data_4575 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Letter to the Editor: Backbone resonance assignment of the N-terminal 24 kDa fragment of the gyrase B subunit from S. aureus complexed with novobiocin ; _BMRB_accession_number 4575 _BMRB_flat_file_name bmr4575.str _Entry_type original _Submission_date 2000-01-26 _Accession_date 2000-01-26 _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 Klaus Werner . . 2 Ross Alfred . . 3 Gsell Bernard . . 4 Senn Hans . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 564 "13C chemical shifts" 583 "15N chemical shifts" 202 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-04-03 original author . stop_ _Original_release_date 2000-04-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Klaus, W., Ross, A., Gsell, B., and Senn, H., "Letter to the Editor: Backbone Resonance Assignment of the N-terminal 24 kDa Fragment of the Gyrase B Subunit from S. aureus Complexed with Novobiocin," J. Biomol. NMR 16, 357-358 (2000). ; _Citation_title ; Letter to the Editor: Backbone Resonance Assignment of the N-terminal 24 kDa Fragment of the Gyrase B Subunit from S. aureus Complexed with Novobiocin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20285168 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Klaus Werner . . 2 Ross Alfred . . 3 Gsell Bernard . . 4 Senn Hans . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 16 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 357 _Page_last 358 _Year 2000 _Details . loop_ _Keyword gyrase antibiotics 'drug discovery' 'protein-ligand interaction' 'NMR assignment' stop_ save_ ################################## # Molecular system description # ################################## save_system_gyrase_B _Saveframe_category molecular_system _Mol_system_name 'N-terminal 24 kDa fragment of gyrase B' _Abbreviation_common 'gyrase B' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label gyrB $gyrase_B novobiocin $entity_NOV stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_gyrase_B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'gyrase B fragment' _Abbreviation_common 'gyrase B' _Molecular_mass 24000 _Mol_thiol_state 'not present' _Details ; truncated fragment of gyrase B: residues 24-234 with the point mutation Ala27 -> Val ; ############################## # Polymer residue sequence # ############################## _Residue_count 211 _Mol_residue_sequence ; GLEVVRKRPGMYIGSTSERG LHHLVWEIVDNSIDEALAGY ANQIEVVIEKDNWIKVTDNG RGIPVDIQEKMGRPAVEVIL TVLHAGGKFGGGGYKVSGGL HGVGSSVVNALSQDLEVYVH RNETIYHQAYKKGVPQFDLK EVGTTDKTGTVIRFKADGEI FTETTVYNYETLQQRIRELA FLNKGIQITLRDERDEENVR EDSYHYEGGIK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 24 GLY 2 25 LEU 3 26 GLU 4 27 VAL 5 28 VAL 6 29 ARG 7 30 LYS 8 31 ARG 9 32 PRO 10 33 GLY 11 34 MET 12 35 TYR 13 36 ILE 14 37 GLY 15 38 SER 16 39 THR 17 40 SER 18 41 GLU 19 42 ARG 20 43 GLY 21 44 LEU 22 45 HIS 23 46 HIS 24 47 LEU 25 48 VAL 26 49 TRP 27 50 GLU 28 51 ILE 29 52 VAL 30 53 ASP 31 54 ASN 32 55 SER 33 56 ILE 34 57 ASP 35 58 GLU 36 59 ALA 37 60 LEU 38 61 ALA 39 62 GLY 40 63 TYR 41 64 ALA 42 65 ASN 43 66 GLN 44 67 ILE 45 68 GLU 46 69 VAL 47 70 VAL 48 71 ILE 49 72 GLU 50 73 LYS 51 74 ASP 52 75 ASN 53 76 TRP 54 77 ILE 55 78 LYS 56 79 VAL 57 80 THR 58 81 ASP 59 82 ASN 60 83 GLY 61 84 ARG 62 85 GLY 63 86 ILE 64 87 PRO 65 88 VAL 66 89 ASP 67 90 ILE 68 91 GLN 69 92 GLU 70 93 LYS 71 94 MET 72 95 GLY 73 96 ARG 74 97 PRO 75 98 ALA 76 99 VAL 77 100 GLU 78 101 VAL 79 102 ILE 80 103 LEU 81 104 THR 82 105 VAL 83 106 LEU 84 107 HIS 85 108 ALA 86 109 GLY 87 110 GLY 88 111 LYS 89 112 PHE 90 113 GLY 91 114 GLY 92 115 GLY 93 116 GLY 94 117 TYR 95 118 LYS 96 119 VAL 97 120 SER 98 121 GLY 99 122 GLY 100 123 LEU 101 124 HIS 102 125 GLY 103 126 VAL 104 127 GLY 105 128 SER 106 129 SER 107 130 VAL 108 131 VAL 109 132 ASN 110 133 ALA 111 134 LEU 112 135 SER 113 136 GLN 114 137 ASP 115 138 LEU 116 139 GLU 117 140 VAL 118 141 TYR 119 142 VAL 120 143 HIS 121 144 ARG 122 145 ASN 123 146 GLU 124 147 THR 125 148 ILE 126 149 TYR 127 150 HIS 128 151 GLN 129 152 ALA 130 153 TYR 131 154 LYS 132 155 LYS 133 156 GLY 134 157 VAL 135 158 PRO 136 159 GLN 137 160 PHE 138 161 ASP 139 162 LEU 140 163 LYS 141 164 GLU 142 165 VAL 143 166 GLY 144 167 THR 145 168 THR 146 169 ASP 147 170 LYS 148 171 THR 149 172 GLY 150 173 THR 151 174 VAL 152 175 ILE 153 176 ARG 154 177 PHE 155 178 LYS 156 179 ALA 157 180 ASP 158 181 GLY 159 182 GLU 160 183 ILE 161 184 PHE 162 185 THR 163 186 GLU 164 187 THR 165 188 THR 166 189 VAL 167 190 TYR 168 191 ASN 169 192 TYR 170 193 GLU 171 194 THR 172 195 LEU 173 196 GLN 174 197 GLN 175 198 ARG 176 199 ILE 177 200 ARG 178 201 GLU 179 202 LEU 180 203 ALA 181 204 PHE 182 205 LEU 183 206 ASN 184 207 LYS 185 208 GLY 186 209 ILE 187 210 GLN 188 211 ILE 189 212 THR 190 213 LEU 191 214 ARG 192 215 ASP 193 216 GLU 194 217 ARG 195 218 ASP 196 219 GLU 197 220 GLU 198 221 ASN 199 222 VAL 200 223 ARG 201 224 GLU 202 225 ASP 203 226 SER 204 227 TYR 205 228 HIS 206 229 TYR 207 230 GLU 208 231 GLY 209 232 GLY 210 233 ILE 211 234 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-04 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 4URM "Crystal Structure Of Staph Gyraseb 24kda In Complex With Kibdelomycin" 98.58 231 99.04 99.04 3.05e-146 PDB 4URO "Crystal Structure Of Staph Gyraseb 24kda In Complex With Novobiocin" 98.58 231 99.04 99.04 3.05e-146 DBJ BAA01369 "DNA gyrase B [Staphylococcus aureus]" 100.00 644 99.53 99.53 7.28e-145 DBJ BAB41221 "DNA gyrase subunit B [Staphylococcus aureus subsp. aureus N315]" 100.00 644 99.05 99.53 3.35e-144 DBJ BAB56167 "DNA gyrase subunit B [Staphylococcus aureus subsp. aureus Mu50]" 100.00 644 99.05 99.53 3.35e-144 DBJ BAB93870 "DNA gyrase subunit B [Staphylococcus aureus subsp. aureus MW2]" 100.00 644 99.53 99.53 7.28e-145 DBJ BAC11788 "gyrase B [Staphylococcus aureus]" 57.35 392 100.00 100.00 7.55e-77 EMBL CAA50570 "DNA gyrase [Staphylococcus aureus]" 100.00 644 99.53 99.53 7.28e-145 EMBL CAG39033 "DNA gyrase subunit B [Staphylococcus aureus subsp. aureus MRSA252]" 100.00 643 99.53 99.53 1.08e-144 EMBL CAG41777 "DNA gyrase subunit B [Staphylococcus aureus subsp. aureus MSSA476]" 100.00 643 99.53 99.53 7.23e-145 EMBL CAI79693 "DNA gyrase subunit B [Staphylococcus aureus RF122]" 100.00 644 99.53 99.53 9.55e-145 EMBL CAQ48445 "DNA gyrase, B subunit [Staphylococcus aureus subsp. aureus ST398]" 100.00 644 99.05 99.53 2.64e-144 GB AAW37393 "DNA gyrase, B subunit [Staphylococcus aureus subsp. aureus COL]" 100.00 644 99.05 99.05 2.73e-144 GB ABD21942 "DNA gyrase, B subunit [Staphylococcus aureus subsp. aureus USA300_FPR3757]" 100.00 644 99.53 99.53 7.28e-145 GB ABD29196 "DNA gyrase, B subunit [Staphylococcus aureus subsp. aureus NCTC 8325]" 100.00 644 99.53 99.53 7.28e-145 GB ABD52436 "gyrase B [Staphylococcus aureus]" 53.08 398 97.32 98.21 3.94e-67 GB ABQ47819 "DNA gyrase subunit B [Staphylococcus aureus subsp. aureus JH9]" 100.00 640 99.05 99.53 4.70e-144 REF WP_000255576 "DNA gyrase subunit B [Staphylococcus aureus]" 100.00 644 99.05 99.05 2.73e-144 REF WP_000255577 "DNA gyrase subunit B [Staphylococcus aureus]" 100.00 644 98.10 99.05 1.45e-142 REF WP_000255578 "MULTISPECIES: DNA gyrase subunit B [Bacteria]" 100.00 644 99.05 99.53 3.35e-144 REF WP_000255579 "DNA gyrase subunit B [Staphylococcus argenteus]" 100.00 644 97.63 99.05 3.71e-143 REF WP_000255580 "DNA gyrase subunit B [Staphylococcus aureus]" 100.00 644 99.05 99.05 8.32e-144 SP P0A0K7 "RecName: Full=DNA gyrase subunit B" 100.00 644 99.53 99.53 7.28e-145 SP P0A0K8 "RecName: Full=DNA gyrase subunit B" 100.00 644 99.53 99.53 7.28e-145 SP P66936 "RecName: Full=DNA gyrase subunit B" 100.00 644 99.05 99.53 3.35e-144 SP P66937 "RecName: Full=DNA gyrase subunit B" 100.00 644 99.05 99.53 3.35e-144 SP Q2FKQ1 "RecName: Full=DNA gyrase subunit B" 100.00 644 99.53 99.53 7.28e-145 stop_ save_ ############# # Ligands # ############# save_NOV _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common NOVOBIOCIN _BMRB_code NOV _PDB_code NOV _Molecular_mass 612.624 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? C16 C16 C . 0 . ? C17 C17 C . 0 . ? C18 C18 C . 0 . ? C19 C19 C . 0 . ? C2 C2 C . 0 . ? C20 C20 C . 0 . ? C21 C21 C . 0 . ? C22 C22 C . 0 . ? C23 C23 C . 0 . ? C24 C24 C . 0 . ? C25 C25 C . 0 . ? C26 C26 C . 0 . ? C27 C27 C . 0 . ? C28 C28 C . 0 . ? C29 C29 C . 0 . ? C3 C3 C . 0 . ? C30 C30 C . 0 . ? C31 C31 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? H10 H10 H . 0 . ? H11 H11 H . 0 . ? H11A H11A H . 0 . ? H12 H12 H . 0 . ? H13 H13 H . 0 . ? H15 H15 H . 0 . ? H18 H18 H . 0 . ? H19 H19 H . 0 . ? H201 H201 H . 0 . ? H202 H202 H . 0 . ? H21 H21 H . 0 . ? H21A H21A H . 0 . ? H22 H22 H . 0 . ? H23 H23 H . 0 . ? H231 H231 H . 0 . ? H232 H232 H . 0 . ? H233 H233 H . 0 . ? H241 H241 H . 0 . ? H242 H242 H . 0 . ? H243 H243 H . 0 . ? H251 H251 H . 0 . ? H252 H252 H . 0 . ? H253 H253 H . 0 . ? H261 H261 H . 0 . ? H262 H262 H . 0 . ? H263 H263 H . 0 . ? H27 H27 H . 0 . ? H28 H28 H . 0 . ? H29 H29 H . 0 . ? H30 H30 H . 0 . ? HN11 HN11 H . 0 . ? HN12 HN12 H . 0 . ? HN2 HN2 H . 0 . ? HO3 HO3 H . 0 . ? HO6 HO6 H . 0 . ? HO9 HO9 H . 0 . ? N1 N1 N . 0 . ? N2 N2 N . 0 . ? O1 O1 O . 0 . ? O10 O10 O . 0 . ? O11 O11 O . 0 . ? O2 O2 O . 0 . ? O3 O3 O . 0 . ? O4 O4 O . 0 . ? O5 O5 O . 0 . ? O6 O6 O . 0 . ? O7 O7 O . 0 . ? O8 O8 O . 0 . ? O9 O9 O . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 O1 ? ? SING C1 H11A ? ? SING C1 H12 ? ? SING C1 H13 ? ? SING O1 C27 ? ? SING N1 C12 ? ? SING N1 HN11 ? ? SING N1 HN12 ? ? DOUB C12 O4 ? ? SING C12 O5 ? ? SING O5 C28 ? ? SING C27 C28 ? ? SING C27 C31 ? ? SING C27 H27 ? ? SING C28 C29 ? ? SING C28 H28 ? ? SING C29 O6 ? ? SING C29 C30 ? ? SING C29 H29 ? ? SING O6 HO6 ? ? SING C30 O7 ? ? SING C30 O8 ? ? SING C30 H30 ? ? SING O7 C31 ? ? SING C31 C23 ? ? SING C31 C26 ? ? SING C23 H231 ? ? SING C23 H232 ? ? SING C23 H233 ? ? SING C26 H261 ? ? SING C26 H262 ? ? SING C26 H263 ? ? SING O8 C3 ? ? DOUB C3 C4 ? ? SING C3 C11 ? ? SING C4 C2 ? ? SING C4 C5 ? ? SING C2 H21A ? ? SING C2 H22 ? ? SING C2 H23 ? ? DOUB C5 C9 ? ? SING C5 O10 ? ? SING C9 C10 ? ? SING C9 C8 ? ? DOUB C10 C11 ? ? SING C10 H10 ? ? SING C11 H11 ? ? SING O10 C6 ? ? DOUB C6 O11 ? ? SING C6 C7 ? ? DOUB C7 C8 ? ? SING C7 N2 ? ? SING C8 O9 ? ? SING O9 HO9 ? ? SING N2 C13 ? ? SING N2 HN2 ? ? DOUB C13 O2 ? ? SING C13 C14 ? ? DOUB C14 C15 ? ? SING C14 C19 ? ? SING C15 C16 ? ? SING C15 H15 ? ? DOUB C16 C17 ? ? SING C16 C20 ? ? SING C17 O3 ? ? SING C17 C18 ? ? SING O3 HO3 ? ? DOUB C18 C19 ? ? SING C18 H18 ? ? SING C19 H19 ? ? SING C20 C21 ? ? SING C20 H201 ? ? SING C20 H202 ? ? DOUB C21 C22 ? ? SING C21 H21 ? ? SING C22 C24 ? ? SING C22 C25 ? ? SING C24 H241 ? ? SING C24 H242 ? ? SING C24 H243 ? ? SING C25 H251 ? ? SING C25 H252 ? ? SING C25 H253 ? ? 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 $gyrase_B 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $gyrase_B 'recombinant technology' 'E. coli' Escherichi coli . . 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 $gyrase_B 1.2 mM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version . _Details . save_ save_GARANT _Saveframe_category software _Name GARANT _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label $sample_1 save_ save_15N-edited_NOESY-HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_gyrB _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 308 0.03 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 . . . 1.0 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_gyrB-novo_pH_6.5 _Saveframe_category assigned_chemical_shifts _Details ; no H-H correlations for Arg42, Glu92, Gly110, Lys111, Ala152 ; loop_ _Experiment_label HNCA HNCO CBCA(CO)NH HNCACB HBHA(CO)NH '15N-edited NOESY-HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $gyrB _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name gyrB _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 GLY C C 177.0 0.05 1 2 . 2 LEU N N 119.0 0.05 1 3 . 2 LEU H H 8.37 0.02 1 4 . 2 LEU CA C 56.3 0.05 1 5 . 2 LEU HA H 4.04 0.02 1 6 . 2 LEU CB C 41.4 0.05 1 7 . 2 LEU HB3 H 1.62 0.02 2 8 . 2 LEU C C 177.3 0.05 1 9 . 3 GLU N N 120.3 0.05 1 10 . 3 GLU H H 9.18 0.02 1 11 . 3 GLU CA C 60.1 0.05 1 12 . 3 GLU HA H 3.93 0.02 1 13 . 3 GLU CB C 27.7 0.05 1 14 . 3 GLU HB3 H 2.03 0.02 2 15 . 3 GLU C C 178.4 0.05 1 16 . 4 VAL N N 116.8 0.05 1 17 . 4 VAL H H 7.66 0.02 1 18 . 4 VAL CA C 65.2 0.05 1 19 . 4 VAL HA H 3.82 0.02 1 20 . 4 VAL CB C 31.4 0.05 1 21 . 4 VAL HB H 2.19 0.02 1 22 . 4 VAL C C 177.3 0.05 1 23 . 5 VAL N N 120.5 0.05 1 24 . 5 VAL H H 7.07 0.02 1 25 . 5 VAL CA C 64.2 0.05 1 26 . 5 VAL HA H 3.37 0.02 1 27 . 5 VAL CB C 31.5 0.05 1 28 . 5 VAL C C 176.6 0.05 1 29 . 6 ARG N N 112.9 0.05 1 30 . 6 ARG H H 6.63 0.02 1 31 . 6 ARG CA C 59.0 0.05 1 32 . 6 ARG HA H 3.56 0.02 1 33 . 6 ARG CB C 29.9 0.05 1 34 . 6 ARG C C 177.4 0.05 1 35 . 7 LYS N N 116.0 0.05 1 36 . 7 LYS H H 7.51 0.02 1 37 . 7 LYS CA C 57.8 0.05 1 38 . 7 LYS HA H 4.14 0.02 1 39 . 7 LYS CB C 33.5 0.05 1 40 . 7 LYS HB2 H 1.86 0.02 1 41 . 7 LYS HB3 H 1.86 0.02 1 42 . 7 LYS C C 177.6 0.05 1 43 . 8 ARG N N 116.3 0.05 1 44 . 8 ARG H H 7.20 0.02 1 45 . 8 ARG CA C 53.5 0.05 1 46 . 8 ARG CB C 31.1 0.05 1 47 . 9 PRO CA C 66.1 0.05 1 48 . 9 PRO HA H 4.54 0.02 1 49 . 9 PRO CB C 31.6 0.05 1 50 . 9 PRO C C 180.1 0.05 1 51 . 10 GLY N N 105.6 0.05 1 52 . 10 GLY H H 8.89 0.02 1 53 . 10 GLY CA C 46.4 0.05 1 54 . 10 GLY HA2 H 3.79 0.02 2 55 . 10 GLY HA3 H 3.43 0.02 2 56 . 10 GLY C C 175.7 0.05 1 57 . 11 MET N N 118.1 0.05 1 58 . 11 MET H H 7.51 0.02 1 59 . 11 MET CA C 57.3 0.05 1 60 . 11 MET HA H 4.10 0.02 1 61 . 11 MET CB C 32.4 0.05 1 62 . 11 MET C C 175.7 0.05 1 63 . 12 TYR N N 115.2 0.05 1 64 . 12 TYR H H 7.57 0.02 1 65 . 12 TYR CA C 60.2 0.05 1 66 . 12 TYR HA H 4.39 0.02 1 67 . 12 TYR CB C 41.2 0.05 1 68 . 12 TYR C C 176.3 0.05 1 69 . 13 ILE N N 110.3 0.05 1 70 . 13 ILE H H 7.93 0.02 1 71 . 13 ILE CA C 59.5 0.05 1 72 . 13 ILE HA H 4.32 0.02 1 73 . 13 ILE CB C 41.2 0.05 1 74 . 13 ILE HB H 1.96 0.02 1 75 . 13 ILE C C 175.9 0.05 1 76 . 14 GLY N N 112.7 0.05 1 77 . 14 GLY H H 7.47 0.02 1 78 . 14 GLY CA C 47.5 0.05 1 79 . 14 GLY HA2 H 3.58 0.02 2 80 . 14 GLY HA3 H 4.54 0.02 2 81 . 14 GLY C C 174.4 0.05 1 82 . 15 SER N N 112.6 0.05 1 83 . 15 SER H H 7.47 0.02 1 84 . 15 SER CA C 57.5 0.05 1 85 . 15 SER CB C 64.8 0.05 1 86 . 15 SER HB2 H 3.73 0.02 2 87 . 15 SER C C 172.8 0.05 1 88 . 16 THR N N 108.7 0.05 1 89 . 16 THR H H 8.41 0.02 1 90 . 16 THR CA C 60.9 0.05 1 91 . 16 THR CB C 67.4 0.05 1 92 . 16 THR HB H 4.59 0.02 1 93 . 16 THR C C 174.8 0.05 1 94 . 17 SER N N 117.4 0.05 1 95 . 17 SER H H 7.93 0.02 1 96 . 17 SER CA C 57.7 0.05 1 97 . 17 SER CB C 65.3 0.05 1 98 . 17 SER C C 174.4 0.05 1 99 . 18 GLU N N 120.2 0.05 1 100 . 18 GLU H H 9.12 0.02 1 101 . 18 GLU CA C 57.7 0.05 1 102 . 19 ARG CA C 59.9 0.05 1 103 . 19 ARG HA H 4.29 0.02 1 104 . 19 ARG CB C 30.4 0.05 1 105 . 19 ARG HB3 H 1.79 0.02 2 106 . 19 ARG C C 179.4 0.05 1 107 . 20 GLY N N 109.1 0.05 1 108 . 20 GLY H H 7.11 0.02 1 109 . 20 GLY CA C 47.5 0.05 1 110 . 20 GLY HA2 H 4.38 0.02 2 111 . 20 GLY C C 174.9 0.05 1 112 . 21 LEU N N 120.7 0.05 1 113 . 21 LEU H H 7.69 0.02 1 114 . 21 LEU CA C 57.8 0.05 1 115 . 21 LEU HA H 3.18 0.02 1 116 . 21 LEU CB C 42.6 0.05 1 117 . 21 LEU C C 178.7 0.05 1 118 . 22 HIS N N 111.6 0.05 1 119 . 22 HIS H H 7.40 0.02 1 120 . 22 HIS CA C 62.8 0.05 1 121 . 22 HIS HA H 3.84 0.02 1 122 . 22 HIS C C 176.4 0.05 1 123 . 23 HIS N N 118.0 0.05 1 124 . 23 HIS H H 7.93 0.02 1 125 . 23 HIS CA C 59.1 0.05 1 126 . 23 HIS HA H 4.33 0.02 1 127 . 23 HIS CB C 29.3 0.05 1 128 . 23 HIS C C 176.9 0.05 1 129 . 24 LEU N N 115.4 0.05 1 130 . 24 LEU H H 7.45 0.02 1 131 . 24 LEU CA C 58.4 0.05 1 132 . 24 LEU HA H 3.71 0.02 1 133 . 24 LEU CB C 42.1 0.05 1 134 . 24 LEU C C 178.3 0.05 1 135 . 25 VAL N N 113.2 0.05 1 136 . 25 VAL H H 6.70 0.02 1 137 . 25 VAL CA C 66.4 0.05 1 138 . 25 VAL HA H 3.31 0.02 1 139 . 25 VAL CB C 31.0 0.05 1 140 . 25 VAL C C 178.3 0.05 1 141 . 26 TRP N N 117.6 0.05 1 142 . 26 TRP H H 7.14 0.02 1 143 . 26 TRP CA C 58.2 0.05 1 144 . 26 TRP HA H 4.77 0.02 1 145 . 26 TRP CB C 29.8 0.05 1 146 . 26 TRP HB2 H 3.22 0.02 1 147 . 26 TRP HB3 H 3.22 0.02 1 148 . 26 TRP C C 178.8 0.05 1 149 . 27 GLU N N 116.5 0.05 1 150 . 27 GLU H H 7.87 0.02 1 151 . 27 GLU CA C 59.0 0.05 1 152 . 27 GLU HA H 4.13 0.02 1 153 . 27 GLU CB C 29.5 0.05 1 154 . 27 GLU C C 178.3 0.05 1 155 . 28 ILE N N 116.1 0.05 1 156 . 28 ILE H H 7.03 0.02 1 157 . 28 ILE CA C 61.3 0.05 1 158 . 28 ILE HA H 4.08 0.02 1 159 . 28 ILE CB C 36.0 0.05 1 160 . 28 ILE HB H 2.26 0.02 1 161 . 28 ILE C C 179.9 0.05 1 162 . 29 VAL N N 121.0 0.05 1 163 . 29 VAL H H 9.01 0.02 1 164 . 29 VAL CA C 67.6 0.05 1 165 . 29 VAL HA H 3.62 0.02 1 166 . 29 VAL CB C 31.9 0.05 1 167 . 29 VAL C C 178.2 0.05 1 168 . 30 ASP N N 120.1 0.05 1 169 . 30 ASP H H 8.76 0.02 1 170 . 30 ASP CA C 58.0 0.05 1 171 . 30 ASP HA H 4.46 0.02 1 172 . 30 ASP CB C 40.3 0.05 1 173 . 30 ASP C C 178.9 0.05 1 174 . 31 ASN N N 116.4 0.05 1 175 . 31 ASN H H 7.43 0.02 1 176 . 31 ASN CA C 57.0 0.05 1 177 . 31 ASN HA H 4.63 0.02 1 178 . 31 ASN CB C 38.6 0.05 1 179 . 31 ASN HB2 H 3.41 0.02 1 180 . 31 ASN HB3 H 3.41 0.02 1 181 . 31 ASN C C 179.5 0.05 1 182 . 32 SER N N 121.1 0.05 1 183 . 32 SER H H 7.74 0.02 1 184 . 32 SER CA C 64.0 0.05 1 185 . 32 SER HB2 H 2.40 0.02 2 186 . 32 SER C C 176.4 0.05 1 187 . 33 ILE N N 123.4 0.05 1 188 . 33 ILE H H 8.85 0.02 1 189 . 33 ILE CA C 64.1 0.05 1 190 . 33 ILE HA H 3.60 0.02 1 191 . 33 ILE CB C 35.7 0.05 1 192 . 33 ILE HB H 2.31 0.02 1 193 . 33 ILE C C 178.7 0.05 1 194 . 34 ASP N N 120.7 0.05 1 195 . 34 ASP H H 8.29 0.02 1 196 . 34 ASP CA C 58.4 0.05 1 197 . 34 ASP HA H 4.47 0.02 1 198 . 34 ASP CB C 40.7 0.05 1 199 . 34 ASP HB3 H 2.84 0.02 2 200 . 34 ASP C C 179.5 0.05 1 201 . 35 GLU N N 121.2 0.05 1 202 . 35 GLU H H 7.16 0.02 1 203 . 35 GLU CA C 57.4 0.05 1 204 . 35 GLU HA H 4.77 0.02 1 205 . 35 GLU CB C 30.9 0.05 1 206 . 35 GLU HB2 H 2.08 0.02 1 207 . 35 GLU HB3 H 2.08 0.02 1 208 . 35 GLU C C 178.9 0.05 1 209 . 36 ALA N N 125.3 0.05 1 210 . 36 ALA H H 8.06 0.02 1 211 . 36 ALA CA C 54.4 0.05 1 212 . 36 ALA HA H 4.89 0.02 1 213 . 36 ALA HB H 1.41 0.02 1 214 . 36 ALA CB C 18.7 0.05 1 215 . 36 ALA C C 182.1 0.05 1 216 . 37 LEU N N 122.7 0.05 1 217 . 37 LEU H H 9.24 0.02 1 218 . 37 LEU CA C 57.6 0.05 1 219 . 37 LEU HA H 4.05 0.02 1 220 . 37 LEU CB C 41.3 0.05 1 221 . 37 LEU HB3 H 1.90 0.02 2 222 . 37 LEU C C 179.5 0.05 1 223 . 38 ALA N N 118.4 0.05 1 224 . 38 ALA H H 7.60 0.02 1 225 . 38 ALA CA C 53.0 0.05 1 226 . 38 ALA HA H 4.20 0.02 1 227 . 38 ALA HB H 1.55 0.02 1 228 . 38 ALA CB C 19.2 0.05 1 229 . 38 ALA C C 177.2 0.05 1 230 . 39 GLY N N 102.7 0.05 1 231 . 39 GLY H H 7.61 0.02 1 232 . 39 GLY CA C 44.6 0.05 1 233 . 39 GLY HA2 H 3.60 0.02 2 234 . 39 GLY HA3 H 3.90 0.02 2 235 . 39 GLY C C 174.6 0.05 1 236 . 40 TYR N N 116.4 0.05 1 237 . 40 TYR H H 7.42 0.02 1 238 . 40 TYR CA C 60.1 0.05 1 239 . 40 TYR HA H 4.49 0.02 1 240 . 40 TYR CB C 40.9 0.05 1 241 . 40 TYR HB2 H 2.70 0.02 2 242 . 40 TYR HB3 H 3.25 0.02 2 243 . 40 TYR C C 175.0 0.05 1 244 . 41 ALA N N 118.6 0.05 1 245 . 41 ALA H H 7.02 0.02 1 246 . 41 ALA CA C 50.8 0.05 1 247 . 41 ALA HA H 4.48 0.02 1 248 . 41 ALA HB H 1.23 0.02 1 249 . 41 ALA CB C 21.1 0.05 1 250 . 41 ALA C C 176.3 0.05 1 251 . 42 ASN N N 114.6 0.05 1 252 . 42 ASN H H 9.35 0.02 1 253 . 42 ASN CA C 53.8 0.05 1 254 . 42 ASN HA H 4.65 0.02 1 255 . 42 ASN CB C 39.6 0.05 1 256 . 42 ASN HB3 H 2.79 0.02 2 257 . 43 GLN N N 121.5 0.05 1 258 . 43 GLN H H 8.14 0.02 1 259 . 43 GLN CA C 55.7 0.05 1 260 . 43 GLN HA H 5.33 0.02 1 261 . 43 GLN CB C 32.3 0.05 1 262 . 43 GLN C C 174.4 0.05 1 263 . 44 ILE N N 122.6 0.05 1 264 . 44 ILE H H 8.70 0.02 1 265 . 44 ILE CA C 59.8 0.05 1 266 . 44 ILE HA H 5.07 0.02 1 267 . 44 ILE CB C 42.8 0.05 1 268 . 44 ILE C C 174.5 0.05 1 269 . 45 GLU N N 129.2 0.05 1 270 . 45 GLU H H 9.36 0.02 1 271 . 45 GLU CA C 54.9 0.05 1 272 . 45 GLU HA H 5.28 0.02 1 273 . 45 GLU CB C 34.0 0.05 1 274 . 45 GLU HB3 H 2.01 0.02 2 275 . 45 GLU C C 174.4 0.05 1 276 . 46 VAL N N 128.9 0.05 1 277 . 46 VAL H H 9.48 0.02 1 278 . 46 VAL CA C 61.6 0.05 1 279 . 46 VAL HA H 4.85 0.02 1 280 . 46 VAL CB C 33.4 0.05 1 281 . 46 VAL C C 173.7 0.05 1 282 . 47 VAL N N 126.6 0.05 1 283 . 47 VAL H H 9.54 0.02 1 284 . 47 VAL CA C 60.2 0.05 1 285 . 47 VAL HA H 5.13 0.02 1 286 . 47 VAL CB C 35.7 0.05 1 287 . 47 VAL HB H 1.96 0.02 1 288 . 47 VAL C C 175.5 0.05 1 289 . 48 ILE N N 125.0 0.05 1 290 . 48 ILE H H 9.13 0.02 1 291 . 48 ILE CA C 60.7 0.05 1 292 . 48 ILE HA H 4.52 0.02 1 293 . 48 ILE CB C 38.1 0.05 1 294 . 48 ILE HB H 2.14 0.02 1 295 . 48 ILE C C 175.5 0.05 1 296 . 49 GLU N N 124.9 0.05 1 297 . 49 GLU H H 8.82 0.02 1 298 . 49 GLU CA C 55.1 0.05 1 299 . 49 GLU HA H 4.32 0.02 1 300 . 49 GLU CB C 33.8 0.05 1 301 . 49 GLU HB3 H 2.16 0.02 2 302 . 49 GLU C C 176.2 0.05 1 303 . 50 LYS N N 117.6 0.05 1 304 . 50 LYS H H 8.28 0.02 1 305 . 50 LYS CA C 58.8 0.05 1 306 . 50 LYS HA H 4.03 0.02 1 307 . 50 LYS CB C 33.0 0.05 1 308 . 50 LYS HB2 H 1.79 0.02 1 309 . 50 LYS HB3 H 1.79 0.02 1 310 . 50 LYS C C 176.9 0.05 1 311 . 51 ASP N N 118.6 0.05 1 312 . 51 ASP H H 9.21 0.02 1 313 . 51 ASP CA C 56.2 0.05 1 314 . 51 ASP HA H 4.44 0.02 1 315 . 51 ASP CB C 40.2 0.05 1 316 . 51 ASP HB2 H 2.97 0.02 2 317 . 51 ASP HB3 H 3.28 0.02 2 318 . 51 ASP C C 175.2 0.05 1 319 . 52 ASN N N 107.0 0.05 1 320 . 52 ASN H H 8.64 0.02 1 321 . 52 ASN CA C 57.3 0.05 1 322 . 52 ASN HA H 4.17 0.02 1 323 . 52 ASN CB C 38.1 0.05 1 324 . 52 ASN HB3 H 3.15 0.02 2 325 . 52 ASN C C 177.6 0.05 1 326 . 53 TRP N N 119.7 0.05 1 327 . 53 TRP H H 6.79 0.02 1 328 . 53 TRP CA C 59.3 0.05 1 329 . 53 TRP HA H 4.48 0.02 1 330 . 53 TRP CB C 30.3 0.05 1 331 . 53 TRP HB2 H 3.29 0.02 2 332 . 53 TRP C C 174.6 0.05 1 333 . 54 ILE N N 121.4 0.05 1 334 . 54 ILE H H 8.14 0.02 1 335 . 54 ILE CA C 56.3 0.05 1 336 . 54 ILE HA H 4.87 0.02 1 337 . 54 ILE CB C 37.6 0.05 1 338 . 54 ILE C C 174.2 0.05 1 339 . 55 LYS N N 127.0 0.05 1 340 . 55 LYS H H 9.08 0.02 1 341 . 55 LYS CA C 54.7 0.05 1 342 . 55 LYS HA H 5.42 0.02 1 343 . 55 LYS CB C 35.9 0.05 1 344 . 55 LYS HB2 H 1.54 0.02 2 345 . 55 LYS C C 175.4 0.05 1 346 . 56 VAL N N 127.8 0.05 1 347 . 56 VAL H H 9.56 0.02 1 348 . 56 VAL CA C 61.3 0.05 1 349 . 56 VAL HA H 5.33 0.02 1 350 . 56 VAL CB C 34.3 0.05 1 351 . 56 VAL HB H 2.02 0.02 1 352 . 56 VAL C C 175.7 0.05 1 353 . 57 THR N N 124.3 0.05 1 354 . 57 THR H H 9.21 0.02 1 355 . 57 THR CA C 61.6 0.05 1 356 . 57 THR HA H 5.53 0.02 1 357 . 57 THR CB C 71.8 0.05 1 358 . 57 THR C C 173.6 0.05 1 359 . 58 ASP N N 121.2 0.05 1 360 . 58 ASP H H 8.77 0.02 1 361 . 58 ASP CA C 53.1 0.05 1 362 . 58 ASP HA H 5.67 0.02 1 363 . 58 ASP CB C 46.2 0.05 1 364 . 58 ASP C C 174.8 0.05 1 365 . 59 ASN N N 117.1 0.05 1 366 . 59 ASN H H 7.78 0.02 1 367 . 59 ASN CA C 51.6 0.05 1 368 . 59 ASN HA H 5.72 0.02 1 369 . 59 ASN CB C 37.3 0.05 1 370 . 59 ASN HB3 H 2.80 0.02 2 371 . 59 ASN C C 176.2 0.05 1 372 . 60 GLY N N 105.3 0.05 1 373 . 60 GLY H H 9.31 0.02 1 374 . 60 GLY CA C 44.6 0.05 1 375 . 60 GLY HA2 H 4.34 0.02 2 376 . 60 GLY C C 173.3 0.05 1 377 . 61 ARG N N 117.4 0.05 1 378 . 61 ARG H H 9.57 0.02 1 379 . 61 ARG CA C 59.2 0.05 1 380 . 61 ARG HA H 3.81 0.02 1 381 . 61 ARG CB C 32.2 0.05 1 382 . 61 ARG C C 178.3 0.05 1 383 . 62 GLY N N 103.5 0.05 1 384 . 62 GLY H H 7.84 0.02 1 385 . 62 GLY CA C 43.4 0.05 1 386 . 62 GLY C C 172.9 0.05 1 387 . 63 ILE N N 125.9 0.05 1 388 . 63 ILE H H 6.91 0.02 1 389 . 63 ILE CA C 62.0 0.05 1 390 . 64 PRO CA C 64.0 0.05 1 391 . 64 PRO CB C 32.7 0.05 1 392 . 64 PRO HB3 H 3.55 0.02 2 393 . 64 PRO C C 175.3 0.05 1 394 . 65 VAL N N 107.7 0.05 1 395 . 65 VAL H H 7.41 0.02 1 396 . 65 VAL CA C 59.9 0.05 1 397 . 65 VAL HA H 4.16 0.02 1 398 . 65 VAL CB C 32.5 0.05 1 399 . 65 VAL HB H 1.89 0.02 1 400 . 65 VAL C C 174.9 0.05 1 401 . 66 ASP N N 119.0 0.05 1 402 . 66 ASP H H 8.48 0.02 1 403 . 66 ASP CA C 53.3 0.05 1 404 . 66 ASP HA H 4.37 0.02 1 405 . 66 ASP CB C 41.1 0.05 1 406 . 66 ASP HB2 H 2.72 0.02 2 407 . 66 ASP HB3 H 2.53 0.02 2 408 . 66 ASP C C 176.3 0.05 1 409 . 67 ILE N N 122.2 0.05 1 410 . 67 ILE H H 8.62 0.02 1 411 . 67 ILE CA C 61.5 0.05 1 412 . 67 ILE HA H 3.60 0.02 1 413 . 67 ILE CB C 37.1 0.05 1 414 . 67 ILE HB H 1.77 0.02 1 415 . 67 ILE C C 176.4 0.05 1 416 . 68 GLN N N 127.9 0.05 1 417 . 68 GLN H H 8.21 0.02 1 418 . 68 GLN CA C 54.8 0.05 1 419 . 68 GLN CB C 29.8 0.05 1 420 . 69 GLU CA C 59.3 0.05 1 421 . 69 GLU HA H 3.93 0.02 1 422 . 69 GLU CB C 30.2 0.05 1 423 . 69 GLU HB2 H 2.01 0.02 1 424 . 69 GLU HB3 H 2.01 0.02 1 425 . 69 GLU C C 177.6 0.05 1 426 . 70 LYS N N 117.5 0.05 1 427 . 70 LYS H H 8.57 0.02 1 428 . 70 LYS CA C 59.0 0.05 1 429 . 70 LYS HA H 4.04 0.02 1 430 . 70 LYS CB C 31.9 0.05 1 431 . 70 LYS HB3 H 1.87 0.02 2 432 . 70 LYS C C 177.6 0.05 1 433 . 71 MET N N 114.5 0.05 1 434 . 71 MET H H 7.79 0.02 1 435 . 71 MET CA C 56.0 0.05 1 436 . 71 MET HA H 4.51 0.02 1 437 . 71 MET CB C 33.8 0.05 1 438 . 71 MET C C 177.4 0.05 1 439 . 72 GLY N N 106.6 0.05 1 440 . 72 GLY H H 8.32 0.02 1 441 . 72 GLY CA C 46.2 0.05 1 442 . 72 GLY HA2 H 3.75 0.02 2 443 . 72 GLY HA3 H 3.96 0.02 2 444 . 72 GLY C C 173.1 0.05 1 445 . 73 ARG N N 114.4 0.05 1 446 . 73 ARG H H 6.77 0.02 1 447 . 73 ARG CA C 51.0 0.05 1 448 . 73 ARG CB C 30.9 0.05 1 449 . 74 PRO CA C 63.1 0.05 1 450 . 74 PRO HA H 4.11 0.02 1 451 . 74 PRO CB C 33.5 0.05 1 452 . 74 PRO C C 178.3 0.05 1 453 . 75 ALA N N 125.9 0.05 1 454 . 75 ALA H H 8.29 0.02 1 455 . 75 ALA CA C 56.9 0.05 1 456 . 75 ALA HA H 3.81 0.02 1 457 . 75 ALA HB H 1.23 0.02 1 458 . 75 ALA CB C 16.9 0.05 1 459 . 75 ALA C C 179.3 0.05 1 460 . 76 VAL N N 111.9 0.05 1 461 . 76 VAL H H 7.15 0.02 1 462 . 76 VAL CA C 64.5 0.05 1 463 . 76 VAL HA H 3.61 0.02 1 464 . 76 VAL CB C 29.9 0.05 1 465 . 76 VAL HB H 1.95 0.02 1 466 . 76 VAL C C 173.5 0.05 1 467 . 77 GLU N N 120.2 0.05 1 468 . 77 GLU H H 6.51 0.02 1 469 . 77 GLU CA C 59.2 0.05 1 470 . 77 GLU HA H 4.11 0.02 1 471 . 77 GLU CB C 31.5 0.05 1 472 . 77 GLU C C 180.1 0.05 1 473 . 78 VAL N N 121.5 0.05 1 474 . 78 VAL H H 7.63 0.02 1 475 . 78 VAL CA C 67.0 0.05 1 476 . 78 VAL HA H 3.33 0.02 1 477 . 78 VAL CB C 31.9 0.05 1 478 . 78 VAL HB H 2.21 0.02 1 479 . 78 VAL C C 177.7 0.05 1 480 . 79 ILE N N 117.7 0.05 1 481 . 79 ILE H H 8.33 0.02 1 482 . 79 ILE CA C 63.1 0.05 1 483 . 79 ILE HA H 3.61 0.02 1 484 . 79 ILE CB C 37.4 0.05 1 485 . 79 ILE HB H 1.83 0.02 1 486 . 79 ILE C C 177.0 0.05 1 487 . 80 LEU N N 114.4 0.05 1 488 . 80 LEU H H 7.28 0.02 1 489 . 80 LEU CA C 55.6 0.05 1 490 . 80 LEU HA H 3.84 0.02 1 491 . 80 LEU CB C 41.2 0.05 1 492 . 80 LEU HB3 H 1.66 0.02 2 493 . 80 LEU C C 178.5 0.05 1 494 . 81 THR N N 106.2 0.05 1 495 . 81 THR H H 7.55 0.02 1 496 . 81 THR CA C 62.1 0.05 1 497 . 81 THR HA H 4.65 0.02 1 498 . 81 THR CB C 71.9 0.05 1 499 . 81 THR HB H 4.41 0.02 1 500 . 81 THR C C 173.5 0.05 1 501 . 82 VAL N N 122.3 0.05 1 502 . 82 VAL H H 7.75 0.02 1 503 . 82 VAL CA C 62.1 0.05 1 504 . 82 VAL HA H 4.26 0.02 1 505 . 82 VAL CB C 32.9 0.05 1 506 . 82 VAL HB H 2.10 0.02 1 507 . 82 VAL C C 175.8 0.05 1 508 . 83 LEU N N 128.7 0.05 1 509 . 83 LEU H H 8.46 0.02 1 510 . 83 LEU CA C 55.9 0.05 1 511 . 83 LEU HA H 4.03 0.02 1 512 . 83 LEU CB C 42.7 0.05 1 513 . 84 HIS N N 119.8 0.05 1 514 . 84 HIS H H 8.39 0.02 1 515 . 84 HIS CA C 56.0 0.05 1 516 . 84 HIS HA H 4.61 0.02 1 517 . 84 HIS CB C 29.4 0.05 1 518 . 84 HIS HB2 H 3.15 0.02 2 519 . 84 HIS C C 175.1 0.05 1 520 . 85 ALA N N 124.0 0.05 1 521 . 85 ALA H H 8.09 0.02 1 522 . 85 ALA CA C 53.5 0.05 1 523 . 85 ALA HA H 4.14 0.02 1 524 . 85 ALA HB H 1.38 0.02 1 525 . 85 ALA CB C 19.7 0.05 1 526 . 85 ALA C C 178.3 0.05 1 527 . 86 GLY N N 106.6 0.05 1 528 . 86 GLY H H 8.48 0.02 1 529 . 86 GLY CA C 46.1 0.05 1 530 . 86 GLY HA2 H 3.95 0.02 2 531 . 87 GLY N N 115.6 0.05 1 532 . 87 GLY H H 8.39 0.02 1 533 . 88 LYS CA C 56.7 0.05 1 534 . 88 LYS HA H 4.20 0.02 1 535 . 88 LYS CB C 32.9 0.05 1 536 . 88 LYS HB3 H 1.55 0.02 2 537 . 88 LYS C C 176.5 0.05 1 538 . 89 PHE N N 118.8 0.05 1 539 . 89 PHE H H 8.04 0.02 1 540 . 89 PHE CA C 57.9 0.05 1 541 . 89 PHE HA H 4.57 0.02 1 542 . 89 PHE CB C 39.8 0.05 1 543 . 89 PHE HB2 H 2.86 0.02 2 544 . 89 PHE HB3 H 3.11 0.02 2 545 . 89 PHE C C 176.3 0.05 1 546 . 90 GLY N N 109.2 0.05 1 547 . 90 GLY H H 8.15 0.02 1 548 . 90 GLY CA C 45.9 0.05 1 549 . 90 GLY HA2 H 3.88 0.02 2 550 . 90 GLY C C 175.0 0.05 1 551 . 91 GLY N N 107.6 0.05 1 552 . 91 GLY H H 8.15 0.02 1 553 . 91 GLY C C 174.1 0.05 1 554 . 92 GLY N N 108.3 0.05 1 555 . 92 GLY H H 8.24 0.02 1 556 . 92 GLY HA2 H 3.93 0.02 2 557 . 93 GLY N N 121.0 0.05 1 558 . 93 GLY H H 8.13 0.02 1 559 . 93 GLY CA C 45.5 0.05 1 560 . 94 TYR N N 119.8 0.05 1 561 . 94 TYR H H 7.99 0.02 1 562 . 94 TYR CA C 58.3 0.05 1 563 . 94 TYR HA H 4.49 0.02 1 564 . 94 TYR CB C 39.1 0.05 1 565 . 94 TYR HB3 H 2.94 0.02 2 566 . 94 TYR C C 175.7 0.05 1 567 . 95 LYS N N 122.7 0.05 1 568 . 95 LYS H H 8.13 0.02 1 569 . 95 LYS CA C 56.4 0.05 1 570 . 95 LYS HA H 4.28 0.02 1 571 . 95 LYS CB C 33.4 0.05 1 572 . 95 LYS HB3 H 1.70 0.02 2 573 . 95 LYS C C 176.3 0.05 1 574 . 96 VAL N N 120.0 0.05 1 575 . 96 VAL H H 8.02 0.02 1 576 . 96 VAL CA C 62.5 0.05 1 577 . 96 VAL HA H 4.09 0.02 1 578 . 96 VAL CB C 33.0 0.05 1 579 . 96 VAL HB H 2.05 0.02 1 580 . 96 VAL C C 176.3 0.05 1 581 . 97 SER N N 118.3 0.05 1 582 . 97 SER H H 8.29 0.02 1 583 . 97 SER CA C 58.7 0.05 1 584 . 97 SER HA H 4.43 0.02 1 585 . 97 SER CB C 64.0 0.05 1 586 . 97 SER HB3 H 3.86 0.02 2 587 . 97 SER C C 175.2 0.05 1 588 . 98 GLY N N 110.6 0.05 1 589 . 98 GLY H H 8.38 0.02 1 590 . 98 GLY CA C 45.8 0.05 1 591 . 98 GLY HA2 H 3.97 0.02 2 592 . 98 GLY C C 175.0 0.05 1 593 . 99 GLY N N 108.3 0.05 1 594 . 99 GLY H H 8.34 0.02 1 595 . 99 GLY CA C 45.6 0.05 1 596 . 99 GLY C C 174.2 0.05 1 597 . 100 LEU N N 121.0 0.05 1 598 . 100 LEU H H 8.14 0.02 1 599 . 100 LEU CA C 55.5 0.05 1 600 . 100 LEU HA H 4.29 0.02 1 601 . 100 LEU CB C 42.6 0.05 1 602 . 100 LEU HB2 H 1.49 0.02 1 603 . 100 LEU HB3 H 1.49 0.02 1 604 . 100 LEU C C 177.2 0.05 1 605 . 101 HIS N N 118.1 0.05 1 606 . 101 HIS H H 8.39 0.02 1 607 . 101 HIS CA C 55.8 0.05 1 608 . 101 HIS HA H 4.76 0.02 1 609 . 101 HIS C C 175.5 0.05 1 610 . 102 GLY N N 109.6 0.05 1 611 . 102 GLY H H 8.56 0.02 1 612 . 102 GLY CA C 46.2 0.05 1 613 . 102 GLY HA2 H 4.09 0.02 1 614 . 102 GLY HA3 H 4.09 0.02 1 615 . 102 GLY C C 175.1 0.05 1 616 . 103 VAL N N 116.7 0.05 1 617 . 103 VAL H H 8.31 0.02 1 618 . 103 VAL CA C 62.8 0.05 1 619 . 103 VAL HA H 4.37 0.02 1 620 . 103 VAL C C 176.9 0.05 1 621 . 104 GLY N N 110.0 0.05 1 622 . 104 GLY H H 8.53 0.02 1 623 . 104 GLY CA C 46.3 0.05 1 624 . 104 GLY HA2 H 4.28 0.02 2 625 . 104 GLY C C 175.3 0.05 1 626 . 105 SER N N 115.6 0.05 1 627 . 105 SER H H 8.38 0.02 1 628 . 105 SER CA C 62.8 0.05 1 629 . 105 SER CB C 63.0 0.05 1 630 . 105 SER HB3 H 3.56 0.02 2 631 . 105 SER C C 175.6 0.05 1 632 . 106 SER N N 115.8 0.05 1 633 . 106 SER H H 8.04 0.02 1 634 . 106 SER CA C 60.4 0.05 1 635 . 106 SER HA H 4.14 0.02 1 636 . 106 SER CB C 62.5 0.05 1 637 . 106 SER HB3 H 3.58 0.02 2 638 . 106 SER C C 176.4 0.05 1 639 . 107 VAL N N 122.9 0.05 1 640 . 107 VAL H H 7.05 0.02 1 641 . 107 VAL CA C 66.6 0.05 1 642 . 107 VAL HA H 3.30 0.02 1 643 . 107 VAL C C 176.8 0.05 1 644 . 108 VAL N N 117.0 0.05 1 645 . 108 VAL H H 7.04 0.02 1 646 . 108 VAL CA C 66.5 0.05 1 647 . 108 VAL HA H 3.15 0.02 1 648 . 108 VAL CB C 31.0 0.05 1 649 . 108 VAL C C 178.4 0.05 1 650 . 109 ASN N N 116.6 0.05 1 651 . 109 ASN H H 7.54 0.02 1 652 . 109 ASN CA C 55.4 0.05 1 653 . 109 ASN HA H 4.12 0.02 1 654 . 109 ASN CB C 38.3 0.05 1 655 . 109 ASN HB2 H 2.95 0.02 2 656 . 109 ASN HB3 H 2.39 0.02 2 657 . 109 ASN C C 176.9 0.05 1 658 . 110 ALA N N 117.1 0.05 1 659 . 110 ALA H H 7.97 0.02 1 660 . 110 ALA CA C 55.0 0.05 1 661 . 110 ALA HA H 3.38 0.02 1 662 . 110 ALA HB H 1.33 0.02 1 663 . 110 ALA CB C 19.5 0.05 1 664 . 110 ALA C C 177.2 0.05 1 665 . 111 LEU N N 111.3 0.05 1 666 . 111 LEU H H 7.05 0.02 1 667 . 111 LEU CA C 53.9 0.05 1 668 . 111 LEU HA H 4.16 0.02 1 669 . 111 LEU CB C 40.9 0.05 1 670 . 111 LEU HB2 H 2.06 0.02 2 671 . 111 LEU HB3 H 1.80 0.02 2 672 . 111 LEU C C 174.3 0.05 1 673 . 112 SER N N 115.4 0.05 1 674 . 112 SER H H 7.54 0.02 1 675 . 112 SER CA C 59.7 0.05 1 676 . 112 SER HA H 4.83 0.02 1 677 . 112 SER CB C 64.1 0.05 1 678 . 112 SER C C 175.3 0.05 1 679 . 113 GLN N N 123.7 0.05 1 680 . 113 GLN H H 8.53 0.02 1 681 . 113 GLN CA C 58.3 0.05 1 682 . 113 GLN HA H 4.03 0.02 1 683 . 113 GLN CB C 29.7 0.05 1 684 . 113 GLN HB3 H 1.93 0.02 2 685 . 113 GLN C C 175.4 0.05 1 686 . 114 ASP N N 114.2 0.05 1 687 . 114 ASP H H 7.06 0.02 1 688 . 114 ASP CA C 54.5 0.05 1 689 . 114 ASP HA H 5.58 0.02 1 690 . 114 ASP CB C 49.0 0.05 1 691 . 114 ASP HB2 H 2.18 0.02 2 692 . 114 ASP HB3 H 2.87 0.02 2 693 . 114 ASP C C 173.9 0.05 1 694 . 115 LEU N N 122.2 0.05 1 695 . 115 LEU H H 8.50 0.02 1 696 . 115 LEU CA C 56.7 0.05 1 697 . 115 LEU HA H 5.47 0.02 1 698 . 115 LEU CB C 44.5 0.05 1 699 . 115 LEU HB3 H 1.78 0.02 2 700 . 115 LEU C C 174.8 0.05 1 701 . 116 GLU N N 124.1 0.05 1 702 . 116 GLU H H 10.40 0.02 1 703 . 116 GLU CA C 55.0 0.05 1 704 . 116 GLU HA H 5.18 0.02 1 705 . 116 GLU CB C 35.7 0.05 1 706 . 116 GLU C C 173.7 0.05 1 707 . 117 VAL N N 119.2 0.05 1 708 . 117 VAL H H 8.72 0.02 1 709 . 117 VAL CA C 58.4 0.05 1 710 . 117 VAL HA H 5.77 0.02 1 711 . 117 VAL CB C 36.1 0.05 1 712 . 117 VAL HB H 1.86 0.02 1 713 . 117 VAL C C 174.4 0.05 1 714 . 118 TYR N N 126.8 0.05 1 715 . 118 TYR H H 9.73 0.02 1 716 . 118 TYR CA C 56.9 0.05 1 717 . 118 TYR HA H 5.76 0.02 1 718 . 118 TYR CB C 40.5 0.05 1 719 . 118 TYR HB2 H 2.91 0.02 1 720 . 118 TYR HB3 H 2.91 0.02 1 721 . 118 TYR C C 175.0 0.05 1 722 . 119 VAL N N 123.1 0.05 1 723 . 119 VAL H H 9.58 0.02 1 724 . 119 VAL CA C 62.4 0.05 1 725 . 119 VAL HA H 4.78 0.02 1 726 . 119 VAL CB C 35.8 0.05 1 727 . 119 VAL C C 174.8 0.05 1 728 . 120 HIS N N 129.6 0.05 1 729 . 120 HIS H H 9.55 0.02 1 730 . 120 HIS CA C 55.5 0.05 1 731 . 120 HIS HA H 5.14 0.02 1 732 . 120 HIS CB C 29.9 0.05 1 733 . 120 HIS C C 173.8 0.05 1 734 . 121 ARG N N 122.1 0.05 1 735 . 121 ARG H H 9.04 0.02 1 736 . 121 ARG CA C 57.2 0.05 1 737 . 121 ARG HA H 4.57 0.02 1 738 . 121 ARG CB C 34.1 0.05 1 739 . 121 ARG C C 175.5 0.05 1 740 . 122 ASN N N 122.2 0.05 1 741 . 122 ASN H H 9.59 0.02 1 742 . 122 ASN CA C 55.1 0.05 1 743 . 122 ASN HA H 4.40 0.02 1 744 . 122 ASN CB C 37.9 0.05 1 745 . 122 ASN HB3 H 3.14 0.02 2 746 . 122 ASN C C 176.1 0.05 1 747 . 123 GLU N N 111.2 0.05 1 748 . 123 GLU H H 9.10 0.02 1 749 . 123 GLU CA C 58.8 0.05 1 750 . 123 GLU CB C 27.2 0.05 1 751 . 123 GLU HB2 H 2.35 0.02 2 752 . 123 GLU HB3 H 2.53 0.02 2 753 . 123 GLU C C 176.2 0.05 1 754 . 124 THR N N 119.7 0.05 1 755 . 124 THR H H 8.03 0.02 1 756 . 124 THR CA C 62.4 0.05 1 757 . 124 THR HA H 4.60 0.02 1 758 . 124 THR CB C 72.3 0.05 1 759 . 124 THR HB H 3.95 0.02 1 760 . 124 THR C C 169.7 0.05 1 761 . 125 ILE N N 121.9 0.05 1 762 . 125 ILE H H 7.58 0.02 1 763 . 125 ILE CA C 60.0 0.05 1 764 . 125 ILE HA H 4.76 0.02 1 765 . 125 ILE CB C 38.8 0.05 1 766 . 125 ILE HB H 1.11 0.02 1 767 . 125 ILE C C 175.0 0.05 1 768 . 126 TYR N N 127.2 0.05 1 769 . 126 TYR H H 9.74 0.02 1 770 . 126 TYR CA C 56.4 0.05 1 771 . 126 TYR HA H 5.46 0.02 1 772 . 126 TYR CB C 41.2 0.05 1 773 . 126 TYR HB3 H 2.81 0.02 2 774 . 126 TYR C C 176.3 0.05 1 775 . 127 HIS N N 120.7 0.05 1 776 . 127 HIS H H 9.63 0.02 1 777 . 127 HIS CA C 53.9 0.05 1 778 . 127 HIS HA H 5.79 0.02 1 779 . 127 HIS CB C 35.3 0.05 1 780 . 127 HIS HB2 H 2.82 0.02 1 781 . 127 HIS HB3 H 2.82 0.02 1 782 . 127 HIS C C 173.2 0.05 1 783 . 128 GLN N N 125.4 0.05 1 784 . 128 GLN H H 7.70 0.02 1 785 . 128 GLN CA C 56.3 0.05 1 786 . 128 GLN CB C 33.2 0.05 1 787 . 129 ALA CA C 50.1 0.05 1 788 . 129 ALA HA H 5.18 0.02 1 789 . 129 ALA HB H 1.32 0.02 1 790 . 129 ALA CB C 23.3 0.05 1 791 . 129 ALA C C 174.9 0.05 1 792 . 130 TYR N N 117.7 0.05 1 793 . 130 TYR H H 9.44 0.02 1 794 . 130 TYR CA C 55.9 0.05 1 795 . 130 TYR HA H 5.13 0.02 1 796 . 130 TYR CB C 43.5 0.05 1 797 . 130 TYR HB2 H 2.34 0.02 2 798 . 130 TYR HB3 H 2.96 0.02 2 799 . 130 TYR C C 175.9 0.05 1 800 . 131 LYS N N 119.5 0.05 1 801 . 131 LYS H H 8.21 0.02 1 802 . 131 LYS CA C 57.2 0.05 1 803 . 131 LYS HA H 4.98 0.02 1 804 . 131 LYS CB C 37.0 0.05 1 805 . 131 LYS HB3 H 1.68 0.02 2 806 . 131 LYS C C 177.4 0.05 1 807 . 132 LYS N N 125.6 0.05 1 808 . 132 LYS H H 7.86 0.02 1 809 . 132 LYS CA C 57.5 0.05 1 810 . 132 LYS HA H 4.00 0.02 1 811 . 132 LYS CB C 31.0 0.05 1 812 . 132 LYS C C 175.5 0.05 1 813 . 133 GLY N N 102.9 0.05 1 814 . 133 GLY H H 8.48 0.02 1 815 . 133 GLY CA C 44.7 0.05 1 816 . 133 GLY HA2 H 2.95 0.02 2 817 . 133 GLY HA3 H 3.86 0.02 2 818 . 133 GLY C C 173.5 0.05 1 819 . 134 VAL N N 121.7 0.05 1 820 . 134 VAL H H 7.95 0.02 1 821 . 134 VAL CA C 59.9 0.05 1 822 . 134 VAL CB C 33.9 0.05 1 823 . 135 PRO CA C 63.4 0.05 1 824 . 135 PRO HA H 4.13 0.02 1 825 . 135 PRO CB C 31.8 0.05 1 826 . 135 PRO HB3 H 1.77 0.02 2 827 . 135 PRO C C 177.1 0.05 1 828 . 136 GLN N N 120.3 0.05 1 829 . 136 GLN H H 8.69 0.02 1 830 . 136 GLN CA C 55.2 0.05 1 831 . 136 GLN HA H 4.09 0.02 1 832 . 136 GLN CB C 31.2 0.05 1 833 . 136 GLN HB3 H 2.31 0.02 2 834 . 136 GLN C C 174.7 0.05 1 835 . 137 PHE N N 111.5 0.05 1 836 . 137 PHE H H 6.99 0.02 1 837 . 137 PHE CA C 54.8 0.05 1 838 . 137 PHE HA H 4.59 0.02 1 839 . 137 PHE CB C 39.3 0.05 1 840 . 137 PHE HB3 H 3.23 0.02 2 841 . 137 PHE C C 174.4 0.05 1 842 . 138 ASP N N 119.6 0.05 1 843 . 138 ASP H H 8.57 0.02 1 844 . 138 ASP CA C 54.8 0.05 1 845 . 138 ASP HA H 4.45 0.02 1 846 . 138 ASP CB C 41.3 0.05 1 847 . 138 ASP HB3 H 2.77 0.02 2 848 . 138 ASP C C 175.4 0.05 1 849 . 139 LEU N N 121.5 0.05 1 850 . 139 LEU H H 8.81 0.02 1 851 . 139 LEU CA C 56.9 0.05 1 852 . 139 LEU HA H 4.00 0.02 1 853 . 139 LEU CB C 44.0 0.05 1 854 . 139 LEU HB2 H 1.27 0.02 2 855 . 139 LEU HB3 H 1.86 0.02 2 856 . 139 LEU C C 176.4 0.05 1 857 . 140 LYS N N 126.3 0.05 1 858 . 140 LYS H H 8.94 0.02 1 859 . 140 LYS CA C 54.7 0.05 1 860 . 140 LYS HA H 4.95 0.02 1 861 . 140 LYS CB C 36.7 0.05 1 862 . 140 LYS HB3 H 1.87 0.02 2 863 . 140 LYS C C 175.7 0.05 1 864 . 141 GLU N N 122.2 0.05 1 865 . 141 GLU H H 8.68 0.02 1 866 . 141 GLU CA C 55.8 0.05 1 867 . 141 GLU HA H 4.76 0.02 1 868 . 141 GLU CB C 29.8 0.05 1 869 . 141 GLU HB2 H 1.92 0.02 2 870 . 141 GLU HB3 H 1.82 0.02 2 871 . 141 GLU C C 178.2 0.05 1 872 . 142 VAL N N 115.1 0.05 1 873 . 142 VAL H H 8.96 0.02 1 874 . 142 VAL CA C 60.8 0.05 1 875 . 142 VAL HA H 4.65 0.02 1 876 . 142 VAL CB C 32.9 0.05 1 877 . 142 VAL HB H 2.45 0.02 1 878 . 142 VAL C C 175.6 0.05 1 879 . 143 GLY N N 107.6 0.05 1 880 . 143 GLY H H 7.30 0.02 1 881 . 143 GLY CA C 45.2 0.05 1 882 . 143 GLY HA2 H 4.05 0.02 2 883 . 143 GLY HA3 H 4.29 0.02 2 884 . 143 GLY C C 172.0 0.05 1 885 . 144 THR N N 112.1 0.05 1 886 . 144 THR H H 8.19 0.02 1 887 . 144 THR CA C 60.7 0.05 1 888 . 144 THR HA H 4.96 0.02 1 889 . 144 THR CB C 71.3 0.05 1 890 . 144 THR HB H 4.22 0.02 1 891 . 144 THR C C 172.7 0.05 1 892 . 145 THR N N 113.9 0.05 1 893 . 145 THR H H 7.42 0.02 1 894 . 145 THR CA C 59.3 0.05 1 895 . 145 THR HA H 4.67 0.02 1 896 . 145 THR CB C 69.5 0.05 1 897 . 145 THR HB H 3.83 0.02 1 898 . 145 THR C C 171.2 0.05 1 899 . 146 ASP N N 123.0 0.05 1 900 . 146 ASP H H 7.91 0.02 1 901 . 146 ASP CA C 52.6 0.05 1 902 . 146 ASP HA H 4.87 0.02 1 903 . 146 ASP CB C 41.0 0.05 1 904 . 146 ASP HB2 H 2.95 0.02 2 905 . 146 ASP HB3 H 2.50 0.02 2 906 . 146 ASP C C 175.7 0.05 1 907 . 147 LYS N N 121.1 0.05 1 908 . 147 LYS H H 8.35 0.02 1 909 . 147 LYS CA C 54.8 0.05 1 910 . 147 LYS HA H 4.73 0.02 1 911 . 147 LYS CB C 35.3 0.05 1 912 . 147 LYS HB2 H 1.70 0.02 2 913 . 147 LYS C C 175.1 0.05 1 914 . 148 THR N N 107.3 0.05 1 915 . 148 THR H H 7.68 0.02 1 916 . 148 THR CA C 60.0 0.05 1 917 . 148 THR HA H 5.10 0.02 1 918 . 148 THR CB C 71.9 0.05 1 919 . 148 THR C C 174.7 0.05 1 920 . 149 GLY N N 109.8 0.05 1 921 . 149 GLY H H 8.62 0.02 1 922 . 149 GLY CA C 45.2 0.05 1 923 . 149 GLY HA2 H 3.43 0.02 2 924 . 149 GLY HA3 H 5.20 0.02 2 925 . 149 GLY C C 172.4 0.05 1 926 . 150 THR N N 115.6 0.05 1 927 . 150 THR H H 7.41 0.02 1 928 . 150 THR CA C 63.5 0.05 1 929 . 150 THR HA H 5.07 0.02 1 930 . 150 THR CB C 71.5 0.05 1 931 . 150 THR C C 173.1 0.05 1 932 . 151 VAL N N 126.6 0.05 1 933 . 151 VAL H H 9.31 0.02 1 934 . 151 VAL CA C 61.2 0.05 1 935 . 151 VAL HA H 5.10 0.02 1 936 . 151 VAL CB C 35.1 0.05 1 937 . 151 VAL C C 175.7 0.05 1 938 . 152 ILE N N 126.6 0.05 1 939 . 152 ILE H H 9.03 0.02 1 940 . 152 ILE CA C 60.0 0.05 1 941 . 152 ILE HA H 5.25 0.02 1 942 . 152 ILE CB C 40.7 0.05 1 943 . 152 ILE HB H 1.85 0.02 1 944 . 152 ILE C C 174.8 0.05 1 945 . 153 ARG N N 126.5 0.05 1 946 . 153 ARG H H 9.41 0.02 1 947 . 153 ARG CA C 53.9 0.05 1 948 . 153 ARG CB C 35.2 0.05 1 949 . 153 ARG HB2 H 2.06 0.02 2 950 . 153 ARG C C 175.7 0.05 1 951 . 154 PHE N N 120.4 0.05 1 952 . 154 PHE H H 9.61 0.02 1 953 . 154 PHE CA C 57.0 0.05 1 954 . 154 PHE HA H 5.70 0.02 1 955 . 154 PHE CB C 43.1 0.05 1 956 . 154 PHE C C 173.1 0.05 1 957 . 155 LYS N N 125.2 0.05 1 958 . 155 LYS H H 8.59 0.02 1 959 . 155 LYS CA C 53.5 0.05 1 960 . 155 LYS HA H 4.35 0.02 1 961 . 155 LYS CB C 33.1 0.05 1 962 . 155 LYS C C 174.8 0.05 1 963 . 156 ALA N N 130.9 0.05 1 964 . 156 ALA H H 8.21 0.02 1 965 . 156 ALA CA C 53.5 0.05 1 966 . 156 ALA HA H 4.25 0.02 1 967 . 156 ALA HB H 1.18 0.02 1 968 . 156 ALA CB C 20.2 0.05 1 969 . 156 ALA C C 176.1 0.05 1 970 . 157 ASP N N 119.0 0.05 1 971 . 157 ASP H H 8.86 0.02 1 972 . 157 ASP CA C 55.2 0.05 1 973 . 157 ASP HA H 4.63 0.02 1 974 . 157 ASP CB C 42.1 0.05 1 975 . 157 ASP HB2 H 2.92 0.02 2 976 . 157 ASP HB3 H 2.30 0.02 2 977 . 157 ASP C C 178.3 0.05 1 978 . 158 GLY N N 119.3 0.05 1 979 . 158 GLY H H 9.16 0.02 1 980 . 158 GLY CA C 46.9 0.05 1 981 . 158 GLY HA2 H 3.94 0.02 2 982 . 158 GLY C C 174.4 0.05 1 983 . 159 GLU N N 117.8 0.05 1 984 . 159 GLU H H 8.77 0.02 1 985 . 159 GLU CA C 57.8 0.05 1 986 . 159 GLU HA H 4.06 0.02 1 987 . 159 GLU CB C 30.0 0.05 1 988 . 159 GLU HB3 H 1.93 0.02 2 989 . 159 GLU C C 177.1 0.05 1 990 . 160 ILE N N 117.3 0.05 1 991 . 160 ILE H H 7.21 0.02 1 992 . 160 ILE CA C 60.8 0.05 1 993 . 160 ILE CB C 38.1 0.05 1 994 . 160 ILE C C 175.9 0.05 1 995 . 161 PHE N N 120.2 0.05 1 996 . 161 PHE H H 7.95 0.02 1 997 . 161 PHE CA C 57.6 0.05 1 998 . 161 PHE HA H 4.72 0.02 1 999 . 161 PHE CB C 38.0 0.05 1 1000 . 161 PHE HB2 H 2.52 0.02 2 1001 . 161 PHE C C 175.1 0.05 1 1002 . 162 THR N N 109.2 0.05 1 1003 . 162 THR H H 7.38 0.02 1 1004 . 162 THR CA C 63.1 0.05 1 1005 . 162 THR HA H 4.05 0.02 1 1006 . 162 THR CB C 69.4 0.05 1 1007 . 162 THR HB H 4.29 0.02 1 1008 . 162 THR C C 176.3 0.05 1 1009 . 163 GLU N N 123.6 0.05 1 1010 . 163 GLU H H 8.18 0.02 1 1011 . 163 GLU CA C 59.1 0.05 1 1012 . 163 GLU HA H 4.24 0.02 1 1013 . 163 GLU CB C 30.2 0.05 1 1014 . 163 GLU HB3 H 2.20 0.02 2 1015 . 163 GLU C C 177.0 0.05 1 1016 . 164 THR N N 111.0 0.05 1 1017 . 164 THR H H 7.84 0.02 1 1018 . 164 THR CA C 60.9 0.05 1 1019 . 164 THR HA H 4.58 0.02 1 1020 . 164 THR CB C 68.6 0.05 1 1021 . 164 THR HB H 4.41 0.02 1 1022 . 164 THR C C 171.4 0.05 1 1023 . 165 THR N N 113.7 0.05 1 1024 . 165 THR H H 7.76 0.02 1 1025 . 165 THR CA C 60.7 0.05 1 1026 . 165 THR HA H 4.40 0.02 1 1027 . 165 THR CB C 68.4 0.05 1 1028 . 165 THR HB H 4.21 0.02 1 1029 . 165 THR C C 172.7 0.05 1 1030 . 166 VAL N N 122.7 0.05 1 1031 . 166 VAL H H 7.89 0.02 1 1032 . 166 VAL CA C 61.7 0.05 1 1033 . 166 VAL HA H 3.68 0.02 1 1034 . 166 VAL CB C 33.1 0.05 1 1035 . 166 VAL HB H 1.83 0.02 1 1036 . 166 VAL C C 175.5 0.05 1 1037 . 167 TYR N N 123.1 0.05 1 1038 . 167 TYR H H 6.68 0.02 1 1039 . 167 TYR CA C 59.7 0.05 1 1040 . 167 TYR HA H 4.11 0.02 1 1041 . 167 TYR CB C 40.3 0.05 1 1042 . 167 TYR C C 175.8 0.05 1 1043 . 168 ASN N N 125.7 0.05 1 1044 . 168 ASN H H 11.86 0.02 1 1045 . 168 ASN CA C 52.6 0.05 1 1046 . 168 ASN HA H 5.05 0.02 1 1047 . 168 ASN CB C 40.3 0.05 1 1048 . 168 ASN HB2 H 3.11 0.02 2 1049 . 168 ASN HB3 H 2.85 0.02 2 1050 . 168 ASN C C 175.4 0.05 1 1051 . 169 TYR N N 127.5 0.05 1 1052 . 169 TYR H H 9.51 0.02 1 1053 . 169 TYR CA C 63.9 0.05 1 1054 . 169 TYR CB C 40.0 0.05 1 1055 . 169 TYR HB2 H 2.95 0.02 2 1056 . 169 TYR HB3 H 3.74 0.02 2 1057 . 169 TYR C C 176.6 0.05 1 1058 . 170 GLU N N 116.8 0.05 1 1059 . 170 GLU H H 8.59 0.02 1 1060 . 170 GLU CA C 60.9 0.05 1 1061 . 170 GLU HA H 4.09 0.02 1 1062 . 170 GLU CB C 28.9 0.05 1 1063 . 170 GLU HB2 H 2.31 0.02 2 1064 . 170 GLU HB3 H 2.10 0.02 2 1065 . 170 GLU C C 179.3 0.05 1 1066 . 171 THR N N 118.0 0.05 1 1067 . 171 THR H H 7.91 0.02 1 1068 . 171 THR CA C 66.5 0.05 1 1069 . 171 THR HA H 4.22 0.02 1 1070 . 171 THR CB C 68.7 0.05 1 1071 . 171 THR HB H 3.86 0.02 1 1072 . 171 THR C C 177.5 0.05 1 1073 . 172 LEU N N 120.3 0.05 1 1074 . 172 LEU H H 7.67 0.02 1 1075 . 172 LEU CA C 58.8 0.05 1 1076 . 172 LEU HA H 4.49 0.02 1 1077 . 172 LEU CB C 42.0 0.05 1 1078 . 172 LEU HB3 H 1.32 0.02 2 1079 . 172 LEU C C 177.7 0.05 1 1080 . 173 GLN N N 120.3 0.05 1 1081 . 173 GLN H H 9.14 0.02 1 1082 . 173 GLN CA C 60.1 0.05 1 1083 . 173 GLN HA H 3.45 0.02 1 1084 . 173 GLN CB C 29.8 0.05 1 1085 . 173 GLN HB3 H 1.76 0.02 2 1086 . 173 GLN C C 177.2 0.05 1 1087 . 174 GLN N N 115.5 0.05 1 1088 . 174 GLN H H 7.96 0.02 1 1089 . 174 GLN CA C 59.1 0.05 1 1090 . 174 GLN HA H 3.80 0.02 1 1091 . 174 GLN CB C 28.4 0.05 1 1092 . 174 GLN HB3 H 2.08 0.02 2 1093 . 174 GLN C C 178.3 0.05 1 1094 . 175 ARG N N 117.4 0.05 1 1095 . 175 ARG H H 6.94 0.02 1 1096 . 175 ARG CA C 57.2 0.05 1 1097 . 175 ARG HA H 4.00 0.02 1 1098 . 175 ARG CB C 29.8 0.05 1 1099 . 175 ARG HB2 H 1.67 0.02 2 1100 . 175 ARG HB3 H 1.44 0.02 2 1101 . 175 ARG C C 178.0 0.05 1 1102 . 176 ILE N N 119.9 0.05 1 1103 . 176 ILE H H 8.46 0.02 1 1104 . 176 ILE CA C 65.7 0.05 1 1105 . 176 ILE HA H 3.62 0.02 1 1106 . 176 ILE CB C 36.8 0.05 1 1107 . 176 ILE HB H 2.04 0.02 1 1108 . 176 ILE C C 176.7 0.05 1 1109 . 177 ARG N N 120.0 0.05 1 1110 . 177 ARG H H 7.93 0.02 1 1111 . 177 ARG CA C 60.4 0.05 1 1112 . 177 ARG HA H 3.13 0.02 1 1113 . 177 ARG CB C 29.5 0.05 1 1114 . 177 ARG C C 178.2 0.05 1 1115 . 178 GLU N N 117.5 0.05 1 1116 . 178 GLU H H 7.07 0.02 1 1117 . 178 GLU CA C 59.5 0.05 1 1118 . 178 GLU HA H 3.89 0.02 1 1119 . 178 GLU CB C 29.9 0.05 1 1120 . 178 GLU HB2 H 2.01 0.02 2 1121 . 178 GLU C C 179.2 0.05 1 1122 . 179 LEU N N 118.8 0.05 1 1123 . 179 LEU H H 8.54 0.02 1 1124 . 179 LEU CA C 58.1 0.05 1 1125 . 179 LEU HA H 3.84 0.02 1 1126 . 179 LEU CB C 43.1 0.05 1 1127 . 179 LEU HB3 H 1.96 0.02 2 1128 . 179 LEU C C 180.0 0.05 1 1129 . 180 ALA N N 121.6 0.05 1 1130 . 180 ALA H H 8.32 0.02 1 1131 . 180 ALA CA C 54.9 0.05 1 1132 . 180 ALA HA H 4.06 0.02 1 1133 . 180 ALA HB H 1.63 0.02 1 1134 . 180 ALA CB C 18.5 0.05 1 1135 . 180 ALA C C 178.2 0.05 1 1136 . 181 PHE N N 118.0 0.05 1 1137 . 181 PHE H H 8.03 0.02 1 1138 . 181 PHE CA C 61.0 0.05 1 1139 . 181 PHE HA H 3.60 0.02 1 1140 . 181 PHE CB C 39.1 0.05 1 1141 . 181 PHE HB2 H 2.80 0.02 2 1142 . 181 PHE C C 176.8 0.05 1 1143 . 182 LEU N N 116.7 0.05 1 1144 . 182 LEU H H 8.11 0.02 1 1145 . 182 LEU CA C 56.4 0.05 1 1146 . 182 LEU HA H 3.99 0.02 1 1147 . 182 LEU CB C 43.4 0.05 1 1148 . 182 LEU HB2 H 1.46 0.02 2 1149 . 182 LEU HB3 H 1.65 0.02 2 1150 . 182 LEU C C 177.6 0.05 1 1151 . 183 ASN N N 119.7 0.05 1 1152 . 183 ASN H H 7.42 0.02 1 1153 . 183 ASN CA C 51.7 0.05 1 1154 . 183 ASN HA H 4.86 0.02 1 1155 . 183 ASN CB C 39.4 0.05 1 1156 . 183 ASN HB2 H 2.25 0.02 2 1157 . 183 ASN HB3 H 2.78 0.02 2 1158 . 183 ASN C C 172.1 0.05 1 1159 . 184 LYS N N 115.4 0.05 1 1160 . 184 LYS H H 7.19 0.02 1 1161 . 184 LYS CA C 58.3 0.05 1 1162 . 184 LYS HA H 4.06 0.02 1 1163 . 184 LYS CB C 32.5 0.05 1 1164 . 184 LYS HB3 H 1.58 0.02 2 1165 . 184 LYS C C 177.9 0.05 1 1166 . 185 GLY N N 110.0 0.05 1 1167 . 185 GLY H H 8.53 0.02 1 1168 . 185 GLY CA C 45.4 0.05 1 1169 . 185 GLY HA2 H 3.78 0.02 2 1170 . 185 GLY HA3 H 4.41 0.02 2 1171 . 185 GLY C C 174.4 0.05 1 1172 . 186 ILE N N 118.9 0.05 1 1173 . 186 ILE H H 7.75 0.02 1 1174 . 186 ILE CA C 60.6 0.05 1 1175 . 186 ILE HA H 4.35 0.02 1 1176 . 186 ILE CB C 39.2 0.05 1 1177 . 186 ILE HB H 1.85 0.02 1 1178 . 186 ILE C C 175.1 0.05 1 1179 . 187 GLN N N 127.0 0.05 1 1180 . 187 GLN H H 8.08 0.02 1 1181 . 187 GLN CA C 54.9 0.05 1 1182 . 187 GLN HA H 5.22 0.02 1 1183 . 187 GLN CB C 30.7 0.05 1 1184 . 187 GLN HB3 H 2.09 0.02 2 1185 . 187 GLN C C 175.0 0.05 1 1186 . 188 ILE N N 125.9 0.05 1 1187 . 188 ILE H H 8.97 0.02 1 1188 . 188 ILE CA C 60.4 0.05 1 1189 . 188 ILE HA H 5.47 0.02 1 1190 . 188 ILE CB C 40.3 0.05 1 1191 . 188 ILE HB H 1.73 0.02 1 1192 . 188 ILE C C 174.7 0.05 1 1193 . 189 THR N N 124.0 0.05 1 1194 . 189 THR H H 8.75 0.02 1 1195 . 189 THR CA C 61.9 0.05 1 1196 . 189 THR HA H 5.05 0.02 1 1197 . 189 THR CB C 71.9 0.05 1 1198 . 189 THR C C 171.3 0.05 1 1199 . 190 LEU N N 129.5 0.05 1 1200 . 190 LEU H H 9.21 0.02 1 1201 . 190 LEU CA C 53.1 0.05 1 1202 . 190 LEU HA H 5.68 0.02 1 1203 . 190 LEU CB C 46.4 0.05 1 1204 . 190 LEU C C 173.9 0.05 1 1205 . 191 ARG N N 124.4 0.05 1 1206 . 191 ARG H H 9.01 0.02 1 1207 . 191 ARG CA C 54.6 0.05 1 1208 . 191 ARG HA H 5.64 0.02 1 1209 . 191 ARG CB C 35.6 0.05 1 1210 . 191 ARG HB3 H 1.78 0.02 2 1211 . 191 ARG C C 173.8 0.05 1 1212 . 192 ASP N N 124.1 0.05 1 1213 . 192 ASP H H 9.59 0.02 1 1214 . 192 ASP CA C 52.8 0.05 1 1215 . 192 ASP HA H 5.29 0.02 1 1216 . 192 ASP CB C 43.1 0.05 1 1217 . 192 ASP HB2 H 2.85 0.02 2 1218 . 192 ASP HB3 H 2.97 0.02 2 1219 . 192 ASP C C 177.3 0.05 1 1220 . 193 GLU N N 125.3 0.05 1 1221 . 193 GLU H H 9.37 0.02 1 1222 . 193 GLU CA C 54.9 0.05 1 1223 . 193 GLU HA H 4.52 0.02 1 1224 . 193 GLU CB C 30.4 0.05 1 1225 . 193 GLU HB3 H 2.29 0.02 2 1226 . 193 GLU C C 176.1 0.05 1 1227 . 194 ARG N N 118.9 0.05 1 1228 . 194 ARG H H 8.29 0.02 1 1229 . 194 ARG CA C 61.0 0.05 1 1230 . 194 ARG HA H 3.67 0.02 1 1231 . 194 ARG CB C 30.9 0.05 1 1232 . 194 ARG C C 176.8 0.05 1 1233 . 195 ASP N N 117.3 0.05 1 1234 . 195 ASP H H 8.38 0.02 1 1235 . 195 ASP CA C 52.3 0.05 1 1236 . 195 ASP HA H 4.75 0.02 1 1237 . 195 ASP CB C 41.6 0.05 1 1238 . 195 ASP HB2 H 2.75 0.02 2 1239 . 195 ASP C C 176.9 0.05 1 1240 . 196 GLU N N 123.3 0.05 1 1241 . 196 GLU H H 8.81 0.02 1 1242 . 196 GLU CA C 59.1 0.05 1 1243 . 196 GLU HA H 3.84 0.02 1 1244 . 196 GLU CB C 29.6 0.05 1 1245 . 196 GLU HB3 H 2.03 0.02 2 1246 . 196 GLU C C 177.4 0.05 1 1247 . 197 GLU N N 116.2 0.05 1 1248 . 197 GLU H H 8.09 0.02 1 1249 . 197 GLU CA C 56.8 0.05 1 1250 . 197 GLU HA H 4.27 0.02 1 1251 . 197 GLU CB C 30.4 0.05 1 1252 . 197 GLU HB2 H 1.90 0.02 2 1253 . 197 GLU HB3 H 2.12 0.02 2 1254 . 197 GLU C C 176.2 0.05 1 1255 . 198 ASN N N 119.5 0.05 1 1256 . 198 ASN H H 7.75 0.02 1 1257 . 198 ASN CA C 52.3 0.05 1 1258 . 198 ASN HA H 4.83 0.02 1 1259 . 198 ASN CB C 40.1 0.05 1 1260 . 198 ASN HB2 H 2.31 0.02 2 1261 . 198 ASN HB3 H 2.53 0.02 2 1262 . 198 ASN C C 173.7 0.05 1 1263 . 199 VAL N N 124.6 0.05 1 1264 . 199 VAL H H 8.34 0.02 1 1265 . 199 VAL CA C 64.3 0.05 1 1266 . 199 VAL HA H 3.96 0.02 1 1267 . 199 VAL CB C 32.3 0.05 1 1268 . 199 VAL HB H 1.89 0.02 1 1269 . 199 VAL C C 176.2 0.05 1 1270 . 200 ARG N N 128.4 0.05 1 1271 . 200 ARG H H 7.60 0.02 1 1272 . 200 ARG CA C 55.0 0.05 1 1273 . 200 ARG HA H 4.64 0.02 1 1274 . 200 ARG CB C 33.8 0.05 1 1275 . 200 ARG HB2 H 1.42 0.02 2 1276 . 200 ARG HB3 H 1.53 0.02 2 1277 . 200 ARG C C 173.9 0.05 1 1278 . 201 GLU N N 124.3 0.05 1 1279 . 201 GLU H H 8.42 0.02 1 1280 . 201 GLU CA C 55.5 0.05 1 1281 . 201 GLU HA H 5.64 0.02 1 1282 . 201 GLU CB C 34.4 0.05 1 1283 . 201 GLU HB3 H 1.88 0.02 2 1284 . 201 GLU C C 174.4 0.05 1 1285 . 202 ASP N N 124.6 0.05 1 1286 . 202 ASP H H 9.25 0.02 1 1287 . 202 ASP CA C 54.5 0.05 1 1288 . 202 ASP HA H 4.90 0.02 1 1289 . 202 ASP CB C 47.3 0.05 1 1290 . 202 ASP HB3 H 2.43 0.02 2 1291 . 202 ASP C C 173.5 0.05 1 1292 . 203 SER N N 114.4 0.05 1 1293 . 203 SER H H 8.13 0.02 1 1294 . 203 SER CA C 57.1 0.05 1 1295 . 203 SER HA H 5.11 0.02 1 1296 . 203 SER CB C 65.3 0.05 1 1297 . 203 SER HB3 H 3.53 0.02 2 1298 . 203 SER C C 173.0 0.05 1 1299 . 204 TYR N N 123.2 0.05 1 1300 . 204 TYR H H 8.89 0.02 1 1301 . 204 TYR CA C 57.4 0.05 1 1302 . 204 TYR HA H 4.68 0.02 1 1303 . 204 TYR CB C 42.7 0.05 1 1304 . 204 TYR C C 174.3 0.05 1 1305 . 205 HIS N N 119.8 0.05 1 1306 . 205 HIS H H 8.11 0.02 1 1307 . 205 HIS CA C 55.9 0.05 1 1308 . 205 HIS HA H 4.83 0.02 1 1309 . 205 HIS CB C 31.4 0.05 1 1310 . 205 HIS HB3 H 2.93 0.02 2 1311 . 205 HIS C C 172.6 0.05 1 1312 . 206 TYR N N 128.0 0.05 1 1313 . 206 TYR H H 9.71 0.02 1 1314 . 206 TYR CA C 57.8 0.05 1 1315 . 206 TYR HA H 4.55 0.02 1 1316 . 206 TYR CB C 40.3 0.05 1 1317 . 206 TYR HB2 H 2.63 0.02 2 1318 . 206 TYR HB3 H 3.05 0.02 2 1319 . 206 TYR C C 174.8 0.05 1 1320 . 207 GLU N N 121.0 0.05 1 1321 . 207 GLU H H 8.43 0.02 1 1322 . 207 GLU CA C 56.5 0.05 1 1323 . 207 GLU HA H 4.21 0.02 1 1324 . 207 GLU CB C 31.4 0.05 1 1325 . 207 GLU HB2 H 1.89 0.02 2 1326 . 207 GLU HB3 H 2.00 0.02 2 1327 . 207 GLU C C 176.9 0.05 1 1328 . 208 GLY N N 109.1 0.05 1 1329 . 208 GLY H H 8.31 0.02 1 1330 . 208 GLY CA C 45.3 0.05 1 1331 . 208 GLY HA2 H 3.93 0.02 2 1332 . 208 GLY HA3 H 3.78 0.02 2 1333 . 208 GLY C C 174.8 0.05 1 1334 . 209 GLY N N 108.2 0.05 1 1335 . 209 GLY H H 8.22 0.02 1 1336 . 209 GLY CA C 45.5 0.05 1 1337 . 209 GLY HA2 H 3.94 0.02 2 1338 . 209 GLY C C 174.1 0.05 1 1339 . 210 ILE N N 120.0 0.05 1 1340 . 210 ILE H H 7.97 0.02 1 1341 . 210 ILE CA C 61.4 0.05 1 1342 . 210 ILE HA H 4.16 0.02 1 1343 . 210 ILE CB C 38.9 0.05 1 1344 . 210 ILE HB H 1.85 0.02 1 1345 . 210 ILE C C 175.5 0.05 1 1346 . 211 LYS N N 130.0 0.05 1 1347 . 211 LYS H H 7.88 0.02 1 1348 . 211 LYS CA C 57.8 0.05 1 1349 . 211 LYS CB C 34.0 0.05 1 stop_ save_