13e-136 PDB 1JN3 "Fidelity Properties And Structure Of M282l Mutator Mutant Of Dna Polymerase: Subtle Structural Changes Influence The Mechanism " 98.95 251 99.47 100.00 5.19e-136 PDB 1NOM "Dna Polymerase Beta (pol B) (e.c.2.7.7.7), 31-kd Domain; Soaked In The Presence Of Mncl2 (5 Millimolar)" 98.95 248 100.00 100.00 1.97e-136 PDB 1RPL "2.3 Angstroms Crystal Structure Of The Catalytic Domain Of Dna Polymerase Beta" 98.95 251 100.00 100.00 1.51e-136 PDB 1ZQU "Dna Polymerase Beta (Pol B) (E.C.2.7.7.7), 31-Kd Domain; Soaked In The Presence Of Artificial Mother Liquor" 98.95 248 100.00 100.00 1.97e-136 PDB 1ZQV "Dna Polymerase Beta (Pol B) (E.C.2.7.7.7), 31-Kd Domain; Soaked In The Presence Of Cacl2 (150 Millimolar)" 98.95 248 100.00 100.00 1.97e-136 PDB 1ZQW "Dna Polymerase Beta (Pol B) (E.C.2.7.7.7), 31-Kd Domain; Soaked In The Presence Of Cscl (150 Millimolar)" 98.95 248 100.00 100.00 1.97e-136 PDB 1ZQX "Dna Polymerase Beta (Pol B) (E.C.2.7.7.7), 31-Kd Domain; Soaked In The Presence Of Kcl (150 Millimolar)" 98.95 248 100.00 100.00 1.97e-136 PDB 1ZQY "Dna Polymerase Beta (Pol B) (E.C.2.7.7.7), 31-Kd Domain; Soaked In The Presence Of Mgcl2 (50 Millimolar)" 98.95 248 100.00 100.00 1.97e-136 PDB 1ZQZ "Dna Polymerase Beta (Pol B) (E.C.2.7.7.7), 31-Kd Domain; Soaked In The Presence Of Mncl2 (50 Millimolar)" 98.95 248 100.00 100.00 1.97e-136 PDB 2BPC "Crystal Structure Of Rat Dna Polymerase Beta: Evidence For A Common Polymerase Mechanism" 98.95 248 100.00 100.00 1.97e-136 PDB 2BPF "Structures Of Ternary Complexes Of Rat Dna Polymerase Beta, A Dna Template-Primer, And Ddctp" 98.95 335 100.00 100.00 1.13e-136 PDB 2BPG "Structures Of Ternary Complexes Of Rat Dna Polymerase Beta, A Dna Template-Primer, And Ddctp" 98.95 335 100.00 100.00 1.13e-136 PDB 2VAN "Nucleotidyl Transfer Mechanism Of Mismatched Dntp Incorporation By Dna Polymerase B By Structural And Kinetic Analyses" 98.95 245 99.47 99.47 2.39e-135 PDB 3K75 "X-Ray Crystal Structure Of Reduced Xrcc1 Bound To Dna Pol Beta Catalytic Domain" 98.95 252 100.00 100.00 1.97e-136 PDB 3LQC "X-Ray Crystal Structure Of Oxidized Xrcc1 Bound To Dna Pol B Thumb Domain" 98.95 200 100.00 100.00 1.40e-136 PDB 3UXN "Crystal Structure Of Rat Dna Polymerase Beta, Wild Type Apoenzyme" 98.95 335 100.00 100.00 1.13e-136 PDB 3UXO "Crystal Structure Of Rat Dna Polymerase Beta Mutator I260q Apoenzyme" 98.95 335 99.47 99.47 1.48e-135 PDB 3UXP "Co-crystal Structure Of Rat Dna Polymerase Beta Mutator I260q: Enzyme- Dna-ddttp" 98.95 335 99.47 99.47 1.48e-135 PDB 3V72 "Crystal Structure Of Rat Dna Polymerase Beta Mutator E295k: Enzyme- Dsdna" 98.95 335 99.47 100.00 3.90e-136 PDB 3V7J "Co-crystal Structure Of Wild Type Rat Polymerase Beta: Enzyme-dna Binary Complex" 98.95 340 100.00 100.00 2.80e-136 PDB 3V7K "Co-crystal Structure Of K72e Variant Of Rat Polymerase Beta: Enzyme- Dna Binary Complex" 98.95 340 100.00 100.00 2.48e-136 PDB 3V7L "Apo Structure Of Rat Dna Polymerase Beta K72e Variant" 98.95 340 100.00 100.00 2.48e-136 GB AAA41900 "polymerase beta [Rattus norvegicus]" 98.95 318 99.47 99.47 6.29e-136 GB AAA41901 "DNA polymerase beta [Rattus norvegicus]" 98.95 335 99.47 99.47 1.15e-135 GB AAB00389 "high molecular weight DNA polymerase beta [Rattus norvegicus]" 98.95 335 99.47 99.47 1.15e-135 GB AAH98668 "Polymerase (DNA directed), beta [Rattus norvegicus]" 98.95 335 100.00 100.00 1.13e-136 GB EDM09009 "rCG43201 [Rattus norvegicus]" 98.95 335 100.00 100.00 1.13e-136 REF NP_058837 "DNA polymerase beta [Rattus norvegicus]" 98.95 335 100.00 100.00 1.13e-136 SP P06766 "RecName: Full=DNA polymerase beta [Rattus norvegicus]" 98.95 335 100.00 100.00 1.13e-136 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $B-Pol Rat 10116 Eukaryota Metazoa Rattus norvegicus 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 $B-Pol 'recombinant technology' 'E. coli' Escherichia coli BL21 plasmid pET-28a(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_perdeuterated _Saveframe_category sample _Sample_type solution _Details 'AEBSF is 4-(2-aminoethyl)-benzenesulfonyl fluoride.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $B-Pol 1.0 mM 0.6 1.3 ; U-98% 13C; U-99% 15N; U-97% 2H; except V g-methyls, L d-methyls, I d-methyl, and labile protons. ; phosphate 46 mM 40 50 . 'sodium chloride' 135 mM 130 140 . 'sodium azide' 0.002 % 0.015 0.025 . AEBSF 100 uM 90 110 . 'dithiothreitol (DTT)' 1 mM 0.95 1.05 . H2O 90 % . . . D2O 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task 'spectral processing' stop_ _Details ; Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. & Bax, A. (1995) J. Biomol NMR, 6, 277-293. ; save_ save_sbtools _Saveframe_category software _Name sbtools _Version . loop_ _Task 'NMR data processing script generation' stop_ _Details ; Web based program developed by Gryk, M.R. & Maciejewski, M.W. available from sbtools.uchc.edu. ; save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'spectral analysis' stop_ _Details ; Bartels, C., Xia, T., Billeter, M., Guntert, P., and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TROSY_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TROSY 1H-15N HSQC' _Sample_label . save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_2D_CT_1H-13C_HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CT 1H-13C HSQC' _Sample_label . save_ save_3D_TROSY_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _Sample_label . save_ save_3D_TROSY_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _Sample_label . save_ save_3D_TROSY_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _Sample_label . save_ save_2D_CCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CCH-TOCSY' _Sample_label . save_ save_3D_(HM)CMC(CM)HM_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HM)CMC(CM)HM' _Sample_label . save_ save_3D_15N,13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N,13C NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TROSY 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CT 1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCACB' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HNCO' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY HN(CA)CO' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (HM)CMC(CM)HM' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N,13C NOESY' _BMRB_pulse_sequence_accession_number . _Details 'The 2D CCH-TOCSY starts on 13C.' save_ ####################### # Sample conditions # ####################### save_perdeuterated_cond1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 na temperature 298 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_Shift_Set_1 _Saveframe_category assigned_chemical_shifts _Details ; Isotope induced shifts are uncorrected. No correction has been made for Bloch-Siegert effects. ; loop_ _Experiment_label '2D TROSY 1H-15N HSQC' '2D 1H-15N HSQC' '2D CT 1H-13C HSQC' '3D TROSY HNCACB' '3D TROSY HNCO' '3D TROSY HN(CA)CO' '2D CCH-TOCSY' '3D (HM)CMC(CM)HM' '3D 15N,13C NOESY' stop_ loop_ _Sample_label $perdeuterated stop_ _Sample_conditions_label $perdeuterated_cond1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'B-Pol palm-thumb' _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 . 4 ARG H H 8.45 0.01 1 2 . 4 ARG N N 120.45 0.14 1 3 . 4 ARG C C 175.53 0.06 1 4 . 4 ARG CA C 55.17 0.27 1 5 . 4 ARG CB C 30.09 0.27 1 6 . 5 ILE H H 9.42 0.01 1 7 . 5 ILE N N 123.01 0.14 1 8 . 5 ILE C C 174.56 0.06 1 9 . 5 ILE CA C 58.61 0.27 1 10 . 5 ILE CB C 38.31 0.27 1 11 . 5 ILE CG1 C 25.64 0.02 1 12 . 5 ILE CD1 C 13.24 0.02 1 13 . 5 ILE HD1 H 0.67 0.01 1 14 . 6 PRO C C 178.48 0.06 1 15 . 6 PRO CA C 62.51 0.27 1 16 . 6 PRO CB C 31.98 0.27 1 17 . 7 ARG H H 8.41 0.01 1 18 . 7 ARG N N 125.54 0.14 1 19 . 7 ARG C C 177.42 0.06 1 20 . 7 ARG CA C 60.14 0.27 1 21 . 7 ARG CB C 28.58 0.27 1 22 . 8 GLU H H 9.43 0.01 1 23 . 8 GLU N N 115.52 0.14 1 24 . 8 GLU C C 179.81 0.06 1 25 . 8 GLU CA C 59.86 0.27 1 26 . 8 GLU CB C 28.39 0.27 1 27 . 9 GLU H H 7.23 0.01 1 28 . 9 GLU N N 118.78 0.14 1 29 . 9 GLU C C 178.73 0.06 1 30 . 9 GLU CA C 58.49 0.27 1 31 . 9 GLU CB C 29.86 0.27 1 32 . 10 MET H H 7.88 0.01 1 33 . 10 MET N N 120.04 0.14 1 34 . 10 MET C C 179.25 0.06 1 35 . 10 MET CA C 56.59 0.27 1 36 . 10 MET CB C 30.98 0.27 1 37 . 11 LEU H H 8.85 0.01 1 38 . 11 LEU N N 119.05 0.14 1 39 . 11 LEU C C 179.80 0.06 1 40 . 11 LEU CA C 57.94 0.27 1 41 . 11 LEU CB C 41.05 0.27 1 42 . 11 LEU CG C 26.96 0.11 1 43 . 11 LEU CD1 C 25.83 0.02 2 44 . 11 LEU HD1 H 1 0.01 2 45 . 11 LEU CD2 C 23.22 0.02 2 46 . 11 LEU HD2 H 1.08 0.01 2 47 . 12 GLN H H 7.08 0.01 1 48 . 12 GLN N N 118.48 0.14 1 49 . 12 GLN C C 179.18 0.06 1 50 . 12 GLN CA C 58.51 0.27 1 51 . 12 GLN CB C 29.28 0.27 1 52 . 13 MET H H 8.39 0.01 1 53 . 13 MET N N 119.82 0.14 1 54 . 13 MET C C 176.93 0.06 1 55 . 13 MET CA C 59.07 0.27 1 56 . 13 MET CB C 33.91 0.27 1 57 . 14 GLN H H 8.88 0.01 1 58 . 14 GLN N N 118.36 0.14 1 59 . 14 GLN C C 176.08 0.06 1 60 . 14 GLN CA C 59.21 0.27 1 61 . 14 GLN CB C 28.74 0.27 1 62 . 15 ASP H H 7.60 0.01 1 63 . 15 ASP N N 117.84 0.14 1 64 . 15 ASP C C 178.18 0.06 1 65 . 15 ASP CA C 57.44 0.27 1 66 . 15 ASP CB C 40.08 0.27 1 67 . 16 ILE H H 7.17 0.01 1 68 . 16 ILE N N 118.41 0.14 1 69 . 16 ILE C C 177.66 0.06 1 70 . 16 ILE CA C 64.85 0.27 1 71 . 16 ILE CB C 37.23 0.27 1 72 . 16 ILE CG1 C 28.29 0.02 1 73 . 16 ILE CD1 C 14.19 0.02 1 74 . 16 ILE HD1 H 0.65 0.01 1 75 . 17 VAL H H 7.37 0.01 1 76 . 17 VAL N N 116.77 0.14 1 77 . 17 VAL C C 177.24 0.06 1 78 . 17 VAL CA C 66.84 0.27 1 79 . 17 VAL CB C 31.32 0.27 1 80 . 17 VAL CG1 C 20.47 0.02 2 81 . 17 VAL HG1 H 0.63 0.01 2 82 . 17 VAL CG2 C 23.78 0.02 2 83 . 17 VAL HG2 H 0.73 0.01 2 84 . 18 LEU H H 8.82 0.01 1 85 . 18 LEU N N 116.22 0.14 1 86 . 18 LEU C C 180.47 0.06 1 87 . 18 LEU CA C 58.16 0.27 1 88 . 18 LEU CB C 39.43 0.27 1 89 . 18 LEU CG C 27.63 0.11 1 90 . 18 LEU CD1 C 24.52 0.02 2 91 . 18 LEU HD1 H 0.9 0.01 2 92 . 18 LEU CD2 C 22.75 0.02 2 93 . 18 LEU HD2 H 0.85 0.01 2 94 . 19 ASN H H 8.20 0.01 1 95 . 19 ASN N N 116.22 0.14 1 96 . 19 ASN C C 178.41 0.06 1 97 . 19 ASN CA C 55.91 0.27 1 98 . 19 ASN CB C 37.73 0.27 1 99 . 20 GLU H H 8.18 0.01 1 100 . 20 GLU N N 117.27 0.14 1 101 . 20 GLU C C 179.91 0.06 1 102 . 20 GLU CA C 58.25 0.27 1 103 . 20 GLU CB C 27.97 0.27 1 104 . 21 VAL H H 8.23 0.01 1 105 . 21 VAL N N 117.84 0.14 1 106 . 21 VAL C C 176.66 0.06 1 107 . 21 VAL CA C 66.99 0.27 1 108 . 21 VAL CB C 30.78 0.27 1 109 . 21 VAL CG1 C 22.43 0.02 2 110 . 21 VAL HG1 H 0.66 0.01 2 111 . 21 VAL CG2 C 23.69 0.02 2 112 . 21 VAL HG2 H 0.76 0.01 2 113 . 22 LYS H H 7.60 0.01 1 114 . 22 LYS N N 117.71 0.14 1 115 . 22 LYS C C 178.52 0.06 1 116 . 22 LYS CA C 58.22 0.27 1 117 . 22 LYS CB C 31.28 0.27 1 118 . 23 LYS H H 7.32 0.01 1 119 . 23 LYS N N 115.81 0.14 1 120 . 23 LYS C C 178.85 0.06 1 121 . 23 LYS CA C 58.33 0.27 1 122 . 23 LYS CB C 31.75 0.27 1 123 . 24 LEU H H 7.36 0.01 1 124 . 24 LEU N N 118.89 0.14 1 125 . 24 LEU C C 178.09 0.06 1 126 . 24 LEU CA C 56.85 0.27 1 127 . 24 LEU CB C 42.55 0.27 1 128 . 24 LEU CG C 25.84 0.11 1 129 . 24 LEU CD1 C 23.55 0.02 2 130 . 24 LEU HD1 H 0.83 0.01 2 131 . 24 LEU CD2 C 26.11 0.02 2 132 . 24 LEU HD2 H 0.82 0.01 2 133 . 25 ASP H H 7.80 0.01 1 134 . 25 ASP N N 114.60 0.14 1 135 . 25 ASP C C 175.92 0.06 1 136 . 25 ASP CA C 52.20 0.27 1 137 . 25 ASP CB C 42.17 0.27 1 138 . 26 PRO C C 177.06 0.06 1 139 . 26 PRO CA C 63.67 0.27 1 140 . 26 PRO CB C 31.67 0.27 1 141 . 27 GLU H H 8.60 0.01 1 142 . 27 GLU N N 115.53 0.14 1 143 . 27 GLU C C 178.71 0.06 1 144 . 27 GLU CA C 55.98 0.27 1 145 . 27 GLU CB C 28.58 0.27 1 146 . 28 TYR H H 7.56 0.01 1 147 . 28 TYR N N 115.72 0.14 1 148 . 28 TYR C C 177.56 0.06 1 149 . 28 TYR CA C 59.87 0.27 1 150 . 28 TYR CB C 40.16 0.27 1 151 . 29 ILE H H 8.15 0.01 1 152 . 29 ILE N N 119.79 0.14 1 153 . 29 ILE C C 174.04 0.06 1 154 . 29 ILE CA C 61.00 0.27 1 155 . 29 ILE CB C 39.19 0.27 1 156 . 29 ILE CG1 C 26.08 0.02 1 157 . 29 ILE CD1 C 13.43 0.02 1 158 . 29 ILE HD1 H 0.67 0.01 1 159 . 30 ALA H H 8.63 0.01 1 160 . 30 ALA N N 127.72 0.14 1 161 . 30 ALA C C 175.64 0.06 1 162 . 30 ALA CA C 49.55 0.27 1 163 . 30 ALA CB C 21.25 0.27 1 164 . 31 THR H H 8.49 0.01 1 165 . 31 THR N N 115.10 0.14 1 166 . 31 THR C C 173.47 0.06 1 167 . 31 THR CA C 61.65 0.27 1 168 . 31 THR CB C 71.30 0.27 1 169 . 32 VAL H H 9.66 0.01 1 170 . 32 VAL N N 130.67 0.14 1 171 . 32 VAL C C 176.76 0.06 1 172 . 32 VAL CA C 62.55 0.27 1 173 . 32 VAL CB C 30.43 0.27 1 174 . 32 VAL CG1 C 21.68 0.02 2 175 . 32 VAL HG1 H 0.92 0.01 1 176 . 32 VAL CG2 C 23.5 0.02 2 177 . 32 VAL HG2 H 0.92 0.01 1 178 . 33 CYS H H 8.68 0.01 1 179 . 33 CYS N N 125.05 0.14 1 180 . 33 CYS C C 173.39 0.06 1 181 . 33 CYS CA C 58.99 0.27 1 182 . 33 CYS CB C 26.73 0.27 1 183 . 34 GLY H H 7.87 0.01 1 184 . 34 GLY N N 109.07 0.14 1 185 . 34 GLY C C 173.23 0.06 1 186 . 34 GLY CA C 44.94 0.27 1 187 . 35 SER C C 177.51 0.06 1 188 . 36 PHE H H 8.69 0.01 1 189 . 36 PHE N N 123.31 0.14 1 190 . 36 PHE C C 179.67 0.06 1 191 . 36 PHE CA C 60.68 0.27 1 192 . 36 PHE CB C 38.85 0.27 1 193 . 37 ARG H H 7.49 0.01 1 194 . 37 ARG N N 122.86 0.14 1 195 . 37 ARG C C 176.24 0.06 1 196 . 37 ARG CA C 58.38 0.27 1 197 . 37 ARG CB C 27.69 0.27 1 198 . 38 ARG H H 7.02 0.01 1 199 . 38 ARG N N 112.98 0.14 1 200 . 38 ARG C C 175.25 0.06 1 201 . 38 ARG CA C 55.78 0.27 1 202 . 38 ARG CB C 28.85 0.27 1 203 . 39 GLY H H 7.46 0.01 1 204 . 39 GLY N N 104.83 0.14 1 205 . 39 GLY C C 174.56 0.06 1 206 . 39 GLY CA C 44.63 0.27 1 207 . 40 ALA H H 7.50 0.01 1 208 . 40 ALA N N 121.39 0.14 1 209 . 40 ALA C C 179.02 0.06 1 210 . 40 ALA CA C 52.50 0.27 1 211 . 40 ALA CB C 19.63 0.27 1 212 . 41 GLU H H 9.00 0.01 1 213 . 41 GLU N N 120.53 0.14 1 214 . 41 GLU C C 175.88 0.06 1 215 . 41 GLU CA C 57.95 0.27 1 216 . 41 GLU CB C 29.01 0.27 1 217 . 42 SER H H 7.78 0.01 1 218 . 42 SER N N 113.05 0.14 1 219 . 42 SER C C 173.27 0.06 1 220 . 42 SER CA C 57.12 0.27 1 221 . 42 SER CB C 65.20 0.27 1 222 . 43 SER H H 8.96 0.01 1 223 . 43 SER N N 116.25 0.14 1 224 . 43 SER C C 173.37 0.06 1 225 . 43 SER CA C 58.07 0.27 1 226 . 43 SER CB C 67.64 0.27 1 227 . 44 GLY C C 173.32 0.06 1 228 . 44 GLY CA C 45.77 0.27 1 229 . 45 ASP H H 7.84 0.01 1 230 . 45 ASP N N 117.49 0.14 1 231 . 45 ASP C C 172.63 0.06 1 232 . 45 ASP CA C 52.57 0.27 1 233 . 45 ASP CB C 41.32 0.27 1 234 . 46 MET H H 8.11 0.01 1 235 . 46 MET N N 117.27 0.14 1 236 . 46 MET C C 172.84 0.06 1 237 . 46 MET CA C 54.75 0.27 1 238 . 46 MET CB C 33.91 0.27 1 239 . 47 ASP H H 9.32 0.01 1 240 . 47 ASP N N 129.13 0.14 1 241 . 47 ASP C C 174.53 0.06 1 242 . 47 ASP CA C 52.28 0.27 1 243 . 47 ASP CB C 41.28 0.27 1 244 . 48 VAL H H 9.00 0.01 1 245 . 48 VAL N N 123.64 0.14 1 246 . 48 VAL C C 174.07 0.06 1 247 . 48 VAL CA C 61.11 0.27 1 248 . 48 VAL CB C 33.06 0.27 1 249 . 48 VAL CG1 C 20.79 0.02 2 250 . 48 VAL HG1 H 0.7 0.01 2 251 . 48 VAL CG2 C 21.68 0.02 2 252 . 48 VAL HG2 H 0.95 0.01 2 253 . 49 LEU H H 8.96 0.01 1 254 . 49 LEU N N 129.10 0.14 1 255 . 49 LEU C C 176.06 0.06 1 256 . 49 LEU CA C 54.55 0.27 1 257 . 49 LEU CB C 41.70 0.27 1 258 . 49 LEU CG C 29.98 0.11 1 259 . 49 LEU CD1 C 24.99 0.02 2 260 . 49 LEU HD1 H 0.74 0.01 2 261 . 49 LEU CD2 C 23.55 0.02 2 262 . 49 LEU HD2 H 0.7 0.01 2 263 . 50 LEU H H 10.11 0.01 1 264 . 50 LEU N N 133.32 0.14 1 265 . 50 LEU C C 174.00 0.06 1 266 . 50 LEU CA C 53.03 0.27 1 267 . 50 LEU CB C 47.30 0.27 1 268 . 50 LEU CG C 26.81 0.11 1 269 . 50 LEU CD1 C 25.92 0.02 2 270 . 50 LEU HD1 H 0.7 0.01 2 271 . 50 LEU CD2 C 23.22 0.02 2 272 . 50 LEU HD2 H 0.67 0.01 2 273 . 51 THR H H 9.02 0.01 1 274 . 51 THR N N 117.94 0.14 1 275 . 51 THR C C 171.65 0.06 1 276 . 51 THR CA C 60.96 0.27 1 277 . 51 THR CB C 68.68 0.27 1 278 . 52 HIS H H 8.76 0.01 1 279 . 52 HIS N N 122.75 0.14 1 280 . 52 HIS C C 173.62 0.06 1 281 . 52 HIS CA C 54.90 0.27 1 282 . 52 HIS CB C 35.99 0.27 1 283 . 53 PRO C C 176.93 0.06 1 284 . 53 PRO CA C 64.15 0.27 1 285 . 54 ASN H H 11.01 0.01 1 286 . 54 ASN N N 118.12 0.14 1 287 . 54 ASN C C 175.18 0.06 1 288 . 54 ASN CA C 53.40 0.27 1 289 . 54 ASN CB C 37.54 0.27 1 290 . 55 PHE H H 8.49 0.01 1 291 . 55 PHE N N 122.58 0.14 1 292 . 55 PHE C C 172.65 0.06 1 293 . 55 PHE CA C 54.57 0.27 1 294 . 55 PHE CB C 39.19 0.27 1 295 . 56 THR H H 8.32 0.01 1 296 . 56 THR N N 116.12 0.14 1 297 . 56 THR C C 175.59 0.06 1 298 . 56 THR CA C 59.92 0.27 1 299 . 56 THR CB C 71.42 0.27 1 300 . 57 SER C C 175.10 0.06 1 301 . 57 SER CA C 60.84 0.27 1 302 . 58 GLU H H 8.08 0.01 1 303 . 58 GLU N N 119.25 0.14 1 304 . 58 GLU C C 176.60 0.06 1 305 . 58 GLU CA C 56.19 0.27 1 306 . 58 GLU CB C 29.43 0.27 1 307 . 59 SER H H 7.67 0.01 1 308 . 59 SER N N 116.09 0.14 1 309 . 59 SER CA C 57.91 0.27 1 310 . 59 SER CB C 64.01 0.27 1 311 . 60 SER C C 174.65 0.06 1 312 . 60 SER CA C 58.33 0.27 1 313 . 60 SER CB C 62.93 0.27 1 314 . 61 LYS H H 8.45 0.01 1 315 . 61 LYS N N 121.62 0.14 1 316 . 61 LYS C C 176.25 0.06 1 317 . 61 LYS CA C 56.61 0.27 1 318 . 61 LYS CB C 31.86 0.27 1 319 . 62 GLN H H 7.95 0.01 1 320 . 62 GLN N N 120.74 0.14 1 321 . 62 GLN C C 173.25 0.06 1 322 . 62 GLN CA C 52.82 0.27 1 323 . 62 GLN CB C 29.28 0.27 1 324 . 64 LYS C C 177.92 0.06 1 325 . 64 LYS CA C 58.10 0.27 1 326 . 64 LYS CB C 30.90 0.27 1 327 . 65 LEU H H 7.55 0.01 1 328 . 65 LEU N N 116.21 0.14 1 329 . 65 LEU C C 180.41 0.06 1 330 . 65 LEU CA C 56.76 0.27 1 331 . 65 LEU CB C 42.36 0.27 1 332 . 65 LEU CG C 26.22 0.11 1 333 . 65 LEU CD1 C 26.67 0.02 2 334 . 65 LEU HD1 H 0.63 0.01 2 335 . 65 LEU CD2 C 21.31 0.02 2 336 . 65 LEU HD2 H 0.3 0.01 2 337 . 66 LEU H H 7.71 0.01 1 338 . 66 LEU N N 117.98 0.14 1 339 . 66 LEU C C 177.89 0.06 1 340 . 66 LEU CA C 55.95 0.27 1 341 . 66 LEU CB C 41.12 0.27 1 342 . 67 HIS H H 8.39 0.01 1 343 . 67 HIS N N 119.67 0.14 1 344 . 67 HIS C C 177.23 0.06 1 345 . 67 HIS CA C 58.91 0.27 1 346 . 67 HIS CB C 30.40 0.27 1 347 . 68 ARG H H 8.48 0.01 1 348 . 68 ARG N N 115.51 0.14 1 349 . 68 ARG C C 179.16 0.06 1 350 . 68 ARG CA C 58.92 0.27 1 351 . 68 ARG CB C 29.78 0.27 1 352 . 69 VAL H H 6.67 0.01 1 353 . 69 VAL N N 118.34 0.14 1 354 . 69 VAL C C 176.75 0.06 1 355 . 69 VAL CA C 65.75 0.27 1 356 . 69 VAL CB C 31.13 0.27 1 357 . 69 VAL CG1 C 20.56 0.02 2 358 . 69 VAL HG1 H 0.52 0.01 2 359 . 69 VAL CG2 C 22.71 0.02 2 360 . 69 VAL HG2 H 0.6 0.01 2 361 . 70 VAL H H 7.51 0.01 1 362 . 70 VAL N N 119.21 0.14 1 363 . 70 VAL C C 177.36 0.06 1 364 . 70 VAL CA C 66.34 0.27 1 365 . 70 VAL CB C 30.94 0.27 1 366 . 70 VAL CG1 C 20.37 0.02 2 367 . 70 VAL HG1 H 0.14 0.01 2 368 . 70 VAL CG2 C 22.05 0.02 2 369 . 70 VAL HG2 H 0.29 0.01 2 370 . 71 GLU H H 8.50 0.01 1 371 . 71 GLU N N 116.80 0.14 1 372 . 71 GLU C C 179.72 0.06 1 373 . 71 GLU CA C 58.34 0.27 1 374 . 71 GLU CB C 28.51 0.27 1 375 . 72 GLN H H 7.58 0.01 1 376 . 72 GLN N N 120.24 0.14 1 377 . 72 GLN C C 177.75 0.06 1 378 . 72 GLN CA C 57.59 0.27 1 379 . 72 GLN CB C 26.92 0.27 1 380 . 73 LEU H H 8.02 0.01 1 381 . 73 LEU N N 116.64 0.14 1 382 . 73 LEU C C 180.36 0.06 1 383 . 73 LEU CA C 56.52 0.27 1 384 . 73 LEU CB C 40.20 0.27 1 385 . 74 GLN H H 8.46 0.01 1 386 . 74 GLN N N 121.23 0.14 1 387 . 74 GLN C C 179.99 0.06 1 388 . 74 GLN CA C 58.47 0.27 1 389 . 74 GLN CB C 28.12 0.27 1 390 . 75 LYS H H 8.36 0.01 1 391 . 75 LYS N N 125.20 0.14 1 392 . 75 LYS C C 179.23 0.06 1 393 . 75 LYS CA C 59.64 0.27 1 394 . 75 LYS CB C 31.09 0.27 1 395 . 76 VAL H H 7.44 0.01 1 396 . 76 VAL N N 108.08 0.14 1 397 . 76 VAL C C 175.04 0.06 1 398 . 76 VAL CA C 60.84 0.27 1 399 . 76 VAL CB C 29.82 0.27 1 400 . 76 VAL CG1 C 18.51 0.02 2 401 . 76 VAL HG1 H 0.99 0.01 2 402 . 76 VAL CG2 C 20.75 0.02 2 403 . 76 VAL HG2 H 0.94 0.01 2 404 . 77 ARG H H 7.82 0.01 1 405 . 77 ARG N N 114.73 0.14 1 406 . 77 ARG C C 174.15 0.06 1 407 . 77 ARG CA C 56.86 0.27 1 408 . 77 ARG CB C 25.30 0.27 1 409 . 78 PHE H H 7.89 0.01 1 410 . 78 PHE N N 117.13 0.14 1 411 . 78 PHE C C 175.87 0.06 1 412 . 78 PHE CA C 58.63 0.27 1 413 . 78 PHE CB C 39.77 0.27 1 414 . 79 ILE H H 6.74 0.01 1 415 . 79 ILE N N 114.68 0.14 1 416 . 79 ILE C C 176.31 0.06 1 417 . 79 ILE CA C 60.28 0.27 1 418 . 79 ILE CB C 37.81 0.27 1 419 . 79 ILE CG1 C 28.07 0.02 1 420 . 79 ILE CD1 C 14.06 0.02 1 421 . 79 ILE HD1 H 0.63 0.01 1 422 . 80 THR H H 9.01 0.01 1 423 . 80 THR N N 119.66 0.14 1 424 . 80 THR C C 174.92 0.06 1 425 . 80 THR CA C 61.82 0.27 1 426 . 80 THR CB C 68.18 0.27 1 427 . 81 ASP H H 7.66 0.01 1 428 . 81 ASP N N 119.05 0.14 1 429 . 81 ASP C C 174.72 0.06 1 430 . 81 ASP CA C 53.69 0.27 1 431 . 81 ASP CB C 43.63 0.27 1 432 . 82 THR H H 8.79 0.01 1 433 . 82 THR N N 117.92 0.14 1 434 . 82 THR C C 173.25 0.06 1 435 . 82 THR CA C 62.44 0.27 1 436 . 82 THR CB C 70.61 0.27 1 437 . 83 LEU H H 8.81 0.01 1 438 . 83 LEU N N 126.68 0.14 1 439 . 83 LEU C C 177.12 0.06 1 440 . 83 LEU CA C 55.67 0.27 1 441 . 83 LEU CB C 40.85 0.27 1 442 . 83 LEU CG C 27.41 0.11 1 443 . 83 LEU CD1 C 24.66 0.02 2 444 . 83 LEU HD1 H 0.63 0.01 2 445 . 83 LEU CD2 C 22.47 0.02 2 446 . 83 LEU HD2 H 0.71 0.01 2 447 . 84 SER H H 7.95 0.01 1 448 . 84 SER N N 111.67 0.14 1 449 . 84 SER C C 172.14 0.06 1 450 . 84 SER CA C 57.49 0.27 1 451 . 84 SER CB C 63.62 0.27 1 452 . 85 LYS H H 8.95 0.01 1 453 . 85 LYS N N 128.26 0.14 1 454 . 85 LYS C C 174.55 0.06 1 455 . 85 LYS CA C 55.53 0.27 1 456 . 85 LYS CB C 33.37 0.27 1 457 . 86 GLY H H 8.11 0.01 1 458 . 86 GLY N N 113.74 0.14 1 459 . 86 GLY C C 173.52 0.06 1 460 . 86 GLY CA C 43.85 0.27 1 461 . 87 GLU H H 8.73 0.01 1 462 . 87 GLU N N 118.79 0.14 1 463 . 87 GLU C C 177.17 0.06 1 464 . 87 GLU CA C 59.06 0.27 1 465 . 87 GLU CB C 29.84 0.27 1 466 . 88 THR H H 8.30 0.01 1 467 . 88 THR N N 101.65 0.14 1 468 . 88 THR C C 174.05 0.06 1 469 . 88 THR CA C 60.62 0.27 1 470 . 88 THR CB C 69.84 0.27 1 471 . 89 LYS H H 7.26 0.01 1 472 . 89 LYS N N 122.93 0.14 1 473 . 89 LYS C C 173.81 0.06 1 474 . 89 LYS CA C 55.75 0.27 1 475 . 89 LYS CB C 34.76 0.27 1 476 . 90 PHE H H 9.56 0.01 1 477 . 90 PHE N N 128.55 0.14 1 478 . 90 PHE C C 173.21 0.06 1 479 . 90 PHE CA C 55.76 0.27 1 480 . 90 PHE CB C 42.13 0.27 1 481 . 91 MET H H 8.30 0.01 1 482 . 91 MET N N 124.91 0.14 1 483 . 91 MET C C 175.09 0.06 1 484 . 91 MET CA C 53.73 0.27 1 485 . 91 MET CB C 35.53 0.27 1 486 . 92 GLY H H 9.16 0.01 1 487 . 92 GLY N N 111.19 0.14 1 488 . 92 GLY C C 170.75 0.06 1 489 . 92 GLY CA C 45.76 0.27 1 490 . 93 VAL H H 8.53 0.01 1 491 . 93 VAL N N 123.85 0.14 1 492 . 93 VAL C C 174.13 0.06 1 493 . 93 VAL CA C 59.92 0.27 1 494 . 93 VAL CB C 34.80 0.27 1 495 . 93 VAL CG1 C 22.66 0.02 2 496 . 93 VAL HG1 H 1 0.01 2 497 . 93 VAL CG2 C 20.68 0.02 2 498 . 93 VAL HG2 H 0.73 0.01 2 499 . 94 CYS H H 9.74 0.01 1 500 . 94 CYS N N 122.16 0.14 1 501 . 94 CYS C C 171.60 0.06 1 502 . 94 CYS CA C 54.13 0.27 1 503 . 94 CYS CB C 32.67 0.27 1 504 . 95 GLN H H 8.15 0.01 1 505 . 95 GLN N N 118.40 0.14 1 506 . 95 GLN C C 174.44 0.06 1 507 . 95 GLN CA C 54.25 0.27 1 508 . 95 GLN CB C 32.56 0.27 1 509 . 96 LEU H H 9.10 0.01 1 510 . 96 LEU N N 128.06 0.14 1 511 . 96 LEU C C 173.98 0.06 1 512 . 96 LEU CA C 52.82 0.27 1 513 . 96 LEU CB C 40.62 0.27 1 514 . 96 LEU CG C 25.91 0.11 1 515 . 96 LEU CD1 C 24.15 0.02 2 516 . 96 LEU HD1 H 0.62 0.01 2 517 . 96 LEU CD2 C 24.99 0.02 2 518 . 96 LEU HD2 H 0.46 0.01 2 519 . 97 PRO C C 176.60 0.06 1 520 . 97 PRO CA C 62.26 0.27 1 521 . 97 PRO CB C 31.36 0.27 1 522 . 98 SER H H 8.40 0.01 1 523 . 98 SER N N 114.25 0.14 1 524 . 98 SER C C 175.18 0.06 1 525 . 98 SER CA C 56.63 0.27 1 526 . 98 SER CB C 64.39 0.27 1 527 . 99 GLU H H 8.93 0.01 1 528 . 99 GLU N N 123.69 0.14 1 529 . 99 GLU C C 176.50 0.06 1 530 . 99 GLU CA C 56.34 0.27 1 531 . 99 GLU CB C 29.59 0.27 1 532 . 100 ASN H H 8.45 0.01 1 533 . 100 ASN N N 117.37 0.14 1 534 . 100 ASN C C 174.87 0.06 1 535 . 100 ASN CA C 52.95 0.27 1 536 . 100 ASN CB C 38.81 0.27 1 537 . 101 ASP H H 8.40 0.01 1 538 . 101 ASP N N 118.92 0.14 1 539 . 101 ASP C C 176.26 0.06 1 540 . 101 ASP CA C 55.02 0.27 1 541 . 101 ASP CB C 40.20 0.27 1 542 . 102 GLU H H 8.12 0.01 1 543 . 102 GLU N N 118.49 0.14 1 544 . 102 GLU C C 175.98 0.06 1 545 . 102 GLU CA C 56.21 0.27 1 546 . 102 GLU CB C 29.59 0.27 1 547 . 103 ASN H H 8.18 0.01 1 548 . 103 ASN N N 118.91 0.14 1 549 . 103 ASN C C 174.46 0.06 1 550 . 103 ASN CA C 52.58 0.27 1 551 . 103 ASN CB C 39.08 0.27 1 552 . 104 GLU H H 8.38 0.01 1 553 . 104 GLU N N 122.03 0.14 1 554 . 104 GLU C C 176.68 0.06 1 555 . 104 GLU CA C 55.81 0.27 1 556 . 104 GLU CB C 29.89 0.27 1 557 . 105 TYR H H 8.98 0.01 1 558 . 105 TYR N N 123.66 0.14 1 559 . 105 TYR C C 174.40 0.06 1 560 . 105 TYR CA C 57.14 0.27 1 561 . 105 TYR CB C 37.46 0.27 1 562 . 106 PRO C C 175.96 0.06 1 563 . 106 PRO CA C 61.76 0.27 1 564 . 106 PRO CB C 32.06 0.27 1 565 . 107 HIS H H 8.35 0.01 1 566 . 107 HIS N N 118.64 0.14 1 567 . 107 HIS C C 176.11 0.06 1 568 . 107 HIS CA C 56.81 0.27 1 569 . 107 HIS CB C 29.39 0.27 1 570 . 108 ARG H H 9.63 0.01 1 571 . 108 ARG N N 121.59 0.14 1 572 . 108 ARG C C 175.66 0.06 1 573 . 108 ARG CA C 51.85 0.27 1 574 . 108 ARG CB C 32.02 0.27 1 575 . 109 ARG H H 8.71 0.01 1 576 . 109 ARG N N 122.15 0.14 1 577 . 109 ARG C C 174.13 0.06 1 578 . 109 ARG CA C 55.46 0.27 1 579 . 109 ARG CB C 28.89 0.27 1 580 . 110 ILE H H 7.96 0.01 1 581 . 110 ILE N N 118.55 0.14 1 582 . 110 ILE C C 171.92 0.06 1 583 . 110 ILE CA C 57.13 0.27 1 584 . 110 ILE CB C 41.05 0.27 1 585 . 110 ILE CG1 C 28.5 0.02 1 586 . 110 ILE CD1 C 14.22 0.02 1 587 . 110 ILE HD1 H 0.89 0.01 1 588 . 111 ASP H H 8.88 0.01 1 589 . 111 ASP N N 128.02 0.14 1 590 . 111 ASP C C 175.44 0.06 1 591 . 111 ASP CA C 51.79 0.27 1 592 . 111 ASP CB C 42.59 0.27 1 593 . 112 ILE H H 9.27 0.01 1 594 . 112 ILE N N 118.63 0.14 1 595 . 112 ILE C C 174.53 0.06 1 596 . 112 ILE CA C 59.71 0.27 1 597 . 112 ILE CB C 40.35 0.27 1 598 . 112 ILE CG1 C 26.3 0.02 1 599 . 112 ILE CD1 C 13.1 0.02 1 600 . 112 ILE HD1 H 0.53 0.01 1 601 . 113 ARG H H 8.83 0.01 1 602 . 113 ARG N N 125.76 0.14 1 603 . 113 ARG C C 173.78 0.06 1 604 . 113 ARG CA C 53.95 0.27 1 605 . 113 ARG CB C 32.44 0.27 1 606 . 114 LEU H H 8.98 0.01 1 607 . 114 LEU N N 126.43 0.14 1 608 . 114 LEU C C 174.69 0.06 1 609 . 114 LEU CA C 53.51 0.27 1 610 . 114 LEU CB C 43.56 0.27 1 611 . 114 LEU CG C 26.89 0.11 1 612 . 114 LEU CD1 C 22.89 0.02 2 613 . 114 LEU HD1 H 0.78 0.01 2 614 . 114 LEU CD2 C 27.32 0.02 2 615 . 114 LEU HD2 H 0.43 0.01 2 616 . 115 ILE H H 9.19 0.01 1 617 . 115 ILE N N 128.54 0.14 1 618 . 115 ILE C C 173.15 0.06 1 619 . 115 ILE CA C 56.83 0.27 1 620 . 115 ILE CB C 41.70 0.27 1 621 . 115 ILE CG1 C 26.58 0.02 1 622 . 115 ILE CD1 C 13.12 0.02 1 623 . 115 ILE HD1 H 0.99 0.01 1 624 . 116 PRO C C 178.56 0.06 1 625 . 116 PRO CA C 62.23 0.27 1 626 . 117 LYS H H 9.43 0.01 1 627 . 117 LYS N N 125.85 0.14 1 628 . 117 LYS C C 178.48 0.06 1 629 . 117 LYS CA C 59.97 0.27 1 630 . 117 LYS CB C 30.98 0.27 1 631 . 118 ASP H H 9.34 0.01 1 632 . 118 ASP N N 112.69 0.14 1 633 . 118 ASP C C 176.63 0.06 1 634 . 118 ASP CA C 54.35 0.27 1 635 . 118 ASP CB C 38.38 0.27 1 636 . 119 GLN H H 8.00 0.01 1 637 . 119 GLN N N 118.23 0.14 1 638 . 119 GLN C C 176.86 0.06 1 639 . 119 GLN CA C 55.49 0.27 1 640 . 119 GLN CB C 29.01 0.27 1 641 . 120 TYR H H 7.52 0.01 1 642 . 120 TYR N N 120.85 0.14 1 643 . 120 TYR C C 176.41 0.06 1 644 . 120 TYR CA C 61.99 0.27 1 645 . 120 TYR CB C 39.19 0.27 1 646 . 121 TYR H H 7.72 0.01 1 647 . 121 TYR N N 115.06 0.14 1 648 . 121 TYR C C 178.25 0.06 1 649 . 121 TYR CA C 63.61 0.27 1 650 . 121 TYR CB C 36.45 0.27 1 651 . 122 CYS H H 9.24 0.01 1 652 . 122 CYS N N 120.20 0.14 1 653 . 122 CYS C C 177.89 0.06 1 654 . 122 CYS CA C 64.52 0.27 1 655 . 122 CYS CB C 25.88 0.27 1 656 . 123 GLY H H 7.64 0.01 1 657 . 123 GLY N N 110.72 0.14 1 658 . 123 GLY C C 174.79 0.06 1 659 . 123 GLY CA C 47.48 0.27 1 660 . 124 VAL H H 8.85 0.01 1 661 . 124 VAL N N 124.21 0.14 1 662 . 124 VAL C C 179.15 0.06 1 663 . 124 VAL CA C 65.83 0.27 1 664 . 124 VAL CB C 31.79 0.27 1 665 . 124 VAL CG1 C 22.24 0.02 2 666 . 124 VAL HG1 H 0.16 0.01 2 667 . 124 VAL CG2 C 21.03 0.02 2 668 . 124 VAL HG2 H 0.91 0.01 2 669 . 125 LEU H H 8.44 0.01 1 670 . 125 LEU N N 123.30 0.14 1 671 . 125 LEU C C 180.16 0.06 1 672 . 125 LEU CA C 58.81 0.27 1 673 . 125 LEU CB C 42.28 0.27 1 674 . 125 LEU CG C 26.4 0.11 1 675 . 125 LEU CD1 C 25.69 0.02 2 676 . 125 LEU HD1 H 1.09 0.01 2 677 . 125 LEU CD2 C 26.9 0.02 2 678 . 125 LEU HD2 H 1.05 0.01 2 679 . 126 TYR H H 8.17 0.01 1 680 . 126 TYR N N 120.75 0.14 1 681 . 126 TYR C C 179.53 0.06 1 682 . 126 TYR CA C 61.25 0.27 1 683 . 126 TYR CB C 37.84 0.27 1 684 . 127 PHE H H 9.22 0.01 1 685 . 127 PHE N N 113.68 0.14 1 686 . 127 PHE C C 178.38 0.06 1 687 . 127 PHE CA C 60.87 0.27 1 688 . 127 PHE CB C 36.57 0.27 1 689 . 128 THR H H 7.93 0.01 1 690 . 128 THR N N 119.82 0.14 1 691 . 128 THR C C 172.79 0.06 1 692 . 128 THR CA C 66.39 0.27 1 693 . 128 THR CB C 67.87 0.27 1 694 . 129 GLY H H 7.06 0.01 1 695 . 129 GLY N N 107.05 0.14 1 696 . 129 GLY C C 175.24 0.06 1 697 . 129 GLY CA C 42.84 0.27 1 698 . 130 SER H H 7.48 0.01 1 699 . 130 SER N N 115.22 0.14 1 700 . 130 SER CA C 59.15 0.27 1 701 . 130 SER CB C 66.02 0.27 1 702 . 131 ASP C C 178.93 0.06 1 703 . 131 ASP CA C 57.47 0.27 1 704 . 131 ASP CB C 40.01 0.27 1 705 . 132 ILE H H 7.99 0.01 1 706 . 132 ILE N N 120.60 0.14 1 707 . 132 ILE C C 177.55 0.06 1 708 . 132 ILE CA C 63.38 0.27 1 709 . 132 ILE CB C 36.88 0.27 1 710 . 132 ILE CG1 C 27.75 0.02 1 711 . 132 ILE CD1 C 11.93 0.02 1 712 . 132 ILE HD1 H 0.91 0.01 1 713 . 133 PHE H H 7.73 0.01 1 714 . 133 PHE N N 122.73 0.14 1 715 . 133 PHE C C 177.13 0.06 1 716 . 133 PHE CA C 61.63 0.27 1 717 . 133 PHE CB C 38.15 0.27 1 718 . 134 ASN H H 8.59 0.01 1 719 . 134 ASN N N 117.35 0.14 1 720 . 134 ASN C C 178.38 0.06 1 721 . 134 ASN CA C 55.50 0.27 1 722 . 134 ASN CB C 37.34 0.27 1 723 . 135 LYS H H 7.74 0.01 1 724 . 135 LYS N N 120.61 0.14 1 725 . 135 LYS C C 179.55 0.06 1 726 . 135 LYS CA C 59.47 0.27 1 727 . 135 LYS CB C 31.36 0.27 1 728 . 136 ASN H H 8.47 0.01 1 729 . 136 ASN N N 120.77 0.14 1 730 . 136 ASN C C 178.55 0.06 1 731 . 136 ASN CA C 55.19 0.27 1 732 . 136 ASN CB C 36.76 0.27 1 733 . 137 MET H H 9.18 0.01 1 734 . 137 MET N N 124.02 0.14 1 735 . 137 MET C C 177.79 0.06 1 736 . 137 MET CA C 58.83 0.27 1 737 . 137 MET CB C 30.13 0.27 1 738 . 138 ARG H H 8.20 0.01 1 739 . 138 ARG N N 118.12 0.14 1 740 . 138 ARG C C 179.16 0.06 1 741 . 138 ARG CA C 59.59 0.27 1 742 . 138 ARG CB C 29.32 0.27 1 743 . 139 ALA H H 7.84 0.01 1 744 . 139 ALA N N 121.38 0.14 1 745 . 139 ALA C C 180.48 0.06 1 746 . 139 ALA CA C 54.60 0.27 1 747 . 139 ALA CB C 17.31 0.27 1 748 . 140 HIS H H 7.78 0.01 1 749 . 140 HIS N N 118.92 0.14 1 750 . 140 HIS C C 176.91 0.06 1 751 . 140 HIS CA C 59.22 0.27 1 752 . 140 HIS CB C 28.89 0.27 1 753 . 141 ALA H H 8.45 0.01 1 754 . 141 ALA N N 119.25 0.14 1 755 . 141 ALA C C 179.65 0.06 1 756 . 141 ALA CA C 55.17 0.27 1 757 . 141 ALA CB C 17.43 0.27 1 758 . 142 LEU H H 7.80 0.01 1 759 . 142 LEU N N 118.69 0.14 1 760 . 142 LEU C C 181.64 0.06 1 761 . 142 LEU CA C 57.77 0.27 1 762 . 142 LEU CB C 41.28 0.27 1 763 . 142 LEU CG C 26.52 0.11 1 764 . 142 LEU CD1 C 24.06 0.02 2 765 . 142 LEU HD1 H 0.9 0.01 2 766 . 142 LEU CD2 C 24.62 0.02 2 767 . 142 LEU HD2 H 0.87 0.01 2 768 . 143 GLU H H 7.44 0.01 1 769 . 143 GLU N N 120.00 0.14 1 770 . 143 GLU C C 178.41 0.06 1 771 . 143 GLU CA C 58.56 0.27 1 772 . 143 GLU CB C 28.54 0.27 1 773 . 144 LYS H H 7.43 0.01 1 774 . 144 LYS N N 115.72 0.14 1 775 . 144 LYS C C 175.67 0.06 1 776 . 144 LYS CA C 53.52 0.27 1 777 . 144 LYS CB C 30.78 0.27 1 778 . 145 GLY H H 7.81 0.01 1 779 . 145 GLY N N 105.96 0.14 1 780 . 145 GLY C C 173.53 0.06 1 781 . 145 GLY CA C 45.26 0.27 1 782 . 146 PHE H H 8.63 0.01 1 783 . 146 PHE N N 119.82 0.14 1 784 . 146 PHE C C 173.59 0.06 1 785 . 146 PHE CA C 56.38 0.27 1 786 . 146 PHE CB C 42.63 0.27 1 787 . 147 THR H H 9.05 0.01 1 788 . 147 THR N N 112.38 0.14 1 789 . 147 THR C C 173.45 0.06 1 790 . 147 THR CA C 58.07 0.27 1 791 . 147 THR CB C 69.76 0.27 1 792 . 148 ILE H H 8.13 0.01 1 793 . 148 ILE N N 129.52 0.14 1 794 . 148 ILE C C 174.36 0.06 1 795 . 148 ILE CA C 59.41 0.27 1 796 . 148 ILE CB C 40.97 0.27 1 797 . 148 ILE CG1 C 27.4 0.02 1 798 . 148 ILE CD1 C 14.96 0.02 1 799 . 148 ILE HD1 H 0.61 0.01 1 800 . 149 ASN H H 8.57 0.01 1 801 . 149 ASN N N 126.75 0.14 1 802 . 149 ASN C C 173.85 0.06 1 803 . 149 ASN CA C 50.75 0.27 1 804 . 149 ASN CB C 38.00 0.27 1 805 . 150 GLU H H 9.21 0.01 1 806 . 150 GLU N N 116.32 0.14 1 807 . 150 GLU C C 173.48 0.06 1 808 . 150 GLU CA C 58.12 0.27 1 809 . 150 GLU CB C 27.50 0.27 1 810 . 151 TYR H H 7.69 0.01 1 811 . 151 TYR N N 112.75 0.14 1 812 . 151 TYR C C 176.35 0.06 1 813 . 151 TYR CA C 57.86 0.27 1 814 . 151 TYR CB C 41.36 0.27 1 815 . 152 THR H H 8.35 0.01 1 816 . 152 THR N N 107.15 0.14 1 817 . 152 THR C C 172.80 0.06 1 818 . 152 THR CA C 60.19 0.27 1 819 . 152 THR CB C 74.89 0.27 1 820 . 153 ILE H H 9.51 0.01 1 821 . 153 ILE N N 118.64 0.14 1 822 . 153 ILE C C 173.03 0.06 1 823 . 153 ILE CA C 58.65 0.27 1 824 . 153 ILE CB C 40.01 0.27 1 825 . 153 ILE CG1 C 28.51 0.02 1 826 . 153 ILE CD1 C 13.56 0.02 1 827 . 153 ILE HD1 H 0.38 0.01 1 828 . 154 ARG H H 8.39 0.01 1 829 . 154 ARG N N 124.21 0.14 1 830 . 154 ARG C C 173.32 0.06 1 831 . 154 ARG CA C 51.35 0.27 1 832 . 154 ARG CB C 32.52 0.27 1 833 . 155 PRO C C 175.81 0.06 1 834 . 155 PRO CA C 61.66 0.27 1 835 . 155 PRO CB C 30.98 0.27 1 836 . 156 LEU H H 8.06 0.01 1 837 . 156 LEU N N 122.30 0.14 1 838 . 156 LEU C C 177.34 0.06 1 839 . 156 LEU CA C 53.45 0.27 1 840 . 156 LEU CB C 42.71 0.27 1 841 . 156 LEU CG C 26.14 0.11 1 842 . 156 LEU CD1 C 24.8 0.02 2 843 . 156 LEU HD1 H 0.64 0.01 2 844 . 156 LEU CD2 C 23.61 0.02 2 845 . 156 LEU HD2 H 0.59 0.01 2 846 . 157 GLY H H 8.14 0.01 1 847 . 157 GLY N N 109.92 0.14 1 848 . 157 GLY C C 176.08 0.06 1 849 . 157 GLY CA C 43.85 0.27 1 850 . 158 VAL H H 8.52 0.01 1 851 . 158 VAL N N 118.16 0.14 1 852 . 158 VAL C C 177.61 0.06 1 853 . 158 VAL CA C 64.10 0.27 1 854 . 158 VAL CB C 31.44 0.27 1 855 . 158 VAL CG1 C 20.19 0.02 2 856 . 158 VAL HG1 H 1 0.01 2 857 . 158 VAL CG2 C 20.79 0.02 2 858 . 158 VAL HG2 H 1.01 0.01 2 859 . 159 THR H H 8.04 0.01 1 860 . 159 THR N N 109.49 0.14 1 861 . 159 THR C C 175.36 0.06 1 862 . 159 THR CA C 60.87 0.27 1 863 . 159 THR CB C 68.60 0.27 1 864 . 160 GLY H H 7.98 0.01 1 865 . 160 GLY N N 108.87 0.14 1 866 . 160 GLY C C 173.38 0.06 1 867 . 160 GLY CA C 45.08 0.27 1 868 . 161 VAL H H 7.49 0.01 1 869 . 161 VAL N N 119.86 0.14 1 870 . 161 VAL C C 176.25 0.06 1 871 . 161 VAL CA C 61.35 0.27 1 872 . 161 VAL CB C 32.02 0.27 1 873 . 161 VAL CG1 C 20.77 0.02 2 874 . 161 VAL HG1 H 0.79 0.01 2 875 . 161 VAL CG2 C 20.79 0.02 2 876 . 161 VAL HG2 H 0.85 0.01 2 877 . 162 ALA H H 8.73 0.01 1 878 . 162 ALA N N 131.66 0.14 1 879 . 162 ALA C C 178.29 0.06 1 880 . 162 ALA CA C 51.77 0.27 1 881 . 162 ALA CB C 18.43 0.27 1 882 . 163 GLY H H 8.66 0.01 1 883 . 163 GLY N N 108.93 0.14 1 884 . 163 GLY C C 172.71 0.06 1 885 . 163 GLY CA C 43.05 0.27 1 886 . 164 GLU H H 8.25 0.01 1 887 . 164 GLU N N 119.61 0.14 1 888 . 164 GLU C C 174.47 0.06 1 889 . 164 GLU CA C 54.59 0.27 1 890 . 164 GLU CB C 28.04 0.27 1 891 . 165 PRO C C 177.18 0.06 1 892 . 165 PRO CA C 62.92 0.27 1 893 . 165 PRO CB C 31.67 0.27 1 894 . 166 LEU H H 8.44 0.01 1 895 . 166 LEU N N 125.54 0.14 1 896 . 166 LEU C C 175.59 0.06 1 897 . 166 LEU CA C 52.35 0.27 1 898 . 166 LEU CB C 40.01 0.27 1 899 . 166 LEU CG C 26.73 0.11 1 900 . 166 LEU CD1 C 22.71 0.02 2 901 . 166 LEU HD1 H 0.87 0.01 2 902 . 166 LEU CD2 C 24.52 0.02 2 903 . 166 LEU HD2 H 0.2 0.01 2 904 . 167 PRO C C 177.82 0.06 1 905 . 167 PRO CA C 62.89 0.27 1 906 . 167 PRO CB C 30.90 0.27 1 907 . 168 VAL H H 9.31 0.01 1 908 . 168 VAL N N 126.25 0.14 1 909 . 168 VAL C C 175.38 0.06 1 910 . 168 VAL CA C 62.50 0.27 1 911 . 168 VAL CB C 35.30 0.27 1 912 . 168 VAL CG1 C 22.38 0.02 2 913 . 168 VAL HG1 H 1.1 0.01 2 914 . 168 VAL CG2 C 24.9 0.02 2 915 . 168 VAL HG2 H 1.26 0.01 2 916 . 169 ASP H H 10.01 0.01 1 917 . 169 ASP N N 129.38 0.14 1 918 . 169 ASP C C 173.71 0.06 1 919 . 169 ASP CA C 53.66 0.27 1 920 . 169 ASP CB C 42.51 0.27 1 921 . 170 SER H H 7.48 0.01 1 922 . 170 SER N N 110.74 0.14 1 923 . 170 SER C C 174.19 0.06 1 924 . 170 SER CA C 56.53 0.27 1 925 . 170 SER CB C 63.51 0.27 1 926 . 171 GLU H H 9.06 0.01 1 927 . 171 GLU N N 118.78 0.14 1 928 . 171 GLU C C 179.43 0.06 1 929 . 171 GLU CA C 60.24 0.27 1 930 . 171 GLU CB C 31.09 0.27 1 931 . 172 GLN H H 8.60 0.01 1 932 . 172 GLN N N 118.12 0.14 1 933 . 172 GLN C C 177.10 0.06 1 934 . 172 GLN CA C 59.65 0.27 1 935 . 172 GLN CB C 26.61 0.27 1 936 . 173 ASP H H 7.66 0.01 1 937 . 173 ASP N N 117.36 0.14 1 938 . 173 ASP C C 177.57 0.06 1 939 . 173 ASP CA C 57.23 0.27 1 940 . 173 ASP CB C 40.35 0.27 1 941 . 174 ILE H H 7.43 0.01 1 942 . 174 ILE N N 116.57 0.14 1 943 . 174 ILE C C 177.34 0.06 1 944 . 174 ILE CA C 65.79 0.27 1 945 . 174 ILE CB C 37.30 0.27 1 946 . 174 ILE CG1 C 28.72 0.02 1 947 . 174 ILE CD1 C 15.71 0.02 1 948 . 174 ILE HD1 H 1.05 0.01 1 949 . 175 PHE H H 7.09 0.01 1 950 . 175 PHE N N 114.96 0.14 1 951 . 175 PHE C C 177.62 0.06 1 952 . 175 PHE CA C 62.26 0.27 1 953 . 175 PHE CB C 36.73 0.27 1 954 . 176 ASP H H 8.52 0.01 1 955 . 176 ASP N N 118.05 0.14 1 956 . 176 ASP C C 180.76 0.06 1 957 . 176 ASP CA C 57.05 0.27 1 958 . 176 ASP CB C 39.16 0.27 1 959 . 177 TYR H H 8.07 0.01 1 960 . 177 TYR N N 119.40 0.14 1 961 . 177 TYR C C 177.30 0.06 1 962 . 177 TYR CA C 61.21 0.27 1 963 . 177 TYR CB C 37.00 0.27 1 964 . 178 ILE H H 6.80 0.01 1 965 . 178 ILE N N 105.04 0.14 1 966 . 178 ILE C C 173.31 0.06 1 967 . 178 ILE CA C 59.92 0.27 1 968 . 178 ILE CB C 36.96 0.27 1 969 . 178 ILE CG1 C 23.77 0.02 1 970 . 178 ILE CD1 C 14.68 0.02 1 971 . 178 ILE HD1 H 0.3 0.01 1 972 . 179 GLN H H 7.89 0.01 1 973 . 179 GLN N N 116.49 0.14 1 974 . 179 GLN C C 175.17 0.06 1 975 . 179 GLN CA C 56.37 0.27 1 976 . 179 GLN CB C 25.50 0.27 1 977 . 180 TRP H H 8.53 0.01 1 978 . 180 TRP N N 121.31 0.14 1 979 . 180 TRP C C 176.32 0.06 1 980 . 180 TRP CA C 53.05 0.27 1 981 . 180 TRP CB C 33.21 0.27 1 982 . 181 ARG H H 8.24 0.01 1 983 . 181 ARG N N 123.50 0.14 1 984 . 181 ARG C C 176.01 0.06 1 985 . 181 ARG CA C 55.92 0.27 1 986 . 181 ARG CB C 29.12 0.27 1 987 . 182 TYR H H 8.70 0.01 1 988 . 182 TYR N N 124.63 0.14 1 989 . 182 TYR C C 174.02 0.06 1 990 . 182 TYR CA C 60.00 0.27 1 991 . 182 TYR CB C 37.23 0.27 1 992 . 185 PRO C C 176.72 0.06 1 993 . 185 PRO CA C 66.25 0.27 1 994 . 185 PRO CB C 31.52 0.27 1 995 . 186 LYS H H 8.16 0.01 1 996 . 186 LYS N N 112.27 0.14 1 997 . 186 LYS C C 176.67 0.06 1 998 . 186 LYS CA C 57.13 0.27 1 999 . 186 LYS CB C 30.28 0.27 1 1000 . 187 ASP H H 7.94 0.01 1 1001 . 187 ASP N N 119.61 0.14 1 1002 . 187 ASP C C 176.18 0.06 1 1003 . 187 ASP CA C 53.63 0.27 1 1004 . 187 ASP CB C 40.74 0.27 1 1005 . 188 ARG H H 7.23 0.01 1 1006 . 188 ARG N N 119.54 0.14 1 1007 . 188 ARG C C 175.38 0.06 1 1008 . 188 ARG CA C 55.13 0.27 1 1009 . 188 ARG CB C 28.51 0.27 1 1010 . 189 SER H H 7.92 0.01 1 1011 . 189 SER N N 115.37 0.14 1 1012 . 189 SER C C 175.56 0.06 1 1013 . 189 SER CA C 60.68 0.27 1 1014 . 189 SER CB C 62.00 0.27 1 1015 . 190 GLU H H 7.82 0.01 1 1016 . 190 GLU N N 126.04 0.14 1 1017 . 190 GLU C C 178.70 0.06 1 1018 . 190 GLU CA C 57.14 0.27 1 1019 . 190 GLU CB C 31.13 0.27 1 stop_ save_