data_25231 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 14-3-3 Zeta Backbone Assignment ; _BMRB_accession_number 25231 _BMRB_flat_file_name bmr25231.str _Entry_type original _Submission_date 2014-09-16 _Accession_date 2014-09-16 _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 Killoran Ryan C. . 2 Fan Jingsong . . 3 Yang Daiwen . . 4 Choy Wing-Yiu . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 190 "13C chemical shifts" 377 "15N chemical shifts" 189 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-04-28 original BMRB . stop_ _Original_release_date 2015-04-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural Analysis of the 14-3-3 zeta /Chibby Interaction Involved in Wnt/ beta-Catenin Signaling ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25909186 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Killoran Ryan C. . 2 Fan Jingsong . . 3 Yang Daiwen . . 4 Shilton Brian H. . 5 Choy Wing-Yiu . . stop_ _Journal_abbreviation 'Plos One' _Journal_volume 10 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e0123934 _Page_last e0123934 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name '14-3-3 Zeta' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 14-3-3 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 234 _Mol_residue_sequence ; GMDKNELVQKAKLAEQAERY DDMAACMKSVTEQGAELSNE ERNLLSVAYKNVVGARRSSW RVVSSIEQKTEGAEKKQQMA REYREKIETELRDICNDVLS LLEKFLIPNASQAESKVFYL KMKGDYYRYLAEVAAGDDKK GIVDQSQQAYQEAFEISKKE MQPTHPIRLGLALNFSVFYY EILNSPEKACSLAKTAFDEA IAELDTLSEESYKDSTLIMQ LLRDNLTLWTSDTQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 GLY 2 1 MET 3 2 ASP 4 3 LYS 5 4 ASN 6 5 GLU 7 6 LEU 8 7 VAL 9 8 GLN 10 9 LYS 11 10 ALA 12 11 LYS 13 12 LEU 14 13 ALA 15 14 GLU 16 15 GLN 17 16 ALA 18 17 GLU 19 18 ARG 20 19 TYR 21 20 ASP 22 21 ASP 23 22 MET 24 23 ALA 25 24 ALA 26 25 CYS 27 26 MET 28 27 LYS 29 28 SER 30 29 VAL 31 30 THR 32 31 GLU 33 32 GLN 34 33 GLY 35 34 ALA 36 35 GLU 37 36 LEU 38 37 SER 39 38 ASN 40 39 GLU 41 40 GLU 42 41 ARG 43 42 ASN 44 43 LEU 45 44 LEU 46 45 SER 47 46 VAL 48 47 ALA 49 48 TYR 50 49 LYS 51 50 ASN 52 51 VAL 53 52 VAL 54 53 GLY 55 54 ALA 56 55 ARG 57 56 ARG 58 57 SER 59 58 SER 60 59 TRP 61 60 ARG 62 61 VAL 63 62 VAL 64 63 SER 65 64 SER 66 65 ILE 67 66 GLU 68 67 GLN 69 68 LYS 70 69 THR 71 70 GLU 72 71 GLY 73 72 ALA 74 73 GLU 75 74 LYS 76 75 LYS 77 76 GLN 78 77 GLN 79 78 MET 80 79 ALA 81 80 ARG 82 81 GLU 83 82 TYR 84 83 ARG 85 84 GLU 86 85 LYS 87 86 ILE 88 87 GLU 89 88 THR 90 89 GLU 91 90 LEU 92 91 ARG 93 92 ASP 94 93 ILE 95 94 CYS 96 95 ASN 97 96 ASP 98 97 VAL 99 98 LEU 100 99 SER 101 100 LEU 102 101 LEU 103 102 GLU 104 103 LYS 105 104 PHE 106 105 LEU 107 106 ILE 108 107 PRO 109 108 ASN 110 109 ALA 111 110 SER 112 111 GLN 113 112 ALA 114 113 GLU 115 114 SER 116 115 LYS 117 116 VAL 118 117 PHE 119 118 TYR 120 119 LEU 121 120 LYS 122 121 MET 123 122 LYS 124 123 GLY 125 124 ASP 126 125 TYR 127 126 TYR 128 127 ARG 129 128 TYR 130 129 LEU 131 130 ALA 132 131 GLU 133 132 VAL 134 133 ALA 135 134 ALA 136 135 GLY 137 136 ASP 138 137 ASP 139 138 LYS 140 139 LYS 141 140 GLY 142 141 ILE 143 142 VAL 144 143 ASP 145 144 GLN 146 145 SER 147 146 GLN 148 147 GLN 149 148 ALA 150 149 TYR 151 150 GLN 152 151 GLU 153 152 ALA 154 153 PHE 155 154 GLU 156 155 ILE 157 156 SER 158 157 LYS 159 158 LYS 160 159 GLU 161 160 MET 162 161 GLN 163 162 PRO 164 163 THR 165 164 HIS 166 165 PRO 167 166 ILE 168 167 ARG 169 168 LEU 170 169 GLY 171 170 LEU 172 171 ALA 173 172 LEU 174 173 ASN 175 174 PHE 176 175 SER 177 176 VAL 178 177 PHE 179 178 TYR 180 179 TYR 181 180 GLU 182 181 ILE 183 182 LEU 184 183 ASN 185 184 SER 186 185 PRO 187 186 GLU 188 187 LYS 189 188 ALA 190 189 CYS 191 190 SER 192 191 LEU 193 192 ALA 194 193 LYS 195 194 THR 196 195 ALA 197 196 PHE 198 197 ASP 199 198 GLU 200 199 ALA 201 200 ILE 202 201 ALA 203 202 GLU 204 203 LEU 205 204 ASP 206 205 THR 207 206 LEU 208 207 SER 209 208 GLU 210 209 GLU 211 210 SER 212 211 TYR 213 212 LYS 214 213 ASP 215 214 SER 216 215 THR 217 216 LEU 218 217 ILE 219 218 MET 220 219 GLN 221 220 LEU 222 221 LEU 223 222 ARG 224 223 ASP 225 224 ASN 226 225 LEU 227 226 THR 228 227 LEU 229 228 TRP 230 229 THR 231 230 SER 232 231 ASP 233 232 THR 234 233 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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 1A37 "14-3-3 Protein Zeta Bound To Ps-Raf259 Peptide" 99.57 245 100.00 100.00 2.87e-168 PDB 1A38 "14-3-3 Protein Zeta Bound To R18 Peptide" 99.57 245 100.00 100.00 2.87e-168 PDB 1A4O "14-3-3 Protein Zeta Isoform" 99.57 245 100.00 100.00 2.87e-168 PDB 1IB1 "Crystal Structure Of The 14-3-3 Zeta:serotonin N- Acetyltransferase Complex" 99.57 245 100.00 100.00 2.87e-168 PDB 1QJA "14-3-3 ZetaPHOSPHOPEPTIDE COMPLEX (MODE 2)" 99.57 245 100.00 100.00 2.87e-168 PDB 1QJB "14-3-3 ZetaPHOSPHOPEPTIDE COMPLEX (MODE 1)" 99.57 245 100.00 100.00 2.87e-168 PDB 2C1J "Molecular Basis For The Recognition Of Phosphorylated And Phosphoacetylated Histone H3 By 14-3-3" 99.57 258 100.00 100.00 7.13e-169 PDB 2C1N "Molecular Basis For The Recognition Of Phosphorylated And Phosphoacetylated Histone H3 By 14-3-3" 99.57 258 100.00 100.00 7.13e-169 PDB 2O02 "Phosphorylation Independent Interactions Between 14-3-3 And Exoenzyme S: From Structure To Pathogenesis" 98.29 230 100.00 100.00 3.68e-166 PDB 2V7D "14-3-3 Protein Zeta In Complex With Thr758 Phosphorylated Integrin Beta2 Peptide" 99.57 247 100.00 100.00 2.79e-168 PDB 2WH0 "Recognition Of An Intrachain Tandem 14-3-3 Binding Site Within Protein Kinase C Epsilon" 99.57 245 100.00 100.00 2.87e-168 PDB 3CU8 "Impaired Binding Of 14-3-3 To Raf1 Is Linked To Noonan And Leopard Syndrome" 99.57 245 100.00 100.00 2.87e-168 PDB 3NKX "Impaired Binding Of 14-3-3 To Raf1 Is Linked To Noonan And Leopard Syndrome" 99.57 245 100.00 100.00 2.87e-168 PDB 3RDH "X-Ray Induced Covalent Inhibition Of 14-3-3" 99.57 248 100.00 100.00 2.74e-168 PDB 4BG6 "14-3-3 Interaction With Rnd3 Prenyl-phosphorylation Motif" 99.57 245 100.00 100.00 2.87e-168 PDB 4FJ3 "14-3-3 Isoform Zeta In Complex With A Diphoyphorylated C-raf Peptide" 98.29 235 100.00 100.00 4.50e-166 PDB 4HKC "14-3-3-zeta In Complex With S1011 Phosphorylated Integrin Alpha-4 Peptide" 99.57 250 100.00 100.00 4.00e-168 PDB 4IHL "Human 14-3-3 Isoform Zeta In Complex With A Diphoyphorylated C-raf Peptide And Cotylenin A" 98.29 235 100.00 100.00 4.50e-166 PDB 4N7G "Crystal Structure Of 14-3-3zeta In Complex With A Peptide Derived From Exos" 98.29 235 100.00 100.00 4.50e-166 PDB 4N7Y "Crystal Structure Of 14-3-3zeta In Complex With A 8-carbon-linker Cyclic Peptide Derived From Exos" 98.29 235 100.00 100.00 4.50e-166 PDB 4N84 "Crystal Structure Of 14-3-3zeta In Complex With A 12-carbon-linker Cyclic Peptide Derived From Exos" 98.72 230 99.57 99.57 9.90e-165 PDB 4WRQ "Crystal Structure Of 14-3-3 Zeta With Chibby Peptide" 100.00 246 100.00 100.00 2.13e-169 PDB 4ZDR "Crystal Structure Of 14-3-3[zeta]-lkb1 Fusion Protein" 98.29 266 100.00 100.00 4.11e-166 DBJ BAA04534 "14-3-3 protein zeta-subtype [Rattus norvegicus]" 99.57 245 99.57 99.57 2.15e-167 DBJ BAA06402 "mitochondrial import stimulation factor S1 subunit [Rattus sp.]" 99.57 245 99.57 99.57 2.15e-167 DBJ BAA11464 "phospholipase A2 [Mus musculus]" 99.57 245 99.57 99.57 2.15e-167 DBJ BAA11751 "14-3-3 zeta [Mus musculus]" 99.57 245 99.14 99.57 1.30e-166 DBJ BAA13421 "14-3-3 zeta [Mus musculus]" 99.57 245 98.71 99.57 3.81e-166 EMBL CAG31814 "hypothetical protein RCJMB04_11l21 [Gallus gallus]" 99.57 245 99.14 100.00 5.62e-167 EMBL CAH92765 "hypothetical protein [Pongo abelii]" 99.57 245 100.00 100.00 2.87e-168 GB AAA30514 "factor activating exoenzyme S [Bos taurus]" 99.57 245 100.00 100.00 2.87e-168 GB AAA36446 "phospholipase A2 [Homo sapiens]" 99.57 245 100.00 100.00 2.87e-168 GB AAA80544 "14-3-3 zeta isoform [Rattus norvegicus]" 99.57 245 99.14 99.14 2.30e-166 GB AAB22282 "protein kinase C inhibitor protein-1 zeta isoform, 14-3-3 protein, KCIP-1 [sheep, brain, Peptide, 245 aa]" 99.57 245 99.14 99.14 1.93e-166 GB AAB22943 "14-3-3 protein zeta chain [cattle, brain, Peptide, 245 aa]" 99.57 245 99.57 99.57 4.14e-167 PRF 2022313B "14-3-3 Protein:ISOTYPE=zeta" 99.57 245 99.57 99.57 2.15e-167 REF NP_001026514 "14-3-3 protein zeta [Gallus gallus]" 99.57 245 99.14 100.00 5.62e-167 REF NP_001126612 "14-3-3 protein zeta/delta [Pongo abelii]" 99.57 245 100.00 100.00 2.87e-168 REF NP_001129171 "14-3-3 protein zeta/delta [Homo sapiens]" 99.57 245 100.00 100.00 2.87e-168 REF NP_001129172 "14-3-3 protein zeta/delta [Homo sapiens]" 99.57 245 100.00 100.00 2.87e-168 REF NP_001129173 "14-3-3 protein zeta/delta [Homo sapiens]" 99.57 245 100.00 100.00 2.87e-168 SP P29361 "RecName: Full=14-3-3 protein zeta/delta; AltName: Full=Protein kinase C inhibitor protein 1; Short=KCIP-1" 99.57 245 99.14 99.14 1.93e-166 SP P63101 "RecName: Full=14-3-3 protein zeta/delta; AltName: Full=Protein kinase C inhibitor protein 1; Short=KCIP-1; AltName: Full=SEZ-2" 99.57 245 99.57 99.57 2.15e-167 SP P63102 "RecName: Full=14-3-3 protein zeta/delta; AltName: Full=Mitochondrial import stimulation factor S1 subunit; AltName: Full=Protei" 99.57 245 99.57 99.57 2.15e-167 SP P63103 "RecName: Full=14-3-3 protein zeta/delta; AltName: Full=Factor activating exoenzyme S; Short=FAS; AltName: Full=Protein kinase C" 99.57 245 100.00 100.00 2.87e-168 SP P63104 "RecName: Full=14-3-3 protein zeta/delta; AltName: Full=Protein kinase C inhibitor protein 1; Short=KCIP-1" 99.57 245 100.00 100.00 2.87e-168 TPG DAA18059 "TPA: tyrosine 3/tryptophan 5 -monooxygenase activation protein, zeta polypeptide-like [Bos taurus]" 99.57 245 99.57 100.00 1.16e-167 TPG DAA22580 "TPA: 14-3-3 protein zeta/delta [Bos taurus]" 99.57 245 100.00 100.00 2.87e-168 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity E.coli 562 Bacteria . Escherichia coli 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 $entity 'recombinant technology' . Escherichia coli . pDEST17 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_14-3-3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity 0.5 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' DSS 0.1 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium phosphate' 50 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version . loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $14-3-3 save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $14-3-3 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $14-3-3 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $14-3-3 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.2 . M pH 6.8 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D CBCA(CO)NH' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $14-3-3 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 3 ASP H H 8.502 0.020 1 2 2 3 ASP CA C 53.395 0.3 1 3 2 3 ASP CB C 41.312 0.3 1 4 2 3 ASP N N 122.970 0.3 1 5 3 4 LYS H H 8.643 0.020 1 6 3 4 LYS CA C 59.851 0.3 1 7 3 4 LYS CB C 30.947 0.3 1 8 3 4 LYS N N 123.995 0.3 1 9 4 5 ASN H H 8.259 0.020 1 10 4 5 ASN CA C 56.103 0.3 1 11 4 5 ASN CB C 37.582 0.3 1 12 4 5 ASN N N 116.671 0.3 1 13 5 6 GLU H H 7.986 0.020 1 14 5 6 GLU CA C 59.259 0.3 1 15 5 6 GLU CB C 28.873 0.3 1 16 5 6 GLU N N 121.847 0.3 1 17 6 7 LEU H H 7.735 0.020 1 18 6 7 LEU CA C 57.719 0.3 1 19 6 7 LEU CB C 42.082 0.3 1 20 6 7 LEU N N 119.747 0.3 1 21 7 8 VAL H H 7.978 0.020 1 22 7 8 VAL CA C 66.545 0.3 1 23 7 8 VAL CB C 30.710 0.3 1 24 7 8 VAL N N 119.894 0.3 1 25 8 9 GLN H H 7.766 0.020 1 26 8 9 GLN CA C 58.522 0.3 1 27 8 9 GLN CB C 27.297 0.3 1 28 8 9 GLN N N 118.528 0.3 1 29 9 10 LYS H H 8.433 0.020 1 30 9 10 LYS CA C 59.855 0.3 1 31 9 10 LYS CB C 31.083 0.3 1 32 9 10 LYS N N 121.944 0.3 1 33 10 11 ALA H H 8.492 0.020 1 34 10 11 ALA CA C 55.261 0.3 1 35 10 11 ALA CB C 17.856 0.3 1 36 10 11 ALA N N 124.682 0.3 1 37 11 12 LYS H H 8.008 0.020 1 38 11 12 LYS CA C 59.375 0.3 1 39 11 12 LYS CB C 31.293 0.3 1 40 11 12 LYS N N 117.455 0.3 1 41 12 13 LEU H H 7.696 0.020 1 42 12 13 LEU CA C 57.560 0.3 1 43 12 13 LEU CB C 41.462 0.3 1 44 12 13 LEU N N 122.581 0.3 1 45 13 14 ALA H H 8.158 0.020 1 46 13 14 ALA CA C 54.893 0.3 1 47 13 14 ALA CB C 16.765 0.3 1 48 13 14 ALA N N 121.751 0.3 1 49 14 15 GLU H H 8.205 0.020 1 50 14 15 GLU CA C 59.734 0.3 1 51 14 15 GLU CB C 28.992 0.3 1 52 14 15 GLU N N 119.308 0.3 1 53 15 16 GLN H H 7.605 0.020 1 54 15 16 GLN CA C 58.530 0.3 1 55 15 16 GLN CB C 27.559 0.3 1 56 15 16 GLN N N 119.258 0.3 1 57 16 17 ALA H H 7.876 0.020 1 58 16 17 ALA CA C 51.266 0.3 1 59 16 17 ALA CB C 17.979 0.3 1 60 16 17 ALA N N 118.144 0.3 1 61 17 18 GLU H H 7.688 0.020 1 62 17 18 GLU CA C 57.075 0.3 1 63 17 18 GLU CB C 25.962 0.3 1 64 17 18 GLU N N 115.788 0.3 1 65 18 19 ARG H H 8.080 0.020 1 66 18 19 ARG CA C 53.632 0.3 1 67 18 19 ARG CB C 28.163 0.3 1 68 18 19 ARG N N 122.335 0.3 1 69 19 20 TYR H H 7.477 0.020 1 70 19 20 TYR CA C 62.161 0.3 1 71 19 20 TYR CB C 36.277 0.3 1 72 19 20 TYR N N 120.089 0.3 1 73 20 21 ASP H H 8.385 0.020 1 74 20 21 ASP CA C 57.558 0.3 1 75 20 21 ASP CB C 38.438 0.3 1 76 20 21 ASP N N 120.040 0.3 1 77 21 22 ASP H H 7.758 0.020 1 78 21 22 ASP CA C 56.464 0.3 1 79 21 22 ASP CB C 39.158 0.3 1 80 21 22 ASP N N 122.337 0.3 1 81 22 23 MET H H 7.782 0.020 1 82 22 23 MET CA C 60.088 0.3 1 83 22 23 MET CB C 39.239 0.3 1 84 22 23 MET N N 121.554 0.3 1 85 23 24 ALA H H 8.565 0.020 1 86 23 24 ALA CA C 55.172 0.3 1 87 23 24 ALA CB C 15.428 0.3 1 88 23 24 ALA N N 121.700 0.3 1 89 24 25 ALA H H 7.587 0.020 1 90 24 25 ALA CA C 55.012 0.3 1 91 24 25 ALA CB C 17.008 0.3 1 92 24 25 ALA N N 120.040 0.3 1 93 25 26 CYS H H 7.798 0.020 1 94 25 26 CYS CA C 63.616 0.3 1 95 25 26 CYS CB C 26.814 0.3 1 96 25 26 CYS N N 115.847 0.3 1 97 26 27 MET H H 7.674 0.020 1 98 26 27 MET CA C 54.658 0.3 1 99 26 27 MET CB C 27.415 0.3 1 100 26 27 MET N N 114.665 0.3 1 101 27 28 LYS H H 9.378 0.020 1 102 27 28 LYS CA C 60.216 0.3 1 103 27 28 LYS CB C 30.565 0.3 1 104 27 28 LYS N N 128.295 0.3 1 105 31 32 GLU H H 7.810 0.020 1 106 31 32 GLU CA C 56.960 0.3 1 107 31 32 GLU CB C 28.390 0.3 1 108 31 32 GLU N N 118.468 0.3 1 109 32 33 GLN H H 7.133 0.020 1 110 32 33 GLN CA C 56.844 0.3 1 111 32 33 GLN CB C 26.810 0.3 1 112 32 33 GLN N N 116.671 0.3 1 113 33 34 GLY H H 7.508 0.020 1 114 33 34 GLY CA C 46.110 0.3 1 115 33 34 GLY N N 104.806 0.3 1 116 34 35 ALA H H 7.548 0.020 1 117 34 35 ALA CA C 50.552 0.3 1 118 34 35 ALA CB C 19.278 0.3 1 119 34 35 ALA N N 122.677 0.3 1 120 35 36 GLU H H 8.463 0.020 1 121 35 36 GLU CA C 57.008 0.3 1 122 35 36 GLU CB C 29.347 0.3 1 123 35 36 GLU N N 121.896 0.3 1 124 36 37 LEU H H 8.392 0.020 1 125 36 37 LEU CA C 54.106 0.3 1 126 36 37 LEU CB C 40.542 0.3 1 127 36 37 LEU N N 125.313 0.3 1 128 37 38 SER H H 9.159 0.020 1 129 37 38 SER CA C 56.594 0.3 1 130 37 38 SER CB C 64.768 0.3 1 131 37 38 SER N N 120.577 0.3 1 132 40 41 GLU H H 7.665 0.020 1 133 40 41 GLU CA C 59.022 0.3 1 134 40 41 GLU CB C 29.406 0.3 1 135 40 41 GLU N N 119.845 0.3 1 136 41 42 ARG H H 8.831 0.020 1 137 41 42 ARG CA C 59.141 0.3 1 138 41 42 ARG CB C 29.110 0.3 1 139 41 42 ARG N N 120.187 0.3 1 140 42 43 ASN H H 7.563 0.020 1 141 42 43 ASN CA C 56.466 0.3 1 142 42 43 ASN CB C 37.708 0.3 1 143 42 43 ASN N N 118.429 0.3 1 144 43 44 LEU H H 8.064 0.020 1 145 43 44 LEU CA C 57.838 0.3 1 146 43 44 LEU CB C 41.549 0.3 1 147 43 44 LEU N N 120.284 0.3 1 148 44 45 LEU H H 8.228 0.020 1 149 44 45 LEU CA C 58.768 0.3 1 150 44 45 LEU CB C 41.335 0.3 1 151 44 45 LEU N N 119.356 0.3 1 152 45 46 SER H H 7.947 0.020 1 153 45 46 SER CA C 61.066 0.3 1 154 45 46 SER CB C 62.886 0.3 1 155 45 46 SER N N 110.714 0.3 1 156 46 47 VAL H H 8.846 0.020 1 157 46 47 VAL CA C 66.153 0.3 1 158 46 47 VAL CB C 31.654 0.3 1 159 46 47 VAL N N 122.287 0.3 1 160 47 48 ALA H H 8.189 0.020 1 161 47 48 ALA CA C 56.465 0.3 1 162 47 48 ALA CB C 17.129 0.3 1 163 47 48 ALA N N 122.728 0.3 1 164 48 49 TYR H H 7.767 0.020 1 165 48 49 TYR CA C 64.218 0.3 1 166 48 49 TYR CB C 37.100 0.3 1 167 48 49 TYR N N 113.937 0.3 1 168 49 50 LYS H H 8.471 0.020 1 169 49 50 LYS CA C 59.132 0.3 1 170 49 50 LYS CB C 31.053 0.3 1 171 49 50 LYS N N 120.723 0.3 1 172 50 51 ASN H H 7.602 0.020 1 173 50 51 ASN CA C 56.230 0.3 1 174 50 51 ASN CB C 38.917 0.3 1 175 50 51 ASN N N 117.893 0.3 1 176 51 52 VAL H H 8.017 0.020 1 177 51 52 VAL CA C 66.397 0.3 1 178 51 52 VAL CB C 31.537 0.3 1 179 51 52 VAL N N 122.095 0.3 1 180 52 53 VAL H H 9.112 0.020 1 181 52 53 VAL CA C 65.541 0.3 1 182 52 53 VAL CB C 30.812 0.3 1 183 52 53 VAL N N 119.946 0.3 1 184 53 54 GLY H H 8.158 0.020 1 185 53 54 GLY CA C 46.788 0.3 1 186 53 54 GLY N N 112.131 0.3 1 187 54 55 ALA H H 7.414 0.020 1 188 54 55 ALA CA C 54.471 0.3 1 189 54 55 ALA CB C 17.257 0.3 1 190 54 55 ALA N N 123.118 0.3 1 191 55 56 ARG H H 6.843 0.020 1 192 55 56 ARG CA C 59.496 0.3 1 193 55 56 ARG CB C 30.079 0.3 1 194 55 56 ARG N N 117.991 0.3 1 195 59 60 TRP H H 9.089 0.020 1 196 59 60 TRP CA C 63.168 0.3 1 197 59 60 TRP CB C 28.577 0.3 1 198 59 60 TRP N N 122.823 0.3 1 199 60 61 ARG H H 8.411 0.020 1 200 60 61 ARG CA C 60.109 0.3 1 201 60 61 ARG CB C 29.237 0.3 1 202 60 61 ARG N N 120.090 0.3 1 203 61 62 VAL H H 7.616 0.020 1 204 61 62 VAL CA C 66.039 0.3 1 205 61 62 VAL CB C 31.229 0.3 1 206 61 62 VAL N N 119.930 0.3 1 207 62 63 VAL H H 8.173 0.020 1 208 62 63 VAL CA C 66.753 0.3 1 209 62 63 VAL CB C 30.803 0.3 1 210 62 63 VAL N N 119.649 0.3 1 211 63 64 SER H H 8.432 0.020 1 212 63 64 SER CA C 61.569 0.3 1 213 63 64 SER N N 115.499 0.3 1 214 64 65 SER H H 7.352 0.020 1 215 64 65 SER CB C 62.036 0.3 1 216 64 65 SER N N 116.085 0.3 1 217 65 66 ILE H H 7.516 0.020 1 218 65 66 ILE CA C 64.708 0.3 1 219 65 66 ILE CB C 37.462 0.3 1 220 65 66 ILE N N 123.067 0.3 1 221 66 67 GLU H H 8.463 0.020 1 222 66 67 GLU CA C 59.307 0.3 1 223 66 67 GLU CB C 29.477 0.3 1 224 66 67 GLU N N 123.020 0.3 1 225 67 68 GLN H H 7.696 0.020 1 226 67 68 GLN CA C 57.440 0.3 1 227 67 68 GLN CB C 28.000 0.3 1 228 67 68 GLN N N 115.450 0.3 1 229 68 69 LYS H H 7.665 0.020 1 230 68 69 LYS CA C 56.585 0.3 1 231 68 69 LYS CB C 31.893 0.3 1 232 68 69 LYS N N 118.526 0.3 1 233 69 70 THR H H 7.493 0.020 1 234 69 70 THR CA C 62.041 0.3 1 235 69 70 THR CB C 68.811 0.3 1 236 69 70 THR N N 113.692 0.3 1 237 70 71 GLU H H 7.876 0.020 1 238 70 71 GLU CA C 56.771 0.3 1 239 70 71 GLU CB C 29.347 0.3 1 240 70 71 GLU N N 123.897 0.3 1 241 71 72 GLY H H 8.627 0.020 1 242 71 72 GLY CA C 45.221 0.3 1 243 71 72 GLY N N 112.276 0.3 1 244 72 73 ALA H H 8.048 0.020 1 245 72 73 ALA CA C 51.026 0.3 1 246 72 73 ALA CB C 17.619 0.3 1 247 72 73 ALA N N 125.118 0.3 1 248 73 74 GLU H H 8.392 0.020 1 249 73 74 GLU CA C 59.259 0.3 1 250 73 74 GLU CB C 28.873 0.3 1 251 73 74 GLU N N 121.993 0.3 1 252 75 76 LYS H H 7.626 0.020 1 253 75 76 LYS CA C 59.010 0.3 1 254 75 76 LYS CB C 31.521 0.3 1 255 75 76 LYS N N 120.138 0.3 1 256 76 77 GLN H H 8.314 0.020 1 257 76 77 GLN CA C 59.259 0.3 1 258 76 77 GLN CB C 27.985 0.3 1 259 76 77 GLN N N 120.772 0.3 1 260 77 78 GLN H H 8.087 0.020 1 261 77 78 GLN CA C 58.430 0.3 1 262 77 78 GLN CB C 26.978 0.3 1 263 77 78 GLN N N 119.063 0.3 1 264 78 79 MET H H 7.806 0.020 1 265 78 79 MET CA C 58.279 0.3 1 266 78 79 MET CB C 31.894 0.3 1 267 78 79 MET N N 118.624 0.3 1 268 79 80 ALA H H 7.970 0.020 1 269 79 80 ALA CA C 54.994 0.3 1 270 79 80 ALA CB C 15.961 0.3 1 271 79 80 ALA N N 122.140 0.3 1 272 80 81 ARG H H 8.361 0.020 1 273 80 81 ARG CA C 59.274 0.3 1 274 80 81 ARG CB C 28.880 0.3 1 275 80 81 ARG N N 119.796 0.3 1 276 81 82 GLU H H 8.174 0.020 1 277 81 82 GLU CA C 58.891 0.3 1 278 81 82 GLU CB C 28.629 0.3 1 279 81 82 GLU N N 117.605 0.3 1 280 83 84 ARG H H 8.909 0.020 1 281 83 84 ARG CA C 60.621 0.3 1 282 83 84 ARG CB C 27.299 0.3 1 283 83 84 ARG N N 121.372 0.3 1 284 84 85 GLU H H 8.463 0.020 1 285 84 85 GLU CA C 59.611 0.3 1 286 84 85 GLU CB C 28.387 0.3 1 287 84 85 GLU N N 118.233 0.3 1 288 85 86 LYS H H 7.641 0.020 1 289 85 86 LYS CA C 59.372 0.3 1 290 85 86 LYS CB C 31.065 0.3 1 291 85 86 LYS N N 122.777 0.3 1 292 86 87 ILE H H 7.939 0.020 1 293 86 87 ILE CA C 65.425 0.3 1 294 86 87 ILE CB C 37.471 0.3 1 295 86 87 ILE N N 121.650 0.3 1 296 87 88 GLU H H 9.097 0.020 1 297 87 88 GLU CA C 59.860 0.3 1 298 87 88 GLU CB C 29.231 0.3 1 299 87 88 GLU N N 119.557 0.3 1 300 88 89 THR H H 8.087 0.020 1 301 88 89 THR CA C 66.825 0.3 1 302 88 89 THR CB C 68.364 0.3 1 303 88 89 THR N N 116.427 0.3 1 304 89 90 GLU H H 7.336 0.020 1 305 89 90 GLU CA C 59.081 0.3 1 306 89 90 GLU CB C 29.643 0.3 1 307 89 90 GLU N N 120.577 0.3 1 308 90 91 LEU H H 8.390 0.020 1 309 90 91 LEU CA C 59.024 0.3 1 310 90 91 LEU CB C 42.182 0.3 1 311 90 91 LEU N N 119.850 0.3 1 312 91 92 ARG H H 8.885 0.020 1 313 91 92 ARG CA C 59.978 0.3 1 314 91 92 ARG CB C 28.631 0.3 1 315 91 92 ARG N N 119.991 0.3 1 316 92 93 ASP H H 8.126 0.020 1 317 92 93 ASP CA C 57.445 0.3 1 318 92 93 ASP CB C 39.165 0.3 1 319 92 93 ASP N N 120.137 0.3 1 320 93 94 ILE H H 8.040 0.020 1 321 93 94 ILE CA C 64.942 0.3 1 322 93 94 ILE CB C 38.315 0.3 1 323 93 94 ILE N N 121.409 0.3 1 324 94 95 CYS H H 8.370 0.020 1 325 94 95 CYS CA C 64.090 0.3 1 326 94 95 CYS CB C 26.574 0.3 1 327 94 95 CYS N N 116.284 0.3 1 328 95 96 ASN H H 8.768 0.020 1 329 95 96 ASN CA C 56.000 0.3 1 330 95 96 ASN CB C 37.337 0.3 1 331 95 96 ASN N N 116.525 0.3 1 332 99 100 SER H H 7.884 0.020 1 333 99 100 SER CA C 61.443 0.3 1 334 99 100 SER CB C 62.039 0.3 1 335 99 100 SER N N 115.694 0.3 1 336 100 101 LEU H H 7.735 0.020 1 337 100 101 LEU CA C 57.838 0.3 1 338 100 101 LEU CB C 41.016 0.3 1 339 100 101 LEU N N 121.554 0.3 1 340 107 108 PRO CA C 65.193 0.3 1 341 107 108 PRO CB C 29.961 0.3 1 342 108 109 ASN H H 6.460 0.020 1 343 108 109 ASN CA C 52.227 0.3 1 344 108 109 ASN CB C 39.163 0.3 1 345 108 109 ASN N N 110.958 0.3 1 346 109 110 ALA H H 7.180 0.020 1 347 109 110 ALA CA C 52.270 0.3 1 348 109 110 ALA CB C 16.790 0.3 1 349 109 110 ALA N N 123.897 0.3 1 350 110 111 SER H H 8.666 0.020 1 351 110 111 SER CA C 59.252 0.3 1 352 110 111 SER CB C 63.405 0.3 1 353 110 111 SER N N 120.235 0.3 1 354 111 112 GLN H H 7.485 0.020 1 355 111 112 GLN CA C 53.803 0.3 1 356 111 112 GLN CB C 30.084 0.3 1 357 111 112 GLN N N 119.063 0.3 1 358 113 114 GLU H H 8.799 0.020 1 359 113 114 GLU CA C 59.911 0.3 1 360 113 114 GLU CB C 28.518 0.3 1 361 113 114 GLU N N 114.669 0.3 1 362 114 115 SER H H 6.937 0.020 1 363 114 115 SER CA C 60.371 0.3 1 364 114 115 SER CB C 61.798 0.3 1 365 114 115 SER N N 112.428 0.3 1 366 115 116 LYS H H 7.915 0.020 1 367 115 116 LYS CA C 60.621 0.3 1 368 115 116 LYS CB C 31.776 0.3 1 369 115 116 LYS N N 122.677 0.3 1 370 116 117 VAL H H 8.502 0.020 1 371 116 117 VAL CA C 67.002 0.3 1 372 116 117 VAL CB C 30.446 0.3 1 373 116 117 VAL N N 116.524 0.3 1 374 117 118 PHE H H 7.767 0.020 1 375 117 118 PHE CA C 62.102 0.3 1 376 117 118 PHE CB C 38.798 0.3 1 377 117 118 PHE N N 119.649 0.3 1 378 118 119 TYR H H 8.549 0.020 1 379 118 119 TYR CA C 59.253 0.3 1 380 118 119 TYR CB C 37.946 0.3 1 381 118 119 TYR N N 117.650 0.3 1 382 121 122 MET H H 8.534 0.020 1 383 121 122 MET CA C 59.532 0.3 1 384 121 122 MET CB C 31.172 0.3 1 385 121 122 MET N N 120.044 0.3 1 386 122 123 LYS H H 8.345 0.020 1 387 122 123 LYS CA C 59.498 0.3 1 388 122 123 LYS CB C 32.381 0.3 1 389 122 123 LYS N N 121.457 0.3 1 390 123 124 GLY H H 7.939 0.020 1 391 123 124 GLY CA C 46.785 0.3 1 392 123 124 GLY N N 107.103 0.3 1 393 124 125 ASP H H 8.604 0.020 1 394 124 125 ASP CA C 56.586 0.3 1 395 124 125 ASP CB C 39.403 0.3 1 396 124 125 ASP N N 122.923 0.3 1 397 125 126 TYR H H 8.330 0.020 1 398 125 126 TYR CA C 62.881 0.3 1 399 125 126 TYR CB C 36.254 0.3 1 400 125 126 TYR N N 116.280 0.3 1 401 130 131 ALA H H 8.604 0.020 1 402 130 131 ALA CA C 54.524 0.3 1 403 130 131 ALA CB C 17.364 0.3 1 404 130 131 ALA N N 123.604 0.3 1 405 131 132 GLU H H 7.721 0.020 1 406 131 132 GLU CA C 58.518 0.3 1 407 131 132 GLU CB C 29.446 0.3 1 408 131 132 GLU N N 115.501 0.3 1 409 132 133 VAL H H 6.554 0.020 1 410 132 133 VAL CA C 59.006 0.3 1 411 132 133 VAL CB C 30.449 0.3 1 412 132 133 VAL N N 105.148 0.3 1 413 133 134 ALA H H 7.102 0.020 1 414 133 134 ALA CA C 51.618 0.3 1 415 133 134 ALA CB C 19.396 0.3 1 416 133 134 ALA N N 126.095 0.3 1 417 134 135 ALA H H 8.698 0.020 1 418 134 135 ALA CA C 51.026 0.3 1 419 134 135 ALA CB C 20.403 0.3 1 420 134 135 ALA N N 123.556 0.3 1 421 135 136 GLY H H 8.549 0.020 1 422 135 136 GLY CA C 46.169 0.3 1 423 135 136 GLY N N 108.224 0.3 1 424 137 138 ASP H H 8.205 0.020 1 425 137 138 ASP CA C 55.137 0.3 1 426 137 138 ASP CB C 40.128 0.3 1 427 137 138 ASP N N 118.722 0.3 1 428 138 139 LYS H H 7.274 0.020 1 429 138 139 LYS CA C 60.148 0.3 1 430 138 139 LYS CB C 31.953 0.3 1 431 138 139 LYS N N 119.601 0.3 1 432 139 140 LYS H H 7.860 0.020 1 433 139 140 LYS CA C 59.618 0.3 1 434 139 140 LYS CB C 31.048 0.3 1 435 139 140 LYS N N 117.892 0.3 1 436 140 141 GLY H H 8.040 0.020 1 437 140 141 GLY CA C 46.465 0.3 1 438 140 141 GLY N N 105.147 0.3 1 439 141 142 ILE H H 7.305 0.020 1 440 141 142 ILE CA C 64.223 0.3 1 441 141 142 ILE CB C 37.712 0.3 1 442 141 142 ILE N N 123.362 0.3 1 443 142 143 VAL H H 8.470 0.020 1 444 142 143 VAL CA C 67.123 0.3 1 445 142 143 VAL CB C 30.685 0.3 1 446 142 143 VAL N N 121.267 0.3 1 447 143 144 ASP H H 7.946 0.020 1 448 143 144 ASP CA C 57.075 0.3 1 449 143 144 ASP CB C 39.763 0.3 1 450 143 144 ASP N N 118.674 0.3 1 451 144 145 GLN H H 7.297 0.020 1 452 144 145 GLN CA C 58.403 0.3 1 453 144 145 GLN CB C 26.334 0.3 1 454 144 145 GLN N N 118.576 0.3 1 455 146 147 GLN H H 8.236 0.020 1 456 146 147 GLN CA C 59.371 0.3 1 457 146 147 GLN CB C 27.781 0.3 1 458 146 147 GLN N N 116.429 0.3 1 459 147 148 GLN H H 8.056 0.020 1 460 147 148 GLN CA C 58.404 0.3 1 461 147 148 GLN CB C 27.498 0.3 1 462 147 148 GLN N N 115.792 0.3 1 463 148 149 ALA H H 7.180 0.020 1 464 148 149 ALA CA C 54.657 0.3 1 465 148 149 ALA CB C 16.285 0.3 1 466 148 149 ALA N N 123.166 0.3 1 467 149 150 TYR H H 7.587 0.020 1 468 149 150 TYR CA C 59.616 0.3 1 469 149 150 TYR CB C 34.437 0.3 1 470 149 150 TYR N N 115.262 0.3 1 471 150 151 GLN H H 8.510 0.020 1 472 150 151 GLN CA C 58.768 0.3 1 473 150 151 GLN CB C 27.663 0.3 1 474 150 151 GLN N N 118.430 0.3 1 475 151 152 GLU H H 8.033 0.020 1 476 151 152 GLU CA C 59.134 0.3 1 477 151 152 GLU CB C 28.757 0.3 1 478 151 152 GLU N N 121.064 0.3 1 479 157 158 LYS H H 7.633 0.020 1 480 157 158 LYS CA C 58.412 0.3 1 481 157 158 LYS CB C 31.144 0.3 1 482 157 158 LYS N N 119.504 0.3 1 483 158 159 LYS H H 7.078 0.020 1 484 158 159 LYS CA C 57.436 0.3 1 485 158 159 LYS CB C 33.266 0.3 1 486 158 159 LYS N N 116.966 0.3 1 487 159 160 GLU H H 7.917 0.020 1 488 159 160 GLU CA C 56.231 0.3 1 489 159 160 GLU CB C 31.397 0.3 1 490 159 160 GLU N N 113.298 0.3 1 491 160 161 MET H H 7.860 0.020 1 492 160 161 MET CA C 54.224 0.3 1 493 160 161 MET CB C 35.330 0.3 1 494 160 161 MET N N 117.062 0.3 1 495 161 162 GLN H H 9.167 0.020 1 496 161 162 GLN CA C 54.343 0.3 1 497 161 162 GLN CB C 27.452 0.3 1 498 161 162 GLN N N 122.872 0.3 1 499 162 163 PRO CA C 64.768 0.3 1 500 162 163 PRO CB C 31.813 0.3 1 501 163 164 THR H H 6.812 0.020 1 502 163 164 THR CA C 60.148 0.3 1 503 163 164 THR CB C 68.736 0.3 1 504 163 164 THR N N 125.069 0.3 1 505 164 165 HIS H H 7.962 0.020 1 506 164 165 HIS CA C 56.475 0.3 1 507 164 165 HIS CB C 31.776 0.3 1 508 164 165 HIS N N 127.071 0.3 1 509 167 168 ARG H H 6.804 0.020 1 510 167 168 ARG CA C 59.738 0.3 1 511 167 168 ARG CB C 29.355 0.3 1 512 167 168 ARG N N 122.043 0.3 1 513 168 169 LEU H H 8.557 0.020 1 514 168 169 LEU CA C 57.556 0.3 1 515 168 169 LEU CB C 41.941 0.3 1 516 168 169 LEU N N 119.651 0.3 1 517 169 170 GLY H H 8.525 0.020 1 518 169 170 GLY CA C 46.423 0.3 1 519 169 170 GLY N N 107.250 0.3 1 520 170 171 LEU H H 7.915 0.020 1 521 170 171 LEU CA C 57.560 0.3 1 522 170 171 LEU CB C 40.008 0.3 1 523 170 171 LEU N N 123.122 0.3 1 524 171 172 ALA H H 8.056 0.020 1 525 171 172 ALA CA C 55.376 0.3 1 526 171 172 ALA CB C 16.890 0.3 1 527 171 172 ALA N N 122.046 0.3 1 528 172 173 LEU H H 8.416 0.020 1 529 172 173 LEU CA C 58.164 0.3 1 530 172 173 LEU CB C 40.370 0.3 1 531 172 173 LEU N N 119.065 0.3 1 532 176 177 VAL H H 8.229 0.020 1 533 176 177 VAL CA C 66.999 0.3 1 534 176 177 VAL CB C 30.712 0.3 1 535 176 177 VAL N N 124.391 0.3 1 536 177 178 PHE H H 8.268 0.020 1 537 177 178 PHE CA C 61.677 0.3 1 538 177 178 PHE CB C 37.831 0.3 1 539 177 178 PHE N N 121.751 0.3 1 540 178 179 TYR H H 8.267 0.020 1 541 178 179 TYR CA C 62.034 0.3 1 542 178 179 TYR CB C 36.739 0.3 1 543 178 179 TYR N N 120.434 0.3 1 544 179 180 TYR H H 8.033 0.020 1 545 179 180 TYR CA C 62.883 0.3 1 546 179 180 TYR CB C 38.675 0.3 1 547 179 180 TYR N N 119.065 0.3 1 548 180 181 GLU H H 9.190 0.020 1 549 180 181 GLU CA C 57.920 0.3 1 550 180 181 GLU CB C 30.086 0.3 1 551 180 181 GLU N N 114.620 0.3 1 552 181 182 ILE H H 7.727 0.020 1 553 181 182 ILE CA C 58.892 0.3 1 554 181 182 ILE CB C 33.105 0.3 1 555 181 182 ILE N N 116.478 0.3 1 556 182 183 LEU H H 6.703 0.020 1 557 182 183 LEU CA C 53.936 0.3 1 558 182 183 LEU CB C 40.970 0.3 1 559 182 183 LEU N N 116.234 0.3 1 560 183 184 ASN H H 6.560 0.020 1 561 183 184 ASN CA C 53.326 0.3 1 562 183 184 ASN CB C 36.494 0.3 1 563 183 184 ASN N N 114.909 0.3 1 564 184 185 SER H H 8.134 0.020 1 565 184 185 SER CA C 53.682 0.3 1 566 184 185 SER CB C 62.521 0.3 1 567 184 185 SER N N 111.349 0.3 1 568 185 186 PRO CA C 64.821 0.3 1 569 185 186 PRO CB C 30.924 0.3 1 570 186 187 GLU H H 8.682 0.020 1 571 186 187 GLU CA C 59.737 0.3 1 572 186 187 GLU CB C 27.666 0.3 1 573 186 187 GLU N N 118.185 0.3 1 574 187 188 LYS H H 7.235 0.020 1 575 187 188 LYS CA C 58.193 0.3 1 576 187 188 LYS CB C 30.473 0.3 1 577 187 188 LYS N N 120.187 0.3 1 578 188 189 ALA H H 7.563 0.020 1 579 188 189 ALA CA C 55.409 0.3 1 580 188 189 ALA CB C 19.929 0.3 1 581 188 189 ALA N N 121.358 0.3 1 582 189 190 CYS H H 8.502 0.020 1 583 189 190 CYS CA C 63.481 0.3 1 584 189 190 CYS CB C 26.575 0.3 1 585 189 190 CYS N N 113.937 0.3 1 586 190 191 SER H H 7.727 0.020 1 587 190 191 SER CA C 61.068 0.3 1 588 190 191 SER CB C 62.154 0.3 1 589 190 191 SER N N 114.181 0.3 1 590 191 192 LEU H H 7.634 0.020 1 591 191 192 LEU CA C 58.371 0.3 1 592 191 192 LEU CB C 41.134 0.3 1 593 191 192 LEU N N 123.556 0.3 1 594 192 193 ALA H H 8.111 0.020 1 595 192 193 ALA CA C 55.350 0.3 1 596 192 193 ALA CB C 17.679 0.3 1 597 192 193 ALA N N 120.675 0.3 1 598 193 194 LYS H H 8.713 0.020 1 599 193 194 LYS CA C 59.135 0.3 1 600 193 194 LYS CB C 31.772 0.3 1 601 193 194 LYS N N 117.550 0.3 1 602 194 195 THR H H 7.907 0.020 1 603 194 195 THR CA C 66.648 0.3 1 604 194 195 THR CB C 68.328 0.3 1 605 194 195 THR N N 114.718 0.3 1 606 195 196 ALA H H 7.868 0.020 1 607 195 196 ALA CA C 54.639 0.3 1 608 195 196 ALA CB C 17.975 0.3 1 609 195 196 ALA N N 122.188 0.3 1 610 196 197 PHE H H 8.338 0.020 1 611 196 197 PHE CA C 62.040 0.3 1 612 196 197 PHE CB C 39.146 0.3 1 613 196 197 PHE N N 119.601 0.3 1 614 197 198 ASP H H 9.073 0.020 1 615 197 198 ASP CA C 56.890 0.3 1 616 197 198 ASP CB C 39.180 0.3 1 617 197 198 ASP N N 120.187 0.3 1 618 198 199 GLU H H 8.479 0.020 1 619 198 199 GLU CA C 58.963 0.3 1 620 198 199 GLU CB C 28.814 0.3 1 621 198 199 GLU N N 119.405 0.3 1 622 199 200 ALA H H 7.289 0.020 1 623 199 200 ALA CA C 54.224 0.3 1 624 199 200 ALA CB C 18.212 0.3 1 625 199 200 ALA N N 120.579 0.3 1 626 200 201 ILE H H 8.228 0.020 1 627 200 201 ILE CA C 62.161 0.3 1 628 200 201 ILE CB C 35.647 0.3 1 629 200 201 ILE N N 118.185 0.3 1 630 201 202 ALA H H 7.203 0.020 1 631 201 202 ALA CA C 53.691 0.3 1 632 201 202 ALA CB C 17.856 0.3 1 633 201 202 ALA N N 120.772 0.3 1 634 202 203 GLU H H 7.219 0.020 1 635 202 203 GLU CA C 55.172 0.3 1 636 202 203 GLU CB C 29.762 0.3 1 637 202 203 GLU N N 115.108 0.3 1 638 203 204 LEU H H 7.430 0.020 1 639 203 204 LEU CA C 57.682 0.3 1 640 203 204 LEU CB C 41.583 0.3 1 641 203 204 LEU N N 123.366 0.3 1 642 204 205 ASP H H 8.291 0.020 1 643 204 205 ASP CA C 55.861 0.3 1 644 204 205 ASP CB C 39.765 0.3 1 645 204 205 ASP N N 115.890 0.3 1 646 205 206 THR H H 7.704 0.020 1 647 205 206 THR CA C 61.688 0.3 1 648 205 206 THR CB C 69.506 0.3 1 649 205 206 THR N N 109.249 0.3 1 650 206 207 LEU H H 7.415 0.020 1 651 206 207 LEU CA C 54.817 0.3 1 652 206 207 LEU CB C 42.260 0.3 1 653 206 207 LEU N N 123.458 0.3 1 654 207 208 SER H H 8.338 0.020 1 655 207 208 SER CA C 57.434 0.3 1 656 207 208 SER CB C 63.729 0.3 1 657 207 208 SER N N 118.429 0.3 1 658 208 209 GLU H H 8.658 0.020 1 659 208 209 GLU CA C 59.022 0.3 1 660 208 209 GLU CB C 28.873 0.3 1 661 208 209 GLU N N 122.384 0.3 1 662 209 210 GLU H H 8.643 0.020 1 663 209 210 GLU CA C 58.765 0.3 1 664 209 210 GLU CB C 28.508 0.3 1 665 209 210 GLU N N 118.868 0.3 1 666 210 211 SER H H 7.681 0.020 1 667 210 211 SER CA C 59.500 0.3 1 668 210 211 SER CB C 63.303 0.3 1 669 210 211 SER N N 114.913 0.3 1 670 211 212 TYR H H 8.189 0.020 1 671 211 212 TYR CA C 60.740 0.3 1 672 211 212 TYR CB C 37.877 0.3 1 673 211 212 TYR N N 122.384 0.3 1 674 212 213 LYS H H 8.220 0.020 1 675 212 213 LYS CA C 59.437 0.3 1 676 212 213 LYS CB C 30.947 0.3 1 677 212 213 LYS N N 121.700 0.3 1 678 213 214 ASP H H 8.009 0.020 1 679 213 214 ASP CA C 56.771 0.3 1 680 213 214 ASP CB C 39.890 0.3 1 681 213 214 ASP N N 118.478 0.3 1 682 214 215 SER H H 8.291 0.020 1 683 214 215 SER CA C 62.991 0.3 1 684 214 215 SER CB C 61.984 0.3 1 685 214 215 SER N N 115.157 0.3 1 686 215 216 THR H H 8.103 0.020 1 687 215 216 THR CA C 65.786 0.3 1 688 215 216 THR CB C 68.209 0.3 1 689 215 216 THR N N 114.864 0.3 1 690 216 217 LEU H H 7.540 0.020 1 691 216 217 LEU CA C 58.193 0.3 1 692 216 217 LEU CB C 40.660 0.3 1 693 216 217 LEU N N 123.458 0.3 1 694 217 218 ILE H H 7.211 0.020 1 695 217 218 ILE CA C 64.208 0.3 1 696 217 218 ILE CB C 36.614 0.3 1 697 217 218 ILE N N 117.989 0.3 1 698 218 219 MET H H 8.291 0.020 1 699 218 219 MET CA C 59.742 0.3 1 700 218 219 MET CB C 32.503 0.3 1 701 218 219 MET N N 118.771 0.3 1 702 219 220 GLN H H 7.797 0.020 1 703 219 220 GLN CA C 58.290 0.3 1 704 219 220 GLN CB C 27.178 0.3 1 705 219 220 GLN N N 118.337 0.3 1 706 220 221 LEU H H 7.430 0.020 1 707 220 221 LEU CA C 57.541 0.3 1 708 220 221 LEU CB C 40.601 0.3 1 709 220 221 LEU N N 119.749 0.3 1 710 222 223 ARG H H 7.876 0.020 1 711 222 223 ARG CA C 58.405 0.3 1 712 222 223 ARG CB C 28.628 0.3 1 713 222 223 ARG N N 118.868 0.3 1 714 223 224 ASP H H 8.721 0.020 1 715 223 224 ASP CA C 56.890 0.3 1 716 223 224 ASP CB C 38.884 0.3 1 717 223 224 ASP N N 121.798 0.3 1 718 224 225 ASN H H 7.579 0.020 1 719 224 225 ASN CA C 54.758 0.3 1 720 224 225 ASN CB C 34.974 0.3 1 721 224 225 ASN N N 120.675 0.3 1 722 225 226 LEU H H 7.657 0.020 1 723 225 226 LEU CA C 58.043 0.3 1 724 225 226 LEU CB C 40.732 0.3 1 725 225 226 LEU N N 119.112 0.3 1 726 226 227 THR H H 7.939 0.020 1 727 226 227 THR CA C 66.009 0.3 1 728 226 227 THR CB C 68.179 0.3 1 729 226 227 THR N N 116.622 0.3 1 730 227 228 LEU H H 7.258 0.020 1 731 227 228 LEU CA C 57.541 0.3 1 732 227 228 LEU CB C 40.957 0.3 1 733 227 228 LEU N N 123.604 0.3 1 734 228 229 TRP H H 8.664 0.020 1 735 228 229 TRP CA C 56.336 0.3 1 736 228 229 TRP CB C 30.199 0.3 1 737 228 229 TRP N N 118.873 0.3 1 738 229 230 THR H H 7.712 0.020 1 739 229 230 THR CA C 62.280 0.3 1 740 229 230 THR CB C 69.684 0.3 1 741 229 230 THR N N 109.786 0.3 1 742 230 231 SER H H 7.688 0.020 1 743 230 231 SER CA C 59.022 0.3 1 744 230 231 SER CB C 63.287 0.3 1 745 230 231 SER N N 118.282 0.3 1 746 231 232 ASP H H 8.291 0.020 1 747 231 232 ASP CA C 54.343 0.3 1 748 231 232 ASP CB C 40.601 0.3 1 749 231 232 ASP N N 122.433 0.3 1 750 232 233 THR H H 7.954 0.020 1 751 232 233 THR CA C 61.551 0.3 1 752 232 233 THR CB C 69.537 0.3 1 753 232 233 THR N N 114.083 0.3 1 754 233 234 GLN H H 7.892 0.020 1 755 233 234 GLN CA C 57.186 0.3 1 756 233 234 GLN CB C 29.525 0.3 1 stop_ save_