data_4107 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Acid Denatured Cold Shock Protein A (CspA) ; _BMRB_accession_number 4107 _BMRB_flat_file_name bmr4107.str _Entry_type original _Submission_date 1998-02-16 _Accession_date 1998-02-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; NMR assignments for acid denatured (pH 2, temperature = 20 C) cold shock protein A. Residual structure in the acid denatured protein induces aggregation, and eventually fibril formation. NMR experiments aimed at understanding the mechanisms of aggregation & polymerization are in progress. NMR assignments for acid denatured CspA made use of additional data for the acid/urea denatured protein (pH 2.7/ 6M urea), to overcome problems with broad lines in the acid denatured state. The acid & acid/urea denatured forms of the protein are in fast exchange. NMR assignments for the acid/urea denatured protein have been deposited in a separate entry. Denatured (e.g. non-native) protein. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alexandrescu Andrei T. . 2 Rathgeb-Szabo K. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 222 "13C chemical shifts" 124 "15N chemical shifts" 66 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1998-03-04 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4108 'chemical shifts for CspA in the acid/urea denatured state' stop_ _Original_release_date 1998-03-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Alexandrescu, A. T., and Rathgeb-Szabo, K., "NMR Assignments for Acid-Denatured Cold Shock Protein A," J. Biomol. NMR 11, 461-462 (1998). ; _Citation_title 'NMR Assignments for Acid-Denatured Cold Shock Protein A' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98356294 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alexandrescu Andrei T. . 2 Rathgeb-Szabo K. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 11 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 461 _Page_last 462 _Year 1998 _Details . loop_ _Keyword aggregation CspA 'fibril formation' 'protein folding' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., Sykes, B. D., "1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR," J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_CspA _Saveframe_category molecular_system _Mol_system_name CspA _Abbreviation_common CspA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CspA $CspA stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'transcription regulator' 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 2015-08-11 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 4108 "Cold shock protein A" 100.00 70 100.00 100.00 1.53e-41 BMRB 4296 "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 $CspA 'E. coli' 562 Eubacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Details $CspA 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET11-cspA ; synthetic (Clone is a gift from M. Inouye, Rutgers University: Reference - S. Chatterjee, W. Jiang, S.D. Emerson, M. Inouye, "The Backbone Structure of the Major Cold-Shock Protein CS7.4 of Escherichia coli in Solution Includes Extensive B-sheet Structure", J. Biochem., 114, pp 663-669, (1993).) ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CspA 1 mM [U-15N] stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CspA 2 mM [U-15N;U-13C] stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity+600 _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.0 0.2 n/a temperature 293 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio_citation_label DSS C 13 methyl ppm 0.00 external indirect . . . 0.251449530 $citation_one DSS H 1 methyl ppm 0.00 internal direct . . . . . DSS N 15 methyl ppm 0.00 external indirect . . . 0.101329118 $citation_one 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_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name CspA _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 CA C 57.6 0.4 1 2 . 2 SER CB C 63.2 0.4 1 3 . 3 GLY H H 8.65 0.01 1 4 . 3 GLY HA2 H 3.93 0.01 2 5 . 3 GLY CA C 45.2 0.4 1 6 . 3 GLY N N 109.6 0.1 1 7 . 4 LYS H H 8.31 0.01 1 8 . 4 LYS HA H 4.29 0.01 1 9 . 4 LYS HB2 H 1.71 0.01 4 10 . 4 LYS HG2 H 1.35 0.01 4 11 . 4 LYS CA C 56.3 0.4 1 12 . 4 LYS CB C 33.1 0.4 1 13 . 4 LYS N N 121.3 0.1 1 14 . 5 MET H H 8.47 0.01 1 15 . 5 MET HA H 4.5 0.01 1 16 . 5 MET HB2 H 1.99 0.01 2 17 . 5 MET HG2 H 2.49 0.01 2 18 . 5 MET CA C 55.5 0.4 1 19 . 5 MET CB C 33.1 0.4 1 20 . 5 MET N N 122.2 0.1 1 21 . 6 THR H H 8.1 0.01 1 22 . 6 THR HA H 4.29 0.01 4 23 . 6 THR HG2 H 1.13 0.01 1 24 . 6 THR CA C 61.9 0.4 1 25 . 6 THR CB C 70.1 0.4 1 26 . 6 THR N N 115.6 0.1 1 27 . 7 GLY H H 8.34 0.01 1 28 . 7 GLY HA2 H 3.86 0.01 2 29 . 7 GLY CA C 45.2 0.4 1 30 . 7 GLY N N 111.1 0.1 1 31 . 8 ILE H H 7.94 0.01 1 32 . 8 ILE HA H 4.07 0.01 1 33 . 8 ILE HB H 1.78 0.01 1 34 . 8 ILE HG2 H 0.78 0.01 1 35 . 8 ILE HD1 H 1.06 0.01 1 36 . 8 ILE CA C 61.1 0.4 1 37 . 8 ILE CB C 38.7 0.4 1 38 . 8 ILE N N 120.4 0.1 1 39 . 9 VAL H H 8.13 0.01 1 40 . 9 VAL HA H 3.93 0.01 1 41 . 9 VAL HB H 1.85 0.01 1 42 . 9 VAL HG1 H 0.78 0.01 2 43 . 9 VAL CA C 62.4 0.4 1 44 . 9 VAL CB C 32.7 0.4 1 45 . 9 VAL N N 125.2 0.1 1 46 . 10 LYS H H 8.19 0.01 1 47 . 10 LYS HA H 4.14 0.01 1 48 . 10 LYS HB2 H 1.49 0.01 4 49 . 10 LYS HG2 H 1.21 0.01 4 50 . 10 LYS CA C 61.9 0.4 1 51 . 10 LYS CB C 33.1 0.4 1 52 . 10 LYS N N 125.3 0.1 1 53 . 11 TRP H H 7.96 0.01 1 54 . 11 TRP HA H 4.57 0.01 1 55 . 11 TRP HB2 H 3.14 0.01 2 56 . 11 TRP CA C 57.2 0.4 1 57 . 11 TRP CB C 30.1 0.4 1 58 . 11 TRP N N 122.00 0.1 1 59 . 12 PHE H H 7.82 0.01 1 60 . 12 PHE HA H 4.36 0.01 1 61 . 12 PHE HB2 H 2.78 0.01 2 62 . 12 PHE CA C 57.2 0.4 1 63 . 12 PHE CB C 39.6 0.4 1 64 . 12 PHE N N 121.8 0.1 1 65 . 13 ASN H H 8.05 0.01 1 66 . 13 ASN HA H 4.43 0.01 1 67 . 13 ASN HB2 H 2.64 0.01 2 68 . 13 ASN HB3 H 2.49 0.01 2 69 . 13 ASN CA C 52.9 0.4 1 70 . 13 ASN CB C 38.7 0.4 1 71 . 13 ASN N N 120.7 0.1 1 72 . 14 ALA H H 8.08 0.01 1 73 . 14 ALA HA H 4.07 0.01 1 74 . 14 ALA HB H 1.28 0.01 1 75 . 14 ALA CB C 18.9 0.4 1 76 . 14 ALA N N 124.5 0.1 1 77 . 15 ASP H H 8.21 0.01 1 78 . 15 ASP HA H 4.5 0.01 1 79 . 15 ASP HB2 H 2.78 0.01 2 80 . 15 ASP CA C 52.9 0.4 1 81 . 15 ASP CB C 37.9 0.4 1 82 . 15 ASP N N 117.1 0.1 1 83 . 16 LYS H H 7.99 0.01 1 84 . 16 LYS HA H 4.14 0.01 1 85 . 16 LYS HB2 H 1.64 0.01 4 86 . 16 LYS HG2 H 1.28 0.01 4 87 . 16 LYS CA C 56.3 0.4 1 88 . 16 LYS N N 120.8 0.1 1 89 . 17 GLY H H 8.11 0.01 1 90 . 17 GLY HA2 H 3.78 0.01 2 91 . 17 GLY CA C 45.2 0.4 1 92 . 17 GLY N N 109.00 0.1 1 93 . 18 PHE H H 8.01 0.01 1 94 . 18 PHE HA H 4.5 0.01 1 95 . 18 PHE HB2 H 2.93 0.01 2 96 . 18 PHE CA C 58.1 0.4 1 97 . 18 PHE CB C 39.6 0.4 1 98 . 18 PHE N N 119.8 0.1 1 99 . 19 GLY H H 8.23 0.01 1 100 . 19 GLY HA2 H 3.71 0.01 2 101 . 19 GLY CA C 45.2 0.4 1 102 . 19 GLY N N 110.2 0.1 1 103 . 20 PHE H H 7.88 0.01 1 104 . 20 PHE HA H 4.57 0.01 1 105 . 20 PHE HB2 H 2.93 0.01 2 106 . 20 PHE CA C 58.1 0.4 1 107 . 20 PHE CB C 39.6 0.4 1 108 . 20 PHE N N 119.8 0.1 1 109 . 21 ILE H H 8.03 0.01 1 110 . 21 ILE HA H 4.14 0.01 1 111 . 21 ILE HB H 1.71 0.01 1 112 . 21 ILE HG2 H 0.78 0.01 1 113 . 21 ILE CA C 60.6 0.4 1 114 . 21 ILE CB C 39.1 0.4 1 115 . 21 ILE N N 123.1 0.1 1 116 . 22 THR H H 8.16 0.01 1 117 . 22 THR HA H 4.5 0.01 4 118 . 22 THR HB H 4.07 0.01 4 119 . 22 THR HG2 H 1.21 0.01 1 120 . 22 THR CA C 59.8 0.4 1 121 . 22 THR CB C 63.6 0.4 1 122 . 22 THR N N 121.2 0.1 1 123 . 24 ASP H H 8.46 0.01 1 124 . 24 ASP HA H 4.64 0.01 1 125 . 24 ASP HB2 H 2.85 0.01 2 126 . 24 ASP CA C 53.3 0.4 1 127 . 24 ASP CB C 38.3 0.4 1 128 . 24 ASP N N 118.8 0.1 1 129 . 25 ASP H H 8.4 0.01 1 130 . 25 ASP HA H 4.64 0.01 1 131 . 25 ASP HB2 H 2.85 0.01 2 132 . 25 ASP CA C 52.9 0.4 1 133 . 25 ASP CB C 38.3 0.4 1 134 . 25 ASP N N 119.3 0.1 1 135 . 26 GLY H H 8.26 0.01 1 136 . 26 GLY HA2 H 3.86 0.01 2 137 . 26 GLY CA C 45.6 0.4 1 138 . 26 GLY N N 109.1 0.1 1 139 . 27 SER H H 8.05 0.01 1 140 . 27 SER HA H 4.36 0.01 1 141 . 27 SER HB2 H 3.78 0.01 2 142 . 27 SER CA C 58.5 0.4 1 143 . 27 SER CB C 64.1 0.4 1 144 . 27 SER N N 115.5 0.1 1 145 . 28 LYS H H 8.24 0.01 1 146 . 28 LYS HA H 4.21 0.01 1 147 . 28 LYS HB2 H 1.71 0.01 4 148 . 28 LYS HG2 H 1.35 0.01 4 149 . 28 LYS CA C 56.3 0.4 1 150 . 28 LYS CB C 33.1 0.4 1 151 . 28 LYS N N 122.5 0.1 1 152 . 29 ASP H H 8.33 0.01 1 153 . 29 ASP HA H 4.64 0.01 1 154 . 29 ASP HB2 H 2.85 0.01 2 155 . 29 ASP CA C 52.9 0.4 1 156 . 29 ASP CB C 37.9 0.4 1 157 . 29 ASP N N 119.5 0.1 1 158 . 30 VAL H H 7.84 0.01 1 159 . 30 VAL HA H 4.00 0.01 1 160 . 30 VAL HB H 1.92 0.01 1 161 . 30 VAL HG1 H 0.7 0.01 2 162 . 30 VAL CA C 62.4 0.4 1 163 . 30 VAL CB C 32.7 0.4 1 164 . 30 VAL N N 120.00 0.1 1 165 . 31 PHE H H 8.15 0.01 1 166 . 31 PHE HA H 4.57 0.01 1 167 . 31 PHE HB2 H 2.93 0.01 2 168 . 31 PHE CA C 57.6 0.4 1 169 . 31 PHE CB C 39.6 0.4 1 170 . 31 PHE N N 123.7 0.1 1 171 . 32 VAL H H 7.89 0.01 1 172 . 32 VAL HA H 3.93 0.01 1 173 . 32 VAL HB H 1.78 0.01 1 174 . 32 VAL HG1 H 0.7 0.01 2 175 . 32 VAL CA C 62.4 0.4 1 176 . 32 VAL CB C 33.1 0.4 1 177 . 32 VAL N N 121.8 0.1 1 178 . 33 HIS H H 8.37 0.01 1 179 . 33 HIS HA H 4.57 0.01 1 180 . 33 HIS HB2 H 3.07 0.01 2 181 . 33 HIS CA C 55.00 0.4 1 182 . 33 HIS CB C 29.3 0.4 1 183 . 33 HIS N N 122.00 0.1 1 184 . 34 PHE H H 8.27 0.01 1 185 . 34 PHE HA H 4.57 0.01 1 186 . 34 PHE HB2 H 3.00 0.01 2 187 . 34 PHE CA C 58.1 0.4 1 188 . 34 PHE CB C 40.00 0.4 1 189 . 34 PHE N N 122.7 0.1 1 190 . 35 SER H H 8.2 0.01 1 191 . 35 SER HA H 4.29 0.01 1 192 . 35 SER HB2 H 3.71 0.01 2 193 . 35 SER CA C 58.1 0.4 1 194 . 35 SER CB C 64.1 0.4 1 195 . 35 SER N N 118.00 0.1 1 196 . 36 ALA H H 8.25 0.01 1 197 . 36 ALA HA H 4.21 0.01 1 198 . 36 ALA HB H 1.35 0.01 1 199 . 36 ALA CA C 52.9 0.4 1 200 . 36 ALA CB C 19.4 0.4 1 201 . 36 ALA N N 126.3 0.1 1 202 . 37 ILE H H 7.93 0.01 1 203 . 37 ILE HA H 4.00 0.01 1 204 . 37 ILE HB H 1.78 0.01 1 205 . 37 ILE HG2 H 0.78 0.01 1 206 . 37 ILE HD1 H 1.13 0.01 1 207 . 37 ILE CA C 61.5 0.4 1 208 . 37 ILE CB C 38.7 0.4 1 209 . 37 ILE N N 119.3 0.1 1 210 . 38 GLN H H 8.27 0.01 1 211 . 38 GLN HA H 4.21 0.01 1 212 . 38 GLN HB2 H 1.92 0.01 2 213 . 38 GLN HG2 H 2.28 0.01 2 214 . 38 GLN CA C 55.9 0.4 1 215 . 38 GLN CB C 29.3 0.4 1 216 . 38 GLN N N 124.1 0.1 1 217 . 39 ASN H H 8.39 0.01 1 218 . 39 ASN HA H 4.64 0.01 1 219 . 39 ASN HB2 H 2.71 0.01 2 220 . 39 ASN CA C 53.3 0.4 1 221 . 39 ASN CB C 38.7 0.4 1 222 . 39 ASN N N 120.00 0.1 1 223 . 40 ASP H H 8.3 0.01 1 224 . 40 ASP HA H 4.64 0.01 1 225 . 40 ASP HB2 H 2.71 0.01 2 226 . 40 ASP CA C 52.9 0.4 1 227 . 40 ASP CB C 37.9 0.4 1 228 . 40 ASP N N 119.6 0.1 1 229 . 41 GLY H H 8.29 0.01 1 230 . 41 GLY HA2 H 3.78 0.01 2 231 . 41 GLY CA C 45.6 0.4 1 232 . 41 GLY N N 109.00 0.1 1 233 . 42 TYR H H 7.89 0.01 1 234 . 42 TYR HA H 4.43 0.01 1 235 . 42 TYR HB2 H 2.92 0.01 2 236 . 42 TYR CA C 58.1 0.4 1 237 . 42 TYR CB C 38.7 0.4 1 238 . 42 TYR N N 120.1 0.1 1 239 . 43 LYS H H 8.03 0.01 1 240 . 43 LYS HA H 4.21 0.01 1 241 . 43 LYS HB2 H 1.64 0.01 4 242 . 43 LYS HG2 H 1.28 0.01 4 243 . 43 LYS CA C 56.3 0.4 1 244 . 43 LYS CB C 33.1 0.4 1 245 . 43 LYS N N 123.1 0.1 1 246 . 44 SER H H 8.07 0.01 1 247 . 44 SER HA H 4.29 0.01 1 248 . 44 SER HB2 H 3.78 0.01 2 249 . 44 SER CA C 58.5 0.4 1 250 . 44 SER CB C 63.6 0.4 1 251 . 44 SER N N 116.3 0.1 1 252 . 45 LEU H H 8.15 0.01 1 253 . 45 LEU HA H 4.29 0.01 1 254 . 45 LEU HB2 H 1.56 0.01 2 255 . 45 LEU HD1 H 0.78 0.01 2 256 . 45 LEU CA C 55.5 0.4 1 257 . 45 LEU CB C 42.2 0.4 1 258 . 45 LEU N N 123.7 0.1 1 259 . 46 ASP H H 8.38 0.01 1 260 . 46 ASP HA H 4.64 0.01 1 261 . 46 ASP HB2 H 2.78 0.01 2 262 . 46 ASP CA C 53.3 0.4 1 263 . 46 ASP CB C 37.9 0.4 1 264 . 46 ASP N N 119.00 0.1 1 265 . 47 GLU H H 8.22 0.01 1 266 . 47 GLU HA H 4.29 0.01 1 267 . 47 GLU HB2 H 2.07 0.01 2 268 . 47 GLU HB3 H 1.92 0.01 2 269 . 47 GLU HG2 H 2.42 0.01 2 270 . 47 GLU CA C 56.3 0.4 1 271 . 47 GLU CB C 28.8 0.4 1 272 . 47 GLU N N 120.6 0.1 1 273 . 48 GLY H H 8.33 0.01 1 274 . 48 GLY HA2 H 3.86 0.01 1 275 . 48 GLY CA C 45.6 0.4 1 276 . 48 GLY N N 109.4 0.1 1 277 . 49 GLN H H 8.08 0.01 1 278 . 49 GLN HA H 4.21 0.01 1 279 . 49 GLN HB2 H 1.92 0.01 2 280 . 49 GLN HG2 H 2.28 0.01 2 281 . 49 GLN CA C 55.9 0.4 1 282 . 49 GLN CB C 29.7 0.4 1 283 . 49 GLN N N 119.8 0.1 1 284 . 50 LYS H H 8.31 0.01 1 285 . 50 LYS HA H 4.29 0.01 1 286 . 50 LYS HB2 H 1.71 0.01 4 287 . 50 LYS HG2 H 1.35 0.01 4 288 . 50 LYS CA C 56.3 0.4 1 289 . 50 LYS CB C 33.1 0.4 1 290 . 50 LYS N N 122.9 0.1 1 291 . 51 VAL H H 8.09 0.01 1 292 . 51 VAL HA H 4.07 0.01 1 293 . 51 VAL HB H 1.92 0.01 1 294 . 51 VAL HG1 H 0.78 0.01 2 295 . 51 VAL CA C 62.4 0.4 1 296 . 51 VAL CB C 33.1 0.4 1 297 . 51 VAL N N 121.5 0.1 1 298 . 52 SER H H 8.23 0.01 1 299 . 52 SER HA H 4.36 0.01 1 300 . 52 SER HB2 H 3.71 0.01 2 301 . 52 SER CA C 58.1 0.4 1 302 . 52 SER CB C 64.1 0.4 1 303 . 52 SER N N 119.3 0.1 1 304 . 53 PHE H H 8.19 0.01 1 305 . 53 PHE HA H 4.64 0.01 1 306 . 53 PHE HB2 H 3.00 0.01 2 307 . 53 PHE CA C 57.6 0.4 1 308 . 53 PHE CB C 40.00 0.4 1 309 . 53 PHE N N 122.5 0.1 1 310 . 54 THR H H 8.09 0.01 1 311 . 54 THR HA H 4.29 0.01 4 312 . 54 THR HB H 4.00 0.01 4 313 . 54 THR HG2 H 1.06 0.01 1 314 . 54 THR CA C 61.9 0.4 1 315 . 54 THR CB C 70.1 0.4 1 316 . 54 THR N N 116.6 0.1 1 317 . 55 ILE H H 8.14 0.01 1 318 . 55 ILE HA H 4.07 0.01 1 319 . 55 ILE HB H 1.78 0.01 1 320 . 55 ILE HG2 H 0.85 0.01 1 321 . 55 ILE HD1 H 1.12 0.01 1 322 . 55 ILE CA C 61.5 0.4 1 323 . 55 ILE CB C 38.7 0.4 1 324 . 55 ILE N N 123.7 0.1 1 325 . 56 GLU H H 8.38 0.01 1 326 . 56 GLU HA H 4.36 0.01 1 327 . 56 GLU HB2 H 2.06 0.01 2 328 . 56 GLU HB3 H 1.92 0.01 2 329 . 56 GLU HG2 H 2.42 0.01 2 330 . 56 GLU CA C 55.9 0.4 1 331 . 56 GLU CB C 28.8 0.4 1 332 . 56 GLU N N 124.6 0.1 1 333 . 57 SER H H 8.3 0.01 1 334 . 57 SER HA H 4.36 0.01 1 335 . 57 SER HB2 H 3.78 0.01 2 336 . 57 SER CA C 58.5 0.4 1 337 . 57 SER CB C 64.1 0.4 1 338 . 57 SER N N 117.3 0.1 1 339 . 58 GLY H H 8.34 0.01 1 340 . 58 GLY HA2 H 3.86 0.01 2 341 . 58 GLY CA C 45.2 0.4 1 342 . 58 GLY N N 111.1 0.1 1 343 . 59 ALA H H 8.05 0.01 1 344 . 59 ALA HA H 4.21 0.01 1 345 . 59 ALA HB H 1.35 0.01 1 346 . 59 ALA CA C 52.5 0.4 1 347 . 59 ALA CB C 19.4 0.4 1 348 . 59 ALA N N 123.8 0.1 1 349 . 60 LYS H H 8.28 0.01 1 350 . 60 LYS HA H 4.29 0.01 1 351 . 60 LYS HB2 H 1.71 0.01 4 352 . 60 LYS HG2 H 1.42 0.01 4 353 . 60 LYS CA C 56.3 0.4 1 354 . 60 LYS CB C 33.6 0.4 1 355 . 60 LYS N N 120.4 0.1 1 356 . 61 GLY H H 8.13 0.01 1 357 . 61 GLY HA2 H 4.00 0.01 2 358 . 61 GLY CA C 44.7 0.4 1 359 . 61 GLY N N 110.00 0.1 1 360 . 62 PRO HA H 4.36 0.01 1 361 . 62 PRO CA C 63.2 0.4 1 362 . 62 PRO CB C 32.3 0.4 1 363 . 63 ALA H H 8.35 0.01 1 364 . 63 ALA HA H 4.21 0.01 1 365 . 63 ALA HB H 1.35 0.01 1 366 . 63 ALA CA C 52.5 0.4 1 367 . 63 ALA CB C 19.4 0.4 1 368 . 63 ALA N N 124.3 0.1 1 369 . 64 ALA H H 8.16 0.01 1 370 . 64 ALA HA H 4.21 0.01 1 371 . 64 ALA HB H 1.35 0.01 1 372 . 64 ALA CA C 52.5 0.4 1 373 . 64 ALA CB C 19.4 0.4 1 374 . 64 ALA N N 123.2 0.1 1 375 . 65 GLY H H 8.22 0.01 1 376 . 65 GLY HA2 H 3.86 0.01 2 377 . 65 GLY CA C 45.2 0.4 1 378 . 65 GLY N N 107.6 0.1 1 379 . 66 ASN H H 8.22 0.01 1 380 . 66 ASN HA H 4.71 0.01 1 381 . 66 ASN HB2 H 2.71 0.01 2 382 . 66 ASN CA C 53.3 0.4 1 383 . 66 ASN CB C 39.1 0.4 1 384 . 66 ASN N N 118.7 0.1 1 385 . 67 VAL H H 8.11 0.01 1 386 . 67 VAL HA H 4.14 0.01 1 387 . 67 VAL HB H 2.07 0.01 1 388 . 67 VAL HG1 H 0.85 0.01 2 389 . 67 VAL CA C 62.4 0.4 1 390 . 67 VAL CB C 32.7 0.4 1 391 . 67 VAL N N 120.3 0.1 1 392 . 68 THR H H 8.21 0.01 1 393 . 68 THR HA H 4.14 0.01 4 394 . 68 THR HB H 4.29 0.01 4 395 . 68 THR HG2 H 1.13 0.01 1 396 . 68 THR CA C 61.9 0.4 1 397 . 68 THR CB C 69.7 0.4 1 398 . 68 THR N N 117.9 0.1 1 399 . 69 SER H H 8.2 0.01 1 400 . 69 SER HA H 4.43 0.01 1 401 . 69 SER HB2 H 3.78 0.01 2 402 . 69 SER CA C 58.1 0.4 1 403 . 69 SER CB C 64.1 0.4 1 404 . 69 SER N N 118.5 0.1 1 405 . 70 LEU H H 8.25 0.01 1 406 . 70 LEU HA H 4.36 0.01 1 407 . 70 LEU HB2 H 1.56 0.01 2 408 . 70 LEU HD1 H 0.85 0.01 2 409 . 70 LEU HD2 H 0.78 0.01 2 410 . 70 LEU CA C 54.2 0.4 1 411 . 70 LEU CB C 42.4 0.4 1 412 . 70 LEU N N 124.6 0.1 1 stop_ save_