data_19004 ####################### # 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 C-terminal His-tag ; _BMRB_accession_number 19004 _BMRB_flat_file_name bmr19004.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" 267 "13C chemical shifts" 820 "15N chemical shifts" 267 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 19005 (His)6CcPCN 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 CcP(His)6CN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label protein $cytochrome_c_peroxidase cofactor_HEME $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 ; MKTLVHVASVEKGRSYEDFQ KVYNAIALKLREDDEYDNYI GYGPVLVRLAWHTSGTWDKH DNTGGSYGGTYRFKKEFNDP SNAGLQNGFKFLEPIHKEFP WISSGDLFSLGGVTAVQEMQ GPKIPWRCGRVDTPEDTTPD NGRLPDADKDADYVRTFFQR LNMNDREVVALMGAHALGKT HLKNSGYEGPWGAANNVFTN EFYLNLLNEDWKLEKNDANN EQWDSKSGYMMLPTDYSLIQ DPKYLSIVKEYANDQDKFFK DFSKAFEKLLENGITFPKDA PSPFIFKTLEEQGLHHHHHH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 LYS 3 3 THR 4 4 LEU 5 5 VAL 6 6 HIS 7 7 VAL 8 8 ALA 9 9 SER 10 10 VAL 11 11 GLU 12 12 LYS 13 13 GLY 14 14 ARG 15 15 SER 16 16 TYR 17 17 GLU 18 18 ASP 19 19 PHE 20 20 GLN 21 21 LYS 22 22 VAL 23 23 TYR 24 24 ASN 25 25 ALA 26 26 ILE 27 27 ALA 28 28 LEU 29 29 LYS 30 30 LEU 31 31 ARG 32 32 GLU 33 33 ASP 34 34 ASP 35 35 GLU 36 36 TYR 37 37 ASP 38 38 ASN 39 39 TYR 40 40 ILE 41 41 GLY 42 42 TYR 43 43 GLY 44 44 PRO 45 45 VAL 46 46 LEU 47 47 VAL 48 48 ARG 49 49 LEU 50 50 ALA 51 51 TRP 52 52 HIS 53 53 THR 54 54 SER 55 55 GLY 56 56 THR 57 57 TRP 58 58 ASP 59 59 LYS 60 60 HIS 61 61 ASP 62 62 ASN 63 63 THR 64 64 GLY 65 65 GLY 66 66 SER 67 67 TYR 68 68 GLY 69 69 GLY 70 70 THR 71 71 TYR 72 72 ARG 73 73 PHE 74 74 LYS 75 75 LYS 76 76 GLU 77 77 PHE 78 78 ASN 79 79 ASP 80 80 PRO 81 81 SER 82 82 ASN 83 83 ALA 84 84 GLY 85 85 LEU 86 86 GLN 87 87 ASN 88 88 GLY 89 89 PHE 90 90 LYS 91 91 PHE 92 92 LEU 93 93 GLU 94 94 PRO 95 95 ILE 96 96 HIS 97 97 LYS 98 98 GLU 99 99 PHE 100 100 PRO 101 101 TRP 102 102 ILE 103 103 SER 104 104 SER 105 105 GLY 106 106 ASP 107 107 LEU 108 108 PHE 109 109 SER 110 110 LEU 111 111 GLY 112 112 GLY 113 113 VAL 114 114 THR 115 115 ALA 116 116 VAL 117 117 GLN 118 118 GLU 119 119 MET 120 120 GLN 121 121 GLY 122 122 PRO 123 123 LYS 124 124 ILE 125 125 PRO 126 126 TRP 127 127 ARG 128 128 CYS 129 129 GLY 130 130 ARG 131 131 VAL 132 132 ASP 133 133 THR 134 134 PRO 135 135 GLU 136 136 ASP 137 137 THR 138 138 THR 139 139 PRO 140 140 ASP 141 141 ASN 142 142 GLY 143 143 ARG 144 144 LEU 145 145 PRO 146 146 ASP 147 147 ALA 148 148 ASP 149 149 LYS 150 150 ASP 151 151 ALA 152 152 ASP 153 153 TYR 154 154 VAL 155 155 ARG 156 156 THR 157 157 PHE 158 158 PHE 159 159 GLN 160 160 ARG 161 161 LEU 162 162 ASN 163 163 MET 164 164 ASN 165 165 ASP 166 166 ARG 167 167 GLU 168 168 VAL 169 169 VAL 170 170 ALA 171 171 LEU 172 172 MET 173 173 GLY 174 174 ALA 175 175 HIS 176 176 ALA 177 177 LEU 178 178 GLY 179 179 LYS 180 180 THR 181 181 HIS 182 182 LEU 183 183 LYS 184 184 ASN 185 185 SER 186 186 GLY 187 187 TYR 188 188 GLU 189 189 GLY 190 190 PRO 191 191 TRP 192 192 GLY 193 193 ALA 194 194 ALA 195 195 ASN 196 196 ASN 197 197 VAL 198 198 PHE 199 199 THR 200 200 ASN 201 201 GLU 202 202 PHE 203 203 TYR 204 204 LEU 205 205 ASN 206 206 LEU 207 207 LEU 208 208 ASN 209 209 GLU 210 210 ASP 211 211 TRP 212 212 LYS 213 213 LEU 214 214 GLU 215 215 LYS 216 216 ASN 217 217 ASP 218 218 ALA 219 219 ASN 220 220 ASN 221 221 GLU 222 222 GLN 223 223 TRP 224 224 ASP 225 225 SER 226 226 LYS 227 227 SER 228 228 GLY 229 229 TYR 230 230 MET 231 231 MET 232 232 LEU 233 233 PRO 234 234 THR 235 235 ASP 236 236 TYR 237 237 SER 238 238 LEU 239 239 ILE 240 240 GLN 241 241 ASP 242 242 PRO 243 243 LYS 244 244 TYR 245 245 LEU 246 246 SER 247 247 ILE 248 248 VAL 249 249 LYS 250 250 GLU 251 251 TYR 252 252 ALA 253 253 ASN 254 254 ASP 255 255 GLN 256 256 ASP 257 257 LYS 258 258 PHE 259 259 PHE 260 260 LYS 261 261 ASP 262 262 PHE 263 263 SER 264 264 LYS 265 265 ALA 266 266 PHE 267 267 GLU 268 268 LYS 269 269 LEU 270 270 LEU 271 271 GLU 272 272 ASN 273 273 GLY 274 274 ILE 275 275 THR 276 276 PHE 277 277 PRO 278 278 LYS 279 279 ASP 280 280 ALA 281 281 PRO 282 282 SER 283 283 PRO 284 284 PHE 285 285 ILE 286 286 PHE 287 287 LYS 288 288 THR 289 289 LEU 290 290 GLU 291 291 GLU 292 292 GLN 293 293 GLY 294 294 LEU 295 295 HIS 296 296 HIS 297 297 HIS 298 298 HIS 299 299 HIS 300 300 HIS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 1839 "glucose oxidase" 97.00 294 99.31 100.00 0.00e+00 BMRB 19005 cytochrome_c_peroxidase 97.67 300 100.00 100.00 0.00e+00 BMRB 19075 cytochrome_c_peroxidase 100.00 300 100.00 100.00 0.00e+00 BMRB 19076 cytochrome_c_peroxidase 97.67 300 100.00 100.00 0.00e+00 BMRB 19884 High_pH 97.67 295 99.66 99.66 0.00e+00 BMRB 25551 CcP 97.00 294 99.31 99.31 0.00e+00 PDB 1A2F "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 96.67 291 98.97 98.97 0.00e+00 PDB 1A2G "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 96.67 291 98.97 98.97 0.00e+00 PDB 1AA4 "Specificity Of Ligand Binding In A Buried Polar Cavity Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1AC4 "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (2,3,4-Trimethyl-1,3-Thiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AC8 "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (3,4,5-Trimethylthiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEB "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Methylthiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AED "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3,4- Dimethylthiazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEE "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Aniline)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEF "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Aminopyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEG "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (4- Aminopyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEH "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2-Amino-4- Methylthiazole" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEJ "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (1- Vinylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEK "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Indoline)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEM "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Imidazo[1,2- A]pyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEN "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2-Amino-5- Methylthiazole" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEO "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2- Aminopyridine)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEQ "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (2-Ethylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AES "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Imidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AET "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (1-Methylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEU "Specificity Of Ligand Binding In A Polar Cavity Of Cytochrome C Peroxidase (2-Methylimidazole)" 98.00 294 98.64 98.98 0.00e+00 PDB 1AEV "Introduction Of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation Of 2- Aminothiazole" 98.00 294 98.64 98.98 0.00e+00 PDB 1BEJ "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 98.97 0.00e+00 PDB 1BEK "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 97.00 291 98.63 98.97 0.00e+00 PDB 1BEM "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 98.97 0.00e+00 PDB 1BEP "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 97.00 291 98.97 99.31 0.00e+00 PDB 1BEQ "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 99.31 0.00e+00 PDB 1BES "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 97.00 291 98.63 99.31 0.00e+00 PDB 1BJ9 "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 97.00 291 98.97 99.31 0.00e+00 PDB 1BVA "Manganese Binding Mutant In Cytochrome C Peroxidase" 98.00 294 98.30 98.64 0.00e+00 PDB 1CCA "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" 99.00 297 98.32 98.32 0.00e+00 PDB 1CCB "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" 99.00 297 97.98 98.32 0.00e+00 PDB 1CCC "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" 99.00 297 97.98 97.98 0.00e+00 PDB 1CCE "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" 96.67 291 98.97 98.97 0.00e+00 PDB 1CCG "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" 96.67 291 98.97 98.97 0.00e+00 PDB 1CCI "How Flexible Are Proteins? Trapping Of A Flexible Loop" 98.00 294 98.98 98.98 0.00e+00 PDB 1CCJ "Conformer Selection By Ligand Binding Observed With Protein Crystallography" 98.00 294 98.98 98.98 0.00e+00 PDB 1CCK "Altering Substrate Specificity Of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosi" 96.67 291 98.97 99.31 0.00e+00 PDB 1CCL "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 96.67 291 98.97 98.97 0.00e+00 PDB 1CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 99.31 99.31 0.00e+00 PDB 1CMP "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1CMQ "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1CMT "The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 1CMU "The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase" 98.00 294 98.64 98.98 0.00e+00 PDB 1CPD "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 97.00 296 98.97 98.97 0.00e+00 PDB 1CPE "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 97.00 296 98.97 98.97 0.00e+00 PDB 1CPF "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 97.00 296 98.97 98.97 0.00e+00 PDB 1CPG "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 98.00 296 97.96 98.64 0.00e+00 PDB 1CYF "Identifying The Physiological Electron Transfer Site Of Cytochrome C Peroxidase By Structure-Based Engineering" 97.00 296 98.63 98.63 0.00e+00 PDB 1DCC "2.2 Angstrom Structure Of Oxyperoxidase: A Model For The Enzyme:peroxide Complex" 97.00 296 98.97 99.31 0.00e+00 PDB 1DJ1 "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase" 97.00 291 98.97 98.97 0.00e+00 PDB 1DJ5 "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase With N-Hydroxyguanidine Bound" 97.00 291 98.97 98.97 0.00e+00 PDB 1DS4 "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, Ph 6, 100k" 97.33 292 98.97 98.97 0.00e+00 PDB 1DSE "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, With Phosphate Bound, Ph 6, 100k" 97.33 292 98.63 98.97 0.00e+00 PDB 1DSG "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 5, Room Temperature." 97.33 292 98.97 98.97 0.00e+00 PDB 1DSO "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 6, Room Temperature." 97.33 292 98.97 98.97 0.00e+00 PDB 1DSP "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 7, Room Temperature" 97.33 292 98.97 98.97 0.00e+00 PDB 1EBE "Laue Diffraction Study On The Structure Of Cytochrome C Peroxidase Compound I" 97.00 294 99.66 100.00 0.00e+00 PDB 1JCI "Stabilization Of The Engineered Cation-Binding Loop In Cytochrome C Peroxidase (Ccp)" 97.00 294 97.94 97.94 0.00e+00 PDB 1JDR "Crystal Structure Of A Proximal Domain Potassium Binding Variant Of Cytochrome C Peroxidase" 97.00 294 98.28 98.28 0.00e+00 PDB 1KOK "Crystal Structure Of Mesopone Cytochrome C Peroxidase (Mpccp)" 97.00 294 100.00 100.00 0.00e+00 PDB 1KRJ "Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp)" 97.00 294 98.28 98.28 0.00e+00 PDB 1KXM "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" 97.33 290 98.29 98.29 0.00e+00 PDB 1KXN "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" 97.00 289 98.28 98.28 0.00e+00 PDB 1MK8 "Crystal Structure Of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link" 97.00 294 99.66 100.00 0.00e+00 PDB 1MKQ "Crystal Structure Of The Mutant Variant Of Cytochrome C Peroxidase In The 'open' Uncross-Linked Form" 97.00 294 99.66 100.00 0.00e+00 PDB 1MKR "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase (Plate Like Crystals)" 97.00 294 99.66 100.00 0.00e+00 PDB 1ML2 "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase With Zn(Ii)-(20-Oxo-Protoporphyrin Ix)" 97.00 294 99.66 100.00 0.00e+00 PDB 1RYC "Cytochrome C Peroxidase W191g From Saccharomyces Cerevisiae" 98.00 294 98.98 98.98 0.00e+00 PDB 1S6V "Structure Of A Cytochrome C Peroxidase-Cytochrome C Site Specific Cross-Link" 97.00 294 99.31 99.31 0.00e+00 PDB 1S73 "Crystal Structure Of Mesopone Cytochrome C Peroxidase (R- Isomer) [mpccp-R]" 97.00 294 100.00 100.00 0.00e+00 PDB 1SBM "Crystal Structure Of Reduced Mesopone Cytochrome C Peroxidase (R-Isomer)" 97.00 294 100.00 100.00 0.00e+00 PDB 1SDQ "Structure Of Reduced-No Adduct Of Mesopone Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 1SOG "Cyrstal Structure Of Cytochrome C Peroxidase Mutant: Ccpk2m2" 97.00 294 97.59 97.94 0.00e+00 PDB 1STQ "Cyrstal Structure Of Cytochrome C Peroxidase Mutant: Ccpk2m3" 97.00 294 97.25 97.59 0.00e+00 PDB 1U74 "Electron Transfer Complex Between Cytochrome C And Cytochrome C Peroxidase" 97.00 296 99.31 99.31 0.00e+00 PDB 1U75 "Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc- Porphyrin Substituted Cytochrome C Peroxidase" 97.00 296 99.31 99.31 0.00e+00 PDB 1Z53 "The 1.13 Angstrom Structure Of Iron-Free Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 1ZBY "High-resolution Crystal Structure Of Native (resting) Cytochrome C Peroxidase (ccp)" 97.00 294 100.00 100.00 0.00e+00 PDB 1ZBZ "High-Resolution Crystal Structure Of Compound I Intermediate Of Cytochrome C Peroxidase (Ccp)" 97.00 294 100.00 100.00 0.00e+00 PDB 2ANZ "Cytochrome C Peroxidase In Complex With 2,6-Diaminopyridine" 98.00 294 98.64 98.98 0.00e+00 PDB 2AQD "Cytochrome C Peroxidase (Ccp) In Complex With 2,5- Diaminopyridine" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS1 "Cytochrome C Peroxidase In Complex With Thiopheneamidine" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS2 "Cytochrome C Peroxidase In Complex With 2-Iminopiperidine" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS3 "Cytochrome C Peroxidase In Complex With Phenol" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS4 "Cytochrome C Peroxidase In Complex With 3-Fluorocatechol" 98.00 294 98.98 98.98 0.00e+00 PDB 2AS6 "Cytochrome C Peroxidase In Complex With Cyclopentylamine" 98.00 294 98.98 98.98 0.00e+00 PDB 2B0Z "Crystal Structure Of The Protein-Protein Complex Between F82i Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2B10 "Crystal Structure Of The Protein-Protein Complex Between F82s Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2B11 "Crystal Structure Of The Protein-Protein Complex Between F82w Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2B12 "Crystal Structure Of The Protein-Protein Complex Between F82y Cytochrome C And Cytochrome C Peroxidase" 97.00 294 100.00 100.00 0.00e+00 PDB 2BCN "Solvent Isotope Effects On Interfacial Protein Electron Transfer Between Cytochrome C And Cytochrome C Peroxidase" 97.00 296 99.31 99.31 0.00e+00 PDB 2CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 98.97 99.31 0.00e+00 PDB 2CEP "Role Of Met-230 In Intramolecular Electron Transfer Between The Oxyferryl Heme And Trp 191 In Cytochrome C Peroxidase Compound " 97.00 296 98.97 99.31 0.00e+00 PDB 2CYP "Crystal Structure Of Yeast Cytochrome C Peroxidase Refined At 1.7-Angstroms Resolution" 97.00 294 100.00 100.00 0.00e+00 PDB 2EUN "Cytochrome C Peroxidase (ccp) In Complex With 2,4- Diaminopyrimidine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUO "Cytochrome C Peroxidase (ccp) In Complex With 1-methyl-1- Lambda-5-pyridin-3-yl-amine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUP "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-5- Picoline" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUQ "Cytochrome C Peroxydase (Ccp) In Complex With 3- Thienylmethylamine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUR "Cytochrome C Peroxidase (Ccp) In Complex With 4- Pyridylcarbinol" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUS "Cytochrome C Peroxidase (Ccp) In Complex With Benzylamine" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUT "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-4- Picoline" 98.00 294 98.98 98.98 0.00e+00 PDB 2EUU "Cytochrome C Peroxidase (Ccp) In Complex With 1h-Imidazol-2- Ylmethanol" 98.00 294 98.98 98.98 0.00e+00 PDB 2GB8 "Solution Structure Of The Complex Between Yeast Iso-1- Cytochrome C And Yeast Cytochrome C Peroxidase" 97.00 294 99.31 99.31 0.00e+00 PDB 2IA8 "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" 97.00 291 98.28 98.63 0.00e+00 PDB 2ICV "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" 97.00 291 98.28 98.63 0.00e+00 PDB 2JTI "Solution Structure Of The Yeast Iso-1-Cytochrome C (T12a) : Yeast Cytochrome C Peroxidase Complex" 97.00 294 99.31 99.31 0.00e+00 PDB 2N18 "Dominant Form Of The Low-affinity Complex Of Yeast Cytochrome C And Cytochrome C Peroxidase" 97.00 294 99.31 99.31 0.00e+00 PDB 2PCB "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 97.00 296 99.31 99.31 0.00e+00 PDB 2PCC "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 97.00 296 99.31 99.31 0.00e+00 PDB 2RBT "N-Methylbenzylamine In Complex With Cytochrome C Peroxidase W191g" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBU "Cytochrome C Peroxidase In Complex With Cyclopentane-Carboximidamide" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBV "Cytochrome C Peroxidase In Complex With (1-Methyl-1h-Pyrrol-2-Yl)- Methylamine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBW "Cytochrome C Peroxidase W191g In Complex With 1,2-dimethyl-1h-pyridin- 5-amine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBX "Cytochrome C Peroxidase W191g In Complex With Pyrimidine-2,4,6- Triamine." 97.33 292 98.63 98.97 0.00e+00 PDB 2RBY "1-methyl-5-imidazolecarboxaldehyde In Complex With Cytochrome C Peroxidase W191g" 97.33 292 98.63 98.97 0.00e+00 PDB 2RBZ "Cytochrome C Peroxidase W191g In Complex 3-Methoxypyridine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RC0 "Cytochrome C Peroxidase W191g In Complex With 2-Imino-4- Methylpiperdine" 97.33 292 98.63 98.97 0.00e+00 PDB 2RC1 "Cytochrome C Peroxidase W191g In Complex With 2,4,5-Trimethyl-3- Oxazoline" 97.33 292 98.63 98.97 0.00e+00 PDB 2RC2 "Cytochrome C Peroxidase W191g In Complex With 1-Methyl-2-Vinyl- Pyridinium" 97.33 292 98.63 98.97 0.00e+00 PDB 2V23 "Structure Of Cytochrome C Peroxidase Mutant N184r Y36a" 98.67 296 98.31 98.65 0.00e+00 PDB 2V2E "Structure Of Isoniazid (Inh) Bound To Cytochrome C Peroxidase Mutant N184r Y36a" 98.00 294 98.98 99.32 0.00e+00 PDB 2X07 "Cytochrome C Peroxidase: Engineered Ascorbate Binding Site" 97.00 293 98.63 99.31 0.00e+00 PDB 2X08 "Cytochrome C Peroxidase: Ascorbate Bound To The Engineered Ascorbate Binding Site" 97.00 293 98.63 99.31 0.00e+00 PDB 2XIL "The Structure Of Cytochrome C Peroxidase Compound I" 98.00 294 99.66 100.00 0.00e+00 PDB 2XJ5 "The Structure Of Cytochrome C Peroxidase Compound Ii" 98.00 294 100.00 100.00 0.00e+00 PDB 2XJ8 "The Structure Of Ferrous Cytochrome C Peroxidase" 98.00 294 100.00 100.00 0.00e+00 PDB 2Y5A "Cytochrome C Peroxidase (Ccp) W191g Bound To 3-Aminopyridine" 98.00 294 98.98 98.98 0.00e+00 PDB 2YCG "Structure Of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method" 97.00 294 100.00 100.00 0.00e+00 PDB 3CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 98.97 99.31 0.00e+00 PDB 3CCX "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 3E2O "Crystal Structure Of Cytochrome C Peroxidase, N184r Mutant" 97.00 294 99.31 99.31 0.00e+00 PDB 3EXB "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Pathway Excised In A Complex With A Peptide Wire" 99.00 295 97.31 97.31 0.00e+00 PDB 3M23 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M25 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M26 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M27 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M28 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M29 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2A "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2B "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2C "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2D "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2E "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2F "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2G "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2H "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3M2I "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 97.00 291 99.66 99.66 0.00e+00 PDB 3R98 "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" 97.00 293 100.00 100.00 0.00e+00 PDB 3R99 "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" 97.00 293 100.00 100.00 0.00e+00 PDB 4A6Z "Cytochrome C Peroxidase With Bound Guaiacol" 98.67 296 98.31 98.65 0.00e+00 PDB 4A71 "Cytochrome C Peroxidase In Complex With Phenol" 98.67 296 98.65 98.65 0.00e+00 PDB 4A78 "Cytochrome C Peroxidase M119w In Complex With Guiacol" 98.67 296 98.65 98.65 0.00e+00 PDB 4A7M "Cytochrome C Peroxidase S81w Mutant" 98.67 296 98.99 98.99 0.00e+00 PDB 4CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 97.00 296 98.97 99.31 0.00e+00 PDB 4CCX "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" 98.00 294 98.98 98.98 0.00e+00 PDB 4CVI "Neutron Structure Of Ferric Cytochrome C Peroxidase - Deuterium Exchanged At Room Temperature" 98.00 294 99.66 99.66 0.00e+00 PDB 4CVJ "Neutron Structure Of Compound I Intermediate Of Cytochrome C Peroxidase - Deuterium Exchanged 100 K" 98.00 294 100.00 100.00 0.00e+00 PDB 4JB4 "Expression, Purification, Characterization, And Solution Nmr Study Of Highly Deuterated Yeast Cytochrome C Peroxidase With Enha" 100.00 300 100.00 100.00 0.00e+00 PDB 4JM5 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-amino-5-methylthiazole" 97.00 289 98.28 98.28 0.00e+00 PDB 4JM6 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,4-diaminopyrimidine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JM8 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,6-diaminopyridine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JM9 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-amino-1-methylpyridinium" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMA "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-fluorocatechol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMB "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 5,6,7,8-tetrahydrothieno[2,3-b]quinolin-4-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMS "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-5-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMT "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridin-6-ylmethanol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMV "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-6-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMW "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Phenol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JMZ "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With N-methyl-1h-benzimidazol-2-amine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JN0 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridine-6-carbaldehyde" 97.00 289 98.28 98.28 0.00e+00 PDB 4JPL "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-azaindole" 97.00 289 98.28 98.28 0.00e+00 PDB 4JPT "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Quinazoline-2,4-diamine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JPU "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Benzamidine" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQJ "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinoline" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQK "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-(2-aminopyridin-1-ium-1-yl)ethanol" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQM "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinazoline" 97.00 289 98.28 98.28 0.00e+00 PDB 4JQN "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-hydroxybenzaldehyde" 97.00 289 98.28 98.28 0.00e+00 PDB 4NFG "K13r Mutant Of Horse Cytochrome C And Yeast Cytochrome C Peroxidase Complex" 98.00 294 99.66 99.66 0.00e+00 PDB 4NVA "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVB "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVC "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVD "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVE "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVF "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVG "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVH "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVI "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVJ "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVK "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVL "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4NVM "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVN "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4NVO "Predicting Protein Conformational Response In Prospective Ligand Discovery" 97.00 289 98.28 98.28 0.00e+00 PDB 4OQ7 "Predicting Protein Conformational Response In Prospective Ligand Discovery." 97.00 289 98.28 98.28 0.00e+00 PDB 4P4Q "Complex Of Yeast Cytochrome C Peroxidase (w191f) With Iso-1 Cytochrome C" 97.00 294 98.97 99.31 0.00e+00 PDB 4XV4 "Ccp Gateless Cavity" 97.00 289 98.28 98.28 0.00e+00 PDB 4XV5 "Ccp Gateless Cavity" 98.00 292 98.30 98.30 0.00e+00 PDB 4XV6 "Ccp Gateless Cavity" 97.00 289 98.28 98.28 0.00e+00 PDB 4XV7 "Ccp Gateless Cavity" 98.00 292 98.30 98.30 0.00e+00 PDB 4XV8 "Ccp Gateless Cavity" 98.00 292 98.30 98.30 0.00e+00 PDB 4XVA "Crystal Structure Of Wild Type Cytochrome C Peroxidase" 97.00 293 100.00 100.00 0.00e+00 PDB 5CCP "Histidine 52 Is A Critical Residue For Rapid Formation Of Cytochrome C Peroxidase Compound I" 97.00 296 98.97 98.97 0.00e+00 PDB 6CCP "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" 97.00 296 98.97 99.31 0.00e+00 PDB 7CCP "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" 97.00 296 98.97 98.97 0.00e+00 DBJ GAA24787 "K7_Ccp1p [Saccharomyces cerevisiae Kyokai no. 7]" 97.00 363 100.00 100.00 0.00e+00 EMBL CAA44288 "Cytochrome c peroxidase [Saccharomyces cerevisiae]" 97.00 361 100.00 100.00 0.00e+00 EMBL CAA82145 "CCP1 [Saccharomyces cerevisiae]" 97.00 361 100.00 100.00 0.00e+00 EMBL CAY81144 "Ccp1p [Saccharomyces cerevisiae EC1118]" 97.00 362 99.66 99.66 0.00e+00 GB AAA88709 "cytochrome c peroxidase [Saccharomyces cerevisiae]" 97.00 362 99.31 99.31 0.00e+00 GB AAS56247 "YKR066C [Saccharomyces cerevisiae]" 97.00 361 99.66 100.00 0.00e+00 GB AHY76301 "Ccp1p [Saccharomyces cerevisiae YJM993]" 97.00 363 99.31 99.31 0.00e+00 GB AJP40095 "Ccp1p [Saccharomyces cerevisiae YJM1078]" 97.00 362 99.66 99.66 0.00e+00 GB AJS30293 "Ccp1p [Saccharomyces cerevisiae YJM189]" 97.00 362 99.31 99.31 0.00e+00 REF NP_012992 "Ccp1p [Saccharomyces cerevisiae S288c]" 97.00 361 100.00 100.00 0.00e+00 SP P00431 "RecName: Full=Cytochrome c peroxidase, mitochondrial; Short=CCP; Flags: Precursor" 97.00 361 100.00 100.00 0.00e+00 TPG DAA09217 "TPA: Ccp1p [Saccharomyces cerevisiae S288c]" 97.00 361 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_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 1.1 1.25 '[U-13C; U-15N; U-2H]' 'sodium phosphate' 20 mM . . 'natural abundance' 'sodium chloride' 100 mM . . 'natural abundance' D2O 5 % . . 'natural abundance' H2O 95 % . . '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_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HN(CA)CB_6 _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 HN(CO)CA' '3D HNCO' '3D HN(CA)CO' '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 2 LYS H H 8.30 0.04 1 2 2 2 LYS C C 175.85 0.2 1 3 2 2 LYS CA C 55.94 0.2 1 4 2 2 LYS CB C 32.13 0.2 1 5 2 2 LYS N N 123.62 0.2 1 6 3 3 THR H H 8.14 0.04 1 7 3 3 THR C C 173.90 0.2 1 8 3 3 THR CA C 61.51 0.2 1 9 3 3 THR CB C 69.38 0.2 1 10 3 3 THR N N 118.41 0.2 1 11 4 4 LEU H H 8.17 0.04 1 12 4 4 LEU C C 175.99 0.2 1 13 4 4 LEU CA C 54.57 0.2 1 14 4 4 LEU CB C 41.47 0.2 1 15 4 4 LEU N N 126.86 0.2 1 16 5 5 VAL H H 8.13 0.04 1 17 5 5 VAL C C 174.57 0.2 1 18 5 5 VAL CA C 60.79 0.2 1 19 5 5 VAL CB C 32.99 0.2 1 20 5 5 VAL N N 124.14 0.2 1 21 6 6 HIS H H 8.68 0.04 1 22 6 6 HIS C C 172.34 0.2 1 23 6 6 HIS CA C 51.74 0.2 1 24 6 6 HIS CB C 27.03 0.2 1 25 6 6 HIS N N 125.07 0.2 1 26 7 7 VAL H H 8.84 0.04 1 27 7 7 VAL C C 177.91 0.2 1 28 7 7 VAL CA C 61.42 0.2 1 29 7 7 VAL CB C 31.23 0.2 1 30 7 7 VAL N N 124.98 0.2 1 31 8 8 ALA H H 8.50 0.04 1 32 8 8 ALA C C 177.04 0.2 1 33 8 8 ALA CA C 52.32 0.2 1 34 8 8 ALA CB C 19.51 0.2 1 35 8 8 ALA N N 135.58 0.2 1 36 9 9 SER H H 9.49 0.04 1 37 9 9 SER C C 172.89 0.2 1 38 9 9 SER CA C 56.10 0.2 1 39 9 9 SER CB C 63.44 0.2 1 40 9 9 SER N N 120.82 0.2 1 41 10 10 VAL H H 8.46 0.04 1 42 10 10 VAL C C 180.94 0.2 1 43 10 10 VAL CA C 59.16 0.2 1 44 10 10 VAL N N 128.15 0.2 1 45 11 11 GLU C C 176.76 0.2 1 46 11 11 GLU CA C 59.11 0.2 1 47 12 12 LYS H H 8.17 0.04 1 48 12 12 LYS C C 178.79 0.2 1 49 12 12 LYS CA C 58.14 0.2 1 50 12 12 LYS CB C 31.51 0.2 1 51 12 12 LYS N N 123.64 0.2 1 52 13 13 GLY H H 8.86 0.04 1 53 13 13 GLY C C 173.89 0.2 1 54 13 13 GLY CA C 45.06 0.2 1 55 13 13 GLY N N 113.29 0.2 1 56 14 14 ARG H H 7.67 0.04 1 57 14 14 ARG C C 175.53 0.2 1 58 14 14 ARG CA C 52.66 0.2 1 59 14 14 ARG CB C 29.02 0.2 1 60 14 14 ARG N N 119.05 0.2 1 61 15 15 SER H H 9.36 0.04 1 62 15 15 SER C C 174.26 0.2 1 63 15 15 SER CA C 56.43 0.2 1 64 15 15 SER CB C 65.88 0.2 1 65 15 15 SER N N 118.73 0.2 1 66 16 16 TYR H H 8.91 0.04 1 67 16 16 TYR C C 176.06 0.2 1 68 16 16 TYR CA C 61.38 0.2 1 69 16 16 TYR CB C 37.76 0.2 1 70 16 16 TYR N N 122.15 0.2 1 71 17 17 GLU H H 8.79 0.04 1 72 17 17 GLU C C 179.12 0.2 1 73 17 17 GLU CA C 59.42 0.2 1 74 17 17 GLU CB C 28.23 0.2 1 75 17 17 GLU N N 117.12 0.2 1 76 18 18 ASP H H 7.51 0.04 1 77 18 18 ASP C C 177.91 0.2 1 78 18 18 ASP CA C 57.37 0.2 1 79 18 18 ASP CB C 41.44 0.2 1 80 18 18 ASP N N 117.82 0.2 1 81 19 19 PHE H H 7.38 0.04 1 82 19 19 PHE C C 177.30 0.2 1 83 19 19 PHE CA C 62.20 0.2 1 84 19 19 PHE CB C 38.72 0.2 1 85 19 19 PHE N N 116.01 0.2 1 86 20 20 GLN H H 8.76 0.04 1 87 20 20 GLN C C 177.65 0.2 1 88 20 20 GLN CA C 57.32 0.2 1 89 20 20 GLN CB C 26.85 0.2 1 90 20 20 GLN N N 121.72 0.2 1 91 21 21 LYS H H 7.32 0.04 1 92 21 21 LYS C C 178.77 0.2 1 93 21 21 LYS CA C 59.77 0.2 1 94 21 21 LYS CB C 31.18 0.2 1 95 21 21 LYS N N 119.55 0.2 1 96 22 22 VAL H H 6.76 0.04 1 97 22 22 VAL C C 177.03 0.2 1 98 22 22 VAL CA C 65.41 0.2 1 99 22 22 VAL CB C 29.01 0.2 1 100 22 22 VAL N N 121.96 0.2 1 101 23 23 TYR H H 7.77 0.04 1 102 23 23 TYR C C 177.32 0.2 1 103 23 23 TYR CA C 60.26 0.2 1 104 23 23 TYR CB C 36.65 0.2 1 105 23 23 TYR N N 120.62 0.2 1 106 24 24 ASN H H 8.65 0.04 1 107 24 24 ASN C C 176.75 0.2 1 108 24 24 ASN CA C 54.91 0.2 1 109 24 24 ASN CB C 36.28 0.2 1 110 24 24 ASN N N 118.02 0.2 1 111 25 25 ALA H H 7.76 0.04 1 112 25 25 ALA C C 181.00 0.2 1 113 25 25 ALA CA C 54.89 0.2 1 114 25 25 ALA CB C 18.32 0.2 1 115 25 25 ALA N N 123.18 0.2 1 116 26 26 ILE H H 7.90 0.04 1 117 26 26 ILE C C 176.80 0.2 1 118 26 26 ILE CA C 65.01 0.2 1 119 26 26 ILE CB C 36.73 0.2 1 120 26 26 ILE N N 120.30 0.2 1 121 27 27 ALA H H 8.90 0.04 1 122 27 27 ALA C C 180.30 0.2 1 123 27 27 ALA CA C 54.62 0.2 1 124 27 27 ALA CB C 18.28 0.2 1 125 27 27 ALA N N 122.18 0.2 1 126 28 28 LEU C C 179.63 0.2 1 127 28 28 LEU CA C 57.18 0.2 1 128 28 28 LEU CB C 40.51 0.2 1 129 29 29 LYS H H 7.47 0.04 1 130 29 29 LYS C C 178.54 0.2 1 131 29 29 LYS CA C 59.27 0.2 1 132 29 29 LYS CB C 30.65 0.2 1 133 29 29 LYS N N 123.43 0.2 1 134 30 30 LEU H H 8.38 0.04 1 135 30 30 LEU C C 180.03 0.2 1 136 30 30 LEU CA C 56.77 0.2 1 137 30 30 LEU CB C 41.15 0.2 1 138 30 30 LEU N N 119.64 0.2 1 139 31 31 ARG H H 7.09 0.04 1 140 31 31 ARG C C 177.16 0.2 1 141 31 31 ARG CA C 57.19 0.2 1 142 31 31 ARG CB C 29.72 0.2 1 143 31 31 ARG N N 116.39 0.2 1 144 32 32 GLU H H 7.71 0.04 1 145 32 32 GLU C C 177.54 0.2 1 146 32 32 GLU CA C 57.91 0.2 1 147 32 32 GLU CB C 29.89 0.2 1 148 32 32 GLU N N 118.98 0.2 1 149 33 33 ASP H H 8.38 0.04 1 150 33 33 ASP C C 177.28 0.2 1 151 33 33 ASP CA C 52.48 0.2 1 152 33 33 ASP CB C 38.33 0.2 1 153 33 33 ASP N N 122.85 0.2 1 154 34 34 ASP H H 8.01 0.04 1 155 34 34 ASP C C 176.22 0.2 1 156 34 34 ASP CA C 54.31 0.2 1 157 34 34 ASP CB C 39.27 0.2 1 158 34 34 ASP N N 119.26 0.2 1 159 35 35 GLU H H 8.21 0.04 1 160 35 35 GLU C C 176.81 0.2 1 161 35 35 GLU CA C 56.42 0.2 1 162 35 35 GLU CB C 28.67 0.2 1 163 35 35 GLU N N 118.04 0.2 1 164 36 36 TYR H H 6.52 0.04 1 165 36 36 TYR C C 173.72 0.2 1 166 36 36 TYR CA C 58.21 0.2 1 167 36 36 TYR CB C 39.90 0.2 1 168 36 36 TYR N N 121.16 0.2 1 169 37 37 ASP H H 7.71 0.04 1 170 37 37 ASP N N 127.81 0.2 1 171 40 40 ILE C C 178.59 0.2 1 172 41 41 GLY H H 8.14 0.04 1 173 41 41 GLY C C 172.92 0.2 1 174 41 41 GLY CA C 43.82 0.2 1 175 41 41 GLY N N 106.88 0.2 1 176 42 42 TYR H H 9.05 0.04 1 177 42 42 TYR C C 174.56 0.2 1 178 42 42 TYR CA C 59.48 0.2 1 179 42 42 TYR CB C 38.17 0.2 1 180 42 42 TYR N N 115.45 0.2 1 181 43 43 GLY H H 8.81 0.04 1 182 43 43 GLY CA C 47.67 0.2 1 183 43 43 GLY N N 108.44 0.2 1 184 45 45 VAL C C 176.71 0.2 1 185 45 45 VAL CA C 64.71 0.2 1 186 45 45 VAL CB C 29.00 0.2 1 187 46 46 LEU H H 7.18 0.04 1 188 46 46 LEU C C 181.00 0.2 1 189 46 46 LEU CA C 57.04 0.2 1 190 46 46 LEU CB C 39.57 0.2 1 191 46 46 LEU N N 121.82 0.2 1 192 47 47 VAL H H 7.05 0.04 1 193 47 47 VAL C C 176.64 0.2 1 194 47 47 VAL CA C 66.49 0.2 1 195 47 47 VAL CB C 29.01 0.2 1 196 47 47 VAL N N 122.07 0.2 1 197 48 48 ARG H H 6.74 0.04 1 198 48 48 ARG C C 177.91 0.2 1 199 48 48 ARG CA C 58.94 0.2 1 200 48 48 ARG CB C 28.46 0.2 1 201 48 48 ARG N N 120.10 0.2 1 202 49 49 LEU H H 8.58 0.04 1 203 49 49 LEU C C 179.35 0.2 1 204 49 49 LEU CA C 58.69 0.2 1 205 49 49 LEU CB C 40.25 0.2 1 206 49 49 LEU N N 122.12 0.2 1 207 50 50 ALA H H 7.77 0.04 1 208 50 50 ALA C C 179.24 0.2 1 209 50 50 ALA CA C 54.88 0.2 1 210 50 50 ALA CB C 17.36 0.2 1 211 50 50 ALA N N 124.09 0.2 1 212 51 51 TRP H H 7.70 0.04 1 213 51 51 TRP C C 177.40 0.2 1 214 51 51 TRP CA C 58.71 0.2 1 215 51 51 TRP CB C 28.84 0.2 1 216 51 51 TRP N N 121.13 0.2 1 217 52 52 HIS H H 9.88 0.04 1 218 52 52 HIS C C 177.28 0.2 1 219 52 52 HIS CA C 59.97 0.2 1 220 52 52 HIS CB C 28.31 0.2 1 221 52 52 HIS N N 121.08 0.2 1 222 53 53 THR H H 8.20 0.04 1 223 53 53 THR C C 175.53 0.2 1 224 53 53 THR CA C 63.77 0.2 1 225 53 53 THR CB C 69.18 0.2 1 226 53 53 THR N N 107.88 0.2 1 227 54 54 SER H H 6.90 0.04 1 228 54 54 SER C C 177.38 0.2 1 229 54 54 SER CA C 60.39 0.2 1 230 54 54 SER CB C 63.30 0.2 1 231 54 54 SER N N 114.01 0.2 1 232 55 55 GLY H H 8.85 0.04 1 233 55 55 GLY C C 169.72 0.2 1 234 55 55 GLY CA C 45.75 0.2 1 235 55 55 GLY N N 113.23 0.2 1 236 56 56 THR H H 6.52 0.04 1 237 56 56 THR C C 173.77 0.2 1 238 56 56 THR CA C 60.38 0.2 1 239 56 56 THR CB C 70.04 0.2 1 240 56 56 THR N N 103.80 0.2 1 241 57 57 TRP H H 7.02 0.04 1 242 57 57 TRP C C 173.73 0.2 1 243 57 57 TRP CA C 58.77 0.2 1 244 57 57 TRP CB C 27.69 0.2 1 245 57 57 TRP N N 122.08 0.2 1 246 58 58 ASP H H 7.43 0.04 1 247 58 58 ASP C C 174.95 0.2 1 248 58 58 ASP CA C 52.06 0.2 1 249 58 58 ASP CB C 42.11 0.2 1 250 58 58 ASP N N 126.02 0.2 1 251 59 59 LYS H H 6.66 0.04 1 252 59 59 LYS C C 177.15 0.2 1 253 59 59 LYS CA C 56.40 0.2 1 254 59 59 LYS CB C 31.24 0.2 1 255 59 59 LYS N N 122.68 0.2 1 256 60 60 HIS H H 8.75 0.04 1 257 60 60 HIS C C 175.47 0.2 1 258 60 60 HIS CA C 58.44 0.2 1 259 60 60 HIS CB C 27.21 0.2 1 260 60 60 HIS N N 119.20 0.2 1 261 61 61 ASP H H 6.82 0.04 1 262 61 61 ASP C C 176.07 0.2 1 263 61 61 ASP CA C 51.93 0.2 1 264 61 61 ASP CB C 40.96 0.2 1 265 61 61 ASP N N 114.24 0.2 1 266 62 62 ASN H H 8.28 0.04 1 267 62 62 ASN C C 174.57 0.2 1 268 62 62 ASN CA C 53.24 0.2 1 269 62 62 ASN CB C 38.10 0.2 1 270 62 62 ASN N N 117.65 0.2 1 271 63 63 THR H H 7.66 0.04 1 272 63 63 THR C C 175.83 0.2 1 273 63 63 THR CA C 60.65 0.2 1 274 63 63 THR CB C 71.67 0.2 1 275 63 63 THR N N 108.59 0.2 1 276 64 64 GLY H H 8.58 0.04 1 277 64 64 GLY C C 176.15 0.2 1 278 64 64 GLY CA C 44.56 0.2 1 279 64 64 GLY N N 105.63 0.2 1 280 65 65 GLY H H 8.22 0.04 1 281 65 65 GLY C C 173.37 0.2 1 282 65 65 GLY CA C 43.85 0.2 1 283 65 65 GLY N N 107.86 0.2 1 284 66 66 SER H H 8.68 0.04 1 285 66 66 SER C C 177.70 0.2 1 286 66 66 SER CA C 59.84 0.2 1 287 66 66 SER CB C 63.74 0.2 1 288 66 66 SER N N 112.14 0.2 1 289 67 67 TYR H H 8.49 0.04 1 290 67 67 TYR C C 175.55 0.2 1 291 67 67 TYR CA C 62.64 0.2 1 292 67 67 TYR CB C 37.40 0.2 1 293 67 67 TYR N N 122.70 0.2 1 294 68 68 GLY H H 8.56 0.04 1 295 68 68 GLY C C 176.28 0.2 1 296 68 68 GLY CA C 46.14 0.2 1 297 68 68 GLY N N 99.31 0.2 1 298 69 69 GLY H H 7.88 0.04 1 299 69 69 GLY C C 178.00 0.2 1 300 69 69 GLY CA C 47.17 0.2 1 301 69 69 GLY N N 109.90 0.2 1 302 70 70 THR H H 7.91 0.04 1 303 70 70 THR C C 174.56 0.2 1 304 70 70 THR CA C 64.48 0.2 1 305 70 70 THR CB C 67.44 0.2 1 306 70 70 THR N N 112.54 0.2 1 307 71 71 TYR H H 8.56 0.04 1 308 71 71 TYR C C 171.37 0.2 1 309 71 71 TYR CA C 59.82 0.2 1 310 71 71 TYR CB C 39.10 0.2 1 311 71 71 TYR N N 124.74 0.2 1 312 72 72 ARG H H 7.00 0.04 1 313 72 72 ARG C C 176.37 0.2 1 314 72 72 ARG CA C 55.85 0.2 1 315 72 72 ARG CB C 28.65 0.2 1 316 72 72 ARG N N 108.53 0.2 1 317 73 73 PHE H H 8.42 0.04 1 318 73 73 PHE C C 176.78 0.2 1 319 73 73 PHE CA C 57.46 0.2 1 320 73 73 PHE CB C 38.09 0.2 1 321 73 73 PHE N N 123.82 0.2 1 322 74 74 LYS H H 8.97 0.04 1 323 74 74 LYS C C 177.32 0.2 1 324 74 74 LYS CA C 59.12 0.2 1 325 74 74 LYS CB C 31.84 0.2 1 326 74 74 LYS N N 122.53 0.2 1 327 75 75 LYS H H 8.79 0.04 1 328 75 75 LYS C C 177.90 0.2 1 329 75 75 LYS CA C 59.90 0.2 1 330 75 75 LYS CB C 31.82 0.2 1 331 75 75 LYS N N 117.93 0.2 1 332 76 76 GLU H H 6.91 0.04 1 333 76 76 GLU C C 179.77 0.2 1 334 76 76 GLU CA C 57.88 0.2 1 335 76 76 GLU CB C 30.28 0.2 1 336 76 76 GLU N N 119.25 0.2 1 337 77 77 PHE H H 8.83 0.04 1 338 77 77 PHE C C 178.21 0.2 1 339 77 77 PHE CA C 61.01 0.2 1 340 77 77 PHE CB C 37.90 0.2 1 341 77 77 PHE N N 125.62 0.2 1 342 78 78 ASN H H 8.19 0.04 1 343 78 78 ASN C C 174.91 0.2 1 344 78 78 ASN CA C 52.76 0.2 1 345 78 78 ASN CB C 38.12 0.2 1 346 78 78 ASN N N 112.70 0.2 1 347 79 79 ASP H H 7.77 0.04 1 348 79 79 ASP C C 178.46 0.2 1 349 79 79 ASP CA C 53.06 0.2 1 350 79 79 ASP CB C 42.37 0.2 1 351 79 79 ASP N N 124.90 0.2 1 352 80 80 PRO C C 181.03 0.2 1 353 80 80 PRO CA C 65.95 0.2 1 354 80 80 PRO CB C 31.57 0.2 1 355 81 81 SER H H 9.44 0.04 1 356 81 81 SER C C 175.19 0.2 1 357 81 81 SER CA C 62.26 0.2 1 358 81 81 SER CB C 63.88 0.2 1 359 81 81 SER N N 116.02 0.2 1 360 82 82 ASN H H 9.59 0.04 1 361 82 82 ASN C C 176.90 0.2 1 362 82 82 ASN CA C 52.59 0.2 1 363 82 82 ASN CB C 39.00 0.2 1 364 82 82 ASN N N 115.97 0.2 1 365 83 83 ALA H H 8.49 0.04 1 366 83 83 ALA C C 178.95 0.2 1 367 83 83 ALA CA C 55.89 0.2 1 368 83 83 ALA CB C 18.51 0.2 1 369 83 83 ALA N N 128.74 0.2 1 370 84 84 GLY H H 9.16 0.04 1 371 84 84 GLY C C 176.66 0.2 1 372 84 84 GLY CA C 45.17 0.2 1 373 84 84 GLY N N 115.45 0.2 1 374 85 85 LEU H H 8.79 0.04 1 375 85 85 LEU C C 178.61 0.2 1 376 85 85 LEU CA C 56.79 0.2 1 377 85 85 LEU CB C 40.17 0.2 1 378 85 85 LEU N N 120.09 0.2 1 379 86 86 GLN H H 10.12 0.04 1 380 86 86 GLN C C 178.65 0.2 1 381 86 86 GLN CA C 59.15 0.2 1 382 86 86 GLN CB C 26.12 0.2 1 383 86 86 GLN N N 123.14 0.2 1 384 87 87 ASN H H 7.62 0.04 1 385 87 87 ASN C C 178.30 0.2 1 386 87 87 ASN CA C 56.08 0.2 1 387 87 87 ASN CB C 38.02 0.2 1 388 87 87 ASN N N 116.67 0.2 1 389 88 88 GLY H H 7.66 0.04 1 390 88 88 GLY C C 173.70 0.2 1 391 88 88 GLY CA C 46.49 0.2 1 392 88 88 GLY N N 107.43 0.2 1 393 89 89 PHE H H 8.25 0.04 1 394 89 89 PHE C C 177.63 0.2 1 395 89 89 PHE CA C 62.05 0.2 1 396 89 89 PHE CB C 39.35 0.2 1 397 89 89 PHE N N 123.28 0.2 1 398 90 90 LYS H H 8.61 0.04 1 399 90 90 LYS C C 178.95 0.2 1 400 90 90 LYS CA C 58.42 0.2 1 401 90 90 LYS CB C 31.27 0.2 1 402 90 90 LYS N N 118.04 0.2 1 403 91 91 PHE H H 7.14 0.04 1 404 91 91 PHE C C 175.67 0.2 1 405 91 91 PHE CA C 60.38 0.2 1 406 91 91 PHE CB C 37.67 0.2 1 407 91 91 PHE N N 121.16 0.2 1 408 92 92 LEU H H 7.19 0.04 1 409 92 92 LEU C C 178.53 0.2 1 410 92 92 LEU CA C 55.04 0.2 1 411 92 92 LEU CB C 41.89 0.2 1 412 92 92 LEU N N 114.20 0.2 1 413 93 93 GLU H H 7.71 0.04 1 414 93 93 GLU C C 175.96 0.2 1 415 93 93 GLU CA C 61.38 0.2 1 416 93 93 GLU CB C 26.62 0.2 1 417 93 93 GLU N N 123.12 0.2 1 418 94 94 PRO C C 179.86 0.2 1 419 94 94 PRO CA C 64.97 0.2 1 420 94 94 PRO CB C 29.91 0.2 1 421 95 95 ILE H H 6.61 0.04 1 422 95 95 ILE C C 177.54 0.2 1 423 95 95 ILE CA C 62.94 0.2 1 424 95 95 ILE CB C 35.53 0.2 1 425 95 95 ILE N N 119.23 0.2 1 426 96 96 HIS H H 8.19 0.04 1 427 96 96 HIS C C 177.52 0.2 1 428 96 96 HIS CA C 55.34 0.2 1 429 96 96 HIS CB C 28.66 0.2 1 430 96 96 HIS N N 121.23 0.2 1 431 97 97 LYS H H 7.62 0.04 1 432 97 97 LYS C C 177.81 0.2 1 433 97 97 LYS CA C 58.03 0.2 1 434 97 97 LYS CB C 31.13 0.2 1 435 97 97 LYS N N 115.38 0.2 1 436 98 98 GLU H H 7.06 0.04 1 437 98 98 GLU C C 175.71 0.2 1 438 98 98 GLU CA C 57.29 0.2 1 439 98 98 GLU CB C 28.57 0.2 1 440 98 98 GLU N N 119.45 0.2 1 441 99 99 PHE H H 7.35 0.04 1 442 99 99 PHE C C 172.45 0.2 1 443 99 99 PHE CA C 53.56 0.2 1 444 99 99 PHE CB C 37.15 0.2 1 445 99 99 PHE N N 116.85 0.2 1 446 103 103 SER C C 175.13 0.2 1 447 103 103 SER CA C 57.27 0.2 1 448 103 103 SER CB C 64.41 0.2 1 449 104 104 SER H H 10.29 0.04 1 450 104 104 SER C C 174.50 0.2 1 451 104 104 SER CA C 63.43 0.2 1 452 104 104 SER CB C 61.54 0.2 1 453 104 104 SER N N 120.89 0.2 1 454 105 105 GLY H H 9.59 0.04 1 455 105 105 GLY C C 179.05 0.2 1 456 105 105 GLY CA C 45.82 0.2 1 457 105 105 GLY N N 109.27 0.2 1 458 106 106 ASP H H 7.63 0.04 1 459 106 106 ASP C C 176.04 0.2 1 460 106 106 ASP CA C 57.85 0.2 1 461 106 106 ASP CB C 38.19 0.2 1 462 106 106 ASP N N 124.85 0.2 1 463 107 107 LEU H H 7.92 0.04 1 464 107 107 LEU C C 178.16 0.2 1 465 107 107 LEU CA C 57.95 0.2 1 466 107 107 LEU CB C 39.96 0.2 1 467 107 107 LEU N N 122.29 0.2 1 468 108 108 PHE H H 8.75 0.04 1 469 108 108 PHE C C 179.38 0.2 1 470 108 108 PHE CA C 57.16 0.2 1 471 108 108 PHE CB C 37.16 0.2 1 472 108 108 PHE N N 116.20 0.2 1 473 109 109 SER H H 7.89 0.04 1 474 109 109 SER C C 175.81 0.2 1 475 109 109 SER CA C 61.23 0.2 1 476 109 109 SER CB C 62.97 0.2 1 477 109 109 SER N N 112.54 0.2 1 478 110 110 LEU H H 8.62 0.04 1 479 110 110 LEU C C 180.64 0.2 1 480 110 110 LEU CA C 56.88 0.2 1 481 110 110 LEU CB C 40.32 0.2 1 482 110 110 LEU N N 127.53 0.2 1 483 111 111 GLY H H 8.66 0.04 1 484 111 111 GLY C C 174.37 0.2 1 485 111 111 GLY CA C 47.42 0.2 1 486 111 111 GLY N N 109.01 0.2 1 487 112 112 GLY H H 6.91 0.04 1 488 112 112 GLY C C 173.91 0.2 1 489 112 112 GLY CA C 46.59 0.2 1 490 112 112 GLY N N 105.11 0.2 1 491 113 113 VAL H H 7.31 0.04 1 492 113 113 VAL C C 176.69 0.2 1 493 113 113 VAL CA C 67.13 0.2 1 494 113 113 VAL CB C 31.58 0.2 1 495 113 113 VAL N N 121.97 0.2 1 496 114 114 THR H H 8.47 0.04 1 497 114 114 THR C C 175.50 0.2 1 498 114 114 THR CA C 65.78 0.2 1 499 114 114 THR CB C 67.74 0.2 1 500 114 114 THR N N 115.55 0.2 1 501 115 115 ALA H H 7.43 0.04 1 502 115 115 ALA C C 177.87 0.2 1 503 115 115 ALA CA C 55.30 0.2 1 504 115 115 ALA CB C 18.43 0.2 1 505 115 115 ALA N N 120.91 0.2 1 506 116 116 VAL H H 7.41 0.04 1 507 116 116 VAL C C 178.53 0.2 1 508 116 116 VAL CA C 67.64 0.2 1 509 116 116 VAL CB C 30.34 0.2 1 510 116 116 VAL N N 114.96 0.2 1 511 117 117 GLN H H 7.83 0.04 1 512 117 117 GLN CA C 59.19 0.2 1 513 117 117 GLN CB C 27.41 0.2 1 514 117 117 GLN N N 114.86 0.2 1 515 118 118 GLU H H 8.95 0.04 1 516 118 118 GLU C C 177.93 0.2 1 517 118 118 GLU CA C 57.69 0.2 1 518 118 118 GLU CB C 28.17 0.2 1 519 118 118 GLU N N 119.63 0.2 1 520 119 119 MET H H 7.40 0.04 1 521 119 119 MET C C 173.43 0.2 1 522 119 119 MET CA C 56.00 0.2 1 523 119 119 MET CB C 30.80 0.2 1 524 119 119 MET N N 119.95 0.2 1 525 120 120 GLN H H 7.39 0.04 1 526 120 120 GLN C C 175.94 0.2 1 527 120 120 GLN CA C 57.21 0.2 1 528 120 120 GLN CB C 24.36 0.2 1 529 120 120 GLN N N 109.04 0.2 1 530 121 121 GLY H H 8.00 0.04 1 531 121 121 GLY C C 169.68 0.2 1 532 121 121 GLY CA C 44.30 0.2 1 533 121 121 GLY N N 105.78 0.2 1 534 125 125 PRO C C 175.94 0.2 1 535 125 125 PRO CA C 61.79 0.2 1 536 125 125 PRO CB C 29.97 0.2 1 537 126 126 TRP C C 173.36 0.2 1 538 126 126 TRP CA C 56.50 0.2 1 539 126 126 TRP CB C 31.55 0.2 1 540 127 127 ARG H H 7.90 0.04 1 541 127 127 ARG C C 172.39 0.2 1 542 127 127 ARG CA C 52.76 0.2 1 543 127 127 ARG CB C 33.01 0.2 1 544 127 127 ARG N N 126.62 0.2 1 545 128 128 CYS H H 6.27 0.04 1 546 128 128 CYS C C 173.30 0.2 1 547 128 128 CYS CA C 53.50 0.2 1 548 128 128 CYS CB C 31.71 0.2 1 549 128 128 CYS N N 113.81 0.2 1 550 129 129 GLY H H 10.06 0.04 1 551 129 129 GLY C C 175.45 0.2 1 552 129 129 GLY CA C 44.30 0.2 1 553 129 129 GLY N N 107.39 0.2 1 554 130 130 ARG H H 8.62 0.04 1 555 130 130 ARG CA C 57.56 0.2 1 556 130 130 ARG CB C 24.83 0.2 1 557 130 130 ARG N N 123.72 0.2 1 558 131 131 VAL C C 172.29 0.2 1 559 131 131 VAL CA C 60.62 0.2 1 560 131 131 VAL CB C 33.72 0.2 1 561 132 132 ASP H H 8.18 0.04 1 562 132 132 ASP C C 177.73 0.2 1 563 132 132 ASP CA C 54.65 0.2 1 564 132 132 ASP CB C 38.25 0.2 1 565 132 132 ASP N N 124.28 0.2 1 566 133 133 THR H H 8.73 0.04 1 567 133 133 THR C C 174.15 0.2 1 568 133 133 THR CA C 59.31 0.2 1 569 133 133 THR CB C 67.84 0.2 1 570 133 133 THR N N 117.18 0.2 1 571 134 134 PRO C C 177.75 0.2 1 572 134 134 PRO CA C 62.83 0.2 1 573 134 134 PRO CB C 32.17 0.2 1 574 135 135 GLU H H 8.75 0.04 1 575 135 135 GLU C C 178.91 0.2 1 576 135 135 GLU CA C 59.84 0.2 1 577 135 135 GLU CB C 28.35 0.2 1 578 135 135 GLU N N 124.47 0.2 1 579 136 136 ASP H H 8.55 0.04 1 580 136 136 ASP C C 176.63 0.2 1 581 136 136 ASP CA C 55.22 0.2 1 582 136 136 ASP CB C 38.74 0.2 1 583 136 136 ASP N N 118.02 0.2 1 584 137 137 THR H H 8.07 0.04 1 585 137 137 THR C C 174.67 0.2 1 586 137 137 THR CA C 61.85 0.2 1 587 137 137 THR CB C 69.69 0.2 1 588 137 137 THR N N 110.71 0.2 1 589 138 138 THR H H 7.66 0.04 1 590 138 138 THR C C 173.04 0.2 1 591 138 138 THR CA C 61.93 0.2 1 592 138 138 THR CB C 68.93 0.2 1 593 138 138 THR N N 124.10 0.2 1 594 139 139 PRO C C 176.20 0.2 1 595 139 139 PRO CA C 62.20 0.2 1 596 139 139 PRO CB C 30.63 0.2 1 597 140 140 ASP H H 8.41 0.04 1 598 140 140 ASP C C 176.23 0.2 1 599 140 140 ASP CA C 54.33 0.2 1 600 140 140 ASP CB C 40.14 0.2 1 601 140 140 ASP N N 120.20 0.2 1 602 141 141 ASN H H 8.89 0.04 1 603 141 141 ASN C C 175.13 0.2 1 604 141 141 ASN CA C 53.61 0.2 1 605 141 141 ASN CB C 39.02 0.2 1 606 141 141 ASN N N 117.79 0.2 1 607 142 142 GLY H H 8.60 0.04 1 608 142 142 GLY C C 176.33 0.2 1 609 142 142 GLY CA C 45.20 0.2 1 610 142 142 GLY N N 111.06 0.2 1 611 143 143 ARG H H 9.22 0.04 1 612 143 143 ARG C C 176.31 0.2 1 613 143 143 ARG CA C 56.31 0.2 1 614 143 143 ARG CB C 30.01 0.2 1 615 143 143 ARG N N 120.33 0.2 1 616 144 144 LEU H H 8.17 0.04 1 617 144 144 LEU C C 175.51 0.2 1 618 144 144 LEU CA C 52.07 0.2 1 619 144 144 LEU CB C 38.11 0.2 1 620 144 144 LEU N N 121.62 0.2 1 621 145 145 PRO C C 175.95 0.2 1 622 145 145 PRO CA C 62.63 0.2 1 623 145 145 PRO CB C 28.91 0.2 1 624 146 146 ASP H H 7.54 0.04 1 625 146 146 ASP C C 172.96 0.2 1 626 146 146 ASP CA C 52.78 0.2 1 627 146 146 ASP CB C 42.48 0.2 1 628 146 146 ASP N N 121.12 0.2 1 629 147 147 ALA H H 7.56 0.04 1 630 147 147 ALA C C 176.53 0.2 1 631 147 147 ALA CA C 50.83 0.2 1 632 147 147 ALA CB C 20.41 0.2 1 633 147 147 ALA N N 116.25 0.2 1 634 148 148 ASP H H 8.01 0.04 1 635 148 148 ASP C C 176.04 0.2 1 636 148 148 ASP CA C 52.17 0.2 1 637 148 148 ASP CB C 38.70 0.2 1 638 148 148 ASP N N 115.69 0.2 1 639 149 149 LYS H H 5.79 0.04 1 640 149 149 LYS C C 172.49 0.2 1 641 149 149 LYS CA C 53.12 0.2 1 642 149 149 LYS CB C 34.69 0.2 1 643 149 149 LYS N N 118.15 0.2 1 644 150 150 ASP H H 6.81 0.04 1 645 150 150 ASP C C 176.24 0.2 1 646 150 150 ASP CA C 51.08 0.2 1 647 150 150 ASP CB C 42.25 0.2 1 648 150 150 ASP N N 115.97 0.2 1 649 151 151 ALA H H 8.39 0.04 1 650 151 151 ALA C C 179.08 0.2 1 651 151 151 ALA CA C 55.02 0.2 1 652 151 151 ALA CB C 18.69 0.2 1 653 151 151 ALA N N 119.76 0.2 1 654 152 152 ASP H H 7.65 0.04 1 655 152 152 ASP C C 178.99 0.2 1 656 152 152 ASP CA C 56.67 0.2 1 657 152 152 ASP CB C 39.92 0.2 1 658 152 152 ASP N N 115.44 0.2 1 659 153 153 TYR H H 7.69 0.04 1 660 153 153 TYR C C 176.86 0.2 1 661 153 153 TYR CA C 60.95 0.2 1 662 153 153 TYR CB C 37.18 0.2 1 663 153 153 TYR N N 121.80 0.2 1 664 154 154 VAL H H 7.91 0.04 1 665 154 154 VAL C C 176.90 0.2 1 666 154 154 VAL CA C 67.24 0.2 1 667 154 154 VAL CB C 30.83 0.2 1 668 154 154 VAL N N 122.74 0.2 1 669 155 155 ARG H H 8.56 0.04 1 670 155 155 ARG C C 180.32 0.2 1 671 155 155 ARG CA C 59.74 0.2 1 672 155 155 ARG CB C 28.72 0.2 1 673 155 155 ARG N N 121.36 0.2 1 674 156 156 THR H H 7.93 0.04 1 675 156 156 THR C C 176.90 0.2 1 676 156 156 THR CA C 65.93 0.2 1 677 156 156 THR CB C 68.21 0.2 1 678 156 156 THR N N 115.86 0.2 1 679 157 157 PHE H H 8.75 0.04 1 680 157 157 PHE C C 177.67 0.2 1 681 157 157 PHE CA C 61.14 0.2 1 682 157 157 PHE CB C 37.30 0.2 1 683 157 157 PHE N N 125.88 0.2 1 684 158 158 PHE H H 7.93 0.04 1 685 158 158 PHE C C 179.06 0.2 1 686 158 158 PHE CA C 61.67 0.2 1 687 158 158 PHE CB C 38.72 0.2 1 688 158 158 PHE N N 114.19 0.2 1 689 159 159 GLN H H 7.53 0.04 1 690 159 159 GLN C C 180.09 0.2 1 691 159 159 GLN CA C 58.77 0.2 1 692 159 159 GLN CB C 26.67 0.2 1 693 159 159 GLN N N 121.74 0.2 1 694 160 160 ARG H H 7.25 0.04 1 695 160 160 ARG C C 174.78 0.2 1 696 160 160 ARG CA C 57.80 0.2 1 697 160 160 ARG CB C 29.40 0.2 1 698 160 160 ARG N N 123.57 0.2 1 699 161 161 LEU H H 6.43 0.04 1 700 161 161 LEU C C 175.53 0.2 1 701 161 161 LEU CA C 53.23 0.2 1 702 161 161 LEU CB C 42.47 0.2 1 703 161 161 LEU N N 112.22 0.2 1 704 162 162 ASN H H 7.76 0.04 1 705 162 162 ASN C C 173.99 0.2 1 706 162 162 ASN CA C 53.20 0.2 1 707 162 162 ASN CB C 37.25 0.2 1 708 162 162 ASN N N 113.41 0.2 1 709 163 163 MET H H 7.33 0.04 1 710 163 163 MET C C 176.27 0.2 1 711 163 163 MET CA C 52.41 0.2 1 712 163 163 MET CB C 32.67 0.2 1 713 163 163 MET N N 114.04 0.2 1 714 164 164 ASN H H 9.85 0.04 1 715 164 164 ASN C C 174.38 0.2 1 716 164 164 ASN CA C 50.33 0.2 1 717 164 164 ASN CB C 38.42 0.2 1 718 164 164 ASN N N 126.37 0.2 1 719 165 165 ASP H H 7.99 0.04 1 720 165 165 ASP C C 176.87 0.2 1 721 165 165 ASP CA C 57.48 0.2 1 722 165 165 ASP CB C 40.15 0.2 1 723 165 165 ASP N N 114.70 0.2 1 724 166 166 ARG H H 7.64 0.04 1 725 166 166 ARG C C 177.30 0.2 1 726 166 166 ARG CA C 60.06 0.2 1 727 166 166 ARG CB C 29.39 0.2 1 728 166 166 ARG N N 117.96 0.2 1 729 167 167 GLU H H 7.78 0.04 1 730 167 167 GLU C C 177.96 0.2 1 731 167 167 GLU CA C 59.08 0.2 1 732 167 167 GLU CB C 29.63 0.2 1 733 167 167 GLU N N 117.54 0.2 1 734 168 168 VAL H H 8.20 0.04 1 735 168 168 VAL C C 177.23 0.2 1 736 168 168 VAL CA C 66.94 0.2 1 737 168 168 VAL CB C 30.36 0.2 1 738 168 168 VAL N N 118.07 0.2 1 739 169 169 VAL H H 8.09 0.04 1 740 169 169 VAL C C 180.45 0.2 1 741 169 169 VAL CA C 67.08 0.2 1 742 169 169 VAL CB C 31.21 0.2 1 743 169 169 VAL N N 117.28 0.2 1 744 170 170 ALA H H 9.11 0.04 1 745 170 170 ALA C C 180.15 0.2 1 746 170 170 ALA CA C 55.66 0.2 1 747 170 170 ALA CB C 16.15 0.2 1 748 170 170 ALA N N 123.38 0.2 1 749 171 171 LEU H H 8.75 0.04 1 750 171 171 LEU C C 179.89 0.2 1 751 171 171 LEU CA C 58.42 0.2 1 752 171 171 LEU CB C 41.31 0.2 1 753 171 171 LEU N N 118.03 0.2 1 754 172 172 MET H H 8.67 0.04 1 755 172 172 MET C C 179.39 0.2 1 756 172 172 MET CA C 58.36 0.2 1 757 172 172 MET CB C 32.16 0.2 1 758 172 172 MET N N 118.71 0.2 1 759 173 173 GLY H H 8.96 0.04 1 760 173 173 GLY C C 177.71 0.2 1 761 173 173 GLY CA C 47.31 0.2 1 762 173 173 GLY N N 105.14 0.2 1 763 174 174 ALA H H 10.10 0.04 1 764 174 174 ALA CA C 55.49 0.2 1 765 174 174 ALA CB C 20.83 0.2 1 766 174 174 ALA N N 124.11 0.2 1 767 175 175 HIS C C 172.84 0.2 1 768 175 175 HIS CA C 59.16 0.2 1 769 176 176 ALA H H 8.52 0.04 1 770 176 176 ALA C C 179.61 0.2 1 771 176 176 ALA CA C 54.94 0.2 1 772 176 176 ALA CB C 18.47 0.2 1 773 176 176 ALA N N 116.71 0.2 1 774 177 177 LEU H H 8.30 0.04 1 775 177 177 LEU C C 173.59 0.2 1 776 177 177 LEU CA C 51.60 0.2 1 777 177 177 LEU N N 116.84 0.2 1 778 178 178 GLY H H 8.25 0.04 1 779 178 178 GLY C C 173.53 0.2 1 780 178 178 GLY CA C 43.76 0.2 1 781 178 178 GLY N N 100.75 0.2 1 782 179 179 LYS H H 7.11 0.04 1 783 179 179 LYS C C 171.20 0.2 1 784 179 179 LYS CA C 54.15 0.2 1 785 179 179 LYS CB C 30.55 0.2 1 786 179 179 LYS N N 116.50 0.2 1 787 180 180 THR H H 6.14 0.04 1 788 180 180 THR C C 175.92 0.2 1 789 180 180 THR CA C 59.13 0.2 1 790 180 180 THR CB C 68.88 0.2 1 791 180 180 THR N N 104.56 0.2 1 792 181 181 HIS H H 9.44 0.04 1 793 181 181 HIS C C 176.99 0.2 1 794 181 181 HIS CA C 54.01 0.2 1 795 181 181 HIS CB C 29.27 0.2 1 796 181 181 HIS N N 123.63 0.2 1 797 182 182 LEU H H 8.66 0.04 1 798 182 182 LEU C C 180.71 0.2 1 799 182 182 LEU CA C 59.34 0.2 1 800 182 182 LEU CB C 41.85 0.2 1 801 182 182 LEU N N 131.88 0.2 1 802 183 183 LYS H H 8.79 0.04 1 803 183 183 LYS C C 177.25 0.2 1 804 183 183 LYS CA C 57.55 0.2 1 805 183 183 LYS CB C 31.10 0.2 1 806 183 183 LYS N N 114.23 0.2 1 807 184 184 ASN H H 7.99 0.04 1 808 184 184 ASN C C 176.67 0.2 1 809 184 184 ASN CA C 54.07 0.2 1 810 184 184 ASN CB C 38.21 0.2 1 811 184 184 ASN N N 116.08 0.2 1 812 185 185 SER H H 8.19 0.04 1 813 185 185 SER C C 175.95 0.2 1 814 185 185 SER CA C 58.82 0.2 1 815 185 185 SER CB C 67.32 0.2 1 816 185 185 SER N N 110.05 0.2 1 817 186 186 GLY H H 8.41 0.04 1 818 186 186 GLY C C 171.54 0.2 1 819 186 186 GLY CA C 44.96 0.2 1 820 186 186 GLY N N 110.84 0.2 1 821 187 187 TYR H H 7.37 0.04 1 822 187 187 TYR C C 170.53 0.2 1 823 187 187 TYR CA C 57.85 0.2 1 824 187 187 TYR CB C 39.52 0.2 1 825 187 187 TYR N N 119.55 0.2 1 826 188 188 GLU H H 7.51 0.04 1 827 188 188 GLU C C 175.98 0.2 1 828 188 188 GLU CA C 54.57 0.2 1 829 188 188 GLU CB C 32.75 0.2 1 830 188 188 GLU N N 117.82 0.2 1 831 189 189 GLY H H 6.70 0.04 1 832 189 189 GLY CA C 42.55 0.2 1 833 189 189 GLY N N 117.68 0.2 1 834 190 190 PRO C C 174.48 0.2 1 835 191 191 TRP H H 7.73 0.04 1 836 191 191 TRP C C 177.48 0.2 1 837 191 191 TRP CA C 61.76 0.2 1 838 191 191 TRP CB C 31.46 0.2 1 839 191 191 TRP N N 122.00 0.2 1 840 192 192 GLY H H 7.26 0.04 1 841 192 192 GLY C C 172.41 0.2 1 842 192 192 GLY CA C 44.66 0.2 1 843 192 192 GLY N N 102.74 0.2 1 844 193 193 ALA H H 9.70 0.04 1 845 193 193 ALA C C 179.05 0.2 1 846 193 193 ALA CA C 52.65 0.2 1 847 193 193 ALA CB C 19.72 0.2 1 848 193 193 ALA N N 122.89 0.2 1 849 194 194 ALA H H 8.56 0.04 1 850 194 194 ALA C C 177.56 0.2 1 851 194 194 ALA CA C 51.13 0.2 1 852 194 194 ALA CB C 16.77 0.2 1 853 194 194 ALA N N 124.70 0.2 1 854 195 195 ASN H H 8.04 0.04 1 855 195 195 ASN C C 175.40 0.2 1 856 195 195 ASN CA C 54.23 0.2 1 857 195 195 ASN CB C 38.00 0.2 1 858 195 195 ASN N N 113.71 0.2 1 859 196 196 ASN H H 7.79 0.04 1 860 196 196 ASN C C 173.21 0.2 1 861 196 196 ASN CA C 51.27 0.2 1 862 196 196 ASN CB C 36.34 0.2 1 863 196 196 ASN N N 114.97 0.2 1 864 197 197 VAL H H 7.24 0.04 1 865 197 197 VAL C C 173.63 0.2 1 866 197 197 VAL CA C 60.58 0.2 1 867 197 197 VAL CB C 33.98 0.2 1 868 197 197 VAL N N 116.92 0.2 1 869 198 198 PHE H H 9.02 0.04 1 870 198 198 PHE C C 173.60 0.2 1 871 198 198 PHE CA C 59.02 0.2 1 872 198 198 PHE CB C 38.68 0.2 1 873 198 198 PHE N N 128.70 0.2 1 874 199 199 THR H H 7.00 0.04 1 875 199 199 THR C C 173.59 0.2 1 876 199 199 THR CA C 60.29 0.2 1 877 199 199 THR CB C 73.02 0.2 1 878 199 199 THR N N 117.88 0.2 1 879 200 200 ASN H H 9.01 0.04 1 880 200 200 ASN C C 176.32 0.2 1 881 200 200 ASN CA C 53.01 0.2 1 882 200 200 ASN CB C 37.06 0.2 1 883 200 200 ASN N N 116.80 0.2 1 884 201 201 GLU H H 8.78 0.04 1 885 201 201 GLU C C 176.48 0.2 1 886 201 201 GLU CA C 59.89 0.2 1 887 201 201 GLU CB C 28.95 0.2 1 888 201 201 GLU N N 120.10 0.2 1 889 202 202 PHE H H 8.46 0.04 1 890 202 202 PHE C C 176.16 0.2 1 891 202 202 PHE CA C 62.48 0.2 1 892 202 202 PHE CB C 39.98 0.2 1 893 202 202 PHE N N 118.61 0.2 1 894 203 203 TYR H H 6.95 0.04 1 895 203 203 TYR C C 178.27 0.2 1 896 203 203 TYR CA C 59.93 0.2 1 897 203 203 TYR CB C 37.34 0.2 1 898 203 203 TYR N N 115.74 0.2 1 899 204 204 LEU H H 7.28 0.04 1 900 204 204 LEU C C 179.27 0.2 1 901 204 204 LEU CA C 57.72 0.2 1 902 204 204 LEU CB C 41.01 0.2 1 903 204 204 LEU N N 116.75 0.2 1 904 205 205 ASN H H 9.12 0.04 1 905 205 205 ASN C C 178.66 0.2 1 906 205 205 ASN CA C 55.32 0.2 1 907 205 205 ASN CB C 35.12 0.2 1 908 205 205 ASN N N 119.47 0.2 1 909 206 206 LEU H H 8.48 0.04 1 910 206 206 LEU C C 178.51 0.2 1 911 206 206 LEU CA C 58.73 0.2 1 912 206 206 LEU CB C 41.24 0.2 1 913 206 206 LEU N N 123.88 0.2 1 914 207 207 LEU H H 7.45 0.04 1 915 207 207 LEU C C 179.47 0.2 1 916 207 207 LEU CA C 56.40 0.2 1 917 207 207 LEU CB C 42.41 0.2 1 918 207 207 LEU N N 113.04 0.2 1 919 208 208 ASN H H 8.58 0.04 1 920 208 208 ASN C C 177.13 0.2 1 921 208 208 ASN CA C 54.46 0.2 1 922 208 208 ASN CB C 39.71 0.2 1 923 208 208 ASN N N 114.81 0.2 1 924 209 209 GLU H H 7.87 0.04 1 925 209 209 GLU C C 173.86 0.2 1 926 209 209 GLU CA C 55.07 0.2 1 927 209 209 GLU CB C 29.37 0.2 1 928 209 209 GLU N N 119.13 0.2 1 929 210 210 ASP H H 8.15 0.04 1 930 210 210 ASP C C 175.42 0.2 1 931 210 210 ASP CA C 52.46 0.2 1 932 210 210 ASP CB C 40.38 0.2 1 933 210 210 ASP N N 120.00 0.2 1 934 211 211 TRP H H 7.91 0.04 1 935 211 211 TRP C C 176.70 0.2 1 936 211 211 TRP CA C 56.10 0.2 1 937 211 211 TRP CB C 32.62 0.2 1 938 211 211 TRP N N 124.87 0.2 1 939 212 212 LYS H H 9.23 0.04 1 940 212 212 LYS C C 174.13 0.2 1 941 212 212 LYS CA C 54.81 0.2 1 942 212 212 LYS CB C 35.09 0.2 1 943 212 212 LYS N N 124.31 0.2 1 944 213 213 LEU H H 8.08 0.04 1 945 213 213 LEU C C 176.30 0.2 1 946 213 213 LEU CA C 54.55 0.2 1 947 213 213 LEU CB C 39.28 0.2 1 948 213 213 LEU N N 131.23 0.2 1 949 214 214 GLU H H 8.85 0.04 1 950 214 214 GLU C C 174.21 0.2 1 951 214 214 GLU CA C 53.98 0.2 1 952 214 214 GLU CB C 31.65 0.2 1 953 214 214 GLU N N 127.31 0.2 1 954 215 215 LYS H H 8.19 0.04 1 955 215 215 LYS C C 176.94 0.2 1 956 215 215 LYS CA C 55.08 0.2 1 957 215 215 LYS CB C 32.59 0.2 1 958 215 215 LYS N N 119.94 0.2 1 959 216 216 ASN H H 8.41 0.04 1 960 216 216 ASN C C 178.05 0.2 1 961 216 216 ASN CA C 50.44 0.2 1 962 216 216 ASN CB C 38.64 0.2 1 963 216 216 ASN N N 122.77 0.2 1 964 217 217 ASP H H 8.62 0.04 1 965 217 217 ASP C C 176.66 0.2 1 966 217 217 ASP CA C 56.39 0.2 1 967 217 217 ASP CB C 39.77 0.2 1 968 217 217 ASP N N 117.53 0.2 1 969 218 218 ALA H H 8.05 0.04 1 970 218 218 ALA C C 175.84 0.2 1 971 218 218 ALA CA C 50.98 0.2 1 972 218 218 ALA CB C 17.51 0.2 1 973 218 218 ALA N N 122.52 0.2 1 974 219 219 ASN H H 8.13 0.04 1 975 219 219 ASN C C 173.76 0.2 1 976 219 219 ASN CA C 54.29 0.2 1 977 219 219 ASN CB C 36.81 0.2 1 978 219 219 ASN N N 112.81 0.2 1 979 220 220 ASN H H 7.36 0.04 1 980 220 220 ASN C C 174.31 0.2 1 981 220 220 ASN CA C 51.14 0.2 1 982 220 220 ASN CB C 39.56 0.2 1 983 220 220 ASN N N 115.65 0.2 1 984 221 221 GLU H H 8.11 0.04 1 985 221 221 GLU C C 175.07 0.2 1 986 221 221 GLU CA C 55.36 0.2 1 987 221 221 GLU CB C 29.23 0.2 1 988 221 221 GLU N N 119.91 0.2 1 989 222 222 GLN H H 8.68 0.04 1 990 222 222 GLN C C 172.01 0.2 1 991 222 222 GLN CA C 53.58 0.2 1 992 222 222 GLN CB C 31.65 0.2 1 993 222 222 GLN N N 117.55 0.2 1 994 223 223 TRP H H 8.32 0.04 1 995 223 223 TRP C C 174.74 0.2 1 996 223 223 TRP CA C 55.73 0.2 1 997 223 223 TRP CB C 28.75 0.2 1 998 223 223 TRP N N 123.63 0.2 1 999 224 224 ASP H H 9.49 0.04 1 1000 224 224 ASP C C 176.59 0.2 1 1001 224 224 ASP CA C 51.97 0.2 1 1002 224 224 ASP CB C 42.33 0.2 1 1003 224 224 ASP N N 120.32 0.2 1 1004 225 225 SER H H 8.93 0.04 1 1005 225 225 SER C C 177.07 0.2 1 1006 225 225 SER CA C 54.81 0.2 1 1007 225 225 SER CB C 65.25 0.2 1 1008 225 225 SER N N 118.96 0.2 1 1009 226 226 LYS H H 8.73 0.04 1 1010 226 226 LYS C C 177.58 0.2 1 1011 226 226 LYS CA C 57.93 0.2 1 1012 226 226 LYS CB C 30.61 0.2 1 1013 226 226 LYS N N 125.01 0.2 1 1014 227 227 SER H H 7.45 0.04 1 1015 227 227 SER C C 173.16 0.2 1 1016 227 227 SER CA C 57.50 0.2 1 1017 227 227 SER CB C 61.66 0.2 1 1018 227 227 SER N N 113.04 0.2 1 1019 228 228 GLY H H 7.60 0.04 1 1020 228 228 GLY C C 174.07 0.2 1 1021 228 228 GLY CA C 44.13 0.2 1 1022 228 228 GLY N N 106.64 0.2 1 1023 229 229 TYR H H 6.40 0.04 1 1024 229 229 TYR C C 174.75 0.2 1 1025 229 229 TYR CA C 52.54 0.2 1 1026 229 229 TYR CB C 39.17 0.2 1 1027 229 229 TYR N N 120.07 0.2 1 1028 230 230 MET H H 9.18 0.04 1 1029 230 230 MET C C 172.58 0.2 1 1030 230 230 MET CA C 53.42 0.2 1 1031 230 230 MET CB C 36.95 0.2 1 1032 230 230 MET N N 124.20 0.2 1 1033 231 231 MET H H 8.65 0.04 1 1034 231 231 MET C C 176.70 0.2 1 1035 231 231 MET CA C 53.46 0.2 1 1036 231 231 MET CB C 35.83 0.2 1 1037 231 231 MET N N 113.13 0.2 1 1038 232 232 LEU H H 10.14 0.04 1 1039 232 232 LEU C C 177.66 0.2 1 1040 232 232 LEU CA C 52.19 0.2 1 1041 232 232 LEU CB C 39.08 0.2 1 1042 232 232 LEU N N 121.98 0.2 1 1043 233 233 PRO C C 179.19 0.2 1 1044 233 233 PRO CA C 66.90 0.2 1 1045 233 233 PRO CB C 29.92 0.2 1 1046 234 234 THR H H 6.87 0.04 1 1047 234 234 THR C C 177.17 0.2 1 1048 234 234 THR CA C 64.46 0.2 1 1049 234 234 THR CB C 66.00 0.2 1 1050 234 234 THR N N 106.59 0.2 1 1051 235 235 ASP H H 6.45 0.04 1 1052 235 235 ASP C C 177.38 0.2 1 1053 235 235 ASP CA C 57.85 0.2 1 1054 235 235 ASP CB C 44.85 0.2 1 1055 235 235 ASP N N 121.66 0.2 1 1056 236 236 TYR H H 8.04 0.04 1 1057 236 236 TYR C C 177.45 0.2 1 1058 236 236 TYR CA C 60.26 0.2 1 1059 236 236 TYR CB C 38.76 0.2 1 1060 236 236 TYR N N 118.99 0.2 1 1061 237 237 SER H H 7.68 0.04 1 1062 237 237 SER C C 175.61 0.2 1 1063 237 237 SER CA C 61.61 0.2 1 1064 237 237 SER CB C 62.01 0.2 1 1065 237 237 SER N N 113.85 0.2 1 1066 238 238 LEU H H 7.66 0.04 1 1067 238 238 LEU C C 176.77 0.2 1 1068 238 238 LEU CA C 56.28 0.2 1 1069 238 238 LEU CB C 40.63 0.2 1 1070 238 238 LEU N N 120.70 0.2 1 1071 239 239 ILE H H 7.26 0.04 1 1072 239 239 ILE C C 177.31 0.2 1 1073 239 239 ILE CA C 59.75 0.2 1 1074 239 239 ILE CB C 37.12 0.2 1 1075 239 239 ILE N N 102.74 0.2 1 1076 240 240 GLN H H 7.30 0.04 1 1077 240 240 GLN C C 175.90 0.2 1 1078 240 240 GLN CA C 55.88 0.2 1 1079 240 240 GLN CB C 29.13 0.2 1 1080 240 240 GLN N N 120.85 0.2 1 1081 241 241 ASP H H 7.34 0.04 1 1082 241 241 ASP C C 173.88 0.2 1 1083 241 241 ASP CA C 50.44 0.2 1 1084 241 241 ASP CB C 43.94 0.2 1 1085 241 241 ASP N N 123.02 0.2 1 1086 242 242 PRO C C 179.44 0.2 1 1087 242 242 PRO CA C 64.76 0.2 1 1088 243 243 LYS H H 7.45 0.04 1 1089 243 243 LYS C C 180.32 0.2 1 1090 243 243 LYS CA C 58.22 0.2 1 1091 243 243 LYS CB C 30.68 0.2 1 1092 243 243 LYS N N 118.82 0.2 1 1093 244 244 TYR H H 8.52 0.04 1 1094 244 244 TYR C C 179.09 0.2 1 1095 244 244 TYR CA C 57.47 0.2 1 1096 244 244 TYR CB C 36.82 0.2 1 1097 244 244 TYR N N 121.32 0.2 1 1098 245 245 LEU H H 8.77 0.04 1 1099 245 245 LEU C C 178.31 0.2 1 1100 245 245 LEU CA C 58.13 0.2 1 1101 245 245 LEU CB C 40.58 0.2 1 1102 245 245 LEU N N 122.31 0.2 1 1103 246 246 SER H H 7.10 0.04 1 1104 246 246 SER C C 176.64 0.2 1 1105 246 246 SER CA C 61.22 0.2 1 1106 246 246 SER CB C 62.59 0.2 1 1107 246 246 SER N N 110.19 0.2 1 1108 247 247 ILE H H 7.35 0.04 1 1109 247 247 ILE C C 176.90 0.2 1 1110 247 247 ILE CA C 64.24 0.2 1 1111 247 247 ILE CB C 37.46 0.2 1 1112 247 247 ILE N N 123.71 0.2 1 1113 248 248 VAL H H 8.63 0.04 1 1114 248 248 VAL C C 178.61 0.2 1 1115 248 248 VAL CA C 66.67 0.2 1 1116 248 248 VAL CB C 30.93 0.2 1 1117 248 248 VAL N N 122.43 0.2 1 1118 249 249 LYS H H 8.20 0.04 1 1119 249 249 LYS C C 179.15 0.2 1 1120 249 249 LYS CA C 59.85 0.2 1 1121 249 249 LYS CB C 31.88 0.2 1 1122 249 249 LYS N N 115.81 0.2 1 1123 250 250 GLU H H 7.29 0.04 1 1124 250 250 GLU C C 180.15 0.2 1 1125 250 250 GLU CA C 59.14 0.2 1 1126 250 250 GLU CB C 29.11 0.2 1 1127 250 250 GLU N N 120.63 0.2 1 1128 251 251 TYR H H 7.85 0.04 1 1129 251 251 TYR C C 179.01 0.2 1 1130 251 251 TYR CA C 55.67 0.2 1 1131 251 251 TYR CB C 35.49 0.2 1 1132 251 251 TYR N N 120.09 0.2 1 1133 252 252 ALA H H 8.69 0.04 1 1134 252 252 ALA C C 177.74 0.2 1 1135 252 252 ALA CA C 54.51 0.2 1 1136 252 252 ALA CB C 18.12 0.2 1 1137 252 252 ALA N N 122.06 0.2 1 1138 253 253 ASN H H 7.34 0.04 1 1139 253 253 ASN C C 175.11 0.2 1 1140 253 253 ASN CA C 53.80 0.2 1 1141 253 253 ASN CB C 39.81 0.2 1 1142 253 253 ASN N N 112.54 0.2 1 1143 254 254 ASP H H 7.73 0.04 1 1144 254 254 ASP C C 174.39 0.2 1 1145 254 254 ASP CA C 52.90 0.2 1 1146 254 254 ASP CB C 41.28 0.2 1 1147 254 254 ASP N N 120.55 0.2 1 1148 255 255 GLN H H 9.18 0.04 1 1149 255 255 GLN C C 176.93 0.2 1 1150 255 255 GLN CA C 59.43 0.2 1 1151 255 255 GLN CB C 29.79 0.2 1 1152 255 255 GLN N N 126.15 0.2 1 1153 256 256 ASP H H 8.20 0.04 1 1154 256 256 ASP C C 178.55 0.2 1 1155 256 256 ASP CA C 57.55 0.2 1 1156 256 256 ASP CB C 40.28 0.2 1 1157 256 256 ASP N N 119.00 0.2 1 1158 257 257 LYS H H 7.70 0.04 1 1159 257 257 LYS C C 178.15 0.2 1 1160 257 257 LYS CA C 58.37 0.2 1 1161 257 257 LYS CB C 31.52 0.2 1 1162 257 257 LYS N N 122.19 0.2 1 1163 258 258 PHE H H 7.53 0.04 1 1164 258 258 PHE C C 176.18 0.2 1 1165 258 258 PHE CA C 58.56 0.2 1 1166 258 258 PHE CB C 37.23 0.2 1 1167 258 258 PHE N N 118.77 0.2 1 1168 259 259 PHE H H 9.07 0.04 1 1169 259 259 PHE C C 178.31 0.2 1 1170 259 259 PHE CA C 59.89 0.2 1 1171 259 259 PHE CB C 36.76 0.2 1 1172 259 259 PHE N N 121.31 0.2 1 1173 260 260 LYS H H 7.98 0.04 1 1174 260 260 LYS C C 179.84 0.2 1 1175 260 260 LYS CA C 59.31 0.2 1 1176 260 260 LYS CB C 31.72 0.2 1 1177 260 260 LYS N N 119.04 0.2 1 1178 261 261 ASP H H 8.45 0.04 1 1179 261 261 ASP C C 179.91 0.2 1 1180 261 261 ASP CA C 56.85 0.2 1 1181 261 261 ASP CB C 38.61 0.2 1 1182 261 261 ASP N N 122.01 0.2 1 1183 262 262 PHE H H 9.92 0.04 1 1184 262 262 PHE C C 176.53 0.2 1 1185 262 262 PHE CA C 62.85 0.2 1 1186 262 262 PHE CB C 38.30 0.2 1 1187 262 262 PHE N N 123.80 0.2 1 1188 263 263 SER H H 8.26 0.04 1 1189 263 263 SER C C 176.44 0.2 1 1190 263 263 SER CA C 61.21 0.2 1 1191 263 263 SER CB C 62.33 0.2 1 1192 263 263 SER N N 112.88 0.2 1 1193 264 264 LYS H H 7.14 0.04 1 1194 264 264 LYS C C 179.38 0.2 1 1195 264 264 LYS CA C 58.49 0.2 1 1196 264 264 LYS CB C 32.05 0.2 1 1197 264 264 LYS N N 117.41 0.2 1 1198 265 265 ALA H H 8.02 0.04 1 1199 265 265 ALA C C 178.56 0.2 1 1200 265 265 ALA CA C 54.72 0.2 1 1201 265 265 ALA CB C 17.28 0.2 1 1202 265 265 ALA N N 123.08 0.2 1 1203 266 266 PHE H H 9.22 0.04 1 1204 266 266 PHE C C 177.30 0.2 1 1205 266 266 PHE CA C 59.80 0.2 1 1206 266 266 PHE CB C 38.54 0.2 1 1207 266 266 PHE N N 120.28 0.2 1 1208 267 267 GLU H H 7.79 0.04 1 1209 267 267 GLU C C 177.15 0.2 1 1210 267 267 GLU CA C 59.58 0.2 1 1211 267 267 GLU CB C 25.51 0.2 1 1212 267 267 GLU N N 117.54 0.2 1 1213 268 268 LYS H H 7.46 0.04 1 1214 268 268 LYS C C 178.72 0.2 1 1215 268 268 LYS CA C 59.04 0.2 1 1216 268 268 LYS CB C 31.92 0.2 1 1217 268 268 LYS N N 118.88 0.2 1 1218 269 269 LEU H H 8.16 0.04 1 1219 269 269 LEU C C 179.50 0.2 1 1220 269 269 LEU CA C 57.11 0.2 1 1221 269 269 LEU CB C 41.56 0.2 1 1222 269 269 LEU N N 119.70 0.2 1 1223 270 270 LEU H H 7.47 0.04 1 1224 270 270 LEU C C 178.08 0.2 1 1225 270 270 LEU CA C 56.08 0.2 1 1226 270 270 LEU CB C 40.18 0.2 1 1227 270 270 LEU N N 118.16 0.2 1 1228 271 271 GLU H H 7.56 0.04 1 1229 271 271 GLU C C 176.10 0.2 1 1230 271 271 GLU CA C 55.20 0.2 1 1231 271 271 GLU CB C 29.33 0.2 1 1232 271 271 GLU N N 119.95 0.2 1 1233 272 272 ASN H H 7.12 0.04 1 1234 272 272 ASN C C 176.39 0.2 1 1235 272 272 ASN CA C 52.94 0.2 1 1236 272 272 ASN CB C 36.77 0.2 1 1237 272 272 ASN N N 123.20 0.2 1 1238 273 273 GLY H H 8.29 0.04 1 1239 273 273 GLY C C 174.58 0.2 1 1240 273 273 GLY CA C 45.27 0.2 1 1241 273 273 GLY N N 110.04 0.2 1 1242 274 274 ILE H H 7.53 0.04 1 1243 274 274 ILE C C 175.24 0.2 1 1244 274 274 ILE CA C 61.03 0.2 1 1245 274 274 ILE CB C 37.67 0.2 1 1246 274 274 ILE N N 121.76 0.2 1 1247 275 275 THR H H 8.73 0.04 1 1248 275 275 THR C C 172.59 0.2 1 1249 275 275 THR CA C 61.42 0.2 1 1250 275 275 THR CB C 69.32 0.2 1 1251 275 275 THR N N 125.06 0.2 1 1252 276 276 PHE H H 9.11 0.04 1 1253 276 276 PHE C C 173.76 0.2 1 1254 276 276 PHE CA C 55.40 0.2 1 1255 276 276 PHE CB C 38.00 0.2 1 1256 276 276 PHE N N 129.34 0.2 1 1257 277 277 PRO C C 177.13 0.2 1 1258 277 277 PRO CA C 61.92 0.2 1 1259 277 277 PRO CB C 32.26 0.2 1 1260 278 278 LYS H H 8.76 0.04 1 1261 278 278 LYS C C 176.83 0.2 1 1262 278 278 LYS CA C 58.47 0.2 1 1263 278 278 LYS CB C 31.19 0.2 1 1264 278 278 LYS N N 121.69 0.2 1 1265 279 279 ASP H H 8.13 0.04 1 1266 279 279 ASP C C 175.81 0.2 1 1267 279 279 ASP CA C 52.49 0.2 1 1268 279 279 ASP CB C 38.98 0.2 1 1269 279 279 ASP N N 114.93 0.2 1 1270 280 280 ALA H H 7.48 0.04 1 1271 280 280 ALA C C 175.26 0.2 1 1272 280 280 ALA CA C 50.44 0.2 1 1273 280 280 ALA CB C 16.88 0.2 1 1274 280 280 ALA N N 124.18 0.2 1 1275 281 281 PRO C C 176.93 0.2 1 1276 281 281 PRO CA C 62.13 0.2 1 1277 281 281 PRO CB C 30.68 0.2 1 1278 282 282 SER H H 8.26 0.04 1 1279 282 282 SER C C 170.88 0.2 1 1280 282 282 SER CA C 57.73 0.2 1 1281 282 282 SER CB C 60.85 0.2 1 1282 282 282 SER N N 119.30 0.2 1 1283 283 283 PRO C C 175.67 0.2 1 1284 283 283 PRO CA C 62.96 0.2 1 1285 283 283 PRO CB C 31.19 0.2 1 1286 284 284 PHE H H 9.02 0.04 1 1287 284 284 PHE C C 174.91 0.2 1 1288 284 284 PHE CA C 53.75 0.2 1 1289 284 284 PHE CB C 39.40 0.2 1 1290 284 284 PHE N N 124.90 0.2 1 1291 285 285 ILE H H 7.84 0.04 1 1292 285 285 ILE C C 176.69 0.2 1 1293 285 285 ILE CA C 58.72 0.2 1 1294 285 285 ILE CB C 36.62 0.2 1 1295 285 285 ILE N N 120.47 0.2 1 1296 286 286 PHE H H 9.77 0.04 1 1297 286 286 PHE C C 177.03 0.2 1 1298 286 286 PHE CA C 58.82 0.2 1 1299 286 286 PHE CB C 38.90 0.2 1 1300 286 286 PHE N N 130.06 0.2 1 1301 287 287 LYS H H 8.61 0.04 1 1302 287 287 LYS C C 176.82 0.2 1 1303 287 287 LYS CA C 54.76 0.2 1 1304 287 287 LYS CB C 33.17 0.2 1 1305 287 287 LYS N N 123.70 0.2 1 1306 288 288 THR H H 8.55 0.04 1 1307 288 288 THR C C 178.49 0.2 1 1308 288 288 THR CA C 59.76 0.2 1 1309 288 288 THR CB C 70.13 0.2 1 1310 288 288 THR N N 110.65 0.2 1 1311 289 289 LEU H H 9.46 0.04 1 1312 289 289 LEU C C 180.66 0.2 1 1313 289 289 LEU CA C 58.74 0.2 1 1314 289 289 LEU CB C 38.81 0.2 1 1315 289 289 LEU N N 122.25 0.2 1 1316 290 290 GLU H H 8.95 0.04 1 1317 290 290 GLU C C 180.81 0.2 1 1318 290 290 GLU CA C 59.09 0.2 1 1319 290 290 GLU CB C 28.48 0.2 1 1320 290 290 GLU N N 120.60 0.2 1 1321 291 291 GLU H H 7.94 0.04 1 1322 291 291 GLU C C 178.55 0.2 1 1323 291 291 GLU CA C 58.33 0.2 1 1324 291 291 GLU CB C 29.37 0.2 1 1325 291 291 GLU N N 121.01 0.2 1 1326 292 292 GLN H H 7.48 0.04 1 1327 292 292 GLN C C 175.57 0.2 1 1328 292 292 GLN CA C 55.67 0.2 1 1329 292 292 GLN CB C 31.35 0.2 1 1330 292 292 GLN N N 116.90 0.2 1 1331 293 293 GLY H H 7.79 0.04 1 1332 293 293 GLY C C 174.27 0.2 1 1333 293 293 GLY CA C 45.04 0.2 1 1334 293 293 GLY N N 108.29 0.2 1 1335 294 294 LEU H H 7.66 0.04 1 1336 294 294 LEU C C 175.90 0.2 1 1337 294 294 LEU CA C 53.40 0.2 1 1338 294 294 LEU CB C 40.31 0.2 1 1339 294 294 LEU N N 122.07 0.2 1 1340 295 295 HIS H H 8.10 0.04 1 1341 295 295 HIS C C 174.60 0.2 1 1342 295 295 HIS CA C 54.90 0.2 1 1343 295 295 HIS CB C 29.43 0.2 1 1344 295 295 HIS N N 120.77 0.2 1 1345 296 296 HIS H H 8.65 0.04 1 1346 296 296 HIS C C 174.26 0.2 1 1347 296 296 HIS CA C 55.31 0.2 1 1348 296 296 HIS CB C 29.69 0.2 1 1349 296 296 HIS N N 122.28 0.2 1 1350 297 297 HIS H H 8.22 0.04 1 1351 297 297 HIS C C 178.89 0.2 1 1352 297 297 HIS CA C 56.71 0.2 1 1353 297 297 HIS CB C 29.07 0.2 1 1354 297 297 HIS N N 125.75 0.2 1 stop_ save_