data_4116 #Corrected using PDB structure: 2GYKE # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 48 S H 10.86 8.26 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.07 1.61 1.91 N/A -1.29 -0.21 # #bmr4116.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4116.str file): #HA CA CB CO N HN #N/A +1.76 +1.76 N/A -1.29 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 +/-0.21 +/-0.20 N/A +/-0.39 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.917 0.983 0.998 N/A 0.810 0.715 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.099 0.946 0.886 N/A 1.744 0.237 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Chemical Shift Assignments of the Colicin E9 Immunity Protein from Escherichia coli ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boetzel R. . . 2 Czisch M. . . 3 MacDonald C. J. . 4 Kaptein R. . . 5 Hemmings A. M. . 5 James Richard . . 6 Kleanthous Colin . . 7 Moore Geoffrey R. . stop_ _BMRB_accession_number 4116 _BMRB_flat_file_name bmr4116.str _Entry_type new _Submission_date 1997-03-04 _Accession_date 1997-03-04 _Entry_origination author _NMR_STAR_version 2.1 _Experimental_method NMR _Details ; The data reported here represents the immunity protein Im9 (residues 3-86) of colicin E9 DNase. This study reports 1H, 13C and 15N chemical shifts for backbone and sidechains obtained from triple-resonance data. ; loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 439 '13C chemical shifts' 239 '15N chemical shifts' 85 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Boetzel, R., Czisch, M., MacDonald, C. J., Kaptein, R., Hemmings, A.M., James, R., Kleanthous, C., Moore, G. R., "Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9," J. Biomol. NMR 12, 567-568 (1998). ; _Citation_title ; Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 99109973 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Boetzel R. . . 2 Czisch M. . . 3 MacDonald C. J. . 4 Kaptein R. . . 5 Hemmings A. M. . 5 James Richard . . 6 Kleanthous Colin . . 7 Moore Geoffrey R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 12 _Journal_issue 4 _Page_first 567 _Page_last 568 _Year 1998 loop_ _Keyword NMR 'nuclear magnetic resonance' protein 'resonance assignments' 'immunity protein' colicin 'secondary structure' 'protein-protein interaction' stop_ save_ ################################## # Molecular system description # ################################## save_system_IM9 _Saveframe_category molecular_system _Mol_system_name 'Im9 immunity protein' _Abbreviation_common IM9 loop_ _Mol_system_component_name _Mol_label IM9 $IM9 stop_ _System_physical_state native _System_oligomer_state monomer _System_type simple _System_paramagnetic no loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1EMV "A Chain A, Crystal Structure Of Colicin E9 Dnase Domain With Its Cognate Immunity Protein Im9 (1.7 Angstroms)" . PDB 1IMQ "Colicin E9 Immunity Protein Im9, Nmr, Minimized Average Structure" . PDB 1E0H "A Chain A, Inhibitor Protein Im9 Bound To Its Partner E9 Dnase" . PDB 1IMP "Colicin E9 Immunity Protein Im9, Nmr, 21 Structures" . stop_ save_ ######################## # Monomeric polymers # ######################## save_IM9 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Im9 immunity protein' _Name_variant . _Abbreviation_common IM9 ############################## # Polymer residue sequence # ############################## _Residue_count 86 _Mol_residue_sequence ; MELKHSISDYTEAEFLQLVT TICNADTSSEEELVKLVTHF EEMTEHPSGSDLIYYPKEGD DDSPSGIVNTVKQWRAANGK SGFKQG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLU 3 LEU 4 LYS 5 HIS 6 SER 7 ILE 8 SER 9 ASP 10 TYR 11 THR 12 GLU 13 ALA 14 GLU 15 PHE 16 LEU 17 GLN 18 LEU 19 VAL 20 THR 21 THR 22 ILE 23 CYS 24 ASN 25 ALA 26 ASP 27 THR 28 SER 29 SER 30 GLU 31 GLU 32 GLU 33 LEU 34 VAL 35 LYS 36 LEU 37 VAL 38 THR 39 HIS 40 PHE 41 GLU 42 GLU 43 MET 44 THR 45 GLU 46 HIS 47 PRO 48 SER 49 GLY 50 SER 51 ASP 52 LEU 53 ILE 54 TYR 55 TYR 56 PRO 57 LYS 58 GLU 59 GLY 60 ASP 61 ASP 62 ASP 63 SER 64 PRO 65 SER 66 GLY 67 ILE 68 VAL 69 ASN 70 THR 71 VAL 72 LYS 73 GLN 74 TRP 75 ARG 76 ALA 77 ALA 78 ASN 79 GLY 80 LYS 81 SER 82 GLY 83 PHE 84 LYS 85 GLN 86 GLY stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-01 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1E0H "A Chain A, Inhibitor Protein Im9 Bound ToIts Partner E9 Dnase" 100.00 86 100 100 10e-44 PDB 1EMV "A Chain A, Crystal Structure Of Colicin E9Dnase Domain With Its Cognate Immunity Protein Im9 (1.7Angstroms)" 100.00 86 100 100 3e-44 PDB 1IMP "Colicin E9 Immunity Protein Im9, Nmr, 21Structures" 100.00 86 100 100 10e-44 PDB 1IMQ "Colicin E9 Immunity Protein Im9, Nmr,Minimized Average Structure" 100.00 86 100 100 3e-44 PDB 1FR2 "A Chain A, Crystal Structure Of The E9 DnaseDomain With A Mutant Immunity Protein Im9(E41a)" 100.00 86 99 99 10e-44 PDB 1BXI "A Chain A, Crystal Structure Of TheEscherichia Coli Colicin E9 Dnase Domain With ItsCognate Immunity Protein Im9" 100.00 86 98 99 1e-42 EMBL CAA33863.1 "E9 immunity protein (86 AA) [PlasmidColE9-J]" 100.00 86 100 100 3e-44 GenBank AAA23076.1 "E9imm peptide" 100.00 86 99 100 10e-44 PIR A32535 "colicin E9 immunity protein - Escherichiacoli plasmid ColE9-J" 100.00 86 99 100 10e-44 SWISS-PROT P13479 "IMM9_ECOLI Colicin E9 immunity protein(ImmE9) (Microcin E9 immunity protein)" 100.00 86 100 100 3e-44 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 _Plasmid $IM9 '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 $IM9 'recombinant technology' 'E. coli' Escherichia coli JM1 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 _Isotopic_labeling $IM9 4.0 mM '[U-100%15N; U-100%13C]' H2O 90 % . D2O 10 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer ? _Model . _Field_strength 500 save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer ? _Model . _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 6.2 . na temperature 298 . 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 dioxane H 1 'methylene protons' ppm 3.77 internal direct . . C 13 . ppm . . . . DSS N 15 'methyl protons' ppm 0.00 . indirect 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD 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 stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name IM9 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 3 LEU H H 8.51 . 1 2 3 LEU N N 124.11 . 1 3 3 LEU HA H 4.45 . 1 4 3 LEU CA C 54.18 . 1 5 3 LEU HB2 H 1.57 . 1 6 3 LEU HB3 H 0.91 . 1 7 3 LEU CB C 40.94 . 1 8 3 LEU HG H 1.59 . 1 9 3 LEU HD1 H 0.65 . 1 10 3 LEU HD2 H 0.56 . 1 11 3 LEU CD1 C 24.41 . 1 12 3 LEU CD2 C 21.87 . 1 13 4 LYS H H 7.91 . 1 14 4 LYS N N 121.51 . 1 15 4 LYS HA H 4.35 . 1 16 4 LYS CA C 55.09 . 1 17 4 LYS HB2 H 1.34 . 1 18 4 LYS CB C 33.07 . 1 19 4 LYS HG2 H 1.16 . 1 20 4 LYS HG3 H 1.03 . 1 21 4 LYS CG C 25.32 . 1 22 4 LYS HD2 H 1.34 . 1 23 4 LYS HD3 H 1.21 . 1 24 4 LYS CD C 28.62 . 1 25 4 LYS HE2 H 2.75 . 1 26 4 LYS HE3 H 2.75 . 1 27 4 LYS CE C 42.07 . 1 28 5 HIS H H 8.86 . 1 29 5 HIS N N 114.91 . 1 30 5 HIS HA H 4.76 . 1 31 5 HIS CA C 56.91 . 1 32 5 HIS HB2 H 3.44 . 1 33 5 HIS HB3 H 3.28 . 1 34 5 HIS CB C 29.60 . 1 35 5 HIS HD2 H 7.35 . 1 36 5 HIS HE1 H 8.53 . 1 37 6 SER H H 8.02 . 1 38 6 SER N N 113.01 . 1 39 6 SER HA H 4.78 . 1 40 6 SER CA C 57.22 . 1 41 6 SER HB2 H 3.93 . 1 42 6 SER HB3 H 3.70 . 1 43 6 SER CB C 65.31 . 1 44 7 ILE H H 9.38 . 1 45 7 ILE N N 126.41 . 1 46 7 ILE HA H 4.12 . 1 47 7 ILE CA C 65.14 . 1 48 7 ILE HB H 1.66 . 1 49 7 ILE CB C 36.63 . 1 50 7 ILE HG12 H 0.92 . 1 51 7 ILE HG13 H 0.92 . 1 52 7 ILE CG1 C 30.24 . 1 53 7 ILE HG2 H 0.51 . 1 54 7 ILE CG2 C 14.98 . 1 55 7 ILE HD1 H -0.14 . 1 56 7 ILE CD1 C 12.71 . 1 57 8 SER H H 7.58 . 1 58 8 SER N N 112.11 . 1 59 8 SER HA H 4.80 . 1 60 8 SER CA C 58.84 . 1 61 8 SER HB2 H 3.98 . 1 62 8 SER HB3 H 3.91 . 1 63 8 SER CB C 62.97 . 1 64 9 ASP H H 7.95 . 1 65 9 ASP N N 117.71 . 1 66 9 ASP HA H 4.83 . 1 67 9 ASP CA C 54.56 . 1 68 9 ASP HB2 H 2.85 . 1 69 9 ASP CB C 42.50 . 1 70 10 TYR H H 8.31 . 1 71 10 TYR N N 119.81 . 1 72 10 TYR HA H 4.95 . 1 73 10 TYR CA C 58.19 . 1 74 10 TYR HB2 H 3.57 . 1 75 10 TYR HB3 H 3.57 . 1 76 10 TYR CB C 40.06 . 1 77 10 TYR HD1 H 7.46 . 1 78 10 TYR HD2 H 7.46 . 1 79 10 TYR HE1 H 7.01 . 1 80 10 TYR HE2 H 7.01 . 1 81 11 THR H H 8.97 . 1 82 11 THR N N 111.31 . 1 83 11 THR HA H 5.03 . 1 84 11 THR CA C 60.54 . 1 85 11 THR HB H 4.73 . 1 86 11 THR CB C 70.53 . 1 87 11 THR HG2 H 1.28 . 1 88 11 THR CG2 C 21.69 . 1 89 12 GLU H H 9.35 . 1 90 12 GLU N N 123.51 . 1 91 12 GLU HA H 2.44 . 1 92 12 GLU CA C 60.04 . 1 93 12 GLU HB2 H 1.86 . 1 94 12 GLU HB3 H 1.83 . 1 95 12 GLU CB C 28.89 . 1 96 12 GLU HG2 H 2.02 . 1 97 12 GLU HG3 H 1.81 . 1 98 12 GLU CG C 35.68 . 1 99 13 ALA H H 8.45 . 1 100 13 ALA N N 118.41 . 1 101 13 ALA HA H 4.12 . 1 102 13 ALA CA C 54.86 . 1 103 13 ALA HB H 1.43 . 1 104 13 ALA CB C 18.03 . 1 105 14 GLU H H 8.04 . 1 106 14 GLU N N 118.82 . 1 107 14 GLU HA H 4.17 . 1 108 14 GLU CA C 58.42 . 1 109 14 GLU HB2 H 2.76 . 1 110 14 GLU HB3 H 2.35 . 1 111 14 GLU CB C 31.17 . 1 112 14 GLU HG2 H 2.56 . 1 113 14 GLU HG3 H 2.45 . 1 114 14 GLU CG C 36.89 . 1 115 15 PHE H H 8.79 . 1 116 15 PHE N N 123.11 . 1 117 15 PHE HA H 3.93 . 1 118 15 PHE CA C 62.06 . 1 119 15 PHE HB2 H 2.89 . 1 120 15 PHE HB3 H 2.71 . 1 121 15 PHE CB C 40.31 . 1 122 16 LEU H H 9.09 . 1 123 16 LEU N N 119.21 . 1 124 16 LEU HA H 3.97 . 1 126 16 LEU HB2 H 2.08 . 1 127 16 LEU HB3 H 1.63 . 1 128 16 LEU CB C 40.85 . 1 129 16 LEU HG H 1.48 . 1 130 16 LEU CG C 27.01 . 1 131 16 LEU HD1 H 0.95 . 1 132 16 LEU HD2 H 0.84 . 1 133 16 LEU CD1 C 25.14 . 1 134 16 LEU CD2 C 23.33 . 1 135 17 GLN H H 7.95 . 1 136 17 GLN N N 121.81 . 1 137 17 GLN HA H 4.10 . 1 138 17 GLN CA C 58.79 . 1 139 17 GLN HB2 H 2.28 . 1 140 17 GLN HB3 H 2.28 . 1 141 17 GLN CB C 27.40 . 1 142 17 GLN HG2 H 2.48 . 1 143 17 GLN CG C 33.38 . 1 144 17 GLN HE21 H 7.49 . 1 145 17 GLN HE22 H 6.96 . 1 146 17 GLN NE2 N 112.85 . 1 147 18 LEU H H 7.54 . 1 148 18 LEU N N 122.91 . 1 149 18 LEU HB2 H 1.82 . 1 150 18 LEU HB3 H 1.58 . 1 151 18 LEU CB C 40.52 . 1 152 18 LEU HG H 1.44 . 1 153 18 LEU CG C 27.47 . 1 154 18 LEU HD1 H 1.06 . 1 155 18 LEU HD2 H 0.72 . 1 156 18 LEU CD1 C 24.71 . 1 157 18 LEU CD2 C 25.54 . 1 158 19 VAL H H 8.25 . 1 159 19 VAL N N 117.31 . 1 160 19 VAL HA H 3.16 . 1 161 19 VAL CA C 66.93 . 1 162 19 VAL HB H 1.94 . 1 163 19 VAL CB C 31.73 . 1 164 19 VAL HG1 H 0.90 . 1 165 19 VAL CG1 C 22.92 . 1 166 19 VAL HG2 H 0.78 . 1 167 19 VAL CG2 C 24.37 . 1 168 20 THR H H 8.75 . 1 169 20 THR N N 117.71 . 1 170 20 THR HA H 3.57 . 1 171 20 THR CA C 68.00 . 1 172 20 THR HB H 4.36 . 1 173 20 THR CB C 68.65 . 1 174 20 THR HG2 H 1.24 . 1 175 20 THR CG2 C 20.59 . 1 176 21 THR H H 8.18 . 1 177 21 THR N N 118.81 . 1 178 21 THR HA H 3.90 . 1 179 21 THR CA C 67.45 . 1 180 21 THR HB H 4.50 . 1 181 21 THR CB C 68.50 . 1 182 21 THR HG2 H 1.14 . 1 183 21 THR CG2 C 21.35 . 1 184 22 ILE H H 7.76 . 1 185 22 ILE N N 119.21 . 1 186 22 ILE HA H 3.46 . 1 187 22 ILE CA C 65.53 . 1 188 22 ILE HB H 1.77 . 1 189 22 ILE CB C 38.05 . 1 190 22 ILE HG12 H 1.85 . 1 191 22 ILE HG13 H 1.85 . 1 192 22 ILE CG1 C 28.86 . 1 193 22 ILE HG2 H 0.73 . 1 194 22 ILE CG2 C 18.09 . 1 195 22 ILE HD1 H 0.60 . 1 196 22 ILE CD1 C 13.89 . 1 197 23 CYS H H 8.87 . 1 198 23 CYS N N 118.91 . 1 199 23 CYS HA H 3.81 . 1 200 23 CYS CA C 64.11 . 1 201 23 CYS HB2 H 3.00 . 1 202 23 CYS HB3 H 2.68 . 1 203 23 CYS CB C 26.52 . 1 204 24 ASN H H 8.16 . 1 205 24 ASN N N 114.81 . 1 206 24 ASN HA H 4.68 . 1 207 24 ASN CA C 52.68 . 1 208 24 ASN HB2 H 2.98 . 1 209 24 ASN HB3 H 2.73 . 1 210 24 ASN CB C 38.00 . 1 211 24 ASN HD21 H 7.93 . 1 212 24 ASN HD22 H 7.00 . 1 213 24 ASN ND2 N 112.30 . 1 214 25 ALA H H 8.16 . 1 215 25 ALA N N 124.01 . 1 216 25 ALA HA H 3.91 . 1 217 25 ALA CA C 52.57 . 1 218 25 ALA HB H 1.50 . 1 219 25 ALA CB C 16.65 . 1 220 26 ASP H H 8.42 . 1 221 26 ASP N N 119.01 . 1 222 26 ASP HA H 4.91 . 1 223 26 ASP CA C 53.06 . 1 224 26 ASP HB2 H 2.91 . 1 225 26 ASP HB3 H 2.43 . 1 226 26 ASP CB C 40.17 . 1 227 27 THR H H 7.80 . 1 228 27 THR N N 107.81 . 1 229 27 THR HA H 4.62 . 1 230 27 THR CA C 59.65 . 1 231 27 THR HB H 4.49 . 1 232 27 THR CB C 70.80 . 1 233 27 THR HG2 H 0.97 . 1 234 27 THR CG2 C 22.16 . 1 235 28 SER H H 8.97 . 1 236 28 SER N N 115.11 . 1 237 28 SER HA H 4.48 . 1 238 28 SER CA C 59.45 . 1 239 28 SER HB2 H 4.04 . 1 240 28 SER HB3 H 4.00 . 1 241 28 SER CB C 63.57 . 1 242 29 SER H H 7.66 . 1 243 29 SER N N 112.21 . 1 244 29 SER HA H 4.82 . 1 245 29 SER CA C 56.73 . 1 246 29 SER HB2 H 4.30 . 1 247 29 SER HB3 H 4.07 . 1 248 29 SER CB C 65.96 . 1 249 30 GLU H H 9.33 . 1 250 30 GLU N N 124.51 . 1 251 30 GLU HA H 4.14 . 1 252 30 GLU CA C 58.63 . 1 253 30 GLU HB2 H 2.11 . 1 254 30 GLU CB C 29.15 . 1 255 30 GLU HG2 H 2.38 . 1 256 30 GLU CG C 35.97 . 1 257 31 GLU H H 8.84 . 1 258 31 GLU N N 118.81 . 1 259 31 GLU HA H 4.06 . 1 260 31 GLU CA C 59.68 . 1 261 31 GLU HB2 H 2.15 . 1 262 31 GLU HB3 H 2.00 . 1 263 31 GLU CB C 28.78 . 1 264 31 GLU HG2 H 2.39 . 1 265 31 GLU CG C 36.29 . 1 266 32 GLU H H 7.94 . 1 267 32 GLU N N 119.11 . 1 268 32 GLU HA H 4.08 . 1 269 32 GLU CA C 58.71 . 1 270 32 GLU HB2 H 2.14 . 1 271 32 GLU CB C 29.97 . 1 272 33 LEU H H 7.48 . 1 273 33 LEU N N 120.01 . 1 274 33 LEU HA H 4.10 . 1 275 33 LEU CA C 58.12 . 1 276 33 LEU HB2 H 1.75 . 1 277 33 LEU HB3 H 1.04 . 1 278 33 LEU CB C 40.46 . 1 279 33 LEU HG H 1.76 . 1 280 33 LEU CG C 26.72 . 1 281 33 LEU HD1 H 1.05 . 1 282 33 LEU HD2 H 1.06 . 1 283 33 LEU CD1 C 25.87 . 1 284 33 LEU CD2 C 23.78 . 1 285 34 VAL H H 7.78 . 1 286 34 VAL N N 119.62 . 1 287 34 VAL HA H 3.70 . 1 288 34 VAL CA C 66.52 . 1 289 34 VAL HB H 2.02 . 1 290 34 VAL CB C 31.45 . 1 291 34 VAL HG1 H 1.15 . 1 292 34 VAL CG1 C 22.54 . 1 293 34 VAL HG2 H 1.03 . 1 294 34 VAL CG2 C 20.78 . 1 295 35 LYS H H 7.78 . 1 296 35 LYS N N 119.61 . 1 297 35 LYS HA H 4.16 . 1 298 35 LYS CA C 59.41 . 1 299 35 LYS HB2 H 2.03 . 1 300 35 LYS HB3 H 2.03 . 1 301 35 LYS CB C 32.15 . 1 302 35 LYS HG2 H 1.67 . 1 303 35 LYS HG3 H 1.44 . 1 304 35 LYS CG C 24.93 . 1 305 35 LYS HE2 H 2.97 . 1 306 35 LYS HE3 H 2.97 . 1 307 35 LYS CE C 41.85 . 1 308 36 LEU H H 8.21 . 1 309 36 LEU N N 120.11 . 1 310 36 LEU HA H 4.22 . 1 311 36 LEU CA C 58.00 . 1 312 36 LEU HB2 H 2.17 . 1 313 36 LEU HB3 H 1.45 . 1 314 36 LEU CB C 41.65 . 1 315 36 LEU HG H 2.05 . 1 316 36 LEU CG C 26.08 . 1 317 36 LEU HD1 H 0.88 . 1 318 36 LEU HD2 H 0.88 . 1 319 36 LEU CD1 C 22.58 . 1 320 36 LEU CD2 C 25.57 . 1 321 37 VAL H H 8.21 . 1 322 37 VAL N N 121.21 . 1 323 37 VAL HA H 3.58 . 1 324 37 VAL CA C 67.79 . 1 325 37 VAL HB H 2.39 . 1 326 37 VAL CB C 31.12 . 1 327 37 VAL HG1 H 1.25 . 1 328 37 VAL CG1 C 24.33 . 1 329 37 VAL HG2 H 1.19 . 1 330 37 VAL CG2 C 22.50 . 1 331 38 THR H H 8.71 . 1 332 38 THR N N 116.71 . 1 333 38 THR HA H 4.23 . 1 334 38 THR CA C 66.63 . 1 335 38 THR HB H 4.39 . 1 336 38 THR CB C 68.91 . 1 337 38 THR HG2 H 1.42 . 1 338 38 THR CG2 C 21.57 . 1 339 39 HIS H H 8.30 . 1 340 39 HIS N N 121.11 . 1 341 39 HIS HA H 4.62 . 1 342 39 HIS CA C 59.72 . 1 343 39 HIS HB2 H 3.69 . 1 344 39 HIS HB3 H 3.33 . 1 345 39 HIS CB C 28.46 . 1 346 39 HIS HD2 H 6.87 . 1 347 39 HIS HE1 H 8.61 . 1 348 40 PHE H H 9.11 . 1 349 40 PHE N N 119.71 . 1 350 40 PHE HA H 3.90 . 1 351 40 PHE CA C 62.34 . 1 352 40 PHE HB2 H 3.82 . 1 353 40 PHE HB3 H 2.95 . 1 354 40 PHE CB C 38.62 . 1 355 41 GLU H H 8.76 . 1 356 41 GLU N N 121.11 . 1 357 41 GLU HA H 3.65 . 1 358 41 GLU CA C 60.71 . 1 359 41 GLU HB2 H 2.69 . 1 360 41 GLU CB C 29.23 . 1 361 41 GLU HG2 H 3.05 . 1 362 41 GLU HG3 H 2.09 . 1 363 41 GLU CG C 37.14 . 1 364 42 GLU H H 8.54 . 1 365 42 GLU N N 119.61 . 1 366 42 GLU HA H 4.04 . 1 367 42 GLU CA C 58.67 . 1 368 42 GLU HB2 H 2.28 . 1 369 42 GLU CB C 29.73 . 1 370 42 GLU HG2 H 2.63 . 1 371 41 GLU CG C 36.08 . 1 372 43 MET H H 8.86 . 1 373 43 MET N N 113.81 . 1 374 43 MET HA H 4.51 . 1 375 43 MET CA C 55.69 . 1 376 43 MET HB2 H 2.08 . 1 377 43 MET HB3 H 1.46 . 1 378 43 MET CB C 36.02 . 1 379 43 MET HG2 H 2.17 . 1 380 43 MET HG3 H 1.86 . 1 381 43 MET CG C 33.00 . 1 382 43 MET HE H 1.97 . 1 383 43 MET CE C 20.56 . 1 384 44 THR H H 7.88 . 1 385 44 THR N N 104.81 . 1 386 44 THR HA H 3.54 . 1 387 44 THR CA C 65.39 . 1 388 44 THR HB H 3.80 . 1 389 44 THR CB C 69.33 . 1 390 44 THR HG2 H 0.77 . 1 391 44 THR CG2 C 22.62 . 1 392 45 GLU H H 7.36 . 1 394 45 GLU HA H 3.89 . 1 395 45 GLU CA C 57.32 . 1 396 45 GLU HB2 H 2.47 . 1 397 45 GLU CB C 28.79 . 1 398 45 GLU HG2 H 2.25 . 1 399 45 GLU HG3 H 2.19 . 1 400 45 GLU CG C 37.56 . 1 401 46 HIS H H 7.47 . 1 402 46 HIS N N 119.11 . 1 403 46 HIS HA H 2.99 . 1 404 46 HIS CA C 55.54 . 1 405 46 HIS HB2 H 2.66 . 1 406 46 HIS CB C 31.34 . 1 407 46 HIS HD2 H 6.18 . 1 408 46 HIS HE1 H 7.60 . 1 409 47 PRO HA H 4.24 . 1 410 47 PRO CA C 64.59 . 1 411 47 PRO HB2 H 2.28 . 1 412 47 PRO HB3 H 1.90 . 1 414 47 PRO HG2 H 1.83 . 1 415 47 PRO HG3 H 1.66 . 1 416 47 PRO CG C 26.54 . 1 417 47 PRO HD2 H 2.70 . 1 418 47 PRO HD3 H 1.12 . 1 419 47 PRO CD C 50.10 . 1 420 48 SER H H 11.07 . 1 421 48 SER N N 117.41 . 1 422 48 SER HA H 4.59 . 1 423 48 SER CA C 59.87 . 1 424 48 SER HB2 H 3.93 . 1 425 48 SER HB3 H 3.88 . 1 426 48 SER CB C 63.09 . 1 427 49 GLY H H 8.19 . 1 428 49 GLY N N 108.11 . 1 429 49 GLY HA2 H 4.14 . 1 430 49 GLY HA3 H 3.87 . 1 431 49 GLY CA C 46.90 . 1 432 50 SER H H 10.14 . 1 433 50 SER N N 119.76 . 1 434 50 SER HA H 4.08 . 1 435 50 SER CA C 60.45 . 1 436 50 SER HB2 H 4.32 . 1 437 50 SER HB3 H 4.06 . 1 438 50 SER CB C 62.86 . 1 439 51 ASP H H 8.78 . 1 440 51 ASP N N 126.11 . 1 441 51 ASP HA H 4.63 . 1 442 51 ASP CA C 57.21 . 1 443 51 ASP HB2 H 3.22 . 1 444 51 ASP HB3 H 2.87 . 1 445 51 ASP CB C 38.93 . 1 446 52 LEU H H 7.41 . 1 447 52 LEU N N 114.21 . 1 448 52 LEU HA H 3.90 . 1 449 52 LEU CA C 57.18 . 1 450 52 LEU HB2 H 1.65 . 1 451 52 LEU HB3 H 1.38 . 1 452 52 LEU CB C 43.27 . 1 453 52 LEU HG H 1.51 . 1 454 52 LEU CG C 26.49 . 1 455 52 LEU HD1 H 0.51 . 1 456 52 LEU HD2 H 0.37 . 1 457 52 LEU CD1 C 22.19 . 1 458 52 LEU CD2 C 24.73 . 1 459 53 ILE H H 6.89 . 1 460 53 ILE N N 110.71 . 1 461 53 ILE HA H 3.54 . 1 462 53 ILE CA C 62.03 . 1 463 53 ILE HB H 1.10 . 1 464 53 ILE CB C 39.50 . 1 465 53 ILE HG12 H 0.88 . 1 466 53 ILE HG13 H 0.35 . 1 467 53 ILE CG1 C 27.78 . 1 468 53 ILE HG2 H -0.07 . 1 469 53 ILE CG2 C 16.11 . 1 470 53 ILE HD1 H -0.15 . 1 471 53 ILE CD1 C 12.66 . 1 472 54 TYR H H 7.39 . 1 474 54 TYR HA H 4.20 . 1 475 54 TYR CA C 60.26 . 1 476 54 TYR HB2 H 2.69 . 1 477 54 TYR HB3 H 2.56 . 1 478 54 TYR CB C 39.81 . 1 479 54 TYR HD1 H 7.14 . 1 480 54 TYR HD2 H 7.14 . 1 481 54 TYR HE1 H 6.71 . 1 482 54 TYR HE2 H 6.71 . 1 483 55 TYR H H 8.81 . 1 484 55 TYR N N 117.01 . 1 485 55 TYR HA H 4.98 . 1 486 55 TYR CA C 55.41 . 1 487 55 TYR HB2 H 3.20 . 1 488 55 TYR HB3 H 2.56 . 1 489 55 TYR CB C 39.30 . 1 490 55 TYR HD1 H 7.20 . 1 491 55 TYR HD2 H 7.20 . 1 492 55 TYR HE1 H 6.82 . 1 493 55 TYR HE2 H 6.82 . 1 494 56 PRO HA H 4.37 . 1 495 56 PRO CA C 62.74 . 1 496 56 PRO HB2 H 2.25 . 1 497 56 PRO CB C 31.17 . 1 498 56 PRO HG2 H 1.96 . 1 499 56 PRO HG3 H 1.93 . 1 500 56 PRO CG C 27.02 . 1 501 56 PRO HD2 H 3.42 . 1 502 56 PRO HD3 H 3.15 . 1 503 56 PRO CD C 50.03 . 1 504 57 LYS H H 8.86 . 1 505 57 LYS N N 122.11 . 1 506 57 LYS HA H 4.31 . 1 507 57 LYS CA C 55.09 . 1 508 57 LYS HB2 H 1.81 . 1 510 57 LYS HG2 H 1.57 . 1 511 57 LYS CG C 24.43 . 1 512 57 LYS HD2 H 1.75 . 1 513 57 LYS CD C 28.44 . 1 514 57 LYS HE2 H 3.11 . 1 515 57 LYS HE3 H 3.11 . 1 516 57 LYS CE C 42.02 . 1 517 58 GLU H H 8.71 . 1 518 58 GLU N N 122.91 . 1 519 58 GLU HA H 4.08 . 1 520 58 GLU CA C 58.11 . 1 521 58 GLU HB2 H 2.06 . 1 522 58 GLU HB3 H 1.98 . 1 523 58 GLU CB C 28.91 . 1 524 58 GLU HG2 H 2.31 . 1 525 58 GLU CG C 35.73 . 1 526 59 GLY H H 8.94 . 1 527 59 GLY N N 113.81 . 1 528 59 GLY HA2 H 4.31 . 1 529 59 GLY HA3 H 3.75 . 1 530 59 GLY CA C 44.90 . 1 531 60 ASP H H 8.04 . 1 532 60 ASP N N 121.21 . 1 533 60 ASP HA H 4.71 . 1 534 60 ASP CA C 53.88 . 1 535 60 ASP HB2 H 2.89 . 1 536 60 ASP HB3 H 2.62 . 1 537 60 ASP CB C 40.36 . 1 538 61 ASP H H 8.69 . 1 539 61 ASP N N 120.71 . 1 540 61 ASP HA H 4.63 . 1 541 61 ASP CA C 53.40 . 1 542 62 ASP H H 8.41 . 1 544 62 ASP HA H 4.48 . 1 545 62 ASP CA C 52.68 . 1 546 62 ASP HB2 H 2.98 . 1 547 62 ASP HB3 H 2.37 . 1 548 62 ASP CB C 39.73 . 1 549 63 SER H H 8.16 . 1 550 63 SER N N 115.01 . 1 551 63 SER HA H 4.63 . 1 552 63 SER CA C 57.21 . 1 553 63 SER HB2 H 4.23 . 1 554 63 SER HB3 H 4.12 . 1 555 63 SER CB C 62.86 . 1 556 64 PRO HA H 4.09 . 1 557 64 PRO CA C 66.45 . 1 558 64 PRO HB2 H 2.07 . 1 559 64 PRO HB3 H 1.96 . 1 561 64 PRO HG2 H 2.08 . 1 562 64 PRO CG C 28.30 . 1 563 64 PRO HD2 H 3.93 . 1 564 64 PRO HD3 H 3.89 . 1 565 64 PRO CD C 48.96 . 1 566 65 SER H H 8.31 . 1 567 65 SER N N 109.21 . 1 568 65 SER HA H 4.03 . 1 569 65 SER CA C 61.49 . 1 570 65 SER HB2 H 3.91 . 1 571 65 SER HB3 H 3.84 . 1 572 65 SER CB C 62.18 . 1 573 66 GLY H H 8.11 . 1 574 66 GLY N N 114.31 . 1 575 66 GLY HA2 H 3.90 . 1 576 66 GLY HA3 H 3.82 . 1 577 66 GLY CA C 46.80 . 1 578 67 ILE H H 8.82 . 1 579 67 ILE N N 124.61 . 1 580 67 ILE HA H 3.90 . 1 581 67 ILE CA C 65.23 . 1 582 67 ILE HB H 1.89 . 1 583 67 ILE CB C 38.13 . 1 584 67 ILE HG12 H 1.73 . 1 585 67 ILE HG13 H 1.73 . 1 586 67 ILE CG1 C 29.02 . 1 587 67 ILE HG2 H 0.87 . 1 588 67 ILE CG2 C 17.36 . 1 589 67 ILE HD1 H 0.46 . 1 590 67 ILE CD1 C 14.92 . 1 591 68 VAL H H 8.40 . 1 592 68 VAL N N 118.63 . 1 593 68 VAL HA H 3.65 . 1 594 68 VAL CA C 68.43 . 1 595 68 VAL HB H 2.41 . 1 596 68 VAL CB C 30.95 . 1 597 68 VAL HG1 H 1.27 . 1 598 68 VAL CG1 C 24.92 . 1 599 68 VAL HG2 H 1.23 . 1 600 68 VAL CG2 C 22.04 . 1 601 69 ASN H H 8.40 . 1 602 69 ASN N N 118.11 . 1 603 69 ASN HA H 4.61 . 1 604 69 ASN CA C 56.97 . 1 605 69 ASN HB2 H 3.07 . 1 606 69 ASN HB3 H 3.01 . 1 607 69 ASN CB C 38.05 . 1 608 69 ASN HD21 H 7.90 . 1 609 69 ASN HD22 H 7.03 . 1 610 69 ASN ND2 N 114.40 . 1 611 70 THR H H 8.87 . 1 612 70 THR N N 119.81 . 1 613 70 THR HA H 4.06 . 1 614 70 THR CA C 67.37 . 1 615 70 THR HB H 4.54 . 1 616 70 THR CB C 68.03 . 1 617 70 THR HG2 H 1.24 . 1 618 70 THR CG2 C 22.23 . 1 619 71 VAL H H 8.61 . 1 620 71 VAL N N 121.31 . 1 621 71 VAL HA H 3.66 . 1 622 71 VAL CA C 68.00 . 1 623 71 VAL HB H 2.55 . 1 624 71 VAL CB C 31.75 . 1 625 71 VAL HG1 H 1.14 . 1 626 71 VAL CG1 C 22.96 . 1 627 71 VAL HG2 H 0.81 . 1 628 71 VAL CG2 C 20.60 . 1 629 72 LYS H H 9.27 . 1 630 72 LYS N N 120.11 . 1 631 72 LYS HA H 3.98 . 1 632 72 LYS CA C 59.68 . 1 633 72 LYS HB2 H 2.19 . 1 634 72 LYS CB C 33.25 . 1 635 72 LYS HG2 H 1.78 . 1 636 72 LYS HG3 H 1.63 . 1 637 72 LYS CG C 24.70 . 1 638 72 LYS HD2 H 1.93 . 1 639 72 LYS CD C 30.01 . 1 640 72 LYS HE2 H 3.16 . 1 641 72 LYS HE3 H 3.16 . 1 642 72 LYS CE C 41.77 . 1 643 73 GLN H H 8.80 . 1 644 73 GLN N N 117.51 . 1 645 73 GLN HA H 4.23 . 1 646 73 GLN CA C 58.35 . 1 647 73 GLN HB2 H 2.30 . 1 648 73 GLN HB3 H 2.30 . 1 649 73 GLN CB C 28.06 . 1 650 73 GLN HG2 H 2.72 . 1 651 73 GLN HG3 H 2.59 . 1 652 73 GLN CG C 33.60 . 1 653 73 GLN HE21 H 7.68 . 1 654 73 GLN HE22 H 7.03 . 1 655 73 GLN NE2 N 92.49 . 1 656 74 TRP H H 8.57 . 1 657 74 TRP N N 121.21 . 1 658 74 TRP HA H 4.26 . 1 659 74 TRP CA C 62.86 . 1 660 74 TRP HB2 H 3.68 . 1 661 74 TRP HB3 H 3.54 . 1 662 74 TRP CB C 28.71 . 1 663 74 TRP HD1 H 7.29 . 1 664 74 TRP HE1 H 10.21 . 1 665 74 TRP HE3 H 7.38 . 1 666 74 TRP HZ2 H 7.32 . 1 667 74 TRP HZ3 H 7.02 . 1 668 74 TRP HH2 H 7.02 . 1 669 75 ARG H H 9.08 . 1 670 75 ARG N N 118.31 . 1 671 75 ARG HA H 3.30 . 1 672 75 ARG CA C 60.93 . 1 673 75 ARG HB2 H 2.37 . 1 674 75 ARG HB3 H 1.82 . 1 675 75 ARG CB C 29.59 . 1 676 75 ARG HD2 H 3.32 . 1 677 75 ARG HD3 H 3.10 . 1 678 75 ARG CD C 41.85 . 1 679 75 ARG HE H 7.51 . 1 680 75 ARG HH21 H 6.85 . 1 681 75 ARG HH22 H 6.85 . 1 682 76 ALA H H 7.79 . 1 683 76 ALA N N 119.81 . 1 684 76 ALA HA H 4.20 . 1 685 76 ALA CA C 54.87 . 1 686 76 ALA HB H 1.50 . 1 687 76 ALA CB C 17.66 . 1 688 77 ALA H H 8.10 . 1 689 77 ALA N N 119.21 . 1 690 77 ALA HA H 4.17 . 1 691 77 ALA CA C 53.66 . 1 692 77 ALA HB H 1.43 . 1 694 78 ASN H H 7.13 . 1 695 78 ASN N N 113.01 . 1 696 78 ASN HA H 4.56 . 1 697 78 ASN CA C 52.98 . 1 698 78 ASN HB2 H 2.33 . 1 699 78 ASN HB3 H 1.30 . 1 700 78 ASN CB C 38.74 . 1 701 78 ASN HD21 H 6.53 . 1 702 78 ASN HD22 H 6.46 . 1 703 78 ASN ND2 N 116.40 . 1 704 79 GLY H H 7.66 . 1 705 79 GLY N N 107.21 . 1 706 79 GLY HA2 H 3.87 . 1 707 79 GLY HA3 H 3.87 . 1 709 80 LYS H H 8.11 . 1 710 80 LYS N N 117.51 . 1 711 80 LYS HA H 4.57 . 1 712 80 LYS CA C 53.84 . 1 713 80 LYS HB2 H 2.00 . 1 714 80 LYS HB3 H 1.39 . 1 716 80 LYS HG2 H 1.31 . 1 717 80 LYS HG3 H 1.13 . 1 718 80 LYS CG C 24.95 . 1 719 80 LYS HD2 H 1.67 . 1 720 80 LYS HD3 H 1.47 . 1 721 80 LYS CD C 28.64 . 1 722 80 LYS HE2 H 3.17 . 1 723 80 LYS HE3 H 2.87 . 1 724 80 LYS CE C 42.23 . 1 725 81 SER H H 8.73 . 1 726 81 SER N N 117.11 . 1 727 81 SER HB2 H 3.97 . 1 728 81 SER CB C 63.75 . 1 729 82 GLY H H 8.40 . 1 730 82 GLY N N 118.61 . 1 731 82 GLY HA2 H 4.27 . 1 732 82 GLY HA3 H 3.58 . 1 733 82 GLY CA C 42.89 . 1 734 83 PHE H H 7.88 . 1 735 83 PHE N N 115.51 . 1 736 83 PHE HA H 4.69 . 1 737 83 PHE CA C 58.34 . 1 738 83 PHE HB2 H 3.70 . 1 739 83 PHE HB3 H 2.69 . 1 741 84 LYS H H 8.66 . 1 742 84 LYS N N 123.31 . 1 743 84 LYS HA H 4.25 . 1 744 84 LYS CA C 56.95 . 1 745 84 LYS HB2 H 1.49 . 1 747 84 LYS HG2 H 1.49 . 1 748 84 LYS CG C 24.19 . 1 749 84 LYS HE2 H 3.02 . 1 750 84 LYS HE3 H 3.02 . 1 751 84 LYS CE C 42.03 . 1 752 85 GLN H H 8.80 . 1 754 85 GLN HA H 4.36 . 1 756 85 GLN HB2 H 2.11 . 1 757 85 GLN HB3 H 2.22 . 1 758 85 GLN HG2 H 2.53 . 1 759 86 GLY H H 8.17 . 1 761 86 GLY HA2 H 3.87 . 1 762 86 GLY HA3 H 3.87 . 1 stop_ save_