data_16949 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; PDZ3 of ZO-1 ; _BMRB_accession_number 16949 _BMRB_flat_file_name bmr16949.str _Entry_type original _Submission_date 2010-05-24 _Accession_date 2010-05-24 _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 Wang Xingsheng . . 2 Tash Brian . . 3 Flanagan John M. . 4 Tian Fang . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 residual_dipolar_couplings 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 98 "13C chemical shifts" 193 "15N chemical shifts" 98 "residual dipolar couplings" 170 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-08-02 original author . stop_ _Original_release_date 2012-08-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protein Backbone Resonance Assignment Assisted with Predicted Local Structures' _Citation_status 'in preparation' _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 Wang Xingsheng . . 2 Tash Brian . . 3 'M. Flanagan' John . . 4 Tian Fang . . stop_ _Journal_abbreviation 'Not known' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword 'backbone resonance assignment' 'predicted structures' 'residual dipolar couplings' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'PDZ3 of ZO-1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PDZ3_of_ZO-1 $PDZ3_of_ZO-1 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_PDZ3_of_ZO-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PDZ3_of_ZO-1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; GHMPNSTHEDGILRPSMKLV KFRKGDSVGLRLAGGNDVGI FVAGVLEDSPAAKEGLEEGD QILRVNNVDFTNIIREEAVL FLLDLPKGEEVTILAQKKKD VYRRIVESDVGDS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 HIS 3 MET 4 PRO 5 ASN 6 SER 7 THR 8 HIS 9 GLU 10 ASP 11 GLY 12 ILE 13 LEU 14 ARG 15 PRO 16 SER 17 MET 18 LYS 19 LEU 20 VAL 21 LYS 22 PHE 23 ARG 24 LYS 25 GLY 26 ASP 27 SER 28 VAL 29 GLY 30 LEU 31 ARG 32 LEU 33 ALA 34 GLY 35 GLY 36 ASN 37 ASP 38 VAL 39 GLY 40 ILE 41 PHE 42 VAL 43 ALA 44 GLY 45 VAL 46 LEU 47 GLU 48 ASP 49 SER 50 PRO 51 ALA 52 ALA 53 LYS 54 GLU 55 GLY 56 LEU 57 GLU 58 GLU 59 GLY 60 ASP 61 GLN 62 ILE 63 LEU 64 ARG 65 VAL 66 ASN 67 ASN 68 VAL 69 ASP 70 PHE 71 THR 72 ASN 73 ILE 74 ILE 75 ARG 76 GLU 77 GLU 78 ALA 79 VAL 80 LEU 81 PHE 82 LEU 83 LEU 84 ASP 85 LEU 86 PRO 87 LYS 88 GLY 89 GLU 90 GLU 91 VAL 92 THR 93 ILE 94 LEU 95 ALA 96 GLN 97 LYS 98 LYS 99 LYS 100 ASP 101 VAL 102 TYR 103 ARG 104 ARG 105 ILE 106 VAL 107 GLU 108 SER 109 ASP 110 VAL 111 GLY 112 ASP 113 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-01 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 PDB 3SHU "Crystal Structure Of Zo-1 Pdz3" 81.42 95 100.00 100.00 2.60e-55 PDB 3SHW "Crystal Structure Of Zo-1 Pdz3-Sh3-Guk Supramodule Complex With Connexin-45 Peptide" 86.73 468 100.00 100.00 1.06e-56 PDB 3TSV "Crystal Structure Of The Third Pdz Domain Of The Human Zo-1 Maguk Protein" 88.50 124 100.00 100.00 5.98e-62 PDB 3TSW "Crystal Structure Of The Pdz3-Sh3-Guk Core Module Of Human Zo-1" 90.27 391 100.00 100.00 1.54e-60 PDB 3TSZ "Crystal Structure Of Pdz3-Sh3-Guk Core Module From Human Zo-1 In Complex With 12mer Peptide From Human Jam-A Cytoplasmic Tail" 90.27 391 100.00 100.00 1.54e-60 PDB 4Q2Q "Zo1 Pdz3 In Complex With A Phage-derived Peptide" 76.99 102 98.85 100.00 1.29e-51 DBJ BAA03274 "ZO-1 [Mus musculus domesticus]" 100.00 1745 97.35 98.23 1.98e-63 EMBL CAC41969 "tight junction protein 1 [Bos taurus]" 59.29 90 100.00 100.00 4.67e-37 EMBL CAC41992 "tight junction protein 1 [Ovis aries]" 59.29 82 100.00 100.00 3.08e-37 EMBL CAH18091 "hypothetical protein [Homo sapiens]" 85.84 1267 98.97 98.97 3.18e-53 GB ADB79761 "TJP1-like protein [Varecia variegata variegata]" 100.00 481 98.23 99.12 1.76e-67 GB KFO12263 "Tight junction protein ZO-1, partial [Balearica regulorum gibbericeps]" 100.00 1405 97.35 99.12 1.20e-64 GB KFP69448 "Tight junction protein ZO-1, partial [Acanthisitta chloris]" 100.00 1583 97.35 99.12 6.09e-64 GB KFP80555 "Tight junction protein ZO-1, partial [Apaloderma vittatum]" 88.50 995 100.00 100.00 5.19e-57 GB KFW05584 "Tight junction protein ZO-1, partial [Eurypyga helias]" 100.00 1400 97.35 99.12 1.39e-64 REF XP_002825269 "PREDICTED: tight junction protein ZO-1 [Pongo abelii]" 85.84 1267 100.00 100.00 3.07e-54 REF XP_005196258 "PREDICTED: tight junction protein ZO-1 isoform X2 [Bos taurus]" 100.00 1416 98.23 99.12 2.45e-64 REF XP_005196259 "PREDICTED: tight junction protein ZO-1 isoform X3 [Bos taurus]" 100.00 1409 98.23 99.12 2.32e-64 REF XP_005196260 "PREDICTED: tight junction protein ZO-1 isoform X4 [Bos taurus]" 100.00 1349 98.23 99.12 1.82e-64 REF XP_005196261 "PREDICTED: tight junction protein ZO-1 isoform X5 [Bos taurus]" 100.00 1329 98.23 99.12 2.04e-64 TPG DAA17567 "TPA: tight junction protein 1 (zona occludens 1) [Bos taurus]" 87.61 1287 100.00 100.00 8.57e-56 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PDZ3_of_ZO-1 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 $PDZ3_of_ZO-1 'recombinant technology' . Escherichia coli . pET 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 $PDZ3_of_ZO-1 1 mM '[U-100% 13C; U-100% 15N]' $PDZ3_of_ZO-1 0.5 mM '[U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _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' 0.1 . M pH 7.0 . pH pressure 1 . atm temperature 298 . 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 HNCACB' '3D CBCA(CO)NH' '3D 1H-15N NOESY' 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 PDZ3_of_ZO-1 _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 4 4 PRO CA C 63.364 . 1 2 4 4 PRO CB C 32.410 . 1 3 5 5 ASN H H 8.601 . 1 4 5 5 ASN CA C 53.727 . 1 5 5 5 ASN CB C 39.113 . 1 6 5 5 ASN N N 118.62 . 1 7 6 6 SER H H 8.263 . 1 8 6 6 SER CA C 58.783 . 1 9 6 6 SER CB C 64.284 . 1 10 6 6 SER N N 115.69 . 1 11 7 7 THR H H 8.241 . 1 12 7 7 THR CA C 62.416 . 1 13 7 7 THR CB C 70.096 . 1 14 7 7 THR N N 115.17 . 1 15 8 8 HIS H H 8.308 . 1 16 8 8 HIS CA C 56.714 . 1 17 8 8 HIS CB C 31.290 . 1 18 8 8 HIS N N 121.26 . 1 19 9 9 GLU H H 8.406 . 1 20 9 9 GLU CA C 57.113 . 1 21 9 9 GLU CB C 30.675 . 1 22 9 9 GLU N N 122.41 . 1 23 10 10 ASP H H 8.474 . 1 24 10 10 ASP CA C 55.154 . 1 25 10 10 ASP CB C 41.444 . 1 26 10 10 ASP N N 121.67 . 1 27 11 11 GLY H H 8.342 . 1 28 11 11 GLY CA C 46.027 . 1 29 11 11 GLY N N 108.58 . 1 30 12 12 ILE H H 7.867 . 1 31 12 12 ILE CA C 61.268 . 1 32 12 12 ILE CB C 38.799 . 1 33 12 12 ILE N N 120.17 . 1 34 13 13 LEU H H 8.316 . 1 35 13 13 LEU CA C 55.466 . 1 36 13 13 LEU CB C 42.585 . 1 37 13 13 LEU N N 126.15 . 1 38 14 14 ARG H H 8.191 . 1 39 14 14 ARG CA C 54.480 . 1 40 14 14 ARG CB C 29.984 . 1 41 14 14 ARG N N 123.73 . 1 42 16 16 SER H H 8.393 . 1 43 16 16 SER CA C 59.333 . 1 44 16 16 SER CB C 63.722 . 1 45 16 16 SER N N 114.63 . 1 46 17 17 MET H H 8.105 . 1 47 17 17 MET CA C 55.294 . 1 48 17 17 MET CB C 34.386 . 1 49 17 17 MET N N 121.46 . 1 50 18 18 LYS H H 9.135 . 1 51 18 18 LYS CA C 55.504 . 1 52 18 18 LYS CB C 36.097 . 1 53 18 18 LYS N N 121.52 . 1 54 19 19 LEU H H 8.472 . 1 55 19 19 LEU CA C 54.058 . 1 56 19 19 LEU CB C 43.807 . 1 57 19 19 LEU N N 126.21 . 1 58 20 20 VAL H H 9.311 . 1 59 20 20 VAL CA C 60.808 . 1 60 20 20 VAL CB C 34.994 . 1 61 20 20 VAL N N 126.18 . 1 62 21 21 LYS H H 8.860 . 1 63 21 21 LYS CA C 54.985 . 1 64 21 21 LYS CB C 36.073 . 1 65 21 21 LYS N N 125.84 . 1 66 22 22 PHE H H 8.171 . 1 67 22 22 PHE CA C 55.683 . 1 68 22 22 PHE CB C 40.924 . 1 69 22 22 PHE N N 117.13 . 1 70 23 23 ARG H H 8.967 . 1 71 23 23 ARG CA C 55.595 . 1 72 23 23 ARG CB C 31.022 . 1 73 23 23 ARG N N 120.35 . 1 74 24 24 LYS H H 7.959 . 1 75 24 24 LYS CA C 58.108 . 1 76 24 24 LYS CB C 33.634 . 1 77 24 24 LYS N N 126.70 . 1 78 25 25 GLY H H 8.449 . 1 79 25 25 GLY CA C 44.718 . 1 80 25 25 GLY N N 117.69 . 1 81 26 26 ASP CA C 57.288 . 1 82 26 26 ASP CB C 41.342 . 1 83 27 27 SER H H 7.872 . 1 84 27 27 SER CA C 56.728 . 1 85 27 27 SER CB C 65.213 . 1 86 27 27 SER N N 109.74 . 1 87 28 28 VAL CA C 64.997 . 1 88 28 28 VAL CB C 32.182 . 1 89 29 29 GLY H H 7.287 . 1 90 29 29 GLY CA C 46.773 . 1 91 29 29 GLY N N 114.93 . 1 92 30 30 LEU H H 7.099 . 1 93 30 30 LEU CA C 53.602 . 1 94 30 30 LEU CB C 46.001 . 1 95 30 30 LEU N N 115.34 . 1 96 31 31 ARG H H 8.570 . 1 97 31 31 ARG CA C 55.136 . 1 98 31 31 ARG CB C 32.548 . 1 99 31 31 ARG N N 123.60 . 1 100 32 32 LEU H H 9.131 . 1 101 32 32 LEU CA C 53.859 . 1 102 32 32 LEU CB C 44.793 . 1 103 32 32 LEU N N 124.17 . 1 104 33 33 ALA H H 9.368 . 1 105 33 33 ALA CA C 50.985 . 1 106 33 33 ALA CB C 24.008 . 1 107 33 33 ALA N N 124.16 . 1 108 34 34 GLY H H 8.943 . 1 109 34 34 GLY CA C 44.609 . 1 110 34 34 GLY N N 107.60 . 1 111 35 35 GLY H H 8.506 . 1 112 35 35 GLY CA C 45.518 . 1 113 35 35 GLY N N 109.30 . 1 114 36 36 ASN H H 8.670 . 1 115 36 36 ASN CA C 55.550 . 1 116 36 36 ASN CB C 37.931 . 1 117 36 36 ASN N N 118.04 . 1 118 37 37 ASP H H 8.779 . 1 119 37 37 ASP CA C 55.686 . 1 120 37 37 ASP CB C 40.603 . 1 121 37 37 ASP N N 118.20 . 1 122 38 38 VAL H H 7.783 . 1 123 38 38 VAL CA C 62.839 . 1 124 38 38 VAL CB C 33.653 . 1 125 38 38 VAL N N 114.17 . 1 126 39 39 GLY H H 7.678 . 1 127 39 39 GLY CA C 44.360 . 1 128 39 39 GLY N N 108.79 . 1 129 40 40 ILE H H 9.035 . 1 130 40 40 ILE CA C 57.587 . 1 131 40 40 ILE CB C 36.849 . 1 132 40 40 ILE N N 120.34 . 1 133 41 41 PHE H H 9.103 . 1 134 41 41 PHE CA C 55.656 . 1 135 41 41 PHE CB C 44.486 . 1 136 41 41 PHE N N 124.43 . 1 137 42 42 VAL H H 9.123 . 1 138 42 42 VAL CA C 63.583 . 1 139 42 42 VAL CB C 31.803 . 1 140 42 42 VAL N N 120.62 . 1 141 43 43 ALA H H 9.292 . 1 142 43 43 ALA CA C 51.788 . 1 143 43 43 ALA CB C 20.748 . 1 144 43 43 ALA N N 132.82 . 1 145 44 44 GLY H H 7.442 . 1 146 44 44 GLY CA C 45.709 . 1 147 44 44 GLY N N 104.36 . 1 148 45 45 VAL H H 8.558 . 1 149 45 45 VAL CA C 59.723 . 1 150 45 45 VAL CB C 34.650 . 1 151 45 45 VAL N N 120.64 . 1 152 46 46 LEU H H 8.389 . 1 153 46 46 LEU CA C 55.529 . 1 154 46 46 LEU CB C 42.279 . 1 155 46 46 LEU N N 128.00 . 1 156 48 48 ASP H H 8.816 . 1 157 48 48 ASP CA C 55.426 . 1 158 48 48 ASP CB C 40.306 . 1 159 48 48 ASP N N 117.61 . 1 160 49 49 SER H H 7.705 . 1 161 49 49 SER CA C 57.121 . 1 162 49 49 SER CB C 63.931 . 1 163 49 49 SER N N 114.86 . 1 164 51 51 ALA H H 7.571 . 1 165 51 51 ALA CA C 55.406 . 1 166 51 51 ALA CB C 18.452 . 1 167 51 51 ALA N N 116.61 . 1 168 52 52 ALA H H 7.263 . 1 169 52 52 ALA CA C 54.591 . 1 170 52 52 ALA CB C 18.957 . 1 171 52 52 ALA N N 119.11 . 1 172 53 53 LYS H H 8.206 . 1 173 53 53 LYS CA C 59.213 . 1 174 53 53 LYS CB C 32.371 . 1 175 53 53 LYS N N 120.05 . 1 176 54 54 GLU H H 7.629 . 1 177 54 54 GLU CA C 55.667 . 1 178 54 54 GLU CB C 30.304 . 1 179 54 54 GLU N N 114.55 . 1 180 55 55 GLY H H 7.497 . 1 181 55 55 GLY CA C 46.194 . 1 182 55 55 GLY N N 104.33 . 1 183 56 56 LEU H H 7.741 . 1 184 56 56 LEU CA C 55.837 . 1 185 56 56 LEU CB C 42.669 . 1 186 56 56 LEU N N 122.06 . 1 187 57 57 GLU H H 8.775 . 1 188 57 57 GLU CA C 54.745 . 1 189 57 57 GLU CB C 35.515 . 1 190 57 57 GLU N N 121.54 . 1 191 58 58 GLU H H 8.450 . 1 192 58 58 GLU CA C 57.581 . 1 193 58 58 GLU CB C 29.662 . 1 194 58 58 GLU N N 119.93 . 1 195 59 59 GLY H H 8.947 . 1 196 59 59 GLY CA C 45.156 . 1 197 59 59 GLY N N 115.39 . 1 198 60 60 ASP H H 7.807 . 1 199 60 60 ASP CA C 55.089 . 1 200 60 60 ASP CB C 40.783 . 1 201 60 60 ASP N N 120.59 . 1 202 61 61 GLN H H 9.339 . 1 203 61 61 GLN CA C 54.312 . 1 204 61 61 GLN CB C 29.741 . 1 205 61 61 GLN N N 123.96 . 1 206 62 62 ILE H H 8.757 . 1 207 62 62 ILE CA C 61.386 . 1 208 62 62 ILE CB C 37.933 . 1 209 62 62 ILE N N 126.51 . 1 210 63 63 LEU H H 9.200 . 1 211 63 63 LEU CA C 55.998 . 1 212 63 63 LEU CB C 42.568 . 1 213 63 63 LEU N N 127.75 . 1 214 64 64 ARG H H 7.765 . 1 215 64 64 ARG CA C 55.735 . 1 216 64 64 ARG CB C 35.487 . 1 217 64 64 ARG N N 120.32 . 1 218 65 65 VAL H H 8.101 . 1 219 65 65 VAL CA C 61.283 . 1 220 65 65 VAL CB C 33.424 . 1 221 65 65 VAL N N 123.25 . 1 222 66 66 ASN H H 9.776 . 1 223 66 66 ASN CA C 55.274 . 1 224 66 66 ASN CB C 35.437 . 1 225 66 66 ASN N N 126.61 . 1 226 67 67 ASN CA C 53.730 . 1 227 67 67 ASN CB C 38.702 . 1 228 68 68 VAL H H 8.617 . 1 229 68 68 VAL CA C 63.133 . 1 230 68 68 VAL CB C 32.609 . 1 231 68 68 VAL N N 124.01 . 1 232 69 69 ASP H H 8.574 . 1 233 69 69 ASP CA C 55.501 . 1 234 69 69 ASP CB C 41.541 . 1 235 69 69 ASP N N 127.31 . 1 236 70 70 PHE H H 8.717 . 1 237 70 70 PHE CA C 57.043 . 1 238 70 70 PHE CB C 40.353 . 1 239 70 70 PHE N N 130.48 . 1 240 71 71 THR H H 8.940 . 1 241 71 71 THR CA C 65.293 . 1 242 71 71 THR CB C 69.519 . 1 243 71 71 THR N N 115.98 . 1 244 73 73 ILE H H 7.781 . 1 245 73 73 ILE CA C 59.902 . 1 246 73 73 ILE CB C 42.001 . 1 247 73 73 ILE N N 120.59 . 1 248 74 74 ILE H H 7.952 . 1 249 74 74 ILE CA C 61.451 . 1 250 74 74 ILE CB C 38.948 . 1 251 74 74 ILE N N 122.53 . 1 252 75 75 ARG H H 9.059 . 1 253 75 75 ARG CA C 61.249 . 1 254 75 75 ARG CB C 29.860 . 1 255 75 75 ARG N N 127.61 . 1 256 76 76 GLU H H 9.395 . 1 257 76 76 GLU CA C 61.223 . 1 258 76 76 GLU CB C 29.726 . 1 259 76 76 GLU N N 116.45 . 1 260 77 77 GLU H H 6.832 . 1 261 77 77 GLU CA C 59.130 . 1 262 77 77 GLU CB C 29.738 . 1 263 77 77 GLU N N 117.07 . 1 264 78 78 ALA H H 7.764 . 1 265 78 78 ALA CA C 55.505 . 1 266 78 78 ALA CB C 19.195 . 1 267 78 78 ALA N N 124.71 . 1 268 79 79 VAL H H 8.234 . 1 269 79 79 VAL CA C 66.865 . 1 270 79 79 VAL CB C 32.689 . 1 271 79 79 VAL N N 116.73 . 1 272 80 80 LEU H H 7.614 . 1 273 80 80 LEU CA C 58.039 . 1 274 80 80 LEU CB C 42.173 . 1 275 80 80 LEU N N 119.66 . 1 276 81 81 PHE H H 8.232 . 1 277 81 81 PHE CA C 61.658 . 1 278 81 81 PHE CB C 39.307 . 1 279 81 81 PHE N N 119.42 . 1 280 82 82 LEU H H 7.790 . 1 281 82 82 LEU CA C 57.731 . 1 282 82 82 LEU CB C 41.963 . 1 283 82 82 LEU N N 115.50 . 1 284 83 83 LEU H H 8.081 . 1 285 83 83 LEU CA C 58.289 . 1 286 83 83 LEU CB C 42.666 . 1 287 83 83 LEU N N 121.46 . 1 288 84 84 ASP H H 7.964 . 1 289 84 84 ASP CA C 55.429 . 1 290 84 84 ASP CB C 41.308 . 1 291 84 84 ASP N N 117.07 . 1 292 85 85 LEU H H 6.938 . 1 293 85 85 LEU CA C 53.465 . 1 294 85 85 LEU CB C 41.440 . 1 295 85 85 LEU N N 121.60 . 1 296 88 88 GLY H H 8.972 . 1 297 88 88 GLY CA C 45.670 . 1 298 88 88 GLY N N 113.28 . 1 299 89 89 GLU H H 7.134 . 1 300 89 89 GLU CA C 55.202 . 1 301 89 89 GLU CB C 31.454 . 1 302 89 89 GLU N N 117.95 . 1 303 90 90 GLU H H 9.143 . 1 304 90 90 GLU CA C 57.712 . 1 305 90 90 GLU CB C 31.387 . 1 306 90 90 GLU N N 125.28 . 1 307 91 91 VAL H H 9.245 . 1 308 91 91 VAL CA C 60.788 . 1 309 91 91 VAL CB C 33.560 . 1 310 91 91 VAL N N 129.93 . 1 311 92 92 THR H H 8.363 . 1 312 92 92 THR CA C 61.252 . 1 313 92 92 THR CB C 70.190 . 1 314 92 92 THR N N 120.20 . 1 315 93 93 ILE H H 9.687 . 1 316 93 93 ILE CA C 60.696 . 1 317 93 93 ILE CB C 41.601 . 1 318 93 93 ILE N N 128.19 . 1 319 94 94 LEU H H 8.477 . 1 320 94 94 LEU CA C 53.757 . 1 321 94 94 LEU CB C 44.541 . 1 322 94 94 LEU N N 129.18 . 1 323 95 95 ALA H H 9.474 . 1 324 95 95 ALA CA C 50.160 . 1 325 95 95 ALA CB C 24.177 . 1 326 95 95 ALA N N 130.30 . 1 327 96 96 GLN H H 8.895 . 1 328 96 96 GLN CA C 54.348 . 1 329 96 96 GLN CB C 32.881 . 1 330 96 96 GLN N N 117.79 . 1 331 97 97 LYS H H 8.928 . 1 332 97 97 LYS CA C 57.934 . 1 333 97 97 LYS CB C 32.868 . 1 334 97 97 LYS N N 127.80 . 1 335 98 98 LYS H H 8.194 . 1 336 98 98 LYS CA C 55.624 . 1 337 98 98 LYS CB C 34.390 . 1 338 98 98 LYS N N 129.57 . 1 339 101 101 VAL H H 7.528 . 1 340 101 101 VAL CA C 65.026 . 1 341 101 101 VAL CB C 32.600 . 1 342 101 101 VAL N N 121.07 . 1 343 102 102 TYR H H 8.127 . 1 344 102 102 TYR CA C 60.228 . 1 345 102 102 TYR CB C 38.887 . 1 346 102 102 TYR N N 120.58 . 1 347 103 103 ARG H H 8.028 . 1 348 103 103 ARG CA C 57.968 . 1 349 103 103 ARG CB C 30.256 . 1 350 103 103 ARG N N 117.68 . 1 351 104 104 ARG H H 7.430 . 1 352 104 104 ARG CA C 57.810 . 1 353 104 104 ARG CB C 30.686 . 1 354 104 104 ARG N N 117.83 . 1 355 105 105 ILE H H 7.724 . 1 356 105 105 ILE CA C 63.117 . 1 357 105 105 ILE CB C 38.497 . 1 358 105 105 ILE N N 119.69 . 1 359 106 106 VAL H H 7.724 . 1 360 106 106 VAL CA C 63.651 . 1 361 106 106 VAL CB C 32.262 . 1 362 106 106 VAL N N 119.69 . 1 363 107 107 GLU H H 8.044 . 1 364 107 107 GLU CA C 57.424 . 1 365 107 107 GLU CB C 30.202 . 1 366 107 107 GLU N N 121.74 . 1 367 108 108 SER H H 7.925 . 1 368 108 108 SER CA C 59.023 . 1 369 108 108 SER CB C 64.294 . 1 370 108 108 SER N N 115.17 . 1 371 109 109 ASP H H 8.223 . 1 372 109 109 ASP CA C 54.659 . 1 373 109 109 ASP CB C 41.419 . 1 374 109 109 ASP N N 122.65 . 1 375 110 110 VAL H H 8.038 . 1 376 110 110 VAL CA C 62.756 . 1 377 110 110 VAL CB C 32.962 . 1 378 110 110 VAL N N 119.24 . 1 379 111 111 GLY H H 8.397 . 1 380 111 111 GLY CA C 45.635 . 1 381 111 111 GLY N N 111.77 . 1 382 112 112 ASP H H 8.274 . 1 383 112 112 ASP CA C 54.586 . 1 384 112 112 ASP CB C 41.789 . 1 385 112 112 ASP N N 121.13 . 1 386 113 113 SER H H 7.955 . 1 387 113 113 SER CA C 60.487 . 1 388 113 113 SER CB C 64.983 . 1 389 113 113 SER N N 121.16 . 1 stop_ save_ save_RDC_list_1 _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $sample_1 stop_ loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error DHN 10 ASP N 10 ASP H 0.1 ? ? . . . DHN 11 GLY N 11 GLY H -1.3 ? ? . . . DHN 12 ILE N 12 ILE H -1 ? ? . . . DHN 13 LEU N 13 LEU H -1.3 ? ? . . . DHN 14 ARG N 14 ARG H -3.1 ? ? . . . DHN 18 LYS N 18 LYS H -0.8 ? ? . . . DHN 19 LEU N 19 LEU H -1.9 ? ? . . . DHN 20 VAL N 20 VAL H -3.2 ? ? . . . DHN 21 LYS N 21 LYS H -3.3 ? ? . . . DHN 22 PHE N 22 PHE H -5.6 ? ? . . . DHN 23 ARG N 23 ARG H -5.3 ? ? . . . DHN 24 LYS N 24 LYS H -4.7 ? ? . . . DHN 25 GLY N 25 GLY H 5 ? ? . . . DHN 27 SER N 27 SER H -1.5 ? ? . . . DHN 30 LEU N 30 LEU H 1.7 ? ? . . . DHN 31 ARG N 31 ARG H 1.2 ? ? . . . DHN 32 LEU N 32 LEU H 4.2 ? ? . . . DHN 34 GLY N 34 GLY H 1.7 ? ? . . . DHN 35 GLY N 35 GLY H 2.2 ? ? . . . DHN 36 ASN N 36 ASN H 3.8 ? ? . . . DHN 37 ASP N 37 ASP H 0.4 ? ? . . . DHN 38 VAL N 38 VAL H 2.4 ? ? . . . DHN 39 GLY N 39 GLY H -0.2 ? ? . . . DHN 40 ILE N 40 ILE H 0.2 ? ? . . . DHN 41 PHE N 41 PHE H 2.6 ? ? . . . DHN 42 VAL N 42 VAL H 2.4 ? ? . . . DHN 43 ALA N 43 ALA H 3.3 ? ? . . . DHN 44 GLY N 44 GLY H -2.6 ? ? . . . DHN 45 VAL N 45 VAL H -1.3 ? ? . . . DHN 46 LEU N 46 LEU H -3.3 ? ? . . . DHN 47 GLU N 47 GLU H 1.8 ? ? . . . DHN 48 ASP N 48 ASP H -0.5 ? ? . . . DHN 49 SER N 49 SER H 5 ? ? . . . DHN 51 ALA N 51 ALA H 2.3 ? ? . . . DHN 52 ALA N 52 ALA H 2.3 ? ? . . . DHN 54 GLU N 54 GLU H 2.1 ? ? . . . DHN 55 GLY N 55 GLY H -3.9 ? ? . . . DHN 56 LEU N 56 LEU H 3 ? ? . . . DHN 57 GLU N 57 GLU H -6.2 ? ? . . . DHN 58 GLU N 58 GLU H 2.6 ? ? . . . DHN 59 GLY N 59 GLY H 2.8 ? ? . . . DHN 61 GLN N 61 GLN H 3.7 ? ? . . . DHN 62 ILE N 62 ILE H 1.9 ? ? . . . DHN 63 LEU N 63 LEU H -2.1 ? ? . . . DHN 65 VAL N 65 VAL H -5.9 ? ? . . . DHN 66 ASN N 66 ASN H -4.6 ? ? . . . DHN 68 VAL N 68 VAL H -7.3 ? ? . . . DHN 69 ASP N 69 ASP H -4.6 ? ? . . . DHN 70 PHE N 70 PHE H 0.9 ? ? . . . DHN 71 THR N 71 THR H 1.3 ? ? . . . DHN 72 ASN N 72 ASN H 3.5 ? ? . . . DHN 74 ILE N 74 ILE H 0.2 ? ? . . . DHN 75 ARG N 75 ARG H 3.9 ? ? . . . DHN 76 GLU N 76 GLU H 1.5 ? ? . . . DHN 77 GLU N 77 GLU H 2.9 ? ? . . . DHN 78 ALA N 78 ALA H 4.7 ? ? . . . DHN 79 VAL N 79 VAL H 2.4 ? ? . . . DHN 80 LEU N 80 LEU H -0.1 ? ? . . . DHN 81 PHE N 81 PHE H 4 ? ? . . . DHN 82 LEU N 82 LEU H 4.4 ? ? . . . DHN 84 ASP N 84 ASP H 1.3 ? ? . . . DHN 85 LEU N 85 LEU H 4.6 ? ? . . . DHN 87 LYS N 87 LYS H 2.7 ? ? . . . DHN 88 GLY N 88 GLY H 2.9 ? ? . . . DHN 89 GLU N 89 GLU H 2.1 ? ? . . . DHN 90 GLU N 90 GLU H 1.8 ? ? . . . DHN 91 VAL N 91 VAL H -7.1 ? ? . . . DHN 92 THR N 92 THR H -3.5 ? ? . . . DHN 93 ILE N 93 ILE H -4.3 ? ? . . . DHN 94 LEU N 94 LEU H -1.6 ? ? . . . DHN 95 ALA N 95 ALA H -0.1 ? ? . . . DHN 96 GLN N 96 GLN H 1.8 ? ? . . . DHN 97 LYS N 97 LYS H 2 ? ? . . . DHN 98 LYS N 98 LYS H 0 ? ? . . . DHN 99 LYS N 99 LYS H 2.2 ? ? . . . DHN 101 VAL N 101 VAL H 4.1 ? ? . . . DHN 102 TYR N 102 TYR H 3.4 ? ? . . . DHN 103 ARG N 103 ARG H 2.1 ? ? . . . DHN 107 GLU N 107 GLU H -1.7 ? ? . . . DHN 108 SER N 108 SER H 0.7 ? ? . . . DHN 109 ASP N 109 ASP H -0.7 ? ? . . . DHN 110 VAL N 110 VAL H -1.3 ? ? . . . DHN 111 GLY N 111 GLY H -0.2 ? ? . . . DHN 112 ASP N 112 ASP H -0.8 ? ? . . . DHN 113 SER N 113 SER H -0.1 ? ? . . . stop_ _Details 'in 5% PEG' _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 600.133 _Text_data_format . _Text_data . save_ save_RDC_list_2 _Saveframe_category residual_dipolar_couplings loop_ _Sample_label $sample_1 stop_ loop_ _Residual_dipolar_coupling_ID _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name _Residual_dipolar_coupling_value _Atom_one_mol_system_component_name _Atom_two_mol_system_component_name _Residual_dipolar_coupling_min_value _Residual_dipolar_coupling_max_value _Residual_dipolar_coupling_value_error DHN 10 ASP N 10 ASP H 0.7 ? ? . . . DHN 11 GLY N 11 GLY H -0.1 ? ? . . . DHN 12 ILE N 12 ILE H -1.2 ? ? . . . DHN 13 LEU N 13 LEU H -0.4 ? ? . . . DHN 14 ARG N 14 ARG H -2.6 ? ? . . . DHN 18 LYS N 18 LYS H 0.5 ? ? . . . DHN 19 LEU N 19 LEU H 0.4 ? ? . . . DHN 20 VAL N 20 VAL H 6.7 ? ? . . . DHN 21 LYS N 21 LYS H 5.8 ? ? . . . DHN 22 PHE N 22 PHE H 9.3 ? ? . . . DHN 23 ARG N 23 ARG H 9.3 ? ? . . . DHN 24 LYS N 24 LYS H 8.2 ? ? . . . DHN 25 GLY N 25 GLY H 3.3 ? ? . . . DHN 27 SER N 27 SER H 1.6 ? ? . . . DHN 30 LEU N 30 LEU H 3.2 ? ? . . . DHN 31 ARG N 31 ARG H -1.6 ? ? . . . DHN 32 LEU N 32 LEU H -10.6 ? ? . . . DHN 34 GLY N 34 GLY H -3.8 ? ? . . . DHN 35 GLY N 35 GLY H -11.9 ? ? . . . DHN 36 ASN N 36 ASN H -5 ? ? . . . DHN 37 ASP N 37 ASP H -3.7 ? ? . . . DHN 38 VAL N 38 VAL H -11.7 ? ? . . . DHN 39 GLY N 39 GLY H -3.7 ? ? . . . DHN 40 ILE N 40 ILE H -4.4 ? ? . . . DHN 41 PHE N 41 PHE H -8.8 ? ? . . . DHN 42 VAL N 42 VAL H -15.3 ? ? . . . DHN 43 ALA N 43 ALA H 0 ? ? . . . DHN 44 GLY N 44 GLY H 8.1 ? ? . . . DHN 45 VAL N 45 VAL H 8.6 ? ? . . . DHN 46 LEU N 46 LEU H 9.6 ? ? . . . DHN 47 GLU N 47 GLU H -3.9 ? ? . . . DHN 48 ASP N 48 ASP H -8.3 ? ? . . . DHN 49 SER N 49 SER H 2.9 ? ? . . . DHN 51 ALA N 51 ALA H -12.9 ? ? . . . DHN 52 ALA N 52 ALA H -13.5 ? ? . . . DHN 54 GLU N 54 GLU H -9.1 ? ? . . . DHN 55 GLY N 55 GLY H -7.2 ? ? . . . DHN 56 LEU N 56 LEU H -4.3 ? ? . . . DHN 57 GLU N 57 GLU H 0 ? ? . . . DHN 58 GLU N 58 GLU H 2.5 ? ? . . . DHN 59 GLY N 59 GLY H -7.4 ? ? . . . DHN 61 GLN N 61 GLN H -14.5 ? ? . . . DHN 62 ILE N 62 ILE H -4.6 ? ? . . . DHN 63 LEU N 63 LEU H 5.2 ? ? . . . DHN 65 VAL N 65 VAL H 10.9 ? ? . . . DHN 66 ASN N 66 ASN H 8.8 ? ? . . . DHN 68 VAL N 68 VAL H 6.7 ? ? . . . DHN 69 ASP N 69 ASP H 10.2 ? ? . . . DHN 70 PHE N 70 PHE H -6.4 ? ? . . . DHN 71 THR N 71 THR H 2.9 ? ? . . . DHN 72 ASN N 72 ASN H 4.8 ? ? . . . DHN 74 ILE N 74 ILE H 7 ? ? . . . DHN 75 ARG N 75 ARG H 3.9 ? ? . . . DHN 76 GLU N 76 GLU H 5.1 ? ? . . . DHN 77 GLU N 77 GLU H -2.4 ? ? . . . DHN 78 ALA N 78 ALA H 4.3 ? ? . . . DHN 79 VAL N 79 VAL H 5 ? ? . . . DHN 80 LEU N 80 LEU H 4.8 ? ? . . . DHN 81 PHE N 81 PHE H 1.9 ? ? . . . DHN 82 LEU N 82 LEU H 4.3 ? ? . . . DHN 84 ASP N 84 ASP H 1.2 ? ? . . . DHN 85 LEU N 85 LEU H 5.4 ? ? . . . DHN 87 LYS N 87 LYS H -9.3 ? ? . . . DHN 88 GLY N 88 GLY H 7.5 ? ? . . . DHN 89 GLU N 89 GLU H -3.6 ? ? . . . DHN 90 GLU N 90 GLU H 6.5 ? ? . . . DHN 91 VAL N 91 VAL H 10.5 ? ? . . . DHN 92 THR N 92 THR H 7.5 ? ? . . . DHN 93 ILE N 93 ILE H 7.3 ? ? . . . DHN 94 LEU N 94 LEU H 1.3 ? ? . . . DHN 95 ALA N 95 ALA H -0.9 ? ? . . . DHN 96 GLN N 96 GLN H -8.9 ? ? . . . DHN 97 LYS N 97 LYS H -8.3 ? ? . . . DHN 98 LYS N 98 LYS H -12 ? ? . . . DHN 99 LYS N 99 LYS H -3.3 ? ? . . . DHN 101 VAL N 101 VAL H 1.6 ? ? . . . DHN 102 TYR N 102 TYR H -1.7 ? ? . . . DHN 103 ARG N 103 ARG H -9.2 ? ? . . . DHN 107 GLU N 107 GLU H -4.7 ? ? . . . DHN 108 SER N 108 SER H 1.1 ? ? . . . DHN 109 ASP N 109 ASP H -0.2 ? ? . . . DHN 110 VAL N 110 VAL H -0.9 ? ? . . . DHN 111 GLY N 111 GLY H -0.1 ? ? . . . DHN 112 ASP N 112 ASP H -0.5 ? ? . . . DHN 113 SER N 113 SER H -0.3 ? ? . . . stop_ _Details 'in Pf1 phage' _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 600.133 _Text_data_format . _Text_data . save_