data_1672 #Corrected using PDB structure: 2BC5C # #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 # 58 M HA 4.71 3.96 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.09 N/A N/A N/A -4.20 -0.08 # #bmr1672.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr1672.str file): #HA CA CB CO N HN #N/A N/A N/A N/A -4.20 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.02 N/A N/A N/A +/-0.36 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.832 N/A N/A N/A 0.858 0.685 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.115 N/A N/A N/A 1.753 0.248 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N NMR Resonance Assignments and Preliminary Structural Characterization of Escherichia coli Apocytochrome b562 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Feng Yiqing . . 2 Wand A. Joshua . 3 Sligar Stephen G. . stop_ _BMRB_accession_number 1672 _BMRB_flat_file_name bmr1672.str _Entry_type revision _Submission_date 1995-07-31 _Accession_date 1996-04-13 _Entry_origination BMRB _NMR_STAR_version 2.1 _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' 498 '15N chemical shifts' 108 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-13 revision BMRB 'Link to the Protein Data Bank added' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Feng, Yiqing, Wand, A. Joshua, Sligar, Stephen G., "1H and 15N NMR Resonance Assignments and Preliminary Structural Characterization of Escherichia coli Apocytochrome b562," Biochemistry 30 (31), 7711-7717 (1991). ; _Citation_title ; 1H and 15N NMR Resonance Assignments and Preliminary Structural Characterization of Escherichia coli Apocytochrome b562 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Feng Yiqing . . 2 Wand A. Joshua . 3 Sligar Stephen G. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 30 _Journal_issue 31 _Page_first 7711 _Page_last 7717 _Year 1991 save_ ################################## # Molecular system description # ################################## save_system_cytochrome_b562 _Saveframe_category molecular_system _Mol_system_name 'cytochrome b562' _Abbreviation_common ? loop_ _Mol_system_component_name _Mol_label 'cytochrome b562' $cytochrome_b562 stop_ _System_physical_state ? _System_oligomer_state ? _System_paramagnetic ? loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 256B "A Chain A, Cytochrome b562 (Oxidized)" . PDB 1QPU "A Chain A, Solution Structure Of Oxidized Escherichia Coli Cytochrome B562" . PDB 1APC "Cytochrome B562 (Apo Form) (Nmr, 1 Structure)" . PDB 1QQ3 "A Chain A, The Solution Structure Of The Heme Binding Variant Arg98cys Of Oxidized Escherichia Coli Cytochrome B562" . stop_ save_ ######################## # Monomeric polymers # ######################## save_cytochrome_b562 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome b562' _Name_variant 'apo form' _Abbreviation_common ? ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; ADLEDNMETLNDNLKVIEKA DNAAQVKDALTKMRAAALDA QKATPPKLEDKSPDSPEMKD FRHGFDILVGQIDDALKLAN EGKVKEAQAAAEQLKTTRNA YHQKYR ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 ASP 3 LEU 4 GLU 5 ASP 6 ASN 7 MET 8 GLU 9 THR 10 LEU 11 ASN 12 ASP 13 ASN 14 LEU 15 LYS 16 VAL 17 ILE 18 GLU 19 LYS 20 ALA 21 ASP 22 ASN 23 ALA 24 ALA 25 GLN 26 VAL 27 LYS 28 ASP 29 ALA 30 LEU 31 THR 32 LYS 33 MET 34 ARG 35 ALA 36 ALA 37 ALA 38 LEU 39 ASP 40 ALA 41 GLN 42 LYS 43 ALA 44 THR 45 PRO 46 PRO 47 LYS 48 LEU 49 GLU 50 ASP 51 LYS 52 SER 53 PRO 54 ASP 55 SER 56 PRO 57 GLU 58 MET 59 LYS 60 ASP 61 PHE 62 ARG 63 HIS 64 GLY 65 PHE 66 ASP 67 ILE 68 LEU 69 VAL 70 GLY 71 GLN 72 ILE 73 ASP 74 ASP 75 ALA 76 LEU 77 LYS 78 LEU 79 ALA 80 ASN 81 GLU 82 GLY 83 LYS 84 VAL 85 LYS 86 GLU 87 ALA 88 GLN 89 ALA 90 ALA 91 ALA 92 GLU 93 GLN 94 LEU 95 LYS 96 THR 97 THR 98 ARG 99 ASN 100 ALA 101 TYR 102 HIS 103 GLN 104 LYS 105 TYR 106 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 1APC "Cytochrome B562 (Apo Form) (Nmr, 1 Structure)" 100.00 106 100 100 4e-54 PDB 1QPU "A Chain A, Solution Structure Of OxidizedEscherichia Coli Cytochrome B562" 100.00 106 100 100 4e-54 PDB 256B "A Chain A, Cytochrome b562 (Oxidized)" 100.00 106 100 100 4e-54 PDB 1QQ3 "A Chain A, The Solution Structure Of The HemeBinding Variant Arg98cys Of Oxidized Escherichia ColiCytochrome B562" 100.00 106 99 99 4e-53 PDB 1LM3 "B Chain B, A Multi-Generation Analysis OfCytochrome B562 Redox Variants: Evolutionary StrategiesFor Modulating Redox Potential Revealed Using A LibraryApproach" 100.00 106 98 99 2e-52 PDB 1M6T "A Chain A, Crystal Structure Of B562ril, ARedesigned Four Helix Bundle" 100.00 106 98 98 2e-51 EMBL CAA47706.1 "cytochrome b562 [Escherichia coli]" 82.81 128 100 100 4e-54 GenBank AAN45672.1 "Soluble cytochrome B562 precursor[Shigella flexneri 2a str. 301]" 92.98 114 99 99 6e-41 GenBank AAB20782.1 "cytochrome b562 [Escherichia coli]" 82.81 128 100 100 4e-54 PIR CBEC62 "cytochrome b562 precursor [validated] -Escherichia coli (strain K-12)" 82.81 128 100 100 4e-54 REF NP_709965.1 "Soluble cytochrome B562 precursor[Shigella flexneri 2a str. 301]" 92.98 114 99 99 6e-41 SWISS-PROT P00192 "C562_ECOLI Soluble cytochrome b562 precursor(Cytochrome b-562)" 82.81 128 100 100 4e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Genus _Species _Strain $cytochrome_b562 . ? Azotobacter vinelandii 'ATCC 13705' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Genus _Species _Strain $cytochrome_b562 'not available' Escherichia coli TB-1 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 ? ? ? ? stop_ save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.2 . na temperature 293 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Chem_shift_value TSP H 0 'external [15]NH4Cl' N 24.93 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_data_set_one _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'cytochrome b562' 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 1 ALA HA H 4.18 . 1 2 1 ALA HB H 1.57 . 1 3 2 ASP H H 8.98 . 1 4 2 ASP HA H 4.68 . 1 5 2 ASP HB2 H 2.91 . 2 6 2 ASP HB3 H 3.04 . 2 7 2 ASP N N 119.80 . 1 8 3 LEU H H 8.76 . 1 9 3 LEU HA H 4.09 . 1 10 3 LEU HB2 H 1.62 . 2 11 3 LEU HB3 H 1.92 . 2 12 3 LEU HG H 1.73 . 1 13 3 LEU HD1 H 1.04 . 2 14 3 LEU HD2 H 1.18 . 2 15 3 LEU N N 122.20 . 1 16 4 GLU H H 8.77 . 1 17 4 GLU HA H 4.10 . 1 18 4 GLU HB2 H 2.05 . 2 19 4 GLU HB3 H 2.52 . 2 20 4 GLU N N 117.40 . 1 21 5 ASP H H 8.06 . 1 22 5 ASP HA H 4.52 . 1 23 5 ASP HB2 H 2.83 . 1 24 5 ASP HB3 H 2.83 . 1 25 5 ASP N N 119.70 . 1 26 6 ASN H H 8.08 . 1 27 6 ASN HA H 4.61 . 1 28 6 ASN HB2 H 2.61 . 2 29 6 ASN HB3 H 2.77 . 2 30 6 ASN ND2 N 118.50 . 1 31 6 ASN HD21 H 6.37 . 2 32 6 ASN HD22 H 8.42 . 2 33 6 ASN N N 117.70 . 1 34 7 MET H H 8.67 . 1 35 7 MET HA H 4.55 . 1 36 7 MET HB2 H 2.41 . 1 37 7 MET HB3 H 2.41 . 1 38 7 MET N N 118.10 . 1 39 8 GLU H H 8.35 . 1 40 8 GLU HA H 4.28 . 1 41 8 GLU HB2 H 2.33 . 2 42 8 GLU HB3 H 2.57 . 2 43 8 GLU N N 122.10 . 1 44 9 THR H H 8.43 . 1 45 9 THR HA H 4.12 . 1 46 9 THR HB H 4.46 . 1 47 9 THR HG2 H 1.20 . 1 48 9 THR N N 117.40 . 1 49 10 LEU H H 8.24 . 1 50 10 LEU HA H 4.06 . 1 51 10 LEU HB2 H 1.98 . 2 52 10 LEU HB3 H 2.23 . 2 53 10 LEU HD1 H 1.01 . 1 54 10 LEU HD2 H 1.01 . 1 55 10 LEU N N 122.60 . 1 56 11 ASN H H 8.14 . 1 57 11 ASN HA H 4.46 . 1 58 11 ASN HB2 H 2.90 . 2 59 11 ASN HB3 H 3.02 . 2 60 11 ASN ND2 N 118.80 . 1 61 11 ASN HD21 H 7.09 . 2 62 11 ASN HD22 H 7.90 . 2 63 11 ASN N N 117.30 . 1 64 12 ASP H H 9.32 . 1 65 12 ASP HA H 4.43 . 1 66 12 ASP HB2 H 2.75 . 2 67 12 ASP HB3 H 2.90 . 2 68 12 ASP N N 119.40 . 1 69 13 ASN H H 7.94 . 1 70 13 ASN HA H 4.58 . 1 71 13 ASN HB2 H 2.58 . 2 72 13 ASN HB3 H 2.71 . 2 73 13 ASN N N 116.70 . 1 74 14 LEU H H 8.15 . 1 75 14 LEU HA H 4.15 . 1 76 14 LEU HB2 H 1.76 . 2 77 14 LEU HB3 H 1.87 . 2 78 14 LEU N N 122.90 . 1 79 15 LYS H H 7.42 . 1 80 15 LYS HA H 4.17 . 1 81 15 LYS HB2 H 1.94 . 2 82 15 LYS HB3 H 2.07 . 2 83 15 LYS N N 117.80 . 1 84 16 VAL H H 7.30 . 1 85 16 VAL HA H 3.60 . 1 86 16 VAL HB H 2.47 . 1 87 16 VAL HG1 H 0.99 . 2 88 16 VAL HG2 H 1.15 . 2 89 16 VAL N N 118.40 . 1 90 17 ILE H H 7.97 . 1 91 17 ILE HA H 3.43 . 1 92 17 ILE HB H 2.17 . 1 93 17 ILE HG2 H 1.01 . 1 94 17 ILE HD1 H 0.89 . 1 95 17 ILE N N 119.00 . 1 96 18 GLU H H 8.05 . 1 97 18 GLU HA H 3.98 . 1 98 18 GLU HB2 H 2.34 . 1 99 18 GLU HB3 H 2.34 . 1 100 18 GLU N N 117.30 . 1 101 19 LYS H H 7.26 . 1 102 19 LYS HA H 4.48 . 1 103 19 LYS HB2 H 1.82 . 2 104 19 LYS HB3 H 2.04 . 2 105 19 LYS HG2 H 1.57 . 2 106 19 LYS HG3 H 1.71 . 2 107 19 LYS N N 114.70 . 1 108 20 ALA H H 7.37 . 1 109 20 ALA HA H 4.20 . 1 110 20 ALA HB H 1.52 . 1 111 20 ALA N N 123.30 . 1 112 21 ASP H H 8.83 . 1 113 21 ASP HA H 4.85 . 1 114 21 ASP HB2 H 2.73 . 2 115 21 ASP HB3 H 2.87 . 2 116 21 ASP N N 115.90 . 1 117 22 ASN H H 7.73 . 1 118 22 ASN HA H 5.01 . 1 119 22 ASN HB2 H 2.95 . 2 120 22 ASN HB3 H 3.04 . 2 121 22 ASN N N 112.20 . 1 122 23 ALA H H 9.13 . 1 123 23 ALA HA H 3.83 . 1 124 23 ALA HB H 1.55 . 1 125 23 ALA N N 121.90 . 1 126 24 ALA H H 8.53 . 1 127 24 ALA HA H 4.09 . 1 128 24 ALA HB H 1.54 . 1 129 24 ALA N N 121.60 . 1 130 25 GLN H H 8.16 . 1 131 25 GLN HA H 4.19 . 1 132 25 GLN HB2 H 2.40 . 1 133 25 GLN HB3 H 2.40 . 1 134 25 GLN HG2 H 1.95 . 2 135 25 GLN HG3 H 2.67 . 2 136 25 GLN NE2 N 114.90 . 1 137 25 GLN HE21 H 7.16 . 2 138 25 GLN HE22 H 7.47 . 2 139 25 GLN N N 116.90 . 1 140 26 VAL H H 7.26 . 1 141 26 VAL HA H 3.55 . 1 142 26 VAL HB H 2.22 . 1 143 26 VAL HG1 H 0.94 . 2 144 26 VAL HG2 H 1.11 . 2 145 26 VAL N N 117.70 . 1 146 27 LYS H H 8.86 . 1 147 27 LYS HA H 3.78 . 1 148 27 LYS HB2 H 1.83 . 2 149 27 LYS HB3 H 2.03 . 2 150 27 LYS HG2 H 1.34 . 2 151 27 LYS HG3 H 1.37 . 2 152 27 LYS HD2 H 1.69 . 1 153 27 LYS HD3 H 1.69 . 1 154 27 LYS HE2 H 2.97 . 1 155 27 LYS HE3 H 2.97 . 1 156 27 LYS N N 119.10 . 1 157 28 ASP H H 8.31 . 1 158 28 ASP HA H 4.40 . 1 159 28 ASP HB2 H 2.73 . 2 160 28 ASP HB3 H 2.85 . 2 161 28 ASP N N 120.30 . 1 162 29 ALA H H 7.64 . 1 163 29 ALA HA H 4.25 . 1 164 29 ALA HB H 1.63 . 1 165 29 ALA N N 121.10 . 1 166 30 LEU H H 8.63 . 1 167 30 LEU HA H 4.18 . 1 168 30 LEU HB2 H 2.14 . 1 169 30 LEU HB3 H 2.14 . 1 170 30 LEU HG H 1.35 . 1 171 30 LEU HD1 H 0.74 . 2 172 30 LEU HD2 H 0.99 . 2 173 30 LEU N N 117.60 . 1 174 31 THR H H 8.42 . 1 175 31 THR HA H 3.82 . 1 176 31 THR HB H 4.53 . 1 177 31 THR HG2 H 1.34 . 1 178 31 THR N N 116.10 . 1 179 32 LYS H H 7.76 . 1 180 32 LYS HA H 4.15 . 1 181 32 LYS HB2 H 1.68 . 2 182 32 LYS HB3 H 1.78 . 2 183 32 LYS N N 122.60 . 1 184 33 MET H H 8.50 . 1 185 33 MET HA H 3.78 . 1 186 33 MET HB2 H 2.45 . 1 187 33 MET HB3 H 2.45 . 1 188 33 MET HG2 H 2.21 . 1 189 33 MET HG3 H 2.21 . 1 190 33 MET N N 118.70 . 1 191 34 ARG H H 8.70 . 1 192 34 ARG HA H 3.70 . 1 193 34 ARG HB2 H 2.08 . 1 194 34 ARG HB3 H 2.08 . 1 195 34 ARG HG2 H 1.95 . 1 196 34 ARG HG3 H 1.95 . 1 197 34 ARG N N 120.40 . 1 198 35 ALA H H 7.30 . 1 199 35 ALA HA H 4.13 . 1 200 35 ALA HB H 1.56 . 1 201 35 ALA N N 117.20 . 1 202 36 ALA H H 7.74 . 1 203 36 ALA HA H 4.20 . 1 204 36 ALA HB H 1.56 . 1 205 36 ALA N N 120.40 . 1 206 37 ALA H H 8.60 . 1 207 37 ALA HA H 3.92 . 1 208 37 ALA HB H 1.54 . 1 209 37 ALA N N 120.20 . 1 210 38 LEU H H 7.86 . 1 211 38 LEU HA H 3.98 . 1 212 38 LEU HB2 H 1.88 . 1 213 38 LEU HB3 H 1.88 . 1 214 38 LEU HD1 H 0.94 . 1 215 38 LEU HD2 H 0.94 . 1 216 38 LEU N N 115.70 . 1 217 39 ASP H H 7.82 . 1 218 39 ASP HA H 4.42 . 1 219 39 ASP HB2 H 2.68 . 2 220 39 ASP HB3 H 2.73 . 2 221 39 ASP N N 119.50 . 1 222 40 ALA H H 8.38 . 1 223 40 ALA HA H 3.82 . 1 224 40 ALA HB H 0.94 . 1 225 40 ALA N N 123.40 . 1 226 41 GLN H H 7.09 . 1 227 41 GLN HA H 3.36 . 1 228 41 GLN HB2 H 2.20 . 2 229 41 GLN HB3 H 1.79 . 2 230 41 GLN HG2 H 2.48 . 1 231 41 GLN HG3 H 2.48 . 1 232 41 GLN N N 112.70 . 1 233 42 LYS H H 7.12 . 1 234 42 LYS HA H 4.33 . 1 235 42 LYS HB2 H 1.91 . 2 236 42 LYS HB3 H 2.08 . 2 237 42 LYS HG2 H 1.54 . 2 238 42 LYS HG3 H 1.73 . 2 239 42 LYS N N 113.90 . 1 240 43 ALA H H 7.83 . 1 241 43 ALA HA H 4.45 . 1 242 43 ALA HB H 1.61 . 1 243 43 ALA N N 123.50 . 1 244 44 THR H H 8.21 . 1 245 44 THR HA H 4.37 . 1 246 44 THR HB H 3.95 . 1 247 44 THR HG2 H 1.14 . 1 248 44 THR N N 113.90 . 1 249 46 PRO HA H 4.35 . 1 250 46 PRO HB2 H 2.03 . 2 251 46 PRO HB3 H 2.44 . 2 252 46 PRO HG2 H 2.16 . 1 253 46 PRO HG3 H 2.16 . 1 254 46 PRO HD2 H 3.81 . 1 255 46 PRO HD3 H 3.81 . 1 256 47 LYS H H 8.59 . 1 257 47 LYS HA H 4.23 . 1 258 47 LYS HB2 H 1.94 . 2 259 47 LYS HB3 H 2.00 . 2 260 47 LYS N N 114.40 . 1 261 48 LEU H H 7.89 . 1 262 48 LEU HA H 4.55 . 1 263 48 LEU HB2 H 1.69 . 1 264 48 LEU HB3 H 1.69 . 1 265 48 LEU HG H 1.46 . 1 266 48 LEU HD1 H 0.72 . 2 267 48 LEU HD2 H 0.83 . 2 268 48 LEU N N 117.60 . 1 269 49 GLU HA H 3.98 . 1 270 50 ASP H H 8.50 . 1 271 50 ASP HA H 4.70 . 1 272 50 ASP HB2 H 2.83 . 1 273 50 ASP HB3 H 2.83 . 1 274 50 ASP N N 116.00 . 1 275 51 LYS H H 7.77 . 1 276 51 LYS HA H 4.55 . 1 277 51 LYS HB2 H 2.02 . 1 278 51 LYS HB3 H 2.02 . 1 279 51 LYS N N 119.40 . 1 280 52 SER H H 8.85 . 1 281 52 SER HA H 4.79 . 1 282 52 SER HB2 H 4.23 . 2 283 52 SER HB3 H 4.01 . 2 284 52 SER N N 116.90 . 1 285 54 ASP H H 8.05 . 1 286 54 ASP HA H 4.83 . 1 287 54 ASP HB2 H 2.66 . 2 288 54 ASP HB3 H 2.84 . 2 289 54 ASP N N 113.60 . 1 290 55 SER H H 7.90 . 1 291 55 SER HA H 4.64 . 1 292 55 SER N N 116.30 . 1 293 56 PRO HA H 4.00 . 1 294 57 GLU H H 9.62 . 1 295 57 GLU HA H 4.22 . 1 296 57 GLU HB2 H 2.08 . 1 297 57 GLU HB3 H 2.08 . 1 298 57 GLU HG2 H 2.47 . 1 299 57 GLU HG3 H 2.47 . 1 300 57 GLU N N 116.30 . 1 301 58 MET H H 7.84 . 1 302 58 MET HA H 4.80 . 1 303 58 MET N N 119.10 . 1 304 59 LYS H H 8.68 . 1 305 59 LYS HA H 4.11 . 1 306 59 LYS HB2 H 1.68 . 2 307 59 LYS HB3 H 1.97 . 2 308 59 LYS N N 120.50 . 1 309 60 ASP H H 8.52 . 1 310 60 ASP HA H 4.64 . 1 311 60 ASP HB2 H 2.94 . 1 312 60 ASP HB3 H 2.94 . 1 313 60 ASP N N 120.00 . 1 314 61 PHE H H 8.23 . 1 315 61 PHE HA H 4.40 . 1 316 61 PHE HB2 H 3.29 . 2 317 61 PHE HB3 H 3.49 . 2 318 61 PHE HD1 H 7.23 . 1 319 61 PHE HD2 H 7.23 . 1 320 61 PHE HE1 H 7.49 . 1 321 61 PHE HE2 H 7.49 . 1 322 61 PHE HZ H 7.29 . 1 323 61 PHE N N 121.20 . 1 324 62 ARG H H 8.73 . 1 325 62 ARG HA H 4.05 . 1 326 62 ARG HB2 H 2.19 . 2 327 62 ARG HB3 H 2.39 . 2 328 62 ARG HG2 H 2.05 . 1 329 62 ARG HG3 H 2.05 . 1 330 62 ARG N N 117.10 . 1 331 63 HIS H H 8.85 . 1 332 63 HIS HA H 4.71 . 1 333 63 HIS HB2 H 3.57 . 2 334 63 HIS HB3 H 3.62 . 2 335 63 HIS HD2 H 7.49 . 1 336 63 HIS HE1 H 8.77 . 1 337 63 HIS N N 118.70 . 1 338 64 GLY H H 8.10 . 1 339 64 GLY HA2 H 3.30 . 2 340 64 GLY HA3 H 3.64 . 2 341 64 GLY N N 105.30 . 1 342 65 PHE H H 7.10 . 1 343 65 PHE HA H 4.20 . 1 344 65 PHE HB2 H 2.80 . 2 345 65 PHE HB3 H 3.02 . 2 346 65 PHE HD1 H 6.94 . 1 347 65 PHE HD2 H 6.94 . 1 348 65 PHE HE1 H 6.69 . 1 349 65 PHE HE2 H 6.69 . 1 350 65 PHE HZ H 7.04 . 1 351 65 PHE N N 117.00 . 1 352 66 ASP H H 7.70 . 1 353 66 ASP HA H 4.50 . 1 354 66 ASP HB2 H 2.76 . 2 355 66 ASP HB3 H 2.89 . 2 356 66 ASP N N 121.30 . 1 357 67 ILE H H 7.66 . 1 358 67 ILE HA H 3.69 . 1 359 67 ILE HB H 1.85 . 1 360 67 ILE HG12 H 0.95 . 2 361 67 ILE HG13 H 1.20 . 2 362 67 ILE HG2 H 0.84 . 1 363 67 ILE HD1 H 0.70 . 1 364 67 ILE N N 119.80 . 1 365 68 LEU H H 7.46 . 1 366 68 LEU HA H 4.26 . 1 367 68 LEU HB2 H 1.72 . 2 368 68 LEU HB3 H 1.82 . 2 369 68 LEU HD1 H 0.93 . 1 370 68 LEU HD2 H 0.93 . 1 371 68 LEU N N 120.60 . 1 372 69 VAL H H 8.78 . 1 373 69 VAL HA H 3.48 . 1 374 69 VAL HB H 2.25 . 1 375 69 VAL HG1 H 0.99 . 2 376 69 VAL HG2 H 1.12 . 2 377 69 VAL N N 118.40 . 1 378 70 GLY H H 7.94 . 1 379 70 GLY HA2 H 3.94 . 2 380 70 GLY HA3 H 3.96 . 2 381 70 GLY N N 105.50 . 1 382 71 GLN H H 7.99 . 1 383 71 GLN HA H 4.23 . 1 384 71 GLN HB2 H 2.52 . 2 385 71 GLN HB3 H 1.99 . 2 386 71 GLN HG2 H 2.38 . 1 387 71 GLN HG3 H 2.38 . 1 388 71 GLN NE2 N 111.50 . 1 389 71 GLN HE21 H 6.26 . 2 390 71 GLN HE22 H 7.37 . 2 391 71 GLN N N 120.60 . 1 392 72 ILE H H 8.77 . 1 393 72 ILE HA H 3.56 . 1 394 72 ILE HB H 2.13 . 1 395 72 ILE HG2 H 1.01 . 1 396 72 ILE HD1 H 0.75 . 1 397 72 ILE N N 123.00 . 1 398 73 ASP H H 9.09 . 1 399 73 ASP HA H 4.65 . 1 400 73 ASP HB2 H 2.65 . 2 401 73 ASP HB3 H 2.96 . 2 402 73 ASP N N 121.40 . 1 403 74 ASP H H 8.21 . 1 404 74 ASP HA H 4.53 . 1 405 74 ASP HB2 H 2.73 . 2 406 74 ASP HB3 H 2.90 . 2 407 74 ASP N N 122.00 . 1 408 75 ALA H H 7.96 . 1 409 75 ALA HA H 4.13 . 1 410 75 ALA HB H 1.54 . 1 411 75 ALA N N 122.90 . 1 412 76 LEU H H 9.27 . 1 413 76 LEU HA H 3.88 . 1 414 76 LEU HB2 H 1.70 . 2 415 76 LEU HB3 H 2.04 . 2 416 76 LEU HG H 1.34 . 1 417 76 LEU HD1 H 0.74 . 2 418 76 LEU HD2 H 0.99 . 2 419 76 LEU N N 121.00 . 1 420 77 LYS H H 7.94 . 1 421 77 LYS HA H 4.09 . 1 422 77 LYS HB2 H 2.05 . 2 423 77 LYS HB3 H 1.64 . 2 424 77 LYS HG2 H 1.77 . 1 425 77 LYS HG3 H 1.77 . 1 426 77 LYS N N 120.00 . 1 427 78 LEU H H 7.12 . 1 428 78 LEU HA H 4.15 . 1 429 78 LEU HB2 H 2.05 . 1 430 78 LEU HB3 H 2.05 . 1 431 78 LEU HD1 H 0.83 . 1 432 78 LEU HD2 H 0.83 . 1 433 78 LEU N N 117.10 . 1 434 79 ALA H H 8.58 . 1 435 79 ALA HA H 3.73 . 1 436 79 ALA HB H 1.40 . 1 437 79 ALA N N 121.70 . 1 438 80 ASN H H 9.01 . 1 439 80 ASN HA H 4.52 . 1 440 80 ASN HB2 H 2.88 . 2 441 80 ASN HB3 H 3.04 . 2 442 80 ASN ND2 N 114.70 . 1 443 80 ASN HD21 H 6.95 . 2 444 80 ASN HD22 H 7.46 . 2 445 80 ASN N N 117.90 . 1 446 81 GLU H H 7.57 . 1 447 81 GLU HA H 4.48 . 1 448 81 GLU HB2 H 2.26 . 2 449 81 GLU HB3 H 2.68 . 2 450 81 GLU HG2 H 2.48 . 1 451 81 GLU HG3 H 2.48 . 1 452 81 GLU N N 117.10 . 1 453 82 GLY H H 7.98 . 1 454 82 GLY HA2 H 3.61 . 2 455 82 GLY HA3 H 4.34 . 2 456 82 GLY N N 106.60 . 1 457 83 LYS H H 7.99 . 1 458 83 LYS HA H 4.55 . 1 459 83 LYS HB2 H 1.83 . 1 460 83 LYS HB3 H 1.83 . 1 461 83 LYS HG2 H 1.35 . 1 462 83 LYS HG3 H 1.35 . 1 463 83 LYS N N 123.40 . 1 464 84 VAL H H 7.73 . 1 465 84 VAL HA H 3.28 . 1 466 84 VAL HB H 2.10 . 1 467 84 VAL HG1 H 0.80 . 2 468 84 VAL HG2 H 0.92 . 2 469 84 VAL N N 121.60 . 1 470 85 LYS H H 8.64 . 1 471 85 LYS HA H 4.51 . 1 472 85 LYS HB2 H 1.94 . 2 473 85 LYS HB3 H 1.83 . 2 474 85 LYS N N 119.40 . 1 475 86 GLU H H 9.45 . 1 476 86 GLU HA H 4.10 . 1 477 86 GLU HB2 H 2.09 . 2 478 86 GLU HB3 H 2.13 . 2 479 86 GLU HG2 H 2.38 . 2 480 86 GLU HG3 H 2.58 . 2 481 86 GLU N N 120.90 . 1 482 87 ALA H H 8.59 . 1 483 87 ALA HA H 4.12 . 1 484 87 ALA HB H 1.52 . 1 485 87 ALA N N 124.00 . 1 486 88 GLN H H 8.77 . 1 487 88 GLN HA H 3.78 . 1 488 88 GLN HB2 H 2.54 . 1 489 88 GLN HB3 H 2.54 . 1 490 88 GLN N N 116.30 . 1 491 89 ALA H H 8.21 . 1 492 89 ALA HA H 4.23 . 1 493 89 ALA HB H 1.56 . 1 494 89 ALA N N 122.00 . 1 495 90 ALA H H 8.16 . 1 496 90 ALA HA H 4.20 . 1 497 90 ALA HB H 1.55 . 1 498 90 ALA N N 121.10 . 1 499 91 ALA H H 8.42 . 1 500 91 ALA HA H 4.00 . 1 501 91 ALA HB H 1.54 . 1 502 91 ALA N N 120.40 . 1 503 92 GLU H H 7.80 . 1 504 92 GLU HA H 4.14 . 1 505 92 GLU N N 115.40 . 1 506 93 GLN H H 7.53 . 1 507 93 GLN HA H 4.25 . 1 508 93 GLN HB2 H 2.29 . 2 509 93 GLN HB3 H 2.16 . 2 510 93 GLN HG2 H 2.51 . 2 511 93 GLN HG3 H 2.57 . 2 512 93 GLN NE2 N 116.00 . 1 513 93 GLN HE21 H 6.99 . 2 514 93 GLN HE22 H 7.61 . 2 515 93 GLN N N 116.10 . 1 516 94 LEU H H 7.84 . 1 517 94 LEU HA H 4.19 . 1 518 94 LEU HB2 H 2.01 . 1 519 94 LEU HB3 H 2.01 . 1 520 94 LEU N N 118.70 . 1 521 95 LYS H H 7.78 . 1 522 95 LYS HA H 4.00 . 1 523 95 LYS HB2 H 1.98 . 1 524 95 LYS HB3 H 1.98 . 1 525 95 LYS N N 117.40 . 1 526 96 THR H H 7.72 . 1 527 96 THR HA H 4.22 . 1 528 96 THR HB H 4.44 . 1 529 96 THR HG2 H 1.28 . 1 530 96 THR N N 112.20 . 1 531 97 THR H H 7.82 . 1 532 97 THR HA H 4.12 . 1 533 97 THR HB H 4.24 . 1 534 97 THR HG2 H 1.16 . 1 535 97 THR N N 117.40 . 1 536 98 ARG H H 8.46 . 1 537 98 ARG HA H 4.12 . 1 538 98 ARG HB2 H 1.82 . 2 539 98 ARG HB3 H 1.97 . 2 540 98 ARG N N 120.90 . 1 541 99 ASN H H 8.37 . 1 542 99 ASN HA H 4.58 . 1 543 99 ASN HB2 H 2.92 . 1 544 99 ASN HB3 H 2.92 . 1 545 99 ASN N N 117.80 . 1 546 100 ALA H H 8.07 . 1 547 100 ALA HA H 4.14 . 1 548 100 ALA HB H 1.30 . 1 549 100 ALA N N 122.10 . 1 550 101 TYR H H 8.15 . 1 551 101 TYR HA H 4.39 . 1 552 101 TYR HB2 H 2.92 . 2 553 101 TYR HB3 H 3.18 . 2 554 101 TYR HD1 H 7.16 . 1 555 101 TYR HD2 H 7.16 . 1 556 101 TYR HE1 H 6.74 . 1 557 101 TYR HE2 H 6.74 . 1 558 101 TYR N N 116.40 . 1 559 102 HIS H H 8.25 . 1 560 102 HIS HA H 4.56 . 1 561 102 HIS HB2 H 3.38 . 2 562 102 HIS HB3 H 3.42 . 2 563 102 HIS HD2 H 7.34 . 1 564 102 HIS HE1 H 8.44 . 1 565 102 HIS N N 118.60 . 1 566 103 GLN H H 8.20 . 1 567 103 GLN HA H 4.14 . 1 568 103 GLN HB2 H 2.07 . 1 569 103 GLN HB3 H 2.07 . 1 570 103 GLN HG2 H 2.37 . 1 571 103 GLN HG3 H 2.37 . 1 572 103 GLN NE2 N 114.70 . 1 573 103 GLN HE21 H 6.63 . 2 574 103 GLN HE22 H 7.44 . 2 575 103 GLN N N 117.70 . 1 576 104 LYS H H 7.84 . 1 577 104 LYS HA H 4.13 . 1 578 104 LYS HB2 H 1.49 . 1 579 104 LYS HB3 H 1.49 . 1 580 104 LYS HG2 H 1.21 . 1 581 104 LYS HG3 H 1.21 . 1 582 104 LYS HD2 H 1.58 . 1 583 104 LYS HD3 H 1.58 . 1 584 104 LYS HE2 H 2.90 . 1 585 104 LYS HE3 H 2.90 . 1 586 104 LYS N N 118.70 . 1 587 105 TYR H H 8.09 . 1 588 105 TYR HA H 4.74 . 1 589 105 TYR HB2 H 2.85 . 2 590 105 TYR HB3 H 3.28 . 2 591 105 TYR HD1 H 7.21 . 1 592 105 TYR HD2 H 7.21 . 1 593 105 TYR HE1 H 6.91 . 1 594 105 TYR HE2 H 6.91 . 1 595 105 TYR N N 117.90 . 1 596 106 ARG H H 7.59 . 1 597 106 ARG HA H 4.21 . 1 598 106 ARG HB2 H 1.61 . 2 599 106 ARG HB3 H 1.74 . 2 600 106 ARG HG2 H 1.81 . 1 601 106 ARG HG3 H 1.81 . 1 602 106 ARG NE N 89.10 . 1 603 106 ARG HD2 H 3.15 . 1 604 106 ARG HD3 H 3.15 . 1 605 106 ARG HE H 7.35 . 1 606 106 ARG N N 125.00 . 1 stop_ save_