data_5768 #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 4.91 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 110.14 120.40 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.04 N/A N/A N/A 0.11 0.17 # #bmr5768.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5768.str file): #HA CA CB CO N HN #N/A N/A N/A N/A +0.11 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 +/-0.45 +/-0.10 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.862 N/A N/A N/A 0.830 0.477 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.134 N/A N/A N/A 1.859 0.410 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of Copper-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 5768 _BMRB_flat_file_name bmr5768.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' 373 '15N chemical shifts' 77 stop_ loop_ _Related_BMRB_accession_number _Relationship 5769 "free form" 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 protein" 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_mutation "copper ion (I)" $CU_1+ stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1OQ6 ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_CopA_mutation _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 other bound' ############################## # 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_ ############# # Ligands # ############# save_CU_1+ _Saveframe_category ligand _Mol_type non-polymer _Name_common 'COPPER (I) ION' _Abbreviation_common Cu _Name_IUPAC . _BMRB_code CU_1+ _PDB_code CU1 _Mol_empirical_formula CU1 _Mol_charge 1+ _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU ? 1+ ? ? stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single coordination CopA 17 CYS SG "copper ion (I)" . . CU single coordination CopA 20 CYS SG "copper ion (I)" . . CU 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_mutation "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_mutation '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_mutation 1.2 mM [U-15N] phosphate 20 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_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 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 117.04 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 3.75 0.001 . 5 4 GLU N N 122.85 0.000 . 6 4 GLU H H 8.38 0.000 . 7 4 GLU HA H 4.21 0.000 . 8 4 GLU HB2 H 1.90 0.000 . 9 4 GLU HB3 H 1.81 0.000 . 10 4 GLU HG2 H 2.12 0.000 . 11 4 GLU HG3 H 2.04 0.000 . 12 5 GLN N N 119.31 0.000 . 13 5 GLN H H 7.98 0.000 . 14 5 GLN HA H 4.41 0.000 . 15 5 GLN HB2 H 1.78 0.001 . 16 5 GLN HB3 H 1.65 0.000 . 17 5 GLN HG2 H 2.09 0.000 . 18 5 GLN HG3 H 2.02 0.000 . 19 5 GLN NE2 N 110.99 0.000 . 20 5 GLN HE21 H 7.31 0.001 . 21 5 GLN HE22 H 6.52 0.000 . 22 6 LYS N N 122.29 0.000 . 23 6 LYS H H 8.56 0.000 . 24 6 LYS HA H 4.38 0.000 . 25 6 LYS HB2 H 1.24 0.000 . 26 6 LYS HB3 H 0.64 0.000 . 27 6 LYS HG2 H 1.13 0.000 . 28 6 LYS HG3 H 1.08 0.000 . 29 6 LYS HD2 H 1.57 0.002 . 30 7 GLU N N 119.31 0.000 . 31 7 GLU H H 8.05 0.000 . 32 7 GLU HA H 5.49 0.004 . 33 7 GLU HB2 H 1.83 0.002 . 34 7 GLU HB3 H 1.75 0.000 . 35 7 GLU HG2 H 2.00 0.002 . 36 8 ILE N N 121.96 0.012 . 37 8 ILE H H 9.09 0.001 . 38 8 ILE HA H 4.70 0.000 . 39 8 ILE HB H 1.85 0.000 . 40 8 ILE HG2 H 0.88 0.002 . 41 8 ILE HG12 H 1.41 0.000 . 42 8 ILE HD1 H 1.08 0.000 . 43 9 ALA N N 127.39 0.000 . 44 9 ALA H H 8.15 0.000 . 45 9 ALA HA H 5.38 0.000 . 46 9 ALA HB H 1.16 0.000 . 47 10 MET N N 120.06 0.014 . 48 10 MET H H 8.90 0.000 . 49 10 MET HA H 4.61 0.000 . 50 10 MET HB2 H 1.79 0.000 . 51 10 MET HB3 H 1.62 0.000 . 52 10 MET HG2 H 2.38 0.001 . 53 10 MET HG3 H 2.18 0.001 . 54 11 GLN N N 124.08 0.016 . 55 11 GLN H H 8.90 0.000 . 56 11 GLN HA H 4.91 0.000 . 57 11 GLN HB2 H 2.00 0.002 . 58 11 GLN HG2 H 2.16 0.000 . 59 11 GLN NE2 N 111.27 0.000 . 60 11 GLN HE21 H 7.52 0.000 . 61 11 GLN HE22 H 6.84 0.001 . 62 12 VAL N N 123.70 0.000 . 63 12 VAL H H 8.44 0.000 . 64 12 VAL HA H 4.96 0.000 . 65 12 VAL HB H 1.55 0.000 . 66 12 VAL HG1 H 0.78 0.000 . 67 12 VAL HG2 H 0.67 0.001 . 68 13 SER N N 122.31 0.000 . 69 13 SER H H 9.45 0.000 . 70 13 SER HA H 4.82 0.004 . 71 13 SER HB2 H 3.84 0.000 . 72 13 SER HB3 H 3.70 0.000 . 73 14 GLY N N 109.11 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 3.65 0.000 . 77 15 MET N N 120.59 0.000 . 78 15 MET H H 9.18 0.000 . 79 15 MET HA H 4.75 0.000 . 80 15 MET HB2 H 2.48 0.000 . 81 15 MET HB3 H 1.30 0.000 . 82 15 MET HG2 H 2.02 0.009 . 83 15 MET HG3 H 1.66 0.000 . 85 16 THR H H 9.11 0.002 . 86 16 THR HA H 4.47 0.000 . 87 16 THR HB H 3.21 0.000 . 88 16 THR HG2 H 1.10 0.000 . 89 17 CYS N N 115.77 0.000 . 90 17 CYS H H 7.92 0.000 . 91 17 CYS HA H 4.87 0.000 . 92 17 CYS HB2 H 3.32 0.000 . 93 17 CYS HB3 H 3.12 0.000 . 94 19 ALA N N 124.13 0.000 . 95 19 ALA H H 9.12 0.000 . 96 19 ALA HA H 4.21 0.000 . 97 19 ALA HB H 1.44 0.004 . 98 20 CYS N N 122.71 0.000 . 99 20 CYS H H 8.13 0.000 . 100 20 CYS HA H 3.98 0.000 . 101 20 CYS HB2 H 3.20 0.005 . 102 20 CYS HB3 H 2.50 0.003 . 103 21 ALA N N 118.89 0.000 . 104 21 ALA H H 6.52 0.000 . 105 21 ALA HA H 3.70 0.000 . 106 21 ALA HB H 1.32 0.001 . 107 22 ALA N N 117.61 0.000 . 108 22 ALA H H 7.58 0.000 . 109 22 ALA HA H 4.07 0.000 . 110 22 ALA HB H 1.38 0.000 . 111 23 ARG N N 117.61 0.000 . 112 23 ARG H H 7.72 0.000 . 113 23 ARG HA H 3.95 0.000 . 114 23 ARG HB2 H 2.00 0.000 . 115 23 ARG HG2 H 1.82 0.000 . 116 23 ARG HG3 H 1.57 0.000 . 117 23 ARG HD2 H 3.32 0.001 . 118 24 ILE N N 120.02 0.000 . 119 24 ILE H H 7.66 0.000 . 120 24 ILE HA H 3.42 0.001 . 121 24 ILE HB H 1.52 0.000 . 122 24 ILE HG2 H 0.31 0.000 . 123 24 ILE HG12 H 0.85 0.000 . 124 24 ILE HG13 H 0.46 0.002 . 125 24 ILE HD1 H -0.09 0.000 . 126 25 GLU N N 118.46 0.000 . 127 25 GLU H H 8.27 0.000 . 128 25 GLU HA H 3.39 0.004 . 129 25 GLU HB2 H 2.04 0.000 . 130 25 GLU HB3 H 1.83 0.000 . 131 25 GLU HG2 H 2.44 0.000 . 132 26 LYS N N 115.58 0.000 . 133 26 LYS H H 8.24 0.000 . 134 26 LYS HA H 3.81 0.000 . 135 26 LYS HB2 H 1.80 0.000 . 136 26 LYS HB3 H 1.68 0.000 . 137 26 LYS HG2 H 1.30 0.000 . 138 26 LYS HD2 H 1.56 0.001 . 139 26 LYS HD3 H 1.48 0.009 . 140 26 LYS HE2 H 2.93 0.000 . 141 26 LYS HE3 H 2.85 0.000 . 142 27 GLY N N 104.43 0.000 . 143 27 GLY H H 7.77 0.000 . 144 27 GLY HA2 H 3.73 0.000 . 145 27 GLY HA3 H 3.44 0.000 . 146 28 LEU N N 120.06 0.011 . 147 28 LEU H H 8.22 0.000 . 148 28 LEU HA H 4.05 0.000 . 149 28 LEU HB2 H 1.65 0.000 . 150 28 LEU HB3 H 1.00 0.000 . 151 28 LEU HG H 1.11 0.000 . 152 28 LEU HD1 H 0.74 0.007 . 153 28 LEU HD2 H 0.48 0.002 . 154 29 LYS N N 114.75 0.000 . 155 29 LYS H H 7.97 0.000 . 156 29 LYS HA H 3.73 0.000 . 157 29 LYS HB2 H 1.83 0.002 . 158 29 LYS HB3 H 1.70 0.000 . 159 29 LYS HG2 H 1.46 0.000 . 160 29 LYS HD2 H 1.19 0.002 . 161 29 LYS HE2 H 3.34 0.000 . 162 29 LYS HE3 H 3.03 0.000 . 164 30 ARG H H 6.88 0.000 . 165 30 ARG HA H 4.24 0.000 . 166 30 ARG HB2 H 1.93 0.000 . 167 30 ARG HB3 H 1.68 0.000 . 168 30 ARG HG2 H 1.78 0.000 . 169 30 ARG HD2 H 3.09 0.002 . 170 31 MET N N 123.25 0.000 . 171 31 MET H H 7.77 0.000 . 172 31 MET HA H 4.45 0.000 . 173 31 MET HB2 H 2.05 0.001 . 174 31 MET HB3 H 2.13 0.000 . 175 31 MET HG2 H 2.63 0.001 . 176 31 MET HG3 H 2.46 0.000 . 177 32 PRO HA H 4.20 0.000 . 178 32 PRO HB2 H 2.25 0.000 . 179 32 PRO HB3 H 2.10 0.000 . 180 32 PRO HG2 H 1.92 0.000 . 181 32 PRO HG3 H 1.83 0.000 . 182 32 PRO HD2 H 4.01 0.005 . 183 32 PRO HD3 H 3.56 0.000 . 184 33 GLY N N 110.53 0.000 . 185 33 GLY H H 8.50 0.000 . 186 33 GLY HA2 H 4.14 0.000 . 187 33 GLY HA3 H 3.69 0.000 . 188 34 VAL N N 120.73 0.000 . 189 34 VAL H H 7.56 0.001 . 190 34 VAL HA H 4.05 0.000 . 191 34 VAL HB H 2.35 0.003 . 192 34 VAL HG1 H 0.75 0.000 . 193 34 VAL HG2 H 0.61 0.000 . 194 35 THR N N 125.02 0.000 . 195 35 THR H H 9.11 0.000 . 196 35 THR HA H 4.13 0.000 . 197 35 THR HB H 3.77 0.000 . 198 35 THR HG2 H 1.02 0.000 . 199 36 ASP N N 118.05 0.007 . 200 36 ASP H H 8.00 0.000 . 201 36 ASP HA H 4.62 0.000 . 202 36 ASP HB2 H 2.52 0.002 . 203 36 ASP HB3 H 2.27 0.000 . 204 37 ALA N N 121.15 0.000 . 205 37 ALA H H 8.15 0.000 . 206 37 ALA HA H 5.11 0.000 . 207 37 ALA HB H 1.12 0.000 . 208 38 ASN N N 117.34 0.008 . 209 38 ASN H H 8.71 0.000 . 210 38 ASN HA H 4.95 0.000 . 211 38 ASN HB2 H 2.48 0.000 . 212 38 ASN ND2 N 114.25 0.000 . 213 38 ASN HD21 H 7.59 0.002 . 214 38 ASN HD22 H 6.65 0.002 . 215 39 VAL N N 126.11 0.000 . 216 39 VAL H H 9.78 0.000 . 217 39 VAL HA H 4.35 0.000 . 218 39 VAL HB H 1.85 0.000 . 219 39 VAL HG1 H 0.84 0.004 . 220 39 VAL HG2 H 0.58 0.000 . 221 40 ASN N N 126.82 0.000 . 222 40 ASN H H 8.92 0.000 . 223 40 ASN HA H 4.78 0.000 . 224 40 ASN HB2 H 3.04 0.005 . 225 40 ASN HB3 H 2.39 0.000 . 226 40 ASN ND2 N 111.93 0.000 . 227 40 ASN HD21 H 7.35 0.000 . 228 40 ASN HD22 H 6.84 0.000 . 229 41 LEU N N 125.50 0.000 . 230 41 LEU H H 8.77 0.000 . 231 41 LEU HA H 3.72 0.000 . 232 41 LEU HB2 H 1.51 0.000 . 233 41 LEU HB3 H 1.44 0.000 . 234 41 LEU HG H 1.40 0.000 . 235 41 LEU HD1 H 0.64 0.000 . 236 41 LEU HD2 H 0.55 0.000 . 237 42 ALA N N 119.60 0.000 . 238 42 ALA H H 8.03 0.000 . 239 42 ALA HA H 4.05 0.000 . 240 42 ALA HB H 1.41 0.000 . 241 43 THR N N 104.29 0.000 . 242 43 THR H H 7.21 0.000 . 243 43 THR HA H 4.34 0.002 . 244 43 THR HB H 4.42 0.000 . 245 43 THR HG2 H 0.96 0.000 . 246 44 GLU N N 120.02 0.000 . 247 44 GLU H H 7.76 0.000 . 248 44 GLU HA H 3.37 0.000 . 249 44 GLU HB2 H 2.43 0.006 . 250 44 GLU HB3 H 2.21 0.000 . 251 44 GLU HG2 H 2.05 0.000 . 252 45 THR N N 110.14 0.010 . 253 45 THR H H 7.62 0.000 . 254 45 THR HA H 5.08 0.002 . 255 45 THR HB H 3.61 0.000 . 256 45 THR HG2 H 0.95 0.000 . 257 46 VAL N N 124.91 0.000 . 258 46 VAL H H 9.24 0.000 . 259 46 VAL HA H 4.53 0.007 . 260 46 VAL HB H 1.65 0.000 . 261 46 VAL HG1 H 0.95 0.000 . 262 46 VAL HG2 H 0.56 0.000 . 263 47 ASN N N 126.68 0.000 . 264 47 ASN H H 8.73 0.000 . 265 47 ASN HA H 5.51 0.004 . 266 47 ASN HB2 H 2.52 0.000 . 267 47 ASN ND2 N 112.12 0.000 . 268 47 ASN HD21 H 7.43 0.000 . 269 47 ASN HD22 H 6.78 0.000 . 270 48 VAL N N 124.27 0.000 . 271 48 VAL H H 9.15 0.000 . 272 48 VAL HA H 4.63 0.000 . 273 48 VAL HB H 1.87 0.000 . 274 48 VAL HG1 H 0.99 0.001 . 275 48 VAL HG2 H 0.73 0.007 . 276 49 ILE N N 127.81 0.000 . 277 49 ILE H H 8.45 0.000 . 278 49 ILE HA H 5.12 0.003 . 279 49 ILE HB H 1.46 0.000 . 280 49 ILE HG2 H 0.75 0.000 . 281 49 ILE HG12 H 0.88 0.003 . 282 49 ILE HD1 H 0.67 0.000 . 284 50 TYR H H 9.31 0.000 . 285 50 TYR HA H 5.49 0.000 . 286 50 TYR HB2 H 2.65 0.000 . 287 50 TYR HB3 H 2.47 0.000 . 288 50 TYR HD1 H 6.50 0.002 . 289 50 TYR HE1 H 6.39 0.000 . 290 51 ASP N N 119.31 0.000 . 291 51 ASP H H 8.85 0.000 . 292 51 ASP HA H 5.00 0.000 . 293 51 ASP HB2 H 2.96 0.001 . 294 51 ASP HB3 H 2.47 0.000 . 295 52 PRO HA H 5.08 0.000 . 296 52 PRO HB2 H 2.14 0.000 . 297 52 PRO HG2 H 1.92 0.002 . 298 52 PRO HG3 H 1.68 0.000 . 299 52 PRO HD2 H 4.02 0.004 . 300 52 PRO HD3 H 3.56 0.003 . 301 53 ALA N N 121.01 0.000 . 302 53 ALA H H 8.55 0.000 . 303 53 ALA HA H 4.24 0.000 . 304 53 ALA HB H 1.38 0.000 . 305 54 GLU N N 115.58 0.019 . 306 54 GLU H H 7.74 0.000 . 307 54 GLU HA H 4.40 0.000 . 308 54 GLU HB2 H 1.93 0.000 . 309 54 GLU HB3 H 1.76 0.000 . 310 54 GLU HG2 H 2.12 0.000 . 311 55 THR N N 114.16 0.011 . 312 55 THR H H 8.01 0.000 . 313 55 THR HA H 4.49 0.001 . 314 55 THR HB H 4.13 0.000 . 315 55 THR HG2 H 0.86 0.000 . 316 55 THR HG1 H 5.35 0.000 . 317 56 GLY N N 105.07 0.000 . 318 56 GLY H H 7.90 0.003 . 319 56 GLY HA2 H 4.14 0.000 . 320 56 GLY HA3 H 3.88 0.000 . 321 57 THR N N 110.14 0.000 . 322 57 THR H H 8.19 0.000 . 323 57 THR HA H 3.31 0.002 . 324 57 THR HB H 3.97 0.000 . 325 57 THR HG2 H 1.08 0.000 . 326 58 ALA N N 124.31 0.000 . 327 58 ALA H H 8.37 0.000 . 328 58 ALA HA H 3.99 0.000 . 329 58 ALA HB H 1.27 0.000 . 330 59 ALA N N 120.77 0.000 . 331 59 ALA H H 7.67 0.000 . 332 59 ALA HB H 1.29 0.000 . 333 60 ILE N N 120.42 0.009 . 334 60 ILE H H 7.47 0.000 . 335 60 ILE HA H 3.21 0.000 . 336 60 ILE HB H 1.46 0.000 . 337 60 ILE HG2 H 0.47 0.000 . 338 60 ILE HG12 H 1.78 0.002 . 339 60 ILE HG13 H 0.64 0.000 . 340 60 ILE HD1 H -0.06 0.003 . 341 61 GLN N N 118.17 0.001 . 342 61 GLN H H 8.21 0.000 . 343 61 GLN HA H 3.64 0.000 . 344 61 GLN HB2 H 2.01 0.000 . 345 61 GLN HG2 H 2.29 0.000 . 346 61 GLN HG3 H 2.14 0.000 . 347 61 GLN NE2 N 109.14 0.000 . 348 61 GLN HE21 H 7.19 0.000 . 349 61 GLN HE22 H 6.56 0.001 . 350 62 GLU N N 117.58 0.000 . 351 62 GLU H H 8.02 0.000 . 352 62 GLU HA H 3.96 0.004 . 353 62 GLU HB2 H 2.07 0.000 . 354 62 GLU HB3 H 1.98 0.000 . 355 62 GLU HG2 H 2.28 0.000 . 356 63 LYS N N 119.71 0.000 . 357 63 LYS H H 7.63 0.000 . 358 63 LYS HA H 3.96 0.006 . 359 63 LYS HB2 H 1.96 0.001 . 360 63 LYS HB3 H 1.80 0.001 . 361 63 LYS HG2 H 1.47 0.000 . 362 63 LYS HG3 H 1.09 0.005 . 363 63 LYS HD2 H 1.60 0.001 . 364 63 LYS HE2 H 2.80 0.002 . 365 63 LYS HE3 H 2.67 0.000 . 366 64 ILE N N 117.82 0.000 . 367 64 ILE H H 7.54 0.000 . 368 64 ILE HA H 3.33 0.001 . 369 64 ILE HB H 1.84 0.000 . 370 64 ILE HG2 H 0.63 0.000 . 371 64 ILE HG12 H 0.89 0.000 . 372 64 ILE HG13 H 0.75 0.002 . 373 64 ILE HD1 H 0.68 0.000 . 374 65 GLU N N 118.29 0.000 . 375 65 GLU H H 7.90 0.000 . 376 65 GLU HA H 4.63 0.000 . 377 65 GLU HB2 H 2.13 0.004 . 378 65 GLU HB3 H 1.98 0.003 . 379 65 GLU HG2 H 2.46 0.000 . 380 65 GLU HG3 H 2.33 0.000 . 381 66 LYS N N 122.66 0.011 . 382 66 LYS H H 8.66 0.000 . 383 66 LYS HA H 3.97 0.000 . 384 66 LYS HB2 H 1.97 0.000 . 385 66 LYS HB3 H 1.83 0.002 . 386 66 LYS HG2 H 1.45 0.000 . 387 66 LYS HD2 H 1.55 0.002 . 388 66 LYS HE2 H 2.88 0.000 . 389 66 LYS HE3 H 2.83 0.000 . 390 67 LEU N N 118.41 0.000 . 391 67 LEU H H 7.85 0.000 . 392 67 LEU HA H 4.15 0.000 . 393 67 LEU HB2 H 2.22 0.001 . 394 67 LEU HB3 H 1.50 0.000 . 395 67 LEU HG H 1.93 0.002 . 396 67 LEU HD1 H 0.78 0.000 . 397 67 LEU HD2 H 0.75 0.000 . 398 68 GLY N N 104.24 0.000 . 399 68 GLY H H 7.65 0.000 . 400 68 GLY HA2 H 3.87 0.000 . 401 68 GLY HA3 H 3.36 0.000 . 402 69 TYR N N 119.83 0.000 . 403 69 TYR H H 7.17 0.000 . 404 69 TYR HA H 4.58 0.000 . 405 69 TYR HB2 H 3.08 0.000 . 406 69 TYR HB3 H 2.19 0.000 . 407 69 TYR HD1 H 6.69 0.002 . 408 69 TYR HE1 H 6.70 0.000 . 409 70 HIS N N 115.10 0.000 . 410 70 HIS H H 7.69 0.000 . 411 70 HIS HA H 5.07 0.000 . 412 70 HIS HB2 H 3.02 0.000 . 413 70 HIS HB3 H 2.89 0.000 . 414 71 VAL N N 125.14 0.000 . 415 71 VAL H H 8.86 0.000 . 416 71 VAL HA H 4.37 0.000 . 417 71 VAL HB H 1.85 0.000 . 418 71 VAL HG1 H 0.89 0.001 . 419 71 VAL HG2 H 0.78 0.001 . 420 72 VAL N N 128.45 0.000 . 421 72 VAL H H 8.45 0.000 . 422 72 VAL HA H 3.82 0.000 . 423 72 VAL HB H 1.76 0.003 . 424 72 VAL HG1 H 0.77 0.000 . 425 72 VAL HG2 H 0.69 0.000 . 426 73 ILE N N 126.82 0.000 . 427 73 ILE H H 8.20 0.000 . 428 73 ILE HA H 4.16 0.001 . 429 73 ILE HB H 1.73 0.000 . 430 73 ILE HG2 H 0.78 0.000 . 431 73 ILE HG12 H 1.34 0.000 . 432 73 ILE HG13 H 1.06 0.000 . 433 73 ILE HD1 H 0.71 0.002 . 434 74 GLU N N 125.85 0.000 . 435 74 GLU H H 8.55 0.002 . 436 74 GLU HA H 4.16 0.000 . 437 74 GLU HB2 H 1.96 0.002 . 438 74 GLU HB3 H 1.88 0.001 . 439 74 GLU HG2 H 2.17 0.000 . 441 75 GLY H H 8.44 0.000 . 442 75 GLY HA2 H 3.84 0.000 . 443 75 GLY HA3 H 3.77 0.000 . 445 76 ARG H H 7.72 0.000 . 446 76 ARG HA H 4.14 0.000 . 447 76 ARG HB2 H 1.76 0.000 . 448 76 ARG HB3 H 1.62 0.000 . 449 76 ARG HG2 H 1.49 0.000 . 450 76 ARG HD2 H 3.08 0.000 . stop_ save_