data_17162 ####################### # 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 bright state ; _BMRB_accession_number 17162 _BMRB_flat_file_name bmr17162.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 a photochromic green fluorescent protein.' 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" 196 "13C chemical shifts" 392 "15N chemical shifts" 196 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 dark 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 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 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Dronpa _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 17163 Dronpa_-_Dark_state 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 Thu Jan 5 16:09:00 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 '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 '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 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 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 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 7.899 0.02 1 2 3 6 VAL CA C 59.387 0.02 1 3 3 6 VAL CB C 29.055 0.02 1 4 3 6 VAL N N 117.4 0.02 1 5 4 7 ILE H H 7.774 0.02 1 6 4 7 ILE CA C 56.519 0.02 1 7 4 7 ILE CB C 33.045 0.02 1 8 4 7 ILE N N 120.125 0.002 1 9 5 8 LYS H H 7.843 0.02 1 10 5 8 LYS CA C 50.533 0.02 1 11 5 8 LYS CB C 30.426 0.02 1 12 5 8 LYS N N 128.492 0.003 1 13 6 9 PRO CA C 61.962 0.02 1 14 6 9 PRO CB C 29.33 0.02 1 15 7 10 ASP H H 7.044 0.02 1 16 7 10 ASP CA C 50.439 0.02 1 17 7 10 ASP CB C 40.406 0.02 1 18 7 10 ASP N N 112.599 0.02 1 19 8 11 MET H H 9.084 0.001 1 20 8 11 MET CA C 51.555 0.02 1 21 8 11 MET CB C 34.569 0.02 1 22 8 11 MET N N 119.617 0.003 1 23 9 12 LYS H H 8.686 0.02 1 24 9 12 LYS CA C 53.176 0.02 1 25 9 12 LYS CB C 32.609 0.02 1 26 9 12 LYS N N 121.882 0.005 1 27 10 13 ILE H H 7.826 0.02 1 28 10 13 ILE CA C 58.333 0.02 1 29 10 13 ILE CB C 41.951 0.02 1 30 10 13 ILE N N 119.259 0.002 1 31 11 14 LYS H H 8.886 0.02 1 32 11 14 LYS CA C 53.615 0.02 1 33 11 14 LYS CB C 33.748 0.02 1 34 11 14 LYS N N 128.94 0.003 1 35 12 15 LEU H H 8.569 0.02 1 36 12 15 LEU CA C 50.422 0.02 1 37 12 15 LEU CB C 45.612 0.02 1 38 12 15 LEU N N 117.603 0.02 1 39 13 16 ARG H H 7.575 0.02 1 40 13 16 ARG CA C 53.74 0.02 1 41 13 16 ARG CB C 30.228 0.02 1 42 13 16 ARG N N 120.698 0.02 1 43 14 17 MET H H 9.503 0.02 1 44 14 17 MET CA C 50.803 0.02 1 45 14 17 MET CB C 36.081 0.02 1 46 14 17 MET N N 126.327 0.02 1 47 16 19 GLY H H 7.693 0.02 1 48 16 19 GLY CA C 43.782 0.02 1 49 16 19 GLY N N 108.583 0.02 1 50 17 20 ALA H H 8.083 0.02 1 51 17 20 ALA CA C 49.523 0.02 1 52 17 20 ALA CB C 18.851 0.02 1 53 17 20 ALA N N 119.411 0.005 1 54 18 21 VAL H H 8.081 0.02 1 55 18 21 VAL CA C 58.149 0.02 1 56 18 21 VAL CB C 32.392 0.02 1 57 18 21 VAL N N 119.327 0.02 1 58 19 22 ASN H H 9.336 0.02 1 59 19 22 ASN CA C 50.876 0.02 1 60 19 22 ASN CB C 33.481 0.02 1 61 19 22 ASN N N 129.376 0.02 1 62 20 23 GLY H H 9.015 0.02 1 63 20 23 GLY CA C 42.256 0.02 1 64 20 23 GLY N N 102.652 0.02 1 65 21 24 HIS H H 8.281 0.02 1 66 21 24 HIS CA C 51.424 0.02 1 67 21 24 HIS CB C 28.603 0.02 1 68 21 24 HIS N N 123.807 0.02 1 69 22 25 PRO CA C 58.87 0.02 1 70 22 25 PRO CB C 29.773 0.02 1 71 23 26 PHE H H 8.404 0.02 1 72 23 26 PHE CA C 53.943 0.02 1 73 23 26 PHE CB C 39.053 0.02 1 74 23 26 PHE N N 114.648 0.001 1 75 24 27 ALA H H 8.649 0.02 1 76 24 27 ALA CA C 49.371 0.02 1 77 24 27 ALA CB C 19.508 0.02 1 78 24 27 ALA N N 120.247 0.02 1 79 25 28 ILE H H 9.298 0.02 1 80 25 28 ILE CA C 57.618 0.02 1 81 25 28 ILE CB C 42.051 0.02 1 82 25 28 ILE N N 123.63 0.02 1 83 26 29 GLU H H 8.756 0.02 1 84 26 29 GLU CA C 51.569 0.02 1 85 26 29 GLU CB C 30.918 0.02 1 86 26 29 GLU N N 124.621 0.02 1 87 27 30 GLY H H 8.296 0.02 1 88 27 30 GLY CA C 42.633 0.02 1 89 27 30 GLY N N 106.425 0.02 1 90 28 31 VAL H H 8.267 0.02 1 91 28 31 VAL CA C 57.195 0.02 1 92 28 31 VAL CB C 32.968 0.02 1 93 28 31 VAL N N 117.399 0.02 1 94 29 32 GLY H H 8.969 0.02 1 95 29 32 GLY CA C 42.988 0.02 1 96 29 32 GLY N N 111.09 0.02 1 97 30 33 LEU H H 8.863 0.001 1 98 30 33 LEU CA C 52.064 0.02 1 99 30 33 LEU CB C 42.627 0.02 1 100 30 33 LEU N N 122.731 0.009 1 101 31 34 GLY H H 9.233 0.02 1 102 31 34 GLY CA C 42.776 0.02 1 103 31 34 GLY N N 108.408 0.02 1 104 32 35 LYS H H 9.03 0.02 1 105 32 35 LYS CA C 49.887 0.02 1 106 32 35 LYS CB C 31.971 0.02 1 107 32 35 LYS N N 121.161 0.001 1 108 33 36 PRO CA C 63.175 0.02 1 109 33 36 PRO CB C 30.494 0.02 1 110 34 37 PHE H H 8.458 0.02 1 111 34 37 PHE CA C 56.371 0.02 1 112 34 37 PHE CB C 34.566 0.02 1 113 34 37 PHE N N 109.964 0.004 1 114 35 38 GLU H H 7.139 0.02 1 115 35 38 GLU CA C 53.111 0.02 1 116 35 38 GLU CB C 28.195 0.02 1 117 35 38 GLU N N 114.497 0.02 1 118 36 39 GLY H H 7.822 0.02 1 119 36 39 GLY CA C 43.169 0.02 1 120 36 39 GLY N N 105.722 0.02 1 121 37 40 LYS H H 7.09 0.02 1 122 37 40 LYS CA C 52.09 0.02 1 123 37 40 LYS CB C 34.588 0.02 1 124 37 40 LYS N N 114.897 0.02 1 125 38 41 GLN H H 8.233 0.02 1 126 38 41 GLN CA C 52.334 0.02 1 127 38 41 GLN CB C 28.295 0.02 1 128 38 41 GLN N N 115.735 0.002 1 129 39 42 SER H H 8.563 0.02 1 130 39 42 SER CA C 54.148 0.02 1 131 39 42 SER CB C 62.964 0.02 1 132 39 42 SER N N 114.368 0.02 1 133 40 43 MET H H 8.747 0.02 1 134 40 43 MET CA C 52.019 0.02 1 135 40 43 MET CB C 33.029 0.02 1 136 40 43 MET N N 115.601 0.02 1 137 41 44 ASP H H 8.853 0.02 1 138 41 44 ASP CA C 51.614 0.02 1 139 41 44 ASP CB C 40.949 0.02 1 140 41 44 ASP N N 120.76 0.02 1 141 42 45 LEU H H 9.451 0.02 1 142 42 45 LEU CA C 51.338 0.02 1 143 42 45 LEU CB C 41.629 0.02 1 144 42 45 LEU N N 125.402 0.02 1 145 43 46 LYS H H 9.326 0.02 1 146 43 46 LYS CA C 51.494 0.02 1 147 43 46 LYS CB C 33.529 0.02 1 148 43 46 LYS N N 124.634 0.02 1 149 44 47 VAL H H 8.607 0.02 1 150 44 47 VAL CA C 61.398 0.02 1 151 44 47 VAL CB C 29.231 0.02 1 152 44 47 VAL N N 126.243 0.02 1 153 45 48 LYS H H 9.031 0.02 1 154 45 48 LYS CA C 52.506 0.02 1 155 45 48 LYS CB C 30.821 0.02 1 156 45 48 LYS N N 129.544 0.02 1 157 46 49 GLU H H 8.057 0.02 1 158 46 49 GLU CA C 52.48 0.02 1 159 46 49 GLU CB C 30.64 0.02 1 160 46 49 GLU N N 117.354 0.002 1 161 47 50 GLY H H 8.861 0.02 1 162 47 50 GLY CA C 43.106 0.02 1 163 47 50 GLY N N 108.749 0.02 1 164 48 51 GLY H H 8.543 0.02 1 165 48 51 GLY CA C 40.649 0.02 1 166 48 51 GLY N N 106.847 0.02 1 167 51 54 PRO CA C 60.053 0.02 1 168 51 54 PRO CB C 27.634 0.02 1 169 52 55 PHE H H 5.672 0.02 1 170 52 55 PHE CA C 50.239 0.02 1 171 52 55 PHE CB C 39.536 0.02 1 172 52 55 PHE N N 110.929 0.02 1 173 53 56 ALA H H 7.943 0.02 1 174 53 56 ALA CA C 49.782 0.02 1 175 53 56 ALA CB C 17.929 0.02 1 176 53 56 ALA N N 120.591 0.02 1 177 54 57 TYR H H 7.756 0.02 1 178 54 57 TYR CA C 58.304 0.02 1 179 54 57 TYR CB C 36.404 0.02 1 180 54 57 TYR N N 128.429 0.02 1 181 55 58 ASP H H 7.696 0.001 1 182 55 58 ASP CA C 55.063 0.02 1 183 55 58 ASP CB C 39.133 0.02 1 184 55 58 ASP N N 111.167 0.003 1 185 56 59 ILE H H 7.253 0.001 1 186 56 59 ILE CA C 62.466 0.02 1 187 56 59 ILE CB C 34.53 0.02 1 188 56 59 ILE N N 110.064 0.003 1 189 57 60 LEU H H 8.593 0.02 1 190 57 60 LEU CA C 52.587 0.02 1 191 57 60 LEU CB C 40.905 0.02 1 192 57 60 LEU N N 120.85 0.02 1 193 58 61 THR H H 7.269 0.02 1 194 58 61 THR CA C 64.434 0.02 1 195 58 61 THR CB C 64.265 0.02 1 196 58 61 THR N N 107.737 0.02 1 197 59 62 THR H H 7.758 0.003 1 198 59 62 THR CA C 60.125 0.02 1 199 59 62 THR CB C 65.067 0.02 1 200 59 62 THR N N 109.692 0.02 1 201 60 63 VAL H H 7.355 0.02 1 202 60 63 VAL CA C 61.087 0.02 1 203 60 63 VAL CB C 26.851 0.02 1 204 60 63 VAL N N 123.63 0.02 1 205 61 64 PHE H H 6.142 0.02 1 206 61 64 PHE CA C 56.832 0.02 1 207 61 64 PHE CB C 36.527 0.02 1 208 61 64 PHE N N 114.668 0.02 1 209 62 65 GYC H H 7.436 0.02 1 210 62 65 GYC CA C 49.362 0.02 1 211 62 65 GYC CB C 24.75 0.02 1 212 62 65 GYC N N 115.672 0.02 1 213 65 66 ASN H H 9.184 0.001 1 214 65 66 ASN CA C 50.009 0.02 1 215 65 66 ASN CB C 35.562 0.02 1 216 65 66 ASN N N 115.135 0.02 1 217 66 67 ARG H H 7.041 0.02 1 218 66 67 ARG CA C 49.976 0.02 1 219 66 67 ARG CB C 23.549 0.02 1 220 66 67 ARG N N 132.741 0.02 1 221 67 68 VAL H H 6.575 0.02 1 222 67 68 VAL CA C 61.048 0.02 1 223 67 68 VAL CB C 29.336 0.02 1 224 67 68 VAL N N 116.066 0.02 1 225 68 69 PHE H H 6.801 0.02 1 226 68 69 PHE CA C 53.738 0.02 1 227 68 69 PHE CB C 33.911 0.02 1 228 68 69 PHE N N 115.94 0.02 1 229 69 70 ALA H H 7.824 0.02 1 230 69 70 ALA CA C 49.065 0.02 1 231 69 70 ALA CB C 17.238 0.02 1 232 69 70 ALA N N 125.171 0.02 1 233 70 71 LYS H H 8.134 0.02 1 234 70 71 LYS CA C 53.599 0.02 1 235 70 71 LYS CB C 30.123 0.02 1 236 70 71 LYS N N 123 0.02 1 237 71 72 TYR H H 9.245 0.02 1 238 71 72 TYR CA C 53.396 0.02 1 239 71 72 TYR CB C 38.078 0.02 1 240 71 72 TYR N N 134.111 0.02 1 241 72 73 PRO CA C 59.24 0.02 1 242 72 73 PRO CB C 29.833 0.02 1 243 73 74 GLU H H 8.786 0.02 1 244 73 74 GLU CA C 55.821 0.02 1 245 73 74 GLU CB C 26.678 0.02 1 246 73 74 GLU N N 117.427 0.02 1 247 74 75 ASN H H 7.966 0.001 1 248 74 75 ASN CA C 50.065 0.02 1 249 74 75 ASN CB C 34.44 0.02 1 250 74 75 ASN N N 111.865 0.02 1 251 75 76 ILE H H 7.268 0.02 1 252 75 76 ILE CA C 58.02 0.02 1 253 75 76 ILE CB C 38.541 0.02 1 254 75 76 ILE N N 120.625 0.002 1 255 76 77 VAL H H 8.04 0.02 1 256 76 77 VAL CA C 61.387 0.02 1 257 76 77 VAL CB C 29.038 0.02 1 258 76 77 VAL N N 127.843 0.001 1 259 77 78 ASP H H 8.146 0.02 1 260 77 78 ASP CA C 48.298 0.02 1 261 77 78 ASP CB C 37.312 0.02 1 262 77 78 ASP N N 127.501 0.02 1 263 78 79 TYR H H 8.732 0.02 1 264 78 79 TYR CA C 57.288 0.02 1 265 78 79 TYR CB C 38.473 0.02 1 266 78 79 TYR N N 126.347 0.02 1 267 79 80 PHE H H 6.649 0.02 1 268 79 80 PHE CA C 56.961 0.02 1 269 79 80 PHE CB C 35.012 0.02 1 270 79 80 PHE N N 110.885 0.02 1 271 80 81 LYS H H 8.168 0.02 1 272 80 81 LYS CA C 58.45 0.02 1 273 80 81 LYS CB C 28.214 0.02 1 274 80 81 LYS N N 119.951 0.005 1 275 81 82 GLN H H 6.822 0.02 1 276 81 82 GLN CA C 55.207 0.02 1 277 81 82 GLN CB C 28.784 0.02 1 278 81 82 GLN N N 112.967 0.02 1 279 82 83 SER H H 6.964 0.02 1 280 82 83 SER CA C 58.762 0.02 1 281 82 83 SER CB C 60.337 0.02 1 282 82 83 SER N N 111.865 0.002 1 283 83 84 PHE H H 6.825 0.02 1 284 83 84 PHE CA C 56.814 0.02 1 285 83 84 PHE CB C 36.023 0.02 1 286 83 84 PHE N N 120.137 0.02 1 287 84 85 PRO CA C 61.393 0.02 1 288 84 85 PRO CB C 32.86 0.02 1 289 85 86 GLU H H 10.484 0.02 1 290 85 86 GLU CA C 59.839 0.02 1 291 85 86 GLU CB C 25.255 0.02 1 292 85 86 GLU N N 126.347 0.02 1 293 86 87 GLY H H 8.191 0.02 1 294 86 87 GLY CA C 41.175 0.02 1 295 86 87 GLY N N 103.227 0.02 1 296 87 88 TYR H H 7.721 0.02 1 297 87 88 TYR CA C 52.56 0.02 1 298 87 88 TYR CB C 37.139 0.02 1 299 87 88 TYR N N 112.078 0.02 1 300 88 89 SER H H 8.757 0.02 1 301 88 89 SER CA C 53.114 0.02 1 302 88 89 SER CB C 64.706 0.02 1 303 88 89 SER N N 113.475 0.02 1 304 89 90 TRP H H 8.79 0.02 1 305 89 90 TRP CA C 51.984 0.02 1 306 89 90 TRP CB C 31.774 0.02 1 307 89 90 TRP N N 114.569 0.02 1 308 90 91 GLU H H 8.62 0.02 1 309 90 91 GLU CA C 52.061 0.02 1 310 90 91 GLU CB C 30.363 0.02 1 311 90 91 GLU N N 119.604 0.02 1 312 91 92 ARG H H 9.458 0.02 1 313 91 92 ARG CA C 51.369 0.02 1 314 91 92 ARG CB C 36.148 0.02 1 315 91 92 ARG N N 125.437 0.02 1 316 92 93 SER H H 8.67 0.02 1 317 92 93 SER CA C 53.848 0.02 1 318 92 93 SER CB C 62.659 0.02 1 319 92 93 SER N N 120.91 0.02 1 320 93 94 MET H H 8.706 0.02 1 321 93 94 MET CA C 52.418 0.02 1 322 93 94 MET CB C 32.606 0.02 1 323 93 94 MET N N 124.279 0.013 1 324 95 96 TYR H H 9.086 0.001 1 325 95 96 TYR CA C 56.808 0.02 1 326 95 96 TYR CB C 37.558 0.02 1 327 95 96 TYR N N 126.37 0.02 1 328 96 97 GLU H H 8.089 0.02 1 329 96 97 GLU CA C 56.263 0.02 1 330 96 97 GLU CB C 27.451 0.02 1 331 96 97 GLU N N 117.608 0.02 1 332 97 98 ASP H H 7.997 0.02 1 333 97 98 ASP CA C 49.475 0.02 1 334 97 98 ASP CB C 37.85 0.02 1 335 97 98 ASP N N 117.467 0.02 1 336 98 99 GLY H H 7.869 0.02 1 337 98 99 GLY CA C 42.201 0.02 1 338 98 99 GLY N N 107.019 0.02 1 339 99 100 GLY H H 6.909 0.02 1 340 99 100 GLY CA C 42.725 0.02 1 341 99 100 GLY N N 104.19 0.02 1 342 100 101 ILE H H 8.436 0.02 1 343 100 101 ILE CA C 57.401 0.02 1 344 100 101 ILE CB C 38.962 0.02 1 345 100 101 ILE N N 124.927 0.005 1 346 101 102 CYS H H 9.093 0.02 1 347 101 102 CYS CA C 52.047 0.02 1 348 101 102 CYS CB C 28.29 0.02 1 349 101 102 CYS N N 121.562 0.001 1 350 102 103 ASN H H 8.9 0.02 1 351 102 103 ASN CA C 49.445 0.02 1 352 102 103 ASN CB C 39.678 0.02 1 353 102 103 ASN N N 122.184 0.02 1 354 103 104 ALA H H 8.757 0.02 1 355 103 104 ALA CA C 47.43 0.02 1 356 103 104 ALA CB C 22.439 0.02 1 357 103 104 ALA N N 123.374 0.02 1 358 104 105 THR H H 8.54 0.02 1 359 104 105 THR CA C 56.67 0.02 1 360 104 105 THR CB C 68.948 0.02 1 361 104 105 THR N N 111.604 0.02 1 362 105 106 ASN H H 7.392 0.02 1 363 105 106 ASN CA C 48.16 0.02 1 364 105 106 ASN CB C 36.036 0.02 1 365 105 106 ASN N N 116.967 0.02 1 366 106 107 ASP H H 8.029 0.02 1 367 106 107 ASP CA C 51.523 0.02 1 368 106 107 ASP CB C 40.725 0.02 1 369 106 107 ASP N N 127.815 0.002 1 370 107 108 ILE H H 8.043 0.02 1 371 107 108 ILE CA C 59.329 0.02 1 372 107 108 ILE CB C 36.047 0.02 1 373 107 108 ILE N N 126.126 0.001 1 374 108 109 THR H H 9.153 0.02 1 375 108 109 THR CA C 57.086 0.02 1 376 108 109 THR CB C 69.602 0.02 1 377 108 109 THR N N 119.659 0.02 1 378 109 110 LEU H H 8.961 0.02 1 379 109 110 LEU CA C 51.564 0.02 1 380 109 110 LEU CB C 43.404 0.02 1 381 109 110 LEU N N 122.252 0.02 1 382 110 111 ASP H H 8.913 0.02 1 383 110 111 ASP CA C 49.914 0.02 1 384 110 111 ASP CB C 39.34 0.02 1 385 110 111 ASP N N 128.193 0.02 1 386 111 112 GLY H H 8.926 0.02 1 387 111 112 GLY CA C 44.894 0.02 1 388 111 112 GLY N N 116.28 0.02 1 389 112 113 ASP H H 8.263 0.02 1 390 112 113 ASP CA C 50.015 0.02 1 391 112 113 ASP CB C 37.329 0.02 1 392 112 113 ASP N N 126.942 0.02 1 393 113 114 CYS H H 7.714 0.02 1 394 113 114 CYS CA C 53.657 0.02 1 395 113 114 CYS CB C 26.594 0.02 1 396 113 114 CYS N N 120.056 0.02 1 397 114 115 TYR H H 9.123 0.02 1 398 114 115 TYR CA C 56.066 0.02 1 399 114 115 TYR CB C 38.374 0.02 1 400 114 115 TYR N N 128.292 0.003 1 401 115 116 ILE H H 9.116 0.02 1 402 115 116 ILE CA C 56.671 0.02 1 403 115 116 ILE CB C 35.53 0.02 1 404 115 116 ILE N N 123.674 0.005 1 405 116 117 TYR H H 8.674 0.02 1 406 116 117 TYR CA C 49.97 0.02 1 407 116 117 TYR CB C 35.155 0.02 1 408 116 117 TYR N N 123.969 0.02 1 409 117 118 GLU H H 8.473 0.02 1 410 117 118 GLU CA C 53.554 0.02 1 411 117 118 GLU CB C 28.573 0.02 1 412 117 118 GLU N N 126.347 0.02 1 413 119 120 ARG H H 8.301 0.02 1 414 119 120 ARG CA C 50.642 0.02 1 415 119 120 ARG CB C 29.036 0.02 1 416 119 120 ARG N N 129.618 0.02 1 417 120 121 PHE H H 8.322 0.02 1 418 120 121 PHE CA C 54.071 0.02 1 419 120 121 PHE CB C 42.328 0.02 1 420 120 121 PHE N N 126.763 0.02 1 421 121 122 ASP H H 8.327 0.02 1 422 121 122 ASP CA C 51.197 0.02 1 423 121 122 ASP CB C 42.315 0.02 1 424 121 122 ASP N N 126.379 0.02 1 425 122 123 GLY H H 9.433 0.02 1 426 122 123 GLY CA C 43.497 0.02 1 427 122 123 GLY N N 110.734 0.02 1 428 123 124 VAL H H 9.31 0.02 1 429 123 124 VAL CA C 57.151 0.02 1 430 123 124 VAL CB C 33.591 0.02 1 431 123 124 VAL N N 121.988 0.02 1 432 124 125 ASN H H 8.634 0.02 1 433 124 125 ASN CA C 50.919 0.02 1 434 124 125 ASN CB C 33.822 0.02 1 435 124 125 ASN N N 113.89 0.02 1 436 125 126 PHE H H 8.56 0.02 1 437 125 126 PHE CA C 55.92 0.02 1 438 125 126 PHE CB C 35.108 0.02 1 439 125 126 PHE N N 118.049 0.002 1 440 128 129 ASN H H 8.045 0.001 1 441 128 129 ASN CA C 48.853 0.02 1 442 128 129 ASN CB C 34.718 0.02 1 443 128 129 ASN N N 110.388 0.02 1 444 129 130 GLY H H 7.263 0.02 1 445 129 130 GLY CA C 42.269 0.02 1 446 129 130 GLY N N 105.533 0.02 1 447 130 131 PRO CA C 61.133 0.02 1 448 130 131 PRO CB C 29.373 0.02 1 449 131 132 VAL H H 6.599 0.02 1 450 131 132 VAL CA C 62.842 0.02 1 451 131 132 VAL CB C 28.268 0.02 1 452 131 132 VAL N N 116.574 0.02 1 453 132 133 MET H H 8.957 0.02 1 454 132 133 MET CA C 52.107 0.02 1 455 132 133 MET CB C 25.222 0.02 1 456 132 133 MET N N 119.265 0.02 1 457 133 134 GLN H H 7.48 0.02 1 458 133 134 GLN CA C 52.126 0.02 1 459 133 134 GLN CB C 25.2 0.02 1 460 133 134 GLN N N 111.777 0.02 1 461 134 135 LYS H H 7.188 0.001 1 462 134 135 LYS CA C 55.384 0.02 1 463 134 135 LYS CB C 25.553 0.02 1 464 134 135 LYS N N 115.978 0.02 1 465 135 136 ARG H H 8.38 0.02 1 466 135 136 ARG CA C 52.127 0.02 1 467 135 136 ARG CB C 28.248 0.02 1 468 135 136 ARG N N 115.382 0.002 1 469 136 137 THR H H 7.861 0.001 1 470 136 137 THR CA C 58.819 0.02 1 471 136 137 THR CB C 65.607 0.02 1 472 136 137 THR N N 111.083 0.02 1 473 137 138 VAL H H 8.718 0.02 1 474 137 138 VAL CA C 61.706 0.02 1 475 137 138 VAL CB C 30.249 0.02 1 476 137 138 VAL N N 120.621 0.02 1 477 138 139 LYS H H 6.924 0.02 1 478 138 139 LYS CA C 53.003 0.02 1 479 138 139 LYS CB C 30.281 0.02 1 480 138 139 LYS N N 112.18 0.02 1 481 139 140 TRP H H 8.646 0.001 1 482 139 140 TRP CA C 54.255 0.02 1 483 139 140 TRP CB C 27.407 0.02 1 484 139 140 TRP N N 121.822 0.02 1 485 140 141 GLU H H 9.047 0.02 1 486 140 141 GLU CA C 51.672 0.02 1 487 140 141 GLU CB C 25.503 0.02 1 488 140 141 GLU N N 123.225 0.001 1 489 141 142 PRO CA C 61.529 0.02 1 490 141 142 PRO CB C 28.833 0.02 1 491 142 143 SER H H 8.542 0.02 1 492 142 143 SER CA C 54.446 0.02 1 493 142 143 SER CB C 66.132 0.02 1 494 142 143 SER N N 120.262 0.02 1 495 143 144 THR H H 8.341 0.02 1 496 143 144 THR CA C 59.845 0.02 1 497 143 144 THR CB C 68.688 0.02 1 498 143 144 THR N N 115.94 0.02 1 499 144 145 GLU H H 9.751 0.02 1 500 144 145 GLU CA C 51.398 0.02 1 501 144 145 GLU CB C 29.756 0.02 1 502 144 145 GLU N N 130.808 0.02 1 503 145 146 LYS H H 9.038 0.001 1 504 145 146 LYS CA C 53.098 0.02 1 505 145 146 LYS CB C 30.927 0.02 1 506 145 146 LYS N N 128.898 0.003 1 507 146 147 LEU H H 8.608 0.001 1 508 146 147 LEU CA C 52.196 0.02 1 509 146 147 LEU CB C 39.739 0.02 1 510 146 147 LEU N N 126.935 0.02 1 511 147 148 TYR H H 8.323 0.02 1 512 147 148 TYR CA C 52.53 0.02 1 513 147 148 TYR CB C 36.554 0.02 1 514 147 148 TYR N N 115.689 0.02 1 515 148 149 VAL H H 8.809 0.001 1 516 148 149 VAL CA C 58.401 0.02 1 517 148 149 VAL CB C 30.013 0.02 1 518 148 149 VAL N N 120.82 0.02 1 519 149 150 ARG H H 8.622 0.02 1 520 149 150 ARG CA C 52.423 0.02 1 521 149 150 ARG CB C 30.718 0.02 1 522 149 150 ARG N N 127.434 0.003 1 523 151 152 GLY H H 8.22 0.02 1 524 151 152 GLY CA C 42.713 0.02 1 525 151 152 GLY N N 102.119 0.02 1 526 152 153 VAL H H 7.664 0.02 1 527 152 153 VAL CA C 57.183 0.02 1 528 152 153 VAL CB C 31.419 0.02 1 529 152 153 VAL N N 117.248 0.02 1 530 153 154 LEU H H 7.904 0.02 1 531 153 154 LEU CA C 51.253 0.02 1 532 153 154 LEU CB C 40.487 0.02 1 533 153 154 LEU N N 123.71 0.02 1 534 154 155 LYS H H 8.982 0.02 1 535 154 155 LYS CA C 50.232 0.02 1 536 154 155 LYS CB C 31.119 0.02 1 537 154 155 LYS N N 127.239 0.02 1 538 155 156 GLY H H 8.512 0.02 1 539 155 156 GLY CA C 42.782 0.02 1 540 155 156 GLY N N 102.669 0.02 1 541 156 157 ASP H H 9.491 0.02 1 542 156 157 ASP CA C 50 0.02 1 543 156 157 ASP CB C 41.13 0.02 1 544 156 157 ASP N N 130.51 0.02 1 545 157 158 VAL H H 8.459 0.02 1 546 157 158 VAL CA C 58.377 0.02 1 547 157 158 VAL CB C 32.422 0.02 1 548 157 158 VAL N N 119.463 0.02 1 549 158 159 ASN H H 8.963 0.02 1 550 158 159 ASN CA C 50.575 0.02 1 551 158 159 ASN CB C 35.528 0.02 1 552 158 159 ASN N N 128.091 0.02 1 553 159 160 MET H H 8.459 0.001 1 554 159 160 MET CA C 50.123 0.02 1 555 159 160 MET CB C 34.109 0.02 1 556 159 160 MET N N 123.251 0.02 1 557 160 161 ALA H H 9.457 0.02 1 558 160 161 ALA CA C 49.729 0.02 1 559 160 161 ALA CB C 18.806 0.02 1 560 160 161 ALA N N 123.537 0.02 1 561 161 162 LEU H H 9.28 0.02 1 562 161 162 LEU CA C 50.567 0.02 1 563 161 162 LEU CB C 40.308 0.02 1 564 161 162 LEU N N 126.219 0.02 1 565 162 163 SER H H 9.009 0.02 1 566 162 163 SER CA C 55.675 0.02 1 567 162 163 SER CB C 61.002 0.02 1 568 162 163 SER N N 119.555 0.02 1 569 163 164 LEU H H 7.639 0.02 1 570 163 164 LEU CA C 50.03 0.02 1 571 163 164 LEU CB C 41.587 0.02 1 572 163 164 LEU N N 122.567 0.02 1 573 164 165 GLU H H 8.377 0.02 1 574 164 165 GLU CA C 55.214 0.02 1 575 164 165 GLU CB C 26.466 0.02 1 576 164 165 GLU N N 123.928 0.02 1 577 166 167 GLY H H 7.749 0.02 1 578 166 167 GLY CA C 41.463 0.02 1 579 166 167 GLY N N 108.382 0.02 1 580 167 168 GLY H H 7.963 0.02 1 581 167 168 GLY CA C 41.242 0.02 1 582 167 168 GLY N N 107.24 0.02 1 583 168 169 HIS H H 8.404 0.02 1 584 168 169 HIS CA C 53.731 0.02 1 585 168 169 HIS CB C 32.6 0.02 1 586 168 169 HIS N N 115.243 0.002 1 587 169 170 TYR H H 9.133 0.02 1 588 169 170 TYR CA C 52.097 0.02 1 589 169 170 TYR CB C 39.184 0.02 1 590 169 170 TYR N N 126.147 0.02 1 591 170 171 ARG H H 9.725 0.02 1 592 170 171 ARG CA C 54.174 0.02 1 593 170 171 ARG CB C 29.148 0.02 1 594 170 171 ARG N N 127.929 0.02 1 595 171 172 CYS H H 8.16 0.02 1 596 171 172 CYS CA C 54.251 0.02 1 597 171 172 CYS CB C 29.66 0.02 1 598 171 172 CYS N N 118.022 0.02 1 599 172 173 ASP H H 8.233 0.02 1 600 172 173 ASP CA C 51.009 0.02 1 601 172 173 ASP CB C 40.023 0.02 1 602 172 173 ASP N N 127.752 0.02 1 603 173 174 PHE H H 9.032 0.02 1 604 173 174 PHE CA C 51.842 0.02 1 605 173 174 PHE CB C 37.591 0.02 1 606 173 174 PHE N N 126.469 0.005 1 607 174 175 LYS H H 8.373 0.02 1 608 174 175 LYS CA C 53.697 0.02 1 609 174 175 LYS CB C 31.636 0.02 1 610 174 175 LYS N N 122.148 0.007 1 611 175 176 THR H H 9.372 0.002 1 612 175 176 THR CA C 58.644 0.02 1 613 175 176 THR CB C 67.01 0.02 1 614 175 176 THR N N 122.482 0.02 1 615 176 177 THR H H 9.15 0.001 1 616 176 177 THR CA C 60.214 0.02 1 617 176 177 THR CB C 67.437 0.02 1 618 176 177 THR N N 123.816 0.02 1 619 177 178 TYR H H 9.568 0.02 1 620 177 178 TYR CA C 54.224 0.02 1 621 177 178 TYR CB C 38.294 0.02 1 622 177 178 TYR N N 128.247 0.02 1 623 178 179 LYS H H 9.456 0.02 1 624 178 179 LYS CA C 53.193 0.02 1 625 178 179 LYS CB C 32.349 0.02 1 626 178 179 LYS N N 120.562 0.02 1 627 179 180 ALA H H 8.748 0.02 1 628 179 180 ALA CA C 49.919 0.02 1 629 179 180 ALA CB C 16.79 0.02 1 630 179 180 ALA N N 129.618 0.02 1 631 180 181 LYS H H 8.206 0.02 1 632 180 181 LYS CA C 54.423 0.02 1 633 180 181 LYS CB C 29.045 0.02 1 634 180 181 LYS N N 119.9 0.002 1 635 181 182 LYS H H 7.521 0.02 1 636 181 182 LYS CA C 51.003 0.02 1 637 181 182 LYS CB C 31.815 0.02 1 638 181 182 LYS N N 115.702 0.02 1 639 182 183 VAL H H 8.108 0.001 1 640 182 183 VAL CA C 61.682 0.02 1 641 182 183 VAL CB C 28.182 0.02 1 642 182 183 VAL N N 120.152 0.002 1 643 183 184 VAL H H 7.521 0.02 1 644 183 184 VAL CA C 56.302 0.02 1 645 183 184 VAL CB C 31.69 0.02 1 646 183 184 VAL N N 123.622 0.02 1 647 184 185 GLN H H 8.264 0.001 1 648 184 185 GLN CA C 53.654 0.02 1 649 184 185 GLN CB C 25.776 0.02 1 650 184 185 GLN N N 123.253 0.008 1 651 185 186 LEU H H 8.175 0.02 1 652 185 186 LEU CA C 49.089 0.02 1 653 185 186 LEU CB C 38.438 0.02 1 654 185 186 LEU N N 123.483 0.02 1 655 186 187 PRO CA C 59.257 0.02 1 656 186 187 PRO CB C 29.611 0.02 1 657 187 188 ASP H H 7.939 0.02 1 658 187 188 ASP CA C 50.177 0.02 1 659 187 188 ASP CB C 39.427 0.02 1 660 187 188 ASP N N 117.805 0.001 1 661 188 189 TYR H H 8.529 0.02 1 662 188 189 TYR CA C 55.335 0.02 1 663 188 189 TYR CB C 35.505 0.02 1 664 188 189 TYR N N 121.673 0.02 1 665 189 190 HIS H H 8.602 0.02 1 666 189 190 HIS CA C 52.735 0.02 1 667 189 190 HIS CB C 25.705 0.02 1 668 189 190 HIS N N 120.45 0.003 1 669 190 191 PHE H H 8.343 0.02 1 670 190 191 PHE CA C 52.575 0.02 1 671 190 191 PHE CB C 39.785 0.02 1 672 190 191 PHE N N 115.14 0.02 1 673 191 192 VAL H H 9.088 0.02 1 674 191 192 VAL CA C 58.786 0.02 1 675 191 192 VAL CB C 32.351 0.02 1 676 191 192 VAL N N 118.578 0.02 1 677 192 193 ASP H H 9.008 0.02 1 678 192 193 ASP CA C 50.592 0.02 1 679 192 193 ASP CB C 38.198 0.02 1 680 192 193 ASP N N 130.541 0.02 1 681 193 194 HIS H H 8.817 0.02 1 682 193 194 HIS CA C 52.184 0.02 1 683 193 194 HIS CB C 30.491 0.02 1 684 193 194 HIS N N 117.351 0.02 1 685 194 195 HIS H H 8.339 0.02 1 686 194 195 HIS CA C 52.592 0.02 1 687 194 195 HIS CB C 29.987 0.02 1 688 194 195 HIS N N 118.953 0.02 1 689 195 196 ILE H H 9.798 0.02 1 690 195 196 ILE CA C 56.083 0.02 1 691 195 196 ILE CB C 41.259 0.02 1 692 195 196 ILE N N 128.247 0.02 1 693 196 197 GLU H H 9.324 0.02 1 694 196 197 GLU CA C 53.049 0.02 1 695 196 197 GLU CB C 32.233 0.02 1 696 196 197 GLU N N 127.414 0.006 1 697 197 198 ILE H H 9.567 0.02 1 698 197 198 ILE CA C 60.255 0.02 1 699 197 198 ILE CB C 34.648 0.02 1 700 197 198 ILE N N 126.741 0.006 1 701 198 199 LYS H H 8.71 0.02 1 702 198 199 LYS CA C 54.25 0.02 1 703 198 199 LYS CB C 29.764 0.02 1 704 198 199 LYS N N 131.357 0.02 1 705 199 200 SER H H 7.742 0.02 1 706 199 200 SER CA C 54.788 0.02 1 707 199 200 SER CB C 62.22 0.02 1 708 199 200 SER N N 110.041 0.02 1 709 200 201 HIS H H 8.021 0.02 1 710 200 201 HIS CA C 51.48 0.02 1 711 200 201 HIS CB C 28.584 0.02 1 712 200 201 HIS N N 115.608 0.02 1 713 201 202 ASP H H 8.191 0.02 1 714 201 202 ASP CA C 49.505 0.02 1 715 201 202 ASP CB C 37.915 0.02 1 716 201 202 ASP N N 119.572 0.002 1 717 203 204 ASP H H 7.844 0.02 1 718 203 204 ASP CA C 50.059 0.02 1 719 203 204 ASP CB C 37.61 0.02 1 720 203 204 ASP N N 113.624 0.02 1 721 204 205 TYR H H 7.981 0.02 1 722 204 205 TYR CA C 58.82 0.02 1 723 204 205 TYR CB C 29.877 0.02 1 724 204 205 TYR N N 115.798 0.02 1 725 205 206 SER H H 8.483 0.02 1 726 205 206 SER CA C 60.016 0.02 1 727 205 206 SER CB C 60.283 0.02 1 728 205 206 SER N N 116.546 0.02 1 729 206 207 ASN H H 8.812 0.02 1 730 206 207 ASN CA C 50.356 0.02 1 731 206 207 ASN CB C 38.797 0.02 1 732 206 207 ASN N N 119.963 0.02 1 733 207 208 VAL H H 8.247 0.02 1 734 207 208 VAL CA C 58.87 0.02 1 735 207 208 VAL CB C 35.014 0.02 1 736 207 208 VAL N N 122.756 0.02 1 737 208 209 ASN H H 8.601 0.02 1 738 208 209 ASN CA C 50.256 0.02 1 739 208 209 ASN CB C 39.617 0.02 1 740 208 209 ASN N N 126.243 0.02 1 741 209 210 LEU H H 9.156 0.02 1 742 209 210 LEU CA C 51.553 0.02 1 743 209 210 LEU CB C 46.018 0.02 1 744 209 210 LEU N N 130.583 0.02 1 745 210 211 HIS H H 9.055 0.02 1 746 210 211 HIS CA C 52.409 0.02 1 747 210 211 HIS CB C 33.009 0.02 1 748 210 211 HIS N N 124.387 0.02 1 749 212 213 HIS H H 8.701 0.02 1 750 212 213 HIS CA C 51.563 0.02 1 751 212 213 HIS CB C 30.337 0.02 1 752 212 213 HIS N N 123.869 0.02 1 753 213 214 ALA H H 9.201 0.001 1 754 213 214 ALA CA C 48.593 0.02 1 755 213 214 ALA CB C 19.819 0.02 1 756 213 214 ALA N N 128.544 0.003 1 757 214 215 GLU H H 7.874 0.02 1 758 214 215 GLU CA C 53.167 0.02 1 759 214 215 GLU CB C 30.606 0.02 1 760 214 215 GLU N N 118.914 0.02 1 761 215 216 ALA H H 8.728 0.02 1 762 215 216 ALA CA C 47.371 0.02 1 763 215 216 ALA CB C 17.062 0.02 1 764 215 216 ALA N N 127.29 0.02 1 765 216 217 HIS H H 9.063 0.02 1 766 216 217 HIS CA C 52.275 0.02 1 767 216 217 HIS CB C 29.084 0.02 1 768 216 217 HIS N N 113.903 0.02 1 769 217 218 SER H H 8.945 0.02 1 770 217 218 SER CA C 55.608 0.02 1 771 217 218 SER CB C 61.533 0.02 1 772 217 218 SER N N 115.443 0.007 1 773 218 219 GLU H H 9.061 0.02 1 774 218 219 GLU CA C 53.618 0.02 1 775 218 219 GLU CB C 28.138 0.02 1 776 218 219 GLU N N 122.482 0.02 1 777 219 220 LEU H H 8.33 0.02 1 778 219 220 LEU CA C 50.412 0.02 1 779 219 220 LEU CB C 38.688 0.02 1 780 219 220 LEU N N 125.345 0.02 1 781 221 222 ARG H H 7.873 0.02 1 782 221 222 ARG CA C 54.646 0.02 1 783 221 222 ARG CB C 31.001 0.02 1 784 221 222 ARG N N 126.5 0.002 1 stop_ save_