data_4296 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for E. coli Cold-shock Protein A (CspA) ; _BMRB_accession_number 4296 _BMRB_flat_file_name bmr4296.str _Entry_type original _Submission_date 1999-01-18 _Accession_date 1999-01-19 _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 Feng Wenqing . . 2 Tejero Roberto . . 3 Zimmerman Diane E. . 4 Inouye Masayori . . 5 Montelione Gaetano T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 387 "13C chemical shifts" 244 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-02-10 original author . stop_ _Original_release_date 1999-02-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Feng, W., Tejero, R., Zimmerman, D. E., Inouye, M., and Montelione, G. T., "Solution NMR Structure and Backbone Dynamics of the Major Cold-shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dyanamics in the Single-stranded RNA-binding Site," Biochemistry 37, 10881-10896 (1998). ; _Citation_title ; Solution NMR Structure and Backbone Dynamics of the Major Cold-shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dyanamics in the Single-stranded RNA-binding Site ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98359762 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Feng Wenqing . . 2 Tejero Roberto . . 3 Zimmerman Diane E. . 4 Inouye Masayori . . 5 Montelione Gaetano T. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 37 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10881 _Page_last 10896 _Year 1998 _Details . loop_ _Keyword 'RNA-binding protein' 'DNA-binding protein' '15N relaxation' 'OB fold' 'transcriptional regulation' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Newkirk K., Feng W., Jiang W., Tejero R., Emerson S. D., Inouye M., Montelione G. T., "Solution NMR Structure of the Major Cold Shock Protein (CspA) from Escherichia coli: Identification of a Binding Epitope for DNA," Proc. Natl. Acad. Sci. USA 91, 5114-5118 (1994). ; _Citation_title 'Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7515185 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Newkirk K . . 2 Feng W . . 3 Jiang W . . 4 Tejero R . . 5 Emerson 'S D' D. . 6 Inouye M . . 7 Montelione 'G T' T. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 91 _Journal_issue 11 _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 5114 _Page_last 5118 _Year 1994 _Details ; Sequence-specific 1H and 15N resonance assignments have been determined for the major cold shock protein (CspA) from Escherichia coli with recently developed three-dimensional triple-resonance NMR experiments. By use of these assignments, five antiparallel beta-strands were identified from analysis of NMR data. Strands 1-4 have a classical 3-2-1-4 Greek key beta-sheet topology and there are two beta-bulges, at positions Lys10-Trp11 and Gly65-Asn66. Three-dimensional structures of CspA were generated from NMR data by using simulated annealing with molecular dynamics. The overall chain fold of CspA is a beta-barrel structure, with a tightly packed hydrophobic core. Two-dimensional isotope-edited pulsed-field gradient 15N-1H heteronuclear single-quantum coherence spectroscopy was used to characterize the 15N-1H fingerprint spectrum with and without a 24-base oligodeoxyribonucleotide, 5'-AACGGTTTGACGTACAGACCATTA-3'. Protein-DNA complex formation perturbs a subset of the amide resonances that are located mostly on one face of the CspA molecule. This portion of the CspA molecular surface includes two putative RNA-binding sequence motifs which contribute to an unusual cluster of eight surface aromatic side chains: Trp11, Phe12, Phe18, Phe20, Phe31, His33, Phe34, and Tyr42. These surface aromatic groups, and also residues Lys16, Ser44, and Lys60 located on this same face of CspA, are highly conserved in the family of CspA homologues. These isotope-edited pulsed-field gradient NMR data provide a low-resolution mapping of a DNA-binding epitope on CspA. ; save_ save_ref_2 _Saveframe_category citation _Citation_full 'Zimmerman et al. (1997) J. Mol. Biol. 269, 592 - 610' _Citation_title 'Automated analysis of protein NMR assignments using methods from artificial intelligence.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9217263 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Zimmerman 'D E' E. . 2 Kulikowski 'C A' A. . 3 Huang Y . . 4 Feng W . . 5 Tashiro M . . 6 Shimotakahara S . . 7 Chien C . . 8 Powers R . . 9 Montelione 'G T' T. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 269 _Journal_issue 4 _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 592 _Page_last 610 _Year 1997 _Details ; An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed. ; save_ ################################## # Molecular system description # ################################## save_system_CspA _Saveframe_category molecular_system _Mol_system_name 'Major cold shock protein from E. coli' _Abbreviation_common CspA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CspA monomer' $CspA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state momomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'single-strand RNA binding protein' 'single-strand DNA binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CspA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cold shock protein A' _Abbreviation_common CspA _Molecular_mass 7400 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 70 _Mol_residue_sequence ; MSGKMTGIVKWFNADKGFGF ITPDDGSKDVFVHFSAIQND GYKSLDEGQKVSFTIESGAK GPAAGNVTSL ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 GLY 4 LYS 5 MET 6 THR 7 GLY 8 ILE 9 VAL 10 LYS 11 TRP 12 PHE 13 ASN 14 ALA 15 ASP 16 LYS 17 GLY 18 PHE 19 GLY 20 PHE 21 ILE 22 THR 23 PRO 24 ASP 25 ASP 26 GLY 27 SER 28 LYS 29 ASP 30 VAL 31 PHE 32 VAL 33 HIS 34 PHE 35 SER 36 ALA 37 ILE 38 GLN 39 ASN 40 ASP 41 GLY 42 TYR 43 LYS 44 SER 45 LEU 46 ASP 47 GLU 48 GLY 49 GLN 50 LYS 51 VAL 52 SER 53 PHE 54 THR 55 ILE 56 GLU 57 SER 58 GLY 59 ALA 60 LYS 61 GLY 62 PRO 63 ALA 64 ALA 65 GLY 66 ASN 67 VAL 68 THR 69 SER 70 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 BMRB 4107 "Cold shock protein A" 100.00 70 100.00 100.00 1.53e-41 BMRB 4108 "Cold shock protein A" 100.00 70 100.00 100.00 1.53e-41 PDB 1MJC "Crystal Structure Of Cspa, The Major Cold Shock Protein Of Escherichia Coli" 98.57 69 100.00 100.00 1.69e-40 PDB 2BH8 "Combinatorial Protein 1b11" 50.00 101 100.00 100.00 5.02e-15 PDB 2L15 "Solution Structure Of Cold Shock Protein Cspa Using Combined Nmr And Cs-Rosetta Method" 100.00 70 100.00 100.00 1.53e-41 PDB 3MEF "Major Cold-Shock Protein From Escherichia Coli Solution Nmr Structure" 97.14 69 100.00 100.00 6.30e-40 DBJ BAB37864 "cold shock protein 7.4 [Escherichia coli O157:H7 str. Sakai]" 100.00 70 100.00 100.00 1.53e-41 DBJ BAE77739 "major cold shock protein [Escherichia coli str. K12 substr. W3110]" 100.00 70 100.00 100.00 1.53e-41 DBJ BAG79354 "cold shock protein [Escherichia coli SE11]" 100.00 70 100.00 100.00 1.53e-41 DBJ BAH65698 "cold shock protein [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 70 100.00 100.00 1.53e-41 DBJ BAI28199 "major cold shock protein CspA [Escherichia coli O26:H11 str. 11368]" 100.00 70 100.00 100.00 1.53e-41 EMBL CAD07979 "cold shock protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 70 100.00 100.00 1.53e-41 EMBL CAP78016 "Cold shock protein cspA [Escherichia coli LF82]" 100.00 70 100.00 100.00 1.53e-41 EMBL CAQ33874 "CspA transcriptional activator [Escherichia coli BL21(DE3)]" 100.00 70 100.00 100.00 1.53e-41 EMBL CAQ91030 "major cold shock protein [Escherichia fergusonii ATCC 35469]" 100.00 70 100.00 100.00 1.53e-41 EMBL CAR00519 "major cold shock protein [Escherichia coli IAI1]" 100.00 70 100.00 100.00 1.53e-41 GB AAA23617 "cold shock protein (cspA) [Escherichia coli]" 100.00 70 100.00 100.00 1.53e-41 GB AAB18533 "cold regulated [Escherichia coli str. K-12 substr. MG1655]" 100.00 70 100.00 100.00 1.53e-41 GB AAB66357 "cold shock protein [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 70 98.57 98.57 6.31e-41 GB AAB69447 "cold shock protein [Salmonella enterica subsp. enterica serovar Enteritidis]" 100.00 70 100.00 100.00 1.53e-41 GB AAC06036 "cold shock protein A [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 70 100.00 100.00 1.53e-41 PIR AG0981 "cold shock protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 70 100.00 100.00 1.53e-41 REF NP_312468 "major cold shock protein [Escherichia coli O157:H7 str. Sakai]" 100.00 70 100.00 100.00 1.53e-41 REF NP_418012 "RNA chaperone and antiterminator, cold-inducible [Escherichia coli str. K-12 substr. MG1655]" 100.00 70 100.00 100.00 1.53e-41 REF NP_458276 "cold shock protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 70 100.00 100.00 1.53e-41 REF NP_462550 "cold shock protein CspA [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 70 100.00 100.00 1.53e-41 REF NP_709333 "RNA chaperone/anti-terminator [Shigella flexneri 2a str. 301]" 100.00 70 100.00 100.00 1.53e-41 SP P0A9X9 "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" 100.00 70 100.00 100.00 1.53e-41 SP P0A9Y0 "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" 100.00 70 100.00 100.00 1.53e-41 SP P0A9Y1 "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" 100.00 70 100.00 100.00 1.53e-41 SP P0A9Y2 "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" 100.00 70 100.00 100.00 1.53e-41 SP P0A9Y3 "RecName: Full=Cold shock protein CspA; Short=CSP-A; AltName: Full=7.4 kDa cold shock protein; AltName: Full=CS7.4" 100.00 70 100.00 100.00 1.53e-41 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Gene_mnemonic $CspA 'E. coli' 562 Eubacteria . Escherichia coli cytoplasmic cspA stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $CspA 'recombinant technology' . . . . . 'Produced using plasmid pET11-CspA in E. coli strain BL21(DE3)' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Samples were prepared in H2O containing 5% deuterium oxide for locking purposes. Solutions were buffered at pH* 6.0 +/- 0.1. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CspA . mM 1.0 3.0 '[U-98% 13C; U-90% 15N]' KH2PO4 50 mM . . . NaEDTA 0.1 mM . . . NaN3 1 mM . . . stop_ save_ ############################ # Computer software used # ############################ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version 1.0 loop_ _Task ; automated analysis of backbone N, C, H, and sidechain Cb resonance assignments ; stop_ _Details ; In-house developed software for automatic analysis of resonance assignments from triple-resonance spectra. ; _Citation_label $ref_2 save_ save_Varian_VNMR _Saveframe_category software _Name Varian_VNMR _Version 5.3 loop_ _Vendor _Address _Electronic_address 'Varian Associates' 'Palo Alto, CA' . stop_ loop_ _Task 'Data collection and processing of 3D Fourier transforms' stop_ _Details . save_ save_NMRCompass _Saveframe_category software _Name NMRCompass _Version . loop_ _Vendor _Address _Electronic_address MSI . . stop_ loop_ _Task 'Automatic peak pick of frequency-domain 2D and 3D data sets.' stop_ _Details ; Frequency-domain data generated with VNMR is inport into NMRCompass for automated peak-picking. Peak picking is valadidated by interactive graphics analysis. Peak lists are then input to the AutoAssign software for automated analysis of resonance assignments. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_Most_of_the_triple_resonance_experiments_were_exectuted_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Most of the triple resonance experiments were exectuted' _Sample_label $sample_1 save_ save_with_C-H_or_C-C_phase_labeling_to_aid_assignments_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'with C-H or C-C phase labeling to aid assignments' _Sample_label $sample_1 save_ save_[Tashiro_et_al._J._Biomol._NMR_(1995)_6:_211_-_216;_3 _Saveframe_category NMR_applied_experiment _Experiment_name '[Tashiro et al. J. Biomol. NMR (1995) 6: 211 - 216;' _Sample_label $sample_1 save_ save_Feng_et_al.,_J._Biomol._NMR_(1996)_8,_98_-_104;_Rios_et_al.,_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'Feng et al., J. Biomol. NMR (1996) 8, 98 - 104; Rios et al.,' _Sample_label $sample_1 save_ save_J._Biomol._NMR_(1996)_8,_345_-_350]._5 _Saveframe_category NMR_applied_experiment _Experiment_name 'J. Biomol. NMR (1996) 8, 345 - 350].' _Sample_label $sample_1 save_ save_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label $sample_1 save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HNCA_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_CANH_9 _Saveframe_category NMR_applied_experiment _Experiment_name CANH _Sample_label $sample_1 save_ save_CA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name CA(CO)NH _Sample_label $sample_1 save_ save_HA(CA)NH_11 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)NH _Sample_label $sample_1 save_ save_HA(CA)(CO)NH_12 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)(CO)NH _Sample_label $sample_1 save_ save_CBCANH_13 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_1 save_ save_CBCA(CO)NH_14 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HCCNH-TOCSY_15 _Saveframe_category NMR_applied_experiment _Experiment_name HCCNH-TOCSY _Sample_label $sample_1 save_ save_HCC(CO)NH-TOCSY_16 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH-TOCSY _Sample_label $sample_1 save_ save_homonuclear_2D_H-TOCSY_17 _Saveframe_category NMR_applied_experiment _Experiment_name 'homonuclear 2D H-TOCSY' _Sample_label $sample_1 save_ save_15N-edited_3D_NOESY"_18 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited 3D NOESY"' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Most of the triple resonance experiments were exectuted' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'with C-H or C-C phase labeling to aid assignments' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '[Tashiro et al. J. Biomol. NMR (1995) 6: 211 - 216;' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'Feng et al., J. Biomol. NMR (1996) 8, 98 - 104; Rios et al.,' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'J. Biomol. NMR (1996) 8, 345 - 350].' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name CANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name CA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name HA(CA)(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_15 _Saveframe_category NMR_applied_experiment _Experiment_name HCCNH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_16 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_17 _Saveframe_category NMR_applied_experiment _Experiment_name 'homonuclear 2D H-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_18 _Saveframe_category NMR_applied_experiment _Experiment_name '15N-edited 3D NOESY"' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details 'Samples were prepared in 95% H2O, 5% 2H2O' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.0 0.1 na temperature 303 0.5 K 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 spherical internal . 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_CsCspA_Ecoli_pH6.0_30degC _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CspA monomer' _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 SER HA H 4.39 0.02 1 2 . 2 SER C C 177.2 0.10 1 3 . 2 SER CA C 58.0 0.10 1 4 . 2 SER CB C 63.6 0.10 1 5 . 3 GLY H H 8.43 0.02 1 6 . 3 GLY HA2 H 3.95 0.02 1 7 . 3 GLY HA3 H 3.95 0.02 1 8 . 3 GLY C C 173.4 0.10 1 9 . 3 GLY CA C 45.2 0.10 1 10 . 3 GLY N N 111.0 0.10 1 11 . 4 LYS H H 8.21 0.02 1 12 . 4 LYS HA H 4.28 0.02 1 13 . 4 LYS HB2 H 1.76 0.02 1 14 . 4 LYS HB3 H 1.58 0.02 1 15 . 4 LYS HG2 H 1.52 0.02 2 16 . 4 LYS HG3 H 1.15 0.02 2 17 . 4 LYS HD2 H 1.69 0.02 1 18 . 4 LYS HD3 H 1.69 0.02 1 19 . 4 LYS HE2 H 2.89 0.02 1 20 . 4 LYS HE3 H 2.89 0.02 1 21 . 4 LYS C C 176.0 0.10 1 22 . 4 LYS CA C 56.6 0.10 1 23 . 4 LYS CB C 33.4 0.10 1 24 . 4 LYS CG C 24.6 0.10 1 25 . 4 LYS CD C 28.4 0.10 1 26 . 4 LYS CE C 41.7 0.10 1 27 . 4 LYS N N 120.1 0.10 1 28 . 5 MET H H 8.63 0.02 1 29 . 5 MET HA H 4.57 0.02 1 30 . 5 MET HB3 H 1.40 0.02 1 31 . 5 MET HB2 H 1.06 0.02 1 32 . 5 MET HG2 H 2.38 0.02 2 33 . 5 MET HG3 H 2.24 0.02 2 34 . 5 MET C C 174.1 0.10 1 35 . 5 MET CA C 53.6 0.10 1 36 . 5 MET CB C 34.0 0.10 1 37 . 5 MET CG C 31.5 0.10 1 38 . 5 MET N N 122.7 0.10 1 39 . 6 THR H H 7.69 0.02 1 40 . 6 THR HA H 5.50 0.02 1 41 . 6 THR HB H 4.43 0.02 1 42 . 6 THR HG2 H 1.12 0.02 1 43 . 6 THR C C 175.7 0.10 1 44 . 6 THR CA C 59.4 0.10 1 45 . 6 THR CB C 71.4 0.10 1 46 . 6 THR CG2 C 21.6 0.10 1 47 . 6 THR N N 107.5 0.10 1 48 . 7 GLY H H 8.96 0.02 1 49 . 7 GLY HA2 H 4.58 0.02 2 50 . 7 GLY HA3 H 3.96 0.02 2 51 . 7 GLY C C 171.1 0.10 1 52 . 7 GLY CA C 46.2 0.10 1 53 . 7 GLY N N 108.7 0.10 1 54 . 8 ILE H H 8.20 0.02 1 55 . 8 ILE HA H 5.13 0.02 1 56 . 8 ILE HB H 1.65 0.02 1 57 . 8 ILE HG2 H 0.85 0.02 1 58 . 8 ILE HG12 H 1.54 0.02 2 59 . 8 ILE HG13 H 1.13 0.02 2 60 . 8 ILE HD1 H 0.90 0.02 1 61 . 8 ILE C C 175.6 0.10 1 62 . 8 ILE CA C 58.3 0.10 1 63 . 8 ILE CB C 41.9 0.10 1 64 . 8 ILE CG1 C 27.1 0.10 1 65 . 8 ILE CG2 C 16.7 0.10 1 66 . 8 ILE CD1 C 12.5 0.10 1 67 . 8 ILE N N 118.1 0.10 1 68 . 9 VAL H H 8.83 0.02 1 69 . 9 VAL HA H 3.61 0.02 1 70 . 9 VAL HB H 2.42 0.02 1 71 . 9 VAL HG1 H 0.86 0.02 2 72 . 9 VAL HG2 H 0.56 0.02 2 73 . 9 VAL C C 175.0 0.10 1 74 . 9 VAL CA C 64.4 0.10 1 75 . 9 VAL CB C 31.0 0.10 1 76 . 9 VAL CG1 C 20.7 0.10 1 77 . 9 VAL CG2 C 20.7 0.10 1 78 . 9 VAL N N 126.3 0.10 1 79 . 10 LYS H H 9.11 0.02 1 80 . 10 LYS HA H 4.21 0.02 1 81 . 10 LYS HB2 H 1.55 0.02 1 82 . 10 LYS HB3 H 1.55 0.02 1 83 . 10 LYS HG2 H 2.06 0.02 2 84 . 10 LYS HG3 H 2.04 0.02 2 85 . 10 LYS C C 176.3 0.10 1 86 . 10 LYS CA C 58.5 0.10 1 87 . 10 LYS CB C 33.8 0.10 1 88 . 10 LYS CE C 41.8 0.10 1 89 . 10 LYS N N 135.9 0.10 1 90 . 11 TRP H H 7.45 0.02 1 91 . 11 TRP HA H 4.66 0.02 1 92 . 11 TRP HB3 H 3.54 0.02 1 93 . 11 TRP HB2 H 3.44 0.02 1 94 . 11 TRP HD1 H 7.14 0.02 1 95 . 11 TRP HE1 H 10.47 0.02 1 96 . 11 TRP HE3 H 7.37 0.02 1 97 . 11 TRP HZ2 H 7.50 0.02 1 98 . 11 TRP HZ3 H 7.37 0.02 1 99 . 11 TRP HH2 H 6.74 0.02 1 100 . 11 TRP C C 173.7 0.10 1 101 . 11 TRP CA C 56.2 0.10 1 102 . 11 TRP CB C 31.2 0.10 1 103 . 11 TRP N N 111.2 0.10 1 104 . 11 TRP NE1 N 130.0 0.10 1 105 . 12 PHE H H 9.25 0.02 1 106 . 12 PHE HA H 4.27 0.02 1 107 . 12 PHE HB3 H 2.93 0.02 1 108 . 12 PHE HB2 H 2.47 0.02 1 109 . 12 PHE HD1 H 6.76 0.02 1 110 . 12 PHE HD2 H 6.76 0.02 1 111 . 12 PHE HE1 H 7.01 0.02 1 112 . 12 PHE HE2 H 7.01 0.02 1 113 . 12 PHE HZ H 7.56 0.02 1 114 . 12 PHE C C 172.4 0.10 1 115 . 12 PHE CA C 59.3 0.10 1 116 . 12 PHE CB C 42.2 0.10 1 117 . 12 PHE N N 121.5 0.10 1 118 . 13 ASN H H 8.13 0.02 1 119 . 13 ASN HA H 4.82 0.02 1 120 . 13 ASN HB2 H 2.55 0.02 2 121 . 13 ASN HB3 H 2.45 0.02 2 122 . 13 ASN HD21 H 7.54 0.02 1 123 . 13 ASN HD22 H 7.32 0.02 1 124 . 13 ASN C C 174.1 0.10 1 125 . 13 ASN CA C 51.2 0.10 1 126 . 13 ASN CB C 39.1 0.10 1 127 . 13 ASN N N 126.6 0.10 1 128 . 13 ASN ND2 N 112.7 0.10 1 129 . 14 ALA H H 9.07 0.02 1 130 . 14 ALA HA H 4.09 0.02 1 131 . 14 ALA HB H 1.59 0.02 1 132 . 14 ALA C C 178.6 0.10 1 133 . 14 ALA CA C 54.5 0.10 1 134 . 14 ALA CB C 18.5 0.10 1 135 . 14 ALA N N 128.6 0.10 1 136 . 15 ASP H H 7.98 0.02 1 137 . 15 ASP HA H 4.35 0.02 1 138 . 15 ASP HB2 H 2.77 0.02 2 139 . 15 ASP HB3 H 2.70 0.02 2 140 . 15 ASP C C 177.7 0.10 1 141 . 15 ASP CA C 56.6 0.10 1 142 . 15 ASP CB C 40.5 0.10 1 143 . 15 ASP N N 117.0 0.10 1 144 . 16 LYS H H 7.45 0.02 1 145 . 16 LYS HA H 4.21 0.02 1 146 . 16 LYS HB3 H 1.60 0.02 1 147 . 16 LYS HB2 H 1.09 0.02 1 148 . 16 LYS HG2 H 1.42 0.02 2 149 . 16 LYS HG3 H 1.35 0.02 2 150 . 16 LYS HD2 H 1.67 0.02 2 151 . 16 LYS HD3 H 1.65 0.02 2 152 . 16 LYS HE2 H 3.01 0.02 2 153 . 16 LYS HE3 H 2.97 0.02 2 154 . 16 LYS C C 177.3 0.10 1 155 . 16 LYS CA C 56.1 0.10 1 156 . 16 LYS CB C 33.6 0.10 1 157 . 16 LYS CG C 25.0 0.10 1 158 . 16 LYS CE C 41.2 0.10 1 159 . 16 LYS N N 115.8 0.10 1 160 . 17 GLY H H 8.16 0.02 1 161 . 17 GLY HA2 H 4.10 0.02 2 162 . 17 GLY HA3 H 3.79 0.02 2 163 . 17 GLY C C 172.4 0.10 1 164 . 17 GLY CA C 46.2 0.10 1 165 . 17 GLY N N 107.5 0.10 1 166 . 18 PHE H H 6.66 0.02 1 167 . 18 PHE HA H 5.11 0.02 1 168 . 18 PHE HB2 H 3.01 0.02 2 169 . 18 PHE HB3 H 2.88 0.02 2 170 . 18 PHE HD1 H 7.00 0.02 1 171 . 18 PHE HD2 H 7.00 0.02 1 172 . 18 PHE HE1 H 7.53 0.02 1 173 . 18 PHE HE2 H 7.53 0.02 1 174 . 18 PHE HZ H 7.47 0.02 1 175 . 18 PHE C C 171.9 0.10 1 176 . 18 PHE CA C 54.6 0.10 1 177 . 18 PHE CB C 41.9 0.10 1 178 . 18 PHE N N 112.3 0.10 1 179 . 19 GLY H H 8.04 0.02 1 180 . 19 GLY HA2 H 3.93 0.02 1 181 . 19 GLY HA3 H 3.93 0.02 1 182 . 19 GLY C C 170.4 0.10 1 183 . 19 GLY CA C 45.3 0.10 1 184 . 19 GLY N N 105.3 0.10 1 185 . 20 PHE H H 7.96 0.02 1 186 . 20 PHE HA H 5.29 0.02 1 187 . 20 PHE HB3 H 2.59 0.02 1 188 . 20 PHE HB2 H 2.23 0.02 1 189 . 20 PHE HD1 H 6.79 0.02 1 190 . 20 PHE HD2 H 6.79 0.02 1 191 . 20 PHE HE1 H 7.35 0.02 1 192 . 20 PHE HE2 H 7.35 0.02 1 193 . 20 PHE HZ H 7.24 0.02 1 194 . 20 PHE C C 174.6 0.10 1 195 . 20 PHE CA C 56.6 0.10 1 196 . 20 PHE CB C 45.2 0.10 1 197 . 20 PHE N N 114.9 0.10 1 198 . 21 ILE H H 9.43 0.02 1 199 . 21 ILE HA H 4.24 0.02 1 200 . 21 ILE HB H 0.94 0.02 1 201 . 21 ILE HG2 H 0.12 0.02 1 202 . 21 ILE HG12 H 1.21 0.02 2 203 . 21 ILE HG13 H 0.35 0.02 2 204 . 21 ILE HD1 H -0.09 0.02 1 205 . 21 ILE C C 174.7 0.10 1 206 . 21 ILE CA C 59.3 0.10 1 207 . 21 ILE CB C 42.0 0.10 1 208 . 21 ILE CG1 C 27.3 0.10 1 209 . 21 ILE CG2 C 17.9 0.10 1 210 . 21 ILE CD1 C 13.2 0.10 1 211 . 21 ILE N N 121.7 0.10 1 212 . 22 THR H H 9.37 0.02 1 213 . 22 THR HA H 5.17 0.02 1 214 . 22 THR HB H 3.95 0.02 1 215 . 22 THR HG2 H 1.39 0.02 1 216 . 22 THR CA C 59.3 0.10 1 217 . 22 THR CB C 70.3 0.10 1 218 . 22 THR N N 126.6 0.10 1 219 . 23 PRO HA H 4.77 0.02 1 220 . 23 PRO HB2 H 2.45 0.02 2 221 . 23 PRO HB3 H 2.36 0.02 2 222 . 23 PRO HG2 H 2.30 0.02 2 223 . 23 PRO HG3 H 1.86 0.02 2 224 . 23 PRO HD2 H 4.51 0.02 2 225 . 23 PRO HD3 H 3.85 0.02 2 226 . 23 PRO C C 177.5 0.10 1 227 . 23 PRO CA C 63.0 0.10 1 228 . 23 PRO CB C 33.6 0.10 1 229 . 23 PRO CD C 52.6 0.10 1 230 . 24 ASP H H 9.21 0.02 1 231 . 24 ASP HA H 4.66 0.02 1 232 . 24 ASP HB2 H 2.77 0.02 2 233 . 24 ASP HB3 H 2.50 0.02 2 234 . 24 ASP C C 176.5 0.10 1 235 . 24 ASP CA C 56.6 0.10 1 236 . 24 ASP CB C 40.3 0.10 1 237 . 24 ASP N N 123.1 0.10 1 238 . 25 ASP H H 7.98 0.02 1 239 . 25 ASP HA H 4.55 0.02 1 240 . 25 ASP HB2 H 3.09 0.02 2 241 . 25 ASP HB3 H 2.60 0.02 2 242 . 25 ASP C C 177.6 0.10 1 243 . 25 ASP CA C 53.6 0.10 1 244 . 25 ASP CB C 40.5 0.10 1 245 . 25 ASP N N 117.0 0.10 1 246 . 26 GLY H H 7.69 0.02 1 247 . 26 GLY HA2 H 4.18 0.02 2 248 . 26 GLY HA3 H 3.90 0.02 2 249 . 26 GLY C C 174.7 0.10 1 250 . 26 GLY CA C 45.8 0.10 1 251 . 26 GLY N N 107.5 0.10 1 252 . 27 SER H H 8.00 0.02 1 253 . 27 SER HA H 4.37 0.02 1 254 . 27 SER HB2 H 4.19 0.02 2 255 . 27 SER HB3 H 3.95 0.02 2 256 . 27 SER C C 172.5 0.10 1 257 . 27 SER CA C 58.6 0.10 1 258 . 27 SER CB C 62.9 0.10 1 259 . 27 SER N N 116.0 0.10 1 260 . 28 LYS H H 7.72 0.02 1 261 . 28 LYS HA H 4.09 0.02 1 262 . 28 LYS HB2 H 1.86 0.02 2 263 . 28 LYS HB3 H 1.86 0.02 2 264 . 28 LYS HG2 H 1.60 0.02 1 265 . 28 LYS HG3 H 1.60 0.02 1 266 . 28 LYS HD2 H 1.76 0.02 1 267 . 28 LYS HD3 H 1.76 0.02 1 268 . 28 LYS HE2 H 3.07 0.02 1 269 . 28 LYS HE3 H 3.07 0.02 1 270 . 28 LYS C C 175.1 0.10 1 271 . 28 LYS CA C 56.9 0.10 1 272 . 28 LYS CB C 33.0 0.10 1 273 . 28 LYS CG C 24.1 0.10 1 274 . 28 LYS CD C 29.1 0.10 1 275 . 28 LYS CE C 42.2 0.10 1 276 . 28 LYS N N 117.1 0.10 1 277 . 29 ASP H H 7.93 0.02 1 278 . 29 ASP HA H 4.90 0.02 1 279 . 29 ASP HB3 H 2.45 0.02 1 280 . 29 ASP HB2 H 2.36 0.02 1 281 . 29 ASP C C 176.3 0.10 1 282 . 29 ASP CA C 55.3 0.10 1 283 . 29 ASP CB C 41.1 0.10 1 284 . 29 ASP N N 118.0 0.10 1 285 . 30 VAL H H 9.30 0.02 1 286 . 30 VAL HA H 4.34 0.02 1 287 . 30 VAL HB H 1.66 0.02 1 288 . 30 VAL HG1 H 1.03 0.02 2 289 . 30 VAL HG2 H 0.84 0.02 2 290 . 30 VAL C C 174.7 0.10 1 291 . 30 VAL CA C 60.6 0.10 1 292 . 30 VAL CG1 C 21.9 0.10 1 293 . 30 VAL CG2 C 21.9 0.10 1 294 . 30 VAL N N 120.4 0.10 1 295 . 31 PHE H H 8.55 0.02 1 296 . 31 PHE HA H 3.71 0.02 1 297 . 31 PHE HB2 H 2.86 0.02 2 298 . 31 PHE HB3 H 2.74 0.02 2 299 . 31 PHE HD1 H 6.77 0.02 1 300 . 31 PHE HD2 H 6.77 0.02 1 301 . 31 PHE HE1 H 7.01 0.02 1 302 . 31 PHE HE2 H 7.01 0.02 1 303 . 31 PHE HZ H 6.96 0.02 1 304 . 31 PHE C C 172.6 0.10 1 305 . 31 PHE CA C 58.2 0.10 1 306 . 31 PHE CB C 40.2 0.10 1 307 . 31 PHE N N 129.7 0.10 1 308 . 32 VAL H H 7.77 0.02 1 309 . 32 VAL HA H 4.48 0.02 1 310 . 32 VAL HB H 1.45 0.02 1 311 . 32 VAL HG1 H 0.60 0.02 2 312 . 32 VAL HG2 H 0.47 0.02 2 313 . 32 VAL C C 170.4 0.10 1 314 . 32 VAL CA C 57.9 0.10 1 315 . 32 VAL CB C 34.1 0.10 1 316 . 32 VAL N N 124.3 0.10 1 317 . 33 HIS H H 8.72 0.02 1 318 . 33 HIS HA H 4.78 0.02 1 319 . 33 HIS HB2 H 3.15 0.02 2 320 . 33 HIS HB3 H 2.84 0.02 2 321 . 33 HIS HD2 H 7.33 0.02 1 322 . 33 HIS HE1 H 8.45 0.02 1 323 . 33 HIS C C 177.2 0.10 1 324 . 33 HIS CA C 55.5 0.10 1 325 . 33 HIS CB C 34.1 0.10 1 326 . 33 HIS N N 127.1 0.10 1 327 . 34 PHE H H 8.32 0.02 1 328 . 34 PHE HA H 4.14 0.02 1 329 . 34 PHE HB2 H 3.31 0.02 2 330 . 34 PHE HB3 H 2.99 0.02 2 331 . 34 PHE HD1 H 7.16 0.02 1 332 . 34 PHE HD2 H 7.16 0.02 1 333 . 34 PHE HE1 H 7.36 0.02 1 334 . 34 PHE HE2 H 7.36 0.02 1 335 . 34 PHE HZ H 7.45 0.02 1 336 . 34 PHE C C 176.0 0.10 1 337 . 34 PHE CA C 59.9 0.10 1 338 . 34 PHE CB C 37.2 0.10 1 339 . 34 PHE N N 123.1 0.10 1 340 . 35 SER H H 7.59 0.02 1 341 . 35 SER HA H 3.87 0.02 1 342 . 35 SER HB2 H 3.57 0.02 1 343 . 35 SER HB3 H 3.57 0.02 1 344 . 35 SER C C 175.0 0.10 1 345 . 35 SER CA C 59.9 0.10 1 346 . 35 SER CB C 62.3 0.10 1 347 . 35 SER N N 117.0 0.10 1 348 . 36 ALA H H 8.06 0.02 1 349 . 36 ALA HA H 4.46 0.02 1 350 . 36 ALA HB H 1.61 0.02 1 351 . 36 ALA C C 177.5 0.10 1 352 . 36 ALA CA C 52.3 0.10 1 353 . 36 ALA CB C 22.6 0.10 1 354 . 36 ALA N N 124.1 0.10 1 355 . 37 ILE H H 7.50 0.02 1 356 . 37 ILE HA H 3.89 0.02 1 357 . 37 ILE HB H 1.86 0.02 1 358 . 37 ILE HG2 H 0.81 0.02 1 359 . 37 ILE HG12 H 1.86 0.02 2 360 . 37 ILE HG13 H 1.56 0.02 2 361 . 37 ILE HD1 H 0.41 0.02 1 362 . 37 ILE C C 176.1 0.10 1 363 . 37 ILE CA C 62.6 0.10 1 364 . 37 ILE CB C 37.8 0.10 1 365 . 37 ILE N N 119.2 0.10 1 366 . 38 GLN H H 9.02 0.02 1 367 . 38 GLN HA H 4.36 0.02 1 368 . 38 GLN HB2 H 2.13 0.02 2 369 . 38 GLN HB3 H 1.79 0.02 2 370 . 38 GLN HG2 H 2.33 0.02 2 371 . 38 GLN HG3 H 2.30 0.02 2 372 . 38 GLN HE21 H 7.19 0.02 1 373 . 38 GLN HE22 H 6.85 0.02 1 374 . 38 GLN C C 175.6 0.10 1 375 . 38 GLN CA C 55.2 0.10 1 376 . 38 GLN CB C 28.7 0.10 1 377 . 38 GLN CG C 33.7 0.10 1 378 . 38 GLN N N 127.1 0.10 1 379 . 38 GLN NE2 N 112.1 0.10 1 380 . 39 ASN H H 7.53 0.02 1 381 . 39 ASN HA H 4.61 0.02 1 382 . 39 ASN HB2 H 2.87 0.02 2 383 . 39 ASN HB3 H 2.61 0.02 2 384 . 39 ASN HD21 H 7.76 0.02 1 385 . 39 ASN HD22 H 6.85 0.02 1 386 . 39 ASN C C 174.6 0.10 1 387 . 39 ASN CA C 53.3 0.10 1 388 . 39 ASN CB C 38.9 0.10 1 389 . 39 ASN N N 118.7 0.10 1 390 . 39 ASN ND2 N 112.3 0.10 1 391 . 40 ASP H H 8.59 0.02 1 392 . 40 ASP HA H 4.51 0.02 1 393 . 40 ASP HB2 H 2.70 0.02 2 394 . 40 ASP HB3 H 2.63 0.02 2 395 . 40 ASP C C 176.5 0.10 1 396 . 40 ASP CA C 54.9 0.10 1 397 . 40 ASP CB C 40.8 0.10 1 398 . 40 ASP N N 121.5 0.10 1 399 . 41 GLY H H 8.29 0.02 1 400 . 41 GLY HA2 H 3.97 0.02 2 401 . 41 GLY HA3 H 3.77 0.02 2 402 . 41 GLY C C 173.7 0.10 1 403 . 41 GLY CA C 45.2 0.10 1 404 . 41 GLY N N 108.9 0.10 1 405 . 42 TYR H H 8.08 0.02 1 406 . 42 TYR HA H 4.41 0.02 1 407 . 42 TYR HB2 H 2.95 0.02 1 408 . 42 TYR HB3 H 2.95 0.02 1 409 . 42 TYR HD1 H 7.06 0.02 1 410 . 42 TYR HD2 H 7.06 0.02 1 411 . 42 TYR HE1 H 6.72 0.02 1 412 . 42 TYR HE2 H 6.72 0.02 1 413 . 42 TYR C C 176.0 0.10 1 414 . 42 TYR CA C 58.2 0.10 1 415 . 42 TYR CB C 38.3 0.10 1 416 . 42 TYR N N 121.2 0.10 1 417 . 43 LYS H H 8.27 0.02 1 418 . 43 LYS HA H 4.19 0.02 1 419 . 43 LYS HB2 H 1.46 0.02 2 420 . 43 LYS HB3 H 1.40 0.02 2 421 . 43 LYS HG2 H 1.86 0.02 1 422 . 43 LYS HG3 H 1.86 0.02 1 423 . 43 LYS HD2 H 1.71 0.02 1 424 . 43 LYS HD3 H 1.71 0.02 1 425 . 43 LYS HE2 H 3.11 0.02 2 426 . 43 LYS HE3 H 3.01 0.02 2 427 . 43 LYS C C 174.0 0.10 1 428 . 43 LYS CA C 55.0 0.10 1 429 . 43 LYS CB C 31.8 0.10 1 430 . 43 LYS CG C 24.4 0.10 1 431 . 43 LYS CD C 28.4 0.10 1 432 . 43 LYS CE C 42.8 0.10 1 433 . 43 LYS N N 125.1 0.10 1 434 . 44 SER H H 7.41 0.02 1 435 . 44 SER HA H 3.98 0.02 1 436 . 44 SER HB2 H 3.50 0.02 1 437 . 44 SER HB3 H 3.43 0.02 1 438 . 44 SER C C 171.7 0.10 1 439 . 44 SER CA C 56.2 0.10 1 440 . 44 SER CB C 63.8 0.10 1 441 . 44 SER N N 113.8 0.10 1 442 . 45 LEU H H 5.85 0.02 1 443 . 45 LEU HA H 4.44 0.02 1 444 . 45 LEU HB2 H 1.01 0.02 2 445 . 45 LEU HB3 H 0.43 0.02 2 446 . 45 LEU HG H 0.78 0.02 1 447 . 45 LEU HD1 H 0.48 0.02 2 448 . 45 LEU HD2 H 0.29 0.02 2 449 . 45 LEU C C 174.1 0.10 1 450 . 45 LEU CA C 52.7 0.10 1 451 . 45 LEU CB C 44.9 0.10 1 452 . 45 LEU CG C 32.7 0.10 1 453 . 45 LEU CD1 C 24.2 0.10 1 454 . 45 LEU CD2 C 24.2 0.10 1 455 . 45 LEU N N 119.1 0.10 1 456 . 46 ASP H H 8.21 0.02 1 457 . 46 ASP HA H 4.89 0.02 1 458 . 46 ASP HB2 H 2.62 0.02 2 459 . 46 ASP HB3 H 2.37 0.02 2 460 . 46 ASP C C 175.5 0.10 1 461 . 46 ASP CA C 52.6 0.10 1 462 . 46 ASP CB C 43.8 0.10 1 463 . 46 ASP N N 120.1 0.10 1 464 . 47 GLU H H 8.66 0.02 1 465 . 47 GLU HA H 3.58 0.02 1 466 . 47 GLU HB2 H 2.16 0.02 2 467 . 47 GLU HB3 H 2.01 0.02 2 468 . 47 GLU HG2 H 2.55 0.02 2 469 . 47 GLU HG3 H 2.24 0.02 2 470 . 47 GLU C C 177.3 0.10 1 471 . 47 GLU CA C 58.0 0.10 1 472 . 47 GLU CB C 29.4 0.10 1 473 . 47 GLU CG C 35.5 0.10 1 474 . 47 GLU N N 120.9 0.10 1 475 . 48 GLY H H 9.12 0.02 1 476 . 48 GLY HA2 H 4.35 0.02 2 477 . 48 GLY HA3 H 3.58 0.02 2 478 . 48 GLY C C 173.6 0.10 1 479 . 48 GLY CA C 45.2 0.10 1 480 . 48 GLY N N 113.6 0.10 1 481 . 49 GLN H H 7.77 0.02 1 482 . 49 GLN HA H 4.18 0.02 1 483 . 49 GLN HB2 H 2.21 0.02 2 484 . 49 GLN HB3 H 1.96 0.02 2 485 . 49 GLN HG2 H 2.37 0.02 1 486 . 49 GLN HG3 H 2.37 0.02 1 487 . 49 GLN HE21 H 7.55 0.02 1 488 . 49 GLN HE22 H 6.81 0.02 1 489 . 49 GLN C C 175.6 0.10 1 490 . 49 GLN CA C 56.3 0.10 1 491 . 49 GLN CB C 30.3 0.10 1 492 . 49 GLN CG C 33.7 0.10 1 493 . 49 GLN N N 120.6 0.10 1 494 . 49 GLN NE2 N 111.0 0.10 1 495 . 50 LYS H H 8.79 0.02 1 496 . 50 LYS HA H 5.05 0.02 1 497 . 50 LYS HB2 H 1.91 0.02 1 498 . 50 LYS HB3 H 1.91 0.02 1 499 . 50 LYS HG2 H 1.71 0.02 2 500 . 50 LYS HG3 H 1.50 0.02 2 501 . 50 LYS HD2 H 1.79 0.02 1 502 . 50 LYS HD3 H 1.79 0.02 1 503 . 50 LYS HE2 H 3.02 0.02 1 504 . 50 LYS HE3 H 3.02 0.02 1 505 . 50 LYS C C 177.1 0.10 1 506 . 50 LYS CA C 56.3 0.10 1 507 . 50 LYS CB C 32.9 0.10 1 508 . 50 LYS CG C 25.0 0.10 1 509 . 50 LYS CD C 28.6 0.10 1 510 . 50 LYS CE C 42.1 0.10 1 511 . 50 LYS N N 126.6 0.10 1 512 . 51 VAL H H 8.63 0.02 1 513 . 51 VAL HA H 5.35 0.02 1 514 . 51 VAL HB H 2.17 0.02 1 515 . 51 VAL HG1 H 0.62 0.02 2 516 . 51 VAL HG2 H 0.52 0.02 2 517 . 51 VAL C C 174.3 0.10 1 518 . 51 VAL CA C 58.4 0.10 1 519 . 51 VAL CB C 36.8 0.10 1 520 . 51 VAL CG1 C 22.2 0.10 2 521 . 51 VAL CG2 C 17.6 0.10 2 522 . 51 VAL N N 115.5 0.10 1 523 . 52 SER H H 9.14 0.02 1 524 . 52 SER HA H 5.70 0.02 1 525 . 52 SER HB2 H 3.83 0.02 2 526 . 52 SER HB3 H 3.75 0.02 2 527 . 52 SER C C 173.9 0.10 1 528 . 52 SER CA C 55.8 0.10 1 529 . 52 SER CB C 65.7 0.10 1 530 . 52 SER N N 114.7 0.10 1 531 . 53 PHE H H 8.70 0.02 1 532 . 53 PHE HA H 5.28 0.02 1 533 . 53 PHE HB2 H 3.27 0.02 2 534 . 53 PHE HB3 H 3.20 0.02 2 535 . 53 PHE HD1 H 6.84 0.02 1 536 . 53 PHE HD2 H 6.84 0.02 1 537 . 53 PHE HE1 H 6.77 0.02 1 538 . 53 PHE HE2 H 6.77 0.02 1 539 . 53 PHE HZ H 6.96 0.02 1 540 . 53 PHE C C 172.8 0.10 1 541 . 53 PHE CA C 56.2 0.10 1 542 . 53 PHE CB C 40.2 0.10 1 543 . 53 PHE N N 117.3 0.10 1 544 . 54 THR H H 8.99 0.02 1 545 . 54 THR HA H 4.71 0.02 1 546 . 54 THR HB H 4.20 0.02 1 547 . 54 THR HG2 H 1.15 0.02 1 548 . 54 THR C C 174.5 0.10 1 549 . 54 THR CA C 59.9 0.10 1 550 . 54 THR CB C 70.4 0.10 1 551 . 54 THR CG2 C 22.5 0.10 1 552 . 54 THR N N 110.4 0.10 1 553 . 55 ILE H H 8.66 0.02 1 554 . 55 ILE HA H 4.69 0.02 1 555 . 55 ILE HB H 1.82 0.02 1 556 . 55 ILE HG2 H 0.95 0.02 1 557 . 55 ILE HG12 H 1.72 0.02 2 558 . 55 ILE HG13 H 1.16 0.02 2 559 . 55 ILE HD1 H 1.01 0.02 1 560 . 55 ILE C C 175.6 0.10 1 561 . 55 ILE CA C 61.0 0.10 1 562 . 55 ILE CB C 39.0 0.10 1 563 . 55 ILE CG1 C 28.0 0.10 1 564 . 55 ILE CG2 C 17.9 0.10 1 565 . 55 ILE CD1 C 13.6 0.10 1 566 . 55 ILE N N 120.9 0.10 1 567 . 56 GLU H H 9.18 0.02 1 568 . 56 GLU HA H 4.67 0.02 1 569 . 56 GLU HB2 H 2.06 0.02 1 570 . 56 GLU HB3 H 1.84 0.02 1 571 . 56 GLU HG2 H 2.22 0.02 2 572 . 56 GLU HG3 H 2.13 0.02 2 573 . 56 GLU C C 176.0 0.10 1 574 . 56 GLU CA C 54.2 0.10 1 575 . 56 GLU CB C 31.5 0.10 1 576 . 56 GLU CG C 35.2 0.10 1 577 . 56 GLU N N 127.9 0.10 1 578 . 57 SER H H 8.77 0.02 1 579 . 57 SER HA H 4.50 0.02 1 580 . 57 SER HB2 H 3.88 0.02 2 581 . 57 SER HB3 H 3.79 0.02 2 582 . 57 SER C C 174.4 0.10 1 583 . 57 SER CA C 58.0 0.10 1 584 . 57 SER CB C 62.9 0.10 1 585 . 57 SER N N 118.4 0.10 1 586 . 58 GLY H H 7.82 0.02 1 587 . 58 GLY HA2 H 4.30 0.02 2 588 . 58 GLY HA3 H 3.93 0.02 2 589 . 58 GLY C C 174.6 0.10 1 590 . 58 GLY CA C 44.5 0.10 1 591 . 58 GLY N N 111.9 0.10 1 592 . 59 ALA H H 8.59 0.02 1 593 . 59 ALA HA H 4.13 0.02 1 594 . 59 ALA HB H 1.40 0.02 1 595 . 59 ALA C C 179.1 0.10 1 596 . 59 ALA CA C 54.3 0.10 1 597 . 59 ALA CB C 18.7 0.10 1 598 . 59 ALA N N 123.5 0.10 1 599 . 60 LYS H H 8.37 0.02 1 600 . 60 LYS HA H 4.37 0.02 1 601 . 60 LYS HB2 H 1.80 0.02 2 602 . 60 LYS HB3 H 1.53 0.02 2 603 . 60 LYS HG2 H 1.27 0.02 2 604 . 60 LYS HG3 H 1.15 0.02 2 605 . 60 LYS HD2 H 1.50 0.02 1 606 . 60 LYS HD3 H 1.50 0.02 1 607 . 60 LYS HE2 H 2.82 0.02 1 608 . 60 LYS HE3 H 2.82 0.02 1 609 . 60 LYS C C 175.9 0.10 1 610 . 60 LYS CA C 55.2 0.10 1 611 . 60 LYS CB C 31.8 0.10 1 612 . 60 LYS CG C 24.7 0.10 1 613 . 60 LYS CD C 28.4 0.10 1 614 . 60 LYS CE C 42.1 0.10 1 615 . 60 LYS N N 115.2 0.10 1 616 . 61 GLY H H 7.51 0.02 1 617 . 61 GLY HA2 H 4.36 0.02 2 618 . 61 GLY HA3 H 3.83 0.02 2 619 . 61 GLY CA C 44.2 0.10 1 620 . 61 GLY N N 108.2 0.10 1 621 . 62 PRO HA H 4.89 0.02 1 622 . 62 PRO HB2 H 2.32 0.02 2 623 . 62 PRO HB3 H 1.94 0.02 2 624 . 62 PRO HG2 H 2.24 0.02 2 625 . 62 PRO HG3 H 2.09 0.02 2 626 . 62 PRO HD2 H 3.74 0.02 2 627 . 62 PRO HD3 H 3.68 0.02 2 628 . 62 PRO C C 175.6 0.10 1 629 . 62 PRO CA C 63.0 0.10 1 630 . 62 PRO CB C 32.7 0.10 1 631 . 62 PRO CG C 29.9 0.10 1 632 . 62 PRO CD C 56.0 0.10 1 633 . 63 ALA H H 8.79 0.02 1 634 . 63 ALA HA H 5.18 0.02 1 635 . 63 ALA HB H 1.51 0.02 1 636 . 63 ALA C C 175.2 0.10 1 637 . 63 ALA CA C 50.7 0.10 1 638 . 63 ALA CB C 22.0 0.10 1 639 . 63 ALA N N 126.0 0.10 1 640 . 64 ALA H H 8.90 0.02 1 641 . 64 ALA HA H 5.09 0.02 1 642 . 64 ALA HB H 0.95 0.02 1 643 . 64 ALA C C 177.4 0.10 1 644 . 64 ALA CA C 50.9 0.10 1 645 . 64 ALA CB C 20.1 0.10 1 646 . 64 ALA N N 122.1 0.10 1 647 . 65 GLY H H 9.29 0.02 1 648 . 65 GLY HA2 H 4.67 0.02 2 649 . 65 GLY HA3 H 3.59 0.02 2 650 . 65 GLY C C 172.9 0.10 1 651 . 65 GLY CA C 43.5 0.10 1 652 . 65 GLY N N 108.7 0.10 1 653 . 66 ASN H H 9.22 0.02 1 654 . 66 ASN HA H 4.18 0.02 1 655 . 66 ASN HB2 H 2.81 0.02 1 656 . 66 ASN HB3 H 2.81 0.02 1 657 . 66 ASN HD21 H 7.57 0.02 1 658 . 66 ASN HD22 H 6.87 0.02 1 659 . 66 ASN C C 174.1 0.10 1 660 . 66 ASN CA C 54.3 0.10 1 661 . 66 ASN CB C 38.0 0.10 1 662 . 66 ASN N N 116.4 0.10 1 663 . 66 ASN ND2 N 114.4 0.10 1 664 . 67 VAL H H 8.19 0.02 1 665 . 67 VAL HA H 4.68 0.02 1 666 . 67 VAL HB H 1.82 0.02 1 667 . 67 VAL HG1 H 0.68 0.02 1 668 . 67 VAL HG2 H 0.68 0.02 1 669 . 67 VAL C C 176.0 0.10 1 670 . 67 VAL CA C 63.3 0.10 1 671 . 67 VAL CB C 31.0 0.10 1 672 . 67 VAL CG1 C 21.4 0.10 1 673 . 67 VAL CG2 C 21.4 0.10 1 674 . 67 VAL N N 118.1 0.10 1 675 . 68 THR H H 9.05 0.02 1 676 . 68 THR HA H 4.76 0.02 1 677 . 68 THR HB H 4.16 0.02 1 678 . 68 THR HG2 H 1.13 0.02 1 679 . 68 THR C C 173.9 0.10 1 680 . 68 THR CA C 59.6 0.10 1 681 . 68 THR CB C 71.7 0.10 1 682 . 68 THR N N 120.6 0.10 1 683 . 69 SER H H 8.81 0.02 1 684 . 69 SER HA H 4.66 0.02 1 685 . 69 SER HB3 H 3.93 0.02 1 686 . 69 SER HB2 H 3.83 0.02 1 687 . 69 SER C C 173.8 0.10 1 688 . 69 SER CA C 59.3 0.10 1 689 . 69 SER CB C 63.2 0.10 1 690 . 69 SER N N 119.5 0.10 1 691 . 70 LEU H H 8.00 0.02 1 692 . 70 LEU HA H 4.26 0.02 1 693 . 70 LEU HB2 H 1.39 0.02 1 694 . 70 LEU HB3 H 1.39 0.02 1 695 . 70 LEU HG H 1.61 0.02 1 696 . 70 LEU HD1 H 0.89 0.02 1 697 . 70 LEU HD2 H 0.89 0.02 1 698 . 70 LEU CA C 56.3 0.10 1 699 . 70 LEU CB C 43.3 0.10 1 700 . 70 LEU CG C 27.8 0.10 1 701 . 70 LEU CD1 C 26.4 0.10 2 702 . 70 LEU CD2 C 24.3 0.10 2 703 . 70 LEU N N 131.1 0.10 1 stop_ save_