data_17163 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for a photochromic fluorescent protein Dronpa in the dark state ; _BMRB_accession_number 17163 _BMRB_flat_file_name bmr17163.str _Entry_type original _Submission_date 2010-09-01 _Accession_date 2010-09-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Dronpa is at dark state' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mizuno Hideaki . . 2 Mal Tapas K. . 3 Waelchli Markus . . 4 Fukano Takashi . . 5 Ikura Mitsuhiko . . 6 Miyawaki Atsushi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 171 "13C chemical shifts" 340 "15N chemical shifts" 171 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-12-01 update BMRB 'update entry citation' 2010-11-09 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17163 'photochromic fluorescent protein Dronpa in the bright state' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Molecular basis of photochromism of a fluorescent protein revealed by direct (13)C detection under laser illumination.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21052778 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mizuno Hideaki . . 2 Mal 'Tapas Kumar' . . 3 Walchli Markus . . 4 Fukano Takashi . . 5 Ikura Mitsuhiko . . 6 Miyawaki Atsushi . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 48 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 237 _Page_last 246 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Dronpa _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Dronpa $Dronpa_-_Dark_state 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_Dronpa_-_Dark_state _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dronpa_-_Dark_state _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'photochromic fluorescent protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 225 _Mol_residue_sequence ; GSHMSVIKPDMKIKLRMEGA VNGHPFAIEGVGLGKPFEGK QSMDLKVKEGGPLPFAYDIL TTVFXNRVFAKYPENIVDYF KQSFPEGYSWERSMNYEDGG ICNATNDITLDGDCYIYEIR FDGVNFPANGPVMQKRTVKW EPSTEKLYVRDGVLKGDVNM ALSLEGGGHYRCDFKTTYKA KKVVQLPDYHFVDHHIEIKS HDKDYSNVNLHEHAEAHSEL PRQAK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 HIS 4 1 MET 5 2 SER 6 3 VAL 7 4 ILE 8 5 LYS 9 6 PRO 10 7 ASP 11 8 MET 12 9 LYS 13 10 ILE 14 11 LYS 15 12 LEU 16 13 ARG 17 14 MET 18 15 GLU 19 16 GLY 20 17 ALA 21 18 VAL 22 19 ASN 23 20 GLY 24 21 HIS 25 22 PRO 26 23 PHE 27 24 ALA 28 25 ILE 29 26 GLU 30 27 GLY 31 28 VAL 32 29 GLY 33 30 LEU 34 31 GLY 35 32 LYS 36 33 PRO 37 34 PHE 38 35 GLU 39 36 GLY 40 37 LYS 41 38 GLN 42 39 SER 43 40 MET 44 41 ASP 45 42 LEU 46 43 LYS 47 44 VAL 48 45 LYS 49 46 GLU 50 47 GLY 51 48 GLY 52 49 PRO 53 50 LEU 54 51 PRO 55 52 PHE 56 53 ALA 57 54 TYR 58 55 ASP 59 56 ILE 60 57 LEU 61 58 THR 62 59 THR 63 60 VAL 64 61 PHE 65 62 GYC 66 63 ASN 67 64 ARG 68 65 VAL 69 66 PHE 70 67 ALA 71 68 LYS 72 69 TYR 73 70 PRO 74 71 GLU 75 72 ASN 76 73 ILE 77 74 VAL 78 75 ASP 79 76 TYR 80 77 PHE 81 78 LYS 82 79 GLN 83 80 SER 84 81 PHE 85 82 PRO 86 83 GLU 87 84 GLY 88 85 TYR 89 86 SER 90 87 TRP 91 88 GLU 92 89 ARG 93 90 SER 94 91 MET 95 92 ASN 96 93 TYR 97 94 GLU 98 95 ASP 99 96 GLY 100 97 GLY 101 98 ILE 102 99 CYS 103 100 ASN 104 101 ALA 105 102 THR 106 103 ASN 107 104 ASP 108 105 ILE 109 106 THR 110 107 LEU 111 108 ASP 112 109 GLY 113 110 ASP 114 111 CYS 115 112 TYR 116 113 ILE 117 114 TYR 118 115 GLU 119 116 ILE 120 117 ARG 121 118 PHE 122 119 ASP 123 120 GLY 124 121 VAL 125 122 ASN 126 123 PHE 127 124 PRO 128 125 ALA 129 126 ASN 130 127 GLY 131 128 PRO 132 129 VAL 133 130 MET 134 131 GLN 135 132 LYS 136 133 ARG 137 134 THR 138 135 VAL 139 136 LYS 140 137 TRP 141 138 GLU 142 139 PRO 143 140 SER 144 141 THR 145 142 GLU 146 143 LYS 147 144 LEU 148 145 TYR 149 146 VAL 150 147 ARG 151 148 ASP 152 149 GLY 153 150 VAL 154 151 LEU 155 152 LYS 156 153 GLY 157 154 ASP 158 155 VAL 159 156 ASN 160 157 MET 161 158 ALA 162 159 LEU 163 160 SER 164 161 LEU 165 162 GLU 166 163 GLY 167 164 GLY 168 165 GLY 169 166 HIS 170 167 TYR 171 168 ARG 172 169 CYS 173 170 ASP 174 171 PHE 175 172 LYS 176 173 THR 177 174 THR 178 175 TYR 179 176 LYS 180 177 ALA 181 178 LYS 182 179 LYS 183 180 VAL 184 181 VAL 185 182 GLN 186 183 LEU 187 184 PRO 188 185 ASP 189 186 TYR 190 187 HIS 191 188 PHE 192 189 VAL 193 190 ASP 194 191 HIS 195 192 HIS 196 193 ILE 197 194 GLU 198 195 ILE 199 196 LYS 200 197 SER 201 198 HIS 202 199 ASP 203 200 LYS 204 201 ASP 205 202 TYR 206 203 SER 207 204 ASN 208 205 VAL 209 206 ASN 210 207 LEU 211 208 HIS 212 209 GLU 213 210 HIS 214 211 ALA 215 212 GLU 216 213 ALA 217 214 HIS 218 215 SER 219 216 GLU 220 217 LEU 221 218 PRO 222 219 ARG 223 220 GLN 224 221 ALA 225 222 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-23 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17162 Dronpa 100.00 225 100.00 100.00 1.47e-165 PDB 2GX0 "Crystal Structural And Functional Analysis Of Gfp-Like Fluorescent Protein" 100.00 241 99.11 99.56 6.06e-163 PDB 2GX2 "Crystal Structural And Functional Analysis Of Gfp-Like Fluorescent Protein Dronpa" 100.00 241 99.11 99.56 6.06e-163 PDB 2IE2 "The 1.7 A Crystal Structure Of Dronpa: A Photoswitchable Green Fluorescent Protein" 98.67 222 100.00 100.00 5.85e-163 PDB 2IOV "Bright-State Structure Of The Reversibly Switchable Fluorescent Protein Dronpa" 98.67 255 100.00 100.00 2.40e-162 PDB 2POX "Dark State Structure Of The Reversibly Switchable Fluorescent Protein Dronpa" 98.67 255 100.00 100.00 2.40e-162 PDB 2Z1O "Crystal Structure Of A Photoswitchable Gfp-Like Protein Dronpa In The Bright-State" 100.00 225 100.00 100.00 1.47e-165 PDB 2Z6X "Crystal Structure Of 22g, The Wild-Type Protein Of The Photoswitchable Gfp-Like Protein Dronpa" 98.67 255 97.30 98.20 9.88e-157 PDB 2Z6Y "Crystal Structure Of A Photoswitchable Gfp-Like Protein Dronpa In The Bright-State" 100.00 225 100.00 100.00 1.47e-165 PDB 2Z6Z "Crystal Structure Of A Photoswitchable Gfp-Like Protein Dronpa In The Bright-State" 98.67 255 100.00 100.00 2.40e-162 PDB 4EMQ "Crystal Structure Of A Single Mutant Of Dronpa, The Green-on-state Pdm1-4" 98.67 255 99.55 99.55 1.23e-161 PDB 4HQ8 "Crystal Structure Of A Green-to-red Photoconvertible Dronpa, Pcdronpa In The Green-on-state" 100.00 258 98.22 98.67 3.20e-161 PDB 4HQ9 "Crystal Structure Of A Green-to-red Photoconvertible Dronpa, Pcdronpa In The Green-off-state" 100.00 258 98.22 98.67 3.20e-161 PDB 4HQC "Crystal Structure Of A Green-to-red Photoconvertible Dronpa, Pcdronpa In The Red-on-state" 100.00 258 97.78 98.22 4.10e-160 PDB 4IZN "Structure Of Pcdronpa-a69t Mutant" 98.67 255 97.75 98.20 2.89e-158 PDB 4UTS "Room Temperature Crystal Structure Of The Fast Switching M159t Mutant Of Fluorescent Protein Dronpa" 95.11 214 99.53 99.53 1.51e-155 DBJ BAD72874 "fluorescent protein Dronpa [Echinophyllia sp. SC22]" 99.56 224 98.66 98.66 1.05e-160 GB ABV80244 "fluorescent protein rsFastLime [synthetic construct]" 99.56 237 98.21 98.21 3.11e-159 GB ADE48854 "Dronpa, partial [Plant transformation vector pSITEII-8C1]" 99.56 224 98.66 98.66 1.05e-160 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_GYC _Saveframe_category polymer_residue _Mol_type 'L-PEPTIDE LINKING' _Name_common '[(4Z)-2-[(1R)-1-AMINO-2-MERCAPTOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC ACID' _BMRB_code . _PDB_code GYC _Standard_residue_derivative . _Molecular_mass 321.352 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jan 9 14:27:16 2012 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? SG1 SG1 S . 0 . ? CB1 CB1 C . 0 . ? CA1 CA1 C . 0 . ? C1 C1 C . 0 . ? N2 N2 N . 0 . ? N3 N3 N . 0 . ? C2 C2 C . 0 . ? O2 O2 O . 0 . ? CA2 CA2 C . 0 . ? CA3 CA3 C . 0 . ? CB2 CB2 C . 0 . ? CG2 CG2 C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? CE2 CE2 C . 0 . ? CZ CZ C . 0 . ? OH OH O . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? HXT HXT H . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? HG1 HG1 H . 0 . ? HB11 HB11 H . 0 . ? HB12 HB12 H . 0 . ? HA1 HA1 H . 0 . ? HA31 HA31 H . 0 . ? HA32 HA32 H . 0 . ? HB2 HB2 H . 0 . ? HD1 HD1 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HOH HOH H . 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 N CA1 ? ? SING N HN1 ? ? SING N HN2 ? ? SING SG1 CB1 ? ? SING SG1 HG1 ? ? SING CB1 CA1 ? ? SING CB1 HB11 ? ? SING CB1 HB12 ? ? SING CA1 C1 ? ? SING CA1 HA1 ? ? DOUB C1 N2 ? ? SING C1 N3 ? ? SING N2 CA2 ? ? SING N3 C2 ? ? SING N3 CA3 ? ? DOUB C2 O2 ? ? SING C2 CA2 ? ? DOUB CA2 CB2 ? ? SING CA3 C ? ? SING CA3 HA31 ? ? SING CA3 HA32 ? ? SING CB2 CG2 ? ? SING CB2 HB2 ? ? DOUB CG2 CD1 ? ? SING CG2 CD2 ? ? SING CD1 CE1 ? ? SING CD1 HD1 ? ? DOUB CD2 CE2 ? ? SING CD2 HD2 ? ? DOUB CE1 CZ ? ? SING CE1 HE1 ? ? SING CE2 CZ ? ? SING CE2 HE2 ? ? SING CZ OH ? ? SING OH HOH ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Dronpa_-_Dark_state 'stony corals' 301887 Eukaryota Metazoa Echinophyllia . 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 $Dronpa_-_Dark_state 'recombinant technology' . Escherichia coli . pET28a 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 $Dronpa_-_Dark_state 2.3 mM '[U-99% 13C; U-99% 15N]' H2O 98 % 'natural abundance' D2O 2 % 'natural abundance' 'phosphate buffer' 20 mM 'natural abundance' NaCl 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ 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 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 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' 96.4 . mM pH 7.5 . pH pressure 1 . atm temperature 300 . 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 $citation_1 $citation_1 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 CBCA(CO)NH' '3D HNCACB' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Dronpa _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 3 6 VAL H H 7.906 0.02 1 2 3 6 VAL CA C 59.232 0.02 1 3 3 6 VAL CB C 29.164 0.02 1 4 3 6 VAL N N 117.455 0.02 1 5 4 7 ILE H H 7.759 0.02 1 6 4 7 ILE CA C 56.614 0.02 1 7 4 7 ILE CB C 33.153 0.02 1 8 4 7 ILE N N 120.128 0.02 1 9 5 8 LYS H H 7.908 0.02 1 10 5 8 LYS CA C 50.507 0.02 1 11 5 8 LYS CB C 30.528 0.02 1 12 5 8 LYS N N 128.719 0.02 1 13 6 9 PRO CA C 62.035 0.02 1 14 6 9 PRO CB C 29.26 0.02 1 15 7 10 ASP H H 7.05 0.02 1 16 7 10 ASP CA C 50.495 0.02 1 17 7 10 ASP CB C 40.708 0.02 1 18 7 10 ASP N N 112.591 0.02 1 19 8 11 MET H H 9.01 0.02 1 20 8 11 MET CA C 51.662 0.02 1 21 8 11 MET CB C 34.582 0.02 1 22 8 11 MET N N 118.773 0.005 1 23 9 12 LYS H H 8.663 0.001 1 24 9 12 LYS CA C 53.357 0.02 1 25 9 12 LYS CB C 32.689 0.02 1 26 9 12 LYS N N 121.887 0.02 1 27 10 13 ILE H H 7.805 0.02 1 28 10 13 ILE CA C 58.382 0.02 1 29 10 13 ILE CB C 41.902 0.02 1 30 10 13 ILE N N 119.119 0.02 1 31 11 14 LYS H H 8.878 0.02 1 32 11 14 LYS CA C 53.584 0.02 1 33 11 14 LYS CB C 33.811 0.02 1 34 11 14 LYS N N 128.841 0.02 1 35 12 15 LEU H H 8.561 0.02 1 36 12 15 LEU CA C 50.387 0.02 1 37 12 15 LEU CB C 45.355 0.02 1 38 12 15 LEU N N 117.495 0.02 1 39 13 16 ARG H H 7.551 0.02 1 40 13 16 ARG CA C 53.708 0.02 1 41 13 16 ARG CB C 30.242 0.02 1 42 13 16 ARG N N 120.698 0.02 1 43 14 17 MET H H 9.482 0.001 1 44 14 17 MET CA C 51.357 0.02 1 45 14 17 MET CB C 35.916 0.02 1 46 14 17 MET N N 126.277 0.004 1 47 16 19 GLY H H 7.704 0.02 1 48 16 19 GLY CA C 43.896 0.02 1 49 16 19 GLY N N 108.542 0.02 1 50 17 20 ALA H H 8.111 0.001 1 51 17 20 ALA CA C 49.46 0.02 1 52 17 20 ALA CB C 18.913 0.02 1 53 17 20 ALA N N 119.105 0.02 1 54 18 21 VAL H H 8.058 0.02 1 55 18 21 VAL CA C 58.151 0.02 1 56 18 21 VAL CB C 32.3 0.02 1 57 18 21 VAL N N 119.052 0.02 1 58 19 22 ASN H H 9.335 0.02 1 59 19 22 ASN CA C 50.523 0.02 1 60 19 22 ASN CB C 33.451 0.02 1 61 19 22 ASN N N 129.467 0.02 1 62 20 23 GLY H H 9.018 0.02 1 63 20 23 GLY CA C 42.296 0.02 1 64 20 23 GLY N N 102.559 0.02 1 65 21 24 HIS H H 8.267 0.02 1 66 21 24 HIS CA C 51.378 0.02 1 67 21 24 HIS CB C 28.449 0.02 1 68 21 24 HIS N N 123.671 0.02 1 69 22 25 PRO CA C 58.75 0.02 1 70 22 25 PRO CB C 29.931 0.02 1 71 23 26 PHE H H 8.409 0.001 1 72 23 26 PHE CA C 53.859 0.02 1 73 23 26 PHE CB C 39.134 0.02 1 74 23 26 PHE N N 114.751 0.02 1 75 24 27 ALA H H 8.644 0.02 1 76 24 27 ALA CA C 49.356 0.02 1 77 24 27 ALA CB C 19.643 0.02 1 78 24 27 ALA N N 120.246 0.003 1 79 25 28 ILE H H 9.282 0.001 1 80 25 28 ILE CA C 57.71 0.02 1 81 25 28 ILE CB C 41.995 0.02 1 82 25 28 ILE N N 123.671 0.02 1 83 26 29 GLU H H 8.75 0.02 1 84 26 29 GLU CA C 51.712 0.02 1 85 26 29 GLU CB C 31.199 0.02 1 86 26 29 GLU N N 124.645 0.02 1 87 27 30 GLY H H 8.28 0.02 1 88 27 30 GLY CA C 42.682 0.02 1 89 27 30 GLY N N 106.487 0.02 1 90 28 31 VAL H H 8.275 0.02 1 91 28 31 VAL CA C 57.248 0.02 1 92 28 31 VAL CB C 32.952 0.02 1 93 28 31 VAL N N 117.482 0.004 1 94 29 32 GLY H H 8.925 0.02 1 95 29 32 GLY CA C 43.096 0.02 1 96 29 32 GLY N N 111.294 0.02 1 97 30 33 LEU H H 8.837 0.02 1 98 30 33 LEU CA C 51.899 0.02 1 99 30 33 LEU CB C 42.523 0.02 1 100 30 33 LEU N N 122.846 0.02 1 101 31 34 GLY H H 9.188 0.02 1 102 31 34 GLY CA C 42.731 0.02 1 103 31 34 GLY N N 108.457 0.02 1 104 32 35 LYS H H 8.9 0.02 1 105 32 35 LYS CA C 53.721 0.02 1 106 32 35 LYS CB C 32.142 0.02 1 107 32 35 LYS N N 120.896 0.02 1 108 33 36 PRO CA C 62.782 0.02 1 109 33 36 PRO CB C 30.419 0.02 1 110 34 37 PHE H H 8.5 0.02 1 111 34 37 PHE CA C 55.747 0.02 1 112 34 37 PHE CB C 34.892 0.02 1 113 34 37 PHE N N 109.761 0.02 1 114 35 38 GLU H H 7.21 0.02 1 115 35 38 GLU CA C 53.248 0.02 1 116 35 38 GLU CB C 28.244 0.02 1 117 35 38 GLU N N 115.124 0.004 1 118 36 39 GLY H H 7.801 0.02 1 119 36 39 GLY CA C 44.307 0.02 1 120 36 39 GLY N N 106.425 0.02 1 121 37 40 LYS H H 7.024 0.02 1 122 37 40 LYS CA C 52.095 0.02 1 123 37 40 LYS CB C 34.518 0.02 1 124 37 40 LYS N N 113.444 0.004 1 125 38 41 GLN H H 8.267 0.02 1 126 38 41 GLN CA C 52.387 0.02 1 127 38 41 GLN CB C 28.581 0.02 1 128 38 41 GLN N N 115.345 0.02 1 129 39 42 SER H H 8.573 0.02 1 130 39 42 SER CA C 54.198 0.02 1 131 39 42 SER CB C 62.928 0.02 1 132 39 42 SER N N 114.453 0.02 1 133 40 43 MET H H 8.788 0.001 1 134 40 43 MET CA C 51.861 0.02 1 135 40 43 MET CB C 33.221 0.02 1 136 40 43 MET N N 115.902 0.02 1 137 41 44 ASP H H 8.867 0.02 1 138 41 44 ASP CA C 51.494 0.02 1 139 41 44 ASP CB C 40.913 0.02 1 140 41 44 ASP N N 121.09 0.02 1 141 42 45 LEU H H 9.425 0.02 1 142 42 45 LEU CA C 51.107 0.02 1 143 42 45 LEU CB C 41.863 0.02 1 144 42 45 LEU N N 125.37 0.02 1 145 43 46 LYS H H 9.295 0.02 1 146 43 46 LYS CA C 51.53 0.02 1 147 43 46 LYS CB C 33.5 0.02 1 148 43 46 LYS N N 124.563 0.02 1 149 44 47 VAL H H 8.623 0.02 1 150 44 47 VAL CA C 61.447 0.02 1 151 44 47 VAL CB C 29.164 0.02 1 152 44 47 VAL N N 126.081 0.02 1 153 45 48 LYS H H 9.027 0.02 1 154 45 48 LYS CA C 52.197 0.02 1 155 45 48 LYS CB C 30.568 0.02 1 156 45 48 LYS N N 129.535 0.02 1 157 46 49 GLU H H 8.05 0.02 1 158 46 49 GLU CA C 52.425 0.02 1 159 46 49 GLU CB C 30.735 0.02 1 160 46 49 GLU N N 117.351 0.02 1 161 47 50 GLY H H 8.862 0.02 1 162 47 50 GLY CA C 43.049 0.02 1 163 47 50 GLY N N 108.704 0.02 1 164 48 51 GLY H H 8.544 0.02 1 165 48 51 GLY CA C 40.685 0.02 1 166 48 51 GLY N N 107.02 0.02 1 167 51 54 PRO CA C 59.872 0.02 1 168 51 54 PRO CB C 27.71 0.02 1 169 52 55 PHE H H 5.711 0.02 1 170 52 55 PHE CA C 50.256 0.02 1 171 52 55 PHE CB C 39.71 0.02 1 172 52 55 PHE N N 111.009 0.02 1 173 53 56 ALA H H 7.953 0.02 1 174 53 56 ALA CA C 49.765 0.02 1 175 53 56 ALA CB C 18.001 0.02 1 176 53 56 ALA N N 120.628 0.02 1 177 54 57 TYR H H 7.745 0.02 1 178 54 57 TYR CA C 58.319 0.02 1 179 54 57 TYR CB C 36.405 0.02 1 180 54 57 TYR N N 128.429 0.02 1 181 55 58 ASP H H 7.7 0.02 1 182 55 58 ASP CA C 55.129 0.02 1 183 55 58 ASP CB C 39.217 0.02 1 184 55 58 ASP N N 110.885 0.02 1 185 56 59 ILE H H 7.258 0.02 1 186 56 59 ILE CA C 62.524 0.02 1 187 56 59 ILE CB C 34.408 0.02 1 188 56 59 ILE N N 109.993 0.02 1 189 57 60 LEU H H 8.58 0.02 1 190 57 60 LEU CA C 52.5 0.02 1 191 57 60 LEU CB C 40.982 0.02 1 192 57 60 LEU N N 120.508 0.02 1 193 58 61 THR H H 7.385 0.02 1 194 58 61 THR CA C 64.493 0.02 1 195 58 61 THR CB C 64.439 0.02 1 196 58 61 THR N N 107.614 0.02 1 197 59 62 THR H H 7.869 0.02 1 198 59 62 THR CA C 59.988 0.02 1 199 59 62 THR CB C 65.019 0.02 1 200 59 62 THR N N 109.334 0.02 1 201 60 63 VAL H H 7.269 0.001 1 202 60 63 VAL CA C 61.195 0.02 1 203 60 63 VAL CB C 26.977 0.02 1 204 60 63 VAL N N 123.156 0.02 1 205 61 64 PHE H H 6.196 0.02 1 206 61 64 PHE CA C 56.686 0.02 1 207 61 64 PHE CB C 36.508 0.02 1 208 61 64 PHE N N 114.091 0.005 1 209 62 65 GYC H H 7.321 0.02 1 210 62 65 GYC CA C 48.518 0.02 1 211 62 65 GYC CB C 25.808 0.02 1 212 62 65 GYC N N 113.537 0.008 1 213 70 71 LYS H H 8.048 0.02 1 214 70 71 LYS CA C 53.582 0.02 1 215 70 71 LYS CB C 30.368 0.02 1 216 70 71 LYS N N 122.184 0.02 1 217 71 72 TYR H H 9.228 0.02 1 218 71 72 TYR CA C 53.14 0.02 1 219 71 72 TYR CB C 38.312 0.02 1 220 71 72 TYR N N 133.664 0.006 1 221 72 73 PRO CA C 59.086 0.02 1 222 72 73 PRO CB C 29.816 0.02 1 223 73 74 GLU H H 8.793 0.02 1 224 73 74 GLU CA C 55.777 0.02 1 225 73 74 GLU CB C 26.732 0.02 1 226 73 74 GLU N N 117.478 0.02 1 227 74 75 ASN H H 7.973 0.02 1 228 74 75 ASN CA C 49.947 0.02 1 229 74 75 ASN CB C 34.405 0.02 1 230 74 75 ASN N N 111.814 0.005 1 231 75 76 ILE H H 7.24 0.02 1 232 75 76 ILE CA C 57.886 0.02 1 233 75 76 ILE CB C 38.468 0.02 1 234 75 76 ILE N N 120.4 0.02 1 235 76 77 VAL H H 8.001 0.02 1 236 76 77 VAL CA C 61.265 0.02 1 237 76 77 VAL CB C 29.116 0.02 1 238 76 77 VAL N N 127.722 0.02 1 239 77 78 ASP H H 8.118 0.001 1 240 77 78 ASP CA C 48.433 0.02 1 241 77 78 ASP CB C 37.494 0.02 1 242 77 78 ASP N N 127.586 0.02 1 243 78 79 TYR H H 8.867 0.02 1 244 78 79 TYR CA C 57.743 0.02 1 245 78 79 TYR CB C 38.622 0.02 1 246 78 79 TYR N N 126.645 0.02 1 247 79 80 PHE H H 6.543 0.001 1 248 79 80 PHE CA C 56.686 0.02 1 249 79 80 PHE CB C 34.993 0.02 1 250 79 80 PHE N N 110.885 0.02 1 251 80 81 LYS H H 8.162 0.02 1 252 80 81 LYS CA C 58.678 0.02 1 253 80 81 LYS CB C 28.921 0.02 1 254 80 81 LYS N N 119.315 0.005 1 255 81 82 GLN H H 6.991 0.001 1 256 81 82 GLN CA C 55.555 0.02 1 257 81 82 GLN CB C 29.08 0.02 1 258 81 82 GLN N N 113.256 0.004 1 259 82 83 SER H H 6.947 0.02 1 260 82 83 SER CA C 58.896 0.02 1 261 82 83 SER CB C 60.327 0.02 1 262 82 83 SER N N 111.503 0.005 1 263 83 84 PHE H H 6.823 0.001 1 264 83 84 PHE CA C 57.105 0.02 1 265 83 84 PHE CB C 35.994 0.02 1 266 83 84 PHE N N 120.23 0.01 1 267 84 85 PRO CA C 61.318 0.02 1 268 84 85 PRO CB C 32.883 0.02 1 269 85 86 GLU H H 10.478 0.02 1 270 85 86 GLU CA C 59.852 0.02 1 271 85 86 GLU CB C 25.169 0.02 1 272 85 86 GLU N N 126.645 0.02 1 273 86 87 GLY H H 8.227 0.02 1 274 86 87 GLY CA C 41.082 0.02 1 275 86 87 GLY N N 103.446 0.02 1 276 87 88 TYR H H 7.717 0.02 1 277 87 88 TYR CA C 52.621 0.02 1 278 87 88 TYR CB C 37.044 0.02 1 279 87 88 TYR N N 112.305 0.004 1 280 88 89 SER H H 8.736 0.001 1 281 88 89 SER CA C 52.882 0.02 1 282 88 89 SER CB C 64.541 0.02 1 283 88 89 SER N N 113.479 0.02 1 284 89 90 TRP H H 8.795 0.02 1 285 89 90 TRP CA C 51.97 0.02 1 286 89 90 TRP CB C 32.026 0.02 1 287 89 90 TRP N N 114.751 0.02 1 288 92 93 SER H H 8.887 0.02 1 289 92 93 SER CA C 53.647 0.02 1 290 92 93 SER CB C 62.77 0.02 1 291 92 93 SER N N 121.059 0.006 1 292 93 94 MET H H 8.652 0.02 1 293 93 94 MET CA C 51.424 0.02 1 294 93 94 MET CB C 32.904 0.02 1 295 93 94 MET N N 124.659 0.02 1 296 95 96 TYR H H 9.115 0.02 1 297 95 96 TYR CA C 56.891 0.02 1 298 95 96 TYR CB C 37.58 0.02 1 299 95 96 TYR N N 126.663 0.006 1 300 96 97 GLU H H 8.11 0.001 1 301 96 97 GLU CA C 56.389 0.02 1 302 96 97 GLU CB C 27.519 0.02 1 303 96 97 GLU N N 117.551 0.013 1 304 97 98 ASP H H 8.004 0.001 1 305 97 98 ASP CA C 49.687 0.02 1 306 97 98 ASP CB C 38.091 0.02 1 307 97 98 ASP N N 117.458 0.003 1 308 98 99 GLY H H 7.886 0.02 1 309 98 99 GLY CA C 42.35 0.02 1 310 98 99 GLY N N 107.02 0.02 1 311 99 100 GLY H H 6.871 0.02 1 312 99 100 GLY CA C 42.723 0.02 1 313 99 100 GLY N N 104.046 0.02 1 314 100 101 ILE H H 8.448 0.001 1 315 100 101 ILE CA C 57.479 0.02 1 316 100 101 ILE CB C 38.967 0.02 1 317 100 101 ILE N N 124.942 0.005 1 318 101 102 CYS H H 9.092 0.02 1 319 101 102 CYS CA C 52.164 0.02 1 320 101 102 CYS CB C 28.591 0.02 1 321 101 102 CYS N N 121.887 0.02 1 322 102 103 ASN H H 8.871 0.02 1 323 102 103 ASN CA C 49.456 0.02 1 324 102 103 ASN CB C 39.684 0.02 1 325 102 103 ASN N N 122.075 0.02 1 326 103 104 ALA H H 8.895 0.001 1 327 103 104 ALA CA C 47.409 0.02 1 328 103 104 ALA CB C 22.516 0.02 1 329 103 104 ALA N N 123.717 0.02 1 330 104 105 THR H H 8.587 0.001 1 331 104 105 THR CA C 56.421 0.02 1 332 104 105 THR CB C 68.922 0.02 1 333 104 105 THR N N 111.853 0.02 1 334 105 106 ASN H H 7.33 0.02 1 335 105 106 ASN CA C 48.16 0.02 1 336 105 106 ASN CB C 35.959 0.02 1 337 105 106 ASN N N 117.129 0.02 1 338 106 107 ASP H H 8.02 0.001 1 339 106 107 ASP CA C 51.448 0.02 1 340 106 107 ASP CB C 40.693 0.02 1 341 106 107 ASP N N 127.518 0.02 1 342 107 108 ILE H H 8.054 0.001 1 343 107 108 ILE CA C 59.302 0.02 1 344 107 108 ILE CB C 36.022 0.02 1 345 107 108 ILE N N 126.25 0.02 1 346 108 109 THR H H 9.129 0.02 1 347 108 109 THR CA C 57.202 0.02 1 348 108 109 THR CB C 69.367 0.02 1 349 108 109 THR N N 119.71 0.02 1 350 109 110 LEU H H 8.905 0.02 1 351 109 110 LEU CA C 51.635 0.02 1 352 109 110 LEU CB C 43.051 0.02 1 353 109 110 LEU N N 122.371 0.003 1 354 110 111 ASP H H 8.918 0.02 1 355 110 111 ASP CA C 49.789 0.02 1 356 110 111 ASP CB C 39.34 0.02 1 357 110 111 ASP N N 128.32 0.007 1 358 111 112 GLY H H 8.901 0.02 1 359 111 112 GLY CA C 44.898 0.02 1 360 111 112 GLY N N 116.143 0.02 1 361 112 113 ASP H H 8.252 0.02 1 362 112 113 ASP CA C 50.116 0.02 1 363 112 113 ASP CB C 37.494 0.02 1 364 112 113 ASP N N 126.915 0.02 1 365 113 114 CYS H H 7.696 0.02 1 366 113 114 CYS CA C 53.529 0.02 1 367 113 114 CYS CB C 26.532 0.02 1 368 113 114 CYS N N 120.103 0.02 1 369 114 115 TYR H H 9.144 0.001 1 370 114 115 TYR CA C 56.077 0.02 1 371 114 115 TYR CB C 38.407 0.02 1 372 114 115 TYR N N 128.617 0.02 1 373 115 116 ILE H H 9.1 0.02 1 374 115 116 ILE CA C 56.654 0.02 1 375 115 116 ILE CB C 35.788 0.02 1 376 115 116 ILE N N 123.57 0.02 1 377 116 117 TYR H H 8.666 0.02 1 378 116 117 TYR CA C 49.919 0.02 1 379 116 117 TYR CB C 35.26 0.02 1 380 116 117 TYR N N 124.088 0.02 1 381 117 118 GLU H H 8.463 0.02 1 382 117 118 GLU CA C 53.354 0.02 1 383 117 118 GLU CB C 28.775 0.02 1 384 117 118 GLU N N 125.902 0.02 1 385 119 120 ARG H H 8.292 0.02 1 386 119 120 ARG CA C 50.481 0.02 1 387 119 120 ARG CB C 29.262 0.02 1 388 119 120 ARG N N 129.654 0.006 1 389 120 121 PHE H H 8.262 0.02 1 390 120 121 PHE CA C 54.183 0.02 1 391 120 121 PHE CB C 42.122 0.02 1 392 120 121 PHE N N 126.793 0.005 1 393 121 122 ASP H H 8.341 0.02 1 394 121 122 ASP CA C 51.238 0.02 1 395 121 122 ASP CB C 42.403 0.02 1 396 121 122 ASP N N 126.425 0.006 1 397 122 123 GLY H H 9.447 0.02 1 398 122 123 GLY CA C 43.316 0.02 1 399 122 123 GLY N N 110.691 0.02 1 400 123 124 VAL H H 9.317 0.02 1 401 123 124 VAL CA C 57.248 0.02 1 402 123 124 VAL CB C 33.543 0.02 1 403 123 124 VAL N N 122.035 0.02 1 404 124 125 ASN H H 8.643 0.002 1 405 124 125 ASN CA C 50.78 0.02 1 406 124 125 ASN CB C 33.922 0.02 1 407 124 125 ASN N N 113.967 0.02 1 408 125 126 PHE H H 8.588 0.02 1 409 125 126 PHE CA C 55.801 0.02 1 410 125 126 PHE CB C 34.974 0.02 1 411 125 126 PHE N N 118.097 0.02 1 412 128 129 ASN H H 8.044 0.02 1 413 128 129 ASN CA C 48.927 0.02 1 414 128 129 ASN CB C 34.759 0.02 1 415 128 129 ASN N N 110.364 0.02 1 416 129 130 GLY H H 7.273 0.02 1 417 129 130 GLY CA C 42.285 0.02 1 418 129 130 GLY N N 105.533 0.02 1 419 130 131 PRO CA C 61.332 0.02 1 420 130 131 PRO CB C 29.811 0.02 1 421 131 132 VAL H H 6.66 0.02 1 422 131 132 VAL CA C 62.874 0.02 1 423 131 132 VAL CB C 28.319 0.02 1 424 131 132 VAL N N 116.675 0.02 1 425 133 134 GLN H H 7.501 0.001 1 426 133 134 GLN CA C 52.078 0.02 1 427 133 134 GLN CB C 25.217 0.02 1 428 133 134 GLN N N 111.703 0.004 1 429 134 135 LYS H H 7.198 0.02 1 430 134 135 LYS CA C 55.282 0.02 1 431 134 135 LYS CB C 25.659 0.02 1 432 134 135 LYS N N 115.94 0.02 1 433 135 136 ARG H H 8.455 0.02 1 434 135 136 ARG CA C 52.019 0.02 1 435 135 136 ARG CB C 28.397 0.02 1 436 135 136 ARG N N 115.345 0.02 1 437 136 137 THR H H 7.793 0.02 1 438 136 137 THR CA C 58.84 0.02 1 439 136 137 THR CB C 65.551 0.02 1 440 136 137 THR N N 110.83 0.02 1 441 137 138 VAL H H 8.751 0.02 1 442 137 138 VAL CA C 61.796 0.02 1 443 137 138 VAL CB C 30.263 0.02 1 444 137 138 VAL N N 120.508 0.003 1 445 138 139 LYS H H 6.926 0.02 1 446 138 139 LYS CA C 53.08 0.02 1 447 138 139 LYS CB C 30.276 0.02 1 448 138 139 LYS N N 111.963 0.02 1 449 139 140 TRP H H 8.809 0.001 1 450 139 140 TRP CA C 54.374 0.02 1 451 139 140 TRP CB C 27.566 0.02 1 452 139 140 TRP N N 121.511 0.007 1 453 146 147 LEU H H 8.444 0.02 1 454 146 147 LEU CA C 51.466 0.02 1 455 146 147 LEU CB C 39.782 0.02 1 456 146 147 LEU N N 126.645 0.02 1 457 147 148 TYR H H 8.43 0.02 1 458 147 148 TYR CA C 52.489 0.02 1 459 147 148 TYR CB C 36.566 0.02 1 460 147 148 TYR N N 115.903 0.012 1 461 148 149 VAL H H 8.783 0.02 1 462 148 149 VAL CA C 58.409 0.02 1 463 148 149 VAL CB C 30.137 0.02 1 464 148 149 VAL N N 120.698 0.02 1 465 149 150 ARG H H 8.528 0.02 1 466 149 150 ARG CA C 52.357 0.02 1 467 149 150 ARG CB C 30.733 0.02 1 468 149 150 ARG N N 127.186 0.02 1 469 150 151 ASP H H 9.283 0.02 1 470 150 151 ASP CA C 52.381 0.02 1 471 150 151 ASP CB C 36.609 0.02 1 472 150 151 ASP N N 124.861 0.02 1 473 151 152 GLY H H 8.266 0.02 1 474 151 152 GLY CA C 42.877 0.02 1 475 151 152 GLY N N 102.105 0.02 1 476 152 153 VAL H H 7.673 0.02 1 477 152 153 VAL CA C 56.939 0.02 1 478 152 153 VAL CB C 31.471 0.02 1 479 152 153 VAL N N 116.49 0.007 1 480 153 154 LEU H H 7.7 0.002 1 481 153 154 LEU CA C 51.066 0.02 1 482 153 154 LEU CB C 40.86 0.02 1 483 153 154 LEU N N 122.917 0.005 1 484 154 155 LYS H H 8.978 0.02 1 485 154 155 LYS CA C 49.937 0.02 1 486 154 155 LYS CB C 31.364 0.02 1 487 154 155 LYS N N 127.06 0.006 1 488 155 156 GLY H H 8.401 0.02 1 489 155 156 GLY CA C 42.794 0.02 1 490 155 156 GLY N N 102.347 0.02 1 491 160 161 ALA H H 9.586 0.02 1 492 160 161 ALA CA C 48.985 0.02 1 493 160 161 ALA CB C 19.217 0.02 1 494 160 161 ALA N N 122.378 0.02 1 495 161 162 LEU H H 9.168 0.02 1 496 161 162 LEU CA C 50.506 0.02 1 497 161 162 LEU CB C 40.542 0.02 1 498 161 162 LEU N N 124.861 0.02 1 499 162 163 SER H H 9.017 0.02 1 500 162 163 SER CA C 55.306 0.02 1 501 162 163 SER CB C 60.962 0.02 1 502 162 163 SER N N 119.488 0.02 1 503 163 164 LEU H H 7.655 0.02 1 504 163 164 LEU CA C 49.976 0.02 1 505 163 164 LEU CB C 41.491 0.02 1 506 163 164 LEU N N 122.29 0.02 1 507 164 165 GLU H H 8.402 0.02 1 508 164 165 GLU CA C 55.304 0.02 1 509 164 165 GLU CB C 26.579 0.02 1 510 164 165 GLU N N 123.969 0.02 1 511 166 167 GLY H H 7.777 0.02 1 512 166 167 GLY CA C 41.643 0.02 1 513 166 167 GLY N N 108.314 0.02 1 514 167 168 GLY H H 7.971 0.02 1 515 167 168 GLY CA C 41.184 0.02 1 516 167 168 GLY N N 107.258 0.02 1 517 168 169 HIS H H 8.432 0.02 1 518 168 169 HIS CA C 53.43 0.02 1 519 168 169 HIS CB C 32.201 0.02 1 520 168 169 HIS N N 115.345 0.02 1 521 169 170 TYR H H 9.144 0.02 1 522 169 170 TYR CA C 52.49 0.02 1 523 169 170 TYR CB C 39 0.02 1 524 169 170 TYR N N 126.347 0.02 1 525 170 171 ARG H H 9.664 0.02 1 526 170 171 ARG CA C 53.982 0.02 1 527 170 171 ARG CB C 29.167 0.02 1 528 170 171 ARG N N 127.392 0.02 1 529 171 172 CYS H H 8.55 0.02 1 530 171 172 CYS CA C 54.527 0.02 1 531 171 172 CYS CB C 30.197 0.02 1 532 171 172 CYS N N 118.914 0.02 1 533 172 173 ASP H H 8.383 0.02 1 534 172 173 ASP CA C 51.695 0.02 1 535 172 173 ASP CB C 39.754 0.02 1 536 172 173 ASP N N 129.275 0.011 1 537 173 174 PHE H H 9.318 0.02 1 538 173 174 PHE CA C 53.659 0.02 1 539 173 174 PHE CB C 38.079 0.02 1 540 173 174 PHE N N 129.013 0.011 1 541 174 175 LYS H H 8.343 0.02 1 542 174 175 LYS CA C 53.738 0.02 1 543 174 175 LYS CB C 32.279 0.02 1 544 174 175 LYS N N 121.515 0.01 1 545 175 176 THR H H 9.193 0.02 1 546 175 176 THR CA C 58.794 0.02 1 547 175 176 THR CB C 67.363 0.02 1 548 175 176 THR N N 121.158 0.02 1 549 176 177 THR H H 9.039 0.02 1 550 176 177 THR CA C 59.889 0.02 1 551 176 177 THR CB C 67.548 0.02 1 552 176 177 THR N N 123.511 0.02 1 553 177 178 TYR H H 9.674 0.001 1 554 177 178 TYR CA C 54.336 0.02 1 555 177 178 TYR CB C 38.096 0.02 1 556 177 178 TYR N N 128.969 0.02 1 557 178 179 LYS H H 9.46 0.002 1 558 178 179 LYS CA C 53.034 0.02 1 559 178 179 LYS CB C 32.217 0.02 1 560 178 179 LYS N N 120.536 0.02 1 561 179 180 ALA H H 8.799 0.02 1 562 179 180 ALA CA C 49.887 0.02 1 563 179 180 ALA CB C 16.911 0.02 1 564 179 180 ALA N N 129.648 0.02 1 565 180 181 LYS H H 8.25 0.001 1 566 180 181 LYS CA C 54.52 0.02 1 567 180 181 LYS CB C 29.239 0.02 1 568 180 181 LYS N N 120.06 0.02 1 569 181 182 LYS H H 7.508 0.001 1 570 181 182 LYS CA C 50.964 0.02 1 571 181 182 LYS CB C 31.819 0.02 1 572 181 182 LYS N N 115.516 0.004 1 573 182 183 VAL H H 8.097 0.02 1 574 182 183 VAL CA C 61.692 0.02 1 575 182 183 VAL CB C 28.204 0.02 1 576 182 183 VAL N N 119.432 0.02 1 577 183 184 VAL H H 7.556 0.002 1 578 183 184 VAL CA C 56.076 0.02 1 579 183 184 VAL CB C 31.815 0.02 1 580 183 184 VAL N N 122.626 0.01 1 581 184 185 GLN H H 8.278 0.001 1 582 184 185 GLN CA C 53.516 0.02 1 583 184 185 GLN CB C 25.849 0.02 1 584 184 185 GLN N N 123.076 0.02 1 585 185 186 LEU H H 8.204 0.001 1 586 185 186 LEU CA C 48.994 0.02 1 587 185 186 LEU CB C 38.406 0.02 1 588 185 186 LEU N N 123.374 0.02 1 589 186 187 PRO CA C 58.859 0.02 1 590 186 187 PRO CB C 29.763 0.02 1 591 187 188 ASP H H 7.903 0.02 1 592 187 188 ASP CA C 50.032 0.02 1 593 187 188 ASP CB C 39.411 0.02 1 594 187 188 ASP N N 117.79 0.003 1 595 188 189 TYR H H 8.505 0.02 1 596 188 189 TYR CA C 55.303 0.02 1 597 188 189 TYR CB C 35.476 0.02 1 598 188 189 TYR N N 121.535 0.02 1 599 189 190 HIS H H 8.604 0.02 1 600 189 190 HIS CA C 53.184 0.02 1 601 189 190 HIS CB C 25.153 0.02 1 602 189 190 HIS N N 120 0.02 1 603 190 191 PHE H H 8.32 0.02 1 604 190 191 PHE CA C 53.062 0.02 1 605 190 191 PHE CB C 39.625 0.02 1 606 190 191 PHE N N 115.345 0.02 1 607 196 197 GLU H H 9.297 0.001 1 608 196 197 GLU CA C 52.933 0.02 1 609 196 197 GLU CB C 32.063 0.02 1 610 196 197 GLU N N 127.274 0.006 1 611 197 198 ILE H H 9.579 0.02 1 612 197 198 ILE CA C 60.315 0.02 1 613 197 198 ILE CB C 34.551 0.02 1 614 197 198 ILE N N 126.883 0.002 1 615 198 199 LYS H H 8.707 0.002 1 616 198 199 LYS CA C 54.173 0.02 1 617 198 199 LYS CB C 29.788 0.02 1 618 198 199 LYS N N 131.359 0.02 1 619 199 200 SER H H 7.754 0.02 1 620 199 200 SER CA C 54.773 0.02 1 621 199 200 SER CB C 62.144 0.02 1 622 199 200 SER N N 110.088 0.02 1 623 200 201 HIS H H 8.036 0.02 1 624 200 201 HIS CA C 51.47 0.02 1 625 200 201 HIS CB C 28.541 0.02 1 626 200 201 HIS N N 115.547 0.02 1 627 201 202 ASP H H 8.208 0.001 1 628 201 202 ASP CA C 49.237 0.02 1 629 201 202 ASP CB C 37.922 0.02 1 630 201 202 ASP N N 119.621 0.02 1 631 203 204 ASP H H 7.846 0.02 1 632 203 204 ASP CA C 50.046 0.02 1 633 203 204 ASP CB C 37.656 0.02 1 634 203 204 ASP N N 113.582 0.004 1 635 204 205 TYR H H 7.979 0.02 1 636 204 205 TYR CA C 58.858 0.02 1 637 204 205 TYR CB C 29.878 0.02 1 638 204 205 TYR N N 115.783 0.02 1 639 205 206 SER H H 8.49 0.02 1 640 205 206 SER CA C 60.088 0.02 1 641 205 206 SER CB C 60.383 0.02 1 642 205 206 SER N N 116.582 0.02 1 643 206 207 ASN H H 8.82 0.001 1 644 206 207 ASN CA C 50.256 0.02 1 645 206 207 ASN CB C 38.888 0.02 1 646 206 207 ASN N N 119.966 0.003 1 647 207 208 VAL H H 8.257 0.002 1 648 207 208 VAL CA C 58.854 0.02 1 649 207 208 VAL CB C 35.093 0.02 1 650 207 208 VAL N N 122.823 0.02 1 651 208 209 ASN H H 8.589 0.02 1 652 208 209 ASN CA C 50.123 0.02 1 653 208 209 ASN CB C 39.663 0.02 1 654 208 209 ASN N N 126.182 0.002 1 655 209 210 LEU H H 9.209 0.02 1 656 209 210 LEU CA C 51.062 0.02 1 657 209 210 LEU CB C 45.804 0.02 1 658 209 210 LEU N N 130.226 0.02 1 659 210 211 HIS H H 9.112 0.02 1 660 210 211 HIS CA C 52.164 0.02 1 661 210 211 HIS CB C 33.015 0.02 1 662 210 211 HIS N N 124.227 0.02 1 663 215 216 ALA H H 8.644 0.02 1 664 215 216 ALA CA C 47.198 0.02 1 665 215 216 ALA CB C 17.094 0.02 1 666 215 216 ALA N N 127.352 0.005 1 667 216 217 HIS H H 9.108 0.02 1 668 216 217 HIS CA C 52.312 0.02 1 669 216 217 HIS CB C 29.588 0.02 1 670 216 217 HIS N N 113.768 0.02 1 671 217 218 SER H H 9.001 0.02 1 672 217 218 SER CA C 55.615 0.02 1 673 217 218 SER CB C 61.499 0.02 1 674 217 218 SER N N 115.829 0.004 1 675 218 219 GLU H H 8.941 0.001 1 676 218 219 GLU CA C 53.682 0.02 1 677 218 219 GLU CB C 28.261 0.02 1 678 218 219 GLU N N 122.184 0.02 1 679 219 220 LEU H H 8.278 0.02 1 680 219 220 LEU CA C 50.273 0.02 1 681 219 220 LEU CB C 38.617 0.02 1 682 219 220 LEU N N 125.137 0.005 1 stop_ save_