data_19005 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N backbone chemical shift assignments of the low-spin CN-bound yeast cytochrome c peroxidase with the N-terminal His-tag ; _BMRB_accession_number 19005 _BMRB_flat_file_name bmr19005.str _Entry_type original _Submission_date 2013-02-05 _Accession_date 2013-02-05 _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. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 261 "13C chemical shifts" 789 "15N chemical shifts" 261 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-07-29 update author 'update chemical shifts' 2013-04-02 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 19004 CcP(His)6CN stop_ save_ ############################# # Citation for this entry # ############################# save_citation1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Expression, Purification, Characterization, and Solution Nuclear Magnetic Resonance Study of Highly Deuterated Yeast Cytochrome c Peroxidase with Enhanced Solubility' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23517193 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Volkov Alexander N. . 2 Wohlkonig Alexandre . . 3 Soror Sameh H. . 4 'van Nuland' Nico AJ. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 52 _Journal_issue 13 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2165 _Page_last 2175 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name (His)6CcPCN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label protein $cytochrome_c_peroxidase cofactor_HEM $entity_HEM cofactor_CYN $entity_CYN 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 -6 MET 2 -5 HIS 3 -4 HIS 4 -3 HIS 5 -2 HIS 6 -1 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 19075 cytochrome_c_peroxidase 97.67 300 100.00 100.00 0.00e+00 BMRB 19076 cytochrome_c_peroxidase 100.00 300 100.00 100.00 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_HEM _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'PROTOPORPHYRIN IX CONTAINING FE' _BMRB_code HEM _PDB_code HEM _Molecular_mass 616.487 _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 . ? 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 . ? 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 . ? 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 . ? 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 . ? NA NA N . 0 . ? NB NB N . 0 . ? NC NC N . 0 . ? ND ND N . 0 . ? FE FE FE . 0 . ? HHB HHB H . 0 . ? HHC HHC H . 0 . ? HHD HHD H . 0 . ? HMA HMA H . 0 . ? HMAA HMAA H . 0 . ? HMAB HMAB H . 0 . ? HAA HAA H . 0 . ? HAAA HAAA H . 0 . ? HBA HBA H . 0 . ? HBAA HBAA H . 0 . ? HMB HMB H . 0 . ? HMBA HMBA H . 0 . ? HMBB HMBB H . 0 . ? HAB HAB H . 0 . ? HBB HBB H . 0 . ? HBBA HBBA H . 0 . ? HMC HMC H . 0 . ? HMCA HMCA H . 0 . ? HMCB HMCB H . 0 . ? HAC HAC H . 0 . ? HBC HBC H . 0 . ? HBCA HBCA H . 0 . ? HMD HMD H . 0 . ? HMDA HMDA H . 0 . ? HMDB HMDB H . 0 . ? HAD HAD H . 0 . ? HADA HADA H . 0 . ? HBD HBD H . 0 . ? HBDA HBDA H . 0 . ? H2A H2A H . 0 . ? H2D H2D H . 0 . ? HHA HHA 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 ? ? DOUB C1A C2A ? ? SING C1A NA ? ? SING C2A C3A ? ? SING C2A CAA ? ? DOUB C3A C4A ? ? SING C3A CMA ? ? SING C4A NA ? ? SING CMA HMA ? ? SING CMA HMAA ? ? SING CMA HMAB ? ? SING CAA CBA ? ? SING CAA HAA ? ? SING CAA HAAA ? ? SING CBA CGA ? ? SING CBA HBA ? ? SING CBA HBAA ? ? DOUB CGA O1A ? ? SING CGA O2A ? ? SING C1B C2B ? ? SING C1B NB ? ? DOUB C2B C3B ? ? SING C2B CMB ? ? SING C3B C4B ? ? SING C3B CAB ? ? DOUB C4B NB ? ? SING CMB HMB ? ? SING CMB HMBA ? ? SING CMB HMBB ? ? DOUB CAB CBB ? ? SING CAB HAB ? ? SING CBB HBB ? ? SING CBB HBBA ? ? SING C1C C2C ? ? SING C1C NC ? ? DOUB C2C C3C ? ? SING C2C CMC ? ? SING C3C C4C ? ? SING C3C CAC ? ? SING C4C NC ? ? SING CMC HMC ? ? SING CMC HMCA ? ? SING CMC HMCB ? ? DOUB CAC CBC ? ? SING CAC HAC ? ? SING CBC HBC ? ? SING CBC HBCA ? ? SING C1D C2D ? ? DOUB C1D ND ? ? DOUB C2D C3D ? ? SING C2D CMD ? ? SING C3D C4D ? ? SING C3D CAD ? ? SING C4D ND ? ? SING CMD HMD ? ? SING CMD HMDA ? ? SING CMD HMDB ? ? SING CAD CBD ? ? SING CAD HAD ? ? SING CAD HADA ? ? SING CBD CGD ? ? SING CBD HBD ? ? SING CBD HBDA ? ? DOUB CGD O1D ? ? SING CGD O2D ? ? SING O2A H2A ? ? SING O2D H2D ? ? SING FE NA ? ? SING FE NB ? ? SING FE NC ? ? SING FE ND ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ save_CYN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CYANIDE ION' _BMRB_code CYN _PDB_code CYN _Molecular_mass 26.017 _Mol_charge -1 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C C C . -1 . ? N N N . 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 TRIP C N ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $cytochrome_c_peroxidase . mM 1.25 1.5 '[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_ ############################ # Computer software used # ############################ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_CCPN _Saveframe_category software _Name CCPN _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . 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_ ####################### # 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' 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 protein _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 8 LYS H H 8.32 0.04 1 2 2 8 LYS C C 176.17 0.2 1 3 2 8 LYS CA C 55.82 0.2 1 4 2 8 LYS CB C 32.19 0.2 1 5 2 8 LYS N N 123.75 0.2 1 6 3 9 THR H H 8.13 0.04 1 7 3 9 THR C C 173.94 0.2 1 8 3 9 THR CA C 61.59 0.2 1 9 3 9 THR CB C 69.30 0.2 1 10 3 9 THR N N 118.03 0.2 1 11 4 10 LEU H H 8.14 0.04 1 12 4 10 LEU C C 175.96 0.2 1 13 4 10 LEU CA C 54.60 0.2 1 14 4 10 LEU CB C 41.41 0.2 1 15 4 10 LEU N N 126.72 0.2 1 16 5 11 VAL H H 8.11 0.04 1 17 5 11 VAL C C 174.55 0.2 1 18 5 11 VAL CA C 60.79 0.2 1 19 5 11 VAL CB C 33.01 0.2 1 20 5 11 VAL N N 124.03 0.2 1 21 6 12 HIS H H 8.66 0.04 1 22 6 12 HIS C C 172.39 0.2 1 23 6 12 HIS CA C 51.82 0.2 1 24 6 12 HIS CB C 27.11 0.2 1 25 6 12 HIS N N 125.06 0.2 1 26 7 13 VAL H H 8.82 0.04 1 27 7 13 VAL C C 177.91 0.2 1 28 7 13 VAL CA C 61.45 0.2 1 29 7 13 VAL CB C 31.22 0.2 1 30 7 13 VAL N N 124.82 0.2 1 31 8 14 ALA H H 8.49 0.04 1 32 8 14 ALA C C 176.98 0.2 1 33 8 14 ALA CA C 52.32 0.2 1 34 8 14 ALA CB C 19.54 0.2 1 35 8 14 ALA N N 135.53 0.2 1 36 9 15 SER H H 9.47 0.04 1 37 9 15 SER CA C 55.73 0.2 1 38 9 15 SER CB C 63.52 0.2 1 39 9 15 SER N N 120.32 0.2 1 40 10 16 VAL C C 180.78 0.2 1 41 10 16 VAL CA C 59.00 0.2 1 42 10 16 VAL CB C 28.54 0.2 1 43 11 17 GLU C C 176.69 0.2 1 44 12 18 LYS H H 8.21 0.04 1 45 12 18 LYS C C 178.61 0.2 1 46 12 18 LYS CA C 58.05 0.2 1 47 12 18 LYS CB C 31.41 0.2 1 48 12 18 LYS N N 123.71 0.2 1 49 13 19 GLY H H 8.82 0.04 1 50 13 19 GLY CA C 45.09 0.2 1 51 13 19 GLY N N 112.91 0.2 1 52 14 20 ARG H H 7.64 0.04 1 53 14 20 ARG C C 175.52 0.2 1 54 14 20 ARG CA C 52.81 0.2 1 55 14 20 ARG CB C 29.06 0.2 1 56 14 20 ARG N N 119.12 0.2 1 57 15 21 SER H H 9.33 0.04 1 58 15 21 SER C C 174.35 0.2 1 59 15 21 SER CA C 56.47 0.2 1 60 15 21 SER CB C 65.92 0.2 1 61 15 21 SER N N 118.93 0.2 1 62 16 22 TYR H H 8.89 0.04 1 63 16 22 TYR C C 176.08 0.2 1 64 16 22 TYR CA C 61.32 0.2 1 65 16 22 TYR CB C 37.73 0.2 1 66 16 22 TYR N N 122.07 0.2 1 67 17 23 GLU H H 8.78 0.04 1 68 17 23 GLU C C 179.00 0.2 1 69 17 23 GLU CA C 59.50 0.2 1 70 17 23 GLU CB C 28.17 0.2 1 71 17 23 GLU N N 117.15 0.2 1 72 18 24 ASP H H 7.50 0.04 1 73 18 24 ASP C C 177.98 0.2 1 74 18 24 ASP CA C 57.42 0.2 1 75 18 24 ASP CB C 41.24 0.2 1 76 18 24 ASP N N 117.74 0.2 1 77 19 25 PHE H H 7.40 0.04 1 78 19 25 PHE C C 177.37 0.2 1 79 19 25 PHE CA C 62.31 0.2 1 80 19 25 PHE CB C 38.69 0.2 1 81 19 25 PHE N N 115.96 0.2 1 82 20 26 GLN H H 8.77 0.04 1 83 20 26 GLN C C 177.69 0.2 1 84 20 26 GLN CA C 57.34 0.2 1 85 20 26 GLN CB C 27.00 0.2 1 86 20 26 GLN N N 121.85 0.2 1 87 21 27 LYS H H 7.31 0.04 1 88 21 27 LYS C C 178.85 0.2 1 89 21 27 LYS CA C 59.67 0.2 1 90 21 27 LYS CB C 31.20 0.2 1 91 21 27 LYS N N 119.37 0.2 1 92 22 28 VAL H H 6.77 0.04 1 93 22 28 VAL CA C 65.37 0.2 1 94 22 28 VAL CB C 29.05 0.2 1 95 22 28 VAL N N 121.94 0.2 1 96 23 29 TYR C C 177.35 0.2 1 97 24 30 ASN H H 8.62 0.04 1 98 24 30 ASN C C 176.75 0.2 1 99 24 30 ASN CA C 54.89 0.2 1 100 24 30 ASN CB C 36.20 0.2 1 101 24 30 ASN N N 117.45 0.2 1 102 25 31 ALA H H 7.73 0.04 1 103 25 31 ALA CA C 54.82 0.2 1 104 25 31 ALA CB C 18.36 0.2 1 105 25 31 ALA N N 123.03 0.2 1 106 26 32 ILE C C 176.81 0.2 1 107 27 33 ALA H H 8.91 0.04 1 108 27 33 ALA C C 180.43 0.2 1 109 27 33 ALA CA C 54.69 0.2 1 110 27 33 ALA CB C 18.21 0.2 1 111 27 33 ALA N N 122.07 0.2 1 112 28 34 LEU H H 9.14 0.04 1 113 28 34 LEU C C 179.41 0.2 1 114 28 34 LEU CA C 57.25 0.2 1 115 28 34 LEU CB C 40.54 0.2 1 116 28 34 LEU N N 121.44 0.2 1 117 29 35 LYS H H 7.39 0.04 1 118 29 35 LYS C C 178.38 0.2 1 119 29 35 LYS CA C 59.22 0.2 1 120 29 35 LYS CB C 30.72 0.2 1 121 29 35 LYS N N 123.11 0.2 1 122 30 36 LEU H H 8.45 0.04 1 123 30 36 LEU C C 179.76 0.2 1 124 30 36 LEU CA C 56.67 0.2 1 125 30 36 LEU CB C 41.16 0.2 1 126 30 36 LEU N N 120.20 0.2 1 127 31 37 ARG H H 7.22 0.04 1 128 31 37 ARG C C 177.48 0.2 1 129 31 37 ARG CA C 57.96 0.2 1 130 31 37 ARG CB C 30.61 0.2 1 131 31 37 ARG N N 117.25 0.2 1 132 32 38 GLU H H 7.70 0.04 1 133 32 38 GLU C C 177.66 0.2 1 134 32 38 GLU CA C 57.98 0.2 1 135 32 38 GLU CB C 29.94 0.2 1 136 32 38 GLU N N 118.02 0.2 1 137 33 39 ASP H H 8.45 0.04 1 138 33 39 ASP CA C 52.60 0.2 1 139 33 39 ASP CB C 37.97 0.2 1 140 33 39 ASP N N 123.17 0.2 1 141 35 41 GLU C C 176.99 0.2 1 142 35 41 GLU CA C 56.38 0.2 1 143 35 41 GLU CB C 28.65 0.2 1 144 36 42 TYR H H 6.54 0.04 1 145 36 42 TYR C C 173.74 0.2 1 146 36 42 TYR CA C 58.25 0.2 1 147 36 42 TYR CB C 39.80 0.2 1 148 36 42 TYR N N 120.95 0.2 1 149 37 43 ASP H H 7.68 0.04 1 150 37 43 ASP C C 175.09 0.2 1 151 37 43 ASP CA C 52.72 0.2 1 152 37 43 ASP CB C 37.77 0.2 1 153 37 43 ASP N N 127.58 0.2 1 154 38 44 ASN H H 8.08 0.04 1 155 38 44 ASN C C 174.60 0.2 1 156 38 44 ASN CA C 54.14 0.2 1 157 38 44 ASN CB C 36.33 0.2 1 158 38 44 ASN N N 114.63 0.2 1 159 39 45 TYR H H 7.09 0.04 1 160 39 45 TYR CA C 59.75 0.2 1 161 39 45 TYR CB C 32.58 0.2 1 162 39 45 TYR N N 108.62 0.2 1 163 40 46 ILE C C 178.45 0.2 1 164 41 47 GLY H H 8.12 0.04 1 165 41 47 GLY C C 172.88 0.2 1 166 41 47 GLY CA C 43.84 0.2 1 167 41 47 GLY N N 106.93 0.2 1 168 42 48 TYR H H 9.03 0.04 1 169 42 48 TYR C C 174.50 0.2 1 170 42 48 TYR CA C 59.47 0.2 1 171 42 48 TYR CB C 38.23 0.2 1 172 42 48 TYR N N 115.36 0.2 1 173 43 49 GLY H H 8.85 0.04 1 174 43 49 GLY CA C 47.69 0.2 1 175 43 49 GLY N N 108.54 0.2 1 176 45 51 VAL C C 176.72 0.2 1 177 45 51 VAL CA C 64.66 0.2 1 178 45 51 VAL CB C 28.97 0.2 1 179 46 52 LEU H H 7.16 0.04 1 180 46 52 LEU C C 181.01 0.2 1 181 46 52 LEU CA C 57.10 0.2 1 182 46 52 LEU CB C 39.63 0.2 1 183 46 52 LEU N N 121.79 0.2 1 184 47 53 VAL H H 7.05 0.04 1 185 47 53 VAL C C 176.70 0.2 1 186 47 53 VAL CA C 66.49 0.2 1 187 47 53 VAL CB C 28.99 0.2 1 188 47 53 VAL N N 121.95 0.2 1 189 48 54 ARG H H 6.76 0.04 1 190 48 54 ARG C C 177.89 0.2 1 191 48 54 ARG CA C 58.94 0.2 1 192 48 54 ARG CB C 28.41 0.2 1 193 48 54 ARG N N 120.00 0.2 1 194 49 55 LEU H H 8.57 0.04 1 195 49 55 LEU C C 179.34 0.2 1 196 49 55 LEU CA C 58.71 0.2 1 197 49 55 LEU CB C 40.26 0.2 1 198 49 55 LEU N N 122.02 0.2 1 199 50 56 ALA H H 7.76 0.04 1 200 50 56 ALA C C 179.25 0.2 1 201 50 56 ALA CA C 54.92 0.2 1 202 50 56 ALA CB C 17.36 0.2 1 203 50 56 ALA N N 123.99 0.2 1 204 51 57 TRP H H 7.70 0.04 1 205 51 57 TRP C C 177.40 0.2 1 206 51 57 TRP CA C 58.71 0.2 1 207 51 57 TRP CB C 28.74 0.2 1 208 51 57 TRP N N 121.02 0.2 1 209 52 58 HIS H H 9.88 0.04 1 210 52 58 HIS C C 177.23 0.2 1 211 52 58 HIS CA C 59.97 0.2 1 212 52 58 HIS CB C 28.42 0.2 1 213 52 58 HIS N N 120.96 0.2 1 214 53 59 THR H H 8.19 0.04 1 215 53 59 THR C C 175.52 0.2 1 216 53 59 THR CA C 63.74 0.2 1 217 53 59 THR CB C 69.27 0.2 1 218 53 59 THR N N 107.81 0.2 1 219 54 60 SER H H 6.89 0.04 1 220 54 60 SER C C 177.39 0.2 1 221 54 60 SER CA C 60.43 0.2 1 222 54 60 SER CB C 63.36 0.2 1 223 54 60 SER N N 113.91 0.2 1 224 55 61 GLY H H 8.83 0.04 1 225 55 61 GLY C C 169.74 0.2 1 226 55 61 GLY CA C 45.83 0.2 1 227 55 61 GLY N N 113.03 0.2 1 228 56 62 THR H H 6.51 0.04 1 229 56 62 THR C C 173.77 0.2 1 230 56 62 THR CA C 60.48 0.2 1 231 56 62 THR CB C 70.01 0.2 1 232 56 62 THR N N 103.68 0.2 1 233 57 63 TRP H H 7.00 0.04 1 234 57 63 TRP C C 173.70 0.2 1 235 57 63 TRP CA C 58.80 0.2 1 236 57 63 TRP CB C 27.69 0.2 1 237 57 63 TRP N N 121.99 0.2 1 238 58 64 ASP H H 7.42 0.04 1 239 58 64 ASP C C 174.96 0.2 1 240 58 64 ASP CA C 52.10 0.2 1 241 58 64 ASP CB C 42.17 0.2 1 242 58 64 ASP N N 126.03 0.2 1 243 59 65 LYS H H 6.65 0.04 1 244 59 65 LYS C C 177.12 0.2 1 245 59 65 LYS CA C 56.42 0.2 1 246 59 65 LYS CB C 31.24 0.2 1 247 59 65 LYS N N 122.59 0.2 1 248 60 66 HIS H H 8.72 0.04 1 249 60 66 HIS C C 175.76 0.2 1 250 60 66 HIS CA C 58.56 0.2 1 251 60 66 HIS CB C 27.59 0.2 1 252 60 66 HIS N N 119.43 0.2 1 253 61 67 ASP H H 6.82 0.04 1 254 61 67 ASP C C 176.10 0.2 1 255 61 67 ASP CA C 51.94 0.2 1 256 61 67 ASP CB C 40.99 0.2 1 257 61 67 ASP N N 114.14 0.2 1 258 62 68 ASN H H 8.28 0.04 1 259 62 68 ASN C C 174.47 0.2 1 260 62 68 ASN CA C 53.20 0.2 1 261 62 68 ASN CB C 38.13 0.2 1 262 62 68 ASN N N 117.67 0.2 1 263 63 69 THR H H 7.64 0.04 1 264 63 69 THR C C 175.81 0.2 1 265 63 69 THR CA C 60.63 0.2 1 266 63 69 THR CB C 71.67 0.2 1 267 63 69 THR N N 108.39 0.2 1 268 64 70 GLY H H 8.58 0.04 1 269 64 70 GLY C C 176.11 0.2 1 270 64 70 GLY CA C 44.57 0.2 1 271 64 70 GLY N N 105.54 0.2 1 272 65 71 GLY H H 8.22 0.04 1 273 65 71 GLY C C 173.26 0.2 1 274 65 71 GLY CA C 43.91 0.2 1 275 65 71 GLY N N 107.78 0.2 1 276 66 72 SER H H 8.67 0.04 1 277 66 72 SER C C 177.71 0.2 1 278 66 72 SER CA C 59.85 0.2 1 279 66 72 SER CB C 63.69 0.2 1 280 66 72 SER N N 112.05 0.2 1 281 67 73 TYR H H 8.48 0.04 1 282 67 73 TYR C C 175.53 0.2 1 283 67 73 TYR CA C 62.63 0.2 1 284 67 73 TYR CB C 37.42 0.2 1 285 67 73 TYR N N 122.58 0.2 1 286 68 74 GLY H H 8.53 0.04 1 287 68 74 GLY C C 176.22 0.2 1 288 68 74 GLY CA C 46.19 0.2 1 289 68 74 GLY N N 99.16 0.2 1 290 69 75 GLY H H 7.88 0.04 1 291 69 75 GLY C C 178.01 0.2 1 292 69 75 GLY CA C 47.19 0.2 1 293 69 75 GLY N N 109.84 0.2 1 294 70 76 THR H H 7.89 0.04 1 295 70 76 THR C C 174.59 0.2 1 296 70 76 THR CA C 64.48 0.2 1 297 70 76 THR CB C 67.36 0.2 1 298 70 76 THR N N 112.41 0.2 1 299 71 77 TYR H H 8.56 0.04 1 300 71 77 TYR C C 171.38 0.2 1 301 71 77 TYR CA C 59.85 0.2 1 302 71 77 TYR CB C 39.07 0.2 1 303 71 77 TYR N N 124.68 0.2 1 304 72 78 ARG H H 7.00 0.04 1 305 72 78 ARG C C 176.39 0.2 1 306 72 78 ARG CA C 55.91 0.2 1 307 72 78 ARG CB C 28.71 0.2 1 308 72 78 ARG N N 108.47 0.2 1 309 73 79 PHE H H 8.42 0.04 1 310 73 79 PHE C C 176.81 0.2 1 311 73 79 PHE CA C 57.47 0.2 1 312 73 79 PHE CB C 38.11 0.2 1 313 73 79 PHE N N 123.68 0.2 1 314 74 80 LYS H H 8.97 0.04 1 315 74 80 LYS C C 177.33 0.2 1 316 74 80 LYS CA C 59.15 0.2 1 317 74 80 LYS CB C 31.82 0.2 1 318 74 80 LYS N N 122.44 0.2 1 319 75 81 LYS H H 8.78 0.04 1 320 75 81 LYS C C 177.89 0.2 1 321 75 81 LYS CA C 59.88 0.2 1 322 75 81 LYS CB C 31.82 0.2 1 323 75 81 LYS N N 117.84 0.2 1 324 76 82 GLU H H 6.90 0.04 1 325 76 82 GLU C C 179.77 0.2 1 326 76 82 GLU CA C 57.91 0.2 1 327 76 82 GLU CB C 30.29 0.2 1 328 76 82 GLU N N 119.16 0.2 1 329 77 83 PHE H H 8.82 0.04 1 330 77 83 PHE C C 178.22 0.2 1 331 77 83 PHE CA C 61.07 0.2 1 332 77 83 PHE CB C 38.00 0.2 1 333 77 83 PHE N N 125.52 0.2 1 334 78 84 ASN H H 8.19 0.04 1 335 78 84 ASN C C 174.92 0.2 1 336 78 84 ASN CA C 52.78 0.2 1 337 78 84 ASN CB C 38.13 0.2 1 338 78 84 ASN N N 112.59 0.2 1 339 79 85 ASP H H 7.76 0.04 1 340 79 85 ASP CA C 53.10 0.2 1 341 79 85 ASP CB C 42.38 0.2 1 342 79 85 ASP N N 124.81 0.2 1 343 80 86 PRO C C 181.02 0.2 1 344 80 86 PRO CA C 65.90 0.2 1 345 80 86 PRO CB C 31.58 0.2 1 346 81 87 SER H H 9.44 0.04 1 347 81 87 SER C C 175.17 0.2 1 348 81 87 SER CA C 62.25 0.2 1 349 81 87 SER CB C 63.84 0.2 1 350 81 87 SER N N 115.94 0.2 1 351 82 88 ASN H H 9.59 0.04 1 352 82 88 ASN C C 176.87 0.2 1 353 82 88 ASN CA C 52.63 0.2 1 354 82 88 ASN CB C 38.99 0.2 1 355 82 88 ASN N N 115.85 0.2 1 356 83 89 ALA H H 8.48 0.04 1 357 83 89 ALA C C 178.93 0.2 1 358 83 89 ALA CA C 55.90 0.2 1 359 83 89 ALA CB C 18.52 0.2 1 360 83 89 ALA N N 128.66 0.2 1 361 84 90 GLY H H 9.14 0.04 1 362 84 90 GLY C C 176.64 0.2 1 363 84 90 GLY CA C 45.23 0.2 1 364 84 90 GLY N N 115.32 0.2 1 365 85 91 LEU H H 8.77 0.04 1 366 85 91 LEU C C 178.60 0.2 1 367 85 91 LEU CA C 56.82 0.2 1 368 85 91 LEU CB C 40.25 0.2 1 369 85 91 LEU N N 119.90 0.2 1 370 86 92 GLN H H 10.09 0.04 1 371 86 92 GLN C C 178.62 0.2 1 372 86 92 GLN CA C 59.19 0.2 1 373 86 92 GLN CB C 26.15 0.2 1 374 86 92 GLN N N 123.00 0.2 1 375 87 93 ASN H H 7.61 0.04 1 376 87 93 ASN C C 178.34 0.2 1 377 87 93 ASN CA C 56.10 0.2 1 378 87 93 ASN CB C 38.06 0.2 1 379 87 93 ASN N N 116.56 0.2 1 380 88 94 GLY H H 7.66 0.04 1 381 88 94 GLY C C 173.68 0.2 1 382 88 94 GLY CA C 46.47 0.2 1 383 88 94 GLY N N 107.36 0.2 1 384 89 95 PHE H H 8.22 0.04 1 385 89 95 PHE C C 177.64 0.2 1 386 89 95 PHE CA C 62.06 0.2 1 387 89 95 PHE CB C 39.42 0.2 1 388 89 95 PHE N N 123.19 0.2 1 389 90 96 LYS H H 8.60 0.04 1 390 90 96 LYS C C 178.98 0.2 1 391 90 96 LYS CA C 58.38 0.2 1 392 90 96 LYS CB C 31.26 0.2 1 393 90 96 LYS N N 117.91 0.2 1 394 91 97 PHE H H 7.12 0.04 1 395 91 97 PHE C C 175.62 0.2 1 396 91 97 PHE CA C 60.40 0.2 1 397 91 97 PHE CB C 37.70 0.2 1 398 91 97 PHE N N 121.12 0.2 1 399 92 98 LEU H H 7.16 0.04 1 400 92 98 LEU C C 178.51 0.2 1 401 92 98 LEU CA C 55.09 0.2 1 402 92 98 LEU CB C 41.88 0.2 1 403 92 98 LEU N N 114.08 0.2 1 404 93 99 GLU H H 7.67 0.04 1 405 93 99 GLU CA C 61.41 0.2 1 406 93 99 GLU CB C 26.70 0.2 1 407 93 99 GLU N N 122.91 0.2 1 408 94 100 PRO C C 179.86 0.2 1 409 94 100 PRO CA C 64.93 0.2 1 410 94 100 PRO CB C 29.89 0.2 1 411 95 101 ILE H H 6.61 0.04 1 412 95 101 ILE CA C 63.03 0.2 1 413 95 101 ILE CB C 35.51 0.2 1 414 95 101 ILE N N 119.26 0.2 1 415 96 102 HIS H H 8.16 0.04 1 416 96 102 HIS C C 177.76 0.2 1 417 96 102 HIS CA C 55.40 0.2 1 418 96 102 HIS CB C 29.06 0.2 1 419 96 102 HIS N N 121.43 0.2 1 420 97 103 LYS H H 7.58 0.04 1 421 97 103 LYS C C 177.89 0.2 1 422 97 103 LYS CA C 58.01 0.2 1 423 97 103 LYS CB C 31.17 0.2 1 424 97 103 LYS N N 115.10 0.2 1 425 98 104 GLU H H 7.04 0.04 1 426 98 104 GLU C C 175.75 0.2 1 427 98 104 GLU CA C 57.30 0.2 1 428 98 104 GLU CB C 28.65 0.2 1 429 98 104 GLU N N 119.32 0.2 1 430 99 105 PHE H H 7.35 0.04 1 431 99 105 PHE CA C 53.64 0.2 1 432 99 105 PHE CB C 37.20 0.2 1 433 99 105 PHE N N 116.83 0.2 1 434 103 109 SER C C 175.08 0.2 1 435 103 109 SER CA C 57.30 0.2 1 436 103 109 SER CB C 64.46 0.2 1 437 104 110 SER H H 10.22 0.04 1 438 104 110 SER C C 174.49 0.2 1 439 104 110 SER CA C 63.40 0.2 1 440 104 110 SER CB C 61.55 0.2 1 441 104 110 SER N N 120.66 0.2 1 442 105 111 GLY H H 9.56 0.04 1 443 105 111 GLY C C 179.03 0.2 1 444 105 111 GLY CA C 45.94 0.2 1 445 105 111 GLY N N 109.16 0.2 1 446 106 112 ASP H H 7.66 0.04 1 447 106 112 ASP C C 176.23 0.2 1 448 106 112 ASP CA C 57.85 0.2 1 449 106 112 ASP CB C 38.34 0.2 1 450 106 112 ASP N N 124.90 0.2 1 451 107 113 LEU H H 7.91 0.04 1 452 107 113 LEU C C 178.11 0.2 1 453 107 113 LEU CA C 58.02 0.2 1 454 107 113 LEU CB C 39.99 0.2 1 455 107 113 LEU N N 122.17 0.2 1 456 108 114 PHE H H 8.74 0.04 1 457 108 114 PHE C C 179.34 0.2 1 458 108 114 PHE CA C 57.19 0.2 1 459 108 114 PHE CB C 37.17 0.2 1 460 108 114 PHE N N 116.05 0.2 1 461 109 115 SER H H 7.88 0.04 1 462 109 115 SER C C 175.88 0.2 1 463 109 115 SER CA C 61.20 0.2 1 464 109 115 SER CB C 63.01 0.2 1 465 109 115 SER N N 112.44 0.2 1 466 110 116 LEU H H 8.61 0.04 1 467 110 116 LEU C C 180.58 0.2 1 468 110 116 LEU CA C 56.92 0.2 1 469 110 116 LEU CB C 40.40 0.2 1 470 110 116 LEU N N 127.42 0.2 1 471 111 117 GLY H H 8.65 0.04 1 472 111 117 GLY C C 174.36 0.2 1 473 111 117 GLY CA C 47.38 0.2 1 474 111 117 GLY N N 108.79 0.2 1 475 112 118 GLY H H 6.90 0.04 1 476 112 118 GLY C C 173.93 0.2 1 477 112 118 GLY CA C 46.61 0.2 1 478 112 118 GLY N N 104.86 0.2 1 479 113 119 VAL H H 7.29 0.04 1 480 113 119 VAL C C 176.58 0.2 1 481 113 119 VAL CA C 67.15 0.2 1 482 113 119 VAL CB C 31.62 0.2 1 483 113 119 VAL N N 121.87 0.2 1 484 114 120 THR H H 8.45 0.04 1 485 114 120 THR C C 175.56 0.2 1 486 114 120 THR CA C 65.73 0.2 1 487 114 120 THR CB C 67.75 0.2 1 488 114 120 THR N N 115.43 0.2 1 489 115 121 ALA H H 7.40 0.04 1 490 115 121 ALA C C 177.98 0.2 1 491 115 121 ALA CA C 55.24 0.2 1 492 115 121 ALA CB C 18.51 0.2 1 493 115 121 ALA N N 120.71 0.2 1 494 116 122 VAL H H 7.40 0.04 1 495 116 122 VAL C C 178.41 0.2 1 496 116 122 VAL CA C 67.59 0.2 1 497 116 122 VAL CB C 30.44 0.2 1 498 116 122 VAL N N 114.84 0.2 1 499 117 123 GLN H H 7.80 0.04 1 500 117 123 GLN C C 181.12 0.2 1 501 117 123 GLN CA C 59.19 0.2 1 502 117 123 GLN CB C 27.43 0.2 1 503 117 123 GLN N N 114.68 0.2 1 504 118 124 GLU H H 8.92 0.04 1 505 118 124 GLU C C 178.09 0.2 1 506 118 124 GLU CA C 57.77 0.2 1 507 118 124 GLU CB C 28.15 0.2 1 508 118 124 GLU N N 119.42 0.2 1 509 119 125 MET H H 7.39 0.04 1 510 119 125 MET C C 173.47 0.2 1 511 119 125 MET CA C 56.07 0.2 1 512 119 125 MET CB C 30.87 0.2 1 513 119 125 MET N N 119.76 0.2 1 514 120 126 GLN H H 7.41 0.04 1 515 120 126 GLN C C 176.10 0.2 1 516 120 126 GLN CA C 57.13 0.2 1 517 120 126 GLN CB C 24.22 0.2 1 518 120 126 GLN N N 108.99 0.2 1 519 121 127 GLY H H 8.01 0.04 1 520 121 127 GLY CA C 44.34 0.2 1 521 121 127 GLY N N 105.77 0.2 1 522 125 131 PRO C C 175.78 0.2 1 523 125 131 PRO CA C 61.87 0.2 1 524 125 131 PRO CB C 29.99 0.2 1 525 126 132 TRP H H 9.02 0.04 1 526 126 132 TRP C C 173.35 0.2 1 527 126 132 TRP CA C 56.57 0.2 1 528 126 132 TRP CB C 31.74 0.2 1 529 126 132 TRP N N 124.75 0.2 1 530 127 133 ARG H H 7.91 0.04 1 531 127 133 ARG C C 172.35 0.2 1 532 127 133 ARG CA C 52.83 0.2 1 533 127 133 ARG CB C 33.12 0.2 1 534 127 133 ARG N N 126.50 0.2 1 535 128 134 CYS H H 6.22 0.04 1 536 128 134 CYS C C 173.37 0.2 1 537 128 134 CYS CA C 53.45 0.2 1 538 128 134 CYS CB C 31.75 0.2 1 539 128 134 CYS N N 113.61 0.2 1 540 129 135 GLY H H 10.15 0.04 1 541 129 135 GLY CA C 44.65 0.2 1 542 129 135 GLY N N 107.44 0.2 1 543 131 137 VAL C C 172.24 0.2 1 544 131 137 VAL CA C 60.62 0.2 1 545 131 137 VAL CB C 33.83 0.2 1 546 132 138 ASP H H 8.16 0.04 1 547 132 138 ASP C C 177.76 0.2 1 548 132 138 ASP CA C 54.65 0.2 1 549 132 138 ASP CB C 38.28 0.2 1 550 132 138 ASP N N 124.13 0.2 1 551 133 139 THR H H 8.72 0.04 1 552 133 139 THR CA C 59.33 0.2 1 553 133 139 THR CB C 67.84 0.2 1 554 133 139 THR N N 117.07 0.2 1 555 134 140 PRO C C 177.77 0.2 1 556 134 140 PRO CA C 62.84 0.2 1 557 134 140 PRO CB C 32.26 0.2 1 558 135 141 GLU H H 8.74 0.04 1 559 135 141 GLU C C 178.91 0.2 1 560 135 141 GLU CA C 59.84 0.2 1 561 135 141 GLU CB C 28.37 0.2 1 562 135 141 GLU N N 124.37 0.2 1 563 136 142 ASP H H 8.55 0.04 1 564 136 142 ASP C C 176.64 0.2 1 565 136 142 ASP CA C 55.23 0.2 1 566 136 142 ASP CB C 38.71 0.2 1 567 136 142 ASP N N 117.91 0.2 1 568 137 143 THR H H 8.06 0.04 1 569 137 143 THR C C 174.64 0.2 1 570 137 143 THR CA C 61.88 0.2 1 571 137 143 THR CB C 69.75 0.2 1 572 137 143 THR N N 110.60 0.2 1 573 138 144 THR H H 7.65 0.04 1 574 138 144 THR CA C 61.97 0.2 1 575 138 144 THR CB C 68.91 0.2 1 576 138 144 THR N N 123.96 0.2 1 577 139 145 PRO C C 176.18 0.2 1 578 139 145 PRO CA C 62.24 0.2 1 579 139 145 PRO CB C 30.62 0.2 1 580 140 146 ASP H H 8.40 0.04 1 581 140 146 ASP C C 176.24 0.2 1 582 140 146 ASP CA C 54.33 0.2 1 583 140 146 ASP CB C 40.11 0.2 1 584 140 146 ASP N N 120.10 0.2 1 585 141 147 ASN H H 8.88 0.04 1 586 141 147 ASN C C 175.14 0.2 1 587 141 147 ASN CA C 53.64 0.2 1 588 141 147 ASN CB C 39.05 0.2 1 589 141 147 ASN N N 117.69 0.2 1 590 142 148 GLY H H 8.60 0.04 1 591 142 148 GLY C C 176.35 0.2 1 592 142 148 GLY CA C 45.25 0.2 1 593 142 148 GLY N N 110.96 0.2 1 594 143 149 ARG H H 9.21 0.04 1 595 143 149 ARG C C 176.30 0.2 1 596 143 149 ARG CA C 56.35 0.2 1 597 143 149 ARG CB C 30.07 0.2 1 598 143 149 ARG N N 120.25 0.2 1 599 144 150 LEU H H 8.16 0.04 1 600 144 150 LEU CA C 52.12 0.2 1 601 144 150 LEU CB C 38.13 0.2 1 602 144 150 LEU N N 121.50 0.2 1 603 145 151 PRO C C 175.96 0.2 1 604 145 151 PRO CA C 62.61 0.2 1 605 145 151 PRO CB C 28.90 0.2 1 606 146 152 ASP H H 7.53 0.04 1 607 146 152 ASP C C 172.99 0.2 1 608 146 152 ASP CA C 52.84 0.2 1 609 146 152 ASP CB C 42.50 0.2 1 610 146 152 ASP N N 121.02 0.2 1 611 147 153 ALA H H 7.56 0.04 1 612 147 153 ALA C C 176.51 0.2 1 613 147 153 ALA CA C 50.86 0.2 1 614 147 153 ALA CB C 20.47 0.2 1 615 147 153 ALA N N 116.13 0.2 1 616 148 154 ASP H H 8.01 0.04 1 617 148 154 ASP C C 176.08 0.2 1 618 148 154 ASP CA C 52.24 0.2 1 619 148 154 ASP CB C 38.80 0.2 1 620 148 154 ASP N N 115.56 0.2 1 621 149 155 LYS H H 5.78 0.04 1 622 149 155 LYS C C 172.49 0.2 1 623 149 155 LYS CA C 53.18 0.2 1 624 149 155 LYS CB C 34.63 0.2 1 625 149 155 LYS N N 118.07 0.2 1 626 150 156 ASP H H 6.80 0.04 1 627 150 156 ASP C C 176.25 0.2 1 628 150 156 ASP CA C 51.16 0.2 1 629 150 156 ASP CB C 42.28 0.2 1 630 150 156 ASP N N 115.87 0.2 1 631 151 157 ALA H H 8.38 0.04 1 632 151 157 ALA C C 179.08 0.2 1 633 151 157 ALA CA C 55.05 0.2 1 634 151 157 ALA CB C 18.76 0.2 1 635 151 157 ALA N N 119.64 0.2 1 636 152 158 ASP H H 7.64 0.04 1 637 152 158 ASP C C 178.96 0.2 1 638 152 158 ASP CA C 56.72 0.2 1 639 152 158 ASP CB C 39.94 0.2 1 640 152 158 ASP N N 115.32 0.2 1 641 153 159 TYR H H 7.68 0.04 1 642 153 159 TYR C C 176.82 0.2 1 643 153 159 TYR CA C 60.99 0.2 1 644 153 159 TYR CB C 37.15 0.2 1 645 153 159 TYR N N 121.72 0.2 1 646 154 160 VAL H H 7.90 0.04 1 647 154 160 VAL C C 176.92 0.2 1 648 154 160 VAL CA C 67.27 0.2 1 649 154 160 VAL CB C 30.82 0.2 1 650 154 160 VAL N N 122.66 0.2 1 651 155 161 ARG H H 8.55 0.04 1 652 155 161 ARG C C 180.33 0.2 1 653 155 161 ARG CA C 59.75 0.2 1 654 155 161 ARG CB C 28.73 0.2 1 655 155 161 ARG N N 121.26 0.2 1 656 156 162 THR H H 7.92 0.04 1 657 156 162 THR C C 176.89 0.2 1 658 156 162 THR CA C 65.93 0.2 1 659 156 162 THR CB C 68.17 0.2 1 660 156 162 THR N N 115.71 0.2 1 661 157 163 PHE H H 8.75 0.04 1 662 157 163 PHE C C 177.65 0.2 1 663 157 163 PHE CA C 61.17 0.2 1 664 157 163 PHE CB C 37.37 0.2 1 665 157 163 PHE N N 125.76 0.2 1 666 158 164 PHE H H 7.93 0.04 1 667 158 164 PHE C C 179.07 0.2 1 668 158 164 PHE CA C 61.68 0.2 1 669 158 164 PHE CB C 38.66 0.2 1 670 158 164 PHE N N 114.11 0.2 1 671 159 165 GLN H H 7.54 0.04 1 672 159 165 GLN C C 180.09 0.2 1 673 159 165 GLN CA C 58.80 0.2 1 674 159 165 GLN CB C 26.65 0.2 1 675 159 165 GLN N N 121.57 0.2 1 676 160 166 ARG H H 7.24 0.04 1 677 160 166 ARG C C 174.76 0.2 1 678 160 166 ARG CA C 57.77 0.2 1 679 160 166 ARG CB C 29.43 0.2 1 680 160 166 ARG N N 123.44 0.2 1 681 161 167 LEU H H 6.42 0.04 1 682 161 167 LEU C C 175.52 0.2 1 683 161 167 LEU CA C 53.27 0.2 1 684 161 167 LEU CB C 42.42 0.2 1 685 161 167 LEU N N 112.12 0.2 1 686 162 168 ASN H H 7.75 0.04 1 687 162 168 ASN C C 173.97 0.2 1 688 162 168 ASN CA C 53.21 0.2 1 689 162 168 ASN CB C 37.32 0.2 1 690 162 168 ASN N N 113.32 0.2 1 691 163 169 MET H H 7.32 0.04 1 692 163 169 MET C C 176.27 0.2 1 693 163 169 MET CA C 52.43 0.2 1 694 163 169 MET CB C 32.73 0.2 1 695 163 169 MET N N 113.93 0.2 1 696 164 170 ASN H H 9.83 0.04 1 697 164 170 ASN C C 174.40 0.2 1 698 164 170 ASN CA C 50.35 0.2 1 699 164 170 ASN CB C 38.38 0.2 1 700 164 170 ASN N N 126.22 0.2 1 701 165 171 ASP H H 7.99 0.04 1 702 165 171 ASP C C 176.85 0.2 1 703 165 171 ASP CA C 57.49 0.2 1 704 165 171 ASP CB C 40.16 0.2 1 705 165 171 ASP N N 114.57 0.2 1 706 166 172 ARG H H 7.63 0.04 1 707 166 172 ARG C C 177.31 0.2 1 708 166 172 ARG CA C 60.08 0.2 1 709 166 172 ARG CB C 29.34 0.2 1 710 166 172 ARG N N 117.85 0.2 1 711 167 173 GLU H H 7.76 0.04 1 712 167 173 GLU C C 178.01 0.2 1 713 167 173 GLU CA C 59.07 0.2 1 714 167 173 GLU CB C 29.62 0.2 1 715 167 173 GLU N N 117.45 0.2 1 716 168 174 VAL H H 8.19 0.04 1 717 168 174 VAL C C 177.24 0.2 1 718 168 174 VAL CA C 66.93 0.2 1 719 168 174 VAL CB C 30.35 0.2 1 720 168 174 VAL N N 117.98 0.2 1 721 169 175 VAL H H 8.08 0.04 1 722 169 175 VAL C C 180.45 0.2 1 723 169 175 VAL CA C 67.11 0.2 1 724 169 175 VAL CB C 31.21 0.2 1 725 169 175 VAL N N 117.19 0.2 1 726 170 176 ALA H H 9.10 0.04 1 727 170 176 ALA C C 180.15 0.2 1 728 170 176 ALA CA C 55.66 0.2 1 729 170 176 ALA CB C 16.18 0.2 1 730 170 176 ALA N N 123.30 0.2 1 731 171 177 LEU H H 8.75 0.04 1 732 171 177 LEU C C 179.84 0.2 1 733 171 177 LEU CA C 58.43 0.2 1 734 171 177 LEU CB C 41.33 0.2 1 735 171 177 LEU N N 117.95 0.2 1 736 172 178 MET H H 8.66 0.04 1 737 172 178 MET C C 179.36 0.2 1 738 172 178 MET CA C 58.31 0.2 1 739 172 178 MET CB C 32.19 0.2 1 740 172 178 MET N N 118.58 0.2 1 741 173 179 GLY H H 8.96 0.04 1 742 173 179 GLY C C 177.73 0.2 1 743 173 179 GLY CA C 47.34 0.2 1 744 173 179 GLY N N 105.08 0.2 1 745 174 180 ALA H H 10.10 0.04 1 746 174 180 ALA CA C 55.46 0.2 1 747 174 180 ALA CB C 20.92 0.2 1 748 174 180 ALA N N 124.07 0.2 1 749 175 181 HIS C C 172.82 0.2 1 750 175 181 HIS CA C 59.12 0.2 1 751 176 182 ALA H H 8.51 0.04 1 752 176 182 ALA C C 179.63 0.2 1 753 176 182 ALA CA C 54.99 0.2 1 754 176 182 ALA CB C 18.42 0.2 1 755 176 182 ALA N N 116.57 0.2 1 756 177 183 LEU H H 8.31 0.04 1 757 177 183 LEU C C 173.60 0.2 1 758 177 183 LEU CA C 51.63 0.2 1 759 177 183 LEU CB C 42.04 0.2 1 760 177 183 LEU N N 116.94 0.2 1 761 178 184 GLY H H 8.24 0.04 1 762 178 184 GLY C C 173.50 0.2 1 763 178 184 GLY CA C 43.82 0.2 1 764 178 184 GLY N N 100.64 0.2 1 765 179 185 LYS H H 7.11 0.04 1 766 179 185 LYS C C 171.15 0.2 1 767 179 185 LYS CA C 54.11 0.2 1 768 179 185 LYS CB C 30.55 0.2 1 769 179 185 LYS N N 116.37 0.2 1 770 180 186 THR H H 6.11 0.04 1 771 180 186 THR C C 175.92 0.2 1 772 180 186 THR CA C 59.10 0.2 1 773 180 186 THR CB C 68.86 0.2 1 774 180 186 THR N N 104.37 0.2 1 775 181 187 HIS H H 9.42 0.04 1 776 181 187 HIS C C 177.00 0.2 1 777 181 187 HIS CA C 54.02 0.2 1 778 181 187 HIS CB C 29.30 0.2 1 779 181 187 HIS N N 123.54 0.2 1 780 182 188 LEU H H 8.65 0.04 1 781 182 188 LEU C C 180.71 0.2 1 782 182 188 LEU CA C 59.37 0.2 1 783 182 188 LEU CB C 41.84 0.2 1 784 182 188 LEU N N 131.81 0.2 1 785 183 189 LYS H H 8.78 0.04 1 786 183 189 LYS C C 177.24 0.2 1 787 183 189 LYS CA C 57.55 0.2 1 788 183 189 LYS CB C 31.11 0.2 1 789 183 189 LYS N N 114.11 0.2 1 790 184 190 ASN H H 7.97 0.04 1 791 184 190 ASN C C 176.67 0.2 1 792 184 190 ASN CA C 54.06 0.2 1 793 184 190 ASN CB C 38.15 0.2 1 794 184 190 ASN N N 116.00 0.2 1 795 185 191 SER H H 8.19 0.04 1 796 185 191 SER C C 175.94 0.2 1 797 185 191 SER CA C 58.83 0.2 1 798 185 191 SER CB C 67.35 0.2 1 799 185 191 SER N N 110.00 0.2 1 800 186 192 GLY H H 8.40 0.04 1 801 186 192 GLY C C 171.55 0.2 1 802 186 192 GLY CA C 45.00 0.2 1 803 186 192 GLY N N 110.74 0.2 1 804 187 193 TYR H H 7.36 0.04 1 805 187 193 TYR C C 170.52 0.2 1 806 187 193 TYR CA C 57.86 0.2 1 807 187 193 TYR CB C 39.54 0.2 1 808 187 193 TYR N N 119.48 0.2 1 809 188 194 GLU H H 7.50 0.04 1 810 188 194 GLU C C 175.96 0.2 1 811 188 194 GLU CA C 54.60 0.2 1 812 188 194 GLU CB C 32.74 0.2 1 813 188 194 GLU N N 117.74 0.2 1 814 189 195 GLY H H 6.68 0.04 1 815 189 195 GLY CA C 42.57 0.2 1 816 189 195 GLY N N 117.49 0.2 1 817 190 196 PRO C C 174.59 0.2 1 818 191 197 TRP H H 7.68 0.04 1 819 191 197 TRP C C 177.49 0.2 1 820 191 197 TRP CA C 61.69 0.2 1 821 191 197 TRP CB C 31.46 0.2 1 822 191 197 TRP N N 121.72 0.2 1 823 192 198 GLY H H 7.24 0.04 1 824 192 198 GLY C C 172.45 0.2 1 825 192 198 GLY CA C 44.68 0.2 1 826 192 198 GLY N N 102.62 0.2 1 827 193 199 ALA H H 9.75 0.04 1 828 193 199 ALA C C 179.02 0.2 1 829 193 199 ALA CA C 52.70 0.2 1 830 193 199 ALA CB C 19.79 0.2 1 831 193 199 ALA N N 122.84 0.2 1 832 194 200 ALA H H 8.51 0.04 1 833 194 200 ALA C C 177.67 0.2 1 834 194 200 ALA CA C 51.29 0.2 1 835 194 200 ALA CB C 16.92 0.2 1 836 194 200 ALA N N 124.36 0.2 1 837 195 201 ASN H H 8.10 0.04 1 838 195 201 ASN C C 175.42 0.2 1 839 195 201 ASN CA C 54.41 0.2 1 840 195 201 ASN CB C 37.95 0.2 1 841 195 201 ASN N N 113.57 0.2 1 842 196 202 ASN H H 7.83 0.04 1 843 196 202 ASN C C 173.15 0.2 1 844 196 202 ASN CA C 51.30 0.2 1 845 196 202 ASN CB C 36.59 0.2 1 846 196 202 ASN N N 115.10 0.2 1 847 197 203 VAL H H 7.19 0.04 1 848 197 203 VAL C C 173.70 0.2 1 849 197 203 VAL CA C 60.61 0.2 1 850 197 203 VAL CB C 34.00 0.2 1 851 197 203 VAL N N 116.56 0.2 1 852 198 204 PHE H H 9.05 0.04 1 853 198 204 PHE C C 173.57 0.2 1 854 198 204 PHE CA C 59.11 0.2 1 855 198 204 PHE CB C 38.66 0.2 1 856 198 204 PHE N N 128.75 0.2 1 857 199 205 THR H H 6.98 0.04 1 858 199 205 THR C C 173.57 0.2 1 859 199 205 THR CA C 60.29 0.2 1 860 199 205 THR CB C 73.01 0.2 1 861 199 205 THR N N 117.74 0.2 1 862 200 206 ASN H H 9.01 0.04 1 863 200 206 ASN C C 176.24 0.2 1 864 200 206 ASN CA C 53.03 0.2 1 865 200 206 ASN CB C 37.04 0.2 1 866 200 206 ASN N N 116.68 0.2 1 867 201 207 GLU H H 8.77 0.04 1 868 201 207 GLU C C 176.52 0.2 1 869 201 207 GLU CA C 59.90 0.2 1 870 201 207 GLU CB C 28.95 0.2 1 871 201 207 GLU N N 120.09 0.2 1 872 202 208 PHE H H 8.46 0.04 1 873 202 208 PHE C C 176.14 0.2 1 874 202 208 PHE CA C 62.47 0.2 1 875 202 208 PHE CB C 39.91 0.2 1 876 202 208 PHE N N 118.41 0.2 1 877 203 209 TYR H H 6.94 0.04 1 878 203 209 TYR C C 178.26 0.2 1 879 203 209 TYR CA C 59.94 0.2 1 880 203 209 TYR CB C 37.35 0.2 1 881 203 209 TYR N N 115.63 0.2 1 882 204 210 LEU H H 7.27 0.04 1 883 204 210 LEU C C 179.29 0.2 1 884 204 210 LEU CA C 57.74 0.2 1 885 204 210 LEU CB C 41.02 0.2 1 886 204 210 LEU N N 116.62 0.2 1 887 205 211 ASN H H 9.11 0.04 1 888 205 211 ASN C C 178.64 0.2 1 889 205 211 ASN CA C 55.37 0.2 1 890 205 211 ASN CB C 35.14 0.2 1 891 205 211 ASN N N 119.37 0.2 1 892 206 212 LEU H H 8.48 0.04 1 893 206 212 LEU C C 178.48 0.2 1 894 206 212 LEU CA C 58.77 0.2 1 895 206 212 LEU CB C 41.19 0.2 1 896 206 212 LEU N N 123.77 0.2 1 897 207 213 LEU H H 7.44 0.04 1 898 207 213 LEU C C 179.47 0.2 1 899 207 213 LEU CA C 56.42 0.2 1 900 207 213 LEU CB C 42.41 0.2 1 901 207 213 LEU N N 112.93 0.2 1 902 208 214 ASN H H 8.57 0.04 1 903 208 214 ASN C C 177.13 0.2 1 904 208 214 ASN CA C 54.53 0.2 1 905 208 214 ASN CB C 39.83 0.2 1 906 208 214 ASN N N 114.71 0.2 1 907 209 215 GLU H H 7.86 0.04 1 908 209 215 GLU C C 173.87 0.2 1 909 209 215 GLU CA C 55.08 0.2 1 910 209 215 GLU CB C 29.38 0.2 1 911 209 215 GLU N N 118.99 0.2 1 912 210 216 ASP H H 8.15 0.04 1 913 210 216 ASP C C 175.36 0.2 1 914 210 216 ASP CA C 52.51 0.2 1 915 210 216 ASP CB C 40.41 0.2 1 916 210 216 ASP N N 119.90 0.2 1 917 211 217 TRP H H 7.90 0.04 1 918 211 217 TRP C C 176.72 0.2 1 919 211 217 TRP CA C 56.12 0.2 1 920 211 217 TRP CB C 32.62 0.2 1 921 211 217 TRP N N 124.78 0.2 1 922 212 218 LYS H H 9.22 0.04 1 923 212 218 LYS C C 174.12 0.2 1 924 212 218 LYS CA C 54.85 0.2 1 925 212 218 LYS CB C 35.09 0.2 1 926 212 218 LYS N N 124.25 0.2 1 927 213 219 LEU H H 8.06 0.04 1 928 213 219 LEU C C 176.28 0.2 1 929 213 219 LEU CA C 54.60 0.2 1 930 213 219 LEU CB C 39.31 0.2 1 931 213 219 LEU N N 131.10 0.2 1 932 214 220 GLU H H 8.82 0.04 1 933 214 220 GLU C C 174.37 0.2 1 934 214 220 GLU CA C 54.04 0.2 1 935 214 220 GLU CB C 31.85 0.2 1 936 214 220 GLU N N 127.41 0.2 1 937 215 221 LYS H H 8.22 0.04 1 938 215 221 LYS C C 176.90 0.2 1 939 215 221 LYS CA C 55.12 0.2 1 940 215 221 LYS CB C 32.59 0.2 1 941 215 221 LYS N N 120.04 0.2 1 942 216 222 ASN H H 8.40 0.04 1 943 216 222 ASN C C 178.09 0.2 1 944 216 222 ASN CA C 50.48 0.2 1 945 216 222 ASN CB C 38.67 0.2 1 946 216 222 ASN N N 122.67 0.2 1 947 217 223 ASP H H 8.62 0.04 1 948 217 223 ASP C C 176.69 0.2 1 949 217 223 ASP CA C 56.44 0.2 1 950 217 223 ASP CB C 40.01 0.2 1 951 217 223 ASP N N 117.45 0.2 1 952 218 224 ALA H H 8.04 0.04 1 953 218 224 ALA C C 175.91 0.2 1 954 218 224 ALA CA C 51.03 0.2 1 955 218 224 ALA CB C 17.56 0.2 1 956 218 224 ALA N N 122.43 0.2 1 957 219 225 ASN H H 8.13 0.04 1 958 219 225 ASN C C 173.71 0.2 1 959 219 225 ASN CA C 54.33 0.2 1 960 219 225 ASN CB C 36.81 0.2 1 961 219 225 ASN N N 112.76 0.2 1 962 220 226 ASN H H 7.36 0.04 1 963 220 226 ASN C C 174.32 0.2 1 964 220 226 ASN CA C 51.17 0.2 1 965 220 226 ASN CB C 39.58 0.2 1 966 220 226 ASN N N 115.53 0.2 1 967 221 227 GLU H H 8.11 0.04 1 968 221 227 GLU C C 175.08 0.2 1 969 221 227 GLU CA C 55.50 0.2 1 970 221 227 GLU CB C 29.29 0.2 1 971 221 227 GLU N N 119.91 0.2 1 972 222 228 GLN H H 8.64 0.04 1 973 222 228 GLN C C 171.96 0.2 1 974 222 228 GLN CA C 53.60 0.2 1 975 222 228 GLN CB C 31.68 0.2 1 976 222 228 GLN N N 117.51 0.2 1 977 223 229 TRP H H 8.31 0.04 1 978 223 229 TRP C C 174.75 0.2 1 979 223 229 TRP CA C 55.81 0.2 1 980 223 229 TRP CB C 28.81 0.2 1 981 223 229 TRP N N 123.50 0.2 1 982 224 230 ASP H H 9.46 0.04 1 983 224 230 ASP C C 176.72 0.2 1 984 224 230 ASP CA C 52.15 0.2 1 985 224 230 ASP CB C 42.66 0.2 1 986 224 230 ASP N N 120.32 0.2 1 987 225 231 SER H H 8.91 0.04 1 988 225 231 SER C C 177.08 0.2 1 989 225 231 SER CA C 54.82 0.2 1 990 225 231 SER CB C 65.26 0.2 1 991 225 231 SER N N 118.75 0.2 1 992 226 232 LYS H H 8.70 0.04 1 993 226 232 LYS C C 177.52 0.2 1 994 226 232 LYS CA C 57.93 0.2 1 995 226 232 LYS CB C 30.62 0.2 1 996 226 232 LYS N N 124.83 0.2 1 997 227 233 SER H H 7.44 0.04 1 998 227 233 SER C C 173.17 0.2 1 999 227 233 SER CA C 57.54 0.2 1 1000 227 233 SER CB C 61.63 0.2 1 1001 227 233 SER N N 112.93 0.2 1 1002 228 234 GLY H H 7.59 0.04 1 1003 228 234 GLY C C 174.05 0.2 1 1004 228 234 GLY CA C 44.15 0.2 1 1005 228 234 GLY N N 106.48 0.2 1 1006 229 235 TYR H H 6.39 0.04 1 1007 229 235 TYR C C 174.75 0.2 1 1008 229 235 TYR CA C 52.57 0.2 1 1009 229 235 TYR CB C 39.16 0.2 1 1010 229 235 TYR N N 119.96 0.2 1 1011 230 236 MET H H 9.17 0.04 1 1012 230 236 MET C C 172.60 0.2 1 1013 230 236 MET CA C 53.43 0.2 1 1014 230 236 MET CB C 36.94 0.2 1 1015 230 236 MET N N 124.12 0.2 1 1016 231 237 MET H H 8.63 0.04 1 1017 231 237 MET C C 176.71 0.2 1 1018 231 237 MET CA C 53.50 0.2 1 1019 231 237 MET CB C 35.84 0.2 1 1020 231 237 MET N N 113.00 0.2 1 1021 232 238 LEU H H 10.13 0.04 1 1022 232 238 LEU CA C 52.22 0.2 1 1023 232 238 LEU CB C 39.06 0.2 1 1024 232 238 LEU N N 121.85 0.2 1 1025 233 239 PRO C C 179.21 0.2 1 1026 233 239 PRO CA C 66.87 0.2 1 1027 233 239 PRO CB C 29.94 0.2 1 1028 234 240 THR H H 6.86 0.04 1 1029 234 240 THR C C 177.17 0.2 1 1030 234 240 THR CA C 64.53 0.2 1 1031 234 240 THR CB C 65.97 0.2 1 1032 234 240 THR N N 106.49 0.2 1 1033 235 241 ASP H H 6.45 0.04 1 1034 235 241 ASP C C 177.41 0.2 1 1035 235 241 ASP CA C 57.82 0.2 1 1036 235 241 ASP CB C 44.88 0.2 1 1037 235 241 ASP N N 121.58 0.2 1 1038 236 242 TYR H H 8.03 0.04 1 1039 236 242 TYR C C 177.45 0.2 1 1040 236 242 TYR CA C 60.29 0.2 1 1041 236 242 TYR CB C 38.76 0.2 1 1042 236 242 TYR N N 118.87 0.2 1 1043 237 243 SER H H 7.68 0.04 1 1044 237 243 SER C C 175.63 0.2 1 1045 237 243 SER CA C 61.63 0.2 1 1046 237 243 SER CB C 61.95 0.2 1 1047 237 243 SER N N 113.74 0.2 1 1048 238 244 LEU H H 7.66 0.04 1 1049 238 244 LEU C C 176.81 0.2 1 1050 238 244 LEU CA C 56.32 0.2 1 1051 238 244 LEU CB C 40.59 0.2 1 1052 238 244 LEU N N 120.62 0.2 1 1053 239 245 ILE H H 7.26 0.04 1 1054 239 245 ILE C C 177.32 0.2 1 1055 239 245 ILE CA C 59.71 0.2 1 1056 239 245 ILE CB C 37.21 0.2 1 1057 239 245 ILE N N 102.62 0.2 1 1058 240 246 GLN H H 7.30 0.04 1 1059 240 246 GLN C C 175.86 0.2 1 1060 240 246 GLN CA C 55.91 0.2 1 1061 240 246 GLN CB C 29.20 0.2 1 1062 240 246 GLN N N 120.75 0.2 1 1063 241 247 ASP H H 7.33 0.04 1 1064 241 247 ASP CA C 50.44 0.2 1 1065 241 247 ASP CB C 43.93 0.2 1 1066 241 247 ASP N N 122.93 0.2 1 1067 242 248 PRO C C 179.45 0.2 1 1068 242 248 PRO CA C 64.77 0.2 1 1069 243 249 LYS H H 7.44 0.04 1 1070 243 249 LYS C C 180.34 0.2 1 1071 243 249 LYS CA C 58.27 0.2 1 1072 243 249 LYS CB C 30.66 0.2 1 1073 243 249 LYS N N 118.73 0.2 1 1074 244 250 TYR H H 8.52 0.04 1 1075 244 250 TYR C C 179.09 0.2 1 1076 244 250 TYR CA C 57.49 0.2 1 1077 244 250 TYR CB C 36.86 0.2 1 1078 244 250 TYR N N 121.23 0.2 1 1079 245 251 LEU H H 8.76 0.04 1 1080 245 251 LEU C C 178.32 0.2 1 1081 245 251 LEU CA C 58.18 0.2 1 1082 245 251 LEU CB C 40.59 0.2 1 1083 245 251 LEU N N 122.19 0.2 1 1084 246 252 SER H H 7.09 0.04 1 1085 246 252 SER C C 176.63 0.2 1 1086 246 252 SER CA C 61.22 0.2 1 1087 246 252 SER CB C 62.61 0.2 1 1088 246 252 SER N N 110.08 0.2 1 1089 247 253 ILE H H 7.34 0.04 1 1090 247 253 ILE C C 176.97 0.2 1 1091 247 253 ILE CA C 64.19 0.2 1 1092 247 253 ILE CB C 37.36 0.2 1 1093 247 253 ILE N N 123.63 0.2 1 1094 248 254 VAL H H 8.62 0.04 1 1095 248 254 VAL C C 178.56 0.2 1 1096 248 254 VAL CA C 66.66 0.2 1 1097 248 254 VAL CB C 30.99 0.2 1 1098 248 254 VAL N N 122.36 0.2 1 1099 249 255 LYS H H 8.19 0.04 1 1100 249 255 LYS C C 179.14 0.2 1 1101 249 255 LYS CA C 59.84 0.2 1 1102 249 255 LYS CB C 31.97 0.2 1 1103 249 255 LYS N N 115.68 0.2 1 1104 250 256 GLU H H 7.28 0.04 1 1105 250 256 GLU C C 180.17 0.2 1 1106 250 256 GLU CA C 59.15 0.2 1 1107 250 256 GLU CB C 29.16 0.2 1 1108 250 256 GLU N N 120.50 0.2 1 1109 251 257 TYR H H 7.84 0.04 1 1110 251 257 TYR C C 179.01 0.2 1 1111 251 257 TYR CA C 55.71 0.2 1 1112 251 257 TYR CB C 35.53 0.2 1 1113 251 257 TYR N N 119.98 0.2 1 1114 252 258 ALA H H 8.68 0.04 1 1115 252 258 ALA C C 177.72 0.2 1 1116 252 258 ALA CA C 54.51 0.2 1 1117 252 258 ALA CB C 18.17 0.2 1 1118 252 258 ALA N N 121.93 0.2 1 1119 253 259 ASN H H 7.33 0.04 1 1120 253 259 ASN C C 175.13 0.2 1 1121 253 259 ASN CA C 53.79 0.2 1 1122 253 259 ASN CB C 39.78 0.2 1 1123 253 259 ASN N N 112.44 0.2 1 1124 254 260 ASP H H 7.73 0.04 1 1125 254 260 ASP C C 174.44 0.2 1 1126 254 260 ASP CA C 52.92 0.2 1 1127 254 260 ASP CB C 41.29 0.2 1 1128 254 260 ASP N N 120.45 0.2 1 1129 255 261 GLN H H 9.17 0.04 1 1130 255 261 GLN C C 176.90 0.2 1 1131 255 261 GLN CA C 59.45 0.2 1 1132 255 261 GLN CB C 29.73 0.2 1 1133 255 261 GLN N N 126.05 0.2 1 1134 256 262 ASP H H 8.18 0.04 1 1135 256 262 ASP C C 178.57 0.2 1 1136 256 262 ASP CA C 57.60 0.2 1 1137 256 262 ASP CB C 40.35 0.2 1 1138 256 262 ASP N N 118.86 0.2 1 1139 257 263 LYS H H 7.69 0.04 1 1140 257 263 LYS C C 178.17 0.2 1 1141 257 263 LYS CA C 58.34 0.2 1 1142 257 263 LYS CB C 31.52 0.2 1 1143 257 263 LYS N N 122.11 0.2 1 1144 258 264 PHE H H 7.52 0.04 1 1145 258 264 PHE C C 176.16 0.2 1 1146 258 264 PHE CA C 58.55 0.2 1 1147 258 264 PHE CB C 37.29 0.2 1 1148 258 264 PHE N N 118.69 0.2 1 1149 259 265 PHE H H 9.07 0.04 1 1150 259 265 PHE C C 178.31 0.2 1 1151 259 265 PHE CA C 59.86 0.2 1 1152 259 265 PHE CB C 36.79 0.2 1 1153 259 265 PHE N N 121.15 0.2 1 1154 260 266 LYS H H 7.96 0.04 1 1155 260 266 LYS C C 179.82 0.2 1 1156 260 266 LYS CA C 59.32 0.2 1 1157 260 266 LYS CB C 31.68 0.2 1 1158 260 266 LYS N N 118.94 0.2 1 1159 261 267 ASP H H 8.44 0.04 1 1160 261 267 ASP C C 179.92 0.2 1 1161 261 267 ASP CA C 56.84 0.2 1 1162 261 267 ASP CB C 38.55 0.2 1 1163 261 267 ASP N N 121.91 0.2 1 1164 262 268 PHE H H 9.92 0.04 1 1165 262 268 PHE C C 176.56 0.2 1 1166 262 268 PHE CA C 62.90 0.2 1 1167 262 268 PHE CB C 38.35 0.2 1 1168 262 268 PHE N N 123.72 0.2 1 1169 263 269 SER H H 8.25 0.04 1 1170 263 269 SER C C 176.41 0.2 1 1171 263 269 SER CA C 61.25 0.2 1 1172 263 269 SER CB C 62.35 0.2 1 1173 263 269 SER N N 112.77 0.2 1 1174 264 270 LYS H H 7.13 0.04 1 1175 264 270 LYS C C 179.38 0.2 1 1176 264 270 LYS CA C 58.49 0.2 1 1177 264 270 LYS CB C 32.08 0.2 1 1178 264 270 LYS N N 117.32 0.2 1 1179 265 271 ALA H H 8.01 0.04 1 1180 265 271 ALA C C 178.55 0.2 1 1181 265 271 ALA CA C 54.77 0.2 1 1182 265 271 ALA CB C 17.27 0.2 1 1183 265 271 ALA N N 123.02 0.2 1 1184 266 272 PHE H H 9.21 0.04 1 1185 266 272 PHE C C 177.31 0.2 1 1186 266 272 PHE CA C 59.82 0.2 1 1187 266 272 PHE CB C 38.52 0.2 1 1188 266 272 PHE N N 120.24 0.2 1 1189 267 273 GLU H H 7.78 0.04 1 1190 267 273 GLU C C 177.11 0.2 1 1191 267 273 GLU CA C 59.57 0.2 1 1192 267 273 GLU CB C 25.73 0.2 1 1193 267 273 GLU N N 117.45 0.2 1 1194 268 274 LYS H H 7.44 0.04 1 1195 268 274 LYS C C 178.72 0.2 1 1196 268 274 LYS CA C 59.05 0.2 1 1197 268 274 LYS CB C 31.98 0.2 1 1198 268 274 LYS N N 118.73 0.2 1 1199 269 275 LEU H H 8.15 0.04 1 1200 269 275 LEU C C 179.51 0.2 1 1201 269 275 LEU CA C 57.12 0.2 1 1202 269 275 LEU CB C 41.58 0.2 1 1203 269 275 LEU N N 119.65 0.2 1 1204 270 276 LEU H H 7.46 0.04 1 1205 270 276 LEU C C 178.09 0.2 1 1206 270 276 LEU CA C 56.12 0.2 1 1207 270 276 LEU CB C 40.22 0.2 1 1208 270 276 LEU N N 117.97 0.2 1 1209 271 277 GLU H H 7.55 0.04 1 1210 271 277 GLU C C 176.11 0.2 1 1211 271 277 GLU CA C 55.22 0.2 1 1212 271 277 GLU CB C 29.30 0.2 1 1213 271 277 GLU N N 119.74 0.2 1 1214 272 278 ASN H H 7.11 0.04 1 1215 272 278 ASN C C 176.41 0.2 1 1216 272 278 ASN CA C 52.98 0.2 1 1217 272 278 ASN CB C 36.76 0.2 1 1218 272 278 ASN N N 123.08 0.2 1 1219 273 279 GLY H H 8.28 0.04 1 1220 273 279 GLY C C 174.57 0.2 1 1221 273 279 GLY CA C 45.31 0.2 1 1222 273 279 GLY N N 109.89 0.2 1 1223 274 280 ILE H H 7.51 0.04 1 1224 274 280 ILE C C 175.25 0.2 1 1225 274 280 ILE CA C 61.06 0.2 1 1226 274 280 ILE CB C 37.69 0.2 1 1227 274 280 ILE N N 121.68 0.2 1 1228 275 281 THR H H 8.73 0.04 1 1229 275 281 THR C C 172.59 0.2 1 1230 275 281 THR CA C 61.48 0.2 1 1231 275 281 THR CB C 69.29 0.2 1 1232 275 281 THR N N 125.00 0.2 1 1233 276 282 PHE H H 9.10 0.04 1 1234 276 282 PHE CA C 55.42 0.2 1 1235 276 282 PHE CB C 38.03 0.2 1 1236 276 282 PHE N N 129.23 0.2 1 1237 277 283 PRO C C 177.08 0.2 1 1238 277 283 PRO CA C 61.87 0.2 1 1239 277 283 PRO CB C 32.24 0.2 1 1240 278 284 LYS H H 8.76 0.04 1 1241 278 284 LYS C C 176.76 0.2 1 1242 278 284 LYS CA C 58.49 0.2 1 1243 278 284 LYS CB C 31.12 0.2 1 1244 278 284 LYS N N 121.61 0.2 1 1245 279 285 ASP H H 8.15 0.04 1 1246 279 285 ASP C C 175.77 0.2 1 1247 279 285 ASP CA C 52.54 0.2 1 1248 279 285 ASP CB C 39.00 0.2 1 1249 279 285 ASP N N 114.77 0.2 1 1250 280 286 ALA H H 7.48 0.04 1 1251 280 286 ALA CA C 50.45 0.2 1 1252 280 286 ALA CB C 16.87 0.2 1 1253 280 286 ALA N N 124.08 0.2 1 1254 281 287 PRO C C 176.94 0.2 1 1255 281 287 PRO CA C 62.15 0.2 1 1256 281 287 PRO CB C 30.72 0.2 1 1257 282 288 SER H H 8.24 0.04 1 1258 282 288 SER CA C 57.76 0.2 1 1259 282 288 SER CB C 60.86 0.2 1 1260 282 288 SER N N 119.20 0.2 1 1261 283 289 PRO C C 175.67 0.2 1 1262 283 289 PRO CA C 62.96 0.2 1 1263 283 289 PRO CB C 31.18 0.2 1 1264 284 290 PHE H H 9.02 0.04 1 1265 284 290 PHE C C 174.85 0.2 1 1266 284 290 PHE CA C 53.77 0.2 1 1267 284 290 PHE CB C 39.37 0.2 1 1268 284 290 PHE N N 124.89 0.2 1 1269 285 291 ILE H H 7.80 0.04 1 1270 285 291 ILE C C 176.60 0.2 1 1271 285 291 ILE CA C 58.74 0.2 1 1272 285 291 ILE CB C 36.64 0.2 1 1273 285 291 ILE N N 120.45 0.2 1 1274 286 292 PHE H H 9.83 0.04 1 1275 286 292 PHE C C 177.17 0.2 1 1276 286 292 PHE CA C 58.85 0.2 1 1277 286 292 PHE CB C 38.83 0.2 1 1278 286 292 PHE N N 129.93 0.2 1 1279 287 293 LYS H H 8.64 0.04 1 1280 287 293 LYS C C 176.52 0.2 1 1281 287 293 LYS CA C 54.77 0.2 1 1282 287 293 LYS CB C 33.40 0.2 1 1283 287 293 LYS N N 123.70 0.2 1 1284 288 294 THR H H 8.49 0.04 1 1285 288 294 THR C C 179.08 0.2 1 1286 288 294 THR CA C 59.75 0.2 1 1287 288 294 THR CB C 70.30 0.2 1 1288 288 294 THR N N 109.53 0.2 1 1289 289 295 LEU H H 9.42 0.04 1 1290 289 295 LEU C C 180.48 0.2 1 1291 289 295 LEU CA C 58.98 0.2 1 1292 289 295 LEU CB C 38.91 0.2 1 1293 289 295 LEU N N 122.48 0.2 1 1294 290 296 GLU H H 8.78 0.04 1 1295 290 296 GLU CA C 58.94 0.2 1 1296 290 296 GLU CB C 28.69 0.2 1 1297 290 296 GLU N N 120.09 0.2 1 1298 291 297 GLU H H 7.93 0.04 1 1299 291 297 GLU C C 178.57 0.2 1 1300 291 297 GLU CA C 58.31 0.2 1 1301 291 297 GLU CB C 29.59 0.2 1 1302 291 297 GLU N N 120.34 0.2 1 1303 292 298 GLN H H 7.51 0.04 1 1304 292 298 GLN C C 175.68 0.2 1 1305 292 298 GLN CA C 55.69 0.2 1 1306 292 298 GLN CB C 32.66 0.2 1 1307 292 298 GLN N N 116.24 0.2 1 1308 293 299 GLY H H 7.89 0.04 1 1309 293 299 GLY C C 174.23 0.2 1 1310 293 299 GLY CA C 45.77 0.2 1 1311 293 299 GLY N N 110.12 0.2 1 stop_ save_