data_27930 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Human Kibra WW domain chemical shift ; _BMRB_accession_number 27930 _BMRB_flat_file_name bmr27930.str _Entry_type original _Submission_date 2019-05-29 _Accession_date 2019-05-29 _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 Nyarko Afua . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 109 "13C chemical shifts" 116 "15N chemical shifts" 70 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-12-04 update BMRB 'update entry citation' 2019-10-09 original author 'original release' stop_ _Original_release_date 2019-05-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31597702 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kwok Ethiene . . 2 Rodriguez Diego J. . 3 Kremerskothen Joachim . . 4 Nyarko Afua . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 294 _Journal_issue 46 _Journal_ISSN 1083-351X _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 17383 _Page_last 17394 _Year 2019 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Kibra WW domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Kibra WW domain' $Kibra_WW_domain 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_Kibra_WW_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Kibra_WW_domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; GAHMMPRPELPLPEGWEEAR DFDGKVYYIDHTNRTTSWID PRDRYTKPLTFADCISDELP LGWEEAYDPQVGDYFIDHNT KTTQIEDPRVQWRRE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 ALA 3 -1 HIS 4 0 MET 5 1 MET 6 2 PRO 7 3 ARG 8 4 PRO 9 5 GLU 10 6 LEU 11 7 PRO 12 8 LEU 13 9 PRO 14 10 GLU 15 11 GLY 16 12 TRP 17 13 GLU 18 14 GLU 19 15 ALA 20 16 ARG 21 17 ASP 22 18 PHE 23 19 ASP 24 20 GLY 25 21 LYS 26 22 VAL 27 23 TYR 28 24 TYR 29 25 ILE 30 26 ASP 31 27 HIS 32 28 THR 33 29 ASN 34 30 ARG 35 31 THR 36 32 THR 37 33 SER 38 34 TRP 39 35 ILE 40 36 ASP 41 37 PRO 42 38 ARG 43 39 ASP 44 40 ARG 45 41 TYR 46 42 THR 47 43 LYS 48 44 PRO 49 45 LEU 50 46 THR 51 47 PHE 52 48 ALA 53 49 ASP 54 50 CYS 55 51 ILE 56 52 SER 57 53 ASP 58 54 GLU 59 55 LEU 60 56 PRO 61 57 LEU 62 58 GLY 63 59 TRP 64 60 GLU 65 61 GLU 66 62 ALA 67 63 TYR 68 64 ASP 69 65 PRO 70 66 GLN 71 67 VAL 72 68 GLY 73 69 ASP 74 70 TYR 75 71 PHE 76 72 ILE 77 73 ASP 78 74 HIS 79 75 ASN 80 76 THR 81 77 LYS 82 78 THR 83 79 THR 84 80 GLN 85 81 ILE 86 82 GLU 87 83 ASP 88 84 PRO 89 85 ARG 90 86 VAL 91 87 GLN 92 88 TRP 93 89 ARG 94 90 ARG 95 91 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Kibra_WW_domain Human 9606 Eukaryota Metazoa Homo sapiens 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 $Kibra_WW_domain 'recombinant technology' . Escherichia coli . 'pET 24' 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 $Kibra_WW_domain 180 uM '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $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_ save_3D_HBHA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _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' 10 . mM pH 6.8 . pH pressure 1 . atm temperature 273 . 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 internal indirect . . . . DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal indirect . . . . 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' '3D HBHA(CO)NH' 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 'Kibra WW 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 1 5 MET H H 8.415 0.01 . 2 1 5 MET CA C 53.231 0.00 . 3 1 5 MET CB C 32.462 0.00 . 4 1 5 MET N N 124.080 0.12 . 5 2 6 PRO HA H 4.643 0.00 . 6 2 6 PRO CA C 62.646 0.06 . 7 2 6 PRO CB C 34.454 0.01 . 8 3 7 ARG H H 8.448 0.05 . 9 3 7 ARG CA C 54.128 0.01 . 10 3 7 ARG CB C 29.899 0.00 . 11 3 7 ARG N N 122.536 0.05 . 12 4 8 PRO HA H 4.364 0.00 . 13 4 8 PRO CA C 63.209 0.00 . 14 4 8 PRO CB C 32.029 0.07 . 15 5 9 GLU H H 8.503 0.01 . 16 5 9 GLU CA C 56.334 0.01 . 17 5 9 GLU CB C 30.053 0.06 . 18 5 9 GLU N N 121.440 0.10 . 19 6 10 LEU H H 8.101 0.00 . 20 6 10 LEU CA C 52.768 0.00 . 21 6 10 LEU N N 125.642 0.01 . 22 8 12 LEU H H 8.403 0.00 . 23 8 12 LEU N N 122.872 0.00 . 24 9 13 PRO HA H 4.372 0.00 . 25 9 13 PRO CA C 62.237 0.04 . 26 9 13 PRO CB C 31.418 0.00 . 27 10 14 GLU H H 8.416 0.01 . 28 10 14 GLU HA H 4.110 0.00 . 29 10 14 GLU CA C 58.185 0.02 . 30 10 14 GLU CB C 29.577 0.01 . 31 10 14 GLU N N 121.927 0.09 . 32 11 15 GLY H H 8.834 0.01 . 33 11 15 GLY HA2 H 4.280 0.00 . 34 11 15 GLY CA C 45.371 0.02 . 35 11 15 GLY N N 114.011 0.09 . 36 12 16 TRP H H 7.848 0.05 . 37 12 16 TRP CA C 56.727 0.04 . 38 12 16 TRP CB C 31.480 0.00 . 39 12 16 TRP N N 120.061 0.26 . 40 15 19 ALA H H 7.895 0.00 . 41 15 19 ALA N N 124.397 0.00 . 42 18 22 PHE H H 8.325 0.01 . 43 18 22 PHE HA H 4.361 0.00 . 44 18 22 PHE CA C 57.322 0.00 . 45 18 22 PHE CB C 38.910 0.18 . 46 18 22 PHE N N 119.274 0.13 . 47 19 23 ASP H H 7.889 0.04 . 48 19 23 ASP HA H 4.650 0.00 . 49 19 23 ASP CA C 53.723 0.06 . 50 19 23 ASP CB C 41.240 0.07 . 51 19 23 ASP N N 119.944 1.10 . 52 20 24 GLY H H 8.125 0.01 . 53 20 24 GLY HA2 H 4.219 0.00 . 54 20 24 GLY CA C 45.404 0.02 . 55 20 24 GLY N N 109.439 0.09 . 56 21 25 LYS H H 8.308 0.01 . 57 21 25 LYS CA C 56.781 0.03 . 58 21 25 LYS CB C 32.499 0.00 . 59 21 25 LYS N N 123.821 0.10 . 60 22 26 VAL H H 8.239 0.00 . 61 22 26 VAL HA H 4.525 0.00 . 62 22 26 VAL CA C 62.344 0.00 . 63 22 26 VAL CB C 32.901 0.00 . 64 22 26 VAL N N 124.579 0.00 . 65 23 27 TYR H H 8.420 0.01 . 66 23 27 TYR CA C 55.343 0.00 . 67 23 27 TYR CB C 39.017 0.00 . 68 23 27 TYR N N 124.413 0.09 . 69 25 29 ILE H H 8.063 0.00 . 70 25 29 ILE N N 126.542 0.00 . 71 26 30 ASP H H 8.154 0.00 . 72 26 30 ASP N N 124.358 0.00 . 73 28 32 THR H H 8.205 0.00 . 74 28 32 THR N N 116.850 0.00 . 75 30 34 ARG H H 7.862 0.00 . 76 30 34 ARG N N 116.838 0.00 . 77 34 38 TRP CB C 29.508 0.00 . 78 35 39 ILE H H 8.364 0.20 . 79 35 39 ILE HA H 4.119 0.00 . 80 35 39 ILE N N 127.071 3.71 . 81 36 40 ASP H H 8.353 0.01 . 82 36 40 ASP N N 129.456 0.13 . 83 37 41 PRO HA H 3.896 0.00 . 84 37 41 PRO CA C 63.410 0.07 . 85 38 42 ARG H H 8.376 0.01 . 86 38 42 ARG HA H 3.768 0.00 . 87 38 42 ARG CA C 57.449 0.05 . 88 38 42 ARG CB C 29.890 0.03 . 89 38 42 ARG N N 119.046 0.08 . 90 39 43 ASP H H 7.744 0.01 . 91 39 43 ASP HA H 4.454 0.00 . 92 39 43 ASP CA C 55.054 0.01 . 93 39 43 ASP CB C 40.474 0.04 . 94 39 43 ASP N N 120.040 0.08 . 95 40 44 ARG H H 7.452 0.01 . 96 40 44 ARG HA H 4.067 0.00 . 97 40 44 ARG CA C 56.658 0.00 . 98 40 44 ARG CB C 30.267 0.07 . 99 40 44 ARG N N 119.635 0.09 . 100 41 45 TYR H H 7.838 0.01 . 101 41 45 TYR HA H 4.604 0.00 . 102 41 45 TYR CA C 57.789 0.04 . 103 41 45 TYR CB C 38.621 0.06 . 104 41 45 TYR N N 119.803 0.08 . 105 42 46 THR H H 7.800 0.01 . 106 42 46 THR HA H 4.250 0.00 . 107 42 46 THR CA C 61.938 0.04 . 108 42 46 THR CB C 69.852 0.01 . 109 42 46 THR N N 116.123 0.08 . 110 43 47 LYS H H 8.079 0.00 . 111 43 47 LYS CA C 54.301 0.01 . 112 43 47 LYS CB C 32.596 0.00 . 113 43 47 LYS N N 125.614 0.08 . 114 44 48 PRO HA H 4.373 0.00 . 115 44 48 PRO CA C 62.947 0.03 . 116 44 48 PRO CB C 32.050 0.02 . 117 45 49 LEU H H 8.305 0.01 . 118 45 49 LEU HA H 4.287 0.00 . 119 45 49 LEU CA C 55.469 0.05 . 120 45 49 LEU CB C 42.358 0.01 . 121 45 49 LEU N N 122.917 0.10 . 122 46 50 THR H H 7.925 0.01 . 123 46 50 THR HA H 4.333 0.00 . 124 46 50 THR CA C 61.184 0.05 . 125 46 50 THR CB C 70.312 0.00 . 126 46 50 THR N N 114.064 0.16 . 127 47 51 PHE H H 8.194 0.01 . 128 47 51 PHE HA H 4.539 0.00 . 129 47 51 PHE CA C 58.199 0.01 . 130 47 51 PHE CB C 39.484 0.03 . 131 47 51 PHE N N 122.442 0.09 . 132 48 52 ALA H H 8.093 0.01 . 133 48 52 ALA HA H 4.212 0.01 . 134 48 52 ALA CA C 52.873 0.02 . 135 48 52 ALA CB C 19.298 0.04 . 136 48 52 ALA N N 124.906 0.08 . 137 49 53 ASP H H 8.044 0.00 . 138 49 53 ASP HA H 4.554 0.00 . 139 49 53 ASP CA C 54.525 0.03 . 140 49 53 ASP CB C 41.134 0.03 . 141 49 53 ASP N N 119.067 0.00 . 142 50 54 CYS H H 7.954 0.00 . 143 50 54 CYS HA H 4.472 0.00 . 144 50 54 CYS CA C 58.560 0.00 . 145 50 54 CYS CB C 28.133 0.03 . 146 50 54 CYS N N 118.801 0.00 . 147 51 55 ILE H H 8.142 0.01 . 148 51 55 ILE HA H 4.177 0.00 . 149 51 55 ILE CA C 61.372 0.04 . 150 51 55 ILE CB C 38.547 0.04 . 151 51 55 ILE N N 123.339 0.01 . 152 52 56 SER H H 8.240 0.00 . 153 52 56 SER HA H 4.417 0.00 . 154 52 56 SER CA C 58.309 0.02 . 155 52 56 SER CB C 63.888 0.01 . 156 52 56 SER N N 119.772 0.08 . 157 53 57 ASP H H 8.254 0.01 . 158 53 57 ASP HA H 4.595 0.02 . 159 53 57 ASP CA C 54.379 0.02 . 160 53 57 ASP CB C 40.928 0.03 . 161 53 57 ASP N N 122.929 0.09 . 162 54 58 GLU H H 8.085 0.00 . 163 54 58 GLU CA C 56.162 0.02 . 164 54 58 GLU CB C 30.176 0.00 . 165 54 58 GLU N N 120.326 0.00 . 166 55 59 LEU H H 7.771 0.00 . 167 55 59 LEU N N 122.005 0.00 . 168 56 60 PRO HA H 4.270 0.00 . 169 56 60 PRO CA C 62.790 0.00 . 170 56 60 PRO CB C 32.018 0.00 . 171 57 61 LEU H H 8.231 0.01 . 172 57 61 LEU HA H 4.225 0.00 . 173 57 61 LEU CA C 55.805 0.06 . 174 57 61 LEU CB C 42.090 0.05 . 175 57 61 LEU N N 123.016 0.13 . 176 58 62 GLY H H 8.636 0.01 . 177 58 62 GLY HA2 H 3.990 0.00 . 178 58 62 GLY CA C 45.387 0.01 . 179 58 62 GLY N N 111.534 0.08 . 180 59 63 TRP H H 7.853 0.01 . 181 59 63 TRP CA C 58.091 0.03 . 182 59 63 TRP CB C 29.354 0.00 . 183 59 63 TRP N N 121.781 0.10 . 184 60 64 GLU H H 8.341 0.00 . 185 60 64 GLU HA H 4.382 0.00 . 186 60 64 GLU CA C 55.765 0.01 . 187 60 64 GLU CB C 32.958 0.01 . 188 60 64 GLU N N 126.405 0.00 . 189 61 65 GLU H H 7.992 0.01 . 190 61 65 GLU CA C 52.645 0.00 . 191 61 65 GLU CB C 34.177 0.00 . 192 61 65 GLU N N 121.367 0.08 . 193 62 66 ALA H H 8.031 0.00 . 194 62 66 ALA N N 124.722 0.00 . 195 63 67 TYR H H 7.918 0.00 . 196 63 67 TYR N N 120.590 0.00 . 197 64 68 ASP H H 8.041 0.00 . 198 64 68 ASP N N 125.401 0.00 . 199 65 69 PRO HA H 4.387 0.00 . 200 65 69 PRO CA C 63.645 0.06 . 201 65 69 PRO CB C 32.064 0.00 . 202 66 70 GLN H H 8.356 0.02 . 203 66 70 GLN CA C 57.161 0.00 . 204 66 70 GLN N N 119.538 0.12 . 205 67 71 VAL H H 7.848 0.00 . 206 67 71 VAL N N 119.681 0.00 . 207 68 72 GLY H H 8.220 0.00 . 208 68 72 GLY CA C 45.355 0.01 . 209 68 72 GLY N N 111.499 0.00 . 210 69 73 ASP H H 8.063 0.01 . 211 69 73 ASP CA C 54.335 0.00 . 212 69 73 ASP CB C 41.118 0.00 . 213 69 73 ASP N N 121.105 0.10 . 214 70 74 TYR H H 7.971 0.00 . 215 70 74 TYR N N 120.799 0.00 . 216 71 75 PHE H H 8.029 0.00 . 217 71 75 PHE CA C 58.002 0.03 . 218 71 75 PHE CB C 39.459 0.00 . 219 71 75 PHE N N 121.478 0.18 . 220 72 76 ILE H H 7.790 0.02 . 221 72 76 ILE N N 122.901 0.06 . 222 73 77 ASP H H 8.170 0.01 . 223 73 77 ASP CA C 53.944 0.00 . 224 73 77 ASP CB C 41.143 0.00 . 225 73 77 ASP N N 124.173 0.13 . 226 75 79 ASN H H 7.922 0.00 . 227 75 79 ASN CA C 53.786 0.01 . 228 75 79 ASN CB C 38.872 0.00 . 229 75 79 ASN N N 122.142 0.00 . 230 76 80 THR H H 8.035 0.01 . 231 76 80 THR HA H 4.282 0.00 . 232 76 80 THR CA C 62.299 0.01 . 233 76 80 THR CB C 69.700 0.05 . 234 76 80 THR N N 115.428 0.09 . 235 77 81 LYS H H 8.310 0.01 . 236 77 81 LYS HA H 4.379 0.00 . 237 77 81 LYS CA C 56.431 0.03 . 238 77 81 LYS CB C 32.904 0.01 . 239 77 81 LYS N N 124.327 0.09 . 240 78 82 THR H H 8.117 0.01 . 241 78 82 THR CA C 61.850 0.03 . 242 78 82 THR CB C 69.806 0.06 . 243 78 82 THR N N 115.804 0.09 . 244 79 83 THR HA H 4.332 0.00 . 245 79 83 THR CA C 61.915 0.01 . 246 79 83 THR CB C 69.810 0.04 . 247 79 83 THR N N 95.262 43.60 . 248 80 84 GLN H H 8.334 0.01 . 249 80 84 GLN HA H 4.366 0.00 . 250 80 84 GLN CA C 55.739 0.01 . 251 80 84 GLN CB C 29.540 0.04 . 252 80 84 GLN N N 123.845 0.10 . 253 81 85 ILE H H 8.125 0.00 . 254 81 85 ILE HA H 4.121 0.00 . 255 81 85 ILE CA C 61.159 0.04 . 256 81 85 ILE CB C 38.744 0.06 . 257 81 85 ILE N N 123.072 0.05 . 258 82 86 GLU H H 8.341 0.00 . 259 82 86 GLU HA H 4.254 0.00 . 260 82 86 GLU CA C 56.168 0.04 . 261 82 86 GLU CB C 30.176 0.00 . 262 82 86 GLU N N 125.643 0.09 . 263 83 87 ASP H H 8.090 0.07 . 264 83 87 ASP CA C 52.910 0.00 . 265 83 87 ASP CB C 41.766 0.00 . 266 83 87 ASP N N 124.859 0.38 . 267 84 88 PRO HA H 4.377 0.00 . 268 85 89 ARG H H 8.326 0.02 . 269 85 89 ARG CA C 56.948 0.02 . 270 85 89 ARG CB C 30.192 0.02 . 271 85 89 ARG N N 120.876 1.64 . 272 86 90 VAL H H 7.679 0.01 . 273 86 90 VAL HA H 3.977 0.00 . 274 86 90 VAL CA C 62.603 0.02 . 275 86 90 VAL CB C 32.418 0.04 . 276 86 90 VAL N N 119.337 0.09 . 277 87 91 GLN H H 8.074 0.01 . 278 87 91 GLN CA C 55.982 0.01 . 279 87 91 GLN CB C 29.250 0.01 . 280 87 91 GLN N N 123.237 0.09 . 281 88 92 TRP H H 7.931 0.01 . 282 88 92 TRP CA C 57.088 0.04 . 283 88 92 TRP CB C 29.485 0.00 . 284 88 92 TRP N N 122.546 0.11 . 285 89 93 ARG H H 7.898 0.01 . 286 89 93 ARG HA H 4.209 0.00 . 287 89 93 ARG CA C 55.856 0.00 . 288 89 93 ARG CB C 31.063 0.06 . 289 89 93 ARG N N 123.466 0.09 . 290 90 94 ARG H H 8.178 0.01 . 291 90 94 ARG CA C 56.098 0.00 . 292 90 94 ARG CB C 30.861 0.00 . 293 90 94 ARG N N 123.891 0.01 . 294 91 95 GLU H H 7.891 0.00 . 295 91 95 GLU N N 127.481 0.00 . stop_ save_