data_19075 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N backbone chemical shift assignments of the iron-free protoporphyrin IX yeast cytochrome c peroxidase with the C-terminal His-tag ; _BMRB_accession_number 19075 _BMRB_flat_file_name bmr19075.str _Entry_type original _Submission_date 2013-03-06 _Accession_date 2013-03-06 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Volkov Alexander N. . 2 'van Nuland' Nico AJ. . 3 Vanwetswinkel Sophie . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 183 "13C chemical shifts" 609 "15N chemical shifts" 183 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-07-29 update author 'update chemical shifts' 2013-09-10 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19076 '1H, 13C, and 15N backbone chemical shift assignments of the iron-free protoporphyrin IX yeast cytochrome c peroxidase with the C-terminal His-tag' stop_ save_ ############################# # Citation for this entry # ############################# save_citation1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23832496 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vanwetswinkel Sophie . . 2 'van Nuland' Nico A.J. . 3 Volkov Alexander N. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 57 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 21 _Page_last 26 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CcP-PPIX _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CcP-PPIX $cytochrome_c_peroxidase cofactor $entity_PP9 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytochrome_c_peroxidase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common cytochrome_c_peroxidase _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 300 _Mol_residue_sequence ; MKTLVHVASVEKGRSYEDFQ KVYNAIALKLREDDEYDNYI GYGPVLVRLAWHTSGTWDKH DNTGGSYGGTYRFKKEFNDP SNAGLQNGFKFLEPIHKEFP WISSGDLFSLGGVTAVQEMQ GPKIPWRCGRVDTPEDTTPD NGRLPDADKDADYVRTFFQR LNMNDREVVALMGAHALGKT HLKNSGYEGPWGAANNVFTN EFYLNLLNEDWKLEKNDANN EQWDSKSGYMMLPTDYSLIQ DPKYLSIVKEYANDQDKFFK DFSKAFEKLLENGITFPKDA PSPFIFKTLEEQGLHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 LYS 3 3 THR 4 4 LEU 5 5 VAL 6 6 HIS 7 7 VAL 8 8 ALA 9 9 SER 10 10 VAL 11 11 GLU 12 12 LYS 13 13 GLY 14 14 ARG 15 15 SER 16 16 TYR 17 17 GLU 18 18 ASP 19 19 PHE 20 20 GLN 21 21 LYS 22 22 VAL 23 23 TYR 24 24 ASN 25 25 ALA 26 26 ILE 27 27 ALA 28 28 LEU 29 29 LYS 30 30 LEU 31 31 ARG 32 32 GLU 33 33 ASP 34 34 ASP 35 35 GLU 36 36 TYR 37 37 ASP 38 38 ASN 39 39 TYR 40 40 ILE 41 41 GLY 42 42 TYR 43 43 GLY 44 44 PRO 45 45 VAL 46 46 LEU 47 47 VAL 48 48 ARG 49 49 LEU 50 50 ALA 51 51 TRP 52 52 HIS 53 53 THR 54 54 SER 55 55 GLY 56 56 THR 57 57 TRP 58 58 ASP 59 59 LYS 60 60 HIS 61 61 ASP 62 62 ASN 63 63 THR 64 64 GLY 65 65 GLY 66 66 SER 67 67 TYR 68 68 GLY 69 69 GLY 70 70 THR 71 71 TYR 72 72 ARG 73 73 PHE 74 74 LYS 75 75 LYS 76 76 GLU 77 77 PHE 78 78 ASN 79 79 ASP 80 80 PRO 81 81 SER 82 82 ASN 83 83 ALA 84 84 GLY 85 85 LEU 86 86 GLN 87 87 ASN 88 88 GLY 89 89 PHE 90 90 LYS 91 91 PHE 92 92 LEU 93 93 GLU 94 94 PRO 95 95 ILE 96 96 HIS 97 97 LYS 98 98 GLU 99 99 PHE 100 100 PRO 101 101 TRP 102 102 ILE 103 103 SER 104 104 SER 105 105 GLY 106 106 ASP 107 107 LEU 108 108 PHE 109 109 SER 110 110 LEU 111 111 GLY 112 112 GLY 113 113 VAL 114 114 THR 115 115 ALA 116 116 VAL 117 117 GLN 118 118 GLU 119 119 MET 120 120 GLN 121 121 GLY 122 122 PRO 123 123 LYS 124 124 ILE 125 125 PRO 126 126 TRP 127 127 ARG 128 128 CYS 129 129 GLY 130 130 ARG 131 131 VAL 132 132 ASP 133 133 THR 134 134 PRO 135 135 GLU 136 136 ASP 137 137 THR 138 138 THR 139 139 PRO 140 140 ASP 141 141 ASN 142 142 GLY 143 143 ARG 144 144 LEU 145 145 PRO 146 146 ASP 147 147 ALA 148 148 ASP 149 149 LYS 150 150 ASP 151 151 ALA 152 152 ASP 153 153 TYR 154 154 VAL 155 155 ARG 156 156 THR 157 157 PHE 158 158 PHE 159 159 GLN 160 160 ARG 161 161 LEU 162 162 ASN 163 163 MET 164 164 ASN 165 165 ASP 166 166 ARG 167 167 GLU 168 168 VAL 169 169 VAL 170 170 ALA 171 171 LEU 172 172 MET 173 173 GLY 174 174 ALA 175 175 HIS 176 176 ALA 177 177 LEU 178 178 GLY 179 179 LYS 180 180 THR 181 181 HIS 182 182 LEU 183 183 LYS 184 184 ASN 185 185 SER 186 186 GLY 187 187 TYR 188 188 GLU 189 189 GLY 190 190 PRO 191 191 TRP 192 192 GLY 193 193 ALA 194 194 ALA 195 195 ASN 196 196 ASN 197 197 VAL 198 198 PHE 199 199 THR 200 200 ASN 201 201 GLU 202 202 PHE 203 203 TYR 204 204 LEU 205 205 ASN 206 206 LEU 207 207 LEU 208 208 ASN 209 209 GLU 210 210 ASP 211 211 TRP 212 212 LYS 213 213 LEU 214 214 GLU 215 215 LYS 216 216 ASN 217 217 ASP 218 218 ALA 219 219 ASN 220 220 ASN 221 221 GLU 222 222 GLN 223 223 TRP 224 224 ASP 225 225 SER 226 226 LYS 227 227 SER 228 228 GLY 229 229 TYR 230 230 MET 231 231 MET 232 232 LEU 233 233 PRO 234 234 THR 235 235 ASP 236 236 TYR 237 237 SER 238 238 LEU 239 239 ILE 240 240 GLN 241 241 ASP 242 242 PRO 243 243 LYS 244 244 TYR 245 245 LEU 246 246 SER 247 247 ILE 248 248 VAL 249 249 LYS 250 250 GLU 251 251 TYR 252 252 ALA 253 253 ASN 254 254 ASP 255 255 GLN 256 256 ASP 257 257 LYS 258 258 PHE 259 259 PHE 260 260 LYS 261 261 ASP 262 262 PHE 263 263 SER 264 264 LYS 265 265 ALA 266 266 PHE 267 267 GLU 268 268 LYS 269 269 LEU 270 270 LEU 271 271 GLU 272 272 ASN 273 273 GLY 274 274 ILE 275 275 THR 276 276 PHE 277 277 PRO 278 278 LYS 279 279 ASP 280 280 ALA 281 281 PRO 282 282 SER 283 283 PRO 284 284 PHE 285 285 ILE 286 286 PHE 287 287 LYS 288 288 THR 289 289 LEU 290 290 GLU 291 291 GLU 292 292 GLN 293 293 GLY 294 294 LEU 295 295 HIS 296 296 HIS 297 297 HIS 298 298 HIS 299 299 HIS 300 300 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 BMRB 1839 "glucose oxidase" 97.00 294 99.31 100.00 0.00e+00 BMRB 19004 cytochrome_c_peroxidase 100.00 300 100.00 100.00 0.00e+00 BMRB 19005 cytochrome_c_peroxidase 97.67 300 100.00 100.00 0.00e+00 BMRB 19076 cytochrome_c_peroxidase 97.67 300 100.00 100.00 0.00e+00 BMRB 19884 High_pH 97.67 295 99.66 99.66 0.00e+00 BMRB 25551 CcP 97.00 294 99.31 99.31 0.00e+00 PDB 1A2F "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 96.67 291 98.97 98.97 0.00e+00 PDB 1A2G "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 96.67 291 98.97 98.97 0.00e+00 PDB 1AA4 "Specificity Of Ligand Binding In A Buried Polar Cavity Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1AC4 "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (2,3,4-Trimethyl-1,3-Thiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AC8 "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (3,4,5-Trimethylthiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEB "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Methylthiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AED "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3,4- Dimethylthiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEE "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Aniline)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEF "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Aminopyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEG "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (4- Aminopyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEH "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2-Amino-4- Methylthiazole" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEJ "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (1- Vinylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEK "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Indoline)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEM "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Imidazo[1,2- A]pyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEN "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2-Amino-5- Methylthiazole" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEO "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2- Aminopyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEQ "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (2-Ethylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AES "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Imidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AET "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (1-Methylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEU "Specificity Of Ligand Binding In A Polar Cavity Of Cytochrome C Peroxidase (2-Methylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEV "Introduction Of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation Of 2- Aminothiazole" 98.00 294 98.64 98.98 0.00e+00 PDB 1BEJ "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 98.97 0.00e+00 PDB 1BEK "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 97.00 291 98.63 98.97 0.00e+00 PDB 1BEM "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 98.97 0.00e+00 PDB 1BEP "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 97.00 291 98.97 99.31 0.00e+00 PDB 1BEQ "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 99.31 0.00e+00 PDB 1BES "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 99.31 0.00e+00 PDB 1BJ9 "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 97.00 291 98.97 99.31 0.00e+00 PDB 1BVA "Manganese Binding Mutant In Cytochrome C Peroxidase" 98.00 294 98.30 98.64 0.00e+00 PDB 1CCA "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" 99.00 297 98.32 98.32 0.00e+00 PDB 1CCB "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" 99.00 297 97.98 98.32 0.00e+00 PDB 1CCC "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" 99.00 297 97.98 97.98 0.00e+00 PDB 1CCE "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" 96.67 291 98.97 98.97 0.00e+00 PDB 1CCG "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" 96.67 291 98.97 98.97 0.00e+00 PDB 1CCI "How Flexible Are Proteins? Trapping Of A Flexible Loop" 98.00 294 98.98 98.98 0.00e+00 PDB 1CCJ "Conformer Selection By Ligand Binding Observed With Protein Crystallography" 98.00 294 98.98 98.98 0.00e+00 PDB 1CCK "Altering Substrate Specificity Of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosi" 96.67 291 98.97 99.31 0.00e+00 PDB 1CCL "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 96.67 291 98.97 98.97 0.00e+00 PDB 1CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 99.31 99.31 0.00e+00 PDB 1CMP "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1CMQ "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1CMT "The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1CMU "The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase" 98.00 294 98.64 98.98 0.00e+00 PDB 1CPD "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 97.00 296 98.97 98.97 0.00e+00 PDB 1CPE "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 97.00 296 98.97 98.97 0.00e+00 PDB 1CPF "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 97.00 296 98.97 98.97 0.00e+00 PDB 1CPG "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 98.00 296 97.96 98.64 0.00e+00 PDB 1CYF "Identifying The Physiological Electron Transfer Site Of Cytochrome C Peroxidase By Structure-Based Engineering" 97.00 296 98.63 98.63 0.00e+00 PDB 1DCC "2.2 Angstrom Structure Of Oxyperoxidase: A Model For The Enzyme:peroxide Complex" 97.00 296 98.97 99.31 0.00e+00 PDB 1DJ1 "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase" 97.00 291 98.97 98.97 0.00e+00 PDB 1DJ5 "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase With N-Hydroxyguanidine Bound" 97.00 291 98.97 98.97 0.00e+00 PDB 1DS4 "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, Ph 6, 100k" 97.33 292 98.97 98.97 0.00e+00 PDB 1DSE "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, With Phosphate Bound, Ph 6, 100k" 97.33 292 98.63 98.97 0.00e+00 PDB 1DSG "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 5, Room Temperature." 97.33 292 98.97 98.97 0.00e+00 PDB 1DSO "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 6, Room Temperature." 97.33 292 98.97 98.97 0.00e+00 PDB 1DSP "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 7, Room Temperature" 97.33 292 98.97 98.97 0.00e+00 PDB 1EBE "Laue Diffraction Study On The Structure Of Cytochrome C Peroxidase Compound I" 97.00 294 99.66 100.00 0.00e+00 PDB 1JCI "Stabilization Of The Engineered Cation-Binding Loop In Cytochrome C Peroxidase (Ccp)" 97.00 294 97.94 97.94 0.00e+00 PDB 1JDR "Crystal Structure Of A Proximal Domain Potassium Binding Variant Of Cytochrome C Peroxidase" 97.00 294 98.28 98.28 0.00e+00 PDB 1KOK "Crystal Structure Of Mesopone Cytochrome C Peroxidase (Mpccp)" 97.00 294 100.00 100.00 0.00e+00 PDB 1KRJ "Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp)" 97.00 294 98.28 98.28 0.00e+00 PDB 1KXM "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" 97.33 290 98.29 98.29 0.00e+00 PDB 1KXN "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" 97.00 289 98.28 98.28 0.00e+00 PDB 1MK8 "Crystal Structure Of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link" 97.00 294 99.66 100.00 0.00e+00 PDB 1MKQ "Crystal Structure Of The Mutant Variant Of Cytochrome C Peroxidase In The 'open' Uncross-Linked Form" 97.00 294 99.66 100.00 0.00e+00 PDB 1MKR "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase (Plate Like Crystals)" 97.00 294 99.66 100.00 0.00e+00 PDB 1ML2 "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase With Zn(Ii)-(20-Oxo-Protoporphyrin Ix)" 97.00 294 99.66 100.00 0.00e+00 PDB 1RYC "Cytochrome C Peroxidase W191g From Saccharomyces Cerevisiae" 98.00 294 98.98 98.98 0.00e+00 PDB 1S6V "Structure Of A Cytochrome C Peroxidase-Cytochrome C Site Specific Cross-Link" 97.00 294 99.31 99.31 0.00e+00 PDB 1S73 "Crystal Structure Of Mesopone Cytochrome C Peroxidase (R- Isomer) [mpccp-R]" 97.00 294 100.00 100.00 0.00e+00 PDB 1SBM "Crystal Structure Of Reduced Mesopone Cytochrome C Peroxidase (R-Isomer)" 97.00 294 100.00 100.00 0.00e+00 PDB 1SDQ "Structure Of Reduced-No Adduct Of Mesopone Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 1SOG "Cyrstal Structure Of Cytochrome C Peroxidase Mutant: Ccpk2m2" 97.00 294 97.59 97.94 0.00e+00 PDB 1STQ "Cyrstal Structure Of Cytochrome C Peroxidase Mutant: Ccpk2m3" 97.00 294 97.25 97.59 0.00e+00 PDB 1U74 "Electron Transfer Complex Between Cytochrome C And Cytochrome C Peroxidase" 97.00 296 99.31 99.31 0.00e+00 PDB 1U75 "Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc- Porphyrin Substituted Cytochrome C Peroxidase" 97.00 296 99.31 99.31 0.00e+00 PDB 1Z53 "The 1.13 Angstrom Structure Of Iron-Free Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 1ZBY "High-resolution Crystal Structure Of Native (resting) Cytochrome C Peroxidase (ccp)" 97.00 294 100.00 100.00 0.00e+00 PDB 1ZBZ "High-Resolution Crystal Structure Of Compound I Intermediate Of Cytochrome C Peroxidase (Ccp)" 97.00 294 100.00 100.00 0.00e+00 PDB 2ANZ "Cytochrome C Peroxidase In Complex With 2,6-Diaminopyridine" 98.00 294 98.64 98.98 0.00e+00 PDB 2AQD "Cytochrome C Peroxidase (Ccp) In Complex With 2,5- Diaminopyridine" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS1 "Cytochrome C Peroxidase In Complex With Thiopheneamidine" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS2 "Cytochrome C Peroxidase In Complex With 2-Iminopiperidine" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS3 "Cytochrome C Peroxidase In Complex With Phenol" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS4 "Cytochrome C Peroxidase In Complex With 3-Fluorocatechol" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS6 "Cytochrome C Peroxidase In Complex With Cyclopentylamine" 98.00 294 98.98 98.98 0.00e+00 PDB 2B0Z "Crystal Structure Of The Protein-Protein Complex Between F82i Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2B10 "Crystal Structure Of The Protein-Protein Complex Between F82s Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2B11 "Crystal Structure Of The Protein-Protein Complex Between F82w Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2B12 "Crystal Structure Of The Protein-Protein Complex Between F82y Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2BCN "Solvent Isotope Effects On Interfacial Protein Electron Transfer Between Cytochrome C And Cytochrome C Peroxidase" 97.00 296 99.31 99.31 0.00e+00 PDB 2CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 98.97 99.31 0.00e+00 PDB 2CEP "Role Of Met-230 In Intramolecular Electron Transfer Between The Oxyferryl Heme And Trp 191 In Cytochrome C Peroxidase Compound " 97.00 296 98.97 99.31 0.00e+00 PDB 2CYP "Crystal Structure Of Yeast Cytochrome C Peroxidase Refined At 1.7-Angstroms Resolution" 97.00 294 100.00 100.00 0.00e+00 PDB 2EUN "Cytochrome C Peroxidase (ccp) In Complex With 2,4- Diaminopyrimidine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUO "Cytochrome C Peroxidase (ccp) In Complex With 1-methyl-1- Lambda-5-pyridin-3-yl-amine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUP "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-5- Picoline" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUQ "Cytochrome C Peroxydase (Ccp) In Complex With 3- Thienylmethylamine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUR "Cytochrome C Peroxidase (Ccp) In Complex With 4- Pyridylcarbinol" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUS "Cytochrome C Peroxidase (Ccp) In Complex With Benzylamine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUT "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-4- Picoline" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUU "Cytochrome C Peroxidase (Ccp) In Complex With 1h-Imidazol-2- Ylmethanol" 98.00 294 98.98 98.98 0.00e+00 PDB 2GB8 "Solution Structure Of The Complex Between Yeast Iso-1- Cytochrome C And Yeast Cytochrome C Peroxidase" 97.00 294 99.31 99.31 0.00e+00 PDB 2IA8 "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" 97.00 291 98.28 98.63 0.00e+00 PDB 2ICV "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" 97.00 291 98.28 98.63 0.00e+00 PDB 2JTI "Solution Structure Of The Yeast Iso-1-Cytochrome C (T12a) : Yeast Cytochrome C Peroxidase Complex" 97.00 294 99.31 99.31 0.00e+00 PDB 2N18 "Dominant Form Of The Low-affinity Complex Of Yeast Cytochrome C And Cytochrome C Peroxidase" 97.00 294 99.31 99.31 0.00e+00 PDB 2PCB "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 97.00 296 99.31 99.31 0.00e+00 PDB 2PCC "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 97.00 296 99.31 99.31 0.00e+00 PDB 2RBT "N-Methylbenzylamine In Complex With Cytochrome C Peroxidase W191g" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBU "Cytochrome C Peroxidase In Complex With Cyclopentane-Carboximidamide" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBV "Cytochrome C Peroxidase In Complex With (1-Methyl-1h-Pyrrol-2-Yl)- Methylamine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBW "Cytochrome C Peroxidase W191g In Complex With 1,2-dimethyl-1h-pyridin- 5-amine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBX "Cytochrome C Peroxidase W191g In Complex With Pyrimidine-2,4,6- Triamine." 97.33 292 98.63 98.97 0.00e+00 PDB 2RBY "1-methyl-5-imidazolecarboxaldehyde In Complex With Cytochrome C Peroxidase W191g" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBZ "Cytochrome C Peroxidase W191g In Complex 3-Methoxypyridine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RC0 "Cytochrome C Peroxidase W191g In Complex With 2-Imino-4- Methylpiperdine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RC1 "Cytochrome C Peroxidase W191g In Complex With 2,4,5-Trimethyl-3- Oxazoline" 97.33 292 98.63 98.97 0.00e+00 PDB 2RC2 "Cytochrome C Peroxidase W191g In Complex With 1-Methyl-2-Vinyl- Pyridinium" 97.33 292 98.63 98.97 0.00e+00 PDB 2V23 "Structure Of Cytochrome C Peroxidase Mutant N184r Y36a" 98.67 296 98.31 98.65 0.00e+00 PDB 2V2E "Structure Of Isoniazid (Inh) Bound To Cytochrome C Peroxidase Mutant N184r Y36a" 98.00 294 98.98 99.32 0.00e+00 PDB 2X07 "Cytochrome C Peroxidase: Engineered Ascorbate Binding Site" 97.00 293 98.63 99.31 0.00e+00 PDB 2X08 "Cytochrome C Peroxidase: Ascorbate Bound To The Engineered Ascorbate Binding Site" 97.00 293 98.63 99.31 0.00e+00 PDB 2XIL "The Structure Of Cytochrome C Peroxidase Compound I" 98.00 294 99.66 100.00 0.00e+00 PDB 2XJ5 "The Structure Of Cytochrome C Peroxidase Compound Ii" 98.00 294 100.00 100.00 0.00e+00 PDB 2XJ8 "The Structure Of Ferrous Cytochrome C Peroxidase" 98.00 294 100.00 100.00 0.00e+00 PDB 2Y5A "Cytochrome C Peroxidase (Ccp) W191g Bound To 3-Aminopyridine" 98.00 294 98.98 98.98 0.00e+00 PDB 2YCG "Structure Of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method" 97.00 294 100.00 100.00 0.00e+00 PDB 3CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 98.97 99.31 0.00e+00 PDB 3CCX "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 3E2O "Crystal Structure Of Cytochrome C Peroxidase, N184r Mutant" 97.00 294 99.31 99.31 0.00e+00 PDB 3EXB "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Pathway Excised In A Complex With A Peptide Wire" 99.00 295 97.31 97.31 0.00e+00 PDB 3M23 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M25 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M26 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M27 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M28 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M29 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2A "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2B "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2C "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2D "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2E "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2F "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2G "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2H "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2I "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3R98 "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" 97.00 293 100.00 100.00 0.00e+00 PDB 3R99 "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" 97.00 293 100.00 100.00 0.00e+00 PDB 4A6Z "Cytochrome C Peroxidase With Bound Guaiacol" 98.67 296 98.31 98.65 0.00e+00 PDB 4A71 "Cytochrome C Peroxidase In Complex With Phenol" 98.67 296 98.65 98.65 0.00e+00 PDB 4A78 "Cytochrome C Peroxidase M119w In Complex With Guiacol" 98.67 296 98.65 98.65 0.00e+00 PDB 4A7M "Cytochrome C Peroxidase S81w Mutant" 98.67 296 98.99 98.99 0.00e+00 PDB 4CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 98.97 99.31 0.00e+00 PDB 4CCX "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 4CVI "Neutron Structure Of Ferric Cytochrome C Peroxidase - Deuterium Exchanged At Room Temperature" 98.00 294 99.66 99.66 0.00e+00 PDB 4CVJ "Neutron Structure Of Compound I Intermediate Of Cytochrome C Peroxidase - Deuterium Exchanged 100 K" 98.00 294 100.00 100.00 0.00e+00 PDB 4JB4 "Expression, Purification, Characterization, And Solution Nmr Study Of Highly Deuterated Yeast Cytochrome C Peroxidase With Enha" 100.00 300 100.00 100.00 0.00e+00 PDB 4JM5 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-amino-5-methylthiazole" 97.00 289 98.28 98.28 0.00e+00 PDB 4JM6 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,4-diaminopyrimidine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JM8 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,6-diaminopyridine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JM9 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-amino-1-methylpyridinium" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMA "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-fluorocatechol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMB "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 5,6,7,8-tetrahydrothieno[2,3-b]quinolin-4-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMS "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-5-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMT "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridin-6-ylmethanol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMV "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-6-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMW "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Phenol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMZ "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With N-methyl-1h-benzimidazol-2-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JN0 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridine-6-carbaldehyde" 97.00 289 98.28 98.28 0.00e+00 PDB 4JPL "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-azaindole" 97.00 289 98.28 98.28 0.00e+00 PDB 4JPT "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Quinazoline-2,4-diamine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JPU "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Benzamidine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQJ "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinoline" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQK "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-(2-aminopyridin-1-ium-1-yl)ethanol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQM "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinazoline" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQN "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-hydroxybenzaldehyde" 97.00 289 98.28 98.28 0.00e+00 PDB 4NFG "K13r Mutant Of Horse Cytochrome C And Yeast Cytochrome C Peroxidase Complex" 98.00 294 99.66 99.66 0.00e+00 PDB 4NVA "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVB "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVC "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVD "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVE "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVF "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVG "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVH "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVI "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVJ "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVK "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVL "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVM "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVN "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVO "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4OQ7 "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4P4Q "Complex Of Yeast Cytochrome C Peroxidase (w191f) With Iso-1 Cytochrome C" 97.00 294 98.97 99.31 0.00e+00 PDB 4XV4 "Ccp Gateless Cavity" 97.00 289 98.28 98.28 0.00e+00 PDB 4XV5 "Ccp Gateless Cavity" 98.00 292 98.30 98.30 0.00e+00 PDB 4XV6 "Ccp Gateless Cavity" 97.00 289 98.28 98.28 0.00e+00 PDB 4XV7 "Ccp Gateless Cavity" 98.00 292 98.30 98.30 0.00e+00 PDB 4XV8 "Ccp Gateless Cavity" 98.00 292 98.30 98.30 0.00e+00 PDB 4XVA "Crystal Structure Of Wild Type Cytochrome C Peroxidase" 97.00 293 100.00 100.00 0.00e+00 PDB 5CCP "Histidine 52 Is A Critical Residue For Rapid Formation Of Cytochrome C Peroxidase Compound I" 97.00 296 98.97 98.97 0.00e+00 PDB 6CCP "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" 97.00 296 98.97 99.31 0.00e+00 PDB 7CCP "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" 97.00 296 98.97 98.97 0.00e+00 DBJ GAA24787 "K7_Ccp1p [Saccharomyces cerevisiae Kyokai no. 7]" 97.00 363 100.00 100.00 0.00e+00 EMBL CAA44288 "Cytochrome c peroxidase [Saccharomyces cerevisiae]" 97.00 361 100.00 100.00 0.00e+00 EMBL CAA82145 "CCP1 [Saccharomyces cerevisiae]" 97.00 361 100.00 100.00 0.00e+00 EMBL CAY81144 "Ccp1p [Saccharomyces cerevisiae EC1118]" 97.00 362 99.66 99.66 0.00e+00 GB AAA88709 "cytochrome c peroxidase [Saccharomyces cerevisiae]" 97.00 362 99.31 99.31 0.00e+00 GB AAS56247 "YKR066C [Saccharomyces cerevisiae]" 97.00 361 99.66 100.00 0.00e+00 GB AHY76301 "Ccp1p [Saccharomyces cerevisiae YJM993]" 97.00 363 99.31 99.31 0.00e+00 GB AJP40095 "Ccp1p [Saccharomyces cerevisiae YJM1078]" 97.00 362 99.66 99.66 0.00e+00 GB AJS30293 "Ccp1p [Saccharomyces cerevisiae YJM189]" 97.00 362 99.31 99.31 0.00e+00 REF NP_012992 "Ccp1p [Saccharomyces cerevisiae S288c]" 97.00 361 100.00 100.00 0.00e+00 SP P00431 "RecName: Full=Cytochrome c peroxidase, mitochondrial; Short=CCP; Flags: Precursor" 97.00 361 100.00 100.00 0.00e+00 TPG DAA09217 "TPA: Ccp1p [Saccharomyces cerevisiae S288c]" 97.00 361 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_PP9 _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common 'PROTOPORPHYRIN IX' _BMRB_code PP9 _PDB_code PP9 _Molecular_mass 562.658 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CHA CHA C . 0 . ? CHB CHB C . 0 . ? CHC CHC C . 0 . ? CHD CHD C . 0 . ? NA NA N . 0 . ? C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? CMA CMA C . 0 . ? CAA CAA C . 0 . ? CBA CBA C . 0 . ? CGA CGA C . 0 . ? O1A O1A O . 0 . ? O2A O2A O . 0 . ? NB NB N . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? CMB CMB C . 0 . ? CAB CAB C . 0 . ? CBB CBB C . 0 . ? NC NC N . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? CMC CMC C . 0 . ? CAC CAC C . 0 . ? CBC CBC C . 0 . ? ND ND N . 0 . ? C1D C1D C . 0 . ? C2D C2D C . 0 . ? C3D C3D C . 0 . ? C4D C4D C . 0 . ? CMD CMD C . 0 . ? CAD CAD C . 0 . ? CBD CBD C . 0 . ? CGD CGD C . 0 . ? O1D O1D O . 0 . ? O2D O2D O . 0 . ? HHA HHA H . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HNA HNA H . 0 . ? HMA1 HMA1 H . 0 . ? HMA2 HMA2 H . 0 . ? HMA3 HMA3 H . 0 . ? HAA1 HAA1 H . 0 . ? HAA2 HAA2 H . 0 . ? HBA1 HBA1 H . 0 . ? HBA2 HBA2 H . 0 . ? H2A H2A H . 0 . ? HMB1 HMB1 H . 0 . ? HMB2 HMB2 H . 0 . ? HMB3 HMB3 H . 0 . ? HAB HAB H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HNC HNC H . 0 . ? HMC1 HMC1 H . 0 . ? HMC2 HMC2 H . 0 . ? HMC3 HMC3 H . 0 . ? HAC HAC H . 0 . ? HBC1 HBC1 H . 0 . ? HBC2 HBC2 H . 0 . ? HMD1 HMD1 H . 0 . ? HMD2 HMD2 H . 0 . ? HMD3 HMD3 H . 0 . ? HAD1 HAD1 H . 0 . ? HAD2 HAD2 H . 0 . ? HBD1 HBD1 H . 0 . ? HBD2 HBD2 H . 0 . ? H2D H2D H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING CHA C1A ? ? DOUB CHA C4D ? ? SING CHA HHA ? ? SING CHB C4A ? ? DOUB CHB C1B ? ? SING CHB HHB ? ? SING CHC C4B ? ? DOUB CHC C1C ? ? SING CHC HHC ? ? DOUB CHD C4C ? ? SING CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING NA HNA ? ? DOUB C1A C2A ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING CMA HMA1 ? ? SING CMA HMA2 ? ? SING CMA HMA3 ? ? SING CAA CBA ? ? SING CAA HAA1 ? ? SING CAA HAA2 ? ? SING CBA CGA ? ? SING CBA HBA1 ? ? SING CBA HBA2 ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING O2A H2A ? ? SING NB C1B ? ? DOUB NB C4B ? ? SING C1B C2B ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? SING CMB HMB1 ? ? SING CMB HMB2 ? ? SING CMB HMB3 ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING NC C1C ? ? SING NC C4C ? ? SING NC HNC ? ? SING C1C C2C ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING CMC HMC1 ? ? SING CMC HMC2 ? ? SING CMC HMC3 ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC1 ? ? SING CBC HBC2 ? ? DOUB ND C1D ? ? SING ND C4D ? ? SING C1D C2D ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING CMD HMD1 ? ? SING CMD HMD2 ? ? SING CMD HMD3 ? ? SING CAD CBD ? ? SING CAD HAD1 ? ? SING CAD HAD2 ? ? SING CBD CGD ? ? SING CBD HBD1 ? ? SING CBD HBD2 ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2D H2D ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cytochrome_c_peroxidase 'baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae 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 $cytochrome_c_peroxidase 'recombinant technology' . Escherichia coli . pET24a(+) stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $cytochrome_c_peroxidase 1.2 mM '[U-13C; U-15N; U-2H]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % 'natural abundance' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Uniform NMR System' _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 115 . mM pH 6 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . 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 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCA' '3D HNCO' '3D HN(CA)CB' '3D HN(CO)CA' '3D HN(CA)CO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name CcP-PPIX _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 LYS C C 175.85 0.2 1 2 2 2 LYS CA C 55.96 0.2 1 3 2 2 LYS CB C 32.07 0.2 1 4 3 3 THR H H 8.16 0.04 1 5 3 3 THR C C 173.93 0.2 1 6 3 3 THR CA C 61.47 0.2 1 7 3 3 THR CB C 69.34 0.2 1 8 3 3 THR N N 118.40 0.2 1 9 4 4 LEU H H 8.18 0.04 1 10 4 4 LEU C C 176.04 0.2 1 11 4 4 LEU CA C 54.55 0.2 1 12 4 4 LEU CB C 41.43 0.2 1 13 4 4 LEU N N 126.81 0.2 1 14 5 5 VAL H H 8.14 0.04 1 15 5 5 VAL C C 174.56 0.2 1 16 5 5 VAL CA C 60.78 0.2 1 17 5 5 VAL CB C 32.97 0.2 1 18 5 5 VAL N N 124.03 0.2 1 19 6 6 HIS H H 8.70 0.04 1 20 6 6 HIS C C 172.36 0.2 1 21 6 6 HIS CA C 51.71 0.2 1 22 6 6 HIS CB C 26.98 0.2 1 23 6 6 HIS N N 125.11 0.2 1 24 7 7 VAL H H 8.84 0.04 1 25 7 7 VAL C C 177.94 0.2 1 26 7 7 VAL CA C 61.41 0.2 1 27 7 7 VAL CB C 31.20 0.2 1 28 7 7 VAL N N 124.96 0.2 1 29 8 8 ALA H H 8.53 0.04 1 30 8 8 ALA C C 177.12 0.2 1 31 8 8 ALA CA C 52.34 0.2 1 32 8 8 ALA CB C 19.57 0.2 1 33 8 8 ALA N N 135.63 0.2 1 34 9 9 SER H H 9.52 0.04 1 35 9 9 SER CB C 63.58 0.2 1 36 9 9 SER N N 120.95 0.2 1 37 11 11 GLU C C 176.76 0.2 1 38 11 11 GLU CA C 59.04 0.2 1 39 12 12 LYS H H 8.17 0.04 1 40 12 12 LYS C C 178.81 0.2 1 41 12 12 LYS CA C 58.18 0.2 1 42 12 12 LYS CB C 31.38 0.2 1 43 12 12 LYS N N 123.65 0.2 1 44 13 13 GLY H H 8.87 0.04 1 45 13 13 GLY C C 174.07 0.2 1 46 13 13 GLY CA C 45.12 0.2 1 47 13 13 GLY N N 113.35 0.2 1 48 14 14 ARG H H 7.69 0.04 1 49 14 14 ARG C C 175.54 0.2 1 50 14 14 ARG CA C 52.68 0.2 1 51 14 14 ARG CB C 28.96 0.2 1 52 14 14 ARG N N 119.02 0.2 1 53 15 15 SER H H 9.39 0.04 1 54 15 15 SER C C 174.27 0.2 1 55 15 15 SER CA C 56.43 0.2 1 56 15 15 SER CB C 65.88 0.2 1 57 15 15 SER N N 118.69 0.2 1 58 16 16 TYR H H 8.94 0.04 1 59 16 16 TYR C C 176.12 0.2 1 60 16 16 TYR CA C 61.40 0.2 1 61 16 16 TYR CB C 37.83 0.2 1 62 16 16 TYR N N 122.19 0.2 1 63 17 17 GLU H H 8.83 0.04 1 64 17 17 GLU C C 179.04 0.2 1 65 17 17 GLU CA C 59.42 0.2 1 66 17 17 GLU CB C 28.15 0.2 1 67 17 17 GLU N N 117.12 0.2 1 68 18 18 ASP H H 7.55 0.04 1 69 18 18 ASP C C 177.96 0.2 1 70 18 18 ASP CA C 57.46 0.2 1 71 18 18 ASP CB C 41.32 0.2 1 72 18 18 ASP N N 117.83 0.2 1 73 19 19 PHE H H 7.42 0.04 1 74 19 19 PHE C C 177.37 0.2 1 75 19 19 PHE CA C 62.24 0.2 1 76 19 19 PHE CB C 38.75 0.2 1 77 19 19 PHE N N 116.07 0.2 1 78 20 20 GLN H H 8.79 0.04 1 79 20 20 GLN C C 177.80 0.2 1 80 20 20 GLN CA C 57.29 0.2 1 81 20 20 GLN CB C 26.98 0.2 1 82 20 20 GLN N N 121.70 0.2 1 83 21 21 LYS H H 7.38 0.04 1 84 21 21 LYS C C 178.91 0.2 1 85 21 21 LYS CA C 59.74 0.2 1 86 21 21 LYS CB C 31.25 0.2 1 87 21 21 LYS N N 119.65 0.2 1 88 22 22 VAL H H 6.81 0.04 1 89 22 22 VAL CA C 65.44 0.2 1 90 22 22 VAL CB C 29.04 0.2 1 91 22 22 VAL N N 122.05 0.2 1 92 24 24 ASN C C 176.80 0.2 1 93 24 24 ASN CA C 54.95 0.2 1 94 25 25 ALA H H 7.84 0.04 1 95 25 25 ALA C C 181.17 0.2 1 96 25 25 ALA CA C 54.91 0.2 1 97 25 25 ALA CB C 18.37 0.2 1 98 25 25 ALA N N 123.00 0.2 1 99 26 26 ILE C C 176.88 0.2 1 100 26 26 ILE CA C 65.00 0.2 1 101 27 27 ALA H H 9.00 0.04 1 102 27 27 ALA CA C 54.78 0.2 1 103 27 27 ALA CB C 18.37 0.2 1 104 27 27 ALA N N 122.02 0.2 1 105 28 28 LEU C C 179.72 0.2 1 106 28 28 LEU CA C 57.27 0.2 1 107 29 29 LYS H H 7.57 0.04 1 108 29 29 LYS CB C 30.79 0.2 1 109 29 29 LYS N N 123.59 0.2 1 110 30 30 LEU C C 180.30 0.2 1 111 30 30 LEU CA C 56.90 0.2 1 112 31 31 ARG H H 7.22 0.04 1 113 31 31 ARG C C 177.08 0.2 1 114 31 31 ARG CA C 57.28 0.2 1 115 31 31 ARG CB C 29.75 0.2 1 116 31 31 ARG N N 116.52 0.2 1 117 35 35 GLU C C 177.04 0.2 1 118 35 35 GLU CA C 56.55 0.2 1 119 36 36 TYR H H 6.72 0.04 1 120 36 36 TYR C C 173.86 0.2 1 121 36 36 TYR CA C 58.34 0.2 1 122 36 36 TYR CB C 40.28 0.2 1 123 36 36 TYR N N 121.40 0.2 1 124 40 40 ILE C C 179.01 0.2 1 125 41 41 GLY H H 8.48 0.04 1 126 41 41 GLY C C 173.34 0.2 1 127 41 41 GLY CA C 44.19 0.2 1 128 41 41 GLY N N 107.28 0.2 1 129 42 42 TYR H H 9.42 0.04 1 130 42 42 TYR C C 175.05 0.2 1 131 42 42 TYR CA C 59.85 0.2 1 132 42 42 TYR CB C 38.48 0.2 1 133 42 42 TYR N N 115.86 0.2 1 134 43 43 GLY H H 9.30 0.04 1 135 43 43 GLY C C 174.02 0.2 1 136 43 43 GLY CA C 48.25 0.2 1 137 43 43 GLY N N 108.92 0.2 1 138 55 55 GLY C C 169.87 0.2 1 139 55 55 GLY CA C 45.84 0.2 1 140 56 56 THR H H 6.33 0.04 1 141 56 56 THR C C 173.86 0.2 1 142 56 56 THR CA C 60.18 0.2 1 143 56 56 THR CB C 69.83 0.2 1 144 56 56 THR N N 103.60 0.2 1 145 57 57 TRP H H 7.05 0.04 1 146 57 57 TRP C C 173.84 0.2 1 147 57 57 TRP CA C 58.84 0.2 1 148 57 57 TRP CB C 27.63 0.2 1 149 57 57 TRP N N 122.06 0.2 1 150 58 58 ASP H H 7.47 0.04 1 151 58 58 ASP C C 175.07 0.2 1 152 58 58 ASP CA C 52.07 0.2 1 153 58 58 ASP CB C 42.16 0.2 1 154 58 58 ASP N N 125.90 0.2 1 155 59 59 LYS H H 6.80 0.04 1 156 59 59 LYS C C 177.23 0.2 1 157 59 59 LYS CA C 56.47 0.2 1 158 59 59 LYS CB C 31.31 0.2 1 159 59 59 LYS N N 122.77 0.2 1 160 60 60 HIS H H 8.83 0.04 1 161 60 60 HIS C C 175.49 0.2 1 162 60 60 HIS CA C 58.55 0.2 1 163 60 60 HIS CB C 27.38 0.2 1 164 60 60 HIS N N 119.25 0.2 1 165 61 61 ASP H H 6.84 0.04 1 166 61 61 ASP C C 176.05 0.2 1 167 61 61 ASP CA C 51.88 0.2 1 168 61 61 ASP CB C 40.97 0.2 1 169 61 61 ASP N N 114.32 0.2 1 170 62 62 ASN H H 8.28 0.04 1 171 62 62 ASN C C 174.60 0.2 1 172 62 62 ASN CA C 53.04 0.2 1 173 62 62 ASN CB C 38.20 0.2 1 174 62 62 ASN N N 117.67 0.2 1 175 63 63 THR H H 7.66 0.04 1 176 63 63 THR C C 175.76 0.2 1 177 63 63 THR CA C 60.50 0.2 1 178 63 63 THR CB C 71.69 0.2 1 179 63 63 THR N N 108.64 0.2 1 180 64 64 GLY H H 8.56 0.04 1 181 64 64 GLY C C 176.17 0.2 1 182 64 64 GLY CA C 44.51 0.2 1 183 64 64 GLY N N 105.64 0.2 1 184 65 65 GLY H H 8.19 0.04 1 185 65 65 GLY C C 173.26 0.2 1 186 65 65 GLY CA C 43.99 0.2 1 187 65 65 GLY N N 108.00 0.2 1 188 66 66 SER H H 8.72 0.04 1 189 66 66 SER C C 177.70 0.2 1 190 66 66 SER CA C 59.57 0.2 1 191 66 66 SER CB C 63.75 0.2 1 192 66 66 SER N N 112.03 0.2 1 193 67 67 TYR H H 8.47 0.04 1 194 67 67 TYR C C 175.50 0.2 1 195 67 67 TYR CA C 62.55 0.2 1 196 67 67 TYR CB C 37.47 0.2 1 197 67 67 TYR N N 122.55 0.2 1 198 68 68 GLY H H 8.50 0.04 1 199 68 68 GLY C C 176.10 0.2 1 200 68 68 GLY CA C 46.17 0.2 1 201 68 68 GLY N N 99.21 0.2 1 202 69 69 GLY H H 7.88 0.04 1 203 69 69 GLY C C 177.83 0.2 1 204 69 69 GLY CA C 47.06 0.2 1 205 69 69 GLY N N 110.04 0.2 1 206 70 70 THR H H 7.70 0.04 1 207 70 70 THR C C 174.45 0.2 1 208 70 70 THR CA C 64.23 0.2 1 209 70 70 THR CB C 67.09 0.2 1 210 70 70 THR N N 112.38 0.2 1 211 71 71 TYR C C 171.26 0.2 1 212 71 71 TYR CB C 38.82 0.2 1 213 72 72 ARG H H 6.82 0.04 1 214 72 72 ARG C C 176.24 0.2 1 215 72 72 ARG CA C 55.82 0.2 1 216 72 72 ARG CB C 28.59 0.2 1 217 72 72 ARG N N 108.40 0.2 1 218 73 73 PHE H H 8.26 0.04 1 219 73 73 PHE C C 176.52 0.2 1 220 73 73 PHE CA C 57.23 0.2 1 221 73 73 PHE CB C 37.97 0.2 1 222 73 73 PHE N N 123.59 0.2 1 223 74 74 LYS H H 8.79 0.04 1 224 74 74 LYS C C 177.06 0.2 1 225 74 74 LYS CA C 58.79 0.2 1 226 74 74 LYS CB C 31.60 0.2 1 227 74 74 LYS N N 122.32 0.2 1 228 75 75 LYS H H 8.58 0.04 1 229 75 75 LYS C C 177.60 0.2 1 230 75 75 LYS CA C 59.65 0.2 1 231 75 75 LYS CB C 31.61 0.2 1 232 75 75 LYS N N 117.70 0.2 1 233 76 76 GLU H H 6.64 0.04 1 234 76 76 GLU CA C 57.55 0.2 1 235 76 76 GLU CB C 29.92 0.2 1 236 76 76 GLU N N 119.07 0.2 1 237 77 77 PHE C C 177.83 0.2 1 238 77 77 PHE CA C 60.44 0.2 1 239 78 78 ASN H H 7.82 0.04 1 240 78 78 ASN C C 174.49 0.2 1 241 78 78 ASN CA C 52.41 0.2 1 242 78 78 ASN CB C 37.90 0.2 1 243 78 78 ASN N N 112.60 0.2 1 244 79 79 ASP H H 7.27 0.04 1 245 79 79 ASP C C 177.80 0.2 1 246 79 79 ASP CA C 52.58 0.2 1 247 79 79 ASP CB C 41.65 0.2 1 248 79 79 ASP N N 124.69 0.2 1 249 80 80 PRO C C 179.99 0.2 1 250 80 80 PRO CA C 65.20 0.2 1 251 80 80 PRO CB C 31.04 0.2 1 252 81 81 SER H H 8.55 0.04 1 253 81 81 SER CA C 61.29 0.2 1 254 81 81 SER CB C 62.32 0.2 1 255 81 81 SER N N 115.27 0.2 1 256 82 82 ASN C C 175.92 0.2 1 257 82 82 ASN CA C 51.19 0.2 1 258 82 82 ASN CB C 37.56 0.2 1 259 83 83 ALA H H 7.12 0.04 1 260 83 83 ALA C C 178.27 0.2 1 261 83 83 ALA CA C 54.80 0.2 1 262 83 83 ALA CB C 17.59 0.2 1 263 83 83 ALA N N 127.43 0.2 1 264 84 84 GLY H H 8.62 0.04 1 265 84 84 GLY CA C 44.76 0.2 1 266 84 84 GLY N N 115.12 0.2 1 267 85 85 LEU C C 178.28 0.2 1 268 85 85 LEU CA C 56.25 0.2 1 269 85 85 LEU CB C 38.96 0.2 1 270 86 86 GLN H H 9.64 0.04 1 271 86 86 GLN CA C 58.75 0.2 1 272 86 86 GLN CB C 25.87 0.2 1 273 86 86 GLN N N 122.36 0.2 1 274 90 90 LYS C C 178.95 0.2 1 275 90 90 LYS CA C 58.29 0.2 1 276 90 90 LYS CB C 31.16 0.2 1 277 91 91 PHE H H 7.10 0.04 1 278 91 91 PHE C C 175.76 0.2 1 279 91 91 PHE CA C 60.50 0.2 1 280 91 91 PHE CB C 37.77 0.2 1 281 91 91 PHE N N 121.14 0.2 1 282 92 92 LEU H H 7.18 0.04 1 283 92 92 LEU C C 178.57 0.2 1 284 92 92 LEU CA C 55.01 0.2 1 285 92 92 LEU CB C 41.85 0.2 1 286 92 92 LEU N N 114.18 0.2 1 287 93 93 GLU H H 7.71 0.04 1 288 93 93 GLU C C 175.83 0.2 1 289 93 93 GLU CA C 61.24 0.2 1 290 93 93 GLU CB C 26.59 0.2 1 291 93 93 GLU N N 123.16 0.2 1 292 94 94 PRO C C 179.87 0.2 1 293 95 95 ILE H H 6.63 0.04 1 294 95 95 ILE CA C 63.06 0.2 1 295 95 95 ILE CB C 35.50 0.2 1 296 95 95 ILE N N 119.21 0.2 1 297 96 96 HIS C C 177.55 0.2 1 298 96 96 HIS CB C 28.78 0.2 1 299 97 97 LYS H H 7.64 0.04 1 300 97 97 LYS C C 177.91 0.2 1 301 97 97 LYS CA C 57.98 0.2 1 302 97 97 LYS CB C 31.12 0.2 1 303 97 97 LYS N N 115.44 0.2 1 304 98 98 GLU H H 7.08 0.04 1 305 98 98 GLU C C 175.74 0.2 1 306 98 98 GLU CA C 57.21 0.2 1 307 98 98 GLU CB C 28.54 0.2 1 308 98 98 GLU N N 119.48 0.2 1 309 99 99 PHE H H 7.38 0.04 1 310 99 99 PHE CA C 53.63 0.2 1 311 99 99 PHE CB C 37.02 0.2 1 312 99 99 PHE N N 116.86 0.2 1 313 103 103 SER C C 175.00 0.2 1 314 104 104 SER H H 10.30 0.04 1 315 104 104 SER N N 120.90 0.2 1 316 106 106 ASP C C 176.13 0.2 1 317 106 106 ASP CA C 57.84 0.2 1 318 106 106 ASP CB C 38.26 0.2 1 319 107 107 LEU H H 7.90 0.04 1 320 107 107 LEU C C 178.16 0.2 1 321 107 107 LEU CA C 57.97 0.2 1 322 107 107 LEU CB C 40.01 0.2 1 323 107 107 LEU N N 122.21 0.2 1 324 108 108 PHE H H 8.75 0.04 1 325 108 108 PHE C C 179.47 0.2 1 326 108 108 PHE CA C 57.13 0.2 1 327 108 108 PHE CB C 37.14 0.2 1 328 108 108 PHE N N 116.61 0.2 1 329 109 109 SER C C 176.06 0.2 1 330 109 109 SER CA C 61.31 0.2 1 331 109 109 SER CB C 63.02 0.2 1 332 110 110 LEU H H 8.69 0.04 1 333 110 110 LEU C C 180.85 0.2 1 334 110 110 LEU CA C 56.93 0.2 1 335 110 110 LEU CB C 40.41 0.2 1 336 110 110 LEU N N 127.62 0.2 1 337 111 111 GLY H H 8.79 0.04 1 338 111 111 GLY C C 174.67 0.2 1 339 111 111 GLY CA C 47.65 0.2 1 340 111 111 GLY N N 109.38 0.2 1 341 112 112 GLY H H 7.15 0.04 1 342 112 112 GLY C C 174.39 0.2 1 343 112 112 GLY CA C 46.99 0.2 1 344 112 112 GLY N N 105.37 0.2 1 345 113 113 VAL H H 7.56 0.04 1 346 113 113 VAL CA C 67.30 0.2 1 347 113 113 VAL CB C 31.76 0.2 1 348 113 113 VAL N N 122.13 0.2 1 349 114 114 THR C C 175.86 0.2 1 350 115 115 ALA H H 7.74 0.04 1 351 115 115 ALA CA C 55.63 0.2 1 352 115 115 ALA CB C 18.94 0.2 1 353 115 115 ALA N N 121.15 0.2 1 354 118 118 GLU C C 178.16 0.2 1 355 118 118 GLU CB C 28.32 0.2 1 356 119 119 MET H H 7.58 0.04 1 357 119 119 MET C C 173.56 0.2 1 358 119 119 MET CA C 56.14 0.2 1 359 119 119 MET CB C 30.75 0.2 1 360 119 119 MET N N 120.11 0.2 1 361 120 120 GLN H H 7.48 0.04 1 362 120 120 GLN C C 175.96 0.2 1 363 120 120 GLN CB C 24.47 0.2 1 364 120 120 GLN N N 108.99 0.2 1 365 121 121 GLY H H 8.08 0.04 1 366 121 121 GLY CA C 44.35 0.2 1 367 121 121 GLY N N 105.77 0.2 1 368 125 125 PRO C C 176.02 0.2 1 369 125 125 PRO CA C 61.84 0.2 1 370 125 125 PRO CB C 29.96 0.2 1 371 126 126 TRP H H 9.09 0.04 1 372 126 126 TRP C C 173.38 0.2 1 373 126 126 TRP CA C 56.55 0.2 1 374 126 126 TRP CB C 31.55 0.2 1 375 126 126 TRP N N 124.96 0.2 1 376 127 127 ARG C C 172.42 0.2 1 377 127 127 ARG CA C 52.76 0.2 1 378 127 127 ARG CB C 33.08 0.2 1 379 128 128 CYS H H 6.31 0.04 1 380 128 128 CYS C C 173.28 0.2 1 381 128 128 CYS CA C 53.52 0.2 1 382 128 128 CYS CB C 31.70 0.2 1 383 128 128 CYS N N 113.81 0.2 1 384 130 130 ARG H H 8.67 0.04 1 385 130 130 ARG CA C 57.57 0.2 1 386 130 130 ARG CB C 24.89 0.2 1 387 130 130 ARG N N 123.71 0.2 1 388 131 131 VAL C C 172.28 0.2 1 389 131 131 VAL CA C 60.47 0.2 1 390 132 132 ASP H H 8.16 0.04 1 391 132 132 ASP C C 177.72 0.2 1 392 132 132 ASP CA C 54.56 0.2 1 393 132 132 ASP CB C 38.25 0.2 1 394 132 132 ASP N N 124.23 0.2 1 395 133 133 THR H H 8.63 0.04 1 396 133 133 THR C C 174.07 0.2 1 397 133 133 THR CA C 59.25 0.2 1 398 133 133 THR CB C 67.68 0.2 1 399 133 133 THR N N 117.38 0.2 1 400 134 134 PRO C C 177.69 0.2 1 401 134 134 PRO CA C 62.69 0.2 1 402 134 134 PRO CB C 31.98 0.2 1 403 135 135 GLU H H 8.68 0.04 1 404 135 135 GLU C C 178.87 0.2 1 405 135 135 GLU CA C 59.69 0.2 1 406 135 135 GLU CB C 28.28 0.2 1 407 135 135 GLU N N 124.40 0.2 1 408 136 136 ASP H H 8.49 0.04 1 409 136 136 ASP C C 176.57 0.2 1 410 136 136 ASP CA C 55.16 0.2 1 411 136 136 ASP CB C 38.62 0.2 1 412 136 136 ASP N N 117.92 0.2 1 413 137 137 THR H H 8.00 0.04 1 414 137 137 THR C C 174.55 0.2 1 415 137 137 THR CA C 61.75 0.2 1 416 137 137 THR CB C 69.61 0.2 1 417 137 137 THR N N 110.64 0.2 1 418 138 138 THR H H 7.55 0.04 1 419 138 138 THR C C 172.84 0.2 1 420 138 138 THR CA C 61.82 0.2 1 421 138 138 THR CB C 68.80 0.2 1 422 138 138 THR N N 123.91 0.2 1 423 139 139 PRO C C 176.09 0.2 1 424 139 139 PRO CA C 61.98 0.2 1 425 140 140 ASP H H 8.27 0.04 1 426 140 140 ASP C C 175.92 0.2 1 427 140 140 ASP CA C 54.17 0.2 1 428 140 140 ASP CB C 40.15 0.2 1 429 140 140 ASP N N 120.06 0.2 1 430 141 141 ASN H H 8.64 0.04 1 431 141 141 ASN C C 175.04 0.2 1 432 141 141 ASN CA C 53.28 0.2 1 433 141 141 ASN CB C 38.80 0.2 1 434 141 141 ASN N N 117.40 0.2 1 435 142 142 GLY C C 176.14 0.2 1 436 143 143 ARG H H 8.98 0.04 1 437 143 143 ARG CA C 56.32 0.2 1 438 143 143 ARG CB C 29.95 0.2 1 439 143 143 ARG N N 120.30 0.2 1 440 148 148 ASP C C 176.43 0.2 1 441 148 148 ASP CA C 52.85 0.2 1 442 148 148 ASP CB C 39.20 0.2 1 443 149 149 LYS H H 6.46 0.04 1 444 149 149 LYS C C 172.92 0.2 1 445 149 149 LYS CA C 53.70 0.2 1 446 149 149 LYS CB C 35.53 0.2 1 447 149 149 LYS N N 118.79 0.2 1 448 150 150 ASP H H 7.22 0.04 1 449 150 150 ASP C C 176.64 0.2 1 450 150 150 ASP CA C 51.43 0.2 1 451 150 150 ASP CB C 42.50 0.2 1 452 150 150 ASP N N 116.07 0.2 1 453 151 151 ALA H H 8.66 0.04 1 454 151 151 ALA C C 179.37 0.2 1 455 151 151 ALA CA C 55.24 0.2 1 456 151 151 ALA CB C 18.94 0.2 1 457 151 151 ALA N N 119.97 0.2 1 458 152 152 ASP H H 7.90 0.04 1 459 152 152 ASP C C 179.29 0.2 1 460 152 152 ASP CA C 56.93 0.2 1 461 152 152 ASP CB C 40.08 0.2 1 462 152 152 ASP N N 115.66 0.2 1 463 153 153 TYR H H 8.03 0.04 1 464 153 153 TYR C C 177.47 0.2 1 465 153 153 TYR CA C 61.47 0.2 1 466 153 153 TYR CB C 37.63 0.2 1 467 153 153 TYR N N 122.10 0.2 1 468 154 154 VAL H H 8.52 0.04 1 469 154 154 VAL C C 177.50 0.2 1 470 154 154 VAL CA C 67.96 0.2 1 471 154 154 VAL CB C 31.36 0.2 1 472 154 154 VAL N N 123.22 0.2 1 473 155 155 ARG H H 9.00 0.04 1 474 155 155 ARG C C 180.64 0.2 1 475 155 155 ARG CA C 60.02 0.2 1 476 155 155 ARG CB C 28.93 0.2 1 477 155 155 ARG N N 122.02 0.2 1 478 156 156 THR H H 8.30 0.04 1 479 156 156 THR C C 177.30 0.2 1 480 156 156 THR CA C 66.21 0.2 1 481 156 156 THR CB C 68.44 0.2 1 482 156 156 THR N N 116.39 0.2 1 483 157 157 PHE H H 9.32 0.04 1 484 157 157 PHE C C 178.21 0.2 1 485 157 157 PHE CA C 61.69 0.2 1 486 157 157 PHE CB C 37.99 0.2 1 487 157 157 PHE N N 126.45 0.2 1 488 158 158 PHE H H 8.59 0.04 1 489 158 158 PHE C C 179.47 0.2 1 490 158 158 PHE CA C 62.28 0.2 1 491 158 158 PHE CB C 39.00 0.2 1 492 158 158 PHE N N 114.57 0.2 1 493 159 159 GLN H H 7.93 0.04 1 494 159 159 GLN C C 180.34 0.2 1 495 159 159 GLN CA C 59.05 0.2 1 496 159 159 GLN CB C 26.78 0.2 1 497 159 159 GLN N N 122.18 0.2 1 498 160 160 ARG C C 174.98 0.2 1 499 161 161 LEU H H 6.76 0.04 1 500 161 161 LEU C C 175.80 0.2 1 501 161 161 LEU CA C 53.57 0.2 1 502 161 161 LEU CB C 42.71 0.2 1 503 161 161 LEU N N 112.56 0.2 1 504 162 162 ASN H H 7.99 0.04 1 505 162 162 ASN C C 174.18 0.2 1 506 162 162 ASN CA C 53.43 0.2 1 507 162 162 ASN CB C 37.45 0.2 1 508 162 162 ASN N N 113.67 0.2 1 509 163 163 MET H H 7.69 0.04 1 510 163 163 MET C C 176.54 0.2 1 511 163 163 MET CA C 52.70 0.2 1 512 163 163 MET CB C 33.09 0.2 1 513 163 163 MET N N 114.27 0.2 1 514 164 164 ASN H H 9.99 0.04 1 515 164 164 ASN C C 174.52 0.2 1 516 164 164 ASN CA C 50.44 0.2 1 517 164 164 ASN CB C 38.51 0.2 1 518 164 164 ASN N N 126.44 0.2 1 519 165 165 ASP H H 8.11 0.04 1 520 165 165 ASP C C 176.96 0.2 1 521 165 165 ASP CA C 57.57 0.2 1 522 165 165 ASP CB C 40.28 0.2 1 523 165 165 ASP N N 114.91 0.2 1 524 166 166 ARG H H 7.67 0.04 1 525 166 166 ARG C C 177.22 0.2 1 526 166 166 ARG CA C 60.09 0.2 1 527 166 166 ARG CB C 29.30 0.2 1 528 166 166 ARG N N 117.94 0.2 1 529 167 167 GLU H H 7.88 0.04 1 530 167 167 GLU CA C 59.02 0.2 1 531 167 167 GLU CB C 29.63 0.2 1 532 167 167 GLU N N 117.67 0.2 1 533 181 181 HIS C C 177.26 0.2 1 534 181 181 HIS CA C 54.54 0.2 1 535 181 181 HIS CB C 29.72 0.2 1 536 182 182 LEU H H 9.01 0.04 1 537 182 182 LEU C C 180.73 0.2 1 538 182 182 LEU CA C 59.44 0.2 1 539 182 182 LEU CB C 41.93 0.2 1 540 182 182 LEU N N 131.95 0.2 1 541 183 183 LYS H H 8.88 0.04 1 542 183 183 LYS C C 177.05 0.2 1 543 183 183 LYS CA C 57.51 0.2 1 544 183 183 LYS CB C 31.03 0.2 1 545 183 183 LYS N N 114.17 0.2 1 546 186 186 GLY C C 171.80 0.2 1 547 186 186 GLY CA C 45.11 0.2 1 548 187 187 TYR H H 7.70 0.04 1 549 187 187 TYR C C 171.00 0.2 1 550 187 187 TYR CA C 58.33 0.2 1 551 187 187 TYR CB C 39.99 0.2 1 552 187 187 TYR N N 119.81 0.2 1 553 188 188 GLU C C 176.68 0.2 1 554 188 188 GLU CA C 54.70 0.2 1 555 188 188 GLU CB C 32.22 0.2 1 556 189 189 GLY H H 7.31 0.04 1 557 189 189 GLY CA C 43.00 0.2 1 558 189 189 GLY N N 118.05 0.2 1 559 191 191 TRP C C 176.99 0.2 1 560 191 191 TRP CA C 60.44 0.2 1 561 192 192 GLY H H 7.06 0.04 1 562 192 192 GLY C C 172.30 0.2 1 563 192 192 GLY CA C 44.52 0.2 1 564 192 192 GLY N N 102.93 0.2 1 565 193 193 ALA H H 9.63 0.04 1 566 193 193 ALA C C 179.09 0.2 1 567 193 193 ALA CA C 52.75 0.2 1 568 193 193 ALA CB C 19.83 0.2 1 569 193 193 ALA N N 122.96 0.2 1 570 194 194 ALA H H 8.51 0.04 1 571 194 194 ALA C C 177.49 0.2 1 572 194 194 ALA CA C 50.84 0.2 1 573 194 194 ALA CB C 16.58 0.2 1 574 194 194 ALA N N 124.83 0.2 1 575 195 195 ASN H H 8.05 0.04 1 576 195 195 ASN CA C 54.27 0.2 1 577 195 195 ASN CB C 38.13 0.2 1 578 195 195 ASN N N 113.62 0.2 1 579 196 196 ASN C C 173.33 0.2 1 580 196 196 ASN CA C 51.52 0.2 1 581 197 197 VAL H H 7.38 0.04 1 582 197 197 VAL C C 173.63 0.2 1 583 197 197 VAL CA C 60.83 0.2 1 584 197 197 VAL CB C 33.95 0.2 1 585 197 197 VAL N N 117.24 0.2 1 586 198 198 PHE H H 9.21 0.04 1 587 198 198 PHE C C 173.39 0.2 1 588 198 198 PHE CA C 58.90 0.2 1 589 198 198 PHE CB C 38.65 0.2 1 590 198 198 PHE N N 128.63 0.2 1 591 199 199 THR H H 6.58 0.04 1 592 199 199 THR C C 173.33 0.2 1 593 199 199 THR CA C 60.02 0.2 1 594 199 199 THR CB C 72.68 0.2 1 595 199 199 THR N N 117.52 0.2 1 596 200 200 ASN H H 8.75 0.04 1 597 200 200 ASN C C 175.68 0.2 1 598 200 200 ASN CA C 52.67 0.2 1 599 200 200 ASN CB C 36.64 0.2 1 600 200 200 ASN N N 116.59 0.2 1 601 202 202 PHE C C 175.24 0.2 1 602 203 203 TYR H H 6.16 0.04 1 603 203 203 TYR C C 177.61 0.2 1 604 203 203 TYR CA C 59.39 0.2 1 605 203 203 TYR CB C 36.60 0.2 1 606 203 203 TYR N N 114.98 0.2 1 607 204 204 LEU H H 6.69 0.04 1 608 204 204 LEU C C 178.87 0.2 1 609 204 204 LEU CA C 57.37 0.2 1 610 204 204 LEU CB C 40.53 0.2 1 611 204 204 LEU N N 116.40 0.2 1 612 205 205 ASN H H 8.66 0.04 1 613 205 205 ASN CA C 55.08 0.2 1 614 205 205 ASN CB C 34.77 0.2 1 615 205 205 ASN N N 118.82 0.2 1 616 206 206 LEU C C 178.00 0.2 1 617 206 206 LEU CA C 58.09 0.2 1 618 207 207 LEU H H 7.02 0.04 1 619 207 207 LEU C C 179.23 0.2 1 620 207 207 LEU CA C 56.14 0.2 1 621 207 207 LEU CB C 42.06 0.2 1 622 207 207 LEU N N 112.68 0.2 1 623 208 208 ASN H H 8.34 0.04 1 624 208 208 ASN C C 177.04 0.2 1 625 208 208 ASN CA C 54.31 0.2 1 626 208 208 ASN CB C 39.56 0.2 1 627 208 208 ASN N N 114.54 0.2 1 628 209 209 GLU H H 7.62 0.04 1 629 209 209 GLU C C 173.76 0.2 1 630 209 209 GLU CA C 54.85 0.2 1 631 209 209 GLU CB C 29.23 0.2 1 632 209 209 GLU N N 118.92 0.2 1 633 210 210 ASP H H 8.06 0.04 1 634 210 210 ASP C C 175.24 0.2 1 635 210 210 ASP CA C 52.36 0.2 1 636 210 210 ASP CB C 40.25 0.2 1 637 210 210 ASP N N 119.89 0.2 1 638 211 211 TRP H H 7.82 0.04 1 639 211 211 TRP C C 176.59 0.2 1 640 211 211 TRP CA C 56.01 0.2 1 641 211 211 TRP CB C 32.37 0.2 1 642 211 211 TRP N N 124.71 0.2 1 643 212 212 LYS H H 9.19 0.04 1 644 212 212 LYS C C 174.10 0.2 1 645 212 212 LYS CA C 54.69 0.2 1 646 212 212 LYS CB C 35.07 0.2 1 647 212 212 LYS N N 124.24 0.2 1 648 213 213 LEU H H 8.09 0.04 1 649 213 213 LEU C C 176.31 0.2 1 650 213 213 LEU CA C 54.44 0.2 1 651 213 213 LEU CB C 39.22 0.2 1 652 213 213 LEU N N 131.20 0.2 1 653 214 214 GLU H H 8.89 0.04 1 654 214 214 GLU C C 174.28 0.2 1 655 214 214 GLU CA C 54.01 0.2 1 656 214 214 GLU CB C 31.72 0.2 1 657 214 214 GLU N N 127.25 0.2 1 658 215 215 LYS H H 8.27 0.04 1 659 215 215 LYS C C 176.98 0.2 1 660 215 215 LYS CA C 55.13 0.2 1 661 215 215 LYS CB C 32.65 0.2 1 662 215 215 LYS N N 120.06 0.2 1 663 216 216 ASN H H 8.52 0.04 1 664 216 216 ASN C C 178.14 0.2 1 665 216 216 ASN CA C 50.58 0.2 1 666 216 216 ASN CB C 38.67 0.2 1 667 216 216 ASN N N 122.89 0.2 1 668 217 217 ASP H H 8.73 0.04 1 669 217 217 ASP C C 176.66 0.2 1 670 217 217 ASP CA C 56.47 0.2 1 671 217 217 ASP CB C 39.87 0.2 1 672 217 217 ASP N N 117.57 0.2 1 673 218 218 ALA C C 175.80 0.2 1 674 218 218 ALA CA C 51.00 0.2 1 675 218 218 ALA CB C 17.55 0.2 1 676 219 219 ASN H H 8.20 0.04 1 677 219 219 ASN C C 173.81 0.2 1 678 219 219 ASN CA C 54.29 0.2 1 679 219 219 ASN CB C 36.80 0.2 1 680 219 219 ASN N N 112.99 0.2 1 681 220 220 ASN H H 7.47 0.04 1 682 220 220 ASN C C 174.40 0.2 1 683 220 220 ASN CA C 51.28 0.2 1 684 220 220 ASN CB C 39.68 0.2 1 685 220 220 ASN N N 115.73 0.2 1 686 221 221 GLU H H 8.31 0.04 1 687 221 221 GLU C C 175.38 0.2 1 688 221 221 GLU CA C 55.41 0.2 1 689 221 221 GLU CB C 29.36 0.2 1 690 221 221 GLU N N 120.08 0.2 1 691 222 222 GLN H H 8.83 0.04 1 692 222 222 GLN CA C 53.75 0.2 1 693 222 222 GLN CB C 31.81 0.2 1 694 222 222 GLN N N 117.65 0.2 1 695 223 223 TRP C C 174.73 0.2 1 696 223 223 TRP CA C 55.64 0.2 1 697 223 223 TRP CB C 28.72 0.2 1 698 224 224 ASP H H 9.49 0.04 1 699 224 224 ASP C C 176.51 0.2 1 700 224 224 ASP CA C 51.91 0.2 1 701 224 224 ASP CB C 42.46 0.2 1 702 224 224 ASP N N 120.55 0.2 1 703 225 225 SER H H 8.84 0.04 1 704 225 225 SER C C 177.04 0.2 1 705 225 225 SER CA C 54.69 0.2 1 706 225 225 SER CB C 65.09 0.2 1 707 225 225 SER N N 118.88 0.2 1 708 226 226 LYS H H 8.63 0.04 1 709 226 226 LYS C C 177.58 0.2 1 710 226 226 LYS CA C 57.84 0.2 1 711 226 226 LYS CB C 30.61 0.2 1 712 226 226 LYS N N 124.89 0.2 1 713 227 227 SER H H 7.35 0.04 1 714 227 227 SER C C 173.16 0.2 1 715 227 227 SER CA C 57.39 0.2 1 716 227 227 SER CB C 61.42 0.2 1 717 227 227 SER N N 112.92 0.2 1 718 228 228 GLY H H 7.57 0.04 1 719 228 228 GLY C C 174.12 0.2 1 720 228 228 GLY CA C 44.17 0.2 1 721 228 228 GLY N N 106.63 0.2 1 722 229 229 TYR H H 6.35 0.04 1 723 229 229 TYR C C 174.82 0.2 1 724 229 229 TYR CA C 52.28 0.2 1 725 229 229 TYR CB C 38.80 0.2 1 726 229 229 TYR N N 119.96 0.2 1 727 230 230 MET H H 9.12 0.04 1 728 230 230 MET C C 172.55 0.2 1 729 230 230 MET CA C 53.04 0.2 1 730 230 230 MET CB C 36.39 0.2 1 731 230 230 MET N N 123.81 0.2 1 732 231 231 MET H H 8.61 0.04 1 733 231 231 MET CA C 52.99 0.2 1 734 231 231 MET CB C 35.07 0.2 1 735 231 231 MET N N 112.80 0.2 1 736 236 236 TYR C C 177.07 0.2 1 737 237 237 SER H H 7.69 0.04 1 738 237 237 SER CA C 61.51 0.2 1 739 237 237 SER CB C 62.27 0.2 1 740 237 237 SER N N 113.50 0.2 1 741 240 240 GLN C C 175.82 0.2 1 742 240 240 GLN CA C 55.76 0.2 1 743 241 241 ASP H H 7.22 0.04 1 744 241 241 ASP CA C 50.39 0.2 1 745 241 241 ASP CB C 43.86 0.2 1 746 241 241 ASP N N 122.85 0.2 1 747 242 242 PRO C C 179.40 0.2 1 748 242 242 PRO CA C 64.62 0.2 1 749 243 243 LYS H H 7.44 0.04 1 750 243 243 LYS C C 180.29 0.2 1 751 243 243 LYS CA C 58.15 0.2 1 752 243 243 LYS CB C 30.68 0.2 1 753 243 243 LYS N N 118.80 0.2 1 754 244 244 TYR H H 8.47 0.04 1 755 244 244 TYR C C 178.92 0.2 1 756 244 244 TYR CA C 57.26 0.2 1 757 244 244 TYR CB C 36.76 0.2 1 758 244 244 TYR N N 121.12 0.2 1 759 245 245 LEU H H 8.67 0.04 1 760 245 245 LEU C C 178.19 0.2 1 761 245 245 LEU CA C 57.90 0.2 1 762 245 245 LEU CB C 40.43 0.2 1 763 245 245 LEU N N 122.22 0.2 1 764 246 246 SER H H 7.01 0.04 1 765 246 246 SER C C 176.50 0.2 1 766 246 246 SER CA C 61.10 0.2 1 767 246 246 SER CB C 62.44 0.2 1 768 246 246 SER N N 110.18 0.2 1 769 247 247 ILE H H 7.18 0.04 1 770 247 247 ILE C C 176.54 0.2 1 771 247 247 ILE CA C 63.95 0.2 1 772 247 247 ILE CB C 37.09 0.2 1 773 247 247 ILE N N 123.49 0.2 1 774 248 248 VAL C C 178.24 0.2 1 775 249 249 LYS H H 7.97 0.04 1 776 249 249 LYS C C 178.92 0.2 1 777 249 249 LYS CA C 59.54 0.2 1 778 249 249 LYS CB C 31.69 0.2 1 779 249 249 LYS N N 115.66 0.2 1 780 250 250 GLU H H 7.09 0.04 1 781 250 250 GLU C C 179.98 0.2 1 782 250 250 GLU CA C 59.00 0.2 1 783 250 250 GLU CB C 29.03 0.2 1 784 250 250 GLU N N 120.42 0.2 1 785 251 251 TYR H H 7.56 0.04 1 786 251 251 TYR CA C 55.34 0.2 1 787 251 251 TYR CB C 35.11 0.2 1 788 251 251 TYR N N 119.73 0.2 1 789 252 252 ALA C C 177.47 0.2 1 790 252 252 ALA CA C 54.19 0.2 1 791 253 253 ASN H H 7.10 0.04 1 792 253 253 ASN C C 174.93 0.2 1 793 253 253 ASN CA C 53.52 0.2 1 794 253 253 ASN CB C 39.59 0.2 1 795 253 253 ASN N N 112.30 0.2 1 796 254 254 ASP H H 7.53 0.04 1 797 254 254 ASP C C 174.18 0.2 1 798 254 254 ASP CA C 52.68 0.2 1 799 254 254 ASP CB C 41.10 0.2 1 800 254 254 ASP N N 120.42 0.2 1 801 255 255 GLN H H 9.01 0.04 1 802 255 255 GLN C C 176.76 0.2 1 803 255 255 GLN CA C 59.24 0.2 1 804 255 255 GLN CB C 29.47 0.2 1 805 255 255 GLN N N 125.89 0.2 1 806 256 256 ASP H H 8.06 0.04 1 807 256 256 ASP C C 178.43 0.2 1 808 256 256 ASP CA C 57.46 0.2 1 809 256 256 ASP CB C 40.17 0.2 1 810 256 256 ASP N N 118.90 0.2 1 811 257 257 LYS H H 7.58 0.04 1 812 257 257 LYS C C 178.01 0.2 1 813 257 257 LYS CA C 58.23 0.2 1 814 257 257 LYS CB C 31.30 0.2 1 815 257 257 LYS N N 122.05 0.2 1 816 258 258 PHE H H 7.35 0.04 1 817 258 258 PHE C C 176.00 0.2 1 818 258 258 PHE CA C 58.26 0.2 1 819 258 258 PHE CB C 36.84 0.2 1 820 258 258 PHE N N 118.54 0.2 1 821 259 259 PHE H H 8.90 0.04 1 822 259 259 PHE C C 178.23 0.2 1 823 259 259 PHE CA C 59.82 0.2 1 824 259 259 PHE CB C 36.64 0.2 1 825 259 259 PHE N N 121.24 0.2 1 826 261 261 ASP C C 179.85 0.2 1 827 261 261 ASP CA C 56.75 0.2 1 828 262 262 PHE H H 9.77 0.04 1 829 262 262 PHE C C 176.29 0.2 1 830 262 262 PHE CA C 62.76 0.2 1 831 262 262 PHE CB C 38.12 0.2 1 832 262 262 PHE N N 123.55 0.2 1 833 263 263 SER H H 8.21 0.04 1 834 263 263 SER C C 176.41 0.2 1 835 263 263 SER CA C 61.31 0.2 1 836 263 263 SER CB C 62.29 0.2 1 837 263 263 SER N N 112.99 0.2 1 838 264 264 LYS H H 7.10 0.04 1 839 264 264 LYS C C 179.44 0.2 1 840 264 264 LYS CA C 58.46 0.2 1 841 264 264 LYS CB C 32.12 0.2 1 842 264 264 LYS N N 117.38 0.2 1 843 265 265 ALA H H 8.04 0.04 1 844 265 265 ALA C C 178.78 0.2 1 845 265 265 ALA CA C 54.80 0.2 1 846 265 265 ALA CB C 17.32 0.2 1 847 265 265 ALA N N 123.17 0.2 1 848 266 266 PHE H H 9.32 0.04 1 849 266 266 PHE C C 177.45 0.2 1 850 266 266 PHE CA C 59.86 0.2 1 851 266 266 PHE CB C 38.62 0.2 1 852 266 266 PHE N N 120.25 0.2 1 853 267 267 GLU H H 7.88 0.04 1 854 267 267 GLU C C 177.17 0.2 1 855 267 267 GLU CA C 59.63 0.2 1 856 267 267 GLU CB C 25.77 0.2 1 857 267 267 GLU N N 117.67 0.2 1 858 268 268 LYS H H 7.59 0.04 1 859 268 268 LYS C C 178.93 0.2 1 860 268 268 LYS CA C 59.27 0.2 1 861 268 268 LYS CB C 32.14 0.2 1 862 268 268 LYS N N 118.96 0.2 1 863 269 269 LEU H H 8.39 0.04 1 864 269 269 LEU CA C 57.49 0.2 1 865 269 269 LEU CB C 41.95 0.2 1 866 269 269 LEU N N 120.02 0.2 1 867 270 270 LEU C C 178.12 0.2 1 868 271 271 GLU H H 7.71 0.04 1 869 271 271 GLU C C 176.17 0.2 1 870 271 271 GLU CA C 55.24 0.2 1 871 271 271 GLU CB C 29.50 0.2 1 872 271 271 GLU N N 120.17 0.2 1 873 272 272 ASN H H 7.24 0.04 1 874 272 272 ASN C C 176.42 0.2 1 875 272 272 ASN CA C 53.06 0.2 1 876 272 272 ASN CB C 36.88 0.2 1 877 272 272 ASN N N 123.29 0.2 1 878 273 273 GLY H H 8.36 0.04 1 879 273 273 GLY C C 174.64 0.2 1 880 273 273 GLY CA C 45.31 0.2 1 881 273 273 GLY N N 110.08 0.2 1 882 274 274 ILE H H 7.60 0.04 1 883 274 274 ILE C C 175.28 0.2 1 884 274 274 ILE CA C 61.01 0.2 1 885 274 274 ILE CB C 37.66 0.2 1 886 274 274 ILE N N 121.91 0.2 1 887 275 275 THR H H 8.75 0.04 1 888 275 275 THR C C 172.61 0.2 1 889 275 275 THR CA C 61.45 0.2 1 890 275 275 THR CB C 69.32 0.2 1 891 275 275 THR N N 125.10 0.2 1 892 276 276 PHE H H 9.14 0.04 1 893 276 276 PHE C C 173.76 0.2 1 894 276 276 PHE CA C 55.44 0.2 1 895 276 276 PHE CB C 38.03 0.2 1 896 276 276 PHE N N 129.38 0.2 1 897 277 277 PRO C C 177.12 0.2 1 898 277 277 PRO CA C 61.84 0.2 1 899 277 277 PRO CB C 32.30 0.2 1 900 278 278 LYS H H 8.78 0.04 1 901 278 278 LYS C C 176.81 0.2 1 902 278 278 LYS CA C 58.48 0.2 1 903 278 278 LYS CB C 31.14 0.2 1 904 278 278 LYS N N 121.70 0.2 1 905 279 279 ASP H H 8.15 0.04 1 906 279 279 ASP C C 175.80 0.2 1 907 279 279 ASP CA C 52.53 0.2 1 908 279 279 ASP CB C 38.95 0.2 1 909 279 279 ASP N N 114.97 0.2 1 910 280 280 ALA H H 7.51 0.04 1 911 280 280 ALA C C 175.29 0.2 1 912 280 280 ALA CA C 50.45 0.2 1 913 280 280 ALA CB C 16.87 0.2 1 914 280 280 ALA N N 124.20 0.2 1 915 281 281 PRO C C 176.94 0.2 1 916 281 281 PRO CA C 62.08 0.2 1 917 281 281 PRO CB C 30.65 0.2 1 918 282 282 SER H H 8.29 0.04 1 919 282 282 SER C C 170.95 0.2 1 920 282 282 SER CA C 57.73 0.2 1 921 282 282 SER CB C 60.86 0.2 1 922 282 282 SER N N 119.34 0.2 1 923 283 283 PRO C C 175.75 0.2 1 924 283 283 PRO CA C 62.88 0.2 1 925 284 284 PHE H H 9.08 0.04 1 926 284 284 PHE C C 174.93 0.2 1 927 284 284 PHE CA C 53.79 0.2 1 928 284 284 PHE CB C 39.39 0.2 1 929 284 284 PHE N N 124.91 0.2 1 930 285 285 ILE H H 7.90 0.04 1 931 285 285 ILE C C 176.76 0.2 1 932 285 285 ILE CA C 58.71 0.2 1 933 285 285 ILE CB C 36.63 0.2 1 934 285 285 ILE N N 120.72 0.2 1 935 286 286 PHE H H 9.84 0.04 1 936 286 286 PHE C C 177.07 0.2 1 937 286 286 PHE CA C 58.87 0.2 1 938 286 286 PHE CB C 38.88 0.2 1 939 286 286 PHE N N 130.14 0.2 1 940 287 287 LYS H H 8.66 0.04 1 941 287 287 LYS C C 176.85 0.2 1 942 287 287 LYS CA C 54.75 0.2 1 943 287 287 LYS CB C 33.26 0.2 1 944 287 287 LYS N N 123.72 0.2 1 945 288 288 THR H H 8.60 0.04 1 946 288 288 THR C C 178.57 0.2 1 947 288 288 THR CA C 59.84 0.2 1 948 288 288 THR CB C 70.15 0.2 1 949 288 288 THR N N 110.67 0.2 1 950 289 289 LEU H H 9.54 0.04 1 951 289 289 LEU C C 180.67 0.2 1 952 289 289 LEU CA C 58.79 0.2 1 953 289 289 LEU CB C 38.91 0.2 1 954 289 289 LEU N N 122.27 0.2 1 955 290 290 GLU H H 9.02 0.04 1 956 290 290 GLU CA C 59.16 0.2 1 957 290 290 GLU CB C 28.45 0.2 1 958 290 290 GLU N N 120.61 0.2 1 959 291 291 GLU C C 178.57 0.2 1 960 291 291 GLU CA C 58.33 0.2 1 961 291 291 GLU CB C 29.29 0.2 1 962 292 292 GLN H H 7.54 0.04 1 963 292 292 GLN C C 175.63 0.2 1 964 292 292 GLN CA C 55.70 0.2 1 965 292 292 GLN CB C 31.41 0.2 1 966 292 292 GLN N N 116.98 0.2 1 967 293 293 GLY H H 7.83 0.04 1 968 293 293 GLY C C 174.30 0.2 1 969 293 293 GLY CA C 45.08 0.2 1 970 293 293 GLY N N 108.28 0.2 1 971 294 294 LEU H H 7.71 0.04 1 972 294 294 LEU C C 175.97 0.2 1 973 294 294 LEU CA C 53.45 0.2 1 974 294 294 LEU CB C 40.40 0.2 1 975 294 294 LEU N N 122.15 0.2 1 stop_ save_