data_6758 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignment of the E.coli cytolethal distending toxin CdtB-II subunit ; _BMRB_accession_number 6758 _BMRB_flat_file_name bmr6758.str _Entry_type original _Submission_date 2005-08-02 _Accession_date 2005-08-02 _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 Villar-Lecumberri M. T. . 2 Potter B. M. . 3 Wang Zhonghua . . 4 Dreyfus L. A. . 5 Laity J. H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 T1_relaxation 1 T1rho_relaxation 1 T2_relaxation 1 heteronucl_NOE 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 204 "13C chemical shifts" 614 "15N chemical shifts" 200 "T1 relaxation values" 178 "T2 relaxation values" 180 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-02-07 update BMRB 'complete entry citation' 2006-03-10 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR Assignment of the E. coli-II Cytolethal Distending Toxin CdtB Subunit' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16456702 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Villar-Lecumberri Maria T. . 2 Potter Belinda M. . 3 Wang Zhonghua . . 4 Dreyfus Lawrence A. . 5 Laity John H. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 36 _Journal_issue 'Suppl. 5' _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 14 _Page_last 14 _Year 2006 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full . _Citation_title ; Cloning, sequencing and expression of the Escherichia Coli cytolethal distending toxin genes. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8112838 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pickett C. L. . 2 Cottle D. L. . 3 Pesci E. C. . 4 Bikah G. . . stop_ _Journal_abbreviation 'Infec. Immun.' _Journal_name_full . _Journal_volume 62 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1046 _Page_last 1051 _Year 1994 _Details . save_ save_reference_2 _Saveframe_category citation _Citation_full . _Citation_title ; DNase I homologous residues in CdtB are critical for cytolethal distending toxin-mediated cell cycle arrest ; _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 Elwell C. A. . 2 Dreyfus L. A. . stop_ _Journal_abbreviation 'Mol. Micro.' _Journal_name_full . _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 952 _Page_last 963 _Year 2000 _Details . save_ save_reference_3 _Saveframe_category citation _Citation_full . _Citation_title 'Escherichia coli CdtB mediates cytolethal distending toxin cell cycle arrest.' _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 Elwell C. . . 2 Chao K. L. . 3 Patel K. . . 4 Dreyfus L. A. . stop_ _Journal_abbreviation 'Infec. Immun.' _Journal_name_full . _Journal_volume 69 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 3418 _Page_last 3422 _Year 2001 _Details . save_ save_reference_4 _Saveframe_category citation _Citation_full . _Citation_title 'Assembly and function of a bacterial genotoxin.' _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 Nesic D. . . 2 Hsu Y. . . 3 Stebbins C. E. . stop_ _Journal_abbreviation Nature _Journal_name_full . _Journal_volume 429 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 429 _Page_last 433 _Year 2004 _Details . save_ save_reference_5 _Saveframe_category citation _Citation_full . _Citation_title 'Nuclear localization of the Escherichia coli cytolethal distending toxin CdtB subunit.' _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 McSweeney L. A. . 2 Dreyfus L. A. . stop_ _Journal_abbreviation 'Cell Micro' _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 447 _Page_last 458 _Year 2004 _Details . save_ save_reference_6 _Saveframe_category citation _Citation_full . _Citation_title 'NMRView: A computer program for the visualization and analysis of NMR data.' _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 Johnson B. A. . 2 Blevins R. A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 4 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 603 _Page_last 614 _Year 1994 _Details . save_ save_reference_7 _Saveframe_category citation _Citation_full . _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _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 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details . save_ save_reference_8 _Saveframe_category citation _Citation_full . _Citation_title 'Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer' _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 Farrow N. A. . 2 Zhang O. . . 3 Forman-Kay J. D. . 4 Kay L. E. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full . _Journal_volume 34 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 868 _Page_last 878 _Year 1995 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name EcCdtB-II _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EcCdtB-II $EcCdtB-II stop_ _System_molecular_weight 28735.3 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Catalytic subunit of EcCDT-II' stop_ _Database_query_date . _Details ; Molecular mass refers to the recombinant protein including a His-tag. Mature protein has a molecular weight of 27452.9 Da. ; save_ ######################## # Monomeric polymers # ######################## save_EcCdtB-II _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common EcCdtB-II _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 262 _Mol_residue_sequence ; MAHHHHHHVGTDLTDFRVAT WNLQGASATTESKWNINVRQ LISGENAVDILAVQEAGSPP STAVDTGRVIPSPGIPVREL IWNLSTNSRPQQVYIYFSAV DALGGRVNLALVSNRRADEV FVLSPVRQGGRPLLGIRIGN DAFFTAHAIAMRNNDAPALV EEVYNFFRDSRDPVHQALNW MILGDFNREPADLEMNLTVP VRRASEIISPAAATQTSQRT LDYAVAGNSVAFRPSPLQAG IVYGARRTQISSDHFPVGVS RR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -11 MET 2 -10 ALA 3 -9 HIS 4 -8 HIS 5 -7 HIS 6 -6 HIS 7 -5 HIS 8 -4 HIS 9 -3 VAL 10 -2 GLY 11 -1 THR 12 1 ASP 13 2 LEU 14 3 THR 15 4 ASP 16 5 PHE 17 6 ARG 18 7 VAL 19 8 ALA 20 9 THR 21 10 TRP 22 11 ASN 23 12 LEU 24 13 GLN 25 14 GLY 26 15 ALA 27 16 SER 28 17 ALA 29 18 THR 30 19 THR 31 20 GLU 32 21 SER 33 22 LYS 34 23 TRP 35 24 ASN 36 25 ILE 37 26 ASN 38 27 VAL 39 28 ARG 40 29 GLN 41 30 LEU 42 31 ILE 43 32 SER 44 33 GLY 45 34 GLU 46 35 ASN 47 36 ALA 48 37 VAL 49 38 ASP 50 39 ILE 51 40 LEU 52 41 ALA 53 42 VAL 54 43 GLN 55 44 GLU 56 45 ALA 57 46 GLY 58 47 SER 59 48 PRO 60 49 PRO 61 50 SER 62 51 THR 63 52 ALA 64 53 VAL 65 54 ASP 66 55 THR 67 56 GLY 68 57 ARG 69 58 VAL 70 59 ILE 71 60 PRO 72 61 SER 73 62 PRO 74 63 GLY 75 64 ILE 76 65 PRO 77 66 VAL 78 67 ARG 79 68 GLU 80 69 LEU 81 70 ILE 82 71 TRP 83 72 ASN 84 73 LEU 85 74 SER 86 75 THR 87 76 ASN 88 77 SER 89 78 ARG 90 79 PRO 91 80 GLN 92 81 GLN 93 82 VAL 94 83 TYR 95 84 ILE 96 85 TYR 97 86 PHE 98 87 SER 99 88 ALA 100 89 VAL 101 90 ASP 102 91 ALA 103 92 LEU 104 93 GLY 105 94 GLY 106 95 ARG 107 96 VAL 108 97 ASN 109 98 LEU 110 99 ALA 111 100 LEU 112 101 VAL 113 102 SER 114 103 ASN 115 104 ARG 116 105 ARG 117 106 ALA 118 107 ASP 119 108 GLU 120 109 VAL 121 110 PHE 122 111 VAL 123 112 LEU 124 113 SER 125 114 PRO 126 115 VAL 127 116 ARG 128 117 GLN 129 118 GLY 130 119 GLY 131 120 ARG 132 121 PRO 133 122 LEU 134 123 LEU 135 124 GLY 136 125 ILE 137 126 ARG 138 127 ILE 139 128 GLY 140 129 ASN 141 130 ASP 142 131 ALA 143 132 PHE 144 133 PHE 145 134 THR 146 135 ALA 147 136 HIS 148 137 ALA 149 138 ILE 150 139 ALA 151 140 MET 152 141 ARG 153 142 ASN 154 143 ASN 155 144 ASP 156 145 ALA 157 146 PRO 158 147 ALA 159 148 LEU 160 149 VAL 161 150 GLU 162 151 GLU 163 152 VAL 164 153 TYR 165 154 ASN 166 155 PHE 167 156 PHE 168 157 ARG 169 158 ASP 170 159 SER 171 160 ARG 172 161 ASP 173 162 PRO 174 163 VAL 175 164 HIS 176 165 GLN 177 166 ALA 178 167 LEU 179 168 ASN 180 169 TRP 181 170 MET 182 171 ILE 183 172 LEU 184 173 GLY 185 174 ASP 186 175 PHE 187 176 ASN 188 177 ARG 189 178 GLU 190 179 PRO 191 180 ALA 192 181 ASP 193 182 LEU 194 183 GLU 195 184 MET 196 185 ASN 197 186 LEU 198 187 THR 199 188 VAL 200 189 PRO 201 190 VAL 202 191 ARG 203 192 ARG 204 193 ALA 205 194 SER 206 195 GLU 207 196 ILE 208 197 ILE 209 198 SER 210 199 PRO 211 200 ALA 212 201 ALA 213 202 ALA 214 203 THR 215 204 GLN 216 205 THR 217 206 SER 218 207 GLN 219 208 ARG 220 209 THR 221 210 LEU 222 211 ASP 223 212 TYR 224 213 ALA 225 214 VAL 226 215 ALA 227 216 GLY 228 217 ASN 229 218 SER 230 219 VAL 231 220 ALA 232 221 PHE 233 222 ARG 234 223 PRO 235 224 SER 236 225 PRO 237 226 LEU 238 227 GLN 239 228 ALA 240 229 GLY 241 230 ILE 242 231 VAL 243 232 TYR 244 233 GLY 245 234 ALA 246 235 ARG 247 236 ARG 248 237 THR 249 238 GLN 250 239 ILE 251 240 SER 252 241 SER 253 242 ASP 254 243 HIS 255 244 PHE 256 245 PRO 257 246 VAL 258 247 GLY 259 248 VAL 260 249 SER 261 250 ARG 262 251 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 2F1N "Structure Of Cdtb, The Biologically Active Subunit Of Cytolethal Distending Toxin" 100.00 262 100.00 100.00 0.00e+00 DBJ BAH72965 "cytolethal distending toxin B [Escherichia coli]" 97.33 269 97.65 98.04 1.09e-178 DBJ BAL47193 "cytolethal distending toxin B subunit, partial [Escherichia albertii]" 53.05 139 99.28 99.28 2.02e-91 DBJ BAL47198 "cytolethal distending toxin B subunit, partial [Escherichia albertii]" 53.05 139 100.00 100.00 4.08e-92 DBJ BAL47199 "cytolethal distending toxin B subunit, partial [Escherichia albertii]" 53.05 139 100.00 100.00 4.08e-92 DBJ BAL47200 "cytolethal distending toxin B subunit, partial [Escherichia albertii]" 53.05 139 97.84 97.84 1.89e-89 GB AAA18786 "CdtB [Escherichia coli]" 97.33 269 97.65 98.43 1.31e-178 GB ACH53455 "cytolethal distending toxin B subunit [Escherichia albertii]" 51.15 134 100.00 100.00 5.32e-89 GB ACH53456 "cytolethal distending toxin B subunit, partial [Escherichia albertii]" 51.15 134 100.00 100.00 5.32e-89 GB ACH53457 "cytolethal distending toxin B subunit [Escherichia albertii]" 51.15 134 99.25 99.25 3.38e-88 GB ADD59823 "cytolethal distending toxin subunit B [Escherichia albertii]" 56.87 149 98.66 99.33 1.99e-98 SP Q46669 "RecName: Full=Cytolethal distending toxin subunit B; Short=CDT B; AltName: Full=Deoxyribonuclease CdtB; Flags: Precursor [Esche" 97.33 269 97.65 98.43 1.31e-178 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EcCdtB-II E.coli 562 Eubacteria . Escherichia coli 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 $EcCdtB-II 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '20 mM sodium phosphate,50 mM NaCl, 0.02% Na3N, 0.2 mM DSS, 5% D2O, ~0.4mM rEcCdtB-II' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $EcCdtB-II . mM 0.3 0.5 '[U-13C; U-15N; U-2H]' 'Sodium phosphate' 20 mM . . . 'Sodium Chloride' 50 mM . . . DSS 0.2 mM . . . D2O 5 '% (v/v)' . . . 'Sodium azide' 0.02 '% (w/v)' . . . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task 'Data analysis' stop_ _Details . _Citation_label $reference_6 save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version 97.027.12.56 loop_ _Task 'Raw spectral data processing' stop_ _Details . _Citation_label $reference_7 save_ save_software_3 _Saveframe_category software _Name CurveFit _Version 1.30 loop_ _Task 'Used to calculate RelaxT times' stop_ _Details 'Generously provided by A.G. Palmer, III, Columbia University, New York, NY' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_14.1_T_Varian_Inova_600_Mhz _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details 'triple resonance {1H, 15N, 13C} cryogenically cooled probe (cryoprobe)' 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_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_HNCA _Sample_label $sample_1 save_ save_3D_(HCA)CO(CA)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_(HCA)CO(CA)NH _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_HNCO _Sample_label $sample_1 save_ save_2D_15N-{1H}-HNOE_7 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_15N-{1H}-HNOE _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_(T1_flag)_8 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-15N_HSQC_(T1_flag) _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_(T2_flag)_9 _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-15N_HSQC_(T2_flag) _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name 2D_1H-15N_HSQC _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_3D_HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name 3D_HNCACB _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_3D_CBCA(CO)NH _Saveframe_category NMR_applied_experiment _Experiment_name 3D_CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_3D_HNCA _Saveframe_category NMR_applied_experiment _Experiment_name 3D_HNCA _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_3D_(HCA)CO(CA)NH _Saveframe_category NMR_applied_experiment _Experiment_name 3D_(HCA)CO(CA)NH _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_3D_HNCO _Saveframe_category NMR_applied_experiment _Experiment_name 3D_HNCO _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_2D_15N-{1H}-HNOE _Saveframe_category NMR_applied_experiment _Experiment_name '2D 15N-{1H}-HNOE' _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_2D_1H-15N_HSQC_(T1_flag) _Saveframe_category NMR_applied_experiment _Experiment_name '2D_1H-15N_HSQC (T1 flag)' _BMRB_pulse_sequence_accession_number . _Details BioPack save_ save_2D_1H-15N_HSQC_(T2_flag) _Saveframe_category NMR_applied_experiment _Experiment_name '2D_1H-15N_HSQC (T2 flag)' _BMRB_pulse_sequence_accession_number . _Details BioPack save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 pH temperature 310 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.0 . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 $software_2 stop_ loop_ _Experiment_label 2D_1H-15N_HSQC 3D_HNCACB 3D_CBCA(CO)NH 3D_HNCA 3D_(HCA)CO(CA)NH 3D_HNCO stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name EcCdtB-II _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 12 ASP H H 8.32 0.015 1 2 1 12 ASP C C 177.857 0.08 1 3 1 12 ASP CA C 54.12 0.31 1 4 1 12 ASP CB C 42.2 0.31 1 5 1 12 ASP N N 122.67 0.14 1 6 2 13 LEU H H 8.48 0.015 1 7 2 13 LEU C C 176.89 0.08 1 8 2 13 LEU CA C 56.96 0.31 1 9 2 13 LEU CB C 41.93 0.31 1 10 2 13 LEU N N 122.39 0.14 1 11 4 15 ASP CA C 55.06 0.31 1 12 4 15 ASP CB C 41.32 0.31 1 13 5 16 PHE H H 7.52 0.015 1 14 5 16 PHE C C 175.574 0.08 1 15 5 16 PHE CA C 57.5 0.31 1 16 5 16 PHE CB C 41.96 0.31 1 17 5 16 PHE N N 117.72 0.14 1 18 6 17 ARG H H 9.56 0.015 1 19 6 17 ARG C C 175.958 0.08 1 20 6 17 ARG CA C 56.08 0.31 1 21 6 17 ARG CB C 31.68 0.31 1 22 6 17 ARG N N 125.92 0.14 1 23 7 18 VAL H H 8.38 0.015 1 24 7 18 VAL C C 174.86 0.08 1 25 7 18 VAL CA C 58.88 0.31 1 26 7 18 VAL CB C 35.14 0.31 1 27 8 19 ALA H H 8.59 0.015 1 28 8 19 ALA C C 174.999 0.08 1 29 8 19 ALA CA C 51.66 0.31 1 30 8 19 ALA CB C 23.38 0.31 1 31 8 19 ALA N N 122.1 0.14 1 32 9 20 THR H H 8.84 0.015 1 33 9 20 THR C C 171.647 0.08 1 34 9 20 THR CA C 58.46 0.31 1 35 9 20 THR CB C 70.32 0.31 1 36 9 20 THR N N 116.02 0.14 1 37 10 21 TRP H H 9 0.015 1 38 10 21 TRP C C 175.879 0.08 1 39 10 21 TRP CA C 55.13 0.31 1 40 10 21 TRP CB C 33.06 0.31 1 41 10 21 TRP N N 129.17 0.14 1 42 11 22 ASN H H 8.25 0.015 9 43 11 22 ASN C C 174.936 0.08 9 44 11 22 ASN CA C 53.57 0.31 9 45 11 22 ASN CB C 38.87 0.31 9 46 11 22 ASN N N 119.84 0.14 9 47 12 23 LEU H H 8 0.015 9 48 12 23 LEU CA C 55.53 0.31 9 49 12 23 LEU CB C 42.24 0.31 9 50 12 23 LEU N N 122.81 0.14 9 51 13 24 GLN C C 176.679 0.08 9 52 13 24 GLN CA C 57.81 0.31 9 53 13 24 GLN CB C 27.83 0.31 9 54 14 25 GLY H H 8.62 0.015 9 55 14 25 GLY CA C 45.06 0.31 9 56 14 25 GLY N N 116.17 0.14 9 57 15 26 ALA C C 172.57 0.08 1 58 15 26 ALA CA C 51.2 0.31 1 59 15 26 ALA CB C 21.4 0.31 1 60 16 27 SER H H 6.54 0.015 1 61 16 27 SER CA C 57.4 0.31 1 62 16 27 SER CB C 68.55 0.31 1 63 17 28 ALA CA C 52.25 0.31 1 64 17 28 ALA CB C 21.05 0.31 1 65 18 29 THR H H 8.02 0.015 1 66 18 29 THR CA C 61.37 0.31 1 67 18 29 THR CB C 70.49 0.31 1 68 18 29 THR N N 110.65 0.14 1 69 19 30 THR C C 175.76 0.08 9 70 19 30 THR CA C 62.05 0.31 9 71 19 30 THR CB C 69.68 0.31 9 72 20 31 GLU H H 7.84 0.015 9 73 20 31 GLU CA C 51.91 0.31 9 74 20 31 GLU CB C 32.63 0.31 9 75 20 31 GLU N N 124 0.14 9 76 23 34 TRP C C 176.271 0.08 1 77 23 34 TRP CA C 56.82 0.31 1 78 23 34 TRP CB C 29.76 0.31 1 79 23 34 TRP N N 116.17 0.14 1 80 24 35 ASN H H 8.19 0.015 1 81 24 35 ASN C C 174.526 0.08 1 82 24 35 ASN CA C 53.57 0.31 1 83 24 35 ASN CB C 38.89 0.31 1 84 24 35 ASN N N 119.42 0.14 1 85 25 36 ILE H H 7.83 0.015 1 86 25 36 ILE C C 175.495 0.08 1 87 25 36 ILE CA C 58.24 0.31 1 88 25 36 ILE CB C 38.82 0.31 1 89 25 36 ILE N N 121.54 0.14 1 90 29 40 GLN C C 177.141 0.08 9 91 29 40 GLN CA C 58.43 0.31 9 92 29 40 GLN CB C 28.3 0.31 9 93 29 40 GLN N N 116.17 0.14 9 94 30 41 LEU H H 7.52 0.015 1 95 30 41 LEU C C 177.869 0.08 1 96 30 41 LEU CA C 56.78 0.31 1 97 30 41 LEU CB C 43.23 0.31 1 98 30 41 LEU N N 118.43 0.14 1 99 31 42 ILE H H 7.36 0.015 1 100 31 42 ILE C C 173.996 0.08 1 101 31 42 ILE CA C 59.96 0.31 1 102 31 42 ILE CB C 39.05 0.31 1 103 31 42 ILE N N 109.66 0.14 1 104 32 43 SER H H 7.36 0.015 1 105 32 43 SER C C 173.307 0.08 1 106 32 43 SER CA C 57.36 0.31 1 107 32 43 SER CB C 66.49 0.31 1 108 32 43 SER N N 114.04 0.14 1 109 33 44 GLY H H 8.24 0.015 1 110 33 44 GLY C C 174.811 0.08 1 111 33 44 GLY CA C 44.45 0.31 1 112 33 44 GLY N N 108.81 0.14 1 113 34 45 GLU H H 8.5 0.015 1 114 34 45 GLU C C 176.257 0.08 1 115 34 45 GLU CA C 58.34 0.31 1 116 34 45 GLU CB C 29.61 0.31 1 117 34 45 GLU N N 120.41 0.14 1 118 35 46 ASN H H 8.63 0.015 1 119 35 46 ASN CA C 52.82 0.31 1 120 35 46 ASN CB C 38.28 0.31 1 121 35 46 ASN N N 118.57 0.14 1 122 36 47 ALA H H 6.93 0.015 1 123 36 47 ALA C C 179.077 0.08 1 124 36 47 ALA CA C 52.82 0.31 1 125 36 47 ALA CB C 19.6 0.31 1 126 36 47 ALA N N 121.4 0.14 1 127 37 48 VAL H H 7.84 0.015 1 128 37 48 VAL C C 177.618 0.08 1 129 37 48 VAL CA C 60.49 0.31 1 130 37 48 VAL CB C 29.43 0.31 1 131 37 48 VAL N N 117.16 0.14 1 132 38 49 ASP H H 8.39 0.015 1 133 38 49 ASP C C 175.482 0.08 1 134 38 49 ASP CA C 56.51 0.31 1 135 38 49 ASP CB C 39.43 0.31 1 136 38 49 ASP N N 114.89 0.14 1 137 39 50 ILE H H 8.51 0.015 1 138 39 50 ILE C C 177.17 0.08 1 139 39 50 ILE CA C 62.66 0.31 1 140 39 50 ILE CB C 37.62 0.31 1 141 39 50 ILE N N 117.75 0.14 1 142 40 51 LEU H H 7.43 0.015 1 143 40 51 LEU C C 175.492 0.08 1 144 40 51 LEU CA C 58.24 0.31 1 145 40 51 LEU CB C 38.52 0.31 1 146 40 51 LEU N N 117.3 0.14 1 147 41 52 ALA H H 7.88 0.015 1 148 41 52 ALA CA C 52.57 0.31 1 149 41 52 ALA CB C 19.33 0.31 1 150 41 52 ALA N N 125.41 0.14 1 151 42 53 VAL H H 7.95 0.015 1 152 42 53 VAL CA C 61.08 0.31 1 153 42 53 VAL CB C 32.13 0.31 1 154 42 53 VAL N N 116.02 0.14 1 155 43 54 GLN CA C 58.6 0.31 1 156 43 54 GLN CB C 30.19 0.31 1 157 44 55 GLU H H 7.5 0.015 1 158 44 55 GLU C C 175.944 0.08 1 159 44 55 GLU CA C 57.22 0.31 1 160 44 55 GLU CB C 30.19 0.31 1 161 44 55 GLU N N 114.04 0.14 1 162 45 56 ALA H H 7 0.015 1 163 45 56 ALA CA C 51.24 0.31 1 164 45 56 ALA CB C 21.31 0.31 1 165 45 56 ALA N N 124.08 0.14 1 166 50 61 SER C C 175.328 0.08 1 167 50 61 SER CA C 61.34 0.31 1 168 50 61 SER CB C 62.31 0.31 1 169 51 62 THR H H 7.14 0.015 1 170 51 62 THR C C 175.485 0.08 1 171 51 62 THR CA C 61.34 0.31 1 172 51 62 THR CB C 68.85 0.31 1 173 51 62 THR N N 107.82 0.14 1 174 52 63 ALA H H 7.11 0.015 1 175 52 63 ALA C C 176.187 0.08 1 176 52 63 ALA CA C 51.9 0.31 1 177 52 63 ALA CB C 19.1 0.31 1 178 52 63 ALA N N 126.35 0.14 1 179 53 64 VAL H H 8.38 0.015 1 180 53 64 VAL C C 175.167 0.08 1 181 53 64 VAL CA C 60.82 0.31 1 182 53 64 VAL CB C 34.81 0.31 1 183 53 64 VAL N N 121.26 0.14 1 184 54 65 ASP H H 8.47 0.015 1 185 54 65 ASP C C 177.998 0.08 1 186 54 65 ASP CA C 54.7 0.31 1 187 54 65 ASP CB C 41.82 0.31 1 188 54 65 ASP N N 128.18 0.14 1 189 55 66 THR H H 8.95 0.015 1 190 55 66 THR C C 177.662 0.08 1 191 55 66 THR CA C 62.83 0.31 1 192 55 66 THR CB C 69.79 0.31 1 193 55 66 THR N N 118.71 0.14 1 194 56 67 GLY H H 9.57 0.015 1 195 56 67 GLY C C 174.268 0.08 1 196 56 67 GLY CA C 44.94 0.31 1 197 56 67 GLY N N 112.49 0.14 1 198 57 68 ARG H H 7.77 0.015 1 199 57 68 ARG C C 176 0.08 1 200 57 68 ARG CA C 57.69 0.31 1 201 57 68 ARG CB C 31.52 0.31 1 202 57 68 ARG N N 123.8 0.14 1 203 58 69 VAL H H 8.74 0.015 1 204 58 69 VAL C C 175.952 0.08 1 205 58 69 VAL CA C 63.11 0.31 1 206 58 69 VAL CB C 31.55 0.31 1 207 58 69 VAL N N 130.45 0.14 1 208 59 70 ILE H H 8.7 0.015 1 209 59 70 ILE CA C 58.13 0.31 1 210 59 70 ILE CB C 39.82 0.31 1 211 60 71 PRO C C 176.104 0.08 5 212 60 71 PRO CA C 63.06 0.31 5 213 60 71 PRO CB C 31.39 0.31 5 214 61 72 SER H H 8.1 0.015 5 215 61 72 SER CA C 55.29 0.31 5 216 61 72 SER CB C 64.17 0.31 5 217 61 72 SER N N 117.86 0.14 5 218 62 73 PRO C C 176.896 0.08 1 219 62 73 PRO CA C 62.41 0.31 1 220 62 73 PRO CB C 28.49 0.31 1 221 63 74 GLY H H 8.13 0.015 1 222 63 74 GLY C C 173.693 0.08 1 223 63 74 GLY CA C 46.16 0.31 1 224 63 74 GLY N N 110.09 0.14 1 225 64 75 ILE H H 6.79 0.015 1 226 64 75 ILE CA C 57.97 0.31 1 227 64 75 ILE CB C 40.07 0.31 1 228 64 75 ILE N N 119.56 0.14 1 229 66 77 VAL C C 174.008 0.08 9 230 66 77 VAL CA C 60.7 0.31 9 231 66 77 VAL CB C 34.41 0.31 9 232 67 78 ARG H H 8.32 0.015 1 233 67 78 ARG C C 174.389 0.08 1 234 67 78 ARG CA C 53.45 0.31 1 235 67 78 ARG CB C 33.84 0.31 1 236 67 78 ARG N N 124.51 0.14 1 237 68 79 GLU H H 9.23 0.015 1 238 68 79 GLU C C 173.394 0.08 1 239 68 79 GLU CA C 54.74 0.31 1 240 68 79 GLU CB C 32.92 0.31 1 241 68 79 GLU N N 123.94 0.14 1 242 69 80 LEU H H 9.28 0.015 1 243 69 80 LEU C C 175.748 0.08 1 244 69 80 LEU CA C 52.93 0.31 1 245 69 80 LEU CB C 45.07 0.31 1 246 69 80 LEU N N 125.748 0.14 1 247 70 81 ILE H H 8.92 0.015 1 248 70 81 ILE C C 174.584 0.08 1 249 70 81 ILE CA C 59.65 0.31 1 250 70 81 ILE CB C 40.55 0.31 1 251 70 81 ILE N N 120.27 0.14 1 252 71 82 TRP H H 9.05 0.015 1 253 71 82 TRP C C 173.611 0.08 1 254 71 82 TRP CA C 52.99 0.31 1 255 71 82 TRP CB C 32.31 0.31 1 256 71 82 TRP N N 131.58 0.14 1 257 72 83 ASN H H 8.6 0.015 1 258 72 83 ASN C C 174.306 0.08 1 259 72 83 ASN CA C 53.93 0.31 1 260 72 83 ASN CB C 38.95 0.31 1 261 72 83 ASN N N 127.05 0.14 1 262 73 84 LEU H H 8.21 0.015 1 263 73 84 LEU C C 176.619 0.08 1 264 73 84 LEU CA C 55.15 0.31 1 265 73 84 LEU CB C 41.18 0.31 1 266 73 84 LEU N N 126.63 0.14 1 267 74 85 SER H H 7.68 0.015 1 268 74 85 SER C C 174.355 0.08 1 269 74 85 SER CA C 58.44 0.31 1 270 74 85 SER CB C 64.06 0.31 1 271 74 85 SER N N 113.48 0.14 1 272 75 86 THR H H 8.1 0.015 1 273 75 86 THR C C 175.602 0.08 1 274 75 86 THR CA C 63.05 0.31 1 275 75 86 THR CB C 69.13 0.31 1 276 75 86 THR N N 113.34 0.14 1 277 76 87 ASN H H 7.8 0.015 1 278 77 88 SER CA C 59.58 0.31 5 279 77 88 SER CB C 63.29 0.31 5 280 78 89 ARG H H 7.72 0.015 5 281 78 89 ARG CA C 53.59 0.31 5 282 78 89 ARG CB C 30.36 0.31 5 283 78 89 ARG N N 123.66 0.14 5 284 79 90 PRO C C 176.624 0.08 9 285 80 91 GLN H H 8.11 0.015 1 286 80 91 GLN C C 173.618 0.08 1 287 80 91 GLN CA C 55.61 0.31 1 288 80 91 GLN CB C 30.46 0.31 1 289 80 91 GLN N N 123.94 0.14 1 290 81 92 GLN H H 8.48 0.015 1 291 81 92 GLN C C 174.535 0.08 1 292 81 92 GLN CA C 55.27 0.31 1 293 81 92 GLN CB C 30.5 0.31 1 294 81 92 GLN N N 123.94 0.14 1 295 84 95 ILE C C 175.729 0.08 9 296 84 95 ILE CA C 61.57 0.31 9 297 84 95 ILE CB C 38.06 0.31 9 298 85 96 TYR H H 9.16 0.015 9 299 85 96 TYR CA C 60 0.31 9 300 85 96 TYR CB C 38.04 0.31 9 301 85 96 TYR N N 132.24 0.14 9 302 88 99 ALA C C 178.719 0.08 9 303 88 99 ALA CA C 52.66 0.31 9 304 88 99 ALA CB C 19.48 0.31 9 305 89 100 VAL H H 8.02 0.015 1 306 89 100 VAL C C 174.536 0.08 1 307 89 100 VAL CA C 60.77 0.31 1 308 89 100 VAL CB C 32.12 0.31 1 309 89 100 VAL N N 116.17 0.14 1 310 90 101 ASP H H 8.88 0.015 1 311 90 101 ASP CA C 57.35 0.31 1 312 90 101 ASP CB C 44.05 0.31 1 313 90 101 ASP N N 121.96 0.14 1 314 91 102 ALA C C 178.314 0.08 1 315 91 102 ALA CA C 54.32 0.31 1 316 91 102 ALA CB C 18.73 0.31 1 317 92 103 LEU H H 8.19 0.015 1 318 92 103 LEU C C 177.985 0.08 1 319 92 103 LEU CA C 54.42 0.31 1 320 92 103 LEU CB C 41.9 0.31 1 321 92 103 LEU N N 118.29 0.14 1 322 93 104 GLY H H 7.82 0.015 1 323 93 104 GLY C C 174.787 0.08 1 324 93 104 GLY CA C 45.38 0.31 1 325 93 104 GLY N N 108.95 0.14 1 326 94 105 GLY H H 7.87 0.015 1 327 94 105 GLY C C 174.253 0.08 1 328 94 105 GLY CA C 45 0.31 1 329 94 105 GLY N N 107.54 0.14 1 330 95 106 ARG C C 175.99 0.08 1 331 95 106 ARG CA C 57.65 0.31 1 332 95 106 ARG CB C 31.64 0.31 1 333 95 106 ARG N N 123.8 0.14 1 334 96 107 VAL H H 8.58 0.015 1 335 96 107 VAL N N 129.88 0.14 1 336 97 108 ASN C C 173.529 0.08 9 337 98 109 LEU H H 9.3 0.015 9 338 98 109 LEU C C 175.193 0.08 9 339 98 109 LEU CA C 52.41 0.31 9 340 98 109 LEU CB C 46.07 0.31 9 341 98 109 LEU N N 127.19 0.14 9 342 99 110 ALA H H 8.11 0.015 1 343 99 110 ALA C C 175.721 0.08 1 344 99 110 ALA CA C 50.74 0.31 1 345 99 110 ALA CB C 23.43 0.31 1 346 99 110 ALA N N 117.86 0.14 1 347 100 111 LEU H H 8.89 0.015 1 348 100 111 LEU C C 174.944 0.08 1 349 100 111 LEU CA C 54.78 0.31 1 350 100 111 LEU CB C 47.39 0.31 1 351 100 111 LEU N N 121.11 0.14 1 352 101 112 VAL H H 9.53 0.015 1 353 101 112 VAL C C 174.916 0.08 1 354 101 112 VAL CA C 60.61 0.31 1 355 101 112 VAL CB C 33.3 0.31 1 356 101 112 VAL N N 125.07 0.14 1 357 102 113 SER H H 9.68 0.015 1 358 102 113 SER C C 175.013 0.08 1 359 102 113 SER CA C 55.9 0.31 1 360 102 113 SER CB C 66.19 0.31 1 361 102 113 SER N N 119.84 0.14 1 362 103 114 ASN H H 8.56 0.015 1 363 103 114 ASN C C 174.627 0.08 1 364 103 114 ASN CA C 53.79 0.31 1 365 103 114 ASN CB C 37.05 0.31 1 366 103 114 ASN N N 125.36 0.14 1 367 104 115 ARG H H 8.02 0.015 1 368 104 115 ARG C C 174.792 0.08 1 369 104 115 ARG CA C 54.43 0.31 1 370 104 115 ARG CB C 33.4 0.31 1 371 104 115 ARG N N 119.13 0.14 1 372 105 116 ARG H H 8.43 0.015 1 373 105 116 ARG C C 175.886 0.08 1 374 105 116 ARG CA C 56.62 0.31 1 375 105 116 ARG CB C 29.84 0.31 1 376 105 116 ARG N N 125.92 0.14 1 377 106 117 ALA H H 8.15 0.015 1 378 106 117 ALA C C 178.993 0.08 1 379 106 117 ALA CA C 52.36 0.31 1 380 106 117 ALA CB C 20.27 0.31 1 381 106 117 ALA N N 127.48 0.14 1 382 107 118 ASP H H 8.89 0.015 1 383 107 118 ASP C C 176.806 0.08 1 384 107 118 ASP CA C 57.86 0.31 1 385 107 118 ASP CB C 41.41 0.31 1 386 107 118 ASP N N 126.06 0.14 1 387 108 119 GLU H H 7.24 0.015 1 388 108 119 GLU C C 172.439 0.08 1 389 108 119 GLU CA C 55.03 0.31 1 390 108 119 GLU CB C 34.5 0.31 1 391 108 119 GLU N N 114.75 0.14 1 392 109 120 VAL H H 8.23 0.015 1 393 109 120 VAL C C 173.609 0.08 1 394 109 120 VAL CA C 60.99 0.31 1 395 109 120 VAL CB C 33.35 0.31 1 396 109 120 VAL N N 124.37 0.14 1 397 110 121 PHE H H 8.8 0.015 1 398 110 121 PHE C C 174.214 0.08 1 399 110 121 PHE CA C 54.37 0.31 1 400 110 121 PHE CB C 42.28 0.31 1 401 110 121 PHE N N 126.77 0.14 1 402 111 122 VAL H H 8.26 0.015 1 403 111 122 VAL C C 174.088 0.08 1 404 111 122 VAL CA C 61.43 0.31 1 405 111 122 VAL CB C 33.63 0.31 1 406 111 122 VAL N N 122.67 0.14 1 407 112 123 LEU H H 8.56 0.015 1 408 112 123 LEU C C 176.032 0.08 1 409 112 123 LEU CA C 52.6 0.31 1 410 112 123 LEU CB C 42.47 0.31 1 411 112 123 LEU N N 126.83 0.14 1 412 113 124 SER H H 8.1 0.015 1 413 113 124 SER CA C 58.63 0.31 1 414 113 124 SER CB C 62.35 0.31 1 415 113 124 SER N N 116.73 0.14 1 416 114 125 PRO C C 177.537 0.08 1 417 115 126 VAL H H 8.51 0.015 1 418 115 126 VAL C C 175.345 0.08 1 419 115 126 VAL CA C 61.14 0.31 1 420 115 126 VAL CB C 31.58 0.31 1 421 115 126 VAL N N 115.46 0.14 1 422 116 127 ARG H H 7.11 0.015 1 423 116 127 ARG C C 174.996 0.08 1 424 116 127 ARG CA C 53.93 0.31 1 425 116 127 ARG CB C 33.57 0.31 1 426 116 127 ARG N N 118.85 0.14 1 427 117 128 GLN H H 8.6 0.015 1 428 117 128 GLN CA C 57.88 0.31 1 429 117 128 GLN CB C 27.91 0.31 1 430 117 128 GLN N N 125.36 0.14 1 431 118 129 GLY H H 8.63 0.015 1 432 118 129 GLY C C 174.664 0.08 1 433 118 129 GLY CA C 45.16 0.31 1 434 118 129 GLY N N 116.45 0.14 1 435 119 130 GLY H H 8.13 0.015 1 436 119 130 GLY C C 173.043 0.08 1 437 119 130 GLY CA C 43.9 0.31 1 438 119 130 GLY N N 108.53 0.14 1 439 120 131 ARG H H 9.84 0.015 1 440 120 131 ARG CA C 54.07 0.31 1 441 120 131 ARG CB C 30.73 0.31 1 442 120 131 ARG N N 121.54 0.14 1 443 121 132 PRO C C 173.996 0.08 1 444 122 133 LEU H H 7.89 0.015 1 445 122 133 LEU C C 174.867 0.08 1 446 122 133 LEU CA C 54.38 0.31 1 447 122 133 LEU CB C 46 0.31 1 448 122 133 LEU N N 115.6 0.14 1 449 123 134 LEU H H 6.87 0.015 1 450 123 134 LEU C C 174.343 0.08 1 451 123 134 LEU CA C 53.15 0.31 1 452 123 134 LEU CB C 45.33 0.31 1 453 123 134 LEU N N 122.95 0.14 1 454 124 135 GLY H H 9.4 0.015 1 455 124 135 GLY C C 171.866 0.08 1 456 124 135 GLY CA C 45.04 0.31 1 457 124 135 GLY N N 114.19 0.14 1 458 125 136 ILE H H 8.61 0.015 1 459 125 136 ILE CA C 58.5 0.31 1 460 125 136 ILE CB C 42.45 0.31 1 461 125 136 ILE N N 111.08 0.14 1 462 126 137 ARG H H 8.43 0.015 1 463 126 137 ARG C C 175.26 0.08 1 464 126 137 ARG CA C 53.79 0.31 1 465 126 137 ARG CB C 33.91 0.31 1 466 126 137 ARG N N 124.79 0.14 1 467 127 138 ILE H H 8.97 0.015 1 468 127 138 ILE C C 176.214 0.08 1 469 127 138 ILE CA C 60.62 0.31 1 470 127 138 ILE CB C 40.08 0.31 1 471 127 138 ILE N N 129.32 0.14 1 472 128 139 GLY H H 9.23 0.015 1 473 128 139 GLY C C 174.321 0.08 1 474 128 139 GLY CA C 47.92 0.31 1 475 128 139 GLY N N 117.75 0.14 1 476 129 140 ASN H H 8.72 0.015 1 477 129 140 ASN C C 172.697 0.08 1 478 129 140 ASN CA C 53.48 0.31 1 479 129 140 ASN CB C 39.3 0.31 1 480 129 140 ASN N N 127.62 0.14 1 481 130 141 ASP H H 7.8 0.015 1 482 130 141 ASP C C 172.991 0.08 1 483 130 141 ASP CA C 52.38 0.31 1 484 130 141 ASP CB C 44.23 0.31 1 485 130 141 ASP N N 118.71 0.14 1 486 131 142 ALA H H 8.78 0.015 1 487 131 142 ALA C C 174.965 0.08 1 488 131 142 ALA CA C 49.97 0.31 1 489 131 142 ALA CB C 23.1 0.31 1 490 131 142 ALA N N 123.09 0.14 1 491 132 143 PHE H H 8.67 0.015 1 492 132 143 PHE C C 174.332 0.08 1 493 132 143 PHE CA C 56.51 0.31 1 494 132 143 PHE CB C 43.01 0.31 1 495 132 143 PHE N N 119.28 0.14 1 496 133 144 PHE H H 9.42 0.015 1 497 133 144 PHE CA C 55.86 0.31 1 498 133 144 PHE CB C 43.38 0.31 1 499 133 144 PHE N N 119.56 0.14 1 500 134 145 THR H H 8.95 0.015 1 501 134 145 THR C C 170.82 0.08 1 502 134 145 THR CA C 57.34 0.31 1 503 134 145 THR CB C 71.74 0.31 1 504 134 145 THR N N 115.6 0.14 1 505 135 146 ALA H H 7.79 0.015 1 506 135 146 ALA C C 175.178 0.08 1 507 135 146 ALA CA C 50.22 0.31 1 508 135 146 ALA CB C 23.86 0.31 1 509 135 146 ALA N N 126.63 0.14 1 510 136 147 HIS H H 8.95 0.015 1 511 136 147 HIS C C 175.576 0.08 1 512 136 147 HIS CA C 52.77 0.31 1 513 136 147 HIS CB C 34.17 0.31 1 514 136 147 HIS N N 120.83 0.14 1 515 137 148 ALA H H 8.53 0.015 1 516 137 148 ALA C C 176.578 0.08 1 517 137 148 ALA CA C 52.29 0.31 1 518 137 148 ALA CB C 21 0.31 1 519 137 148 ALA N N 131.14 0.14 1 520 138 149 ILE H H 10.22 0.015 1 521 138 149 ILE C C 176.956 0.08 1 522 138 149 ILE CA C 62.65 0.31 1 523 138 149 ILE CB C 40.06 0.31 1 524 138 149 ILE N N 124.65 0.14 1 525 139 150 ALA H H 8.35 0.015 1 526 139 150 ALA CA C 51.67 0.31 1 527 139 150 ALA CB C 16.1 0.31 1 528 139 150 ALA N N 131.58 0.14 1 529 140 151 MET H H 7.71 0.015 1 530 140 151 MET C C 174.717 0.08 1 531 140 151 MET CA C 54.76 0.31 1 532 140 151 MET CB C 35.05 0.31 1 533 140 151 MET N N 121.68 0.14 1 534 141 152 ARG H H 8.43 0.015 1 535 141 152 ARG CA C 57.15 0.31 1 536 141 152 ARG CB C 29.95 0.31 1 537 141 152 ARG N N 122.81 0.14 1 538 142 153 ASN H H 8.76 0.015 1 539 142 153 ASN C C 174.921 0.08 1 540 142 153 ASN CA C 54.22 0.31 1 541 142 153 ASN CB C 36.87 0.31 1 542 142 153 ASN N N 121.11 0.14 1 543 143 154 ASN H H 8.12 0.015 1 544 143 154 ASN C C 174.38 0.08 1 545 143 154 ASN CA C 51.85 0.31 1 546 143 154 ASN CB C 38.49 0.31 1 547 143 154 ASN N N 117.16 0.14 1 548 144 155 ASP H H 9.83 0.015 1 549 144 155 ASP C C 176.277 0.08 1 550 144 155 ASP CA C 53.47 0.31 1 551 144 155 ASP CB C 38.52 0.31 1 552 144 155 ASP N N 111.15 0.14 1 553 145 156 ALA H H 7.61 0.015 1 554 145 156 ALA CA C 57.4 0.31 1 555 145 156 ALA CB C 17.41 0.31 1 556 145 156 ALA N N 121.68 0.14 1 557 146 157 PRO C C 178.177 0.08 1 558 147 158 ALA H H 7.07 0.015 1 559 147 158 ALA C C 180.56 0.08 1 560 147 158 ALA CA C 54.46 0.31 1 561 147 158 ALA CB C 18.52 0.31 1 562 147 158 ALA N N 119.98 0.14 1 563 148 159 LEU H H 8.42 0.015 1 564 148 159 LEU C C 177.773 0.08 1 565 148 159 LEU CA C 57.89 0.31 1 566 148 159 LEU CB C 41.46 0.31 1 567 148 159 LEU N N 123.24 0.14 1 568 149 160 VAL H H 7.17 0.015 1 569 149 160 VAL C C 177.982 0.08 1 570 149 160 VAL CA C 65.79 0.31 1 571 149 160 VAL CB C 30.83 0.31 1 572 149 160 VAL N N 117.16 0.14 1 573 150 161 GLU H H 7.83 0.015 1 574 150 161 GLU C C 176.882 0.08 1 575 150 161 GLU CA C 59.42 0.31 1 576 150 161 GLU CB C 29.22 0.31 1 577 150 161 GLU N N 118.71 0.14 1 578 151 162 GLU H H 7.14 0.015 1 579 151 162 GLU C C 178.66 0.08 1 580 151 162 GLU CA C 59.28 0.31 1 581 151 162 GLU CB C 28.05 0.31 1 582 151 162 GLU N N 119.84 0.14 1 583 152 163 VAL H H 6.82 0.015 1 584 152 163 VAL C C 175.638 0.08 1 585 152 163 VAL CA C 66.8 0.31 1 586 152 163 VAL CB C 30.61 0.31 1 587 152 163 VAL N N 121.12 0.14 1 588 153 164 TYR H H 7.44 0.015 1 589 153 164 TYR C C 179.235 0.08 1 590 153 164 TYR CA C 60.77 0.31 1 591 153 164 TYR CB C 38.24 0.31 1 592 153 164 TYR N N 118.15 0.14 1 593 154 165 ASN H H 8.77 0.015 1 594 154 165 ASN C C 175.605 0.08 1 595 154 165 ASN CA C 55.43 0.31 1 596 154 165 ASN CB C 38.06 0.31 1 597 154 165 ASN N N 119.56 0.14 1 598 155 166 PHE H H 7.8 0.015 1 599 155 166 PHE C C 177.917 0.08 1 600 155 166 PHE CA C 60.43 0.31 1 601 155 166 PHE CB C 39.07 0.31 1 602 155 166 PHE N N 122.39 0.14 1 603 156 167 PHE H H 6.82 0.015 1 604 156 167 PHE C C 177.651 0.08 1 605 156 167 PHE CA C 61.65 0.31 1 606 156 167 PHE CB C 37.67 0.31 1 607 156 167 PHE N N 114.89 0.14 1 608 157 168 ARG H H 7.66 0.015 1 609 157 168 ARG C C 177.38 0.08 1 610 157 168 ARG CA C 59.4 0.31 1 611 157 168 ARG CB C 30.45 0.31 1 612 157 168 ARG N N 119.7 0.14 1 613 158 169 ASP H H 7.88 0.015 1 614 158 169 ASP CA C 54.22 0.08 1 615 158 169 ASP N N 114.61 0.14 1 616 159 170 SER H H 6.95 0.015 1 617 159 170 SER C C 175.187 0.08 1 618 159 170 SER CA C 59.31 0.31 1 619 159 170 SER CB C 63.52 0.31 1 620 159 170 SER N N 116.31 0.14 1 621 160 171 ARG H H 8.4 0.015 1 622 160 171 ARG C C 175.084 0.08 1 623 160 171 ARG CA C 56.32 0.31 1 624 160 171 ARG CB C 29.71 0.31 1 625 160 171 ARG N N 124.08 0.14 1 626 161 172 ASP H H 7.94 0.015 1 627 161 172 ASP CA C 50.87 0.31 1 628 161 172 ASP CB C 42.41 0.31 1 629 161 172 ASP N N 121.11 0.14 1 630 162 173 PRO C C 178.938 0.08 1 631 163 174 VAL H H 7.64 0.015 1 632 163 174 VAL C C 178.489 0.08 1 633 163 174 VAL CA C 65.19 0.31 1 634 163 174 VAL CB C 30.95 0.31 1 635 163 174 VAL N N 118.43 0.14 1 636 164 175 HIS H H 7.42 0.015 1 637 164 175 HIS C C 176.463 0.08 1 638 164 175 HIS CA C 58.88 0.31 1 639 164 175 HIS CB C 29.73 0.31 1 640 164 175 HIS N N 117.72 0.14 1 641 165 176 GLN H H 7.66 0.015 1 642 165 176 GLN C C 176.511 0.08 1 643 165 176 GLN CA C 57.87 0.31 1 644 165 176 GLN CB C 29.15 0.31 1 645 165 176 GLN N N 116.02 0.14 1 646 166 177 ALA H H 6.77 0.015 1 647 166 177 ALA C C 177.196 0.08 1 648 166 177 ALA CA C 50.9 0.31 1 649 166 177 ALA CB C 18.82 0.31 1 650 166 177 ALA N N 116.17 0.14 1 651 167 178 LEU H H 6.82 0.015 1 652 167 178 LEU C C 177.057 0.08 1 653 167 178 LEU CA C 55.79 0.31 1 654 167 178 LEU CB C 40.93 0.31 1 655 167 178 LEU N N 121.4 0.14 1 656 168 179 ASN H H 7.87 0.015 1 657 168 179 ASN C C 173.721 0.08 1 658 168 179 ASN CA C 52.93 0.31 1 659 168 179 ASN CB C 39.25 0.31 1 660 168 179 ASN N N 119.13 0.14 1 661 169 180 TRP H H 8.26 0.015 1 662 169 180 TRP C C 175.717 0.08 1 663 169 180 TRP CA C 52.93 0.31 1 664 169 180 TRP CB C 33.41 0.31 1 665 169 180 TRP N N 120.69 0.14 1 666 170 181 MET H H 8.67 0.015 1 667 170 181 MET C C 174.702 0.08 1 668 170 181 MET CA C 54.96 0.31 1 669 170 181 MET CB C 37.23 0.31 1 670 170 181 MET N N 120.41 0.14 1 671 171 182 ILE H H 10.11 0.015 1 672 171 182 ILE C C 174.084 0.08 1 673 171 182 ILE CA C 60.87 0.31 1 674 171 182 ILE CB C 40.9 0.31 1 675 171 182 ILE N N 128.83 0.14 1 676 172 183 LEU H H 9.12 0.015 1 677 172 183 LEU C C 174.159 0.08 1 678 172 183 LEU CA C 54.05 0.31 1 679 172 183 LEU CB C 45.2 0.31 1 680 172 183 LEU N N 130.59 0.14 1 681 173 184 GLY H H 7.97 0.015 1 682 173 184 GLY CA C 46.29 0.31 1 683 173 184 GLY N N 106.41 0.14 1 684 174 185 ASP H H 6.19 0.015 1 685 174 185 ASP C C 176.508 0.08 1 686 174 185 ASP CA C 50.78 0.31 1 687 174 185 ASP CB C 38.69 0.31 1 688 174 185 ASP N N 114.33 0.14 1 689 175 186 PHE H H 8.53 0.015 1 690 175 186 PHE C C 176.259 0.08 1 691 175 186 PHE CA C 60.65 0.31 1 692 175 186 PHE CB C 40.12 0.31 1 693 175 186 PHE N N 122.39 0.14 1 694 176 187 ASN H H 8.64 0.015 1 695 176 187 ASN C C 171.283 0.08 1 696 176 187 ASN CA C 55.95 0.31 1 697 176 187 ASN CB C 39.97 0.31 1 698 176 187 ASN N N 116.45 0.14 1 699 177 188 ARG H H 7.22 0.015 1 700 177 188 ARG C C 175.094 0.08 1 701 177 188 ARG CA C 55.36 0.31 1 702 177 188 ARG CB C 33.91 0.31 1 703 177 188 ARG N N 112.07 0.14 1 704 178 189 GLU H H 9.43 0.015 1 705 178 189 GLU CA C 56.56 0.31 1 706 178 189 GLU CB C 28.39 0.31 1 707 178 189 GLU N N 127.76 0.14 1 708 179 190 PRO C C 178.009 0.08 1 709 180 191 ALA H H 8.38 0.015 1 710 180 191 ALA C C 179.803 0.08 1 711 180 191 ALA CA C 55.1 0.31 1 712 180 191 ALA CB C 18.25 0.31 1 713 180 191 ALA N N 118.15 0.14 1 714 181 192 ASP H H 6.83 0.015 1 715 181 192 ASP CA C 56.28 0.31 1 716 181 192 ASP CB C 42.55 0.31 1 717 181 192 ASP N N 118.15 0.14 1 718 182 193 LEU H H 7.89 0.015 1 719 182 193 LEU C C 175.548 0.08 1 720 182 193 LEU CA C 59.41 0.31 1 721 182 193 LEU CB C 41.03 0.31 1 722 182 193 LEU N N 120.69 0.14 1 723 183 194 GLU H H 8.31 0.015 1 724 183 194 GLU C C 178.331 0.08 1 725 183 194 GLU CA C 60.5 0.31 1 726 183 194 GLU CB C 29.92 0.31 1 727 183 194 GLU N N 117.44 0.14 1 728 184 195 MET H H 7.32 0.015 1 729 184 195 MET C C 176.12 0.08 1 730 184 195 MET CA C 57.17 0.31 1 731 184 195 MET CB C 32.57 0.31 1 732 184 195 MET N N 113.34 0.14 1 733 185 196 ASN H H 7.49 0.015 1 734 185 196 ASN CA C 54.33 0.31 1 735 185 196 ASN CB C 41.4 0.31 1 736 185 196 ASN N N 116.87 0.14 1 737 186 197 LEU H H 7.87 0.015 1 738 186 197 LEU C C 177.434 0.08 1 739 186 197 LEU CA C 55.69 0.31 1 740 186 197 LEU CB C 41.99 0.31 1 741 187 198 THR H H 7.97 0.015 1 742 187 198 THR CA C 62.07 0.31 1 743 187 198 THR CB C 69.73 0.31 1 744 187 198 THR N N 115.46 0.14 1 745 188 199 VAL H H 7.83 0.015 1 746 188 199 VAL CA C 59.69 0.31 1 747 188 199 VAL CB C 32.54 0.31 1 748 188 199 VAL N N 123.94 0.14 1 749 189 200 PRO C C 176.751 0.08 1 750 190 201 VAL H H 7.95 0.015 1 751 190 201 VAL C C 176.083 0.08 1 752 190 201 VAL CA C 62.51 0.31 1 753 190 201 VAL CB C 32.83 0.31 1 754 190 201 VAL N N 121.11 0.14 1 755 191 202 ARG H H 8.19 0.015 1 756 191 202 ARG C C 175.952 0.08 1 757 191 202 ARG CA C 55.89 0.31 1 758 191 202 ARG CB C 30.69 0.31 1 759 191 202 ARG N N 125.64 0.14 1 760 192 203 ARG H H 8.27 0.015 1 761 192 203 ARG C C 176.108 0.08 1 762 192 203 ARG CA C 55.97 0.31 1 763 192 203 ARG CB C 30.71 0.31 1 764 192 203 ARG N N 123.94 0.14 1 765 193 204 ALA H H 8.29 0.015 1 766 193 204 ALA C C 177.752 0.08 1 767 193 204 ALA CA C 53.07 0.31 1 768 193 204 ALA CB C 19.26 0.31 1 769 193 204 ALA N N 126.35 0.14 1 770 194 205 SER H H 8.04 0.015 1 771 194 205 SER C C 174.485 0.08 1 772 194 205 SER CA C 58.5 0.31 1 773 194 205 SER CB C 63.382 0.31 1 774 194 205 SER N N 114.75 0.14 1 775 195 206 GLU H H 8.16 0.015 5 776 195 206 GLU C C 176.029 0.08 5 777 195 206 GLU CA C 56.48 0.31 5 778 195 206 GLU CB C 30.38 0.31 5 779 195 206 GLU N N 123.09 0.14 5 780 196 207 ILE H H 7.93 0.015 1 781 196 207 ILE C C 175.975 0.08 1 782 196 207 ILE CA C 61.25 0.31 1 783 196 207 ILE CB C 38.41 0.31 1 784 196 207 ILE N N 122.39 0.14 1 785 197 208 ILE H H 8.02 0.015 1 786 197 208 ILE C C 176.116 0.08 1 787 197 208 ILE CA C 60.98 0.31 1 788 197 208 ILE CB C 38.48 0.31 1 789 197 208 ILE N N 126.06 0.14 1 790 198 209 SER H H 8.22 0.015 1 791 198 209 SER CA C 58.3 0.31 1 792 198 209 SER CB C 64.04 0.31 1 793 198 209 SER N N 120.41 0.14 1 794 199 210 PRO C C 176.889 0.08 1 795 200 211 ALA H H 8.07 0.015 1 796 200 211 ALA CA C 52.76 0.31 1 797 200 211 ALA CB C 19.11 0.31 1 798 200 211 ALA N N 124.08 0.14 1 799 201 212 ALA H H 7.96 0.015 1 800 201 212 ALA CA C 52.72 0.31 1 801 201 212 ALA CB C 19.25 0.31 1 802 201 212 ALA N N 123.38 0.14 1 803 202 213 ALA H H 8.03 0.015 1 804 202 213 ALA C C 177.989 0.08 1 805 202 213 ALA CA C 52.72 0.31 1 806 202 213 ALA CB C 19.25 0.31 1 807 202 213 ALA N N 123.52 0.14 1 808 203 214 THR H H 7.85 0.015 1 809 203 214 THR C C 174.5 0.08 1 810 203 214 THR CA C 62.09 0.31 1 811 203 214 THR CB C 69.78 0.31 1 812 203 214 THR N N 113.2 0.14 1 813 204 215 GLN H H 8.2 0.015 9 814 204 215 GLN C C 176.204 0.08 9 815 204 215 GLN CA C 56.16 0.31 9 816 204 215 GLN CB C 29.45 0.31 9 817 204 215 GLN N N 123.09 0.14 9 818 205 216 THR H H 8.04 0.015 1 819 205 216 THR C C 174.628 0.08 1 820 205 216 THR CA C 62.14 0.31 1 821 205 216 THR CB C 69.54 0.31 1 822 205 216 THR N N 115.6 0.14 1 823 206 217 SER H H 8.13 0.015 1 824 206 217 SER CA C 58.63 0.31 1 825 206 217 SER CB C 64.28 0.31 1 826 206 217 SER N N 118.2 0.14 1 827 207 218 GLN H H 8.16 0.015 5 828 207 218 GLN CA C 56.5 0.31 5 829 207 218 GLN CB C 30.3 0.31 5 830 207 218 GLN N N 123.09 0.14 5 831 208 219 ARG H H 8.27 0.015 1 832 208 219 ARG CA C 55.99 0.31 1 833 208 219 ARG CB C 30.94 0.31 1 834 208 219 ARG N N 123.06 0.14 1 835 209 220 THR H H 7.99 0.015 1 836 209 220 THR CA C 61.95 0.31 1 837 209 220 THR CB C 69.66 0.31 1 838 209 220 THR N N 116.17 0.14 1 839 210 221 LEU C C 173.715 0.08 9 840 210 221 LEU CA C 54.59 0.31 9 841 210 221 LEU CB C 43.44 0.31 9 842 211 222 ASP H H 7.53 0.015 1 843 211 222 ASP C C 174.42 0.08 1 844 211 222 ASP CA C 52.73 0.31 1 845 211 222 ASP CB C 42.97 0.31 1 846 212 223 TYR H H 8.31 0.015 1 847 212 223 TYR C C 170.88 0.08 1 848 212 223 TYR CA C 57.76 0.31 1 849 212 223 TYR CB C 33.88 0.31 1 850 212 223 TYR N N 115.6 0.14 1 851 213 224 ALA H H 8.38 0.015 1 852 213 224 ALA C C 176.04 0.08 1 853 213 224 ALA CA C 50.21 0.31 1 854 213 224 ALA CB C 24.74 0.31 1 855 213 224 ALA N N 120.55 0.14 1 856 214 225 VAL H H 9.2 0.015 1 857 214 225 VAL C C 174.611 0.08 1 858 214 225 VAL CA C 61.53 0.31 1 859 214 225 VAL CB C 35.05 0.31 1 860 214 225 VAL N N 121.11 0.14 1 861 215 226 ALA H H 8.99 0.015 1 862 215 226 ALA C C 175.496 0.08 1 863 215 226 ALA CA C 50.01 0.31 1 864 215 226 ALA CB C 22.41 0.31 1 865 215 226 ALA N N 131.72 0.14 1 866 216 227 GLY H H 8.34 0.015 1 867 216 227 GLY C C 171.662 0.08 1 868 216 227 GLY CA C 45.3 0.31 1 869 216 227 GLY N N 108.16 0.14 1 870 217 228 ASN H H 7.31 0.015 1 871 217 228 ASN C C 175.926 0.08 1 872 217 228 ASN CA C 54.73 0.31 1 873 217 228 ASN CB C 42.17 0.31 1 874 217 228 ASN N N 116.31 0.14 1 875 218 229 SER CA C 61.8 0.31 9 876 218 229 SER CB C 61.8 0.31 9 877 219 230 VAL H H 8.23 0.015 1 878 219 230 VAL C C 175.719 0.08 1 879 219 230 VAL CA C 62.68 0.31 1 880 219 230 VAL CB C 34.48 0.31 1 881 219 230 VAL N N 114.33 0.14 1 882 220 231 ALA H H 8.01 0.015 1 883 220 231 ALA C C 175.145 0.08 1 884 220 231 ALA CA C 51.46 0.31 1 885 220 231 ALA CB C 18.79 0.31 1 886 220 231 ALA N N 127.62 0.14 1 887 221 232 PHE H H 8.47 0.015 1 888 221 232 PHE C C 174.987 0.08 1 889 221 232 PHE CA C 59.28 0.31 1 890 221 232 PHE CB C 39.82 0.31 1 891 221 232 PHE N N 123.09 0.14 1 892 222 233 ARG H H 7.36 0.015 1 893 222 233 ARG CA C 52.72 0.31 1 894 222 233 ARG CB C 31.29 0.31 1 895 222 233 ARG N N 129.74 0.14 1 896 223 234 PRO C C 176.668 0.08 5 897 224 235 SER H H 9.25 0.015 5 898 224 235 SER CA C 56.64 0.31 5 899 224 235 SER CB C 64.52 0.31 5 900 224 235 SER N N 121.68 0.14 5 901 225 236 PRO C C 174.541 0.08 1 902 226 237 LEU H H 7.73 0.015 1 903 226 237 LEU C C 175.796 0.08 1 904 226 237 LEU CA C 53.87 0.31 1 905 226 237 LEU CB C 45.66 0.31 1 906 226 237 LEU N N 125.5 0.14 1 907 227 238 GLN H H 8.79 0.015 1 908 227 238 GLN C C 173.21 0.08 1 909 227 238 GLN CA C 54.12 0.31 1 910 227 238 GLN CB C 32.06 0.31 1 911 227 238 GLN N N 118.57 0.14 1 912 228 239 ALA H H 8.75 0.015 1 913 228 239 ALA C C 177.058 0.08 1 914 228 239 ALA CA C 49.21 0.31 1 915 228 239 ALA CB C 21.51 0.31 1 916 228 239 ALA N N 125.21 0.14 1 917 229 240 GLY H H 8.64 0.015 1 918 229 240 GLY C C 172.136 0.08 1 919 229 240 GLY CA C 44.81 0.31 1 920 229 240 GLY N N 106.97 0.14 1 921 230 241 ILE H H 8.58 0.015 1 922 230 241 ILE C C 176.393 0.08 1 923 230 241 ILE CA C 61.11 0.31 1 924 230 241 ILE CB C 37.19 0.31 1 925 230 241 ILE N N 124.51 0.14 1 926 231 242 VAL H H 7.96 0.015 1 927 231 242 VAL C C 174.95 0.08 1 928 231 242 VAL CA C 61.9 0.31 1 929 231 242 VAL CB C 31.32 0.31 1 930 231 242 VAL N N 128.47 0.14 1 931 232 243 TYR H H 7.83 0.015 1 932 232 243 TYR C C 176.775 0.08 1 933 232 243 TYR CA C 58.98 0.31 1 934 232 243 TYR CB C 39.12 0.31 1 935 232 243 TYR N N 124.65 0.14 1 936 233 244 GLY H H 8.12 0.015 1 937 233 244 GLY C C 173.881 0.08 1 938 233 244 GLY CA C 45.17 0.31 1 939 233 244 GLY N N 109.24 0.14 1 940 234 245 ALA H H 7.87 0.015 1 941 234 245 ALA C C 177.796 0.08 1 942 234 245 ALA CA C 52.93 0.31 1 943 234 245 ALA CB C 19.11 0.31 1 944 234 245 ALA N N 123.94 0.14 1 945 235 246 ARG H H 8.04 0.015 1 946 235 246 ARG CA C 56.37 0.31 1 947 235 246 ARG CB C 30.08 0.31 1 948 235 246 ARG N N 119.13 0.14 1 949 236 247 ARG H H 8.11 0.015 1 950 236 247 ARG C C 176.404 0.08 1 951 236 247 ARG CA C 56.87 0.31 1 952 236 247 ARG CB C 29.97 0.31 1 953 236 247 ARG N N 121.11 0.14 1 954 237 248 THR H H 7.77 0.015 1 955 237 248 THR C C 173.722 0.08 1 956 237 248 THR CA C 61.84 0.31 1 957 237 248 THR CB C 69.74 0.31 1 958 237 248 THR N N 113.62 0.14 1 959 238 249 GLN H H 8.14 0.015 1 960 238 249 GLN C C 176.116 0.08 1 961 238 249 GLN CA C 56.12 0.31 1 962 238 249 GLN CB C 29.37 0.31 1 963 238 249 GLN N N 122.1 0.14 1 964 239 250 ILE H H 8.11 0.015 1 965 239 250 ILE C C 173.941 0.08 1 966 239 250 ILE CA C 61.2 0.31 1 967 239 250 ILE CB C 38.63 0.31 1 968 239 250 ILE N N 122.02 0.14 1 969 240 251 SER H H 8.3 0.015 1 970 240 251 SER CA C 58.58 0.31 1 971 240 251 SER CB C 63.89 0.31 1 972 240 251 SER N N 120.32 0.14 1 973 241 252 SER H H 7.96 0.015 1 974 241 252 SER CA C 57.99 0.31 1 975 241 252 SER CB C 64.42 0.31 1 976 241 252 SER N N 117.72 0.14 1 977 242 253 ASP H H 8.15 0.015 1 978 242 253 ASP C C 175.781 0.08 1 979 242 253 ASP CA C 55.96 0.31 1 980 242 253 ASP CB C 41.54 0.31 1 981 242 253 ASP N N 121.96 0.14 1 982 243 254 HIS CA C 56.9 0.31 9 983 243 254 HIS CB C 29.77 0.31 9 984 244 255 PHE H H 8.19 0.015 9 985 244 255 PHE C C 175.077 0.08 9 986 244 255 PHE CA C 53.58 0.31 9 987 244 255 PHE CB C 38.77 0.31 9 988 245 256 PRO C C 175.961 0.08 1 989 245 256 PRO CA C 61.84 0.31 1 990 245 256 PRO CB C 30.11 0.31 1 991 246 257 VAL H H 8.65 0.015 1 992 246 257 VAL C C 175.327 0.08 1 993 246 257 VAL CA C 61.84 0.31 1 994 246 257 VAL CB C 34.37 0.31 1 995 246 257 VAL N N 124.51 0.14 1 996 247 258 GLY H H 8.93 0.015 1 997 247 258 GLY C C 172.953 0.08 1 998 247 258 GLY CA C 43.87 0.31 1 999 247 258 GLY N N 114.75 0.14 1 1000 248 259 VAL H H 8.93 0.015 1 1001 248 259 VAL C C 174.673 0.08 1 1002 248 259 VAL CA C 61.25 0.31 1 1003 248 259 VAL CB C 34.07 0.31 1 1004 248 259 VAL N N 123.52 0.14 1 1005 249 260 SER H H 8.46 0.015 1 1006 249 260 SER C C 173.136 0.08 1 1007 249 260 SER CA C 57.21 0.31 1 1008 249 260 SER CB C 65.97 0.31 1 1009 249 260 SER N N 118.85 0.14 1 1010 250 261 ARG H H 8.66 0.015 1 1011 250 261 ARG C C 175.723 0.08 1 1012 250 261 ARG CA C 56.82 0.31 1 1013 250 261 ARG CB C 30.68 0.31 1 1014 250 261 ARG N N 121.4 0.14 1 1015 251 262 ARG H H 7.93 0.015 1 1016 251 262 ARG CA C 58.16 0.31 1 1017 251 262 ARG CB C 31.42 0.31 1 1018 251 262 ARG N N 130.02 0.14 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 211 '776,896' '212,216,279,899' '213,282,778,829' '214,280,775,827,897' '215,278,281,777,828,898' '217,283,779,830,900' stop_ save_ save_T1_list_1 _Saveframe_category T1_relaxation _Details ; 15N longitudinal T1 relaxation times were measured by the inversion-recovery method (????????) using standard water flip-back methods [Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12594.]. Spectra was recorded as 128 x 512 complex matrices, with spectral widths of 8385 (1H) and 2200 (15N) Hz, with 16 scans per FID. Relaxation delays collected were: 0.03, 0.05, 0.07, 0.09, 0.20, 0.50, 0.70, 1.0, 1.3, 1.6 s. Duplicate spectra were recorded for 0.03 and 0.05 s to estimate the precision of peak intensities. ; loop_ _Software_label $software_1 $software_2 stop_ loop_ _Sample_label $sample_1 $sample_1 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 599.7 _T1_coherence_type 'single quantum' _T1_value_units s _Mol_system_component_name EcCdtB-II _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 12 ASP N 0.833402784 0.00686274 2 13 LEU N 0.579743753 0.007351885 3 16 PHE N 1.063829787 0.011554663 4 17 ARG N 1.065076153 0.021644125 5 18 VAL N 0.987459267 0.010544725 6 19 ALA N 0.965903603 0.007901052 7 20 THR N 0.962278676 0.01380722 8 21 TRP N 0.954289531 0.053774985 9 23 LEU N 0.924812725 0.012482241 10 25 GLY N 1.072156106 0.06537091 11 29 THR N 0.956388676 0.01326128 12 35 ASN N 1.065984437 0.039598759 13 36 ILE N 0.991866693 0.007433797 14 41 LEU N 0.952925481 0.005571595 15 42 ILE N 0.981257973 0.092164097 16 43 SER N 1.01461039 0.010715151 17 44 GLY N 0.859328005 0.018403935 18 45 GLU N 0.988630746 0.006097195 19 46 ASN N 1.067235859 0.00791735 20 47 ALA N 1.02124183 0.007247319 21 49 ASP N 1.018848701 0.01112349 22 50 ILE N 1.053962901 0.00603286 23 51 LEU N 0.998103603 0.018466489 24 52 ALA N 0.835770999 0.023114168 25 53 VAL N 1.019160212 0.013044577 26 55 GLU N 1.007049345 0.008901076 27 56 ALA N 1.00532824 0.009179217 28 62 THR N 0.964971533 0.0168645 29 63 ALA N 0.958956655 0.000920481 30 64 VAL N 1.090631476 0.012755924 31 65 ASP N 1.076194576 0.006408001 32 66 THR N 0.690894017 0.010712662 33 67 GLY N 0.969367972 0.00292177 34 68 ARG N 0.914829384 0.007254525 35 69 VAL N 1.013993105 0.011647921 36 70 ILE N 1.096852035 0.023721699 37 72 SER N 0.968616815 0.006802615 38 74 GLY N 0.855871277 0.005084384 39 75 ILE N 0.986874568 0.016839173 40 78 ARG N 0.971817298 0.002841571 41 79 GLU N 1.023646228 0.014236491 42 80 LEU N 0.964227172 0.024990357 43 81 ILE N 1.579030475 0.039092502 44 84 LEU N 0.988728495 0.012773758 45 85 SER N 0.883002208 0.017817538 46 86 THR N 0.950931913 0.03380467 47 89 ARG N 0.928160386 0.012661893 48 91 GLN N 0.961168781 0.015966259 49 92 GLN N 0.993245928 0.013397922 50 96 TYR N 0.968616815 0.007945685 51 100 VAL N 0.952653139 0.024100133 52 101 ASP N 1.038745196 0.049630947 53 103 LEU N 0.933706816 0.004291496 54 104 GLY N 0.965903603 0.02596309 55 105 GLY N 1.070778456 0.016887413 56 107 VAL N 1.136363636 0.009374219 57 111 LEU N 1.098659635 0.010971967 58 112 VAL N 1.128286133 0.06774305 59 113 SER N 1.102414287 0.081157733 60 114 ASN N 0.795038957 0.01154275 61 116 ARG N 1.019160212 0.026755487 62 117 ALA N 0.863930886 0.015267286 63 118 ASP N 0.943930527 0.007182275 64 119 GLU N 0.960522524 0.004262811 65 120 VAL N 1.020408163 0.002191285 66 121 PHE N 0.975514584 0.011359984 67 122 VAL N 1.06621175 0.007786747 68 123 LEU N 0.97713504 0.012278238 69 124 SER N 0.324949633 0.001272067 70 126 VAL N 0.923275782 0.025670887 71 127 ARG N 0.958956655 0.004063376 72 128 GLN N 1.038421599 0.012329688 73 129 GLY N 1.03820598 0.002593354 74 130 GLY N 0.951565325 0.011733009 75 131 ARG N 1.090988436 0.033870957 76 133 LEU N 0.971439674 0.009625763 77 134 LEU N 1.025115325 0.002845201 78 135 GLY N 0.975800156 0.003056539 79 136 ILE N 1.170411985 0.027192805 80 138 ILE N 0.667200427 0.005294529 81 139 GLY N 1.02207686 0.015159941 82 140 ASN N 0.992260369 0.003061618 83 142 ALA N 0.995123893 0.004876107 84 143 PHE N 0.659413122 0.002531671 85 145 THR N 1.031459515 0.014784469 86 146 ALA N 0.990982063 0.012026964 87 147 HIS N 0.970120295 0.012197976 88 148 ALA N 0.984348853 0.009785753 89 149 ILE N 1.051193104 0.016726588 90 150 ALA N 0.934230194 0.003768117 91 151 MET N 1.052299274 0.005454058 92 152 ARG N 1.100231049 0.016463536 93 153 ASN N 1.011838511 0.016544871 94 154 ASN N 0.994332306 0.01140037 95 155 ASP N 1.020304051 0.010623784 96 156 ALA N 0.957212597 0.011685766 97 158 ALA N 0.945984297 0.004766797 98 159 LEU N 0.967305088 0.005646848 99 160 VAL N 0.986582478 0.006466181 100 161 GLU N 0.964506173 0.008824565 101 162 GLU N 0.920471281 0.006055171 102 163 VAL N 0.947687642 0.006875168 103 164 TYR N 0.944376239 0.005652261 104 165 ASN N 0.926526452 0.00910229 105 167 PHE N 0.949577438 0.013535342 106 168 ARG N 0.997904401 0.00289624 107 169 ASP N 0.996611521 0.005492898 108 170 SER N 0.92945441 0.003120429 109 171 ARG N 1.01853738 0.016123768 110 172 ASP N 0.988826263 0.005209522 111 174 VAL N 0.93676815 0.006806109 112 176 GLN N 0.922594335 0.003417332 113 177 ALA N 0.971250971 0.010874348 114 178 LEU N 0.947059381 0.006866022 115 179 ASN N 0.997207818 0.008423718 116 180 TRP N 0.966744006 0.016927054 117 181 MET N 0.977517107 0.005573731 118 182 ILE N 0.995123893 0.006679353 119 183 LEU N 0.985221675 0.005662194 120 184 GLY N 0.9765625 0.006238483 121 185 ASP N 1 0.003613007 122 186 PHE N 0.990393186 0.012414676 123 188 ARG N 0.961168781 0.006042748 124 189 GLU N 0.944554642 0.0060157 125 191 ALA N 0.98000784 0.008720655 126 192 ASP N 0.979911808 0.006768014 127 193 LEU N 0.968710646 0.009858686 128 194 GLU N 0.985804416 0.01992826 129 195 MET N 0.982607841 0.01073675 130 196 ASN N 1.03626943 0.012498268 131 198 THR N 0.859401856 0.006698958 132 199 VAL N 0.885818053 0.008076646 133 202 ARG N 1.099989 0.037149958 134 203 ARG N 0.990982063 0.008418297 135 204 ALA N 0.945537065 0.012868149 136 205 SER N 0.989119683 0.01328609 137 206 GLU N 0.974089227 0.00161572 138 207 ILE N 0.73313783 0.005687438 139 208 ILE N 0.87009484 0.008639782 140 211 ALA N 0.975704947 0.023895213 141 213 ALA N 0.90983532 0.005831744 142 214 THR N 0.951927653 0.022161573 143 216 THR N 0.891186169 0.006157693 144 219 ARG N 0.950118765 0.104733556 145 222 ASP N 0.960522524 0.004169739 146 223 TYR N 0.929713648 0.010931634 147 224 ALA N 0.973899494 0.006204397 148 225 VAL N 0.964041261 0.007115387 149 226 ALA N 0.918526683 0.013700407 150 227 GLY N 0.957670944 0.019655092 151 228 ASN N 0.930838686 0.002606661 152 230 VAL N 0.885661146 0.00767457 153 231 ALA N 0.998502247 0.020346454 154 232 PHE N 1.035089535 0.007119949 155 233 ARG N 0.917431193 0.009438767 156 235 SER N 1.02574623 0.036840105 157 237 LEU N 0.983574309 0.007604202 158 238 GLN N 0.978665101 0.00636248 159 239 ALA N 1.019887812 0.007228046 160 240 GLY N 0.986485153 0.010225701 161 241 ILE N 0.991571641 0.01365554 162 242 VAL N 0.956205775 0.012786473 163 243 TYR N 0.864378944 0.006473621 164 244 GLY N 0.806776926 0.006694155 165 246 ARG N 0.924299843 0.00550025 166 247 ARG N 0.839560071 0.005605582 167 248 THR N 0.854189801 0.00854853 168 249 GLN N 0.879120879 0.004505524 169 250 ILE N 0.835701153 0.004282047 170 251 SER N 0.833611204 0.006866187 171 252 SER N 0.934666791 0.014730342 172 255 PHE N 1.060670344 0.005996323 173 257 VAL N 0.905633037 0.018154491 174 258 GLY N 0.987751877 0.013449565 175 259 VAL N 1.047449461 0.013333397 176 260 SER N 0.982800983 0.009459386 177 261 ARG N 0.900414191 0.007768536 178 262 ARG N 0.845308538 0.006843145 stop_ save_ save_T2_list_1 _Saveframe_category T2_relaxation _Details ; 15N transverse T2 relaxation times were measured by the Carr-Purcell-Meiboom-Gill method (????????), using standard water flip-back methods [Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12594.]. Spectra was recorded as 128 x 512 complex matrices, with spectral widths of 8385 (1H) and 2200 (15N) Hz, with 16 scans per FID. Relaxation delays collected were: 0.01, 0.03, 0.05, 0.07, 0.09, 0.11, 0.13, 0.15, 0.19, 0.21 s. Duplicate spectra were recorded for 0.01, 0.03 and 0.05 s to estimate the precision of peak intensities. ; loop_ _Software_label $software_1 $software_2 stop_ loop_ _Experiment_label $2D_1H-15N_HSQC_(T2_flag)_9 stop_ loop_ _Sample_label $sample_1 $sample_1 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 599.7 _T2_coherence_type 'single quantum' _T2_value_units s _Mol_system_component_name EcCdtB-II _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 12 ASP N 0.08807236 0.001711978 . . 2 13 LEU N 0.089688512 0.002127892 . . 3 16 PHE N 0.066338952 0.002519715 . . 4 17 ARG N 0.066331912 0.001770815 . . 5 18 VAL N 0.065505473 0.001707862 . . 6 19 ALA N 0.067892811 0.000885818 . . 7 20 THR N 0.07446959 0.001949123 . . 8 21 TRP N 0.068281292 0.001245233 . . 9 23 LEU N 0.166184731 0.005884923 . . 10 27 SER N 0.060214121 0.001708451 . . 11 29 THR N 0.079291452 0.000898438 . . 12 35 ASN N 0.149637876 0.015087773 . . 13 36 ILE N 0.307285745 0.029380585 . . 14 41 LEU N 0.068901842 0.000880854 . . 15 42 ILE N 0.080729797 0.002871758 . . 16 43 SER N 0.070944628 0.001874264 . . 17 44 GLY N 0.094982998 0.001812116 . . 18 45 GLU N 0.081087217 0.002190597 . . 19 46 ASN N 0.081977964 0.003351364 . . 20 47 ALA N 0.195805839 0.00750818 . . 21 49 ASP N 0.063706441 0.003212734 . . 22 50 ILE N 0.070869713 0.001960847 . . 23 51 LEU N 0.078386492 0.001311929 . . 24 52 ALA N 0.186015365 0.00782065 . . 25 53 VAL N 0.092935939 0.00193262 . . 26 55 GLU N 0.069431908 0.0012185 . . 27 56 ALA N 0.072778085 0.001709811 . . 28 62 THR N 0.075640104 0.001886487 . . 29 63 ALA N 0.070589564 0.001545415 . . 30 64 VAL N 0.07160195 0.001120562 . . 31 65 ASP N 0.069315441 0.001373922 . . 32 66 THR N 0.070383874 0.002042632 . . 33 67 GLY N 0.066601841 0.002720808 . . 34 68 ARG N 0.071415309 0.000976068 . . 35 69 VAL N 0.070678871 0.001465476 . . 36 70 ILE N 0.072137581 0.00127739 . . 37 72 SER N 0.055565434 0.000409624 . . 38 74 GLY N 0.104101603 0.001846313 . . 39 75 ILE N 0.057685763 0.000943256 . . 40 78 ARG N 0.074584008 0.001554839 . . 41 79 GLU N 0.07181999 0.002603599 . . 42 80 LEU N 0.06652342 0.002934048 . . 43 81 ILE N 0.196463654 0.036305602 . . 44 84 LEU N 0.082231432 0.002412471 . . 45 85 SER N 0.124183494 0.004347907 . . 46 86 THR N 0.093116806 0.002457164 . . 47 89 ARG N 0.106564365 0.001881391 . . 48 91 GLN N 0.100687697 0.00176817 . . 49 92 GLN N 0.077987304 0.001375886 . . 50 96 TYR N 0.063358909 0.00308804 . . 51 100 VAL N 0.086428929 0.002350268 . . 52 101 ASP N 0.065453593 0.006084329 . . 53 103 LEU N 0.106884426 0.000837049 . . 54 104 GLY N 0.067407702 0.001924078 . . 55 105 GLY N 0.103942541 0.005449894 . . 56 107 VAL N 0.073850335 0.001359123 . . 57 111 LEU N 0.072835864 0.003697481 . . 58 112 VAL N 0.095336155 0.00309001 . . 59 113 SER N 0.069980475 0.002279603 . . 60 114 ASN N 0.064511551 0.004770274 . . 61 116 ARG N 0.068900418 0.001005209 . . 62 117 ALA N 0.125903357 0.006375275 . . 63 118 ASP N 0.06622999 0.001528951 . . 64 119 GLU N 0.074082305 0.001572105 . . 65 120 VAL N 0.082444309 0.000994018 . . 66 121 PHE N 0.07090338 0.001532044 . . 67 122 VAL N 0.077364651 0.000757298 . . 68 123 LEU N 0.069618975 0.001707701 . . 69 124 SER N 0.080119217 0.00176544 . . 70 126 VAL N 0.074614616 0.001684569 . . 71 127 ARG N 0.066545111 0.001162447 . . 72 128 GLN N 0.078883016 0.001482163 . . 73 129 GLY N 0.066778409 0.000803771 . . 74 130 GLY N 0.082878881 0.001979067 . . 75 131 ARG N 0.069640793 0.002252001 . . 76 133 LEU N 0.070157222 0.001264717 . . 77 134 LEU N 0.077332942 0.001652881 . . 78 135 GLY N 0.062151177 0.003194634 . . 79 136 ILE N 0.068194682 0.001744191 . . 80 138 ILE N 0.069145773 0.001233147 . . 81 139 GLY N 0.067605939 0.002082901 . . 82 140 ASN N 0.07182257 0.001472406 . . 83 142 ALA N 0.072631136 0.00147972 . . 84 143 PHE N 0.070322004 0.002780617 . . 85 144 PHE N 0.066723604 0.00295164 . . 86 145 THR N 0.069071268 0.001997392 . . 87 146 ALA N 0.068603104 0.00078737 . . 88 147 HIS N 0.067800287 0.004248417 . . 89 148 ALA N 0.066515012 0.002592055 . . 90 149 ILE N 0.064796636 0.001586354 . . 91 150 ALA N 0.066637346 0.001527121 . . 92 151 MET N 0.091343387 0.001914097 . . 93 152 ARG N 0.075187405 0.003035986 . . 94 153 ASN N 0.073246122 0.001060229 . . 95 154 ASN N 0.075376695 0.000866643 . . 96 155 ASP N 0.064421782 0.002259999 . . 97 156 ALA N 0.06404878 0.000934812 . . 98 158 ALA N 0.070451807 0.001056956 . . 99 159 LEU N 0.070226199 0.000907675 . . 100 160 VAL N 0.065396663 0.000607323 . . 101 161 GLU N 0.066609826 0.001446088 . . 102 162 GLU N 0.06772223 0.001312798 . . 103 163 VAL N 0.065854028 0.001428045 . . 104 164 TYR N 0.065474593 0.00131809 . . 105 165 ASN N 0.062242084 0.001590827 . . 106 167 PHE N 0.063548551 0.001373867 . . 107 168 ARG N 0.065318066 0.001342379 . . 108 169 ASP N 0.072719869 0.000982962 . . 109 170 SER N 0.077939285 0.002045358 . . 110 171 ARG N 0.074453511 0.001446665 . . 111 172 ASP N 0.085752997 0.001186893 . . 112 174 VAL N 0.073348737 0.001511649 . . 113 176 GLN N 0.067717186 0.000931129 . . 114 177 ALA N 0.068353167 0.001011797 . . 115 178 LEU N 0.064877349 0.001370191 . . 116 179 ASN N 0.069863626 0.001692724 . . 117 180 TRP N 0.067193463 0.000652824 . . 118 181 MET N 0.06791725 0.003028888 . . 119 182 ILE N 0.075886928 0.002180131 . . 120 183 LEU N 0.067835242 0.001086071 . . 121 184 GLY N 0.0735186 0.001316575 . . 122 185 ASP N 0.071723149 0.002649518 . . 123 186 PHE N 0.076597831 0.001724812 . . 124 188 ARG N 0.065019929 0.001280319 . . 125 189 GLU N 0.069833378 0.001137432 . . 126 191 ALA N 0.065537671 0.001267505 . . 127 192 ASP N 0.06535606 0.001353301 . . 128 193 LEU N 0.082922865 0.001975427 . . 129 194 GLU N 0.069652434 0.001643222 . . 130 195 MET N 0.07056416 0.00075692 . . 131 196 ASN N 0.068739388 0.001047691 . . 132 198 THR N 0.187938131 0.007286671 . . 133 199 VAL N 0.178759765 0.019189481 . . 134 202 ARG N 0.242494786 0.019690264 . . 135 203 ARG N 0.155395326 0.011079894 . . 136 204 ALA N 0.167492965 0.010382842 . . 137 205 SER N 0.218727444 0.016223921 . . 138 206 GLU N 0.203591351 0.009546463 . . 139 207 ILE N 0.248855266 0.011839747 . . 140 208 ILE N 0.254310564 0.021963057 . . 141 209 SER N 0.160934709 0.01148503 . . 142 211 ALA N 0.28534741 0.015088221 . . 143 213 ALA N 0.26347684 0.015175596 . . 144 214 THR N 0.329804426 0.027134466 . . 145 216 THR N 0.151947973 0.012312281 . . 146 219 ARG N 0.151745068 0.015848952 . . 147 222 ASP N 0.058429645 0.001583198 . . 148 223 TYR N 0.052924614 0.001117171 . . 149 224 ALA N 0.06472073 0.00122928 . . 150 225 VAL N 0.06717947 0.001078052 . . 151 226 ALA N 0.068273833 0.001635704 . . 152 227 GLY N 0.071447454 0.001065707 . . 153 228 ASN N 0.067412246 0.001156518 . . 154 230 VAL N 0.074338941 0.001755873 . . 155 231 ALA N 0.076175966 0.002052931 . . 156 232 PHE N 0.085596651 0.0016162 . . 157 233 ARG N 0.071660958 0.000902717 . . 158 235 SER N 0.08241713 0.00281765 . . 159 237 LEU N 0.077232005 0.002039333 . . 160 238 GLN N 0.067187594 0.002110554 . . 161 239 ALA N 0.076793119 0.001427824 . . 162 240 GLY N 0.065577641 0.00127577 . . 163 241 ILE N 0.065997888 0.001229003 . . 164 242 VAL N 0.074534532 0.002017562 . . 165 243 TYR N 0.073553208 0.001469486 . . 166 244 GLY N 0.073696312 0.001063335 . . 167 246 ARG N 0.102758025 0.002022041 . . 168 247 ARG N 0.11003279 0.002849316 . . 169 248 THR N 0.098531875 0.002056567 . . 170 249 GLN N 0.095273483 0.001759256 . . 171 250 ILE N 0.113897811 0.003217407 . . 172 251 SER N 0.075640677 0.002881844 . . 173 252 SER N 0.094182356 0.003627677 . . 174 255 PHE N 0.088278395 0.007117786 . . 175 257 VAL N 0.062168564 0.001330757 . . 176 258 GLY N 0.067191206 0.001585531 . . 177 259 VAL N 0.063625779 0.002472006 . . 178 260 SER N 0.063666287 0.001709855 . . 179 261 ARG N 0.070217816 0.001470883 . . 180 262 ARG N 0.080624355 0.001353609 . . stop_ save_ save_heteronucl_NOE_list_1 _Saveframe_category heteronuclear_NOE _Details ; HNOE measurements were measured by the steady-state m ethod, (????????) using standard water flip-back methods [Grzesiek, S., and Bax, A. (1993) J. Am. Chem. Soc. 115, 12594.]. Spectra were recorded as 128 x 512 complex matrices, with spectral widths of 8385 (1H) and 2200 (15N) Hz. Six sets of spectra were calculated with and without 1H saturation to allow for estimation of experimental uncertainties. ; loop_ _Software_label $software_1 $software_2 stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 599.7 _Mol_system_component_name EcCdtB-II _Atom_one_atom_name H _Atom_two_atom_name N _Heteronuclear_NOE_value_type 'relative intensities' _NOE_reference_value 1.0 _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 12 ASP 0.816446825 0.056210884 13 LEU 0.797995813 0.117324552 16 PHE 0.465826195 0.038488546 17 ARG 0.648012793 0.093061092 18 VAL 0.879714288 0.022082199 19 ALA 0.746767723 0.060518201 20 THR 0.542224678 0.061028379 21 TRP 1.070881646 0.067758647 23 LEU 0.681038177 0.109871049 25 GLY 0.710693644 0.157597216 27 SER 0.68876627 0.041924162 29 THR 0.815711918 0.054543361 35 ASN 0.636509777 0.065794274 41 LEU 0.562896346 0.029250373 42 ILE 0.863024172 0.067743399 43 SER 0.852971099 0.05979209 44 GLY 0.569352874 0.081244102 45 GLU 0.460018277 0.040726308 46 ASN 0.794260146 0.164463916 47 ALA 0.658744722 0.036090413 49 ASP 0.943571033 0.112730593 50 ILE 0.595407636 0.043713447 51 LEU 0.736545162 0.115322883 52 ALA 0.608953581 0.048235832 53 VAL 0.677798883 0.027068206 55 GLU 0.49082917 0.03691833 56 ALA 0.97732785 0.061112252 62 THR 0.68475485 0.035929859 63 ALA 0.773241308 0.112564382 64 VAL 0.808372784 0.048023688 65 ASP 0.572847998 0.049818952 66 THR 0.972007887 0.074399831 67 GLY 0.687323359 0.070120664 68 ARG 0.761601369 0.036420885 69 VAL 0.840125292 0.052194279 70 ILE 1.07483769 0.064754124 72 SER 0.692677961 0.038240682 74 GLY 0.472695165 0.017656809 75 ILE 0.625587332 0.108683244 78 ARG 1.158728093 0.09095966 79 GLU 0.653878105 0.089900637 80 LEU 0.865773174 0.125646408 84 LEU 0.564462056 0.096269847 85 SER 0.516234437 0.029930657 86 THR 0.591890589 0.0654021 89 ARG 0.588231713 0.050606322 91 GLN 0.515645149 0.057116876 92 GLN 0.525505964 0.061412937 96 TYR 0.538468605 0.059123981 100 VAL 0.936021322 0.059671077 101 ASP 0.649963906 0.106748598 103 LEU 0.326475692 0.020394514 104 GLY 0.50294481 0.038126897 105 GLY 0.65754386 0 107 VAL 0.634550125 0.109034473 111 LEU 0.71612146 0.126283101 112 VAL 0.588075364 0.061437109 113 SER 1.204047037 0.103789702 116 ARG 0.797672545 0.047377524 117 ALA 0.528776904 0.080931544 118 ASP 0.646984709 0.056225251 119 GLU 0.81045183 0.021594932 120 VAL 0.593430037 0.054778878 121 PHE 0.642953627 0.066070392 122 VAL 0.742396383 0.043474021 123 LEU 0.721334077 0.040467795 124 SER 0.691209335 0.031951198 126 VAL 0.589777598 0.061737351 127 ARG 0.736267716 0.026169044 128 GLN 0.824681151 0.109109957 130 GLY 0.608299762 0.019264444 131 ARG 0.729293268 0.092706213 133 LEU 0.663566411 0.066714465 134 LEU 0.630835455 0.047357948 135 GLY 0.894508003 0.080332503 136 ILE 0.728686898 0.105079988 138 ILE 0.899627417 0.059691771 139 GLY 0.885142891 0.123103143 140 ASN 0.848483793 0.057166005 142 ALA 0.737001578 0.051960777 143 PHE 0.95552304 0.060487054 144 PHE 0.847520735 0.156691588 145 THR 0.816653577 0.056278428 146 ALA 0.741001799 0.053924846 147 HIS 0.924606733 0.044057568 148 ALA 0.51972687 0.049028622 149 ILE 0.610482523 0.048650229 150 ALA 1.097525024 0.072346383 151 MET 0.765224291 0.032749228 152 ARG 0.733422937 0.081613189 153 ASN 0.773383697 0.063645088 154 ASN 0.944142312 0.059450137 155 ASP 0.665365173 0.045831323 156 ALA 0.804384931 0.049330818 158 ALA 0.840689049 0.054853952 159 LEU 0.845570892 0.02261012 160 VAL 0.610690316 0.054984709 161 GLU 0.582757424 0.053879249 162 GLU 0.835789227 0.046768135 163 VAL 0.639094358 0.056065787 165 ASN 0.815948639 0.033049738 167 PHE 0.82811742 0.057354092 168 ARG 0.925137729 0.047827737 169 ASP 0.63129354 0.040135929 170 SER 0.853310662 0.059971265 171 ARG 0.84024859 0.060850923 172 ASP 0.767680254 0.057413854 174 VAL 0.891645533 0.060483121 176 GLN 1.12918654 0.067901318 177 ALA 0.727372957 0.064792376 178 LEU 0.645584786 0.047016413 179 ASN 0.665191439 0.074178845 180 TRP 0.823642314 0.0355951 181 MET 1.035511807 0.104902858 182 ILE 0.773841435 0.088322388 183 LEU 0.741135674 0.086119493 184 GLY 0.923913408 0.06949045 185 ASP 0.762810573 0.121464917 186 PHE 0.67547175 0.084797898 188 ARG 0.755425567 0.109440756 189 GLU 0.695497159 0.044226875 191 ALA 0.921201569 0.049447898 192 ASP 0.581135788 0.05560608 193 LEU 0.656245654 0.035499299 194 GLU 0.966697967 0.035998824 195 MET 1.081116124 0.045601262 196 ASN 0.614091635 0.048356559 198 THR 0.541310222 0.078213038 199 VAL 0.496406084 0.068898359 202 ARG 0.552433834 0.087347879 205 SER 0.68024186 0.104772313 206 GLU 0.270790018 0.033274298 208 ILE 0.784058192 0.098125178 212 ALA 0.878278032 0.134485046 222 ASP 0.692926783 0.033255612 223 TYR 1.055416069 0.061773447 224 ALA 0.927432624 0.071567924 225 VAL 0.604389489 0.060825393 226 ALA 1.124319874 0.051242839 227 GLY 1.046916875 0.083610003 228 ASN 0.910730858 0.054281022 230 VAL 0.662560425 0.063597892 231 ALA 1.068246021 0.082997306 232 PHE 0.62004721 0.044483585 233 ARG 1.105480883 0.106631515 235 SER 0.532350592 0.079219963 237 LEU 0.792120106 0.090003466 238 GLN 0.639443167 0.036634172 239 ALA 0.895684237 0.039439207 240 GLY 0.932923498 0.080426256 241 ILE 0.711537804 0.04767282 242 VAL 0.889285805 0.121863596 243 TYR 0.387521908 0.057035057 244 GLY 0.558896558 0.035498121 246 ARG 0.675314156 0.04341416 247 ARG 0.506667965 0.031587496 248 THR 0.581948365 0.070973329 249 GLN 0.464122904 0.018671246 250 ILE 0.353053091 0.044896928 251 SER 0.910973269 0.23383137 252 SER 0.584284466 0.066851307 253 ASP 0.51577704 0.017094253 255 PHE 0.75429954 0.064729437 257 VAL 1.044316163 0.045264278 258 GLY 0.90554735 0.049020949 259 VAL 0.838470076 0.056896941 260 SER 0.67449899 0.043266595 261 ARG 1.182189421 0.064082523 262 ARG 0.55175365 0.05416986 stop_ save_