data_5769 #Corrected using PDB structure: 1P6TA # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 17 C HA 4.99 3.76 # 57 T HA 3.35 4.11 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 57 T N 110.11 120.40 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.03 N/A N/A N/A 0.07 0.16 # #bmr5769.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5769.str file): #HA CA CB CO N HN #N/A N/A N/A N/A +0.07 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 N/A N/A N/A +/-0.44 +/-0.10 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.857 N/A N/A N/A 0.829 0.447 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.136 N/A N/A N/A 1.813 0.425 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of apo-CopAS46V from Bacillus subtilis ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Ciofi-Baffoni S. . . 4 Gonnelli L. . . 5 Su X. C. . stop_ _BMRB_accession_number 5769 _BMRB_flat_file_name bmr5769.str _Entry_type new _Submission_date 2003-04-11 _Accession_date 2003-04-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 369 '15N chemical shifts' 77 stop_ loop_ _Related_BMRB_accession_number _Relationship 5768 "complex form with copper ion" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; A Core Mutation Affecting the Folding Properties of a Soluble Domain of the ATPase Protein CopA from Bacillus subtilis ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 22770441 _PubMed_ID 12888353 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Banci L. . . 2 Bertini I. . . 3 Ciofi-Baffoni S. . . 4 Gonnelli L. . . 5 Su X. C. . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 331 _Journal_issue 2 _Page_first 473 _Page_last 484 _Year 2003 loop_ _Keyword "CopA" "P-type ATPase" mutation NMR folding "Copper complex" stop_ save_ ################################## # Molecular system description # ################################## save_system_CopA _Saveframe_category molecular_system _Mol_system_name "Potential copper-transporting ATPase" _Abbreviation_common CopA _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CopA $CopA stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1OQ3 ? . PDB 1OPZ ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_CopA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "CPx-type ATPase CopA" _Name_variant S46V _Abbreviation_common CopA _Mol_thiol_state 'all free' ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; MLSEQKEIAMQVSGMTCAAC AARIEKGLKRMPGVTDANVN LATETVNVIYDPAETGTAAI QEKIEKLGYHVVIEGR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 SER 4 GLU 5 GLN 6 LYS 7 GLU 8 ILE 9 ALA 10 MET 11 GLN 12 VAL 13 SER 14 GLY 15 MET 16 THR 17 CYS 18 ALA 19 ALA 20 CYS 21 ALA 22 ALA 23 ARG 24 ILE 25 GLU 26 LYS 27 GLY 28 LEU 29 LYS 30 ARG 31 MET 32 PRO 33 GLY 34 VAL 35 THR 36 ASP 37 ALA 38 ASN 39 VAL 40 ASN 41 LEU 42 ALA 43 THR 44 GLU 45 THR 46 VAL 47 ASN 48 VAL 49 ILE 50 TYR 51 ASP 52 PRO 53 ALA 54 GLU 55 THR 56 GLY 57 THR 58 ALA 59 ALA 60 ILE 61 GLN 62 GLU 63 LYS 64 ILE 65 GLU 66 LYS 67 LEU 68 GLY 69 TYR 70 HIS 71 VAL 72 VAL 73 ILE 74 GLU 75 GLY 76 ARG stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1OPZ "A Chain A, A Core Mutation Affecting TheFolding Properties Of A Soluble Domain Of The AtpaseProtein Copa From Bacillus Subtilis" 100.00 76 100 100 4e-36 PDB 1OQ3 "A Chain A, A Core Mutation Affecting TheFolding Properties Of A Soluble Domain Of The AtpaseProtein Copa From Bacillus Subtilis" 100.00 76 100 100 4e-36 PDB 1OQ6 "A Chain A, Solution Structure Of Copper-S46vCopa From Bacillus Subtilis" 100.00 76 100 100 4e-36 PDB 1P6T "A Chain A, Structure Characterization Of TheWater Soluble Region Of P- Type Atpase Copa FromBacillus Subtilis" 50.33 151 99 99 3e-34 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 _Gene_mnemonic $CopA "Bacillus subtilis" 1423 Eubacteria . Bacillus subtilis pLysS yvgX 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 $CopA 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CopA 1.2 mM [U-15N] phosphate 20 mM . DTT 2 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.6 loop_ _Task processing stop_ _Details Bruker save_ save_Xeasy _Saveframe_category software _Name Xeasy _Version 1.3 loop_ _Task "structure solution" stop_ _Details "Xia, Bartels" save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task "structure solution" stop_ _Details "Gunter, Mumenthaler, Wuthrich" save_ save_AMBER _Saveframe_category software _Name AMBER _Version 5.0 loop_ _Task refinement stop_ _Details ; Pearlman, Case, Caldwell, Ross, cheatham, Ferguson, Seibel, Singh, Weiner, Kollman. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 2D NOESY 2D TOCSY 3D 15N-separated NOESY HNHA HNHB ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a temperature 298 0.1 K 'ionic strength' 20 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio TMS H 1 "methyl protons" ppm 0.00 external direct cylindrical external perpendicular 1.0 TMS N 15 "methyl protons" ppm 0.00 external indirect . . . 0.10132912 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_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name CopA 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 SER N N 116.96 0.000 . 2 3 SER H H 8.27 0.000 . 3 3 SER HA H 4.35 0.000 . 4 3 SER HB2 H 3.74 0.001 . 5 4 GLU N N 122.98 0.000 . 6 4 GLU H H 8.38 0.000 . 7 4 GLU HA H 4.22 0.000 . 8 4 GLU HB2 H 1.90 0.001 . 9 4 GLU HB3 H 1.82 0.000 . 10 4 GLU HG2 H 2.13 0.000 . 11 4 GLU HG3 H 2.06 0.000 . 12 5 GLN N N 119.32 0.000 . 13 5 GLN H H 7.98 0.000 . 14 5 GLN HA H 4.42 0.000 . 15 5 GLN HB2 H 1.80 0.001 . 16 5 GLN HB3 H 1.65 0.000 . 17 5 GLN HG2 H 2.10 0.001 . 18 5 GLN HG3 H 2.03 0.000 . 19 5 GLN NE2 N 111.10 0.000 . 20 5 GLN HE21 H 7.31 0.000 . 21 5 GLN HE22 H 6.53 0.000 . 22 6 LYS N N 122.15 0.000 . 23 6 LYS H H 8.57 0.000 . 24 6 LYS HA H 4.38 0.000 . 25 6 LYS HB2 H 1.26 0.000 . 26 6 LYS HB3 H 0.65 0.000 . 27 6 LYS HG2 H 1.11 0.000 . 28 6 LYS HG3 H 1.07 0.000 . 29 6 LYS HD2 H 1.57 0.002 . 30 7 GLU N N 119.32 0.000 . 31 7 GLU H H 8.06 0.001 . 32 7 GLU HA H 5.50 0.004 . 33 7 GLU HB2 H 1.83 0.002 . 34 7 GLU HB3 H 1.73 0.000 . 35 7 GLU HG2 H 1.99 0.000 . 36 8 ILE N N 121.92 0.000 . 37 8 ILE H H 9.10 0.000 . 38 8 ILE HA H 4.70 0.000 . 39 8 ILE HB H 1.85 0.001 . 40 8 ILE HG2 H 0.88 0.000 . 41 8 ILE HG12 H 1.41 0.003 . 42 8 ILE HD1 H 1.09 0.002 . 43 9 ALA N N 127.47 0.000 . 44 9 ALA H H 8.15 0.000 . 45 9 ALA HA H 5.37 0.001 . 46 9 ALA HB H 1.16 0.003 . 47 10 MET N N 120.03 0.000 . 48 10 MET H H 8.90 0.001 . 49 10 MET HA H 4.62 0.000 . 50 10 MET HB2 H 1.81 0.001 . 51 10 MET HB3 H 1.62 0.000 . 52 10 MET HG2 H 2.39 0.000 . 53 10 MET HG3 H 2.18 0.001 . 54 11 GLN N N 124.04 0.000 . 55 11 GLN H H 8.91 0.000 . 56 11 GLN HA H 4.91 0.000 . 57 11 GLN HB2 H 2.00 0.001 . 58 11 GLN HG2 H 2.17 0.002 . 59 11 GLN NE2 N 111.34 0.000 . 60 11 GLN HE21 H 7.51 0.002 . 61 11 GLN HE22 H 6.84 0.002 . 62 12 VAL N N 123.57 0.000 . 63 12 VAL H H 8.44 0.000 . 64 12 VAL HA H 4.96 0.001 . 65 12 VAL HB H 1.55 0.000 . 66 12 VAL HG1 H 0.78 0.000 . 67 12 VAL HG2 H 0.66 0.001 . 68 13 SER N N 122.27 0.000 . 69 13 SER H H 9.45 0.000 . 70 13 SER HA H 4.84 0.000 . 71 13 SER HB2 H 3.83 0.001 . 72 13 SER HB3 H 3.69 0.001 . 73 14 GLY N N 109.16 0.000 . 74 14 GLY H H 8.55 0.000 . 75 14 GLY HA2 H 4.65 0.000 . 76 14 GLY HA3 H 3.64 0.003 . 77 15 MET N N 120.73 0.000 . 78 15 MET H H 9.12 0.000 . 79 15 MET HA H 4.82 0.006 . 80 15 MET HB3 H 1.37 0.001 . 81 15 MET HB2 H 2.39 0.000 . 82 15 MET HG2 H 2.02 0.000 . 84 16 THR H H 10.24 0.000 . 85 16 THR HA H 4.51 0.002 . 86 16 THR HB H 4.27 0.001 . 87 16 THR HG2 H 1.13 0.002 . 88 17 CYS N N 116.01 0.000 . 89 17 CYS H H 8.04 0.001 . 90 17 CYS HA H 4.96 0.000 . 91 17 CYS HB2 H 3.38 0.000 . 92 17 CYS HB3 H 3.01 0.000 . 93 19 ALA N N 121.92 0.000 . 94 19 ALA H H 8.42 0.000 . 95 19 ALA HA H 4.17 0.000 . 96 19 ALA HB H 1.45 0.002 . 97 20 CYS N N 122.27 0.000 . 98 20 CYS H H 7.67 0.000 . 99 20 CYS HA H 3.94 0.000 . 100 20 CYS HB2 H 3.19 0.001 . 101 20 CYS HB3 H 2.59 0.001 . 102 21 ALA N N 118.85 0.000 . 103 21 ALA H H 6.70 0.000 . 104 21 ALA HA H 3.68 0.000 . 105 21 ALA HB H 1.32 0.001 . 106 22 ALA N N 117.78 0.000 . 107 22 ALA H H 7.76 0.000 . 108 22 ALA HA H 4.07 0.000 . 109 22 ALA HB H 1.36 0.000 . 110 23 ARG N N 118.73 0.000 . 111 23 ARG H H 7.88 0.000 . 112 23 ARG HA H 3.96 0.000 . 113 23 ARG HB2 H 2.00 0.000 . 114 23 ARG HG2 H 1.81 0.000 . 115 23 ARG HG3 H 1.61 0.001 . 116 23 ARG HD2 H 3.32 0.001 . 117 24 ILE N N 120.26 0.000 . 118 24 ILE H H 7.81 0.000 . 119 24 ILE HA H 3.42 0.000 . 120 24 ILE HB H 1.54 0.001 . 121 24 ILE HG2 H 0.30 0.001 . 122 24 ILE HG12 H 0.84 0.000 . 123 24 ILE HG13 H 0.46 0.001 . 124 24 ILE HD1 H -0.10 0.001 . 125 25 GLU N N 118.37 0.000 . 126 25 GLU H H 8.29 0.000 . 127 25 GLU HA H 3.39 0.004 . 128 25 GLU HB2 H 2.06 0.000 . 129 25 GLU HB3 H 1.84 0.000 . 130 25 GLU HG2 H 2.46 0.000 . 131 26 LYS N N 115.54 0.000 . 132 26 LYS H H 8.24 0.000 . 133 26 LYS HA H 3.81 0.000 . 134 26 LYS HB2 H 1.81 0.002 . 135 26 LYS HB3 H 1.70 0.001 . 136 26 LYS HG2 H 1.31 0.001 . 137 26 LYS HD2 H 1.56 0.003 . 138 26 LYS HD3 H 1.49 0.001 . 139 26 LYS HE2 H 2.93 0.000 . 140 26 LYS HE3 H 2.85 0.000 . 141 27 GLY N N 104.44 0.000 . 142 27 GLY H H 7.80 0.000 . 143 27 GLY HA2 H 3.74 0.000 . 144 27 GLY HA3 H 3.44 0.000 . 145 28 LEU N N 120.03 0.000 . 146 28 LEU H H 8.20 0.000 . 147 28 LEU HA H 4.04 0.002 . 148 28 LEU HB2 H 1.65 0.000 . 149 28 LEU HB3 H 0.99 0.000 . 150 28 LEU HG H 1.13 0.002 . 151 28 LEU HD1 H 0.75 0.000 . 152 28 LEU HD2 H 0.48 0.003 . 153 29 LYS N N 114.71 0.000 . 154 29 LYS H H 8.00 0.000 . 155 29 LYS HA H 3.72 0.000 . 156 29 LYS HB2 H 1.84 0.000 . 157 29 LYS HB3 H 1.66 0.000 . 158 29 LYS HE2 H 3.34 0.000 . 159 29 LYS HE3 H 3.04 0.000 . 161 30 ARG H H 6.90 0.000 . 162 30 ARG HA H 4.22 0.000 . 163 30 ARG HB2 H 1.93 0.000 . 164 30 ARG HB3 H 1.69 0.000 . 165 30 ARG HG2 H 1.73 0.001 . 166 30 ARG HD2 H 3.09 0.002 . 167 31 MET N N 123.21 0.000 . 168 31 MET H H 7.77 0.000 . 169 31 MET HA H 4.45 0.000 . 170 31 MET HB2 H 2.05 0.001 . 171 31 MET HB3 H 2.14 0.000 . 172 31 MET HG2 H 2.63 0.002 . 173 31 MET HG3 H 2.46 0.000 . 174 32 PRO HA H 4.20 0.000 . 175 32 PRO HB2 H 2.25 0.000 . 176 32 PRO HB3 H 2.10 0.000 . 177 32 PRO HG2 H 1.93 0.000 . 178 32 PRO HG3 H 1.83 0.000 . 179 33 GLY N N 110.58 0.000 . 180 33 GLY H H 8.52 0.000 . 181 33 GLY HA2 H 4.14 0.003 . 182 33 GLY HA3 H 3.69 0.003 . 183 34 VAL N N 120.73 0.000 . 184 34 VAL H H 7.56 0.001 . 185 34 VAL HA H 4.08 0.001 . 186 34 VAL HB H 2.35 0.002 . 187 34 VAL HG1 H 0.75 0.001 . 188 34 VAL HG2 H 0.61 0.000 . 189 35 THR N N 124.99 0.000 . 190 35 THR H H 9.11 0.001 . 191 35 THR HA H 4.13 0.000 . 192 35 THR HB H 3.77 0.000 . 193 35 THR HG2 H 1.03 0.001 . 194 36 ASP N N 118.02 0.000 . 195 36 ASP H H 8.00 0.000 . 196 36 ASP HA H 4.62 0.000 . 197 36 ASP HB2 H 2.52 0.002 . 198 36 ASP HB3 H 2.28 0.000 . 199 37 ALA N N 121.09 0.000 . 200 37 ALA H H 8.16 0.001 . 201 37 ALA HA H 5.10 0.000 . 202 37 ALA HB H 1.13 0.000 . 203 38 ASN N N 117.31 0.000 . 204 38 ASN H H 8.71 0.000 . 205 38 ASN HA H 4.95 0.000 . 206 38 ASN HB2 H 2.48 0.000 . 207 38 ASN ND2 N 114.41 0.000 . 208 38 ASN HD21 H 7.66 0.000 . 209 38 ASN HD22 H 6.64 0.000 . 210 39 VAL N N 126.17 0.000 . 211 39 VAL H H 9.79 0.000 . 212 39 VAL HA H 4.34 0.000 . 213 39 VAL HB H 1.85 0.001 . 214 39 VAL HG1 H 0.85 0.002 . 215 39 VAL HG2 H 0.59 0.001 . 216 40 ASN N N 126.88 0.000 . 217 40 ASN H H 8.90 0.000 . 218 40 ASN HA H 4.77 0.000 . 219 40 ASN HB2 H 3.05 0.000 . 220 40 ASN HB3 H 2.40 0.000 . 221 40 ASN ND2 N 111.93 0.000 . 222 40 ASN HD21 H 7.36 0.000 . 223 40 ASN HD22 H 6.85 0.000 . 224 41 LEU N N 125.46 0.000 . 225 41 LEU H H 8.76 0.000 . 226 41 LEU HA H 3.71 0.000 . 227 41 LEU HB2 H 1.53 0.000 . 228 41 LEU HB3 H 1.43 0.001 . 229 41 LEU HG H 1.40 0.000 . 230 41 LEU HD1 H 0.66 0.002 . 231 41 LEU HD2 H 0.61 0.002 . 232 42 ALA N N 119.44 0.000 . 233 42 ALA H H 8.01 0.000 . 234 42 ALA HA H 4.04 0.001 . 235 42 ALA HB H 1.42 0.000 . 236 43 THR N N 104.20 0.000 . 237 43 THR H H 7.21 0.000 . 238 43 THR HA H 4.34 0.000 . 239 43 THR HB H 4.40 0.001 . 240 43 THR HG2 H 0.96 0.000 . 241 44 GLU N N 120.14 0.000 . 242 44 GLU H H 7.77 0.000 . 243 44 GLU HA H 3.37 0.001 . 244 44 GLU HB2 H 2.44 0.002 . 245 44 GLU HB3 H 2.21 0.002 . 246 44 GLU HG2 H 2.05 0.000 . 247 45 THR N N 110.11 0.000 . 248 45 THR H H 7.61 0.000 . 249 45 THR HA H 5.08 0.000 . 250 45 THR HB H 3.62 0.000 . 251 45 THR HG2 H 0.96 0.000 . 252 46 VAL N N 124.87 0.000 . 253 46 VAL H H 9.25 0.000 . 254 46 VAL HA H 4.55 0.000 . 255 46 VAL HB H 1.66 0.000 . 256 46 VAL HG1 H 0.95 0.000 . 257 46 VAL HG2 H 0.61 0.000 . 258 47 ASN N N 126.76 0.000 . 259 47 ASN H H 8.73 0.000 . 260 47 ASN HA H 5.52 0.002 . 261 47 ASN HB2 H 2.53 0.000 . 262 47 ASN ND2 N 112.04 0.000 . 263 47 ASN HD21 H 7.45 0.000 . 264 47 ASN HD22 H 6.78 0.001 . 265 48 VAL N N 124.04 0.000 . 266 48 VAL H H 9.16 0.000 . 267 48 VAL HA H 4.63 0.003 . 268 48 VAL HB H 1.88 0.000 . 269 48 VAL HG1 H 1.01 0.000 . 270 48 VAL HG2 H 0.73 0.000 . 271 49 ILE N N 127.58 0.000 . 272 49 ILE H H 8.46 0.000 . 273 49 ILE HA H 5.12 0.002 . 274 49 ILE HB H 1.47 0.000 . 275 49 ILE HG2 H 0.72 0.000 . 276 49 ILE HG12 H 0.88 0.000 . 277 49 ILE HD1 H 0.65 0.001 . 279 50 TYR H H 9.31 0.001 . 280 50 TYR HA H 5.49 0.003 . 281 50 TYR HB2 H 2.65 0.001 . 282 50 TYR HB3 H 2.44 0.002 . 283 50 TYR HD1 H 6.50 0.001 . 284 50 TYR HE1 H 6.41 0.001 . 285 51 ASP N N 119.44 0.000 . 286 51 ASP H H 8.84 0.000 . 287 51 ASP HA H 5.02 0.001 . 288 51 ASP HB2 H 2.95 0.000 . 289 51 ASP HB3 H 2.48 0.003 . 290 52 PRO HA H 5.09 0.003 . 291 52 PRO HB2 H 2.15 0.000 . 292 52 PRO HG2 H 1.90 0.000 . 293 52 PRO HG3 H 1.71 0.000 . 294 52 PRO HD2 H 4.01 0.000 . 295 52 PRO HD3 H 3.56 0.000 . 296 53 ALA N N 120.97 0.000 . 297 53 ALA H H 8.55 0.000 . 298 53 ALA HA H 4.25 0.000 . 299 53 ALA HB H 1.38 0.000 . 300 54 GLU N N 115.54 0.000 . 301 54 GLU H H 7.75 0.000 . 302 54 GLU HA H 4.41 0.000 . 303 54 GLU HB2 H 1.93 0.000 . 304 54 GLU HB3 H 1.76 0.002 . 305 54 GLU HG2 H 2.11 0.002 . 306 55 THR N N 114.12 0.000 . 307 55 THR H H 8.01 0.000 . 308 55 THR HA H 4.48 0.000 . 309 55 THR HB H 4.13 0.000 . 310 55 THR HG2 H 0.87 0.001 . 311 55 THR HG1 H 5.35 0.000 . 312 56 GLY N N 105.03 0.000 . 313 56 GLY H H 7.90 0.000 . 314 56 GLY HA2 H 4.14 0.000 . 315 56 GLY HA3 H 3.89 0.000 . 316 57 THR N N 110.11 0.000 . 317 57 THR H H 8.20 0.000 . 318 57 THR HA H 3.31 0.001 . 319 57 THR HB H 3.98 0.000 . 320 57 THR HG2 H 1.08 0.000 . 321 58 ALA N N 124.28 0.000 . 322 58 ALA H H 8.37 0.001 . 323 58 ALA HA H 3.98 0.000 . 324 58 ALA HB H 1.27 0.002 . 325 59 ALA N N 120.73 0.000 . 326 59 ALA H H 7.68 0.000 . 327 59 ALA HA H 4.00 0.003 . 328 59 ALA HB H 1.29 0.000 . 329 60 ILE N N 120.38 0.000 . 330 60 ILE H H 7.47 0.000 . 331 60 ILE HA H 3.23 0.001 . 332 60 ILE HB H 1.46 0.002 . 333 60 ILE HG2 H 0.48 0.003 . 334 60 ILE HG12 H 0.75 0.002 . 335 60 ILE HG13 H 0.64 0.002 . 336 60 ILE HD1 H -0.06 0.001 . 337 61 GLN N N 118.14 0.000 . 338 61 GLN H H 8.21 0.000 . 339 61 GLN HA H 3.63 0.000 . 340 61 GLN HB2 H 2.01 0.000 . 341 61 GLN HG2 H 2.28 0.005 . 342 61 GLN HG3 H 2.14 0.000 . 343 61 GLN NE2 N 109.33 0.000 . 344 61 GLN HE21 H 7.21 0.000 . 345 61 GLN HE22 H 6.55 0.000 . 346 62 GLU N N 117.55 0.000 . 347 62 GLU H H 8.01 0.000 . 348 62 GLU HA H 3.95 0.000 . 349 62 GLU HB2 H 2.07 0.000 . 350 62 GLU HB3 H 1.99 0.002 . 351 62 GLU HG2 H 2.29 0.003 . 352 63 LYS N N 119.67 0.000 . 353 63 LYS H H 7.63 0.000 . 354 63 LYS HA H 3.96 0.005 . 355 63 LYS HB2 H 1.96 0.001 . 356 63 LYS HB3 H 1.80 0.001 . 357 63 LYS HG2 H 1.49 0.002 . 358 63 LYS HG3 H 1.10 0.000 . 359 63 LYS HD2 H 1.60 0.001 . 360 63 LYS HE2 H 2.81 0.000 . 361 63 LYS HE3 H 2.67 0.000 . 362 64 ILE N N 117.78 0.000 . 363 64 ILE H H 7.52 0.000 . 364 64 ILE HA H 3.33 0.001 . 365 64 ILE HB H 1.83 0.001 . 366 64 ILE HG2 H 0.60 0.000 . 367 64 ILE HG12 H 0.89 0.000 . 368 64 ILE HG13 H 0.75 0.002 . 369 64 ILE HD1 H 0.68 0.001 . 370 65 GLU N N 118.26 0.000 . 371 65 GLU H H 7.90 0.000 . 372 65 GLU HA H 4.63 0.000 . 373 65 GLU HB2 H 2.13 0.002 . 374 65 GLU HG2 H 2.46 0.001 . 375 65 GLU HG3 H 2.31 0.001 . 376 66 LYS N N 122.62 0.000 . 377 66 LYS H H 8.64 0.000 . 378 66 LYS HA H 3.98 0.000 . 379 66 LYS HB2 H 1.97 0.000 . 380 66 LYS HB3 H 1.83 0.002 . 381 66 LYS HG2 H 1.46 0.000 . 382 66 LYS HD2 H 1.55 0.002 . 383 66 LYS HE2 H 2.88 0.000 . 384 66 LYS HE3 H 2.83 0.000 . 385 67 LEU N N 118.37 0.000 . 386 67 LEU H H 7.83 0.000 . 387 67 LEU HA H 4.15 0.000 . 388 67 LEU HB2 H 2.22 0.001 . 389 67 LEU HB3 H 1.50 0.000 . 390 67 LEU HG H 1.93 0.002 . 391 67 LEU HD1 H 0.79 0.001 . 392 67 LEU HD2 H 0.76 0.002 . 393 68 GLY N N 104.20 0.000 . 394 68 GLY H H 7.64 0.000 . 395 68 GLY HA2 H 3.88 0.000 . 396 68 GLY HA3 H 3.36 0.000 . 397 69 TYR N N 119.79 0.000 . 398 69 TYR H H 7.17 0.000 . 399 69 TYR HA H 4.57 0.000 . 400 69 TYR HB2 H 3.07 0.000 . 401 69 TYR HB3 H 2.19 0.000 . 402 69 TYR HD1 H 6.67 0.000 . 403 69 TYR HE1 H 6.73 0.000 . 404 70 HIS N N 115.07 0.000 . 405 70 HIS H H 7.73 0.000 . 406 70 HIS HA H 5.07 0.000 . 407 70 HIS HB2 H 3.05 0.001 . 408 70 HIS HB3 H 2.89 0.000 . 409 70 HIS HD2 H 6.95 0.000 . 410 71 VAL N N 125.10 0.000 . 411 71 VAL H H 8.87 0.000 . 412 71 VAL HA H 4.39 0.000 . 413 71 VAL HB H 1.85 0.000 . 414 71 VAL HG1 H 0.88 0.002 . 415 71 VAL HG2 H 0.80 0.000 . 416 72 VAL N N 128.41 0.000 . 417 72 VAL H H 8.45 0.000 . 418 72 VAL HA H 3.84 0.000 . 419 72 VAL HB H 1.76 0.000 . 420 72 VAL HG1 H 0.77 0.002 . 421 72 VAL HG2 H 0.66 0.000 . 422 73 ILE N N 126.99 0.000 . 423 73 ILE H H 8.26 0.000 . 424 73 ILE HA H 4.17 0.000 . 425 73 ILE HB H 1.73 0.000 . 426 73 ILE HG2 H 0.79 0.000 . 427 73 ILE HG12 H 1.34 0.000 . 428 73 ILE HG13 H 1.06 0.002 . 429 73 ILE HD1 H 0.71 0.000 . 430 74 GLU N N 125.81 0.000 . 431 74 GLU H H 8.55 0.000 . 432 74 GLU HA H 4.17 0.000 . 433 74 GLU HB2 H 1.96 0.002 . 434 74 GLU HB3 H 1.88 0.001 . 435 74 GLU HG2 H 2.16 0.002 . 437 75 GLY H H 8.43 0.000 . 438 75 GLY HA2 H 3.84 0.000 . 439 75 GLY HA3 H 3.77 0.000 . 441 76 ARG H H 7.73 0.000 . 442 76 ARG HA H 4.14 0.000 . 443 76 ARG HB2 H 1.77 0.000 . 444 76 ARG HB3 H 1.63 0.000 . 445 76 ARG HG2 H 1.48 0.000 . 446 76 ARG HD2 H 3.08 0.000 . stop_ save_