data_6172 #Corrected using PDB structure: 1SB6A # #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 # 2 T HA 5.52 4.71 # 7 V HA 5.35 4.37 # 11 A HA 3.38 4.14 # 13 E HA 4.76 3.67 # 14 A HA 4.97 3.72 # 39 K HA 3.54 4.72 # 57 A HA 4.81 4.09 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 39 K N 115.67 127.24 # 64 E N 132.25 118.44 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.06 N/A N/A N/A -0.30 0.13 # #bmr6172.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6172.str file): #HA CA CB CO N HN #N/A N/A N/A N/A -0.30 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 N/A N/A N/A +/-0.54 +/-0.09 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.660 N/A N/A N/A 0.728 0.461 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.168 N/A N/A N/A 2.081 0.351 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of a cyanobacterial copper metallochaperone, ScAtx1 ; 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 Su X. C. . 5 Borrelly G. . . 6 Robinson N. J. . stop_ _BMRB_accession_number 6172 _BMRB_flat_file_name bmr6172.str _Entry_type new _Submission_date 2004-04-02 _Accession_date 2004-04-02 _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' 310 '15N chemical shifts' 67 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution structures of a cyanobacterial copper metallochaperone: insight into an atypical copper binding motif ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 15075318 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 Su X. C. . 5 Borrelly G. P. . 6 Robinson N. J. . stop_ _Journal_abbreviation "J. Biol. Chem." _Journal_volume ? _Journal_issue ? _Page_first ? _Page_last ? _Year 2004 loop_ _Keyword "copper chaperone" structure "new metal binding motif" NMR stop_ save_ ################################## # Molecular system description # ################################## save_system_ScAtx1 _Saveframe_category molecular_system _Mol_system_name "apo ScAtx1" _Abbreviation_common apoScAtx1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "apo ScAtx1" $apoScAtx1 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 1SB6 . . stop_ save_ ######################## # Monomeric polymers # ######################## save_apoScAtx1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common apoScAtx1 _Name_variant . _Abbreviation_common apoScAtx1 _Mol_thiol_state 'all free' ############################## # Polymer residue sequence # ############################## _Residue_count 64 _Mol_residue_sequence ; MTIQLTVPTIACEACAEAVT KAVQNEDAQATVQVDLTSKK VTITSALGEEQLRTAIASAG HEVE ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 ILE 4 GLN 5 LEU 6 THR 7 VAL 8 PRO 9 THR 10 ILE 11 ALA 12 CYS 13 GLU 14 ALA 15 CYS 16 ALA 17 GLU 18 ALA 19 VAL 20 THR 21 LYS 22 ALA 23 VAL 24 GLN 25 ASN 26 GLU 27 ASP 28 ALA 29 GLN 30 ALA 31 THR 32 VAL 33 GLN 34 VAL 35 ASP 36 LEU 37 THR 38 SER 39 LYS 40 LYS 41 VAL 42 THR 43 ILE 44 THR 45 SER 46 ALA 47 LEU 48 GLY 49 GLU 50 GLU 51 GLN 52 LEU 53 ARG 54 THR 55 ALA 56 ILE 57 ALA 58 SER 59 ALA 60 GLY 61 HIS 62 GLU 63 VAL 64 GLU 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 1SB6 "A Chain A, Solution Structure Of ACyanobacterial Copper Metallochaperone, Scatx1" 100.00 64 100 100 8e-28 DBJ BAA17240.1 "ORF_ID:ssr2857~unknown protein[Synechocystis sp. PCC 6803]" 100.00 64 100 100 8e-28 PIR S75326 "hypothetical protein ssr2857 -Synechocystis sp. (strain PCC 6803)" 100.00 64 100 100 8e-28 REF NP_440560.1 "unknown protein [Synechocystis sp.PCC 6803]" 100.00 64 100 100 8e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $apoScAtx1 "Synechocystis sp. PCC 6803" 1148 Eubacteria . Synechocystis "Synechocystis sp. PCC 6803" 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 $apoScAtx1 '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 $apoScAtx1 0.7 mM "[U-15N]" phosphate 50 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, Bartles" 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 ; Pealman, 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 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 2D NOESY 3D 15N-separated NOESY 2D TOCSY HNHA ; 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 . n/a temperature 298 . K 'ionic strength' 50 . 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 "apo ScAtx1" 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 THR HA H 5.46 0.003 . 2 2 THR HB H 3.75 0.003 . 3 2 THR HG2 H 0.96 0.008 . 4 3 ILE N N 126.30 0.003 . 5 3 ILE H H 9.18 0.001 . 6 3 ILE HA H 4.48 0.001 . 7 3 ILE HB H 1.61 0.004 . 8 3 ILE HG2 H 0.91 0.094 . 9 3 ILE HG12 H 1.36 0.001 . 10 3 ILE HD1 H 0.78 0.081 . 11 4 GLN N N 123.49 0.002 . 12 4 GLN H H 8.39 0.002 . 13 4 GLN HA H 5.38 0.005 . 14 4 GLN HB2 H 1.77 0.001 . 15 4 GLN HB3 H 1.62 0.002 . 16 4 GLN HG2 H 2.12 0.003 . 17 4 GLN HG3 H 2.03 0.003 . 18 4 GLN NE2 N 111.90 0.005 . 19 4 GLN HE21 H 7.33 0.003 . 20 4 GLN HE22 H 6.79 0.001 . 21 5 LEU N N 124.43 0.002 . 22 5 LEU H H 8.96 0.001 . 23 5 LEU HA H 4.72 0.001 . 24 5 LEU HB2 H 1.37 0.001 . 25 5 LEU HB3 H 1.28 0.005 . 26 5 LEU HG H 0.97 0.001 . 27 5 LEU HD1 H 0.79 0.002 . 28 5 LEU HD2 H 0.57 0.001 . 29 6 THR N N 119.73 0.003 . 30 6 THR H H 9.30 0.002 . 31 6 THR HA H 4.72 0.001 . 32 6 THR HB H 3.98 0.003 . 33 6 THR HG2 H 1.04 0.002 . 35 7 VAL H H 8.56 0.005 . 36 7 VAL HA H 5.29 0.001 . 37 7 VAL HB H 2.01 0.002 . 38 7 VAL HG1 H 0.84 0.004 . 39 7 VAL HG2 H 0.72 0.006 . 40 8 PRO HA H 4.62 0.001 . 41 8 PRO HB2 H 2.30 0.003 . 42 8 PRO HB3 H 1.96 0.001 . 43 8 PRO HG2 H 1.90 0.004 . 44 8 PRO HD2 H 4.12 0.012 . 45 8 PRO HD3 H 3.50 0.004 . 46 9 THR N N 103.78 0.003 . 47 9 THR H H 7.19 0.007 . 48 9 THR HA H 4.10 0.001 . 49 9 THR HB H 4.07 0.001 . 50 9 THR HG2 H 1.20 0.002 . 51 10 ILE N N 121.30 0.002 . 52 10 ILE H H 7.52 0.002 . 53 10 ILE HA H 3.72 0.002 . 54 10 ILE HB H 1.66 0.002 . 55 10 ILE HG2 H 0.52 0.002 . 56 10 ILE HG12 H 1.44 0.004 . 57 10 ILE HG13 H 0.56 0.001 . 58 10 ILE HD1 H 0.44 0.001 . 59 11 ALA N N 119.73 0.001 . 60 11 ALA H H 7.21 0.002 . 61 11 ALA HA H 3.33 0.009 . 62 11 ALA HB H 1.37 0.002 . 63 12 CYS N N 112.54 0.002 . 64 12 CYS H H 8.13 0.002 . 65 12 CYS HA H 4.27 0.003 . 66 12 CYS HB2 H 2.75 0.005 . 67 12 CYS HB3 H 2.65 0.005 . 68 13 GLU N N 121.61 0.003 . 69 13 GLU H H 8.12 0.003 . 70 13 GLU HA H 4.70 0.001 . 71 13 GLU HB2 H 1.96 0.004 . 72 13 GLU HG2 H 2.27 0.003 . 73 14 ALA N N 115.35 0.003 . 74 14 ALA H H 7.51 0.002 . 75 14 ALA HA H 4.91 0.002 . 76 14 ALA HB H 1.33 0.002 . 77 15 CYS N N 121.30 0.004 . 78 15 CYS H H 7.86 0.001 . 79 15 CYS HA H 4.23 0.002 . 80 15 CYS HB2 H 3.32 0.005 . 81 15 CYS HB3 H 2.74 0.004 . 82 16 ALA N N 120.05 0.006 . 83 16 ALA H H 7.49 0.002 . 84 16 ALA HA H 3.63 0.002 . 85 16 ALA HB H 1.38 0.001 . 86 17 GLU N N 120.36 0.002 . 87 17 GLU H H 8.24 0.002 . 88 17 GLU HA H 3.95 0.002 . 89 17 GLU HB2 H 2.10 0.001 . 90 17 GLU HB3 H 2.03 0.001 . 91 17 GLU HG2 H 2.32 0.004 . 92 17 GLU HG3 H 2.16 0.001 . 93 18 ALA N N 121.92 0.002 . 94 18 ALA H H 7.86 0.003 . 95 18 ALA HA H 4.08 0.006 . 96 18 ALA HB H 1.60 0.002 . 97 19 VAL N N 117.54 0.003 . 98 19 VAL H H 8.03 0.002 . 99 19 VAL HA H 3.30 0.002 . 100 19 VAL HB H 1.82 0.004 . 101 19 VAL HG1 H 0.61 0.001 . 102 19 VAL HG2 H 0.50 0.002 . 103 20 THR N N 116.29 0.002 . 104 20 THR H H 7.82 0.003 . 105 20 THR HA H 3.42 0.001 . 106 20 THR HB H 4.23 0.004 . 107 20 THR HG2 H 0.99 0.004 . 108 20 THR HG1 H 4.56 0.001 . 109 21 LYS N N 119.73 0.002 . 110 21 LYS H H 8.34 0.002 . 111 21 LYS HA H 3.88 0.001 . 112 21 LYS HB2 H 1.75 0.006 . 113 21 LYS HG2 H 1.60 0.002 . 114 21 LYS HG3 H 1.35 0.003 . 115 21 LYS HD2 H 1.49 0.001 . 116 22 ALA N N 119.73 0.002 . 117 22 ALA H H 7.64 0.002 . 118 22 ALA HA H 3.99 0.001 . 119 22 ALA HB H 1.34 0.002 . 120 23 VAL N N 115.98 0.002 . 121 23 VAL H H 7.57 0.003 . 122 23 VAL HA H 3.25 0.004 . 123 23 VAL HB H 1.96 0.002 . 124 23 VAL HG1 H 0.80 0.001 . 125 23 VAL HG2 H 0.60 0.002 . 126 24 GLN N N 117.23 0.002 . 127 24 GLN H H 8.37 0.001 . 128 24 GLN HA H 4.31 0.001 . 129 24 GLN HB2 H 2.00 0.002 . 130 24 GLN HB3 H 1.88 0.003 . 131 24 GLN HG2 H 2.39 0.001 . 132 24 GLN HG3 H 2.25 0.003 . 133 24 GLN NE2 N 108.46 0.003 . 134 24 GLN HE21 H 7.21 0.003 . 135 24 GLN HE22 H 6.59 0.003 . 136 25 ASN N N 115.98 0.003 . 137 25 ASN H H 8.00 0.001 . 138 25 ASN HA H 4.34 0.003 . 139 25 ASN HB2 H 2.78 0.006 . 140 25 ASN HB3 H 2.72 0.002 . 141 25 ASN ND2 N 111.90 0.004 . 142 25 ASN HD21 H 7.55 0.004 . 143 25 ASN HD22 H 6.68 0.001 . 144 26 GLU N N 115.67 0.004 . 145 26 GLU H H 7.16 0.003 . 146 26 GLU HA H 4.29 0.001 . 147 26 GLU HB2 H 2.05 0.001 . 148 26 GLU HB3 H 1.77 0.004 . 149 26 GLU HG2 H 2.21 0.004 . 150 26 GLU HG3 H 2.16 0.006 . 151 27 ASP N N 117.23 0.004 . 152 27 ASP H H 7.73 0.001 . 153 27 ASP HA H 4.57 0.007 . 154 27 ASP HB2 H 2.43 0.001 . 155 28 ALA N N 126.93 0.001 . 156 28 ALA H H 8.70 0.002 . 157 28 ALA HA H 4.25 0.001 . 158 28 ALA HB H 1.38 0.004 . 159 29 GLN N N 112.54 0.002 . 160 29 GLN H H 7.89 0.001 . 161 29 GLN HA H 4.26 0.002 . 162 29 GLN HB2 H 2.23 0.003 . 163 29 GLN HB3 H 2.02 0.003 . 164 29 GLN HG2 H 2.40 0.010 . 165 29 GLN HG3 H 2.27 0.005 . 166 29 GLN NE2 N 111.90 0.002 . 167 29 GLN HE21 H 7.53 0.002 . 168 29 GLN HE22 H 6.74 0.003 . 169 30 ALA N N 122.86 0.003 . 170 30 ALA H H 7.64 0.002 . 171 30 ALA HA H 4.47 0.002 . 172 30 ALA HB H 1.23 0.001 . 173 31 THR N N 114.73 0.003 . 174 31 THR H H 8.59 0.004 . 175 31 THR HA H 4.54 0.005 . 176 31 THR HB H 4.00 0.006 . 177 31 THR HG2 H 1.09 0.002 . 178 32 VAL N N 124.11 0.003 . 179 32 VAL H H 8.75 0.001 . 180 32 VAL HA H 4.56 0.012 . 181 32 VAL HB H 1.90 0.003 . 182 32 VAL HG1 H 0.74 0.002 . 183 32 VAL HG2 H 0.54 0.001 . 184 33 GLN N N 126.62 0.003 . 185 33 GLN H H 8.86 0.001 . 186 33 GLN HA H 4.64 0.001 . 187 33 GLN HB2 H 1.99 0.001 . 188 33 GLN HB3 H 1.83 0.003 . 189 33 GLN HG2 H 2.18 0.002 . 190 33 GLN NE2 N 111.27 0.003 . 191 33 GLN HE21 H 7.42 0.002 . 192 33 GLN HE22 H 6.67 0.002 . 193 34 VAL N N 124.11 0.002 . 194 34 VAL H H 8.94 0.001 . 195 34 VAL HA H 4.33 0.003 . 196 34 VAL HB H 1.88 0.002 . 197 34 VAL HG1 H 0.69 0.002 . 198 34 VAL HG2 H 0.55 0.003 . 199 35 ASP N N 127.24 0.002 . 200 35 ASP H H 8.35 0.002 . 201 35 ASP HA H 4.84 0.002 . 202 35 ASP HB2 H 3.00 0.004 . 203 35 ASP HB3 H 2.35 0.001 . 204 36 LEU N N 124.74 0.002 . 205 36 LEU H H 8.82 0.002 . 206 36 LEU HA H 3.64 0.002 . 207 36 LEU HB2 H 1.62 0.001 . 208 36 LEU HB3 H 1.41 0.003 . 209 36 LEU HG H 1.50 0.001 . 210 36 LEU HD1 H 0.70 0.002 . 211 36 LEU HD2 H 0.48 0.007 . 212 37 THR N N 112.85 0.002 . 213 37 THR H H 8.37 0.001 . 214 37 THR HA H 4.00 0.004 . 215 37 THR HB H 4.19 0.002 . 216 37 THR HG2 H 1.13 0.003 . 217 38 SER N N 114.73 0.002 . 218 38 SER H H 7.71 0.002 . 219 38 SER HA H 4.27 0.012 . 220 38 SER HB2 H 3.81 0.001 . 221 38 SER HB3 H 3.67 0.001 . 222 39 LYS N N 115.67 0.002 . 223 39 LYS H H 7.89 0.001 . 224 39 LYS HA H 3.49 0.001 . 225 39 LYS HB2 H 2.02 0.012 . 226 39 LYS HG2 H 1.23 0.001 . 227 39 LYS HG3 H 1.14 0.003 . 228 39 LYS HD2 H 1.51 0.004 . 229 40 LYS N N 115.35 0.002 . 230 40 LYS H H 7.41 0.002 . 231 40 LYS HA H 4.76 0.002 . 232 40 LYS HB2 H 1.33 0.004 . 233 40 LYS HG2 H 1.22 0.004 . 234 40 LYS HG3 H 1.18 0.007 . 235 40 LYS HD2 H 1.60 0.003 . 236 41 VAL N N 125.99 0.004 . 237 41 VAL H H 9.49 0.002 . 238 41 VAL HA H 4.68 0.004 . 239 41 VAL HB H 1.80 0.001 . 240 41 VAL HG1 H 0.71 0.001 . 241 41 VAL HG2 H 0.61 0.005 . 242 42 THR N N 124.11 0.002 . 243 42 THR H H 9.23 0.001 . 244 42 THR HA H 4.86 0.002 . 245 42 THR HB H 3.91 0.001 . 246 42 THR HG2 H 0.97 0.001 . 247 43 ILE N N 128.18 0.002 . 248 43 ILE H H 9.35 0.001 . 249 43 ILE HA H 4.99 0.001 . 250 43 ILE HB H 1.58 0.002 . 251 43 ILE HG2 H 0.81 0.002 . 252 43 ILE HG12 H 1.50 0.002 . 253 43 ILE HD1 H 0.70 0.014 . 254 44 THR N N 124.74 0.002 . 255 44 THR H H 8.75 0.001 . 256 44 THR HA H 5.17 0.002 . 257 44 THR HB H 4.00 0.003 . 258 44 THR HG2 H 1.03 0.004 . 259 45 SER N N 118.80 0.003 . 260 45 SER H H 8.49 0.002 . 261 45 SER HA H 4.68 0.005 . 262 45 SER HB2 H 3.89 0.002 . 263 45 SER HB3 H 3.33 0.002 . 264 45 SER HG H 6.85 0.002 . 265 46 ALA N N 125.05 0.003 . 266 46 ALA H H 8.50 0.001 . 267 46 ALA HA H 4.34 0.003 . 268 46 ALA HB H 1.29 0.003 . 269 47 LEU N N 119.42 0.003 . 270 47 LEU H H 8.58 0.003 . 271 47 LEU HA H 4.13 0.003 . 272 47 LEU HB2 H 1.62 0.002 . 273 47 LEU HB3 H 1.29 0.002 . 274 47 LEU HG H 1.56 0.006 . 275 47 LEU HD1 H 0.72 0.004 . 276 47 LEU HD2 H 0.70 0.007 . 277 48 GLY N N 103.78 0.002 . 278 48 GLY H H 8.05 0.004 . 279 48 GLY HA2 H 4.21 0.002 . 280 48 GLY HA3 H 3.79 0.001 . 281 49 GLU N N 119.42 0.001 . 282 49 GLU H H 8.64 0.001 . 283 49 GLU HA H 3.59 0.002 . 284 49 GLU HB2 H 2.07 0.005 . 285 49 GLU HB3 H 1.88 0.001 . 286 49 GLU HG2 H 2.10 0.005 . 287 50 GLU N N 117.23 0.001 . 288 50 GLU H H 8.92 0.002 . 289 50 GLU HA H 3.88 0.001 . 290 50 GLU HB2 H 1.97 0.001 . 291 50 GLU HB3 H 1.89 0.004 . 292 50 GLU HG2 H 2.21 0.001 . 293 50 GLU HG3 H 2.07 0.001 . 294 51 GLN N N 118.17 0.002 . 295 51 GLN H H 7.63 0.001 . 296 51 GLN HA H 4.00 0.001 . 297 51 GLN HB2 H 2.25 0.002 . 298 51 GLN HB3 H 1.88 0.001 . 299 51 GLN HG2 H 2.39 0.002 . 300 51 GLN NE2 N 112.84 0.002 . 301 51 GLN HE21 H 7.88 0.003 . 302 51 GLN HE22 H 6.89 0.001 . 303 52 LEU N N 120.05 0.001 . 304 52 LEU H H 7.98 0.001 . 305 52 LEU HA H 3.87 0.001 . 306 52 LEU HB2 H 1.90 0.001 . 307 52 LEU HB3 H 0.99 0.002 . 308 52 LEU HG H 1.64 0.002 . 309 52 LEU HD1 H 0.76 0.002 . 310 52 LEU HD2 H 0.67 0.001 . 311 53 ARG N N 117.54 0.001 . 312 53 ARG H H 8.60 0.002 . 313 53 ARG HA H 3.64 0.001 . 314 53 ARG HB2 H 1.83 0.002 . 315 53 ARG HB3 H 1.76 0.003 . 316 53 ARG HG2 H 1.35 0.003 . 317 53 ARG HD2 H 3.15 0.002 . 318 53 ARG HD3 H 3.05 0.007 . 319 54 THR N N 115.67 0.002 . 320 54 THR H H 7.99 0.001 . 321 54 THR HA H 3.87 0.002 . 322 54 THR HB H 4.14 0.001 . 323 54 THR HG2 H 1.17 0.002 . 324 55 ALA N N 124.74 0.002 . 325 55 ALA H H 7.93 0.001 . 326 55 ALA HA H 4.10 0.002 . 327 55 ALA HB H 1.30 0.002 . 328 56 ILE N N 118.17 0.003 . 329 56 ILE H H 8.04 0.001 . 330 56 ILE HA H 3.30 0.002 . 331 56 ILE HB H 1.60 0.002 . 332 56 ILE HG2 H 0.64 0.004 . 333 56 ILE HG12 H 0.88 0.003 . 334 56 ILE HD1 H 0.46 0.002 . 335 57 ALA N N 121.61 0.003 . 336 57 ALA H H 8.04 0.001 . 337 57 ALA HA H 4.75 0.006 . 338 57 ALA HB H 1.48 0.005 . 339 58 SER N N 115.67 0.003 . 340 58 SER H H 8.27 0.004 . 341 58 SER HA H 4.22 0.004 . 342 58 SER HB2 H 4.01 0.002 . 343 58 SER HB3 H 3.97 0.003 . 344 59 ALA N N 122.55 0.003 . 345 59 ALA H H 7.36 0.003 . 346 59 ALA HA H 4.47 0.003 . 347 59 ALA HB H 1.46 0.003 . 348 60 GLY N N 104.72 0.003 . 349 60 GLY H H 7.98 0.002 . 350 60 GLY HA2 H 3.96 0.001 . 351 60 GLY HA3 H 3.58 0.005 . 352 61 HIS N N 117.86 0.003 . 353 61 HIS H H 6.97 0.001 . 354 61 HIS HA H 4.41 0.004 . 355 61 HIS HB2 H 2.50 0.001 . 356 61 HIS HB3 H 2.31 0.001 . 357 61 HIS HD2 H 6.35 0.003 . 358 61 HIS HE1 H 7.67 0.003 . 359 62 GLU N N 120.36 0.003 . 360 62 GLU H H 8.04 0.003 . 361 62 GLU HA H 4.42 0.006 . 362 62 GLU HB2 H 1.89 0.002 . 363 62 GLU HB3 H 1.73 0.002 . 364 62 GLU HG2 H 2.12 0.004 . 365 62 GLU HG3 H 2.08 0.001 . 366 63 VAL N N 119.42 0.002 . 367 63 VAL H H 8.03 0.002 . 368 63 VAL HA H 4.57 0.003 . 369 63 VAL HB H 1.92 0.003 . 370 63 VAL HG1 H 1.04 0.002 . 371 63 VAL HG2 H 0.86 0.004 . 373 64 GLU H H 8.49 0.002 . 374 64 GLU HA H 3.98 0.004 . 375 64 GLU HB2 H 1.95 0.001 . 376 64 GLU HB3 H 1.74 0.002 . 377 64 GLU HG2 H 2.10 0.002 . stop_ save_