data_5863 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone HN, N, Ca, C and Cb chemical shift assignments and Secondary Structure of FkpA, a 245-residue peptidyl- prolyl cis/trans isomerase with chaperone activity ; _BMRB_accession_number 5863 _BMRB_flat_file_name bmr5863.str _Entry_type original _Submission_date 2003-07-08 _Accession_date 2003-07-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hu Kaifeng . . 2 Pluckthun Andreas . . 3 Pervushin Konstantin . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 219 "13C chemical shifts" 685 "15N chemical shifts" 219 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-13 original author . stop_ _Original_release_date 2004-02-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone HN, N, CA, C' and CB chemical shift assignments and Secondary Structure of FkpA, a 245-residue peptidyl- prolyl cis/trans isomerase with chaperone activity ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14872134 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hu Kaifeng . . 2 Pluckthun Andreas . . 3 Pervushin Konstantin . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 28 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 405 _Page_last 406 _Year 2004 _Details . loop_ _Keyword FkpA sFkpA 'NMR backbone assignments' 'peptidyl-prolyl cis/trans isomerase (PPIase)' 'molecular chaperone' 'FKBP domain' MIP 'Macrophage Infectivity Potentiator' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Kathrin Ramm, A.P., The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA. II. ISOMERASE-INDEPENDENT CHAPERONE ACTIVITY IN VITRO. J. Biol. Chem., 2000. 275: p. 17106-17113. ; _Citation_title 'The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10748201 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ramm K. . . 2 Pluckthun A. . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 275 _Journal_issue 22 _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 17106 _Page_last 17113 _Year 2000 _Details ; We recently identified FkpA by selecting for the increased yield of antibody single-chain Fv (scFv) fragments in phage display, even of those not containing cis-prolines. We have now investigated the properties of FkpA in vitro. The peptidylprolyl cis-trans-isomerase activity of FkpA was found to be among the highest of any such enzyme with a protein substrate, yet FkpA is not able to enhance the proline-limited refolding rate of the disulfide-free hu4D5-8 scFv fragment, probably due to inaccessibility of Pro-L95. Nevertheless, the yield of the soluble and functional scFv fragment was dramatically increased in vitro in the presence of FkpA. Similar effects were observed for an scFv fragment devoid of cis-prolines. We are thus forced to conclude that the observed folding-assisting function is independent of the isomerase activity of the protein. The beneficial effect of FkpA was found to be due to two components. First, FkpA interacts with early folding intermediates, thus preventing their aggregation. Additionally, it has the ability to reactivate inactive protein, possibly also by binding to a partially unfolded species that may exist in equilibrium with the aggregated form, which may thus be released on a productive pathway. These in vitro measurements therefore fully reflect the in vivo results from periplasmic overexpression of FkpA. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Kathrin Ramm, A.P., High Enzymatic Activity and Chaperone Function are Mechanistically Related Features of the Dimeric E. coli Peptidyl-prolyl-isomerase FkpA. Journal of Molecular Biology, 2001. 310(2): p. 485-498. ; _Citation_title 'High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11428902 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ramm K. . . 2 Pluckthun A. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 310 _Journal_issue 2 _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 485 _Page_last 498 _Year 2001 _Details ; We have recently described the existence of a chaperone activity for the dimeric peptidyl-prolyl cis/trans isomerase FkpA from the periplasm of Escherichia coli that is independent of its isomerase activity. We have now investigated the molecular mechanism of these two activities in vitro in greater detail. The isomerase activity with a protein substrate (RNaseT1) is characterized by a 100-fold higher k(cat)/K(M) value than with a short tetrapeptide substrate. This enhanced activity with a protein is due to an increased affinity towards the protein substrate mediated by a polypeptide-binding site that is distinct from the active site. The chaperone activity is also mediated by interaction of folding and unfolding intermediates with a binding site that is most likely identical to the polypeptide-binding site which enhances catalysis. Both activities are thus mechanistically related, being based on the transient interaction with this high-affinity polypeptide-binding site. Only the isomerase activity, but not the chaperone activity, with the substrate citrate synthase can be inhibited by FK520. Experiments with the isolated domains of FkpA imply that both the isomerase and the chaperone site are located on the highly conserved FKBP domain. The additional amino-terminal domain mediates the dimerization and thus places the two active sites of the FKBP domains in juxtaposition, such that they can simultaneously interact with a protein, and this is required for full catalytic activity. ; save_ ################################## # Molecular system description # ################################## save_system_FkpA _Saveframe_category molecular_system _Mol_system_name FkpA _Abbreviation_common FkpA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'FkpA, chain 1' $FkpA 'FkpA, chain 2' $FkpA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'FkpA, chain 1' 1 'FkpA, chain 2' stop_ loop_ _Biological_function 'peptidyl-prolyl cis/trans isomerase(PPIase)' 'molecular chaperone' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FkpA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common FkpA _Abbreviation_common FkpA _Molecular_mass 26223 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 245 _Mol_residue_sequence ; AEAAKPATAADSKAAFKNDD QKSAYALGASLGRYMENSLK EQEKLGIKLDKDQLIAGVQD AFADKSKLSDQEIEQTLQAF EARVKSSAQAKMEKDAADNE AKGKEYREKFAKEKGVKTSS TGLVYQVVEAGKGEAPKDSD TVVVNYKGTLIDGKEFDNSY TRGEPLSFRLDGVIPGWTEG LKNIKKGGKIKLVIPPELAY GKAGVPGIPPNSTLVFDVEL LDVKPAPKADAKPEADAKAA DSAKK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLU 3 ALA 4 ALA 5 LYS 6 PRO 7 ALA 8 THR 9 ALA 10 ALA 11 ASP 12 SER 13 LYS 14 ALA 15 ALA 16 PHE 17 LYS 18 ASN 19 ASP 20 ASP 21 GLN 22 LYS 23 SER 24 ALA 25 TYR 26 ALA 27 LEU 28 GLY 29 ALA 30 SER 31 LEU 32 GLY 33 ARG 34 TYR 35 MET 36 GLU 37 ASN 38 SER 39 LEU 40 LYS 41 GLU 42 GLN 43 GLU 44 LYS 45 LEU 46 GLY 47 ILE 48 LYS 49 LEU 50 ASP 51 LYS 52 ASP 53 GLN 54 LEU 55 ILE 56 ALA 57 GLY 58 VAL 59 GLN 60 ASP 61 ALA 62 PHE 63 ALA 64 ASP 65 LYS 66 SER 67 LYS 68 LEU 69 SER 70 ASP 71 GLN 72 GLU 73 ILE 74 GLU 75 GLN 76 THR 77 LEU 78 GLN 79 ALA 80 PHE 81 GLU 82 ALA 83 ARG 84 VAL 85 LYS 86 SER 87 SER 88 ALA 89 GLN 90 ALA 91 LYS 92 MET 93 GLU 94 LYS 95 ASP 96 ALA 97 ALA 98 ASP 99 ASN 100 GLU 101 ALA 102 LYS 103 GLY 104 LYS 105 GLU 106 TYR 107 ARG 108 GLU 109 LYS 110 PHE 111 ALA 112 LYS 113 GLU 114 LYS 115 GLY 116 VAL 117 LYS 118 THR 119 SER 120 SER 121 THR 122 GLY 123 LEU 124 VAL 125 TYR 126 GLN 127 VAL 128 VAL 129 GLU 130 ALA 131 GLY 132 LYS 133 GLY 134 GLU 135 ALA 136 PRO 137 LYS 138 ASP 139 SER 140 ASP 141 THR 142 VAL 143 VAL 144 VAL 145 ASN 146 TYR 147 LYS 148 GLY 149 THR 150 LEU 151 ILE 152 ASP 153 GLY 154 LYS 155 GLU 156 PHE 157 ASP 158 ASN 159 SER 160 TYR 161 THR 162 ARG 163 GLY 164 GLU 165 PRO 166 LEU 167 SER 168 PHE 169 ARG 170 LEU 171 ASP 172 GLY 173 VAL 174 ILE 175 PRO 176 GLY 177 TRP 178 THR 179 GLU 180 GLY 181 LEU 182 LYS 183 ASN 184 ILE 185 LYS 186 LYS 187 GLY 188 GLY 189 LYS 190 ILE 191 LYS 192 LEU 193 VAL 194 ILE 195 PRO 196 PRO 197 GLU 198 LEU 199 ALA 200 TYR 201 GLY 202 LYS 203 ALA 204 GLY 205 VAL 206 PRO 207 GLY 208 ILE 209 PRO 210 PRO 211 ASN 212 SER 213 THR 214 LEU 215 VAL 216 PHE 217 ASP 218 VAL 219 GLU 220 LEU 221 LEU 222 ASP 223 VAL 224 LYS 225 PRO 226 ALA 227 PRO 228 LYS 229 ALA 230 ASP 231 ALA 232 LYS 233 PRO 234 GLU 235 ALA 236 ASP 237 ALA 238 LYS 239 ALA 240 ALA 241 ASP 242 SER 243 ALA 244 LYS 245 LYS 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 1Q6H "Crystal Structure Of A Truncated Form Of Fkpa From Escherichia Coli" 91.43 224 99.11 99.11 1.72e-153 PDB 1Q6I "Crystal Structure Of A Truncated Form Of Fkpa From Escherichia Coli, In Complex With Immunosuppressant Fk506" 91.43 224 99.11 99.11 1.72e-153 PDB 1Q6U "Crystal Structure Of Fkpa From Escherichia Coli" 100.00 245 100.00 100.00 2.75e-170 DBJ BAB37621 "FKBP-type peptidyl-prolyl cis-trans isomerase [Escherichia coli O157:H7 str. Sakai]" 100.00 270 99.59 99.59 5.27e-170 DBJ BAE77944 "FKBP-type peptidyl-prolyl cis-trans isomerase [Escherichia coli str. K-12 substr. W3110]" 100.00 270 100.00 100.00 1.14e-170 DBJ BAG79132 "peptidyl-prolyl cis-trans isomerase [Escherichia coli SE11]" 100.00 270 99.59 99.59 5.27e-170 DBJ BAI27605 "FKBP-type peptidyl-prolyl cis-trans isomerase [Escherichia coli O26:H11 str. 11368]" 100.00 270 99.59 99.59 5.27e-170 DBJ BAI32775 "FKBP-type peptidyl-prolyl cis-trans isomerase [Escherichia coli O103:H2 str. 12009]" 100.00 270 99.59 99.59 5.27e-170 EMBL CAP77799 "FKBP-type peptidyl-prolyl cis-trans isomerase fkpA [Escherichia coli LF82]" 100.00 270 99.18 99.59 1.77e-169 EMBL CAQ33666 "peptidyl-prolyl cis-trans isomerase; in protein folding [Escherichia coli BL21(DE3)]" 100.00 270 99.59 99.59 5.27e-170 EMBL CAR00285 "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Escherichia coli IAI1]" 100.00 270 99.59 99.59 5.27e-170 EMBL CAR04951 "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Escherichia coli S88]" 100.00 270 99.59 99.59 5.27e-170 EMBL CAR10001 "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Escherichia coli ED1a]" 100.00 270 99.18 99.59 1.77e-169 GB AAA58144 "ORF_f270 [Escherichia coli str. K-12 substr. MG1655]" 100.00 270 100.00 100.00 1.14e-170 GB AAC41459 "fkpA [Escherichia coli]" 100.00 270 100.00 100.00 1.14e-170 GB AAC76372 "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Escherichia coli str. K-12 substr. MG1655]" 100.00 270 100.00 100.00 1.14e-170 GB AAG58454 "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Escherichia coli O157:H7 str. EDL933]" 100.00 270 99.18 99.18 5.12e-169 GB AAN44828 "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Shigella flexneri 2a str. 301]" 100.00 270 99.18 99.59 9.82e-170 REF NP_289894 "FKBP-type peptidylprolyl isomerase [Escherichia coli O157:H7 str. EDL933]" 100.00 270 99.18 99.18 5.12e-169 REF NP_312225 "FKBP-type peptidylprolyl isomerase [Escherichia coli O157:H7 str. Sakai]" 100.00 270 99.59 99.59 5.27e-170 REF NP_417806 "FKBP-type peptidyl-prolyl cis-trans isomerase (rotamase) [Escherichia coli str. K-12 substr. MG1655]" 100.00 270 100.00 100.00 1.14e-170 REF NP_709121 "FKBP-type peptidylprolyl isomerase [Shigella flexneri 2a str. 301]" 100.00 270 99.18 99.59 9.82e-170 REF NP_755985 "FKBP-type peptidyl-prolyl cis-trans isomerase [Escherichia coli CFT073]" 100.00 270 99.59 99.59 5.27e-170 SP P45523 "RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase FkpA; Short=PPIase; AltName: Full=Rotamase; Flags: Precursor [Esche" 100.00 270 100.00 100.00 1.14e-170 SP P65764 "RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase FkpA; Short=PPIase; AltName: Full=Rotamase; Flags: Precursor [Esche" 100.00 270 99.59 99.59 5.27e-170 SP P65765 "RecName: Full=FKBP-type peptidyl-prolyl cis-trans isomerase FkpA; Short=PPIase; AltName: Full=Rotamase; Flags: Precursor [Esche" 100.00 270 99.59 99.59 5.27e-170 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $FkpA 'E. coli' 562 Eubacteria . Escherichia coli SB536 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 $FkpA 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLysS . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $FkpA 0.6 mM 0.5 1.0 '[U-99% 13C; U-99% 15N; U-98% 2H]' 'Mes buffer' 20 mM . . . NaCl 50 mM . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $FkpA 0.5 mM 0.4 0.8 '[U-99% 13C; U-99% 15N; U-98% 2H]' 'Mes buffer' 20 mM . . . NaCl 20 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_Bruker_Avance_600_MHz_spectrometer_equipped_with_a_TXI_cryogenic_probehead._1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Bruker Avance 600 MHz spectrometer equipped with a TXI cryogenic probehead.' _Sample_label . save_ save_3D_TROSY-versions_of_HNCA,_HNCACB,_HNCO_and_HN(CA)CO_run_in_the_high_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-versions of HNCA, HNCACB, HNCO and HN(CA)CO run in the high' _Sample_label . save_ save_resolution_mode,_utilizing_both_N->C_and_C->N_polarization_transfer_periods_to_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'resolution mode, utilizing both N->C and C->N polarization transfer periods to' _Sample_label . save_ save_maximize_spectral_resolution_along_the_15N_dimension._4 _Saveframe_category NMR_applied_experiment _Experiment_name 'maximize spectral resolution along the 15N dimension.' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_4 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_4 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_4 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_4 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_1 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_2 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_3 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_4 _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details ; The sample was equilibrated under these conditions before the spectra were collected. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 n/a temperature 310 1 K 'ionic strength' 0.02 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'FkpA, chain 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 . 2 GLU CA C 55.50 0.1 1 2 . 2 GLU C C 176.132 0.1 1 3 . 2 GLU CB C 29.20 0.1 1 4 . 3 ALA H H 8.415 0.02 1 5 . 3 ALA N N 126.499 0.1 1 6 . 3 ALA CA C 51.62 0.1 1 7 . 3 ALA C C 177.357 0.1 1 8 . 3 ALA CB C 18.52 0.1 1 9 . 4 ALA H H 8.239 0.02 1 10 . 4 ALA N N 124.187 0.1 1 11 . 4 ALA CA C 51.62 0.1 1 12 . 4 ALA C C 177.478 0.1 1 13 . 4 ALA CB C 18.52 0.1 1 14 . 5 LYS H H 8.255 0.02 1 15 . 5 LYS N N 122.645 0.1 1 16 . 5 LYS CA C 53.50 0.1 1 17 . 5 LYS C C 174.725 0.1 1 18 . 5 LYS CB C 31.47 0.1 1 19 . 6 PRO CA C 62.32 0.1 1 20 . 6 PRO C C 176.835 0.1 1 21 . 6 PRO CB C 30.92 0.1 1 22 . 7 ALA H H 8.412 0.02 1 23 . 7 ALA N N 124.958 0.1 1 24 . 7 ALA CA C 52.06 0.1 1 25 . 7 ALA C C 178.101 0.1 1 26 . 7 ALA CB C 18.41 0.1 1 27 . 8 THR H H 8.042 0.02 1 28 . 8 THR N N 113.589 0.1 1 29 . 8 THR CA C 60.59 0.1 1 30 . 8 THR C C 174.565 0.1 1 31 . 8 THR CB C 69.56 0.1 1 32 . 9 ALA H H 8.280 0.02 1 33 . 9 ALA N N 126.692 0.1 1 34 . 9 ALA CA C 52.29 0.1 1 35 . 9 ALA C C 177.799 0.1 1 36 . 9 ALA CB C 18.41 0.1 1 37 . 10 ALA H H 8.132 0.02 1 38 . 10 ALA N N 122.969 0.1 1 39 . 10 ALA CA C 52.29 0.1 1 40 . 10 ALA C C 177.853 0.1 1 41 . 10 ALA CB C 18.41 0.1 1 42 . 11 ASP H H 8.075 0.02 1 43 . 11 ASP N N 119.376 0.1 1 44 . 11 ASP CA C 53.76 0.1 1 45 . 11 ASP C C 176.427 0.1 1 46 . 11 ASP CB C 40.47 0.1 1 47 . 12 SER H H 8.129 0.02 1 48 . 12 SER N N 117.190 0.1 1 49 . 12 SER CA C 58.40 0.1 1 50 . 12 SER C C 174.920 0.1 1 51 . 12 SER CB C 62.72 0.1 1 52 . 13 LYS H H 8.257 0.02 1 53 . 13 LYS N N 123.279 0.1 1 54 . 13 LYS CA C 55.96 0.1 1 55 . 13 LYS C C 176.487 0.1 1 56 . 13 LYS CB C 31.56 0.1 1 57 . 14 ALA H H 7.957 0.02 1 58 . 14 ALA N N 124.520 0.1 1 59 . 14 ALA CA C 51.73 0.1 1 60 . 14 ALA C C 177.150 0.1 1 61 . 14 ALA CB C 18.32 0.1 1 62 . 15 ALA H H 7.845 0.02 1 63 . 15 ALA N N 123.539 0.1 1 64 . 15 ALA CA C 52.00 0.1 1 65 . 15 ALA C C 176.929 0.1 1 66 . 15 ALA CB C 18.95 0.1 1 67 . 16 PHE H H 7.721 0.02 1 68 . 16 PHE N N 116.683 0.1 1 69 . 16 PHE CA C 56.46 0.1 1 70 . 16 PHE C C 176.246 0.1 1 71 . 16 PHE CB C 40.42 0.1 1 72 . 17 LYS H H 8.705 0.02 1 73 . 17 LYS N N 121.974 0.1 1 74 . 17 LYS CA C 57.24 0.1 1 75 . 17 LYS C C 176.266 0.1 1 76 . 17 LYS CB C 33.01 0.1 1 77 . 18 ASN H H 7.439 0.02 1 78 . 18 ASN N N 110.636 0.1 1 79 . 18 ASN CA C 51.87 0.1 1 80 . 18 ASN C C 175.663 0.1 1 81 . 18 ASN CB C 39.49 0.1 1 82 . 19 ASP H H 8.764 0.02 1 83 . 19 ASP N N 120.076 0.1 1 84 . 19 ASP CA C 56.71 0.1 1 85 . 19 ASP C C 178.456 0.1 1 86 . 19 ASP CB C 40.15 0.1 1 87 . 20 ASP H H 8.327 0.02 1 88 . 20 ASP N N 123.946 0.1 1 89 . 20 ASP CA C 57.47 0.1 1 90 . 20 ASP C C 179.862 0.1 1 91 . 20 ASP CB C 39.10 0.1 1 92 . 21 GLN H H 8.205 0.02 1 93 . 21 GLN N N 121.498 0.1 1 94 . 21 GLN CA C 59.19 0.1 1 95 . 21 GLN C C 177.110 0.1 1 96 . 21 GLN CB C 29.42 0.1 1 97 . 22 LYS H H 7.445 0.02 1 98 . 22 LYS N N 119.533 0.1 1 99 . 22 LYS CA C 59.19 0.1 1 100 . 22 LYS C C 178.134 0.1 1 101 . 22 LYS CB C 32.25 0.1 1 102 . 23 SER H H 8.252 0.02 1 103 . 23 SER N N 114.546 0.1 1 104 . 23 SER CA C 62.40 0.1 1 105 . 23 SER C C 174.599 0.1 1 106 . 24 ALA H H 7.086 0.02 1 107 . 24 ALA N N 122.514 0.1 1 108 . 24 ALA CA C 54.68 0.1 1 109 . 24 ALA C C 178.174 0.1 1 110 . 24 ALA CB C 19.41 0.1 1 111 . 25 TYR H H 7.854 0.02 1 112 . 25 TYR N N 118.596 0.1 1 113 . 25 TYR CA C 61.28 0.1 1 114 . 25 TYR C C 177.973 0.1 1 115 . 25 TYR CB C 38.50 0.1 1 116 . 26 ALA H H 8.502 0.02 1 117 . 26 ALA N N 120.034 0.1 1 118 . 26 ALA CA C 55.03 0.1 1 119 . 26 ALA C C 178.978 0.1 1 120 . 26 ALA CB C 17.35 0.1 1 121 . 27 LEU H H 8.073 0.02 1 122 . 27 LEU N N 120.009 0.1 1 123 . 27 LEU CA C 57.99 0.1 1 124 . 27 LEU C C 175.081 0.1 1 125 . 27 LEU CB C 40.87 0.1 1 126 . 28 GLY H H 8.104 0.02 1 127 . 28 GLY N N 108.026 0.1 1 128 . 28 GLY CA C 47.46 0.1 1 129 . 28 GLY C C 175.041 0.1 1 130 . 29 ALA H H 9.907 0.02 1 131 . 29 ALA N N 125.526 0.1 1 132 . 29 ALA CA C 53.98 0.1 1 133 . 29 ALA C C 180.364 0.1 1 134 . 29 ALA CB C 16.85 0.1 1 135 . 31 LEU CA C 57.60 0.1 1 136 . 31 LEU C C 179.480 0.1 1 137 . 32 GLY H H 8.982 0.02 1 138 . 32 GLY N N 107.901 0.1 1 139 . 32 GLY CA C 47.34 0.1 1 140 . 32 GLY C C 175.302 0.1 1 141 . 33 ARG H H 8.531 0.02 1 142 . 33 ARG N N 122.429 0.1 1 143 . 33 ARG CA C 58.02 0.1 1 144 . 33 ARG C C 178.717 0.1 1 145 . 33 ARG CB C 28.57 0.1 1 146 . 34 TYR H H 7.933 0.02 1 147 . 34 TYR N N 121.439 0.1 1 148 . 34 TYR CA C 61.15 0.1 1 149 . 34 TYR C C 177.110 0.1 1 150 . 34 TYR CB C 37.95 0.1 1 151 . 36 GLU CA C 55.78 0.1 1 152 . 36 GLU C C 176.667 0.1 1 153 . 36 GLU CB C 32.38 0.1 1 154 . 37 ASN H H 8.265 0.02 1 155 . 37 ASN N N 121.695 0.1 1 156 . 37 ASN CA C 54.04 0.1 1 157 . 37 ASN C C 176.507 0.1 1 158 . 37 ASN CB C 40.87 0.1 1 159 . 38 SER H H 8.806 0.02 1 160 . 38 SER N N 115.562 0.1 1 161 . 38 SER CA C 58.06 0.1 1 162 . 38 SER C C 174.478 0.1 1 163 . 38 SER CB C 63.69 0.1 1 164 . 39 LEU H H 8.263 0.02 1 165 . 39 LEU N N 122.609 0.1 1 166 . 39 LEU CA C 54.44 0.1 1 167 . 39 LEU C C 176.366 0.1 1 168 . 39 LEU CB C 40.88 0.1 1 169 . 40 LYS H H 8.134 0.02 1 170 . 40 LYS N N 121.908 0.1 1 171 . 40 LYS CA C 56.55 0.1 1 172 . 40 LYS C C 180.284 0.1 1 173 . 40 LYS CB C 29.42 0.1 1 174 . 42 GLN CA C 58.08 0.1 1 175 . 42 GLN C C 177.15 0.1 1 176 . 42 GLN CB C 28.56 0.1 1 177 . 43 GLU H H 8.339 0.02 1 178 . 43 GLU N N 121.905 0.1 1 179 . 43 GLU CA C 59.51 0.1 1 180 . 43 GLU C C 181.288 0.1 1 181 . 43 GLU CB C 32.58 0.1 1 182 . 44 LYS H H 7.446 0.02 1 183 . 44 LYS N N 120.324 0.1 1 184 . 44 LYS CA C 58.60 0.1 1 185 . 44 LYS C C 177.893 0.1 1 186 . 44 LYS CB C 31.59 0.1 1 187 . 45 LEU H H 7.390 0.02 1 188 . 45 LEU N N 117.073 0.1 1 189 . 45 LEU CA C 53.82 0.1 1 190 . 45 LEU C C 177.190 0.1 1 191 . 45 LEU CB C 41.66 0.1 1 192 . 46 GLY H H 7.839 0.02 1 193 . 46 GLY N N 107.025 0.1 1 194 . 46 GLY CA C 44.91 0.1 1 195 . 46 GLY C C 173.835 0.1 1 196 . 47 ILE H H 7.507 0.02 1 197 . 47 ILE N N 123.157 0.1 1 198 . 47 ILE CA C 60.37 0.1 1 199 . 47 ILE C C 174.177 0.1 1 200 . 47 ILE CB C 38.24 0.1 1 201 . 48 LYS H H 8.572 0.02 1 202 . 48 LYS N N 130.391 0.1 1 203 . 48 LYS CA C 54.17 0.1 1 204 . 48 LYS C C 175.422 0.1 1 205 . 48 LYS CB C 32.18 0.1 1 206 . 49 LEU H H 8.359 0.02 1 207 . 49 LEU N N 124.658 0.1 1 208 . 49 LEU CA C 53.47 0.1 1 209 . 49 LEU C C 176.333 0.1 1 210 . 49 LEU CB C 42.52 0.1 1 211 . 50 ASP H H 7.721 0.02 1 212 . 50 ASP N N 121.278 0.1 1 213 . 50 ASP CA C 53.62 0.1 1 214 . 50 ASP C C 176.875 0.1 1 215 . 50 ASP CB C 41.66 0.1 1 216 . 51 LYS H H 8.606 0.02 1 217 . 51 LYS N N 128.494 0.1 1 218 . 51 LYS CA C 59.44 0.1 1 219 . 51 LYS C C 177.893 0.1 1 220 . 51 LYS CB C 31.85 0.1 1 221 . 52 ASP H H 8.157 0.02 1 222 . 52 ASP N N 118.621 0.1 1 223 . 52 ASP CA C 56.94 0.1 1 224 . 52 ASP C C 180.163 0.1 1 225 . 52 ASP CB C 39.62 0.1 1 226 . 53 GLN H H 7.780 0.02 1 227 . 53 GLN N N 120.259 0.1 1 228 . 53 GLN CA C 56.94 0.1 1 229 . 53 GLN C C 177.672 0.1 1 230 . 53 GLN CB C 28.29 0.1 1 231 . 54 LEU H H 7.356 0.02 1 232 . 54 LEU N N 121.773 0.1 1 233 . 54 LEU CA C 58.45 0.1 1 234 . 54 LEU C C 179.153 0.1 1 235 . 54 LEU CB C 41.73 0.1 1 236 . 55 ILE H H 7.624 0.02 1 237 . 55 ILE N N 117.478 0.1 1 238 . 55 ILE CA C 62.74 0.1 1 239 . 55 ILE C C 177.391 0.1 1 240 . 55 ILE CB C 36.46 0.1 1 241 . 56 ALA H H 7.694 0.02 1 242 . 56 ALA N N 124.378 0.1 1 243 . 56 ALA CA C 54.88 0.1 1 244 . 56 ALA C C 179.460 0.1 1 245 . 56 ALA CB C 18.70 0.1 1 246 . 57 GLY H H 7.924 0.02 1 247 . 57 GLY N N 106.179 0.1 1 248 . 57 GLY CA C 46.48 0.1 1 249 . 57 GLY C C 175.683 0.1 1 250 . 58 VAL H H 7.368 0.02 1 251 . 58 VAL N N 121.445 0.1 1 252 . 58 VAL CA C 66.15 0.1 1 253 . 58 VAL C C 177.833 0.1 1 254 . 58 VAL CB C 31.07 0.1 1 255 . 59 GLN H H 8.299 0.02 1 256 . 59 GLN N N 117.300 0.1 1 257 . 59 GLN CA C 58.92 0.1 1 258 . 59 GLN C C 179.922 0.1 1 259 . 59 GLN CB C 28.23 0.1 1 260 . 60 ASP H H 8.997 0.02 1 261 . 60 ASP N N 120.502 0.1 1 262 . 60 ASP CA C 56.45 0.1 1 263 . 60 ASP C C 179.239 0.1 1 264 . 60 ASP CB C 38.61 0.1 1 265 . 61 ALA H H 8.079 0.02 1 266 . 61 ALA N N 122.915 0.1 1 267 . 61 ALA CA C 55.10 0.1 1 268 . 61 ALA C C 181.449 0.1 1 269 . 61 ALA CB C 18.98 0.1 1 270 . 62 PHE H H 8.144 0.02 1 271 . 62 PHE N N 118.938 0.1 1 272 . 62 PHE CA C 59.24 0.1 1 273 . 62 PHE C C 176.145 0.1 1 274 . 62 PHE CB C 38.24 0.1 1 275 . 63 ALA H H 7.368 0.02 1 276 . 63 ALA N N 119.906 0.1 1 277 . 63 ALA CA C 50.94 0.1 1 278 . 63 ALA C C 176.145 0.1 1 279 . 63 ALA CB C 19.01 0.1 1 280 . 64 ASP H H 7.866 0.02 1 281 . 64 ASP N N 117.809 0.1 1 282 . 64 ASP CA C 54.92 0.1 1 283 . 64 ASP C C 175.422 0.1 1 284 . 64 ASP CB C 38.93 0.1 1 285 . 65 LYS H H 8.409 0.02 1 286 . 65 LYS N N 117.759 0.1 1 287 . 65 LYS CA C 53.99 0.1 1 288 . 65 LYS C C 176.306 0.1 1 289 . 65 LYS CB C 32.52 0.1 1 290 . 66 SER H H 8.806 0.02 1 291 . 66 SER N N 114.176 0.1 1 292 . 66 SER CA C 58.93 0.1 1 293 . 66 SER C C 177.933 0.1 1 294 . 66 SER CB C 63.87 0.1 1 295 . 67 LYS H H 9.236 0.02 1 296 . 67 LYS N N 127.530 0.1 1 297 . 67 LYS CA C 57.55 0.1 1 298 . 67 LYS C C 175.603 0.1 1 299 . 67 LYS CB C 32.76 0.1 1 300 . 68 LEU H H 7.670 0.02 1 301 . 68 LEU N N 116.018 0.1 1 302 . 68 LEU CA C 51.95 0.1 1 303 . 68 LEU C C 176.909 0.1 1 304 . 68 LEU CB C 45.31 0.1 1 305 . 69 SER H H 9.526 0.02 1 306 . 69 SER N N 121.647 0.1 1 307 . 69 SER CA C 56.60 0.1 1 308 . 69 SER C C 174.297 0.1 1 309 . 69 SER CB C 64.24 0.1 1 310 . 70 ASP H H 9.036 0.02 1 311 . 70 ASP N N 122.332 0.1 1 312 . 70 ASP CA C 57.93 0.1 1 313 . 70 ASP C C 179.159 0.1 1 314 . 70 ASP CB C 38.67 0.1 1 315 . 71 GLN H H 8.422 0.02 1 316 . 71 GLN N N 119.872 0.1 1 317 . 71 GLN CA C 59.18 0.1 1 318 . 71 GLN C C 178.456 0.1 1 319 . 71 GLN CB C 27.83 0.1 1 320 . 72 GLU H H 7.763 0.02 1 321 . 72 GLU N N 121.054 0.1 1 322 . 72 GLU CA C 59.02 0.1 1 323 . 72 GLU C C 181.228 0.1 1 324 . 72 GLU CB C 30.17 0.1 1 325 . 73 ILE H H 8.864 0.02 1 326 . 73 ILE N N 124.615 0.1 1 327 . 73 ILE CA C 66.95 0.1 1 328 . 73 ILE C C 177.029 0.1 1 329 . 73 ILE CB C 37.45 0.1 1 330 . 74 GLU H H 7.793 0.02 1 331 . 74 GLU N N 119.579 0.1 1 332 . 74 GLU CA C 59.44 0.1 1 333 . 74 GLU C C 179.641 0.1 1 334 . 74 GLU CB C 28.94 0.1 1 335 . 75 GLN H H 8.275 0.02 1 336 . 75 GLN N N 118.235 0.1 1 337 . 75 GLN CA C 58.71 0.1 1 338 . 75 GLN C C 179.641 0.1 1 339 . 75 GLN CB C 28.30 0.1 1 340 . 76 THR H H 8.249 0.02 1 341 . 76 THR N N 118.525 0.1 1 342 . 76 THR CA C 66.95 0.1 1 343 . 76 THR C C 177.270 0.1 1 344 . 76 THR CB C 67.82 0.1 1 345 . 77 LEU H H 8.665 0.02 1 346 . 77 LEU N N 123.367 0.1 1 347 . 77 LEU CA C 57.99 0.1 1 348 . 77 LEU C C 179.601 0.1 1 349 . 77 LEU CB C 39.82 0.1 1 350 . 78 GLN H H 8.230 0.02 1 351 . 78 GLN N N 120.946 0.1 1 352 . 78 GLN CA C 59.18 0.1 1 353 . 78 GLN C C 179.440 0.1 1 354 . 78 GLN CB C 27.58 0.1 1 355 . 79 ALA H H 7.632 0.02 1 356 . 79 ALA N N 123.004 0.1 1 357 . 79 ALA CA C 54.36 0.1 1 358 . 79 ALA C C 180.525 0.1 1 359 . 79 ALA CB C 16.71 0.1 1 360 . 80 PHE H H 8.441 0.02 1 361 . 80 PHE N N 122.389 0.1 1 362 . 80 PHE CA C 60.94 0.1 1 363 . 80 PHE C C 176.893 0.1 1 364 . 80 PHE CB C 38.50 0.1 1 365 . 81 GLU H H 8.620 0.02 1 366 . 81 GLU N N 119.880 0.1 1 367 . 81 GLU CA C 59.24 0.1 1 368 . 81 GLU C C 178.964 0.1 1 369 . 81 GLU CB C 28.56 0.1 1 370 . 82 ALA H H 7.470 0.02 1 371 . 82 ALA N N 120.846 0.1 1 372 . 82 ALA CA C 54.44 0.1 1 373 . 82 ALA C C 180.344 0.1 1 374 . 82 ALA CB C 17.10 0.1 1 375 . 83 ARG H H 7.866 0.02 1 376 . 83 ARG N N 120.469 0.1 1 377 . 83 ARG CA C 58.60 0.1 1 378 . 83 ARG C C 175.081 0.1 1 379 . 83 ARG CB C 31.92 0.1 1 380 . 84 VAL CA C 62.73 0.1 1 381 . 84 VAL C C 177.082 0.1 1 382 . 84 VAL CB C 31.32 0.1 1 383 . 85 LYS H H 8.324 0.02 1 384 . 85 LYS N N 122.125 0.1 1 385 . 85 LYS CA C 55.82 0.1 1 386 . 85 LYS C C 176.808 0.1 1 387 . 85 LYS CB C 32.45 0.1 1 388 . 86 SER H H 7.720 0.02 1 389 . 86 SER N N 122.088 0.1 1 390 . 86 SER CA C 59.18 0.1 1 391 . 86 SER C C 175.904 0.1 1 392 . 86 SER CB C 64.58 0.1 1 393 . 87 SER H H 7.836 0.02 1 394 . 87 SER N N 123.600 0.1 1 395 . 87 SER CA C 59.44 0.1 1 396 . 87 SER CB C 64.68 0.1 1 397 . 89 GLN CA C 55.43 0.1 1 398 . 89 GLN C C 176.045 0.1 1 399 . 89 GLN CB C 30.08 0.1 1 400 . 90 ALA H H 8.229 0.02 1 401 . 90 ALA N N 127.066 0.1 1 402 . 90 ALA CA C 50.29 0.1 1 403 . 90 ALA C C 175.543 0.1 1 404 . 90 ALA CB C 17.89 0.1 1 405 . 91 LYS CA C 57.27 0.1 1 406 . 91 LYS C C 177.872 0.1 1 407 . 91 LYS CB C 32.05 0.1 1 408 . 92 MET H H 8.042 0.02 1 409 . 92 MET N N 122.297 0.1 1 410 . 92 MET CA C 53.99 0.1 1 411 . 92 MET C C 178.636 0.1 1 412 . 92 MET CB C 29.68 0.1 1 413 . 93 GLU H H 8.312 0.02 1 414 . 93 GLU N N 125.429 0.1 1 415 . 93 GLU CA C 56.02 0.1 1 416 . 93 GLU C C 176.748 0.1 1 417 . 93 GLU CB C 32.25 0.1 1 418 . 94 LYS H H 8.317 0.02 1 419 . 94 LYS N N 121.370 0.1 1 420 . 94 LYS CA C 56.68 0.1 1 421 . 94 LYS C C 177.411 0.1 1 422 . 94 LYS CB C 29.55 0.1 1 423 . 95 ASP H H 8.323 0.02 1 424 . 95 ASP N N 121.026 0.1 1 425 . 95 ASP CA C 55.23 0.1 1 426 . 95 ASP C C 177.307 0.1 1 427 . 95 ASP CB C 40.48 0.1 1 428 . 96 ALA H H 7.927 0.02 1 429 . 96 ALA N N 123.648 0.1 1 430 . 96 ALA CA C 52.92 0.1 1 431 . 96 ALA C C 178.556 0.1 1 432 . 96 ALA CB C 18.29 0.1 1 433 . 97 ALA H H 7.992 0.02 1 434 . 97 ALA N N 122.757 0.1 1 435 . 97 ALA CA C 52.92 0.1 1 436 . 97 ALA C C 181.148 0.1 1 437 . 97 ALA CB C 18.29 0.1 1 438 . 98 ASP H H 8.564 0.02 1 439 . 98 ASP N N 122.188 0.1 1 440 . 98 ASP CA C 56.90 0.1 1 441 . 98 ASP C C 178.889 0.1 1 442 . 98 ASP CB C 40.35 0.1 1 443 . 99 ASN H H 8.567 0.02 1 444 . 99 ASN N N 119.478 0.1 1 445 . 99 ASN CA C 55.76 0.1 1 446 . 99 ASN C C 179.139 0.1 1 447 . 99 ASN CB C 41.53 0.1 1 448 . 100 GLU H H 7.953 0.02 1 449 . 100 GLU N N 122.777 0.1 1 450 . 100 GLU CA C 57.74 0.1 1 451 . 100 GLU C C 178.436 0.1 1 452 . 100 GLU CB C 28.33 0.1 1 453 . 101 ALA H H 7.995 0.02 1 454 . 101 ALA N N 124.733 0.1 1 455 . 101 ALA CA C 55.06 0.1 1 456 . 101 ALA C C 181.409 0.1 1 457 . 101 ALA CB C 18.80 0.1 1 458 . 102 LYS H H 8.365 0.02 1 459 . 102 LYS N N 118.805 0.1 1 460 . 102 LYS CA C 58.62 0.1 1 461 . 102 LYS C C 180.806 0.1 1 462 . 102 LYS CB C 32.12 0.1 1 463 . 103 GLY H H 8.654 0.02 1 464 . 103 GLY N N 110.723 0.1 1 465 . 103 GLY CA C 47.57 0.1 1 466 . 103 GLY C C 175.583 0.1 1 467 . 104 LYS H H 8.495 0.02 1 468 . 104 LYS N N 124.346 0.1 1 469 . 104 LYS CA C 60.08 0.1 1 470 . 104 LYS C C 178.476 0.1 1 471 . 104 LYS CB C 32.15 0.1 1 472 . 105 GLU H H 7.443 0.02 1 473 . 105 GLU N N 118.201 0.1 1 474 . 105 GLU CA C 59.18 0.1 1 475 . 105 GLU C C 178.837 0.1 1 476 . 105 GLU CB C 29.06 0.1 1 477 . 106 TYR H H 8.006 0.02 1 478 . 106 TYR N N 120.298 0.1 1 479 . 106 TYR CA C 61.67 0.1 1 480 . 106 TYR C C 178.837 0.1 1 481 . 106 TYR CB C 38.69 0.1 1 482 . 107 ARG H H 8.837 0.02 1 483 . 107 ARG N N 118.979 0.1 1 484 . 107 ARG CA C 60.41 0.1 1 485 . 107 ARG C C 178.054 0.1 1 486 . 107 ARG CB C 29.43 0.1 1 487 . 108 GLU H H 8.249 0.02 1 488 . 108 GLU N N 118.131 0.1 1 489 . 108 GLU CA C 59.05 0.1 1 490 . 108 GLU C C 179.139 0.1 1 491 . 108 GLU CB C 28.82 0.1 1 492 . 109 LYS H H 7.689 0.02 1 493 . 109 LYS N N 119.611 0.1 1 494 . 109 LYS CA C 58.98 0.1 1 495 . 109 LYS C C 180.083 0.1 1 496 . 109 LYS CB C 32.39 0.1 1 497 . 110 PHE H H 8.201 0.02 1 498 . 110 PHE N N 122.907 0.1 1 499 . 110 PHE CA C 59.98 0.1 1 500 . 110 PHE C C 176.527 0.1 1 501 . 110 PHE CB C 38.81 0.1 1 502 . 111 ALA H H 7.850 0.02 1 503 . 111 ALA N N 115.790 0.1 1 504 . 111 ALA CA C 53.25 0.1 1 505 . 111 ALA C C 177.913 0.1 1 506 . 111 ALA CB C 17.97 0.1 1 507 . 112 LYS H H 6.931 0.02 1 508 . 112 LYS N N 114.894 0.1 1 509 . 112 LYS CA C 55.62 0.1 1 510 . 112 LYS C C 177.719 0.1 1 511 . 112 LYS CB C 32.15 0.1 1 512 . 113 GLU H H 7.513 0.02 1 513 . 113 GLU N N 121.289 0.1 1 514 . 113 GLU CA C 56.05 0.1 1 515 . 113 GLU C C 176.855 0.1 1 516 . 113 GLU CB C 28.26 0.1 1 517 . 114 LYS H H 8.305 0.02 1 518 . 114 LYS N N 122.934 0.1 1 519 . 114 LYS CA C 57.38 0.1 1 520 . 114 LYS C C 178.315 0.1 1 521 . 114 LYS CB C 31.03 0.1 1 522 . 115 GLY H H 8.664 0.02 1 523 . 115 GLY N N 112.887 0.1 1 524 . 115 GLY CA C 44.54 0.1 1 525 . 115 GLY C C 173.795 0.1 1 526 . 116 VAL H H 7.199 0.02 1 527 . 116 VAL N N 122.641 0.1 1 528 . 116 VAL CA C 62.36 0.1 1 529 . 116 VAL C C 175.784 0.1 1 530 . 116 VAL CB C 30.03 0.1 1 531 . 117 LYS H H 8.525 0.02 1 532 . 117 LYS N N 128.197 0.1 1 533 . 117 LYS CA C 53.62 0.1 1 534 . 117 LYS C C 174.117 0.1 1 535 . 117 LYS CB C 34.13 0.1 1 536 . 118 THR H H 7.972 0.02 1 537 . 118 THR N N 114.295 0.1 1 538 . 118 THR CA C 60.45 0.1 1 539 . 118 THR C C 175.523 0.1 1 540 . 118 THR CB C 69.79 0.1 1 541 . 119 SER H H 9.447 0.02 1 542 . 119 SER N N 123.376 0.1 1 543 . 119 SER CA C 55.72 0.1 1 544 . 119 SER C C 177.190 0.1 1 545 . 119 SER CB C 64.02 0.1 1 546 . 120 SER H H 8.874 0.02 1 547 . 120 SER N N 120.618 0.1 1 548 . 120 SER CA C 60.94 0.1 1 549 . 120 SER C C 175.801 0.1 1 550 . 120 SER CB C 62.88 0.1 1 551 . 121 THR H H 8.245 0.02 1 552 . 121 THR N N 112.968 0.1 1 553 . 121 THR CA C 62.03 0.1 1 554 . 121 THR C C 175.764 0.1 1 555 . 121 THR CB C 68.67 0.1 1 556 . 122 GLY H H 7.697 0.02 1 557 . 122 GLY N N 108.236 0.1 1 558 . 122 GLY CA C 43.43 0.1 1 559 . 122 GLY C C 173.815 0.1 1 560 . 123 LEU H H 7.397 0.02 1 561 . 123 LEU N N 122.138 0.1 1 562 . 123 LEU CA C 56.16 0.1 1 563 . 123 LEU C C 174.297 0.1 1 564 . 123 LEU CB C 41.10 0.1 1 565 . 124 VAL H H 8.161 0.02 1 566 . 124 VAL N N 129.166 0.1 1 567 . 124 VAL CA C 60.37 0.1 1 568 . 124 VAL C C 175.282 0.1 1 569 . 124 VAL CB C 33.58 0.1 1 570 . 125 TYR H H 9.271 0.02 1 571 . 125 TYR N N 121.853 0.1 1 572 . 125 TYR CA C 55.12 0.1 1 573 . 125 TYR C C 172.088 0.1 1 574 . 125 TYR CB C 41.93 0.1 1 575 . 126 GLN H H 9.245 0.02 1 576 . 126 GLN N N 121.940 0.1 1 577 . 126 GLN CA C 53.17 0.1 1 578 . 126 GLN C C 175.081 0.1 1 579 . 126 GLN CB C 33.10 0.1 1 580 . 127 VAL H H 9.228 0.02 1 581 . 127 VAL N N 130.022 0.1 1 582 . 127 VAL CA C 64.76 0.1 1 583 . 127 VAL C C 175.322 0.1 1 584 . 127 VAL CB C 30.79 0.1 1 585 . 128 VAL H H 8.350 0.02 1 586 . 128 VAL N N 133.431 0.1 1 587 . 128 VAL CA C 64.30 0.1 1 588 . 128 VAL C C 176.427 0.1 1 589 . 128 VAL CB C 31.92 0.1 1 590 . 129 GLU H H 7.997 0.02 1 591 . 129 GLU N N 119.621 0.1 1 592 . 129 GLU CA C 55.10 0.1 1 593 . 129 GLU C C 175.623 0.1 1 594 . 129 GLU CB C 32.58 0.1 1 595 . 130 ALA H H 8.778 0.02 1 596 . 130 ALA N N 127.876 0.1 1 597 . 130 ALA CA C 55.10 0.1 1 598 . 130 ALA C C 179.038 0.1 1 599 . 130 ALA CB C 19.12 0.1 1 600 . 131 GLY H H 8.156 0.02 1 601 . 131 GLY N N 102.901 0.1 1 602 . 131 GLY CA C 43.65 0.1 1 603 . 131 GLY C C 172.891 0.1 1 604 . 132 LYS H H 8.455 0.02 1 605 . 132 LYS N N 118.403 0.1 1 606 . 132 LYS CA C 55.27 0.1 1 607 . 132 LYS C C 175.061 0.1 1 608 . 132 LYS CB C 34.72 0.1 1 609 . 133 GLY H H 8.298 0.02 1 610 . 133 GLY N N 110.750 0.1 1 611 . 133 GLY CA C 44.16 0.1 1 612 . 133 GLY C C 172.831 0.1 1 613 . 134 GLU H H 8.439 0.02 1 614 . 134 GLU N N 123.723 0.1 1 615 . 134 GLU CA C 54.94 0.1 1 616 . 134 GLU C C 176.145 0.1 1 617 . 134 GLU CB C 30.14 0.1 1 618 . 135 ALA H H 8.370 0.02 1 619 . 135 ALA N N 125.737 0.1 1 620 . 135 ALA CA C 49.22 0.1 1 621 . 135 ALA C C 176.085 0.1 1 622 . 135 ALA CB C 17.42 0.1 1 623 . 136 PRO CA C 62.11 0.1 1 624 . 136 PRO C C 174.799 0.1 1 625 . 136 PRO CB C 31.90 0.1 1 626 . 137 LYS H H 9.005 0.02 1 627 . 137 LYS N N 121.001 0.1 1 628 . 137 LYS CA C 53.43 0.1 1 629 . 137 LYS C C 177.270 0.1 1 630 . 137 LYS CB C 33.73 0.1 1 631 . 138 ASP H H 8.097 0.02 1 632 . 138 ASP N N 118.305 0.1 1 633 . 138 ASP CA C 58.22 0.1 1 634 . 138 ASP C C 174.558 0.1 1 635 . 138 ASP CB C 41.52 0.1 1 636 . 139 SER H H 7.212 0.02 1 637 . 139 SER N N 105.375 0.1 1 638 . 139 SER CA C 57.30 0.1 1 639 . 139 SER C C 174.799 0.1 1 640 . 139 SER CB C 63.47 0.1 1 641 . 140 ASP H H 7.857 0.02 1 642 . 140 ASP N N 123.327 0.1 1 643 . 140 ASP CA C 54.72 0.1 1 644 . 140 ASP C C 176.246 0.1 1 645 . 140 ASP CB C 40.55 0.1 1 646 . 141 THR H H 8.367 0.02 1 647 . 141 THR N N 117.126 0.1 1 648 . 141 THR CA C 62.25 0.1 1 649 . 141 THR C C 173.654 0.1 1 650 . 141 THR CB C 69.00 0.1 1 651 . 142 VAL H H 8.815 0.02 1 652 . 142 VAL N N 120.985 0.1 1 653 . 142 VAL CA C 57.82 0.1 1 654 . 142 VAL C C 172.992 0.1 1 655 . 142 VAL CB C 32.47 0.1 1 656 . 143 VAL H H 7.597 0.02 1 657 . 143 VAL N N 121.669 0.1 1 658 . 143 VAL CA C 60.42 0.1 1 659 . 143 VAL C C 176.929 0.1 1 660 . 143 VAL CB C 32.58 0.1 1 661 . 144 VAL H H 9.233 0.02 1 662 . 144 VAL N N 118.600 0.1 1 663 . 144 VAL CA C 58.01 0.1 1 664 . 144 VAL C C 175.362 0.1 1 665 . 144 VAL CB C 34.90 0.1 1 666 . 145 ASN H H 8.308 0.02 1 667 . 145 ASN N N 117.545 0.1 1 668 . 145 ASN CA C 51.16 0.1 1 669 . 145 ASN C C 174.446 0.1 1 670 . 145 ASN CB C 41.75 0.1 1 671 . 146 TYR H H 8.824 0.02 1 672 . 146 TYR N N 115.912 0.1 1 673 . 146 TYR CA C 56.20 0.1 1 674 . 146 TYR C C 171.826 0.1 1 675 . 146 TYR CB C 41.88 0.1 1 676 . 147 LYS H H 8.595 0.02 1 677 . 147 LYS N N 118.287 0.1 1 678 . 147 LYS CA C 55.05 0.1 1 679 . 147 LYS C C 175.121 0.1 1 680 . 147 LYS CB C 35.46 0.1 1 681 . 148 GLY H H 8.783 0.02 1 682 . 148 GLY N N 113.896 0.1 1 683 . 148 GLY CA C 44.54 0.1 1 684 . 148 GLY C C 172.067 0.1 1 685 . 149 THR H H 9.404 0.02 1 686 . 149 THR N N 117.969 0.1 1 687 . 149 THR CA C 58.71 0.1 1 688 . 149 THR C C 174.217 0.1 1 689 . 149 THR CB C 71.66 0.1 1 690 . 150 LEU H H 8.494 0.02 1 691 . 150 LEU N N 120.194 0.1 1 692 . 150 LEU CA C 53.06 0.1 1 693 . 150 LEU C C 181.529 0.1 1 694 . 150 LEU CB C 39.89 0.1 1 695 . 151 ILE H H 9.383 0.02 1 696 . 151 ILE N N 116.639 0.1 1 697 . 151 ILE CA C 64.35 0.1 1 698 . 151 ILE C C 176.668 0.1 1 699 . 151 ILE CB C 36.45 0.1 1 700 . 152 ASP H H 7.528 0.02 1 701 . 152 ASP N N 119.117 0.1 1 702 . 152 ASP CA C 52.73 0.1 1 703 . 152 ASP C C 177.391 0.1 1 704 . 152 ASP CB C 39.44 0.1 1 705 . 153 GLY H H 7.961 0.02 1 706 . 153 GLY N N 108.475 0.1 1 707 . 153 GLY CA C 44.09 0.1 1 708 . 153 GLY C C 174.337 0.1 1 709 . 154 LYS H H 7.818 0.02 1 710 . 154 LYS N N 122.658 0.1 1 711 . 154 LYS CA C 56.60 0.1 1 712 . 154 LYS C C 176.266 0.1 1 713 . 154 LYS CB C 31.35 0.1 1 714 . 155 GLU H H 8.621 0.02 1 715 . 155 GLU N N 128.245 0.1 1 716 . 155 GLU CA C 56.31 0.1 1 717 . 155 GLU C C 176.607 0.1 1 718 . 155 GLU CB C 31.07 0.1 1 719 . 156 PHE CA C 56.03 0.1 1 720 . 156 PHE C C 174.860 0.1 1 721 . 157 ASP H H 7.056 0.02 1 722 . 157 ASP N N 120.588 0.1 1 723 . 157 ASP CA C 54.39 0.1 1 724 . 157 ASP C C 174.799 0.1 1 725 . 157 ASP CB C 42.88 0.1 1 726 . 158 ASN H H 8.159 0.02 1 727 . 158 ASN N N 122.313 0.1 1 728 . 158 ASN CA C 52.95 0.1 1 729 . 158 ASN C C 175.462 0.1 1 730 . 158 ASN CB C 38.56 0.1 1 731 . 159 SER H H 8.824 0.02 1 732 . 159 SER N N 122.019 0.1 1 733 . 159 SER CA C 60.48 0.1 1 734 . 159 SER C C 176.427 0.1 1 735 . 159 SER CB C 61.81 0.1 1 736 . 160 TYR H H 8.298 0.02 1 737 . 160 TYR N N 126.039 0.1 1 738 . 160 TYR CA C 60.55 0.1 1 739 . 160 TYR C C 180.163 0.1 1 740 . 160 TYR CB C 35.01 0.1 1 741 . 161 THR H H 7.615 0.02 1 742 . 161 THR N N 112.801 0.1 1 743 . 161 THR CA C 64.02 0.1 1 744 . 161 THR C C 176.306 0.1 1 745 . 161 THR CB C 67.63 0.1 1 746 . 162 ARG H H 7.098 0.02 1 747 . 162 ARG N N 119.417 0.1 1 748 . 162 ARG CA C 57.27 0.1 1 749 . 162 ARG C C 177.652 0.1 1 750 . 162 ARG CB C 30.14 0.1 1 751 . 163 GLY H H 7.609 0.02 1 752 . 163 GLY N N 106.252 0.1 1 753 . 163 GLY CA C 45.20 0.1 1 754 . 163 GLY C C 173.333 0.1 1 755 . 164 GLU H H 7.091 0.02 1 756 . 164 GLU N N 118.622 0.1 1 757 . 164 GLU CA C 52.51 0.1 1 758 . 164 GLU C C 172.690 0.1 1 759 . 164 GLU CB C 31.25 0.1 1 760 . 165 PRO CA C 62.22 0.1 1 761 . 165 PRO C C 175.864 0.1 1 762 . 165 PRO CB C 31.94 0.1 1 763 . 166 LEU H H 8.635 0.02 1 764 . 166 LEU N N 123.531 0.1 1 765 . 166 LEU CA C 53.72 0.1 1 766 . 166 LEU C C 175.241 0.1 1 767 . 166 LEU CB C 44.77 0.1 1 768 . 167 SER H H 8.196 0.02 1 769 . 167 SER N N 118.810 0.1 1 770 . 167 SER CA C 55.71 0.1 1 771 . 167 SER C C 174.317 0.1 1 772 . 167 SER CB C 64.12 0.1 1 773 . 168 PHE H H 8.323 0.02 1 774 . 168 PHE N N 120.701 0.1 1 775 . 168 PHE CA C 55.71 0.1 1 776 . 168 PHE C C 173.675 0.1 1 777 . 168 PHE CB C 40.28 0.1 1 778 . 169 ARG H H 8.502 0.02 1 779 . 169 ARG N N 122.823 0.1 1 780 . 169 ARG CA C 55.59 0.1 1 781 . 169 ARG C C 179.380 0.1 1 782 . 169 ARG CB C 30.40 0.1 1 783 . 170 LEU H H 8.582 0.02 1 784 . 170 LEU N N 128.739 0.1 1 785 . 170 LEU CA C 58.49 0.1 1 786 . 170 LEU C C 176.587 0.1 1 787 . 170 LEU CB C 40.00 0.1 1 788 . 171 ASP H H 8.089 0.02 1 789 . 171 ASP N N 115.723 0.1 1 790 . 171 ASP CA C 53.17 0.1 1 791 . 171 ASP C C 177.210 0.1 1 792 . 171 ASP CB C 38.67 0.1 1 793 . 172 GLY H H 8.355 0.02 1 794 . 172 GLY N N 107.452 0.1 1 795 . 172 GLY CA C 44.98 0.1 1 796 . 172 GLY C C 174.498 0.1 1 797 . 173 VAL H H 6.563 0.02 1 798 . 173 VAL N N 112.230 0.1 1 799 . 173 VAL CA C 59.24 0.1 1 800 . 173 VAL C C 174.840 0.1 1 801 . 173 VAL CB C 33.76 0.1 1 802 . 174 ILE H H 6.899 0.02 1 803 . 174 ILE N N 111.716 0.1 1 804 . 174 ILE CA C 59.55 0.1 1 805 . 174 ILE C C 175.683 0.1 1 806 . 174 ILE CB C 38.85 0.1 1 807 . 175 PRO CA C 65.08 0.1 1 808 . 175 PRO C C 179.862 0.1 1 809 . 175 PRO CB C 34.49 0.1 1 810 . 176 GLY H H 9.005 0.02 1 811 . 176 GLY N N 102.748 0.1 1 812 . 176 GLY CA C 47.43 0.1 1 813 . 176 GLY C C 175.724 0.1 1 814 . 177 TRP H H 7.837 0.02 1 815 . 177 TRP N N 120.861 0.1 1 816 . 177 TRP CA C 60.00 0.1 1 817 . 177 TRP C C 176.909 0.1 1 818 . 177 TRP CB C 30.40 0.1 1 819 . 178 THR H H 7.740 0.02 1 820 . 178 THR N N 117.664 0.1 1 821 . 178 THR CA C 66.70 0.1 1 822 . 178 THR C C 174.458 0.1 1 823 . 178 THR CB C 68.68 0.1 1 824 . 179 GLU H H 7.954 0.02 1 825 . 179 GLU N N 115.739 0.1 1 826 . 179 GLU CA C 57.86 0.1 1 827 . 179 GLU C C 179.741 0.1 1 828 . 179 GLU CB C 29.43 0.1 1 829 . 180 GLY H H 7.616 0.02 1 830 . 180 GLY N N 105.544 0.1 1 831 . 180 GLY CA C 48.10 0.1 1 832 . 180 GLY C C 175.503 0.1 1 833 . 181 LEU H H 8.407 0.02 1 834 . 181 LEU N N 118.451 0.1 1 835 . 181 LEU CA C 56.31 0.1 1 836 . 181 LEU C C 175.663 0.1 1 837 . 181 LEU CB C 39.67 0.1 1 838 . 182 LYS H H 6.592 0.02 1 839 . 182 LYS N N 112.379 0.1 1 840 . 182 LYS CA C 58.15 0.1 1 841 . 182 LYS C C 177.049 0.1 1 842 . 182 LYS CB C 31.47 0.1 1 843 . 183 ASN H H 7.201 0.02 1 844 . 183 ASN N N 113.727 0.1 1 845 . 183 ASN CA C 53.94 0.1 1 846 . 183 ASN C C 174.016 0.1 1 847 . 183 ASN CB C 39.00 0.1 1 848 . 184 ILE H H 7.304 0.02 1 849 . 184 ILE N N 112.996 0.1 1 850 . 184 ILE CA C 59.48 0.1 1 851 . 184 ILE C C 171.585 0.1 1 852 . 184 ILE CB C 42.65 0.1 1 853 . 185 LYS H H 7.550 0.02 1 854 . 185 LYS N N 114.742 0.1 1 855 . 185 LYS CA C 53.06 0.1 1 856 . 185 LYS C C 175.985 0.1 1 857 . 185 LYS CB C 34.13 0.1 1 858 . 186 LYS H H 7.935 0.02 1 859 . 186 LYS N N 120.881 0.1 1 860 . 186 LYS CA C 60.04 0.1 1 861 . 186 LYS C C 176.306 0.1 1 862 . 186 LYS CB C 32.12 0.1 1 863 . 187 GLY H H 8.703 0.02 1 864 . 187 GLY N N 116.318 0.1 1 865 . 187 GLY CA C 44.54 0.1 1 866 . 187 GLY C C 175.583 0.1 1 867 . 188 GLY H H 8.876 0.02 1 868 . 188 GLY N N 109.924 0.1 1 869 . 188 GLY CA C 44.20 0.1 1 870 . 188 GLY C C 171.907 0.1 1 871 . 189 LYS H H 9.260 0.02 1 872 . 189 LYS N N 118.737 0.1 1 873 . 189 LYS CA C 54.83 0.1 1 874 . 189 LYS C C 174.980 0.1 1 875 . 189 LYS CB C 36.56 0.1 1 876 . 190 ILE H H 9.310 0.02 1 877 . 190 ILE N N 125.344 0.1 1 878 . 190 ILE CA C 58.60 0.1 1 879 . 190 ILE C C 170.641 0.1 1 880 . 190 ILE CB C 42.77 0.1 1 881 . 191 LYS H H 8.853 0.02 1 882 . 191 LYS N N 129.418 0.1 1 883 . 191 LYS CA C 54.27 0.1 1 884 . 191 LYS C C 175.703 0.1 1 885 . 191 LYS CB C 33.46 0.1 1 886 . 192 LEU H H 9.613 0.02 1 887 . 192 LEU N N 125.557 0.1 1 888 . 192 LEU CA C 52.88 0.1 1 889 . 192 LEU C C 174.599 0.1 1 890 . 192 LEU CB C 44.86 0.1 1 891 . 193 VAL H H 9.517 0.02 1 892 . 193 VAL N N 125.988 0.1 1 893 . 193 VAL CA C 61.89 0.1 1 894 . 193 VAL C C 174.599 0.1 1 895 . 193 VAL CB C 31.40 0.1 1 896 . 194 ILE H H 9.529 0.02 1 897 . 194 ILE N N 126.179 0.1 1 898 . 194 ILE CA C 59.05 0.1 1 899 . 194 ILE C C 173.675 0.1 1 900 . 194 ILE CB C 39.92 0.1 1 901 . 196 PRO CA C 64.24 0.1 1 902 . 196 PRO C C 180.103 0.1 1 903 . 196 PRO CB C 29.70 0.1 1 904 . 197 GLU H H 9.848 0.02 1 905 . 197 GLU N N 119.823 0.1 1 906 . 197 GLU CA C 58.72 0.1 1 907 . 197 GLU C C 177.773 0.1 1 908 . 197 GLU CB C 27.27 0.1 1 909 . 198 LEU H H 7.631 0.02 1 910 . 198 LEU N N 118.891 0.1 1 911 . 198 LEU CA C 52.73 0.1 1 912 . 198 LEU C C 174.498 0.1 1 913 . 198 LEU CB C 41.55 0.1 1 914 . 199 ALA H H 7.708 0.02 1 915 . 199 ALA N N 125.771 0.1 1 916 . 199 ALA CA C 50.96 0.1 1 917 . 199 ALA C C 175.422 0.1 1 918 . 199 ALA CB C 18.07 0.1 1 919 . 200 TYR H H 8.557 0.02 1 920 . 200 TYR N N 122.314 0.1 1 921 . 200 TYR CA C 58.49 0.1 1 922 . 200 TYR C C 176.849 0.1 1 923 . 200 TYR CB C 37.34 0.1 1 924 . 201 GLY H H 8.388 0.02 1 925 . 201 GLY N N 107.879 0.1 1 926 . 201 GLY CA C 45.86 0.1 1 927 . 201 GLY C C 175.041 0.1 1 928 . 202 LYS H H 8.641 0.02 1 929 . 202 LYS N N 125.050 0.1 1 930 . 202 LYS CA C 58.04 0.1 1 931 . 202 LYS C C 176.808 0.1 1 932 . 202 LYS CB C 31.42 0.1 1 933 . 203 ALA H H 8.222 0.02 1 934 . 203 ALA N N 118.599 0.1 1 935 . 203 ALA CA C 52.84 0.1 1 936 . 203 ALA C C 179.862 0.1 1 937 . 203 ALA CB C 18.52 0.1 1 938 . 204 GLY H H 7.290 0.02 1 939 . 204 GLY N N 103.205 0.1 1 940 . 204 GLY CA C 44.29 0.1 1 941 . 204 GLY C C 172.148 0.1 1 942 . 205 VAL H H 7.650 0.02 1 943 . 205 VAL N N 115.072 0.1 1 944 . 205 VAL CA C 58.73 0.1 1 945 . 205 VAL C C 173.353 0.1 1 946 . 205 VAL CB C 31.80 0.1 1 947 . 206 PRO CA C 65.44 0.1 1 948 . 206 PRO C C 177.491 0.1 1 949 . 206 PRO CB C 29.82 0.1 1 950 . 207 GLY H H 8.387 0.02 1 951 . 207 GLY N N 113.556 0.1 1 952 . 207 GLY CA C 44.77 0.1 1 953 . 207 GLY C C 173.474 0.1 1 954 . 208 ILE H H 8.400 0.02 1 955 . 208 ILE N N 121.497 0.1 1 956 . 208 ILE CA C 57.42 0.1 1 957 . 208 ILE C C 173.293 0.1 1 958 . 208 ILE CB C 40.48 0.1 1 959 . 211 ASN CA C 52.83 0.1 1 960 . 211 ASN C C 174.518 0.1 1 961 . 212 SER H H 7.857 0.02 1 962 . 212 SER N N 114.349 0.1 1 963 . 212 SER CA C 60.22 0.1 1 964 . 212 SER C C 174.197 0.1 1 965 . 212 SER CB C 63.12 0.1 1 966 . 213 THR H H 8.663 0.02 1 967 . 213 THR N N 124.841 0.1 1 968 . 213 THR CA C 62.62 0.1 1 969 . 213 THR C C 173.233 0.1 1 970 . 213 THR CB C 68.99 0.1 1 971 . 214 LEU H H 8.416 0.02 1 972 . 214 LEU N N 125.203 0.1 1 973 . 214 LEU CA C 52.34 0.1 1 974 . 214 LEU C C 175.041 0.1 1 975 . 214 LEU CB C 44.50 0.1 1 976 . 215 VAL H H 8.619 0.02 1 977 . 215 VAL N N 122.926 0.1 1 978 . 215 VAL CA C 60.52 0.1 1 979 . 215 VAL C C 176.045 0.1 1 980 . 215 VAL CB C 30.58 0.1 1 981 . 216 PHE H H 9.806 0.02 1 982 . 216 PHE N N 123.407 0.1 1 983 . 216 PHE CA C 55.32 0.1 1 984 . 216 PHE C C 174.880 0.1 1 985 . 216 PHE CB C 43.10 0.1 1 986 . 217 ASP H H 8.740 0.02 1 987 . 217 ASP N N 123.511 0.1 1 988 . 217 ASP CA C 54.08 0.1 1 989 . 217 ASP C C 176.286 0.1 1 990 . 217 ASP CB C 42.87 0.1 1 991 . 218 VAL H H 9.041 0.02 1 992 . 218 VAL N N 123.842 0.1 1 993 . 218 VAL CA C 60.93 0.1 1 994 . 218 VAL C C 174.036 0.1 1 995 . 218 VAL CB C 33.69 0.1 1 996 . 219 GLU H H 9.165 0.02 1 997 . 219 GLU N N 127.974 0.1 1 998 . 219 GLU CA C 54.33 0.1 1 999 . 219 GLU C C 174.558 0.1 1 1000 . 219 GLU CB C 32.11 0.1 1 1001 . 220 LEU H H 8.420 0.02 1 1002 . 220 LEU N N 127.616 0.1 1 1003 . 220 LEU CA C 53.62 0.1 1 1004 . 220 LEU C C 174.634 0.1 1 1005 . 220 LEU CB C 42.14 0.1 1 1006 . 221 LEU H H 8.993 0.02 1 1007 . 221 LEU N N 129.296 0.1 1 1008 . 221 LEU CA C 56.34 0.1 1 1009 . 221 LEU C C 177.933 0.1 1 1010 . 221 LEU CB C 41.90 0.1 1 1011 . 222 ASP H H 7.797 0.02 1 1012 . 222 ASP N N 114.032 0.1 1 1013 . 222 ASP CA C 52.84 0.1 1 1014 . 222 ASP C C 173.634 0.1 1 1015 . 222 ASP CB C 43.10 0.1 1 1016 . 223 VAL H H 8.301 0.02 1 1017 . 223 VAL N N 121.229 0.1 1 1018 . 223 VAL CA C 61.14 0.1 1 1019 . 223 VAL C C 174.337 0.1 1 1020 . 223 VAL CB C 34.46 0.1 1 1021 . 224 LYS H H 9.345 0.02 1 1022 . 224 LYS N N 128.400 0.1 1 1023 . 224 LYS CA C 52.06 0.1 1 1024 . 224 LYS C C 173.233 0.1 1 1025 . 224 LYS CB C 32.47 0.1 1 1026 . 225 PRO CA C 61.68 0.1 1 1027 . 225 PRO C C 177.029 0.1 1 1028 . 225 PRO CB C 31.72 0.1 1 1029 . 226 ALA H H 8.522 0.02 1 1030 . 226 ALA N N 126.294 0.1 1 1031 . 226 ALA CA C 50.16 0.1 1 1032 . 226 ALA C C 176.326 0.1 1 1033 . 226 ALA CB C 17.30 0.1 1 1034 . 227 PRO CA C 62.25 0.1 1 1035 . 227 PRO C C 176.931 0.1 1 1036 . 227 PRO CB C 31.77 0.1 1 1037 . 228 LYS H H 8.264 0.02 1 1038 . 228 LYS N N 122.067 0.1 1 1039 . 228 LYS CA C 55.50 0.1 1 1040 . 228 LYS C C 176.594 0.1 1 1041 . 228 LYS CB C 31.77 0.1 1 1042 . 229 ALA H H 8.320 0.02 1 1043 . 229 ALA N N 126.307 0.1 1 1044 . 229 ALA CA C 51.95 0.1 1 1045 . 229 ALA C C 177.478 0.1 1 1046 . 229 ALA CB C 18.52 0.1 1 1047 . 230 ASP H H 8.201 0.02 1 1048 . 230 ASP N N 119.948 0.1 1 1049 . 230 ASP CA C 53.50 0.1 1 1050 . 230 ASP C C 175.871 0.1 1 1051 . 230 ASP CB C 40.33 0.1 1 1052 . 231 ALA H H 7.989 0.02 1 1053 . 231 ALA N N 124.572 0.1 1 1054 . 231 ALA CA C 51.73 0.1 1 1055 . 231 ALA C C 177.297 0.1 1 1056 . 231 ALA CB C 18.06 0.1 1 1057 . 232 LYS H H 8.238 0.02 1 1058 . 232 LYS N N 122.645 0.1 1 1059 . 232 LYS CA C 53.44 0.1 1 1060 . 232 LYS C C 175.489 0.1 1 1061 . 232 LYS CB C 31.49 0.1 1 1062 . 233 PRO CA C 62.47 0.1 1 1063 . 233 PRO C C 177.277 0.1 1 1064 . 233 PRO CB C 30.87 0.1 1 1065 . 234 GLU H H 8.458 0.02 1 1066 . 234 GLU N N 121.489 0.1 1 1067 . 234 GLU CA C 56.24 0.1 1 1068 . 234 GLU C C 176.634 0.1 1 1069 . 234 GLU CB C 29.25 0.1 1 1070 . 235 ALA H H 8.240 0.02 1 1071 . 235 ALA N N 125.150 0.1 1 1072 . 235 ALA CA C 52.33 0.1 1 1073 . 235 ALA C C 177.739 0.1 1 1074 . 235 ALA CB C 18.41 0.1 1 1075 . 236 ASP H H 8.175 0.02 1 1076 . 236 ASP N N 119.755 0.1 1 1077 . 236 ASP CA C 53.88 0.1 1 1078 . 236 ASP C C 176.574 0.1 1 1079 . 236 ASP CB C 40.38 0.1 1 1080 . 237 ALA H H 8.143 0.02 1 1081 . 237 ALA N N 125.343 0.1 1 1082 . 237 ALA CA C 52.77 0.1 1 1083 . 237 ALA C C 178.442 0.1 1 1084 . 237 ALA CB C 18.11 0.1 1 1085 . 238 LYS H H 8.142 0.02 1 1086 . 238 LYS N N 119.562 0.1 1 1087 . 238 LYS CA C 56.31 0.1 1 1088 . 238 LYS C C 177.237 0.1 1 1089 . 238 LYS CB C 31.46 0.1 1 1090 . 239 ALA H H 8.002 0.02 1 1091 . 239 ALA N N 124.765 0.1 1 1092 . 239 ALA CA C 52.48 0.1 1 1093 . 239 ALA C C 178.422 0.1 1 1094 . 239 ALA CB C 18.33 0.1 1 1095 . 240 ALA H H 8.130 0.02 1 1096 . 240 ALA N N 123.031 0.1 1 1097 . 240 ALA CA C 52.67 0.1 1 1098 . 240 ALA C C 178.322 0.1 1 1099 . 240 ALA CB C 18.06 0.1 1 1100 . 241 ASP H H 8.124 0.02 1 1101 . 241 ASP N N 119.562 0.1 1 1102 . 241 ASP CA C 54.60 0.1 1 1103 . 241 ASP C C 177.056 0.1 1 1104 . 241 ASP CB C 40.47 0.1 1 1105 . 242 SER H H 8.079 0.02 1 1106 . 242 SER N N 116.479 0.1 1 1107 . 242 SER CA C 58.60 0.1 1 1108 . 242 SER C C 175.086 0.1 1 1109 . 242 SER CB C 62.58 0.1 1 1110 . 243 ALA H H 8.066 0.02 1 1111 . 243 ALA N N 124.958 0.1 1 1112 . 243 ALA CA C 52.62 0.1 1 1113 . 243 ALA C C 178.442 0.1 1 1114 . 243 ALA CB C 18.18 0.1 1 1115 . 244 LYS H H 7.813 0.02 1 1116 . 244 LYS N N 118.984 0.1 1 1117 . 244 LYS CA C 56.38 0.1 1 1118 . 244 LYS C C 177.056 0.1 1 1119 . 244 LYS CB C 31.58 0.1 1 1120 . 245 LYS H H 7.878 0.02 1 1121 . 245 LYS N N 120.911 0.1 1 1122 . 245 LYS CA C 56.05 0.1 1 1123 . 245 LYS CB C 31.69 0.1 1 stop_ save_