data_19076 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N backbone chemical shift assignments of the resting-state yeast cytochrome c peroxidase with the N-terminal His-tag ; _BMRB_accession_number 19076 _BMRB_flat_file_name bmr19076.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" 195 "13C chemical shifts" 515 "15N chemical shifts" 195 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 19075 '1H, 13C, and 15N backbone chemical shift assignments of the resting-state yeast cytochrome c peroxidase with the N-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 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CcP $cytochrome_c_peroxidase cofactor $entity_HEB 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 ; MHHHHHHKTLVHVASVEKGR SYEDFQKVYNAIALKLREDD EYDNYIGYGPVLVRLAWHTS GTWDKHDNTGGSYGGTYRFK KEFNDPSNAGLQNGFKFLEP IHKEFPWISSGDLFSLGGVT AVQEMQGPKIPWRCGRVDTP EDTTPDNGRLPDADKDADYV RTFFQRLNMNDREVVALMGA HALGKTHLKNSGYEGPWGAA NNVFTNEFYLNLLNEDWKLE KNDANNEQWDSKSGYMMLPT DYSLIQDPKYLSIVKEYAND QDKFFKDFSKAFEKLLENGI TFPKDAPSPFIFKTLEEQGL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -5 MET 2 -4 HIS 3 -3 HIS 4 -2 HIS 5 -1 HIS 6 0 HIS 7 1 HIS 8 2 LYS 9 3 THR 10 4 LEU 11 5 VAL 12 6 HIS 13 7 VAL 14 8 ALA 15 9 SER 16 10 VAL 17 11 GLU 18 12 LYS 19 13 GLY 20 14 ARG 21 15 SER 22 16 TYR 23 17 GLU 24 18 ASP 25 19 PHE 26 20 GLN 27 21 LYS 28 22 VAL 29 23 TYR 30 24 ASN 31 25 ALA 32 26 ILE 33 27 ALA 34 28 LEU 35 29 LYS 36 30 LEU 37 31 ARG 38 32 GLU 39 33 ASP 40 34 ASP 41 35 GLU 42 36 TYR 43 37 ASP 44 38 ASN 45 39 TYR 46 40 ILE 47 41 GLY 48 42 TYR 49 43 GLY 50 44 PRO 51 45 VAL 52 46 LEU 53 47 VAL 54 48 ARG 55 49 LEU 56 50 ALA 57 51 TRP 58 52 HIS 59 53 THR 60 54 SER 61 55 GLY 62 56 THR 63 57 TRP 64 58 ASP 65 59 LYS 66 60 HIS 67 61 ASP 68 62 ASN 69 63 THR 70 64 GLY 71 65 GLY 72 66 SER 73 67 TYR 74 68 GLY 75 69 GLY 76 70 THR 77 71 TYR 78 72 ARG 79 73 PHE 80 74 LYS 81 75 LYS 82 76 GLU 83 77 PHE 84 78 ASN 85 79 ASP 86 80 PRO 87 81 SER 88 82 ASN 89 83 ALA 90 84 GLY 91 85 LEU 92 86 GLN 93 87 ASN 94 88 GLY 95 89 PHE 96 90 LYS 97 91 PHE 98 92 LEU 99 93 GLU 100 94 PRO 101 95 ILE 102 96 HIS 103 97 LYS 104 98 GLU 105 99 PHE 106 100 PRO 107 101 TRP 108 102 ILE 109 103 SER 110 104 SER 111 105 GLY 112 106 ASP 113 107 LEU 114 108 PHE 115 109 SER 116 110 LEU 117 111 GLY 118 112 GLY 119 113 VAL 120 114 THR 121 115 ALA 122 116 VAL 123 117 GLN 124 118 GLU 125 119 MET 126 120 GLN 127 121 GLY 128 122 PRO 129 123 LYS 130 124 ILE 131 125 PRO 132 126 TRP 133 127 ARG 134 128 CYS 135 129 GLY 136 130 ARG 137 131 VAL 138 132 ASP 139 133 THR 140 134 PRO 141 135 GLU 142 136 ASP 143 137 THR 144 138 THR 145 139 PRO 146 140 ASP 147 141 ASN 148 142 GLY 149 143 ARG 150 144 LEU 151 145 PRO 152 146 ASP 153 147 ALA 154 148 ASP 155 149 LYS 156 150 ASP 157 151 ALA 158 152 ASP 159 153 TYR 160 154 VAL 161 155 ARG 162 156 THR 163 157 PHE 164 158 PHE 165 159 GLN 166 160 ARG 167 161 LEU 168 162 ASN 169 163 MET 170 164 ASN 171 165 ASP 172 166 ARG 173 167 GLU 174 168 VAL 175 169 VAL 176 170 ALA 177 171 LEU 178 172 MET 179 173 GLY 180 174 ALA 181 175 HIS 182 176 ALA 183 177 LEU 184 178 GLY 185 179 LYS 186 180 THR 187 181 HIS 188 182 LEU 189 183 LYS 190 184 ASN 191 185 SER 192 186 GLY 193 187 TYR 194 188 GLU 195 189 GLY 196 190 PRO 197 191 TRP 198 192 GLY 199 193 ALA 200 194 ALA 201 195 ASN 202 196 ASN 203 197 VAL 204 198 PHE 205 199 THR 206 200 ASN 207 201 GLU 208 202 PHE 209 203 TYR 210 204 LEU 211 205 ASN 212 206 LEU 213 207 LEU 214 208 ASN 215 209 GLU 216 210 ASP 217 211 TRP 218 212 LYS 219 213 LEU 220 214 GLU 221 215 LYS 222 216 ASN 223 217 ASP 224 218 ALA 225 219 ASN 226 220 ASN 227 221 GLU 228 222 GLN 229 223 TRP 230 224 ASP 231 225 SER 232 226 LYS 233 227 SER 234 228 GLY 235 229 TYR 236 230 MET 237 231 MET 238 232 LEU 239 233 PRO 240 234 THR 241 235 ASP 242 236 TYR 243 237 SER 244 238 LEU 245 239 ILE 246 240 GLN 247 241 ASP 248 242 PRO 249 243 LYS 250 244 TYR 251 245 LEU 252 246 SER 253 247 ILE 254 248 VAL 255 249 LYS 256 250 GLU 257 251 TYR 258 252 ALA 259 253 ASN 260 254 ASP 261 255 GLN 262 256 ASP 263 257 LYS 264 258 PHE 265 259 PHE 266 260 LYS 267 261 ASP 268 262 PHE 269 263 SER 270 264 LYS 271 265 ALA 272 266 PHE 273 267 GLU 274 268 LYS 275 269 LEU 276 270 LEU 277 271 GLU 278 272 ASN 279 273 GLY 280 274 ILE 281 275 THR 282 276 PHE 283 277 PRO 284 278 LYS 285 279 ASP 286 280 ALA 287 281 PRO 288 282 SER 289 283 PRO 290 284 PHE 291 285 ILE 292 286 PHE 293 287 LYS 294 288 THR 295 289 LEU 296 290 GLU 297 291 GLU 298 292 GLN 299 293 GLY 300 294 LEU 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 97.67 300 100.00 100.00 0.00e+00 BMRB 19005 cytochrome_c_peroxidase 100.00 300 100.00 100.00 0.00e+00 BMRB 19075 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" 97.67 294 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 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)" 97.67 294 98.63 98.98 0.00e+00 PDB 1AEU "Specificity Of Ligand Binding In A Polar Cavity Of Cytochrome C Peroxidase (2-Methylimidazole)" 97.67 294 98.63 98.98 0.00e+00 PDB 1AEV "Introduction Of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation Of 2- Aminothiazole" 97.67 294 98.63 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" 97.67 294 98.29 98.63 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" 97.00 297 99.31 99.31 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" 97.00 297 98.97 99.31 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" 97.00 297 98.97 98.97 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" 97.67 294 98.98 98.98 0.00e+00 PDB 1CCJ "Conformer Selection By Ligand Binding Observed With Protein Crystallography" 97.67 294 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" 97.67 294 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" 97.67 294 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" 97.67 294 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" 97.67 294 98.63 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" 97.00 296 98.97 98.97 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" 97.67 294 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" 97.67 294 98.63 98.98 0.00e+00 PDB 2AQD "Cytochrome C Peroxidase (Ccp) In Complex With 2,5- Diaminopyridine" 97.67 294 98.98 98.98 0.00e+00 PDB 2AS1 "Cytochrome C Peroxidase In Complex With Thiopheneamidine" 97.67 294 98.98 98.98 0.00e+00 PDB 2AS2 "Cytochrome C Peroxidase In Complex With 2-Iminopiperidine" 97.67 294 98.98 98.98 0.00e+00 PDB 2AS3 "Cytochrome C Peroxidase In Complex With Phenol" 97.67 294 98.98 98.98 0.00e+00 PDB 2AS4 "Cytochrome C Peroxidase In Complex With 3-Fluorocatechol" 97.67 294 98.98 98.98 0.00e+00 PDB 2AS6 "Cytochrome C Peroxidase In Complex With Cyclopentylamine" 97.67 294 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" 97.67 294 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" 97.67 294 98.98 98.98 0.00e+00 PDB 2EUP "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-5- Picoline" 97.67 294 98.98 98.98 0.00e+00 PDB 2EUQ "Cytochrome C Peroxydase (Ccp) In Complex With 3- Thienylmethylamine" 97.67 294 98.98 98.98 0.00e+00 PDB 2EUR "Cytochrome C Peroxidase (Ccp) In Complex With 4- Pyridylcarbinol" 97.67 294 98.98 98.98 0.00e+00 PDB 2EUS "Cytochrome C Peroxidase (Ccp) In Complex With Benzylamine" 97.67 294 98.98 98.98 0.00e+00 PDB 2EUT "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-4- Picoline" 97.67 294 98.98 98.98 0.00e+00 PDB 2EUU "Cytochrome C Peroxidase (Ccp) In Complex With 1h-Imidazol-2- Ylmethanol" 97.67 294 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" 97.00 296 98.97 99.31 0.00e+00 PDB 2V2E "Structure Of Isoniazid (Inh) Bound To Cytochrome C Peroxidase Mutant N184r Y36a" 97.67 294 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" 97.67 294 99.66 100.00 0.00e+00 PDB 2XJ5 "The Structure Of Cytochrome C Peroxidase Compound Ii" 97.67 294 100.00 100.00 0.00e+00 PDB 2XJ8 "The Structure Of Ferrous Cytochrome C Peroxidase" 97.67 294 100.00 100.00 0.00e+00 PDB 2Y5A "Cytochrome C Peroxidase (Ccp) W191g Bound To 3-Aminopyridine" 97.67 294 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" 97.67 294 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" 97.00 295 98.28 98.28 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" 97.00 296 98.97 99.31 0.00e+00 PDB 4A71 "Cytochrome C Peroxidase In Complex With Phenol" 97.00 296 99.31 99.31 0.00e+00 PDB 4A78 "Cytochrome C Peroxidase M119w In Complex With Guiacol" 97.00 296 99.31 99.31 0.00e+00 PDB 4A7M "Cytochrome C Peroxidase S81w Mutant" 97.00 296 99.66 99.66 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" 97.67 294 98.98 98.98 0.00e+00 PDB 4CVI "Neutron Structure Of Ferric Cytochrome C Peroxidase - Deuterium Exchanged At Room Temperature" 97.67 294 99.66 99.66 0.00e+00 PDB 4CVJ "Neutron Structure Of Compound I Intermediate Of Cytochrome C Peroxidase - Deuterium Exchanged 100 K" 97.67 294 100.00 100.00 0.00e+00 PDB 4JB4 "Expression, Purification, Characterization, And Solution Nmr Study Of Highly Deuterated Yeast Cytochrome C Peroxidase With Enha" 97.67 300 100.00 100.00 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" 97.67 294 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" 97.67 292 98.29 98.29 0.00e+00 PDB 4XV6 "Ccp Gateless Cavity" 97.00 289 98.28 98.28 0.00e+00 PDB 4XV7 "Ccp Gateless Cavity" 97.67 292 98.29 98.29 0.00e+00 PDB 4XV8 "Ccp Gateless Cavity" 97.67 292 98.29 98.29 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_HEB _Saveframe_category ligand _Mol_type NON-POLYMER _Name_common 'HEME B/C' _BMRB_code HEB _PDB_code HEB _Molecular_mass 618.503 _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 FE FE FE . 0 . ? 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 . ? 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 . ? HAB2 HAB2 H . 0 . ? HBB1 HBB1 H . 0 . ? HBB2 HBB2 H . 0 . ? HBB3 HBB3 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 FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? DOUB CHA C1A ? ? SING CHA C4D ? ? SING CHA HHA ? ? DOUB CHB C4A ? ? SING CHB C1B ? ? SING CHB HHB ? ? DOUB CHC C4B ? ? SING CHC C1C ? ? SING CHC HHC ? ? SING CHD C4C ? ? DOUB CHD C1D ? ? SING CHD HHD ? ? SING NA C1A ? ? SING NA C4A ? ? SING C1A C2A ? ? DOUB C2A C3A ? ? SING C2A CAA ? ? SING 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 ? ? DOUB NB C1B ? ? SING 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 ? ? SING CAB CBB ? ? SING CAB HAB ? ? SING CAB HAB2 ? ? SING CBB HBB1 ? ? SING CBB HBB2 ? ? SING CBB HBB3 ? ? SING NC C1C ? ? SING NC C4C ? ? DOUB C1C C2C ? ? SING C2C C3C ? ? SING C2C CMC ? ? DOUB 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 ? ? SING ND C1D ? ? DOUB 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 1.25 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 _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 1 7 HIS C C 174.27 0.2 1 2 1 7 HIS CA C 55.15 0.2 1 3 1 7 HIS CB C 29.29 0.2 1 4 2 8 LYS H H 8.37 0.04 1 5 2 8 LYS C C 176.20 0.2 1 6 2 8 LYS CA C 55.88 0.2 1 7 2 8 LYS CB C 32.21 0.2 1 8 2 8 LYS N N 123.98 0.2 1 9 3 9 THR H H 8.19 0.04 1 10 3 9 THR C C 173.91 0.2 1 11 3 9 THR CA C 61.65 0.2 1 12 3 9 THR CB C 69.27 0.2 1 13 3 9 THR N N 118.53 0.2 1 14 4 10 LEU H H 8.13 0.04 1 15 4 10 LEU C C 175.95 0.2 1 16 4 10 LEU CA C 54.52 0.2 1 17 4 10 LEU CB C 41.40 0.2 1 18 4 10 LEU N N 126.82 0.2 1 19 5 11 VAL H H 8.11 0.04 1 20 5 11 VAL C C 174.53 0.2 1 21 5 11 VAL CA C 60.74 0.2 1 22 5 11 VAL CB C 32.98 0.2 1 23 5 11 VAL N N 123.95 0.2 1 24 6 12 HIS H H 8.67 0.04 1 25 6 12 HIS C C 172.26 0.2 1 26 6 12 HIS CA C 51.68 0.2 1 27 6 12 HIS CB C 26.91 0.2 1 28 6 12 HIS N N 124.93 0.2 1 29 7 13 VAL H H 8.81 0.04 1 30 7 13 VAL C C 177.94 0.2 1 31 7 13 VAL CA C 61.40 0.2 1 32 7 13 VAL CB C 31.21 0.2 1 33 7 13 VAL N N 124.87 0.2 1 34 8 14 ALA H H 8.50 0.04 1 35 8 14 ALA C C 177.06 0.2 1 36 8 14 ALA CA C 52.27 0.2 1 37 8 14 ALA CB C 19.57 0.2 1 38 8 14 ALA N N 135.48 0.2 1 39 9 15 SER H H 9.48 0.04 1 40 9 15 SER C C 172.78 0.2 1 41 9 15 SER CA C 56.11 0.2 1 42 9 15 SER CB C 63.44 0.2 1 43 9 15 SER N N 120.73 0.2 1 44 11 17 GLU C C 176.76 0.2 1 45 12 18 LYS H H 8.15 0.04 1 46 12 18 LYS C C 178.88 0.2 1 47 12 18 LYS CA C 58.14 0.2 1 48 12 18 LYS CB C 31.45 0.2 1 49 12 18 LYS N N 123.50 0.2 1 50 13 19 GLY H H 8.86 0.04 1 51 13 19 GLY CA C 45.14 0.2 1 52 13 19 GLY N N 113.19 0.2 1 53 14 20 ARG H H 7.68 0.04 1 54 14 20 ARG C C 175.55 0.2 1 55 14 20 ARG CA C 52.67 0.2 1 56 14 20 ARG CB C 29.07 0.2 1 57 14 20 ARG N N 118.91 0.2 1 58 15 21 SER H H 9.39 0.04 1 59 15 21 SER C C 174.29 0.2 1 60 15 21 SER CA C 56.50 0.2 1 61 15 21 SER CB C 65.88 0.2 1 62 15 21 SER N N 118.60 0.2 1 63 16 22 TYR H H 8.95 0.04 1 64 16 22 TYR C C 176.19 0.2 1 65 16 22 TYR CA C 61.42 0.2 1 66 16 22 TYR CB C 37.80 0.2 1 67 16 22 TYR N N 122.09 0.2 1 68 17 23 GLU H H 8.84 0.04 1 69 17 23 GLU C C 179.17 0.2 1 70 17 23 GLU CA C 59.50 0.2 1 71 17 23 GLU CB C 28.20 0.2 1 72 17 23 GLU N N 117.09 0.2 1 73 18 24 ASP H H 7.55 0.04 1 74 18 24 ASP C C 178.01 0.2 1 75 18 24 ASP CA C 57.41 0.2 1 76 18 24 ASP CB C 41.40 0.2 1 77 18 24 ASP N N 117.67 0.2 1 78 19 25 PHE H H 7.44 0.04 1 79 19 25 PHE CA C 62.27 0.2 1 80 19 25 PHE CB C 38.73 0.2 1 81 19 25 PHE N N 115.95 0.2 1 82 20 26 GLN H H 8.82 0.04 1 83 20 26 GLN C C 177.80 0.2 1 84 20 26 GLN CA C 57.38 0.2 1 85 20 26 GLN CB C 27.10 0.2 1 86 20 26 GLN N N 121.69 0.2 1 87 21 27 LYS H H 7.38 0.04 1 88 21 27 LYS C C 179.12 0.2 1 89 21 27 LYS CA C 59.77 0.2 1 90 21 27 LYS CB C 31.22 0.2 1 91 21 27 LYS N N 119.46 0.2 1 92 22 28 VAL H H 6.85 0.04 1 93 22 28 VAL CA C 65.39 0.2 1 94 22 28 VAL N N 121.96 0.2 1 95 24 30 ASN H H 8.74 0.04 1 96 24 30 ASN C C 176.86 0.2 1 97 24 30 ASN CA C 54.89 0.2 1 98 24 30 ASN CB C 36.31 0.2 1 99 24 30 ASN N N 117.70 0.2 1 100 25 31 ALA H H 7.84 0.04 1 101 25 31 ALA CA C 54.93 0.2 1 102 25 31 ALA CB C 18.37 0.2 1 103 25 31 ALA N N 123.08 0.2 1 104 27 33 ALA H H 9.13 0.04 1 105 27 33 ALA CA C 54.87 0.2 1 106 27 33 ALA CB C 18.53 0.2 1 107 27 33 ALA N N 122.19 0.2 1 108 28 34 LEU H H 9.31 0.04 1 109 28 34 LEU CA C 57.35 0.2 1 110 28 34 LEU CB C 40.69 0.2 1 111 28 34 LEU N N 121.67 0.2 1 112 29 35 LYS H H 7.57 0.04 1 113 29 35 LYS CA C 59.39 0.2 1 114 29 35 LYS CB C 30.91 0.2 1 115 29 35 LYS N N 123.25 0.2 1 116 30 36 LEU H H 8.73 0.04 1 117 30 36 LEU CA C 56.93 0.2 1 118 30 36 LEU CB C 41.55 0.2 1 119 30 36 LEU N N 120.42 0.2 1 120 31 37 ARG H H 7.48 0.04 1 121 31 37 ARG C C 177.72 0.2 1 122 31 37 ARG CA C 58.22 0.2 1 123 31 37 ARG CB C 30.78 0.2 1 124 31 37 ARG N N 117.52 0.2 1 125 36 42 TYR H H 6.91 0.04 1 126 36 42 TYR C C 174.20 0.2 1 127 36 42 TYR CA C 58.63 0.2 1 128 36 42 TYR CB C 40.25 0.2 1 129 36 42 TYR N N 121.35 0.2 1 130 37 43 ASP H H 8.16 0.04 1 131 37 43 ASP C C 175.66 0.2 1 132 37 43 ASP CA C 53.28 0.2 1 133 37 43 ASP CB C 38.69 0.2 1 134 37 43 ASP N N 128.16 0.2 1 135 38 44 ASN H H 8.52 0.04 1 136 38 44 ASN C C 175.03 0.2 1 137 38 44 ASN CA C 54.55 0.2 1 138 38 44 ASN CB C 36.74 0.2 1 139 38 44 ASN N N 115.09 0.2 1 140 39 45 TYR H H 7.48 0.04 1 141 39 45 TYR CA C 60.08 0.2 1 142 39 45 TYR CB C 33.15 0.2 1 143 39 45 TYR N N 108.88 0.2 1 144 41 47 GLY H H 8.77 0.04 1 145 41 47 GLY CA C 44.47 0.2 1 146 41 47 GLY N N 107.53 0.2 1 147 42 48 TYR H H 9.66 0.04 1 148 42 48 TYR C C 175.57 0.2 1 149 42 48 TYR CA C 60.21 0.2 1 150 42 48 TYR CB C 38.93 0.2 1 151 42 48 TYR N N 116.08 0.2 1 152 43 49 GLY H H 9.77 0.04 1 153 43 49 GLY CA C 48.91 0.2 1 154 43 49 GLY N N 109.51 0.2 1 155 57 63 TRP H H 6.72 0.04 1 156 57 63 TRP C C 173.49 0.2 1 157 57 63 TRP CA C 58.67 0.2 1 158 57 63 TRP CB C 27.54 0.2 1 159 57 63 TRP N N 121.67 0.2 1 160 58 64 ASP H H 7.35 0.04 1 161 58 64 ASP C C 174.96 0.2 1 162 58 64 ASP CA C 52.07 0.2 1 163 58 64 ASP CB C 42.11 0.2 1 164 58 64 ASP N N 125.78 0.2 1 165 59 65 LYS H H 6.80 0.04 1 166 59 65 LYS C C 177.33 0.2 1 167 59 65 LYS CA C 56.53 0.2 1 168 59 65 LYS CB C 31.40 0.2 1 169 59 65 LYS N N 122.74 0.2 1 170 60 66 HIS H H 8.81 0.04 1 171 60 66 HIS C C 175.65 0.2 1 172 60 66 HIS CA C 58.50 0.2 1 173 60 66 HIS CB C 27.19 0.2 1 174 60 66 HIS N N 119.02 0.2 1 175 63 69 THR H H 7.56 0.04 1 176 63 69 THR C C 175.64 0.2 1 177 63 69 THR CA C 60.43 0.2 1 178 63 69 THR CB C 71.54 0.2 1 179 63 69 THR N N 108.27 0.2 1 180 64 70 GLY H H 8.35 0.04 1 181 64 70 GLY CA C 44.28 0.2 1 182 64 70 GLY N N 105.34 0.2 1 183 65 71 GLY H H 7.81 0.04 1 184 65 71 GLY CA C 43.63 0.2 1 185 65 71 GLY N N 107.54 0.2 1 186 66 72 SER H H 8.49 0.04 1 187 66 72 SER CA C 59.52 0.2 1 188 66 72 SER N N 111.73 0.2 1 189 67 73 TYR H H 8.30 0.04 1 190 67 73 TYR CA C 62.47 0.2 1 191 67 73 TYR CB C 37.26 0.2 1 192 67 73 TYR N N 122.31 0.2 1 193 68 74 GLY H H 8.30 0.04 1 194 68 74 GLY CA C 45.96 0.2 1 195 68 74 GLY N N 98.87 0.2 1 196 69 75 GLY H H 7.60 0.04 1 197 69 75 GLY CA C 46.81 0.2 1 198 69 75 GLY N N 109.65 0.2 1 199 70 76 THR H H 7.42 0.04 1 200 70 76 THR C C 173.97 0.2 1 201 70 76 THR CA C 63.94 0.2 1 202 70 76 THR CB C 66.88 0.2 1 203 70 76 THR N N 111.98 0.2 1 204 72 78 ARG H H 6.51 0.04 1 205 72 78 ARG C C 176.00 0.2 1 206 72 78 ARG CA C 55.48 0.2 1 207 72 78 ARG CB C 28.36 0.2 1 208 72 78 ARG N N 107.91 0.2 1 209 73 79 PHE H H 7.95 0.04 1 210 73 79 PHE C C 176.30 0.2 1 211 73 79 PHE CA C 57.08 0.2 1 212 73 79 PHE CB C 37.68 0.2 1 213 73 79 PHE N N 123.26 0.2 1 214 74 80 LYS H H 8.58 0.04 1 215 74 80 LYS C C 176.87 0.2 1 216 74 80 LYS CA C 58.62 0.2 1 217 74 80 LYS CB C 31.48 0.2 1 218 74 80 LYS N N 121.95 0.2 1 219 75 81 LYS H H 8.34 0.04 1 220 75 81 LYS C C 177.25 0.2 1 221 75 81 LYS CA C 59.36 0.2 1 222 75 81 LYS CB C 31.48 0.2 1 223 75 81 LYS N N 117.31 0.2 1 224 76 82 GLU H H 6.28 0.04 1 225 76 82 GLU C C 178.81 0.2 1 226 76 82 GLU CA C 57.08 0.2 1 227 76 82 GLU CB C 29.42 0.2 1 228 76 82 GLU N N 118.52 0.2 1 229 78 84 ASN H H 7.44 0.04 1 230 78 84 ASN C C 173.97 0.2 1 231 78 84 ASN CA C 52.02 0.2 1 232 78 84 ASN CB C 37.51 0.2 1 233 78 84 ASN N N 111.99 0.2 1 234 79 85 ASP H H 6.70 0.04 1 235 79 85 ASP C C 177.41 0.2 1 236 79 85 ASP CA C 52.00 0.2 1 237 79 85 ASP CB C 41.00 0.2 1 238 79 85 ASP N N 123.95 0.2 1 239 89 95 PHE H H 7.81 0.04 1 240 89 95 PHE C C 177.51 0.2 1 241 89 95 PHE CA C 61.65 0.2 1 242 89 95 PHE CB C 38.99 0.2 1 243 89 95 PHE N N 122.90 0.2 1 244 90 96 LYS H H 8.45 0.04 1 245 90 96 LYS C C 179.00 0.2 1 246 90 96 LYS CA C 58.31 0.2 1 247 90 96 LYS CB C 31.07 0.2 1 248 90 96 LYS N N 117.71 0.2 1 249 91 97 PHE H H 7.11 0.04 1 250 91 97 PHE C C 175.83 0.2 1 251 91 97 PHE CA C 60.51 0.2 1 252 91 97 PHE CB C 37.85 0.2 1 253 91 97 PHE N N 121.06 0.2 1 254 92 98 LEU H H 7.15 0.04 1 255 92 98 LEU C C 178.49 0.2 1 256 92 98 LEU CA C 55.08 0.2 1 257 92 98 LEU CB C 41.88 0.2 1 258 92 98 LEU N N 114.12 0.2 1 259 93 99 GLU H H 7.64 0.04 1 260 93 99 GLU C C 175.86 0.2 1 261 93 99 GLU CA C 61.29 0.2 1 262 93 99 GLU CB C 26.54 0.2 1 263 93 99 GLU N N 122.90 0.2 1 264 95 101 ILE H H 6.62 0.04 1 265 95 101 ILE CA C 62.96 0.2 1 266 95 101 ILE CB C 35.33 0.2 1 267 95 101 ILE N N 119.11 0.2 1 268 96 102 HIS C C 177.52 0.2 1 269 97 103 LYS H H 7.58 0.04 1 270 97 103 LYS C C 177.86 0.2 1 271 97 103 LYS CA C 57.94 0.2 1 272 97 103 LYS CB C 31.07 0.2 1 273 97 103 LYS N N 115.22 0.2 1 274 98 104 GLU H H 7.05 0.04 1 275 98 104 GLU C C 175.76 0.2 1 276 98 104 GLU CA C 57.20 0.2 1 277 98 104 GLU CB C 28.57 0.2 1 278 98 104 GLU N N 119.29 0.2 1 279 99 105 PHE H H 7.35 0.04 1 280 99 105 PHE C C 172.38 0.2 1 281 99 105 PHE CA C 53.61 0.2 1 282 99 105 PHE CB C 37.05 0.2 1 283 99 105 PHE N N 116.77 0.2 1 284 104 110 SER H H 10.17 0.04 1 285 104 110 SER CA C 63.24 0.2 1 286 104 110 SER CB C 61.49 0.2 1 287 104 110 SER N N 120.64 0.2 1 288 105 111 GLY H H 9.40 0.04 1 289 105 111 GLY CA C 45.70 0.2 1 290 105 111 GLY N N 108.85 0.2 1 291 106 112 ASP H H 7.49 0.04 1 292 106 112 ASP C C 176.11 0.2 1 293 106 112 ASP CA C 57.78 0.2 1 294 106 112 ASP CB C 38.12 0.2 1 295 106 112 ASP N N 124.51 0.2 1 296 107 113 LEU H H 7.81 0.04 1 297 107 113 LEU C C 178.28 0.2 1 298 107 113 LEU CA C 57.88 0.2 1 299 107 113 LEU CB C 39.96 0.2 1 300 107 113 LEU N N 122.01 0.2 1 301 108 114 PHE H H 8.57 0.04 1 302 108 114 PHE C C 179.33 0.2 1 303 108 114 PHE CA C 56.98 0.2 1 304 108 114 PHE CB C 36.76 0.2 1 305 108 114 PHE N N 116.07 0.2 1 306 109 115 SER H H 7.80 0.04 1 307 109 115 SER C C 175.96 0.2 1 308 109 115 SER CA C 61.17 0.2 1 309 109 115 SER CB C 62.96 0.2 1 310 109 115 SER N N 112.49 0.2 1 311 110 116 LEU H H 8.66 0.04 1 312 110 116 LEU CA C 57.08 0.2 1 313 110 116 LEU N N 127.50 0.2 1 314 111 117 GLY H H 8.78 0.04 1 315 111 117 GLY CA C 47.64 0.2 1 316 111 117 GLY N N 109.06 0.2 1 317 112 118 GLY H H 7.24 0.04 1 318 112 118 GLY CA C 47.36 0.2 1 319 112 118 GLY N N 105.31 0.2 1 320 113 119 VAL H H 7.73 0.04 1 321 113 119 VAL C C 177.13 0.2 1 322 113 119 VAL CA C 67.59 0.2 1 323 113 119 VAL CB C 31.92 0.2 1 324 113 119 VAL N N 122.41 0.2 1 325 117 123 GLN H H 8.27 0.04 1 326 117 123 GLN CA C 59.50 0.2 1 327 117 123 GLN CB C 27.69 0.2 1 328 117 123 GLN N N 115.18 0.2 1 329 118 124 GLU H H 9.32 0.04 1 330 118 124 GLU CA C 57.99 0.2 1 331 118 124 GLU CB C 28.48 0.2 1 332 118 124 GLU N N 119.71 0.2 1 333 119 125 MET H H 7.85 0.04 1 334 119 125 MET CA C 56.45 0.2 1 335 119 125 MET CB C 31.10 0.2 1 336 119 125 MET N N 120.15 0.2 1 337 120 126 GLN H H 7.67 0.04 1 338 120 126 GLN C C 176.23 0.2 1 339 120 126 GLN CA C 57.25 0.2 1 340 120 126 GLN CB C 24.34 0.2 1 341 120 126 GLN N N 109.14 0.2 1 342 121 127 GLY H H 8.28 0.04 1 343 121 127 GLY CA C 44.53 0.2 1 344 121 127 GLY N N 105.95 0.2 1 345 126 132 TRP H H 9.18 0.04 1 346 126 132 TRP C C 173.42 0.2 1 347 126 132 TRP CA C 56.68 0.2 1 348 126 132 TRP CB C 31.80 0.2 1 349 126 132 TRP N N 124.87 0.2 1 350 127 133 ARG H H 8.01 0.04 1 351 127 133 ARG C C 172.36 0.2 1 352 127 133 ARG CA C 52.84 0.2 1 353 127 133 ARG CB C 33.15 0.2 1 354 127 133 ARG N N 126.55 0.2 1 355 128 134 CYS H H 6.31 0.04 1 356 128 134 CYS C C 173.24 0.2 1 357 128 134 CYS CA C 53.54 0.2 1 358 128 134 CYS CB C 31.72 0.2 1 359 128 134 CYS N N 113.65 0.2 1 360 129 135 GLY H H 10.06 0.04 1 361 129 135 GLY N N 107.30 0.2 1 362 132 138 ASP H H 8.06 0.04 1 363 132 138 ASP C C 177.65 0.2 1 364 132 138 ASP CA C 54.50 0.2 1 365 132 138 ASP CB C 38.06 0.2 1 366 132 138 ASP N N 124.02 0.2 1 367 133 139 THR H H 8.51 0.04 1 368 133 139 THR C C 173.93 0.2 1 369 133 139 THR CA C 59.14 0.2 1 370 133 139 THR CB C 67.65 0.2 1 371 133 139 THR N N 116.91 0.2 1 372 135 141 GLU H H 8.56 0.04 1 373 135 141 GLU C C 178.80 0.2 1 374 135 141 GLU CA C 59.61 0.2 1 375 135 141 GLU CB C 28.15 0.2 1 376 135 141 GLU N N 124.16 0.2 1 377 136 142 ASP H H 8.37 0.04 1 378 136 142 ASP C C 176.44 0.2 1 379 136 142 ASP CA C 55.04 0.2 1 380 136 142 ASP CB C 38.46 0.2 1 381 136 142 ASP N N 117.65 0.2 1 382 137 143 THR H H 7.86 0.04 1 383 137 143 THR CB C 69.47 0.2 1 384 137 143 THR N N 110.36 0.2 1 385 138 144 THR H H 7.37 0.04 1 386 138 144 THR CA C 61.61 0.2 1 387 138 144 THR CB C 68.51 0.2 1 388 138 144 THR N N 123.67 0.2 1 389 140 146 ASP H H 8.04 0.04 1 390 140 146 ASP C C 175.68 0.2 1 391 140 146 ASP CA C 53.93 0.2 1 392 140 146 ASP CB C 39.76 0.2 1 393 140 146 ASP N N 119.66 0.2 1 394 141 147 ASN H H 8.38 0.04 1 395 141 147 ASN C C 174.55 0.2 1 396 141 147 ASN CA C 52.97 0.2 1 397 141 147 ASN CB C 38.38 0.2 1 398 141 147 ASN N N 117.13 0.2 1 399 142 148 GLY H H 7.70 0.04 1 400 142 148 GLY CA C 44.75 0.2 1 401 142 148 GLY N N 110.35 0.2 1 402 150 156 ASP H H 7.59 0.04 1 403 150 156 ASP C C 176.99 0.2 1 404 150 156 ASP CA C 51.77 0.2 1 405 150 156 ASP CB C 42.62 0.2 1 406 150 156 ASP N N 116.43 0.2 1 407 151 157 ALA H H 8.79 0.04 1 408 151 157 ALA C C 179.72 0.2 1 409 151 157 ALA CA C 55.48 0.2 1 410 151 157 ALA CB C 19.02 0.2 1 411 151 157 ALA N N 120.12 0.2 1 412 152 158 ASP H H 8.08 0.04 1 413 152 158 ASP CA C 57.19 0.2 1 414 152 158 ASP CB C 40.32 0.2 1 415 152 158 ASP N N 115.79 0.2 1 416 153 159 TYR H H 8.35 0.04 1 417 153 159 TYR C C 178.14 0.2 1 418 153 159 TYR CA C 61.84 0.2 1 419 153 159 TYR CB C 38.14 0.2 1 420 153 159 TYR N N 122.31 0.2 1 421 154 160 VAL H H 9.00 0.04 1 422 154 160 VAL CA C 68.78 0.2 1 423 154 160 VAL N N 123.73 0.2 1 424 155 161 ARG H H 9.38 0.04 1 425 155 161 ARG CA C 60.41 0.2 1 426 155 161 ARG CB C 29.28 0.2 1 427 155 161 ARG N N 122.26 0.2 1 428 156 162 THR H H 8.63 0.04 1 429 156 162 THR C C 177.68 0.2 1 430 156 162 THR CA C 66.57 0.2 1 431 156 162 THR CB C 68.75 0.2 1 432 156 162 THR N N 116.53 0.2 1 433 157 163 PHE H H 9.72 0.04 1 434 157 163 PHE CA C 62.09 0.2 1 435 157 163 PHE CB C 38.64 0.2 1 436 157 163 PHE N N 126.68 0.2 1 437 159 165 GLN H H 8.25 0.04 1 438 159 165 GLN CA C 59.30 0.2 1 439 159 165 GLN CB C 27.05 0.2 1 440 159 165 GLN N N 122.35 0.2 1 441 160 166 ARG H H 7.79 0.04 1 442 160 166 ARG C C 175.05 0.2 1 443 160 166 ARG CA C 58.08 0.2 1 444 160 166 ARG CB C 29.84 0.2 1 445 160 166 ARG N N 123.94 0.2 1 446 161 167 LEU H H 6.99 0.04 1 447 161 167 LEU C C 176.00 0.2 1 448 161 167 LEU CA C 53.71 0.2 1 449 161 167 LEU CB C 43.18 0.2 1 450 161 167 LEU N N 112.71 0.2 1 451 162 168 ASN H H 8.15 0.04 1 452 162 168 ASN C C 174.33 0.2 1 453 162 168 ASN CA C 53.62 0.2 1 454 162 168 ASN CB C 37.54 0.2 1 455 162 168 ASN N N 113.63 0.2 1 456 163 169 MET H H 7.93 0.04 1 457 163 169 MET C C 176.82 0.2 1 458 163 169 MET CA C 53.02 0.2 1 459 163 169 MET CB C 33.51 0.2 1 460 163 169 MET N N 114.37 0.2 1 461 164 170 ASN H H 10.25 0.04 1 462 164 170 ASN C C 174.76 0.2 1 463 164 170 ASN CA C 50.74 0.2 1 464 164 170 ASN CB C 38.63 0.2 1 465 164 170 ASN N N 126.60 0.2 1 466 165 171 ASP H H 8.28 0.04 1 467 165 171 ASP C C 177.16 0.2 1 468 165 171 ASP CA C 57.74 0.2 1 469 165 171 ASP CB C 40.28 0.2 1 470 165 171 ASP N N 114.92 0.2 1 471 166 172 ARG H H 7.83 0.04 1 472 166 172 ARG C C 177.56 0.2 1 473 166 172 ARG CA C 60.20 0.2 1 474 166 172 ARG CB C 29.38 0.2 1 475 166 172 ARG N N 118.18 0.2 1 476 167 173 GLU H H 8.09 0.04 1 477 167 173 GLU CA C 59.46 0.2 1 478 167 173 GLU CB C 30.12 0.2 1 479 167 173 GLU N N 117.70 0.2 1 480 168 174 VAL H H 8.75 0.04 1 481 168 174 VAL CA C 67.72 0.2 1 482 168 174 VAL N N 118.68 0.2 1 483 169 175 VAL H H 8.26 0.04 1 484 169 175 VAL CA C 66.83 0.2 1 485 169 175 VAL N N 117.62 0.2 1 486 182 188 LEU H H 9.44 0.04 1 487 182 188 LEU CA C 59.97 0.2 1 488 182 188 LEU CB C 42.30 0.2 1 489 182 188 LEU N N 132.52 0.2 1 490 183 189 LYS H H 9.22 0.04 1 491 183 189 LYS C C 177.44 0.2 1 492 183 189 LYS CA C 57.78 0.2 1 493 183 189 LYS CB C 31.25 0.2 1 494 183 189 LYS N N 114.45 0.2 1 495 193 199 ALA H H 9.23 0.04 1 496 193 199 ALA CA C 52.51 0.2 1 497 193 199 ALA CB C 19.59 0.2 1 498 193 199 ALA N N 122.31 0.2 1 499 194 200 ALA H H 8.20 0.04 1 500 194 200 ALA CA C 51.09 0.2 1 501 194 200 ALA CB C 16.80 0.2 1 502 194 200 ALA N N 124.18 0.2 1 503 195 201 ASN H H 8.12 0.04 1 504 195 201 ASN CA C 54.55 0.2 1 505 195 201 ASN N N 113.56 0.2 1 506 196 202 ASN H H 8.11 0.04 1 507 196 202 ASN CA C 51.94 0.2 1 508 196 202 ASN N N 115.51 0.2 1 509 197 203 VAL H H 7.46 0.04 1 510 197 203 VAL C C 173.74 0.2 1 511 197 203 VAL CA C 60.81 0.2 1 512 197 203 VAL CB C 34.02 0.2 1 513 197 203 VAL N N 116.99 0.2 1 514 198 204 PHE H H 9.23 0.04 1 515 198 204 PHE C C 173.31 0.2 1 516 198 204 PHE CA C 59.09 0.2 1 517 198 204 PHE CB C 38.83 0.2 1 518 198 204 PHE N N 128.72 0.2 1 519 199 205 THR H H 6.48 0.04 1 520 199 205 THR C C 172.97 0.2 1 521 199 205 THR CA C 59.85 0.2 1 522 199 205 THR CB C 72.59 0.2 1 523 199 205 THR N N 117.26 0.2 1 524 200 206 ASN H H 8.50 0.04 1 525 200 206 ASN C C 175.24 0.2 1 526 200 206 ASN CA C 52.25 0.2 1 527 200 206 ASN CB C 36.35 0.2 1 528 200 206 ASN N N 116.11 0.2 1 529 204 210 LEU H H 6.14 0.04 1 530 204 210 LEU C C 178.41 0.2 1 531 204 210 LEU CA C 56.88 0.2 1 532 204 210 LEU CB C 40.25 0.2 1 533 204 210 LEU N N 115.62 0.2 1 534 205 211 ASN H H 7.92 0.04 1 535 205 211 ASN CA C 54.23 0.2 1 536 205 211 ASN CB C 34.02 0.2 1 537 205 211 ASN N N 118.18 0.2 1 538 206 212 LEU H H 6.98 0.04 1 539 206 212 LEU C C 177.53 0.2 1 540 206 212 LEU CA C 57.48 0.2 1 541 206 212 LEU CB C 39.74 0.2 1 542 206 212 LEU N N 122.32 0.2 1 543 207 213 LEU H H 6.52 0.04 1 544 207 213 LEU C C 179.06 0.2 1 545 207 213 LEU CA C 55.78 0.2 1 546 207 213 LEU CB C 41.77 0.2 1 547 207 213 LEU N N 112.00 0.2 1 548 208 214 ASN H H 7.91 0.04 1 549 208 214 ASN C C 176.67 0.2 1 550 208 214 ASN CA C 53.94 0.2 1 551 208 214 ASN CB C 39.30 0.2 1 552 208 214 ASN N N 114.07 0.2 1 553 209 215 GLU H H 7.23 0.04 1 554 209 215 GLU C C 173.41 0.2 1 555 209 215 GLU CA C 54.56 0.2 1 556 209 215 GLU CB C 28.74 0.2 1 557 209 215 GLU N N 118.40 0.2 1 558 210 216 ASP H H 7.79 0.04 1 559 210 216 ASP C C 175.02 0.2 1 560 210 216 ASP CA C 52.17 0.2 1 561 210 216 ASP CB C 40.14 0.2 1 562 210 216 ASP N N 119.50 0.2 1 563 211 217 TRP H H 7.55 0.04 1 564 211 217 TRP C C 176.46 0.2 1 565 211 217 TRP CA C 55.76 0.2 1 566 211 217 TRP CB C 32.12 0.2 1 567 211 217 TRP N N 124.36 0.2 1 568 212 218 LYS H H 8.97 0.04 1 569 212 218 LYS C C 173.97 0.2 1 570 212 218 LYS CA C 54.62 0.2 1 571 212 218 LYS CB C 34.93 0.2 1 572 212 218 LYS N N 123.95 0.2 1 573 213 219 LEU H H 7.99 0.04 1 574 213 219 LEU C C 176.30 0.2 1 575 213 219 LEU CA C 54.45 0.2 1 576 213 219 LEU CB C 39.22 0.2 1 577 213 219 LEU N N 131.03 0.2 1 578 214 220 GLU H H 8.86 0.04 1 579 214 220 GLU C C 174.32 0.2 1 580 214 220 GLU CA C 54.06 0.2 1 581 214 220 GLU CB C 31.71 0.2 1 582 214 220 GLU N N 127.15 0.2 1 583 215 221 LYS H H 8.30 0.04 1 584 215 221 LYS C C 177.13 0.2 1 585 215 221 LYS CA C 55.27 0.2 1 586 215 221 LYS CB C 32.72 0.2 1 587 215 221 LYS N N 120.04 0.2 1 588 216 222 ASN H H 8.66 0.04 1 589 216 222 ASN C C 178.33 0.2 1 590 216 222 ASN CA C 50.71 0.2 1 591 216 222 ASN CB C 38.91 0.2 1 592 216 222 ASN N N 122.88 0.2 1 593 217 223 ASP H H 8.87 0.04 1 594 217 223 ASP C C 176.97 0.2 1 595 217 223 ASP CA C 56.61 0.2 1 596 217 223 ASP CB C 40.18 0.2 1 597 217 223 ASP N N 117.63 0.2 1 598 218 224 ALA H H 8.34 0.04 1 599 218 224 ALA CA C 51.33 0.2 1 600 218 224 ALA CB C 17.77 0.2 1 601 218 224 ALA N N 122.74 0.2 1 602 219 225 ASN H H 8.37 0.04 1 603 219 225 ASN CA C 54.51 0.2 1 604 219 225 ASN CB C 37.01 0.2 1 605 219 225 ASN N N 112.92 0.2 1 606 220 226 ASN H H 7.69 0.04 1 607 220 226 ASN C C 174.63 0.2 1 608 220 226 ASN CA C 51.59 0.2 1 609 220 226 ASN CB C 40.05 0.2 1 610 220 226 ASN N N 115.82 0.2 1 611 221 227 GLU H H 8.52 0.04 1 612 221 227 GLU C C 175.45 0.2 1 613 221 227 GLU CA C 55.61 0.2 1 614 221 227 GLU CB C 29.40 0.2 1 615 221 227 GLU N N 120.10 0.2 1 616 222 228 GLN H H 8.86 0.04 1 617 222 228 GLN C C 171.78 0.2 1 618 222 228 GLN CA C 53.72 0.2 1 619 222 228 GLN CB C 31.82 0.2 1 620 222 228 GLN N N 117.62 0.2 1 621 223 229 TRP H H 8.02 0.04 1 622 223 229 TRP C C 174.42 0.2 1 623 223 229 TRP CA C 55.46 0.2 1 624 223 229 TRP CB C 28.39 0.2 1 625 223 229 TRP N N 123.20 0.2 1 626 224 230 ASP H H 9.27 0.04 1 627 224 230 ASP C C 176.33 0.2 1 628 224 230 ASP CA C 51.76 0.2 1 629 224 230 ASP CB C 42.30 0.2 1 630 224 230 ASP N N 120.07 0.2 1 631 225 231 SER H H 8.54 0.04 1 632 225 231 SER C C 176.84 0.2 1 633 225 231 SER CA C 54.51 0.2 1 634 225 231 SER CB C 64.81 0.2 1 635 225 231 SER N N 118.43 0.2 1 636 226 232 LYS H H 8.45 0.04 1 637 226 232 LYS C C 177.47 0.2 1 638 226 232 LYS CA C 57.69 0.2 1 639 226 232 LYS CB C 30.47 0.2 1 640 226 232 LYS N N 124.60 0.2 1 641 227 233 SER H H 7.15 0.04 1 642 227 233 SER C C 172.90 0.2 1 643 227 233 SER CA C 57.30 0.2 1 644 227 233 SER CB C 61.30 0.2 1 645 227 233 SER N N 112.61 0.2 1 646 228 234 GLY H H 7.38 0.04 1 647 228 234 GLY C C 173.85 0.2 1 648 228 234 GLY CA C 44.01 0.2 1 649 228 234 GLY N N 106.23 0.2 1 650 229 235 TYR H H 6.04 0.04 1 651 229 235 TYR C C 174.20 0.2 1 652 229 235 TYR CA C 51.95 0.2 1 653 229 235 TYR CB C 38.32 0.2 1 654 229 235 TYR N N 119.58 0.2 1 655 230 236 MET H H 8.35 0.04 1 656 230 236 MET CA C 52.57 0.2 1 657 230 236 MET N N 123.38 0.2 1 658 231 237 MET H H 7.87 0.04 1 659 231 237 MET CA C 51.76 0.2 1 660 231 237 MET N N 111.83 0.2 1 661 237 243 SER H H 7.48 0.04 1 662 237 243 SER N N 113.56 0.2 1 663 238 244 LEU H H 6.98 0.04 1 664 238 244 LEU CA C 55.78 0.2 1 665 238 244 LEU N N 120.08 0.2 1 666 239 245 ILE H H 6.67 0.04 1 667 239 245 ILE C C 176.88 0.2 1 668 239 245 ILE CA C 59.22 0.2 1 669 239 245 ILE CB C 36.56 0.2 1 670 239 245 ILE N N 101.99 0.2 1 671 240 246 GLN H H 7.00 0.04 1 672 240 246 GLN C C 175.83 0.2 1 673 240 246 GLN CA C 55.72 0.2 1 674 240 246 GLN CB C 29.14 0.2 1 675 240 246 GLN N N 120.44 0.2 1 676 241 247 ASP H H 7.20 0.04 1 677 241 247 ASP C C 173.78 0.2 1 678 241 247 ASP CA C 50.41 0.2 1 679 241 247 ASP CB C 43.90 0.2 1 680 241 247 ASP N N 122.74 0.2 1 681 242 248 PRO C C 179.38 0.2 1 682 242 248 PRO CA C 64.56 0.2 1 683 242 248 PRO CB C 30.76 0.2 1 684 243 249 LYS H H 7.44 0.04 1 685 243 249 LYS C C 180.37 0.2 1 686 243 249 LYS CA C 58.20 0.2 1 687 243 249 LYS CB C 30.89 0.2 1 688 243 249 LYS N N 118.67 0.2 1 689 244 250 TYR H H 8.45 0.04 1 690 244 250 TYR C C 178.89 0.2 1 691 244 250 TYR CA C 57.15 0.2 1 692 244 250 TYR CB C 36.65 0.2 1 693 244 250 TYR N N 121.02 0.2 1 694 245 251 LEU H H 8.55 0.04 1 695 245 251 LEU C C 178.03 0.2 1 696 245 251 LEU CA C 57.82 0.2 1 697 245 251 LEU CB C 40.33 0.2 1 698 245 251 LEU N N 121.96 0.2 1 699 246 252 SER H H 6.90 0.04 1 700 246 252 SER C C 176.41 0.2 1 701 246 252 SER CA C 60.94 0.2 1 702 246 252 SER CB C 62.42 0.2 1 703 246 252 SER N N 109.86 0.2 1 704 247 253 ILE H H 7.08 0.04 1 705 247 253 ILE CA C 63.86 0.2 1 706 247 253 ILE CB C 37.15 0.2 1 707 247 253 ILE N N 123.33 0.2 1 708 248 254 VAL H H 8.15 0.04 1 709 248 254 VAL CA C 65.99 0.2 1 710 248 254 VAL CB C 30.25 0.2 1 711 248 254 VAL N N 121.94 0.2 1 712 249 255 LYS H H 7.76 0.04 1 713 249 255 LYS C C 178.82 0.2 1 714 249 255 LYS CA C 59.35 0.2 1 715 249 255 LYS CB C 31.67 0.2 1 716 249 255 LYS N N 115.21 0.2 1 717 250 256 GLU H H 6.93 0.04 1 718 250 256 GLU C C 179.94 0.2 1 719 250 256 GLU CA C 58.82 0.2 1 720 250 256 GLU CB C 28.95 0.2 1 721 250 256 GLU N N 120.11 0.2 1 722 251 257 TYR H H 7.37 0.04 1 723 251 257 TYR C C 178.47 0.2 1 724 251 257 TYR CA C 55.11 0.2 1 725 251 257 TYR CB C 34.86 0.2 1 726 251 257 TYR N N 119.47 0.2 1 727 252 258 ALA H H 8.09 0.04 1 728 252 258 ALA C C 177.33 0.2 1 729 252 258 ALA CA C 53.96 0.2 1 730 252 258 ALA CB C 17.51 0.2 1 731 252 258 ALA N N 121.28 0.2 1 732 253 259 ASN H H 6.94 0.04 1 733 253 259 ASN C C 174.82 0.2 1 734 253 259 ASN CA C 53.49 0.2 1 735 253 259 ASN CB C 39.53 0.2 1 736 253 259 ASN N N 112.00 0.2 1 737 254 260 ASP H H 7.39 0.04 1 738 254 260 ASP C C 174.04 0.2 1 739 254 260 ASP CA C 52.61 0.2 1 740 254 260 ASP CB C 41.01 0.2 1 741 254 260 ASP N N 120.10 0.2 1 742 255 261 GLN H H 8.91 0.04 1 743 255 261 GLN C C 176.72 0.2 1 744 255 261 GLN CA C 59.14 0.2 1 745 255 261 GLN CB C 29.43 0.2 1 746 255 261 GLN N N 125.71 0.2 1 747 256 262 ASP H H 8.01 0.04 1 748 256 262 ASP C C 178.46 0.2 1 749 256 262 ASP CA C 57.42 0.2 1 750 256 262 ASP CB C 40.25 0.2 1 751 256 262 ASP N N 118.73 0.2 1 752 257 263 LYS H H 7.53 0.04 1 753 257 263 LYS C C 178.06 0.2 1 754 257 263 LYS CA C 58.19 0.2 1 755 257 263 LYS CB C 31.30 0.2 1 756 257 263 LYS N N 121.94 0.2 1 757 258 264 PHE H H 7.28 0.04 1 758 258 264 PHE C C 176.01 0.2 1 759 258 264 PHE CA C 58.30 0.2 1 760 258 264 PHE CB C 36.79 0.2 1 761 258 264 PHE N N 118.38 0.2 1 762 259 265 PHE H H 8.90 0.04 1 763 259 265 PHE C C 178.38 0.2 1 764 259 265 PHE CA C 59.78 0.2 1 765 259 265 PHE CB C 36.67 0.2 1 766 259 265 PHE N N 121.04 0.2 1 767 260 266 LYS H H 7.91 0.04 1 768 260 266 LYS C C 179.97 0.2 1 769 260 266 LYS CA C 59.27 0.2 1 770 260 266 LYS CB C 31.72 0.2 1 771 260 266 LYS N N 118.96 0.2 1 772 261 267 ASP H H 8.41 0.04 1 773 261 267 ASP C C 180.14 0.2 1 774 261 267 ASP CA C 56.89 0.2 1 775 261 267 ASP CB C 38.45 0.2 1 776 261 267 ASP N N 121.85 0.2 1 777 262 268 PHE H H 9.91 0.04 1 778 262 268 PHE C C 176.77 0.2 1 779 262 268 PHE CA C 63.04 0.2 1 780 262 268 PHE CB C 38.45 0.2 1 781 262 268 PHE N N 123.67 0.2 1 782 263 269 SER H H 8.42 0.04 1 783 263 269 SER C C 176.72 0.2 1 784 263 269 SER CA C 61.53 0.2 1 785 263 269 SER CB C 62.51 0.2 1 786 263 269 SER N N 113.10 0.2 1 787 264 270 LYS H H 7.31 0.04 1 788 264 270 LYS C C 179.91 0.2 1 789 264 270 LYS CA C 58.73 0.2 1 790 264 270 LYS CB C 32.25 0.2 1 791 264 270 LYS N N 117.54 0.2 1 792 265 271 ALA H H 8.34 0.04 1 793 265 271 ALA CA C 55.19 0.2 1 794 265 271 ALA CB C 17.77 0.2 1 795 265 271 ALA N N 123.28 0.2 1 796 266 272 PHE H H 9.76 0.04 1 797 266 272 PHE CA C 60.34 0.2 1 798 266 272 PHE N N 120.71 0.2 1 799 267 273 GLU H H 8.17 0.04 1 800 267 273 GLU C C 177.50 0.2 1 801 267 273 GLU CA C 59.90 0.2 1 802 267 273 GLU CB C 25.86 0.2 1 803 267 273 GLU N N 117.85 0.2 1 804 268 274 LYS H H 7.82 0.04 1 805 268 274 LYS C C 179.22 0.2 1 806 268 274 LYS CA C 59.38 0.2 1 807 268 274 LYS CB C 32.35 0.2 1 808 268 274 LYS N N 119.05 0.2 1 809 269 275 LEU H H 8.68 0.04 1 810 269 275 LEU C C 179.88 0.2 1 811 269 275 LEU CA C 57.68 0.2 1 812 269 275 LEU CB C 42.38 0.2 1 813 269 275 LEU N N 120.12 0.2 1 814 271 277 GLU H H 7.77 0.04 1 815 271 277 GLU C C 176.23 0.2 1 816 271 277 GLU CA C 55.28 0.2 1 817 271 277 GLU CB C 29.46 0.2 1 818 271 277 GLU N N 120.01 0.2 1 819 272 278 ASN H H 7.27 0.04 1 820 272 278 ASN C C 176.51 0.2 1 821 272 278 ASN CA C 53.10 0.2 1 822 272 278 ASN CB C 36.86 0.2 1 823 272 278 ASN N N 123.22 0.2 1 824 273 279 GLY H H 8.36 0.04 1 825 273 279 GLY C C 174.65 0.2 1 826 273 279 GLY CA C 45.31 0.2 1 827 273 279 GLY N N 109.91 0.2 1 828 274 280 ILE H H 7.57 0.04 1 829 274 280 ILE C C 175.28 0.2 1 830 274 280 ILE CA C 61.01 0.2 1 831 274 280 ILE CB C 37.65 0.2 1 832 274 280 ILE N N 121.74 0.2 1 833 275 281 THR H H 8.73 0.04 1 834 275 281 THR C C 172.58 0.2 1 835 275 281 THR CA C 61.49 0.2 1 836 275 281 THR CB C 69.33 0.2 1 837 275 281 THR N N 125.02 0.2 1 838 276 282 PHE H H 9.15 0.04 1 839 276 282 PHE C C 173.76 0.2 1 840 276 282 PHE CA C 55.42 0.2 1 841 276 282 PHE CB C 38.03 0.2 1 842 276 282 PHE N N 129.30 0.2 1 843 277 283 PRO C C 177.15 0.2 1 844 277 283 PRO CA C 61.76 0.2 1 845 277 283 PRO CB C 32.27 0.2 1 846 278 284 LYS H H 8.79 0.04 1 847 278 284 LYS C C 176.90 0.2 1 848 278 284 LYS CA C 58.51 0.2 1 849 278 284 LYS CB C 31.16 0.2 1 850 278 284 LYS N N 121.58 0.2 1 851 279 285 ASP H H 8.15 0.04 1 852 279 285 ASP C C 175.83 0.2 1 853 279 285 ASP CA C 52.58 0.2 1 854 279 285 ASP CB C 38.98 0.2 1 855 279 285 ASP N N 114.84 0.2 1 856 280 286 ALA H H 7.51 0.04 1 857 280 286 ALA CA C 50.48 0.2 1 858 280 286 ALA CB C 16.88 0.2 1 859 280 286 ALA N N 124.10 0.2 1 860 281 287 PRO C C 176.97 0.2 1 861 281 287 PRO CA C 62.18 0.2 1 862 281 287 PRO CB C 30.67 0.2 1 863 282 288 SER H H 8.30 0.04 1 864 282 288 SER C C 170.86 0.2 1 865 282 288 SER CA C 57.79 0.2 1 866 282 288 SER CB C 60.90 0.2 1 867 282 288 SER N N 119.25 0.2 1 868 283 289 PRO C C 175.79 0.2 1 869 283 289 PRO CA C 63.07 0.2 1 870 283 289 PRO CB C 31.29 0.2 1 871 284 290 PHE H H 9.12 0.04 1 872 284 290 PHE C C 174.95 0.2 1 873 284 290 PHE CA C 53.86 0.2 1 874 284 290 PHE CB C 39.42 0.2 1 875 284 290 PHE N N 124.90 0.2 1 876 285 291 ILE H H 7.92 0.04 1 877 285 291 ILE C C 176.82 0.2 1 878 285 291 ILE CA C 58.82 0.2 1 879 285 291 ILE CB C 36.71 0.2 1 880 285 291 ILE N N 120.46 0.2 1 881 286 292 PHE H H 9.98 0.04 1 882 286 292 PHE C C 177.33 0.2 1 883 286 292 PHE CA C 58.96 0.2 1 884 286 292 PHE CB C 38.99 0.2 1 885 286 292 PHE N N 130.11 0.2 1 886 287 293 LYS H H 8.75 0.04 1 887 287 293 LYS C C 176.69 0.2 1 888 287 293 LYS CA C 54.90 0.2 1 889 287 293 LYS CB C 33.46 0.2 1 890 287 293 LYS N N 123.79 0.2 1 891 288 294 THR H H 8.62 0.04 1 892 288 294 THR C C 179.32 0.2 1 893 288 294 THR CA C 59.89 0.2 1 894 288 294 THR CB C 70.44 0.2 1 895 288 294 THR N N 109.65 0.2 1 896 289 295 LEU H H 9.60 0.04 1 897 289 295 LEU C C 180.66 0.2 1 898 289 295 LEU CA C 59.18 0.2 1 899 289 295 LEU CB C 39.06 0.2 1 900 289 295 LEU N N 122.57 0.2 1 901 290 296 GLU H H 8.92 0.04 1 902 290 296 GLU C C 181.19 0.2 1 903 290 296 GLU CA C 59.03 0.2 1 904 290 296 GLU CB C 28.65 0.2 1 905 290 296 GLU N N 120.17 0.2 1 stop_ save_