data_17817 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Green Proteorhodopsin - Deuterated ; _BMRB_accession_number 17817 _BMRB_flat_file_name bmr17817.str _Entry_type original _Submission_date 2011-07-29 _Accession_date 2011-07-29 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Solid-State NMR sequence specific assignment of deuterated proterhodopsin with protons reintroduced at exchangeable sites.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ward Meaghan . . 2 Shi Lichi . . 3 Lake Evelyn . . 4 Krishnamurthy Sridevi . . 5 Hutchins Howard . . 6 Brown Leonid S. . 7 Ladizhansky Vladimir . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 78 "13C chemical shifts" 198 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-02-15 udpate BMRB 'update entry citation' 2011-10-25 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 15955 'Green Proteorhodopsin' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Proton-detected solid-state NMR reveals intramembrane polar networks in a seven-helical transmembrane protein proteorhodopsin.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21919530 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ward Meaghan E. . 2 Shi Lichi . . 3 Lake Evelyn . . 4 Krishnamurthy Sridevi . . 5 Hutchins Howard . . 6 Brown Leonid S. . 7 Ladizhansky Vladimir . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 133 _Journal_issue 43 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 17434 _Page_last 17443 _Year 2011 _Details . loop_ _Keyword 'double quantum coherence' 'magic angle spinning' 'membrane proteins' 'protein-water interaction' Proteorhodopsin 'proton detection' 'solid state NMR' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name GPR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Green Proteorhodopsin' $GPR retinal $RET stop_ _System_molecular_weight 29500 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GPR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GPR _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function 'proton pump' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 255 _Mol_residue_sequence ; MKLLLILGSVIALPTFAAGG GDLDASDYTGVSFWLVTAAL LASTVFFFVERDRVSAKWKT SLTVSGLVTGIAFWHYMYMR GVWIETGDSPTVFRYIDWLL TVPLLICEFYLILAAATNVA GSLFKKLLVGSLVMLVFGYM GEAGIMAAWPAFIIGCLAWV YMIYELWAGEGKSACNTASP AVQSAYNTMMYIIIFGWAIY PVGYFTGYLMGDGGSALNLN LIYNLADFVNKILFGLIIWN VAVKESSNAHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LEU 4 LEU 5 LEU 6 ILE 7 LEU 8 GLY 9 SER 10 VAL 11 ILE 12 ALA 13 LEU 14 PRO 15 THR 16 PHE 17 ALA 18 ALA 19 GLY 20 GLY 21 GLY 22 ASP 23 LEU 24 ASP 25 ALA 26 SER 27 ASP 28 TYR 29 THR 30 GLY 31 VAL 32 SER 33 PHE 34 TRP 35 LEU 36 VAL 37 THR 38 ALA 39 ALA 40 LEU 41 LEU 42 ALA 43 SER 44 THR 45 VAL 46 PHE 47 PHE 48 PHE 49 VAL 50 GLU 51 ARG 52 ASP 53 ARG 54 VAL 55 SER 56 ALA 57 LYS 58 TRP 59 LYS 60 THR 61 SER 62 LEU 63 THR 64 VAL 65 SER 66 GLY 67 LEU 68 VAL 69 THR 70 GLY 71 ILE 72 ALA 73 PHE 74 TRP 75 HIS 76 TYR 77 MET 78 TYR 79 MET 80 ARG 81 GLY 82 VAL 83 TRP 84 ILE 85 GLU 86 THR 87 GLY 88 ASP 89 SER 90 PRO 91 THR 92 VAL 93 PHE 94 ARG 95 TYR 96 ILE 97 ASP 98 TRP 99 LEU 100 LEU 101 THR 102 VAL 103 PRO 104 LEU 105 LEU 106 ILE 107 CYS 108 GLU 109 PHE 110 TYR 111 LEU 112 ILE 113 LEU 114 ALA 115 ALA 116 ALA 117 THR 118 ASN 119 VAL 120 ALA 121 GLY 122 SER 123 LEU 124 PHE 125 LYS 126 LYS 127 LEU 128 LEU 129 VAL 130 GLY 131 SER 132 LEU 133 VAL 134 MET 135 LEU 136 VAL 137 PHE 138 GLY 139 TYR 140 MET 141 GLY 142 GLU 143 ALA 144 GLY 145 ILE 146 MET 147 ALA 148 ALA 149 TRP 150 PRO 151 ALA 152 PHE 153 ILE 154 ILE 155 GLY 156 CYS 157 LEU 158 ALA 159 TRP 160 VAL 161 TYR 162 MET 163 ILE 164 TYR 165 GLU 166 LEU 167 TRP 168 ALA 169 GLY 170 GLU 171 GLY 172 LYS 173 SER 174 ALA 175 CYS 176 ASN 177 THR 178 ALA 179 SER 180 PRO 181 ALA 182 VAL 183 GLN 184 SER 185 ALA 186 TYR 187 ASN 188 THR 189 MET 190 MET 191 TYR 192 ILE 193 ILE 194 ILE 195 PHE 196 GLY 197 TRP 198 ALA 199 ILE 200 TYR 201 PRO 202 VAL 203 GLY 204 TYR 205 PHE 206 THR 207 GLY 208 TYR 209 LEU 210 MET 211 GLY 212 ASP 213 GLY 214 GLY 215 SER 216 ALA 217 LEU 218 ASN 219 LEU 220 ASN 221 LEU 222 ILE 223 TYR 224 ASN 225 LEU 226 ALA 227 ASP 228 PHE 229 VAL 230 ASN 231 LYS 232 ILE 233 LEU 234 PHE 235 GLY 236 LEU 237 ILE 238 ILE 239 TRP 240 ASN 241 VAL 242 ALA 243 VAL 244 LYS 245 GLU 246 SER 247 SER 248 ASN 249 ALA 250 HIS 251 HIS 252 HIS 253 HIS 254 HIS 255 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15955 GPR 100.00 255 100.00 100.00 0.00e+00 BMRB 17327 proteorhodopsin 94.90 243 97.52 97.52 1.10e-165 PDB 2L6X "Solution Nmr Structure Of Proteorhodopsin" 94.90 243 97.93 97.93 7.07e-167 GB AAG10475 "proteorhodopsin [uncultured marine gamma proteobacterium EBAC31A08]" 97.65 249 100.00 100.00 2.47e-175 GB AAK30175 "proteorhodopsin, partial [uncultured bacterium]" 97.65 252 97.59 99.20 9.84e-172 GB AAK30176 "proteorhodopsin, partial [uncultured bacterium]" 97.25 251 97.58 98.39 5.55e-170 GB AAK30181 "proteorhodopsin, partial [uncultured bacterium]" 97.25 251 97.18 98.39 2.65e-169 GB AAK30183 "proteorhodopsin, partial [uncultured bacterium]" 97.25 251 97.58 98.39 5.55e-170 SP Q9F7P4 "RecName: Full=Green-light absorbing proteorhodopsin; Short=GPR; Flags: Precursor" 97.65 249 100.00 100.00 2.47e-175 stop_ save_ ############# # Ligands # ############# save_RET _Saveframe_category ligand _Mol_type non-polymer _Name_common "RET (RETINAL)" _BMRB_code . _PDB_code RET _Molecular_mass 284.436 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Aug 2 17:47:26 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? C5 C5 C . 0 . ? C6 C6 C . 0 . ? C7 C7 C . 0 . ? C8 C8 C . 0 . ? C9 C9 C . 0 . ? C10 C10 C . 0 . ? C11 C11 C . 0 . ? C12 C12 C . 0 . ? C13 C13 C . 0 . ? C14 C14 C . 0 . ? C15 C15 C . 0 . ? O1 O1 O . 0 . ? C16 C16 C . 0 . ? C17 C17 C . 0 . ? C18 C18 C . 0 . ? C19 C19 C . 0 . ? C20 C20 C . 0 . ? H21 H21 H . 0 . ? H22 H22 H . 0 . ? H31 H31 H . 0 . ? H32 H32 H . 0 . ? H41 H41 H . 0 . ? H42 H42 H . 0 . ? H7 H7 H . 0 . ? H8 H8 H . 0 . ? H10 H10 H . 0 . ? H11 H11 H . 0 . ? H12 H12 H . 0 . ? H14 H14 H . 0 . ? H15 H15 H . 0 . ? H161 H161 H . 0 . ? H162 H162 H . 0 . ? H163 H163 H . 0 . ? H171 H171 H . 0 . ? H172 H172 H . 0 . ? H173 H173 H . 0 . ? H181 H181 H . 0 . ? H182 H182 H . 0 . ? H183 H183 H . 0 . ? H191 H191 H . 0 . ? H192 H192 H . 0 . ? H193 H193 H . 0 . ? H201 H201 H . 0 . ? H202 H202 H . 0 . ? H203 H203 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 C1 C2 ? ? SING C1 C6 ? ? SING C1 C16 ? ? SING C1 C17 ? ? SING C2 C3 ? ? SING C2 H21 ? ? SING C2 H22 ? ? SING C3 C4 ? ? SING C3 H31 ? ? SING C3 H32 ? ? SING C4 C5 ? ? SING C4 H41 ? ? SING C4 H42 ? ? DOUB C5 C6 ? ? SING C5 C18 ? ? SING C6 C7 ? ? DOUB C7 C8 ? ? SING C7 H7 ? ? SING C8 C9 ? ? SING C8 H8 ? ? DOUB C9 C10 ? ? SING C9 C19 ? ? SING C10 C11 ? ? SING C10 H10 ? ? DOUB C11 C12 ? ? SING C11 H11 ? ? SING C12 C13 ? ? SING C12 H12 ? ? DOUB C13 C14 ? ? SING C13 C20 ? ? SING C14 C15 ? ? SING C14 H14 ? ? DOUB C15 O1 ? ? SING C15 H15 ? ? SING C16 H161 ? ? SING C16 H162 ? ? SING C16 H163 ? ? SING C17 H171 ? ? SING C17 H172 ? ? SING C17 H173 ? ? SING C18 H181 ? ? SING C18 H182 ? ? SING C18 H183 ? ? SING C19 H191 ? ? SING C19 H192 ? ? SING C19 H193 ? ? SING C20 H201 ? ? SING C20 H202 ? ? SING C20 H203 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GPR 'Gamma proteobacteria' 1236 Bacteria . Gamma proteobacteria 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 $GPR 'recombinant technology' . Escherichia "coli BL21" . NA stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details 'expressed on 4g/L 13C,2H-glucose, 1g/L 15N ammonium choride in 100% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GPR 7 mg '[U-13C; U-15N; U-2H]' 'sodium chloride' 50 mM 'natural abundance' CHES 50 mM 'natural abundance' DMPC 3.6 mg 'natural abundance' DMPA 0.4 mg 'natural abundance' $RET 0.09 mg 'natural abundance' D2O 60 % 'natural abundance' H2O 40 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Zhengrong and Bax' . . stop_ loop_ _Task 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_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 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_CC_SPC53_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CC SPC53' _Sample_label $sample_1 save_ save_3D_CANH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CANH' _Sample_label $sample_1 save_ save_3D_CONH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CONH' _Sample_label $sample_1 save_ save_3D_DQCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D DQCANH' _Sample_label $sample_1 save_ save_3D_DQCONH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D DQCONH' _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' 100 . mM pH 9 . pH pressure 1 . atm temperature 278 . 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 external indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 external indirect . . . 1 DSS N 15 'methyl protons' ppm 0.00 external 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 CC SPC53' '3D CANH' '3D CONH' '3D DQCANH' '3D DQCONH' 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 'Green Proteorhodopsin' _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 29 29 THR CA C 63.9 0.3 1 2 29 29 THR CB C 69.1 0.3 1 3 30 30 GLY H H 8.24 0.02 1 4 30 30 GLY CA C 45.1 0.3 1 5 30 30 GLY N N 108.8 0.3 1 6 37 37 THR C C 176.5 0.3 1 7 38 38 ALA H H 7.26 0.02 1 8 38 38 ALA C C 178.3 0.3 1 9 38 38 ALA CA C 54.5 0.3 1 10 38 38 ALA N N 120.6 0.3 1 11 39 39 ALA H H 8.07 0.02 1 12 39 39 ALA C C 178.8 0.3 1 13 39 39 ALA CA C 54.5 0.3 1 14 39 39 ALA N N 118.1 0.3 1 15 40 40 LEU H H 8.51 0.02 1 16 40 40 LEU CA C 57.4 0.3 1 17 40 40 LEU N N 119.7 0.3 1 18 81 81 GLY H H 6.81 0.02 1 19 81 81 GLY CA C 46 0.3 1 20 81 81 GLY N N 106.5 0.3 1 21 82 82 VAL H H 7.14 0.02 1 22 82 82 VAL CA C 65.5 0.3 1 23 82 82 VAL N N 123.8 0.3 1 24 86 86 THR H H 8.36 0.02 1 25 86 86 THR C C 176.5 0.3 1 26 86 86 THR CA C 61.7 0.3 1 27 86 86 THR N N 105.6 0.3 1 28 87 87 GLY H H 8.2 0.02 1 29 87 87 GLY C C 171.1 0.3 1 30 87 87 GLY CA C 44.4 0.3 1 31 87 87 GLY N N 112.8 0.3 1 32 88 88 ASP H H 7.69 0.02 1 33 88 88 ASP CA C 52 0.3 1 34 88 88 ASP CB C 43.1 0.3 1 35 88 88 ASP N N 116.6 0.3 1 36 89 89 SER CA C 56.3 0.3 1 37 89 89 SER CB C 64.4 0.3 1 38 90 90 PRO C C 180.1 0.3 1 39 91 91 THR H H 9.29 0.02 1 40 91 91 THR CA C 65.6 0.3 1 41 91 91 THR N N 119.2 0.3 1 42 109 109 PHE C C 177.8 0.3 1 43 109 109 PHE CA C 63.05 0.3 1 44 110 110 TYR H H 6.97 0.02 1 45 110 110 TYR C C 175.8 0.3 1 46 110 110 TYR CA C 61.4 0.3 1 47 110 110 TYR N N 113.6 0.3 1 48 111 111 LEU H H 8.69 0.02 1 49 111 111 LEU C C 181 0.3 1 50 111 111 LEU CA C 58 0.3 1 51 111 111 LEU N N 118.3 0.3 1 52 112 112 ILE H H 8.84 0.02 1 53 112 112 ILE C C 177.4 0.3 1 54 112 112 ILE CA C 64 0.3 1 55 112 112 ILE N N 113.4 0.3 1 56 113 113 LEU H H 6.93 0.02 1 57 113 113 LEU C C 179.4 0.3 1 58 113 113 LEU CA C 56.7 0.3 1 59 113 113 LEU N N 119.1 0.3 1 60 114 114 ALA H H 8.86 0.02 1 61 114 114 ALA C C 179.4 0.3 1 62 114 114 ALA CA C 53.4 0.3 1 63 114 114 ALA CB C 15.7 0.3 1 64 114 114 ALA N N 122.7 0.3 1 65 115 115 ALA H H 6.97 0.02 1 66 115 115 ALA C C 177.8 0.3 1 67 115 115 ALA CA C 52.9 0.3 1 68 115 115 ALA N N 118 0.3 1 69 116 116 ALA H H 7.28 0.02 1 70 116 116 ALA C C 181.7 0.3 1 71 116 116 ALA CA C 52.5 0.3 1 72 116 116 ALA CB C 22.9 0.3 1 73 116 116 ALA N N 117.8 0.3 1 74 125 125 LYS C C 177.7 0.3 1 75 125 125 LYS CA C 60.542 0.3 1 76 126 126 LYS H H 8.22 0.02 1 77 126 126 LYS C C 179 0.3 1 78 126 126 LYS CA C 60 0.3 1 79 126 126 LYS CB C 33.2 0.3 1 80 126 126 LYS N N 116.5 0.3 1 81 127 127 LEU H H 7.71 0.02 1 82 127 127 LEU C C 179.1 0.3 1 83 127 127 LEU CA C 56.6 0.3 1 84 127 127 LEU CB C 39.7 0.3 1 85 127 127 LEU N N 115.2 0.3 1 86 128 128 LEU H H 8.59 0.02 1 87 128 128 LEU C C 179 0.3 1 88 128 128 LEU CA C 57.7 0.3 1 89 128 128 LEU N N 119.8 0.3 1 90 129 129 VAL H H 8.26 0.02 1 91 129 129 VAL C C 177.8 0.3 1 92 129 129 VAL CA C 66.8 0.3 1 93 129 129 VAL CB C 30.2 0.3 1 94 129 129 VAL N N 116.2 0.3 1 95 139 139 TYR C C 176.9 0.3 1 96 140 140 MET H H 8.24 0.02 1 97 140 140 MET C C 179.7 0.3 1 98 140 140 MET CA C 60.2 0.3 1 99 140 140 MET N N 114.8 0.3 1 100 141 141 GLY H H 8.28 0.02 1 101 141 141 GLY C C 176.3 0.3 1 102 141 141 GLY CA C 45.8 0.3 1 103 141 141 GLY N N 107 0.3 1 104 142 142 GLU H H 8.57 0.02 1 105 142 142 GLU C C 178.3 0.3 1 106 142 142 GLU CA C 60.4 0.3 1 107 142 142 GLU CB C 28.1 0.3 1 108 142 142 GLU N N 122.6 0.3 1 109 143 143 ALA H H 8.71 0.02 1 110 143 143 ALA C C 178.5 0.3 1 111 143 143 ALA CA C 51.2 0.3 1 112 143 143 ALA CB C 17.9 0.3 1 113 143 143 ALA N N 117.2 0.3 1 114 144 144 GLY H H 7.42 0.02 1 115 144 144 GLY C C 174.8 0.3 1 116 144 144 GLY CA C 45.3 0.3 1 117 144 144 GLY N N 105.7 0.3 1 118 145 145 ILE H H 8.2 0.02 1 119 145 145 ILE C C 175 0.3 1 120 145 145 ILE CA C 62.5 0.3 1 121 145 145 ILE N N 120.9 0.3 1 122 146 146 MET H H 7.26 0.02 1 123 146 146 MET C C 174.4 0.3 1 124 146 146 MET CA C 52.6 0.3 1 125 146 146 MET N N 114.5 0.3 1 126 147 147 ALA H H 9.04 0.02 1 127 147 147 ALA C C 178.3 0.3 1 128 147 147 ALA CA C 52.8 0.3 1 129 147 147 ALA CB C 17.8 0.3 1 130 147 147 ALA N N 125.2 0.3 1 131 148 148 ALA H H 8.47 0.02 1 132 148 148 ALA C C 182.1 0.3 1 133 148 148 ALA CA C 55.2 0.3 1 134 148 148 ALA CB C 17.9 0.3 1 135 148 148 ALA N N 123.9 0.3 1 136 149 149 TRP H H 9.82 0.02 1 137 149 149 TRP C C 176.6 0.3 1 138 149 149 TRP CA C 62.3 0.3 1 139 149 149 TRP N N 118.4 0.3 1 140 150 150 PRO C C 177.5 0.3 1 141 150 150 PRO CA C 65.6 0.3 1 142 151 151 ALA H H 7.42 0.02 1 143 151 151 ALA C C 178.3 0.3 1 144 151 151 ALA CA C 55.9 0.3 1 145 151 151 ALA CB C 17.6 0.3 1 146 151 151 ALA N N 117.5 0.3 1 147 152 152 PHE H H 7.73 0.02 1 148 152 152 PHE C C 177.8 0.3 1 149 152 152 PHE CA C 60.1 0.3 1 150 152 152 PHE N N 116.3 0.3 1 151 156 156 CYS CA C 64.3 0.3 1 152 156 156 CYS CB C 26.6 0.3 1 153 166 166 LEU CA C 54.9 0.3 1 154 166 166 LEU CB C 40.2 0.3 1 155 168 168 ALA H H 8.69 0.02 1 156 168 168 ALA C C 177.5 0.3 1 157 168 168 ALA CA C 51.2 0.3 1 158 168 168 ALA CB C 21.8 0.3 1 159 168 168 ALA N N 117 0.3 1 160 169 169 GLY H H 7.4 0.02 1 161 169 169 GLY C C 174.7 0.3 1 162 169 169 GLY CA C 44.3 0.3 1 163 169 169 GLY N N 109 0.3 1 164 170 170 GLU H H 9.39 0.02 1 165 170 170 GLU C C 179.9 0.3 1 166 170 170 GLU CA C 58.8 0.3 1 167 170 170 GLU N N 125.7 0.3 1 168 171 171 GLY H H 8.39 0.02 1 169 171 171 GLY C C 174.5 0.3 1 170 171 171 GLY CA C 47.3 0.3 1 171 171 171 GLY N N 105.3 0.3 1 172 172 172 LYS H H 6.36 0.02 1 173 172 172 LYS C C 178.3 0.3 1 174 172 172 LYS CA C 56.8 0.3 1 175 172 172 LYS N N 122.4 0.3 1 176 173 173 SER H H 8.08 0.02 1 177 173 173 SER C C 176.3 0.3 1 178 173 173 SER CA C 61.1 0.3 1 179 173 173 SER CB C 61.9 0.3 1 180 173 173 SER N N 112.1 0.3 1 181 174 174 ALA H H 7.34 0.02 1 182 174 174 ALA C C 180.2 0.3 1 183 174 174 ALA CA C 53.9 0.3 1 184 174 174 ALA CB C 18 0.3 1 185 174 174 ALA N N 121 0.3 1 186 175 175 CYS H H 8.88 0.02 1 187 175 175 CYS C C 176.3 0.3 1 188 175 175 CYS CA C 61.3 0.3 1 189 175 175 CYS CB C 25 0.3 1 190 175 175 CYS N N 122.3 0.3 1 191 176 176 ASN H H 8.04 0.02 1 192 176 176 ASN C C 176.5 0.3 1 193 176 176 ASN CA C 54.5 0.3 1 194 176 176 ASN CB C 37.3 0.3 1 195 176 176 ASN N N 113.9 0.3 1 196 176 176 ASN HD21 H 7.60 0.02 1 197 176 176 ASN HD22 H 6.94 0.02 1 198 176 176 ASN ND2 N 110.1 0.3 1 199 176 176 ASN CG C 175.7 0.3 1 200 177 177 THR H H 7.69 0.02 1 201 177 177 THR C C 174.3 0.3 1 202 177 177 THR CA C 61 0.3 1 203 177 177 THR CB C 69.8 0.3 1 204 177 177 THR CG2 C 20.4 0.3 1 205 177 177 THR N N 107.4 0.3 1 206 178 178 ALA H H 7.79 0.02 1 207 178 178 ALA C C 176.6 0.3 1 208 178 178 ALA CA C 50.1 0.3 1 209 178 178 ALA CB C 19.7 0.3 1 210 178 178 ALA N N 125 0.3 1 211 179 179 SER H H 8.45 0.02 1 212 179 179 SER C C 173.2 0.3 1 213 179 179 SER CA C 56.3 0.3 1 214 179 179 SER CB C 61.8 0.3 1 215 179 179 SER N N 116.8 0.3 1 216 180 180 PRO CA C 65.5 0.3 1 217 180 180 PRO C C 179.6 0.3 1 218 181 181 ALA H H 8.51 0.02 1 219 181 181 ALA C C 181.2 0.3 1 220 181 181 ALA CA C 54.6 0.3 1 221 181 181 ALA CB C 17.3 0.3 1 222 181 181 ALA N N 118.8 0.3 1 223 182 182 VAL H H 7.67 0.02 1 224 182 182 VAL C C 177.3 0.3 1 225 182 182 VAL CA C 66.1 0.3 1 226 182 182 VAL CB C 29.7 0.3 1 227 182 182 VAL N N 121 0.3 1 228 183 183 GLN H H 8.73 0.02 1 229 183 183 GLN C C 178.7 0.3 1 230 183 183 GLN CA C 59.4 0.3 1 231 183 183 GLN CB C 26.6 0.3 1 232 183 183 GLN N N 118.6 0.3 1 233 183 183 GLN NE2 N 111.8 0.3 1 234 183 183 GLN HE21 H 7.43 0.02 1 235 183 183 GLN HE22 H 6.74 0.02 1 236 183 183 GLN CG C 33.2 0.3 1 237 183 183 GLN CD C 180.5 0.3 1 238 184 184 SER H H 8.2 0.02 1 239 184 184 SER C C 177.4 0.3 1 240 184 184 SER CA C 60.9 0.3 1 241 184 184 SER CB C 62.1 0.3 1 242 184 184 SER N N 112 0.3 1 243 185 185 ALA H H 7.73 0.02 1 244 185 185 ALA C C 177.8 0.3 1 245 185 185 ALA CA C 54.9 0.3 1 246 185 185 ALA N N 124.1 0.3 1 247 186 186 TYR H H 8.96 0.02 1 248 186 186 TYR C C 178 0.3 1 249 186 186 TYR CA C 60.7 0.3 1 250 186 186 TYR CB C 39.1 0.3 1 251 186 186 TYR N N 118.3 0.3 1 252 187 187 ASN H H 8.55 0.02 1 253 187 187 ASN C C 173.3 0.3 1 254 187 187 ASN CA C 56.3 0.3 1 255 187 187 ASN N N 116.9 0.3 1 256 189 189 MET CA C 59.4 0.3 1 257 189 189 MET CB C 34.7 0.3 1 258 203 203 GLY H H 8.96 0.02 1 259 203 203 GLY CA C 47.5 0.3 1 260 203 203 GLY N N 111.7 0.3 1 261 206 206 THR H H 8.06 0.02 1 262 206 206 THR C C 176 0.3 1 263 206 206 THR CA C 61.4 0.3 1 264 206 206 THR CB C 71.8 0.3 1 265 206 206 THR N N 105.2 0.3 1 266 207 207 GLY H H 8 0.02 1 267 207 207 GLY C C 177.2 0.3 1 268 207 207 GLY CA C 45 0.3 1 269 207 207 GLY N N 111.7 0.3 1 270 208 208 TYR H H 7.65 0.02 1 271 208 208 TYR CA C 51.3 0.3 1 272 208 208 TYR N N 117.5 0.3 1 273 219 219 LEU C C 178.1 0.3 1 274 219 219 LEU CA C 59.3 0.3 1 275 220 220 ASN H H 8.08 0.02 1 276 220 220 ASN C C 175.1 0.3 1 277 220 220 ASN CA C 57.7 0.3 1 278 220 220 ASN CB C 38.1 0.3 1 279 220 220 ASN N N 114 0.3 1 280 222 222 ILE H H 7.65 0.02 1 281 222 222 ILE C C 177.4 0.3 1 282 222 222 ILE CA C 65.1 0.3 1 283 222 222 ILE CB C 37.4 0.3 1 284 222 222 ILE N N 115 0.3 1 285 223 223 TYR H H 9.23 0.02 1 286 223 223 TYR C C 179.2 0.3 1 287 223 223 TYR CA C 57 0.3 1 288 223 223 TYR N N 117.9 0.3 1 289 224 224 ASN H H 8.22 0.02 1 290 224 224 ASN C C 177.3 0.3 1 291 224 224 ASN CA C 54.5 0.3 1 292 224 224 ASN N N 119.8 0.3 1 293 225 225 LEU H H 7.87 0.02 1 294 225 225 LEU C C 180.1 0.3 1 295 225 225 LEU CA C 56.6 0.3 1 296 225 225 LEU CB C 40.1 0.3 1 297 225 225 LEU N N 115.5 0.3 1 298 226 226 ALA H H 8.92 0.02 1 299 226 226 ALA C C 183.5 0.3 1 300 226 226 ALA CA C 54.4 0.3 1 301 226 226 ALA N N 119.1 0.3 1 302 227 227 ASP H H 7.65 0.02 1 303 227 227 ASP CA C 57.8 0.3 1 304 227 227 ASP N N 118.8 0.3 1 305 230 230 ASN H H 8 0.02 1 306 230 230 ASN CA C 54.5 0.3 1 307 230 230 ASN N N 113.9 0.3 1 308 231 231 LYS H H 7.91 0.02 1 309 231 231 LYS CA C 58.6 0.3 1 310 231 231 LYS N N 112.5 0.3 1 311 233 233 LEU C C 177.9 0.3 1 312 233 233 LEU CA C 58.52 0.3 1 313 234 234 PHE H H 7.16 0.02 1 314 234 234 PHE C C 175.6 0.3 1 315 234 234 PHE CA C 62.2 0.3 1 316 234 234 PHE CB C 40.1 0.3 1 317 234 234 PHE N N 114.9 0.3 1 318 235 235 GLY H H 7.3 0.02 1 319 235 235 GLY C C 176.7 0.3 1 320 235 235 GLY CA C 47 0.3 1 321 235 235 GLY N N 100.8 0.3 1 322 236 236 LEU H H 8.69 0.02 1 323 236 236 LEU C C 179.3 0.3 1 324 236 236 LEU CA C 57.9 0.3 1 325 236 236 LEU N N 123.2 0.3 1 326 238 238 ILE H H 7.05 0.02 1 327 238 238 ILE CA C 64.5 0.3 1 328 238 238 ILE N N 122 0.3 1 329 239 239 TRP C C 175.8 0.3 1 330 239 239 TRP CA C 62.1 0.3 1 331 240 240 ASN H H 8.61 0.02 1 332 240 240 ASN C C 176.5 0.3 1 333 240 240 ASN CA C 56.3 0.3 1 334 240 240 ASN CB C 39.2 0.03 1 335 240 240 ASN N N 114 0.3 1 336 241 241 VAL H H 7.69 0.02 1 337 241 241 VAL C C 174.7 0.3 1 338 241 241 VAL CA C 63.6 0.3 1 339 241 241 VAL CB C 29.6 0.3 1 340 241 241 VAL N N 117.3 0.3 1 341 242 242 ALA H H 8.2 0.02 1 342 242 242 ALA C C 180.7 0.3 1 343 242 242 ALA CA C 53.7 0.3 1 344 242 242 ALA CB C 18.8 0.3 1 345 242 242 ALA N N 125.8 0.3 1 346 248 248 ASN H H 7.24 0.02 1 347 248 248 ASN CA C 52.4 0.3 1 348 248 248 ASN CB C 36.9 0.3 1 349 248 248 ASN N N 114.2 0.3 1 350 249 249 ALA H H 8.96 0.02 1 351 249 249 ALA CA C 52.7 0.3 1 352 249 249 ALA N N 125.4 0.3 1 stop_ save_