data_27130 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N chemical shift assignments of the FnIII-2 domain from Vibrio cholerae RbmA ; _BMRB_accession_number 27130 _BMRB_flat_file_name bmr27130.str _Entry_type original _Submission_date 2017-06-09 _Accession_date 2017-06-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Parsley Nicole . . 2 Lee Hsiau-Wei . . 3 Partch Carrie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 134 "13C chemical shifts" 219 "15N chemical shifts" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-09-14 original BMRB . stop_ _Original_release_date 2017-06-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fong Jiunn C.N. . 2 Rogers Andrew . . 3 Michael Alicia K. . 4 Parsley Nicole C. . 5 Cornell William-Cole . . 6 Lin Yu-Cheng . . 7 Singh Praveen K. . 8 Hartmann Raimo . . 9 Drescher Knut . . 10 Vinogradov Evgeny . . 11 Dietrich Lars . . 12 Partch Carrie L. . 13 Yildiz Fitnat H. . stop_ _Journal_abbreviation Elife _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e26163 _Page_last e26163 _Year 2017 _Details . loop_ _Keyword biofilm 'fibronectin type III' 'secreted protein' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'RbmA FnIII-2 domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RbmA FnIII-2 domain' $RbmA_FnIII-2_domain stop_ _System_molecular_weight 12683.23 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'polysaccharide binding, biofilm formation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RbmA_FnIII-2_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common RbmA_FnIII-2_domain _Molecular_mass 12683.23 _Mol_thiol_state 'not present' loop_ _Biological_function 'polysaccharide binding, biofilm formation' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 117 _Mol_residue_sequence ; GAMDPELNGLTIDIKNQFGI NSVESTGGFVPFTVDLNNGR EGEANVEFWMTAVGPDGLII PVNAREKWVIASGDTYSKVR GINFDKSYPAGEYTINAQVV DIVSGERVEQSMTVVKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 155 GLY 2 156 ALA 3 157 MET 4 158 ASP 5 159 PRO 6 160 GLU 7 161 LEU 8 162 ASN 9 163 GLY 10 164 LEU 11 165 THR 12 166 ILE 13 167 ASP 14 168 ILE 15 169 LYS 16 170 ASN 17 171 GLN 18 172 PHE 19 173 GLY 20 174 ILE 21 175 ASN 22 176 SER 23 177 VAL 24 178 GLU 25 179 SER 26 180 THR 27 181 GLY 28 182 GLY 29 183 PHE 30 184 VAL 31 185 PRO 32 186 PHE 33 187 THR 34 188 VAL 35 189 ASP 36 190 LEU 37 191 ASN 38 192 ASN 39 193 GLY 40 194 ARG 41 195 GLU 42 196 GLY 43 197 GLU 44 198 ALA 45 199 ASN 46 200 VAL 47 201 GLU 48 202 PHE 49 203 TRP 50 204 MET 51 205 THR 52 206 ALA 53 207 VAL 54 208 GLY 55 209 PRO 56 210 ASP 57 211 GLY 58 212 LEU 59 213 ILE 60 214 ILE 61 215 PRO 62 216 VAL 63 217 ASN 64 218 ALA 65 219 ARG 66 220 GLU 67 221 LYS 68 222 TRP 69 223 VAL 70 224 ILE 71 225 ALA 72 226 SER 73 227 GLY 74 228 ASP 75 229 THR 76 230 TYR 77 231 SER 78 232 LYS 79 233 VAL 80 234 ARG 81 235 GLY 82 236 ILE 83 237 ASN 84 238 PHE 85 239 ASP 86 240 LYS 87 241 SER 88 242 TYR 89 243 PRO 90 244 ALA 91 245 GLY 92 246 GLU 93 247 TYR 94 248 THR 95 249 ILE 96 250 ASN 97 251 ALA 98 252 GLN 99 253 VAL 100 254 VAL 101 255 ASP 102 256 ILE 103 257 VAL 104 258 SER 105 259 GLY 106 260 GLU 107 261 ARG 108 262 VAL 109 263 GLU 110 264 GLN 111 265 SER 112 266 MET 113 267 THR 114 268 VAL 115 269 VAL 116 270 LYS 117 271 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 GB APF52364.1 'RbmA protein' . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $RbmA_FnIII-2_domain 'Vibrio cholerae' 666 Bacteria . Vibrio cholerae RbmA 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 _Details $RbmA_FnIII-2_domain 'recombinant technology' . Escherichia coli BL21(DE3) pHisGST-TEV 'residues 160-271 constituting the isolated FnIII-2 domain along with 5 vector residues left after TEV cleavage' 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 $RbmA_FnIII-2_domain 300 mM '[U-100% 13C; U-100% 15N]' HEPES 10 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version v9.2.0-b4 loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C(CO)NH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '10 mM HEPES pH 7.0, 100 mM NaCl, 10% D2O' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7.0 . pH pressure 1 . atm temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_DSS _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 HNCO' '3D HNCACB' '3D CBCA(CO)NH' '3D C(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $DSS _Mol_system_component_name 'RbmA FnIII-2 domain' _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 1 156 2 ALA CA C 53.4950 0.0000 1 2 156 2 ALA CB C 19.3990 0.0000 1 3 157 3 MET H H 8.4480 0.0000 1 4 157 3 MET HG3 H 0.0000 0.0000 2 5 157 3 MET CA C 55.1700 0.0000 1 6 157 3 MET CB C 32.6640 0.0000 1 7 157 3 MET N N 117.6220 0.0000 1 8 158 4 ASP H H 8.0010 0.0000 1 9 158 4 ASP CA C 53.0910 0.0000 1 10 158 4 ASP CB C 40.7280 0.0000 1 11 158 4 ASP N N 122.6470 0.0000 1 12 159 5 PRO CA C 63.5170 0.0000 1 13 159 5 PRO CB C 32.0890 0.0000 1 14 160 6 GLU H H 8.2070 0.0000 1 15 160 6 GLU CA C 55.3470 0.0000 1 16 160 6 GLU CB C 32.3570 0.0000 1 17 160 6 GLU N N 119.6250 0.0000 1 18 161 7 LEU H H 8.7030 0.0000 1 19 161 7 LEU CA C 53.2470 0.0000 1 20 161 7 LEU CB C 42.7120 0.0000 1 21 161 7 LEU N N 123.3160 0.0000 1 22 162 8 ASN H H 9.1200 0.0000 1 23 162 8 ASN HD21 H 7.5955 0.0000 2 24 162 8 ASN HD22 H 6.8447 0.0000 2 25 162 8 ASN CA C 54.2330 0.0000 1 26 162 8 ASN CB C 38.9040 0.0000 1 27 162 8 ASN N N 124.5810 0.0000 1 28 162 8 ASN ND2 N 112.1597 0.0000 1 29 163 9 GLY H H 8.8680 0.0000 1 30 163 9 GLY CA C 45.7560 0.0000 1 31 163 9 GLY N N 109.1390 0.0000 1 32 164 10 LEU H H 7.6700 0.0000 1 33 164 10 LEU CA C 53.4320 0.0000 1 34 164 10 LEU CB C 43.4090 0.0000 1 35 164 10 LEU N N 123.7230 0.0000 1 36 165 11 THR H H 8.8830 0.0000 1 37 165 11 THR CA C 62.0270 0.0000 1 38 165 11 THR CB C 70.0680 0.0000 1 39 165 11 THR N N 120.4200 0.0000 1 40 166 12 ILE H H 8.2920 0.0000 1 41 166 12 ILE CA C 60.5270 0.0000 1 42 166 12 ILE CB C 41.7150 0.0000 1 43 166 12 ILE N N 123.7690 0.0000 1 44 167 13 ASP H H 8.6740 0.0000 1 45 167 13 ASP CA C 53.2190 0.0000 1 46 167 13 ASP CB C 43.7650 0.0000 1 47 167 13 ASP N N 126.6520 0.0000 1 48 168 14 ILE H H 8.7500 0.0000 1 49 168 14 ILE CA C 60.1910 0.0000 1 50 168 14 ILE CB C 39.9090 0.0000 1 51 168 14 ILE N N 127.7680 0.0000 1 52 169 15 LYS H H 8.7950 0.0000 1 53 169 15 LYS CA C 54.8100 0.0000 1 54 169 15 LYS CB C 36.3860 0.0000 1 55 169 15 LYS N N 124.0830 0.0000 1 56 170 16 ASN H H 8.7500 0.0000 1 57 170 16 ASN HD21 H 7.7860 0.0000 2 58 170 16 ASN HD22 H 7.1834 0.0000 2 59 170 16 ASN CA C 53.4460 0.0000 1 60 170 16 ASN CB C 38.1110 0.0000 1 61 170 16 ASN N N 121.1470 0.0000 1 62 170 16 ASN ND2 N 114.8366 0.0000 1 63 171 17 GLN H H 7.8550 0.0000 1 64 171 17 GLN HE21 H 6.8100 0.0000 2 65 171 17 GLN HE22 H 6.0400 0.0000 2 66 171 17 GLN CA C 59.9720 0.0000 1 67 171 17 GLN CB C 29.3440 0.0000 1 68 171 17 GLN N N 129.3670 0.0000 1 69 171 17 GLN NE2 N 106.3800 0.0000 1 70 172 18 PHE H H 9.1800 0.0000 1 71 172 18 PHE CA C 56.3780 0.0000 1 72 172 18 PHE CB C 38.9960 0.0000 1 73 172 18 PHE N N 115.1890 0.0000 1 74 173 19 GLY H H 7.7260 0.0000 1 75 173 19 GLY CA C 47.1070 0.0000 1 76 173 19 GLY N N 110.8780 0.0000 1 77 174 20 ILE H H 7.5120 0.0000 1 78 174 20 ILE CA C 61.2590 0.0000 1 79 174 20 ILE CB C 38.5600 0.0000 1 80 174 20 ILE N N 119.0760 0.0000 1 81 175 21 ASN HD21 H 7.4511 0.0000 2 82 175 21 ASN HD22 H 6.7789 0.0000 2 83 175 21 ASN CA C 53.3290 0.0000 1 84 175 21 ASN CB C 39.7360 0.0000 1 85 175 21 ASN ND2 N 112.1197 0.0000 1 86 176 22 SER H H 7.7110 0.0000 1 87 176 22 SER CA C 56.3620 0.0000 1 88 176 22 SER CB C 65.6140 0.0000 1 89 176 22 SER N N 114.5120 0.0000 1 90 177 23 VAL H H 8.6850 0.0000 1 91 177 23 VAL CA C 59.5440 0.0000 1 92 177 23 VAL CB C 34.5980 0.0000 1 93 177 23 VAL N N 118.8290 0.0000 1 94 178 24 GLU H H 8.2820 0.0000 1 95 178 24 GLU CA C 56.0520 0.0000 1 96 178 24 GLU CB C 30.8280 0.0000 1 97 178 24 GLU N N 121.0350 0.0000 1 98 179 25 SER H H 9.1750 0.0000 1 99 179 25 SER CA C 61.6010 0.0000 1 100 179 25 SER CB C 63.0650 0.0000 1 101 179 25 SER N N 116.8280 0.0000 1 102 180 26 THR H H 7.1100 0.0000 1 103 180 26 THR CA C 62.0380 0.0000 1 104 180 26 THR CB C 68.5050 0.0000 1 105 180 26 THR N N 106.1590 0.0000 1 106 181 27 GLY H H 8.0080 0.0000 1 107 181 27 GLY CA C 43.8370 0.0000 1 108 181 27 GLY N N 109.1070 0.0000 1 109 182 28 GLY H H 8.3880 0.0000 1 110 182 28 GLY CA C 45.3910 0.0000 1 111 182 28 GLY N N 107.6530 0.0000 1 112 183 29 PHE H H 8.5060 0.0000 1 113 183 29 PHE CA C 56.8610 0.0000 1 114 183 29 PHE CB C 41.5880 0.0000 1 115 183 29 PHE N N 122.0070 0.0000 1 116 184 30 VAL H H 8.2420 0.0000 1 117 184 30 VAL CA C 59.3230 0.0000 1 118 184 30 VAL CB C 34.0647 0.0000 1 119 184 30 VAL N N 128.0990 0.0000 1 120 185 31 PRO CA C 61.4220 0.0000 1 121 186 32 PHE H H 8.5740 0.0000 1 122 186 32 PHE CA C 56.5610 0.0000 1 123 186 32 PHE CB C 40.7100 0.0000 1 124 186 32 PHE N N 119.8400 0.0000 1 125 187 33 THR H H 9.0120 0.0000 1 126 187 33 THR CA C 60.5510 0.0000 1 127 187 33 THR CB C 69.7250 0.0000 1 128 187 33 THR N N 112.9690 0.0000 1 129 188 34 VAL H H 8.6820 0.0000 1 130 188 34 VAL CA C 61.2830 0.0000 1 131 188 34 VAL CB C 33.5050 0.0000 1 132 188 34 VAL N N 123.6470 0.0000 1 133 189 35 ASP H H 8.6770 0.0000 1 134 189 35 ASP CA C 53.4070 0.0000 1 135 189 35 ASP CB C 43.7270 0.0000 1 136 189 35 ASP N N 125.8680 0.0000 1 137 190 36 LEU H H 9.1690 0.0000 1 138 190 36 LEU CA C 53.6780 0.0000 1 139 190 36 LEU CB C 45.1460 0.0000 1 140 190 36 LEU N N 124.5680 0.0000 1 141 191 37 ASN H H 8.3810 0.0000 1 142 191 37 ASN HD21 H 7.2837 0.0000 2 143 191 37 ASN HD22 H 6.5870 0.0000 2 144 191 37 ASN CA C 52.7060 0.0000 1 145 191 37 ASN CB C 40.8570 0.0000 1 146 191 37 ASN N N 120.7640 0.0000 1 147 191 37 ASN ND2 N 111.5069 0.0000 1 148 192 38 ASN H H 8.6620 0.0000 1 149 192 38 ASN HD21 H 7.2047 0.0000 2 150 192 38 ASN HD22 H 6.2661 0.0000 2 151 192 38 ASN CA C 52.4430 0.0000 1 152 192 38 ASN CB C 38.3240 0.0000 1 153 192 38 ASN N N 122.4600 0.0000 1 154 192 38 ASN ND2 N 109.1076 0.0000 1 155 193 39 GLY H H 8.2550 0.0000 1 156 193 39 GLY CA C 45.3940 0.0000 1 157 193 39 GLY N N 114.9260 0.0000 1 158 194 40 ARG H H 7.9370 0.0000 1 159 194 40 ARG CA C 55.8000 0.0000 1 160 194 40 ARG CB C 32.3470 0.0000 1 161 194 40 ARG N N 118.8490 0.0000 1 162 195 41 GLU H H 8.7150 0.0000 1 163 195 41 GLU CA C 57.4260 0.0000 1 164 195 41 GLU CB C 29.9400 0.0000 1 165 195 41 GLU N N 118.8530 0.0000 1 166 196 42 GLY H H 7.2860 0.0000 1 167 196 42 GLY CA C 43.4350 0.0000 1 168 196 42 GLY N N 106.7770 0.0000 1 169 197 43 GLU H H 8.2340 0.0000 1 170 197 43 GLU CA C 56.5350 0.0000 1 171 197 43 GLU CB C 31.0270 0.0000 1 172 197 43 GLU N N 118.0750 0.0000 1 173 198 44 ALA H H 8.8540 0.0000 1 174 198 44 ALA CA C 50.5410 0.0000 1 175 198 44 ALA CB C 21.9120 0.0000 1 176 198 44 ALA N N 127.0160 0.0000 1 177 199 45 ASN H H 9.1400 0.0000 1 178 199 45 ASN HD21 H 7.2283 0.0000 2 179 199 45 ASN HD22 H 7.0283 0.0000 2 180 199 45 ASN CA C 52.7630 0.0000 1 181 199 45 ASN CB C 41.6640 0.0000 1 182 199 45 ASN N N 123.6810 0.0000 1 183 199 45 ASN ND2 N 111.5075 0.0000 1 184 200 46 VAL H H 8.7710 0.0000 1 185 200 46 VAL CA C 57.7730 0.0000 1 186 200 46 VAL CB C 35.8080 0.0000 1 187 200 46 VAL N N 114.8520 0.0000 1 188 201 47 GLU H H 9.1430 0.0000 1 189 201 47 GLU CA C 54.1630 0.0000 1 190 201 47 GLU CB C 33.9110 0.0000 1 191 201 47 GLU N N 120.7990 0.0000 1 192 202 48 PHE H H 8.5890 0.0000 1 193 202 48 PHE CA C 55.6080 0.0000 1 194 202 48 PHE CB C 43.0270 0.0000 1 195 202 48 PHE N N 123.8280 0.0000 1 196 203 49 TRP H H 7.7540 0.0000 1 197 203 49 TRP CA C 56.3400 0.0000 1 198 203 49 TRP CB C 32.2790 0.0000 1 199 203 49 TRP N N 124.7740 0.0000 1 200 204 50 MET H H 7.9900 0.0000 1 201 204 50 MET CA C 54.4030 0.0000 1 202 204 50 MET CB C 37.8880 0.0000 1 203 204 50 MET N N 119.2160 0.0000 1 204 205 51 THR H H 8.5300 0.0000 1 205 205 51 THR CA C 60.3930 0.0000 1 206 205 51 THR CB C 72.3070 0.0000 1 207 205 51 THR N N 115.7050 0.0000 1 208 206 52 ALA H H 8.7960 0.0000 1 209 206 52 ALA CA C 50.8200 0.0000 1 210 206 52 ALA CB C 22.4890 0.0000 1 211 206 52 ALA N N 123.8980 0.0000 1 212 207 53 VAL H H 8.7930 0.0000 1 213 207 53 VAL CA C 60.9390 0.0000 1 214 207 53 VAL CB C 34.2680 0.0000 1 215 207 53 VAL N N 121.4840 0.0000 1 216 208 54 GLY H H 9.2260 0.0000 1 217 208 54 GLY CA C 45.0030 0.0000 1 218 208 54 GLY N N 114.5940 0.0000 1 219 209 55 PRO CA C 63.5640 0.0000 1 220 209 55 PRO CB C 32.1980 0.0000 1 221 210 56 ASP H H 8.6150 0.0000 1 222 210 56 ASP CA C 54.7310 0.0000 1 223 210 56 ASP CB C 40.0710 0.0000 1 224 210 56 ASP N N 118.1550 0.0000 1 225 211 57 GLY H H 8.1130 0.0000 1 226 211 57 GLY CA C 45.7330 0.0000 1 227 211 57 GLY N N 105.7160 0.0000 1 228 212 58 LEU H H 7.0220 0.0000 1 229 212 58 LEU CA C 55.6460 0.0000 1 230 212 58 LEU CB C 42.8360 0.0000 1 231 212 58 LEU N N 122.5730 0.0000 1 232 213 59 ILE H H 8.3020 0.0000 1 233 213 59 ILE CA C 60.5880 0.0000 1 234 213 59 ILE CB C 38.7520 0.0000 1 235 213 59 ILE N N 127.2580 0.0000 1 236 214 60 ILE H H 8.4550 0.0000 1 237 214 60 ILE CA C 58.0930 0.0000 1 238 214 60 ILE CB C 39.3240 0.0000 1 239 214 60 ILE N N 127.5260 0.0000 1 240 215 61 PRO CA C 63.2370 0.0000 1 241 215 61 PRO CB C 31.4270 0.0000 1 242 216 62 VAL H H 8.0150 0.0000 1 243 216 62 VAL CA C 62.4860 0.0000 1 244 216 62 VAL CB C 33.8850 0.0000 1 245 216 62 VAL N N 121.7000 0.0000 1 246 217 63 ASN H H 8.3150 0.0000 1 247 217 63 ASN HD21 H 7.9027 0.0000 2 248 217 63 ASN HD22 H 7.3868 0.0000 2 249 217 63 ASN CA C 53.6160 0.0000 1 250 217 63 ASN CB C 41.5030 0.0000 1 251 217 63 ASN N N 119.5200 0.0000 1 252 217 63 ASN ND2 N 113.4200 0.0000 1 253 218 64 ALA H H 8.4810 0.0000 1 254 218 64 ALA CA C 52.3010 0.0000 1 255 218 64 ALA CB C 19.8490 0.0000 1 256 218 64 ALA N N 125.6850 0.0000 1 257 219 65 ARG H H 7.9170 0.0000 1 258 219 65 ARG CA C 57.0190 0.0000 1 259 219 65 ARG CB C 30.7570 0.0000 1 260 219 65 ARG N N 119.6400 0.0000 1 261 220 66 GLU H H 8.7270 0.0000 1 262 220 66 GLU CA C 55.2050 0.0000 1 263 220 66 GLU CB C 34.1800 0.0000 1 264 220 66 GLU N N 123.7860 0.0000 1 265 221 67 LYS H H 8.2870 0.0000 1 266 221 67 LYS CA C 55.3050 0.0000 1 267 221 67 LYS CB C 34.0660 0.0000 1 268 221 67 LYS N N 121.4440 0.0000 1 269 222 68 TRP H H 9.1920 0.0000 1 270 222 68 TRP CA C 53.4780 0.0000 1 271 222 68 TRP CB C 32.3920 0.0000 1 272 222 68 TRP N N 126.4660 0.0000 1 273 223 69 VAL H H 8.2230 0.0000 1 274 223 69 VAL CA C 61.2250 0.0000 1 275 223 69 VAL CB C 33.3570 0.0000 1 276 223 69 VAL N N 122.6280 0.0000 1 277 224 70 ILE H H 8.9260 0.0000 1 278 224 70 ILE CA C 60.0350 0.0000 1 279 224 70 ILE CB C 40.7350 0.0000 1 280 224 70 ILE N N 126.9440 0.0000 1 281 225 71 ALA H H 9.3580 0.0000 1 282 225 71 ALA CA C 52.8660 0.0000 1 283 225 71 ALA CB C 19.2000 0.0000 1 284 225 71 ALA N N 132.4660 0.0000 1 285 226 72 SER H H 8.5540 0.0000 1 286 226 72 SER CA C 59.9940 0.0000 1 287 226 72 SER CB C 62.9280 0.0000 1 288 226 72 SER N N 114.7680 0.0000 1 289 227 73 GLY H H 8.4980 0.0000 1 290 227 73 GLY CA C 46.0860 0.0000 1 291 227 73 GLY N N 117.1560 0.0000 1 292 228 74 ASP H H 7.8850 0.0000 1 293 228 74 ASP CA C 53.4410 0.0000 1 294 228 74 ASP CB C 43.3000 0.0000 1 295 228 74 ASP N N 121.0480 0.0000 1 296 229 75 THR H H 8.1690 0.0000 1 297 229 75 THR CA C 60.3840 0.0000 1 298 229 75 THR CB C 71.2580 0.0000 1 299 229 75 THR N N 113.2880 0.0000 1 300 230 76 TYR H H 8.8930 0.0000 1 301 230 76 TYR CA C 57.0960 0.0000 1 302 230 76 TYR CB C 42.2130 0.0000 1 303 230 76 TYR N N 126.6550 0.0000 1 304 231 77 SER H H 7.9810 0.0000 1 305 231 77 SER CA C 56.9490 0.0000 1 306 231 77 SER CB C 65.0390 0.0000 1 307 231 77 SER N N 120.1780 0.0000 1 308 232 78 LYS H H 8.7810 0.0000 1 309 232 78 LYS CA C 53.3870 0.0000 1 310 232 78 LYS CB C 36.8810 0.0000 1 311 232 78 LYS N N 124.7730 0.0000 1 312 233 79 VAL H H 8.3300 0.0000 1 313 233 79 VAL CA C 61.8070 0.0000 1 314 233 79 VAL CB C 33.0850 0.0000 1 315 233 79 VAL N N 122.5650 0.0000 1 316 234 80 ARG H H 9.2020 0.0000 1 317 234 80 ARG CA C 53.1170 0.0000 1 318 234 80 ARG CB C 34.1870 0.0000 1 319 234 80 ARG N N 130.3290 0.0000 1 320 235 81 GLY H H 8.8304 0.0000 1 321 235 81 GLY CA C 46.1460 0.0000 1 322 235 81 GLY N N 108.0560 0.0000 1 323 236 82 ILE H H 7.3990 0.0000 1 324 236 82 ILE CA C 58.4390 0.0000 1 325 236 82 ILE CB C 41.2720 0.0000 1 326 236 82 ILE N N 117.1490 0.0000 1 327 237 83 ASN H H 8.8030 0.0000 1 328 237 83 ASN HD21 H 7.4709 0.0000 2 329 237 83 ASN HD22 H 6.7908 0.0000 2 330 237 83 ASN CA C 52.8800 0.0000 1 331 237 83 ASN CB C 40.4900 0.0000 1 332 237 83 ASN N N 124.8890 0.0000 1 333 237 83 ASN ND2 N 112.5460 0.0000 1 334 238 84 PHE H H 9.0270 0.0000 1 335 238 84 PHE CA C 57.6540 0.0000 1 336 238 84 PHE CB C 39.6330 0.0000 1 337 238 84 PHE N N 123.8230 0.0000 1 338 239 85 ASP H H 5.4770 0.0000 1 339 239 85 ASP CA C 53.6210 0.0000 1 340 239 85 ASP CB C 43.6690 0.0000 1 341 239 85 ASP N N 124.7370 0.0000 1 342 240 86 LYS H H 8.5030 0.0000 1 343 240 86 LYS CA C 59.1370 0.0000 1 344 240 86 LYS CB C 32.1720 0.0000 1 345 240 86 LYS N N 123.4010 0.0000 1 346 241 87 SER H H 8.4870 0.0000 1 347 241 87 SER CA C 59.7470 0.0000 1 348 241 87 SER CB C 64.1440 0.0000 1 349 241 87 SER N N 113.1980 0.0000 1 350 242 88 TYR H H 7.7210 0.0000 1 351 242 88 TYR CA C 53.9200 0.0000 1 352 242 88 TYR CB C 34.1770 0.0000 1 353 242 88 TYR N N 124.4790 0.0000 1 354 243 89 PRO CA C 62.8080 0.0000 1 355 243 89 PRO CB C 32.4320 0.0000 1 356 244 90 ALA H H 8.3640 0.0000 1 357 244 90 ALA CA C 52.9040 0.0000 1 358 244 90 ALA CB C 19.5470 0.0000 1 359 244 90 ALA N N 123.8950 0.0000 1 360 245 91 GLY H H 9.1140 0.0000 1 361 245 91 GLY CA C 43.8960 0.0000 1 362 245 91 GLY N N 107.6070 0.0000 1 363 246 92 GLU H H 8.4200 0.0000 1 364 246 92 GLU CA C 57.4150 0.0000 1 365 246 92 GLU CB C 31.4610 0.0000 1 366 246 92 GLU N N 119.8960 0.0000 1 367 247 93 TYR H H 9.3710 0.0000 1 368 247 93 TYR CA C 57.0330 0.0000 1 369 247 93 TYR CB C 40.6250 0.0000 1 370 247 93 TYR N N 124.8520 0.0000 1 371 248 94 THR H H 8.9550 0.0000 1 372 248 94 THR CA C 62.2800 0.0000 1 373 248 94 THR CB C 69.8270 0.0000 1 374 248 94 THR N N 118.5240 0.0000 1 375 249 95 ILE H H 9.5900 0.0000 1 376 249 95 ILE CA C 60.0780 0.0000 1 377 249 95 ILE CB C 38.8710 0.0000 1 378 249 95 ILE N N 130.0800 0.0000 1 379 250 96 ASN H H 8.8970 0.0000 1 380 250 96 ASN HD21 H 6.9110 0.0000 2 381 250 96 ASN HD22 H 6.7442 0.0000 2 382 250 96 ASN CA C 52.1890 0.0000 1 383 250 96 ASN CB C 41.4600 0.0000 1 384 250 96 ASN N N 125.7390 0.0000 1 385 250 96 ASN ND2 N 111.0982 0.0000 1 386 251 97 ALA H H 8.8540 0.0000 1 387 251 97 ALA CA C 50.2450 0.0000 1 388 251 97 ALA CB C 21.9730 0.0000 1 389 251 97 ALA N N 127.1430 0.0000 1 390 252 98 GLN H H 8.0930 0.0000 1 391 252 98 GLN HE21 H 6.8414 0.0000 2 392 252 98 GLN HE22 H 6.3283 0.0000 2 393 252 98 GLN CA C 54.1710 0.0000 1 394 252 98 GLN CB C 32.0460 0.0000 1 395 252 98 GLN N N 119.2130 0.0000 1 396 252 98 GLN NE2 N 110.2427 0.0000 1 397 253 99 VAL H H 8.3430 0.0000 1 398 253 99 VAL CA C 60.6890 0.0000 1 399 253 99 VAL CB C 34.5220 0.0000 1 400 253 99 VAL N N 119.6610 0.0000 1 401 254 100 VAL H H 8.9890 0.0000 1 402 254 100 VAL CA C 59.8130 0.0000 1 403 254 100 VAL CB C 36.0080 0.0000 1 404 254 100 VAL N N 125.4600 0.0000 1 405 255 101 ASP H H 8.8790 0.0000 1 406 255 101 ASP CA C 53.7500 0.0000 1 407 255 101 ASP CB C 42.4040 0.0000 1 408 255 101 ASP N N 126.4190 0.0000 1 409 256 102 ILE H H 8.2260 0.0000 1 410 256 102 ILE CA C 63.6780 0.0000 1 411 256 102 ILE CB C 37.9490 0.0000 1 412 256 102 ILE N N 124.2930 0.0000 1 413 257 103 VAL H H 8.6840 0.0000 1 414 257 103 VAL CA C 65.3300 0.0000 1 415 257 103 VAL CB C 31.8670 0.0000 1 416 257 103 VAL N N 121.0900 0.0000 1 417 258 104 SER H H 7.8130 0.0000 1 418 258 104 SER CA C 58.7370 0.0000 1 419 258 104 SER CB C 65.2230 0.0000 1 420 258 104 SER N N 113.3470 0.0000 1 421 259 105 GLY H H 8.6540 0.0000 1 422 259 105 GLY CA C 45.7880 0.0000 1 423 259 105 GLY N N 112.9600 0.0000 1 424 260 106 GLU H H 7.9440 0.0000 1 425 260 106 GLU CA C 51.1070 0.0000 1 426 260 106 GLU CB C 31.1970 0.0000 1 427 260 106 GLU N N 121.3630 0.0000 1 428 261 107 ARG H H 8.4470 0.0000 1 429 261 107 ARG CA C 54.2700 0.0000 1 430 261 107 ARG CB C 35.3350 0.0000 1 431 261 107 ARG N N 118.6680 0.0000 1 432 262 108 VAL H H 8.7820 0.0000 1 433 262 108 VAL CA C 61.3070 0.0000 1 434 262 108 VAL CB C 35.4580 0.0000 1 435 262 108 VAL N N 121.1420 0.0000 1 436 263 109 GLU H H 8.3670 0.0000 1 437 263 109 GLU CA C 54.1410 0.0000 1 438 263 109 GLU CB C 33.7820 0.0000 1 439 263 109 GLU N N 123.1610 0.0000 1 440 264 110 GLN H H 8.7260 0.0000 1 441 264 110 GLN HE21 H 7.3540 0.0000 2 442 264 110 GLN HE22 H 6.9351 0.0000 2 443 264 110 GLN CA C 55.0220 0.0000 1 444 264 110 GLN CB C 33.6740 0.0000 1 445 264 110 GLN N N 122.2520 0.0000 1 446 264 110 GLN NE2 N 111.4445 0.0000 1 447 265 111 SER H H 8.5700 0.0000 1 448 265 111 SER CA C 57.0260 0.0000 1 449 265 111 SER CB C 65.7010 0.0000 1 450 265 111 SER N N 119.6280 0.0000 1 451 266 112 MET H H 9.1560 0.0000 1 452 266 112 MET CA C 55.0620 0.0000 1 453 266 112 MET CB C 36.0580 0.0000 1 454 266 112 MET N N 123.5360 0.0000 1 455 267 113 THR H H 8.5850 0.0000 1 456 267 113 THR CA C 61.8120 0.0000 1 457 267 113 THR CB C 71.4790 0.0000 1 458 267 113 THR N N 116.5030 0.0000 1 459 268 114 VAL H H 8.9970 0.0000 1 460 268 114 VAL CA C 61.1560 0.0000 1 461 268 114 VAL CB C 36.6540 0.0000 1 462 268 114 VAL N N 124.2870 0.0000 1 463 269 115 VAL H H 8.0740 0.0000 1 464 269 115 VAL CA C 60.9990 0.0000 1 465 269 115 VAL CB C 34.5010 0.0000 1 466 269 115 VAL N N 125.1450 0.0000 1 467 270 116 LYS H H 9.3040 0.0000 1 468 270 116 LYS CA C 55.3410 0.0000 1 469 270 116 LYS CB C 35.5300 0.0000 1 470 270 116 LYS N N 128.5960 0.0000 1 471 271 117 LYS H H 8.4080 0.0000 1 472 271 117 LYS CA C 58.3770 0.0000 1 473 271 117 LYS CB C 33.7860 0.0000 1 474 271 117 LYS N N 104.0400 0.0000 1 stop_ save_