data_4107 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Acid Denatured Cold Shock Protein A (CspA) ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Alexandrescu Andrei T. . 2 Rathgeb-Szabo K. . . stop_ _BMRB_accession_number 4107 _BMRB_flat_file_name bmr4107.str _Entry_type new _Submission_date 1998-02-16 _Accession_date 1998-02-17 _Entry_origination author _NMR_STAR_version 2.1 _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_ _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_ _Related_BMRB_accession_number _Relationship 4108 'chemical shifts for CspA in the acid/urea denatured state' stop_ 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 _MEDLINE_UI_code 98356294 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 _Page_first 461 _Page_last 462 _Year 1998 loop_ _Keyword CspA 'protein folding' 'fibril formation' aggregation stop_ save_ ################################## # Molecular system description # ################################## save_system_CspA _Saveframe_category molecular_system _Mol_system_name CspA _Abbreviation_common CspA loop_ _Mol_system_component_name _Mol_label CspA $CspA stop_ _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no loop_ _Biological_function 'transcription regulator' stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1MJC "Major Cold Shock Protein 7.4 (Cspa (Cs 7.4)) Of (Escherichia Coli)" . PDB 3MEF "A Chain A, Major Cold-Shock Protein From Escherichia Coli Solution Nmr Structure" . stop_ 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 ############################## # 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 2008-06-26 _Sequence_homology_query_revised_last_date 2008-06-26 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 1.55e-32 BMRB 4296 "Cold shock protein A" 100.00 70 100.00 100.00 1.55e-32 PDB 1MJC "Crystal Structure Of Cspa, The Major Cold Shock Protein Of Escherichia Coli" 98.57 69 100.00 100.00 9.99e-32 PDB 3MEF "Major Cold-Shock Protein From Escherichia Coli Solution Nmr Structure" 97.14 69 100.00 100.00 2.74e-31 DBJ BAB37864 "cold shock protein 7.4 [Escherichia coli O157:H7 str. Sakai]" 100.00 70 100.00 100.00 1.55e-32 DBJ BAE77739 "major cold shock protein [Escherichia coli W3110]" 100.00 70 100.00 100.00 1.55e-32 EMBL CAD07979 "cold shock protein [Salmonella enterica subsp. enterica serovar Typhi]" 100.00 70 100.00 100.00 1.55e-32 GenBank AAA23617 "cold shock protein (cspA)" 100.00 70 100.00 100.00 1.55e-32 GenBank AAB18533 "cold regulated [Escherichia coli]" 100.00 70 100.00 100.00 1.55e-32 GenBank AAB66357 "DNA-binding protein" 100.00 70 98.57 98.57 4.60e-32 GenBank AAB69447 "cold shock protein [Salmonella enteritidis]" 100.00 70 100.00 100.00 1.55e-32 GenBank AAC06036 "cold shock protein A [Salmonella typhimurium]" 100.00 70 100.00 100.00 1.55e-32 PIR AG0981 "cold shock protein [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 70 100.00 100.00 1.55e-32 REF AP_004238 "major cold shock protein [Escherichia coli W3110]" 100.00 70 100.00 100.00 1.55e-32 REF NP_290141 "major cold shock protein [Escherichia coli O157:H7 EDL933]" 100.00 70 100.00 100.00 1.55e-32 REF NP_312468 "major cold shock protein [Escherichia coli O157:H7 str. Sakai]" 100.00 70 100.00 100.00 1.55e-32 REF NP_418012 "major cold shock protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 70 100.00 100.00 1.55e-32 REF NP_458276 "major cold shock protein [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 70 100.00 100.00 1.55e-32 SWISS-PROT P0A9X9 "Cold shock protein cspA (CSP-A) (7.4 kDa cold shock protein) (CS7.4)" 100.00 70 100.00 100.00 1.55e-32 SWISS-PROT P0A9Y0 "Cold shock protein cspA (CSP-A) (7.4 kDa cold shock protein) (CS7.4)" 100.00 70 100.00 100.00 1.55e-32 SWISS-PROT P0A9Y1 "Cold shock protein cspA (CSP-A) (7.4 kDa cold shock protein) (CS7.4)" 100.00 70 100.00 100.00 1.55e-32 SWISS-PROT P0A9Y2 "Cold shock protein cspA (CSP-A) (7.4 kDa cold shock protein) (CS7.4)" 100.00 70 100.00 100.00 1.55e-32 SWISS-PROT P0A9Y3 "Cold shock protein cspA (CSP-A) (7.4 kDa cold shock protein) (CS7.4)" 100.00 70 100.00 100.00 1.55e-32 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 $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 _Gene_source _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 loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CspA 1 mM . . '[U-15N]' stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _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 save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions 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 loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _Indirect_shift_ratio _Indirect_shift_ratio_citation_label DSS H 1 methyl ppm 0.00 internal direct . . DSS C 13 methyl ppm 0.00 external indirect 0.251449530 $citation_one 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 # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts 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 loop_ _Atom_shift_assign_ID _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_ ####################################### # 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). ; save_