data_19884 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Yeast cytochrome c peroxidase assignment ; _BMRB_accession_number 19884 _BMRB_flat_file_name bmr19884.str _Entry_type original _Submission_date 2014-04-01 _Accession_date 2014-04-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Amide backbone assignment for yeast cytochrome c peroxidase C128A with MSKT as first four residues.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schilder Jesika . . 2 Ubbink Marcellus . . 3 Loehr Frank . . 4 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 240 "13C chemical shifts" 757 "15N chemical shifts" 240 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-06-18 update author 'update chemical shifts' 2014-04-15 update BMRB 'update entry citation' 2014-04-08 original author 'original release' stop_ _Original_release_date 2015-06-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The cytochrome c peroxidase and cytochrome c encounter complex: The other side of the story. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24726731 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Schilder Jesika . . 2 Lohr Frank . . 3 Schwalbe Harald . . 4 Ubbink Marcellus . . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full 'FEBS letters' _Journal_volume 588 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1873 _Page_last 1878 _Year 2014 _Details . loop_ _Keyword 'Electron transfer' 'Paramagnetic NMR' 'Paramagnetic relaxation enhancement' 'Protein complex' 'Spin label' 'Transient complex' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name CcP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CcP High pH' $High_pH stop_ _System_molecular_weight 34259.857 _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_High_pH _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common High_pH _Molecular_mass 33643.3701 _Mol_thiol_state 'not present' loop_ _Biological_function 'Peroxide reduction' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 295 _Mol_residue_sequence ; MSKTLVHVASVEKGRSYEDF QKVYNAIALKLREDDEYDNY IGYGPVLVRLAWHTSGTWDK HDNTGGSYGGTYRFKKEFND PSNAGLQNGFKFLEPIHKEF PWISSGDLFSLGGVTAVQEM QGPKIPWRAGRVDTPEDTTP DNGRLPDADKDADYVRTFFQ RLNMNDREVVALMGAHALGK THLKNSGYEGPWGAANNVFT NEFYLNLLNEDWKLEKNDAN NEQWDSKSGYMMLPTDYSLI QDPKYLSIVKEYANDQDKFF KDFSKAFEKLLENGITFPKD APSPFIFKTLEEQGL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 SER 3 2 LYS 4 3 THR 5 4 LEU 6 5 VAL 7 6 HIS 8 7 VAL 9 8 ALA 10 9 SER 11 10 VAL 12 11 GLU 13 12 LYS 14 13 GLY 15 14 ARG 16 15 SER 17 16 TYR 18 17 GLU 19 18 ASP 20 19 PHE 21 20 GLN 22 21 LYS 23 22 VAL 24 23 TYR 25 24 ASN 26 25 ALA 27 26 ILE 28 27 ALA 29 28 LEU 30 29 LYS 31 30 LEU 32 31 ARG 33 32 GLU 34 33 ASP 35 34 ASP 36 35 GLU 37 36 TYR 38 37 ASP 39 38 ASN 40 39 TYR 41 40 ILE 42 41 GLY 43 42 TYR 44 43 GLY 45 44 PRO 46 45 VAL 47 46 LEU 48 47 VAL 49 48 ARG 50 49 LEU 51 50 ALA 52 51 TRP 53 52 HIS 54 53 THR 55 54 SER 56 55 GLY 57 56 THR 58 57 TRP 59 58 ASP 60 59 LYS 61 60 HIS 62 61 ASP 63 62 ASN 64 63 THR 65 64 GLY 66 65 GLY 67 66 SER 68 67 TYR 69 68 GLY 70 69 GLY 71 70 THR 72 71 TYR 73 72 ARG 74 73 PHE 75 74 LYS 76 75 LYS 77 76 GLU 78 77 PHE 79 78 ASN 80 79 ASP 81 80 PRO 82 81 SER 83 82 ASN 84 83 ALA 85 84 GLY 86 85 LEU 87 86 GLN 88 87 ASN 89 88 GLY 90 89 PHE 91 90 LYS 92 91 PHE 93 92 LEU 94 93 GLU 95 94 PRO 96 95 ILE 97 96 HIS 98 97 LYS 99 98 GLU 100 99 PHE 101 100 PRO 102 101 TRP 103 102 ILE 104 103 SER 105 104 SER 106 105 GLY 107 106 ASP 108 107 LEU 109 108 PHE 110 109 SER 111 110 LEU 112 111 GLY 113 112 GLY 114 113 VAL 115 114 THR 116 115 ALA 117 116 VAL 118 117 GLN 119 118 GLU 120 119 MET 121 120 GLN 122 121 GLY 123 122 PRO 124 123 LYS 125 124 ILE 126 125 PRO 127 126 TRP 128 127 ARG 129 128 ALA 130 129 GLY 131 130 ARG 132 131 VAL 133 132 ASP 134 133 THR 135 134 PRO 136 135 GLU 137 136 ASP 138 137 THR 139 138 THR 140 139 PRO 141 140 ASP 142 141 ASN 143 142 GLY 144 143 ARG 145 144 LEU 146 145 PRO 147 146 ASP 148 147 ALA 149 148 ASP 150 149 LYS 151 150 ASP 152 151 ALA 153 152 ASP 154 153 TYR 155 154 VAL 156 155 ARG 157 156 THR 158 157 PHE 159 158 PHE 160 159 GLN 161 160 ARG 162 161 LEU 163 162 ASN 164 163 MET 165 164 ASN 166 165 ASP 167 166 ARG 168 167 GLU 169 168 VAL 170 169 VAL 171 170 ALA 172 171 LEU 173 172 MET 174 173 GLY 175 174 ALA 176 175 HIS 177 176 ALA 178 177 LEU 179 178 GLY 180 179 LYS 181 180 THR 182 181 HIS 183 182 LEU 184 183 LYS 185 184 ASN 186 185 SER 187 186 GLY 188 187 TYR 189 188 GLU 190 189 GLY 191 190 PRO 192 191 TRP 193 192 GLY 194 193 ALA 195 194 ALA 196 195 ASN 197 196 ASN 198 197 VAL 199 198 PHE 200 199 THR 201 200 ASN 202 201 GLU 203 202 PHE 204 203 TYR 205 204 LEU 206 205 ASN 207 206 LEU 208 207 LEU 209 208 ASN 210 209 GLU 211 210 ASP 212 211 TRP 213 212 LYS 214 213 LEU 215 214 GLU 216 215 LYS 217 216 ASN 218 217 ASP 219 218 ALA 220 219 ASN 221 220 ASN 222 221 GLU 223 222 GLN 224 223 TRP 225 224 ASP 226 225 SER 227 226 LYS 228 227 SER 229 228 GLY 230 229 TYR 231 230 MET 232 231 MET 233 232 LEU 234 233 PRO 235 234 THR 236 235 ASP 237 236 TYR 238 237 SER 239 238 LEU 240 239 ILE 241 240 GLN 242 241 ASP 243 242 PRO 244 243 LYS 245 244 TYR 246 245 LEU 247 246 SER 248 247 ILE 249 248 VAL 250 249 LYS 251 250 GLU 252 251 TYR 253 252 ALA 254 253 ASN 255 254 ASP 256 255 GLN 257 256 ASP 258 257 LYS 259 258 PHE 260 259 PHE 261 260 LYS 262 261 ASP 263 262 PHE 264 263 SER 265 264 LYS 266 265 ALA 267 266 PHE 268 267 GLU 269 268 LYS 270 269 LEU 271 270 LEU 272 271 GLU 273 272 ASN 274 273 GLY 275 274 ILE 276 275 THR 277 276 PHE 278 277 PRO 279 278 LYS 280 279 ASP 281 280 ALA 282 281 PRO 283 282 SER 284 283 PRO 285 284 PHE 286 285 ILE 287 286 PHE 288 287 LYS 289 288 THR 290 289 LEU 291 290 GLU 292 291 GLU 293 292 GLN 294 293 GLY 295 294 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-25 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" 98.64 294 98.97 99.66 0.00e+00 BMRB 19004 cytochrome_c_peroxidase 99.32 300 99.66 99.66 0.00e+00 BMRB 19005 cytochrome_c_peroxidase 99.32 300 99.66 99.66 0.00e+00 BMRB 19075 cytochrome_c_peroxidase 99.32 300 99.66 99.66 0.00e+00 BMRB 19076 cytochrome_c_peroxidase 99.32 300 99.66 99.66 0.00e+00 BMRB 25551 CcP 98.64 294 99.66 99.66 0.00e+00 PDB 1A2F "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 98.31 291 98.62 98.62 0.00e+00 PDB 1A2G "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 98.31 291 98.62 98.62 0.00e+00 PDB 1AA4 "Specificity Of Ligand Binding In A Buried Polar Cavity Of Cytochrome C Peroxidase" 99.32 294 98.63 98.63 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)" 99.32 294 98.29 98.63 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)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEB "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Methylthiazole)" 99.32 294 98.29 98.63 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)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEE "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Aniline)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEF "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Aminopyridine)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEG "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (4- Aminopyridine)" 99.32 294 98.29 98.63 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" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEJ "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (1- Vinylimidazole)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEK "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Indoline)" 99.32 294 98.29 98.63 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)" 99.32 294 98.29 98.63 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" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEO "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2- Aminopyridine)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEQ "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (2-Ethylimidazole)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AES "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Imidazole)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AET "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (1-Methylimidazole)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEU "Specificity Of Ligand Binding In A Polar Cavity Of Cytochrome C Peroxidase (2-Methylimidazole)" 99.32 294 98.29 98.63 0.00e+00 PDB 1AEV "Introduction Of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation Of 2- Aminothiazole" 99.32 294 98.29 98.63 0.00e+00 PDB 1BEJ "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 98.64 291 98.28 98.63 0.00e+00 PDB 1BEK "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 98.64 291 98.28 98.63 0.00e+00 PDB 1BEM "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 98.64 291 98.28 98.63 0.00e+00 PDB 1BEP "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 98.64 291 98.63 98.97 0.00e+00 PDB 1BEQ "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 98.64 291 98.28 98.97 0.00e+00 PDB 1BES "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" 98.64 291 98.28 98.97 0.00e+00 PDB 1BJ9 "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" 98.64 291 98.63 98.97 0.00e+00 PDB 1BVA "Manganese Binding Mutant In Cytochrome C Peroxidase" 99.32 294 97.95 98.29 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" 98.64 297 98.97 98.97 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" 98.64 297 98.63 98.97 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" 98.64 297 98.63 98.63 0.00e+00 PDB 1CCE "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" 98.31 291 98.62 98.62 0.00e+00 PDB 1CCG "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" 98.31 291 98.62 98.62 0.00e+00 PDB 1CCI "How Flexible Are Proteins? Trapping Of A Flexible Loop" 99.32 294 98.63 98.63 0.00e+00 PDB 1CCJ "Conformer Selection By Ligand Binding Observed With Protein Crystallography" 99.32 294 98.63 98.63 0.00e+00 PDB 1CCK "Altering Substrate Specificity Of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosi" 98.31 291 98.62 98.97 0.00e+00 PDB 1CCL "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" 98.31 291 98.62 98.62 0.00e+00 PDB 1CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 100.00 296 97.63 98.31 0.00e+00 PDB 1CMP "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" 99.32 294 98.63 98.63 0.00e+00 PDB 1CMQ "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" 99.32 294 98.63 98.63 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" 99.32 294 98.63 98.63 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" 99.32 294 98.29 98.63 0.00e+00 PDB 1CPD "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 100.00 296 97.29 97.97 0.00e+00 PDB 1CPE "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 100.00 296 97.29 97.97 0.00e+00 PDB 1CPF "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 100.00 296 97.29 97.97 0.00e+00 PDB 1CPG "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" 100.00 296 97.29 97.97 0.00e+00 PDB 1CYF "Identifying The Physiological Electron Transfer Site Of Cytochrome C Peroxidase By Structure-Based Engineering" 100.00 296 97.63 98.31 0.00e+00 PDB 1DCC "2.2 Angstrom Structure Of Oxyperoxidase: A Model For The Enzyme:peroxide Complex" 100.00 296 97.29 98.31 0.00e+00 PDB 1DJ1 "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase" 98.64 291 98.63 98.63 0.00e+00 PDB 1DJ5 "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase With N-Hydroxyguanidine Bound" 98.64 291 98.63 98.63 0.00e+00 PDB 1DS4 "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, Ph 6, 100k" 98.98 292 98.63 98.63 0.00e+00 PDB 1DSE "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, With Phosphate Bound, Ph 6, 100k" 98.98 292 98.29 98.63 0.00e+00 PDB 1DSG "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 5, Room Temperature." 98.98 292 98.63 98.63 0.00e+00 PDB 1DSO "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 6, Room Temperature." 98.98 292 98.63 98.63 0.00e+00 PDB 1DSP "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 7, Room Temperature" 98.98 292 98.63 98.63 0.00e+00 PDB 1EBE "Laue Diffraction Study On The Structure Of Cytochrome C Peroxidase Compound I" 98.64 294 99.31 99.66 0.00e+00 PDB 1JCI "Stabilization Of The Engineered Cation-Binding Loop In Cytochrome C Peroxidase (Ccp)" 98.64 294 97.59 97.59 0.00e+00 PDB 1JDR "Crystal Structure Of A Proximal Domain Potassium Binding Variant Of Cytochrome C Peroxidase" 98.64 294 97.94 97.94 0.00e+00 PDB 1KOK "Crystal Structure Of Mesopone Cytochrome C Peroxidase (Mpccp)" 98.64 294 99.66 99.66 0.00e+00 PDB 1KRJ "Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp)" 98.64 294 97.94 97.94 0.00e+00 PDB 1KXM "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" 98.98 290 97.95 97.95 0.00e+00 PDB 1KXN "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" 98.64 289 97.94 97.94 0.00e+00 PDB 1MK8 "Crystal Structure Of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link" 98.64 294 99.31 99.66 0.00e+00 PDB 1MKQ "Crystal Structure Of The Mutant Variant Of Cytochrome C Peroxidase In The 'open' Uncross-Linked Form" 98.64 294 99.31 99.66 0.00e+00 PDB 1MKR "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase (Plate Like Crystals)" 98.64 294 99.31 99.66 0.00e+00 PDB 1ML2 "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase With Zn(Ii)-(20-Oxo-Protoporphyrin Ix)" 98.64 294 99.31 99.66 0.00e+00 PDB 1RYC "Cytochrome C Peroxidase W191g From Saccharomyces Cerevisiae" 99.32 294 98.63 98.63 0.00e+00 PDB 1S6V "Structure Of A Cytochrome C Peroxidase-Cytochrome C Site Specific Cross-Link" 98.64 294 99.66 99.66 0.00e+00 PDB 1S73 "Crystal Structure Of Mesopone Cytochrome C Peroxidase (R- Isomer) [mpccp-R]" 98.64 294 99.66 99.66 0.00e+00 PDB 1SBM "Crystal Structure Of Reduced Mesopone Cytochrome C Peroxidase (R-Isomer)" 98.64 294 99.66 99.66 0.00e+00 PDB 1SDQ "Structure Of Reduced-No Adduct Of Mesopone Cytochrome C Peroxidase" 98.64 294 99.66 99.66 0.00e+00 PDB 1SOG "Cyrstal Structure Of Cytochrome C Peroxidase Mutant: Ccpk2m2" 98.64 294 97.25 97.59 0.00e+00 PDB 1STQ "Cyrstal Structure Of Cytochrome C Peroxidase Mutant: Ccpk2m3" 98.64 294 96.91 97.25 0.00e+00 PDB 1U74 "Electron Transfer Complex Between Cytochrome C And Cytochrome C Peroxidase" 100.00 296 97.63 98.31 0.00e+00 PDB 1U75 "Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc- Porphyrin Substituted Cytochrome C Peroxidase" 100.00 296 97.63 98.31 0.00e+00 PDB 1Z53 "The 1.13 Angstrom Structure Of Iron-Free Cytochrome C Peroxidase" 98.64 294 99.66 99.66 0.00e+00 PDB 1ZBY "High-resolution Crystal Structure Of Native (resting) Cytochrome C Peroxidase (ccp)" 98.64 294 99.66 99.66 0.00e+00 PDB 1ZBZ "High-Resolution Crystal Structure Of Compound I Intermediate Of Cytochrome C Peroxidase (Ccp)" 98.64 294 99.66 99.66 0.00e+00 PDB 2ANZ "Cytochrome C Peroxidase In Complex With 2,6-Diaminopyridine" 99.32 294 98.29 98.63 0.00e+00 PDB 2AQD "Cytochrome C Peroxidase (Ccp) In Complex With 2,5- Diaminopyridine" 99.32 294 98.63 98.63 0.00e+00 PDB 2AS1 "Cytochrome C Peroxidase In Complex With Thiopheneamidine" 99.32 294 98.63 98.63 0.00e+00 PDB 2AS2 "Cytochrome C Peroxidase In Complex With 2-Iminopiperidine" 99.32 294 98.63 98.63 0.00e+00 PDB 2AS3 "Cytochrome C Peroxidase In Complex With Phenol" 99.32 294 98.63 98.63 0.00e+00 PDB 2AS4 "Cytochrome C Peroxidase In Complex With 3-Fluorocatechol" 99.32 294 98.63 98.63 0.00e+00 PDB 2AS6 "Cytochrome C Peroxidase In Complex With Cyclopentylamine" 99.32 294 98.63 98.63 0.00e+00 PDB 2B0Z "Crystal Structure Of The Protein-Protein Complex Between F82i Cytochrome C And Cytochrome C Peroxidase" 98.64 294 99.66 99.66 0.00e+00 PDB 2B10 "Crystal Structure Of The Protein-Protein Complex Between F82s Cytochrome C And Cytochrome C Peroxidase" 98.64 294 99.66 99.66 0.00e+00 PDB 2B11 "Crystal Structure Of The Protein-Protein Complex Between F82w Cytochrome C And Cytochrome C Peroxidase" 98.64 294 99.66 99.66 0.00e+00 PDB 2B12 "Crystal Structure Of The Protein-Protein Complex Between F82y Cytochrome C And Cytochrome C Peroxidase" 98.64 294 99.66 99.66 0.00e+00 PDB 2BCN "Solvent Isotope Effects On Interfacial Protein Electron Transfer Between Cytochrome C And Cytochrome C Peroxidase" 100.00 296 97.63 98.31 0.00e+00 PDB 2CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 100.00 296 97.29 98.31 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 " 100.00 296 97.29 98.31 0.00e+00 PDB 2CYP "Crystal Structure Of Yeast Cytochrome C Peroxidase Refined At 1.7-Angstroms Resolution" 98.64 294 99.66 99.66 0.00e+00 PDB 2EUN "Cytochrome C Peroxidase (ccp) In Complex With 2,4- Diaminopyrimidine" 99.32 294 98.63 98.63 0.00e+00 PDB 2EUO "Cytochrome C Peroxidase (ccp) In Complex With 1-methyl-1- Lambda-5-pyridin-3-yl-amine" 99.32 294 98.63 98.63 0.00e+00 PDB 2EUP "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-5- Picoline" 99.32 294 98.63 98.63 0.00e+00 PDB 2EUQ "Cytochrome C Peroxydase (Ccp) In Complex With 3- Thienylmethylamine" 99.32 294 98.63 98.63 0.00e+00 PDB 2EUR "Cytochrome C Peroxidase (Ccp) In Complex With 4- Pyridylcarbinol" 99.32 294 98.63 98.63 0.00e+00 PDB 2EUS "Cytochrome C Peroxidase (Ccp) In Complex With Benzylamine" 99.32 294 98.63 98.63 0.00e+00 PDB 2EUT "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-4- Picoline" 99.32 294 98.63 98.63 0.00e+00 PDB 2EUU "Cytochrome C Peroxidase (Ccp) In Complex With 1h-Imidazol-2- Ylmethanol" 99.32 294 98.63 98.63 0.00e+00 PDB 2GB8 "Solution Structure Of The Complex Between Yeast Iso-1- Cytochrome C And Yeast Cytochrome C Peroxidase" 98.64 294 98.97 98.97 0.00e+00 PDB 2IA8 "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" 98.64 291 97.94 98.28 0.00e+00 PDB 2ICV "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" 98.64 291 97.94 98.28 0.00e+00 PDB 2JTI "Solution Structure Of The Yeast Iso-1-Cytochrome C (T12a) : Yeast Cytochrome C Peroxidase Complex" 98.64 294 98.97 98.97 0.00e+00 PDB 2N18 "Dominant Form Of The Low-affinity Complex Of Yeast Cytochrome C And Cytochrome C Peroxidase" 98.64 294 99.66 99.66 0.00e+00 PDB 2PCB "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 100.00 296 97.63 98.31 0.00e+00 PDB 2PCC "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 100.00 296 97.63 98.31 0.00e+00 PDB 2RBT "N-Methylbenzylamine In Complex With Cytochrome C Peroxidase W191g" 98.98 292 98.29 98.63 0.00e+00 PDB 2RBU "Cytochrome C Peroxidase In Complex With Cyclopentane-Carboximidamide" 98.98 292 98.29 98.63 0.00e+00 PDB 2RBV "Cytochrome C Peroxidase In Complex With (1-Methyl-1h-Pyrrol-2-Yl)- Methylamine" 98.98 292 98.29 98.63 0.00e+00 PDB 2RBW "Cytochrome C Peroxidase W191g In Complex With 1,2-dimethyl-1h-pyridin- 5-amine" 98.98 292 98.29 98.63 0.00e+00 PDB 2RBX "Cytochrome C Peroxidase W191g In Complex With Pyrimidine-2,4,6- Triamine." 98.98 292 98.29 98.63 0.00e+00 PDB 2RBY "1-methyl-5-imidazolecarboxaldehyde In Complex With Cytochrome C Peroxidase W191g" 98.98 292 98.29 98.63 0.00e+00 PDB 2RBZ "Cytochrome C Peroxidase W191g In Complex 3-Methoxypyridine" 98.98 292 98.29 98.63 0.00e+00 PDB 2RC0 "Cytochrome C Peroxidase W191g In Complex With 2-Imino-4- Methylpiperdine" 98.98 292 98.29 98.63 0.00e+00 PDB 2RC1 "Cytochrome C Peroxidase W191g In Complex With 2,4,5-Trimethyl-3- Oxazoline" 98.98 292 98.29 98.63 0.00e+00 PDB 2RC2 "Cytochrome C Peroxidase W191g In Complex With 1-Methyl-2-Vinyl- Pyridinium" 98.98 292 98.29 98.63 0.00e+00 PDB 2V23 "Structure Of Cytochrome C Peroxidase Mutant N184r Y36a" 98.64 296 98.63 98.97 0.00e+00 PDB 2V2E "Structure Of Isoniazid (Inh) Bound To Cytochrome C Peroxidase Mutant N184r Y36a" 99.32 294 98.63 98.98 0.00e+00 PDB 2X07 "Cytochrome C Peroxidase: Engineered Ascorbate Binding Site" 98.64 293 98.28 98.97 0.00e+00 PDB 2X08 "Cytochrome C Peroxidase: Ascorbate Bound To The Engineered Ascorbate Binding Site" 98.64 293 98.28 98.97 0.00e+00 PDB 2XIL "The Structure Of Cytochrome C Peroxidase Compound I" 99.32 294 99.32 99.66 0.00e+00 PDB 2XJ5 "The Structure Of Cytochrome C Peroxidase Compound Ii" 99.32 294 99.66 99.66 0.00e+00 PDB 2XJ8 "The Structure Of Ferrous Cytochrome C Peroxidase" 99.32 294 99.66 99.66 0.00e+00 PDB 2Y5A "Cytochrome C Peroxidase (Ccp) W191g Bound To 3-Aminopyridine" 99.32 294 98.63 98.63 0.00e+00 PDB 2YCG "Structure Of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method" 98.64 294 99.66 99.66 0.00e+00 PDB 3CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 100.00 296 97.29 98.31 0.00e+00 PDB 3CCX "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" 99.32 294 98.63 98.63 0.00e+00 PDB 3E2O "Crystal Structure Of Cytochrome C Peroxidase, N184r Mutant" 98.64 294 98.97 98.97 0.00e+00 PDB 3EXB "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Pathway Excised In A Complex With A Peptide Wire" 98.64 295 97.94 97.94 0.00e+00 PDB 3M23 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M25 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M26 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M27 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M28 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M29 "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2A "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2B "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2C "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2D "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2E "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2F "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2G "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2H "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3M2I "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" 98.64 291 99.31 99.31 0.00e+00 PDB 3R98 "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" 98.64 293 99.66 99.66 0.00e+00 PDB 3R99 "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" 98.64 293 99.66 99.66 0.00e+00 PDB 4A6Z "Cytochrome C Peroxidase With Bound Guaiacol" 98.64 296 98.63 98.97 0.00e+00 PDB 4A71 "Cytochrome C Peroxidase In Complex With Phenol" 98.64 296 98.97 98.97 0.00e+00 PDB 4A78 "Cytochrome C Peroxidase M119w In Complex With Guiacol" 98.64 296 98.97 98.97 0.00e+00 PDB 4A7M "Cytochrome C Peroxidase S81w Mutant" 98.64 296 99.31 99.31 0.00e+00 PDB 4CCP "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" 100.00 296 97.29 98.31 0.00e+00 PDB 4CCX "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" 99.32 294 98.63 98.63 0.00e+00 PDB 4CVI "Neutron Structure Of Ferric Cytochrome C Peroxidase - Deuterium Exchanged At Room Temperature" 99.32 294 99.32 99.32 0.00e+00 PDB 4CVJ "Neutron Structure Of Compound I Intermediate Of Cytochrome C Peroxidase - Deuterium Exchanged 100 K" 99.32 294 99.66 99.66 0.00e+00 PDB 4JB4 "Expression, Purification, Characterization, And Solution Nmr Study Of Highly Deuterated Yeast Cytochrome C Peroxidase With Enha" 99.32 300 99.66 99.66 0.00e+00 PDB 4JM5 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-amino-5-methylthiazole" 98.64 289 97.94 97.94 0.00e+00 PDB 4JM6 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,4-diaminopyrimidine" 98.64 289 97.94 97.94 0.00e+00 PDB 4JM8 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,6-diaminopyridine" 98.64 289 97.94 97.94 0.00e+00 PDB 4JM9 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-amino-1-methylpyridinium" 98.64 289 97.94 97.94 0.00e+00 PDB 4JMA "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-fluorocatechol" 98.64 289 97.94 97.94 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" 98.64 289 97.94 97.94 0.00e+00 PDB 4JMS "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-5-amine" 98.64 289 97.94 97.94 0.00e+00 PDB 4JMT "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridin-6-ylmethanol" 98.64 289 97.94 97.94 0.00e+00 PDB 4JMV "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-6-amine" 98.64 289 97.94 97.94 0.00e+00 PDB 4JMW "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Phenol" 98.64 289 97.94 97.94 0.00e+00 PDB 4JMZ "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With N-methyl-1h-benzimidazol-2-amine" 98.64 289 97.94 97.94 0.00e+00 PDB 4JN0 "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridine-6-carbaldehyde" 98.64 289 97.94 97.94 0.00e+00 PDB 4JPL "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-azaindole" 98.64 289 97.94 97.94 0.00e+00 PDB 4JPT "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Quinazoline-2,4-diamine" 98.64 289 97.94 97.94 0.00e+00 PDB 4JPU "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Benzamidine" 98.64 289 97.94 97.94 0.00e+00 PDB 4JQJ "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinoline" 98.64 289 97.94 97.94 0.00e+00 PDB 4JQK "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-(2-aminopyridin-1-ium-1-yl)ethanol" 98.64 289 97.94 97.94 0.00e+00 PDB 4JQM "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinazoline" 98.64 289 97.94 97.94 0.00e+00 PDB 4JQN "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-hydroxybenzaldehyde" 98.64 289 97.94 97.94 0.00e+00 PDB 4NFG "K13r Mutant Of Horse Cytochrome C And Yeast Cytochrome C Peroxidase Complex" 99.32 294 100.00 100.00 0.00e+00 PDB 4NVA "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVB "Predicting Protein Conformational Response In Prospective Ligand Discovery." 98.64 289 97.94 97.94 0.00e+00 PDB 4NVC "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVD "Predicting Protein Conformational Response In Prospective Ligand Discovery." 98.64 289 97.94 97.94 0.00e+00 PDB 4NVE "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVF "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVG "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVH "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVI "Predicting Protein Conformational Response In Prospective Ligand Discovery." 98.64 289 97.94 97.94 0.00e+00 PDB 4NVJ "Predicting Protein Conformational Response In Prospective Ligand Discovery." 98.64 289 97.94 97.94 0.00e+00 PDB 4NVK "Predicting Protein Conformational Response In Prospective Ligand Discovery." 98.64 289 97.94 97.94 0.00e+00 PDB 4NVL "Predicting Protein Conformational Response In Prospective Ligand Discovery." 98.64 289 97.94 97.94 0.00e+00 PDB 4NVM "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVN "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4NVO "Predicting Protein Conformational Response In Prospective Ligand Discovery" 98.64 289 97.94 97.94 0.00e+00 PDB 4OQ7 "Predicting Protein Conformational Response In Prospective Ligand Discovery." 98.64 289 97.94 97.94 0.00e+00 PDB 4P4Q "Complex Of Yeast Cytochrome C Peroxidase (w191f) With Iso-1 Cytochrome C" 98.64 294 98.63 98.97 0.00e+00 PDB 4XV4 "Ccp Gateless Cavity" 98.64 289 97.94 97.94 0.00e+00 PDB 4XV5 "Ccp Gateless Cavity" 99.32 292 97.95 97.95 0.00e+00 PDB 4XV6 "Ccp Gateless Cavity" 98.64 289 97.94 97.94 0.00e+00 PDB 4XV7 "Ccp Gateless Cavity" 99.32 292 97.95 97.95 0.00e+00 PDB 4XV8 "Ccp Gateless Cavity" 99.32 292 97.95 97.95 0.00e+00 PDB 4XVA "Crystal Structure Of Wild Type Cytochrome C Peroxidase" 98.64 293 99.66 99.66 0.00e+00 PDB 5CCP "Histidine 52 Is A Critical Residue For Rapid Formation Of Cytochrome C Peroxidase Compound I" 100.00 296 97.29 97.97 0.00e+00 PDB 6CCP "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" 100.00 296 97.29 98.31 0.00e+00 PDB 7CCP "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" 100.00 296 97.29 97.97 0.00e+00 DBJ GAA24787 "K7_Ccp1p [Saccharomyces cerevisiae Kyokai no. 7]" 98.64 363 99.66 99.66 0.00e+00 EMBL CAA44288 "Cytochrome c peroxidase [Saccharomyces cerevisiae]" 98.64 361 99.66 99.66 0.00e+00 EMBL CAA82145 "CCP1 [Saccharomyces cerevisiae]" 98.64 361 99.66 99.66 0.00e+00 EMBL CAY81144 "Ccp1p [Saccharomyces cerevisiae EC1118]" 98.64 362 99.31 99.31 0.00e+00 GB AAA88709 "cytochrome c peroxidase [Saccharomyces cerevisiae]" 98.64 362 98.97 98.97 0.00e+00 GB AAS56247 "YKR066C [Saccharomyces cerevisiae]" 98.64 361 99.31 99.66 0.00e+00 GB AHY76301 "Ccp1p [Saccharomyces cerevisiae YJM993]" 98.64 363 98.97 98.97 0.00e+00 GB AJP40095 "Ccp1p [Saccharomyces cerevisiae YJM1078]" 98.64 362 99.31 99.31 0.00e+00 GB AJS30293 "Ccp1p [Saccharomyces cerevisiae YJM189]" 98.64 362 98.97 98.97 0.00e+00 REF NP_012992 "Ccp1p [Saccharomyces cerevisiae S288c]" 98.64 361 99.66 99.66 0.00e+00 SP P00431 "RecName: Full=Cytochrome c peroxidase, mitochondrial; Short=CCP; Flags: Precursor" 98.64 361 99.66 99.66 0.00e+00 TPG DAA09217 "TPA: Ccp1p [Saccharomyces cerevisiae S288c]" 98.64 361 99.66 99.66 0.00e+00 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _ATCC_number _Organelle _Gene_mnemonic $High_pH "baker's yeast" 4932 Eukaryota Fungi Saccharomyces cerevisiae D273-10B 25657 mitochondria CCP1 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 $High_pH 'recombinant technology' 'Saccharomyces cerevisiae' Saccharomyces cerevisiae 'Escherichia coli' pET28aCcP stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_CcP_NMR_sample _Saveframe_category sample _Sample_type solution _Details '400uM [15N, 13C, 2H] CcP, 100mM NaCl, 20mM NaPi, pH 6.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $High_pH 0.4 mM '[U-100% 13C; U-100% 15N; U-80% 2H]' NaCl 100 mM 'natural abundance' NaPi 20 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CcpNmr_Analysis _Saveframe_category software _Name CcpNmr_Analysis _Version 2.1 loop_ _Vendor _Address _Electronic_address CCPN 'Department of Biochemistry, Cambridge CB2 1GA, UK' http://www.ccpn.ac.uk stop_ loop_ _Task assignment stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_Topspin _Saveframe_category software _Name Topspin _Version 3.1 loop_ _Vendor _Address _Electronic_address Bruker 'Karlsruhe, Germany' http://www.bruker.com/ stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_Bruker_950MHz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _Details 'with 1H{13C/15N} cryoprobe' save_ save_Bruker_600MHz _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'with 1H{13C/15N} cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC/HMQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC/HMQC' _Sample_label $CcP_NMR_sample save_ save_3D_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $CcP_NMR_sample save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $CcP_NMR_sample save_ save_BESTTR_HN(Ca)CO_950_(H[N[ca[CO]]])_4 _Saveframe_category NMR_applied_experiment _Experiment_name 'BESTTR_HN(Ca)CO_950 (H[N[ca[CO]]])' _Sample_label $CcP_NMR_sample save_ save_BESTTR_HNCO_950_(H[N[trho(N)][CO]])_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'BESTTR_HNCO_950 (H[N[trho(N)][CO]])' _Sample_label $CcP_NMR_sample save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $CcP_NMR_sample save_ save_BESTTR_HN(COCa)Cb_600_(H[N[co[{CA|ca[C]}]]])_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'BESTTR_HN(COCa)Cb_600 (H[N[co[{CA|ca[C]}]]])' _Sample_label $CcP_NMR_sample save_ ####################### # Sample conditions # ####################### save_ccp_assignment _Saveframe_category sample_conditions _Details '400uM CcP, 100mM NaCl, 20mM NaPi, pH 6.0, 293K' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100.000 . mM pH 6.000 . pH pressure 1.000 . atm temperature 293.000 . 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CcpNmr_Analysis stop_ loop_ _Experiment_label '2D 1H-15N HSQC/HMQC' '3D HNCACB' '3D HNCA' 'BESTTR_HN(Ca)CO_950 (H[N[ca[CO]]])' 'BESTTR_HNCO_950 (H[N[trho(N)][CO]])' '3D HN(CO)CA' 'BESTTR_HN(COCa)Cb_600 (H[N[co[{CA|ca[C]}]]])' stop_ loop_ _Sample_label $CcP_NMR_sample stop_ _Sample_conditions_label $ccp_assignment _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'CcP High pH' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 1 MET C C 177.296 . 1 2 2 2 SER H H 8.243 0.002 1 3 2 2 SER C C 174.975 0.017 1 4 2 2 SER CA C 58.129 0.045 1 5 2 2 SER CB C 63.081 0.069 1 6 2 2 SER N N 121.940 0.013 1 7 3 3 LYS H H 8.389 0.013 1 8 3 3 LYS C C 176.208 0.051 1 9 3 3 LYS CA C 55.844 0.103 1 10 3 3 LYS CB C 32.108 0.069 1 11 3 3 LYS N N 123.847 0.13 1 12 4 4 THR H H 8.177 0.013 1 13 4 4 THR C C 173.912 0.013 1 14 4 4 THR CA C 61.600 0.01 1 15 4 4 THR CB C 69.262 0.019 1 16 4 4 THR N N 118.283 0.123 1 17 5 5 LEU H H 8.193 0.013 1 18 5 5 LEU C C 175.913 0.001 1 19 5 5 LEU CA C 54.536 0.004 1 20 5 5 LEU CB C 41.405 0.033 1 21 5 5 LEU N N 127.078 0.112 1 22 6 6 VAL H H 8.144 0.012 1 23 6 6 VAL C C 174.501 0.013 1 24 6 6 VAL CA C 60.717 0.047 1 25 6 6 VAL CB C 33.138 0.013 1 26 6 6 VAL N N 124.368 0.115 1 27 7 7 HIS H H 8.684 0.013 1 28 7 7 HIS C C 172.368 0.012 1 29 7 7 HIS CA C 51.638 0.006 1 30 7 7 HIS CB C 26.959 0.038 1 31 7 7 HIS N N 124.865 0.118 1 32 8 8 VAL H H 8.843 0.014 1 33 8 8 VAL C C 177.815 0.006 1 34 8 8 VAL CA C 61.441 0.013 1 35 8 8 VAL CB C 31.272 0.021 1 36 8 8 VAL N N 124.946 0.111 1 37 9 9 ALA H H 8.459 0.014 1 38 9 9 ALA C C 177.167 0.01 1 39 9 9 ALA CA C 52.278 0.011 1 40 9 9 ALA CB C 19.514 0.024 1 41 9 9 ALA N N 135.147 0.108 1 42 10 10 SER H H 9.429 0.015 1 43 10 10 SER C C 172.815 . 1 44 10 10 SER CA C 56.166 0.02 1 45 10 10 SER CB C 63.105 0.061 1 46 10 10 SER N N 121.287 0.138 1 47 11 11 VAL H H 8.540 0.014 1 48 11 11 VAL CA C 64.199 . 1 49 11 11 VAL N N 128.516 0.134 1 50 12 12 GLU C C 176.551 0.023 1 51 12 12 GLU CA C 58.870 0.024 1 52 12 12 GLU CB C 27.616 . 1 53 13 13 LYS H H 8.263 0.015 1 54 13 13 LYS C C 178.596 0.02 1 55 13 13 LYS CA C 58.029 0.007 1 56 13 13 LYS CB C 31.460 0.019 1 57 13 13 LYS N N 124.341 0.109 1 58 14 14 GLY H H 8.831 0.012 1 59 14 14 GLY C C 174.162 0.001 1 60 14 14 GLY CA C 45.054 0.02 1 61 14 14 GLY N N 113.195 0.128 1 62 15 15 ARG H H 7.576 0.011 1 63 15 15 ARG C C 175.565 0.013 1 64 15 15 ARG CA C 52.628 0.01 1 65 15 15 ARG CB C 28.796 0.023 1 66 15 15 ARG N N 118.753 0.094 1 67 16 16 SER H H 9.447 0.014 1 68 16 16 SER C C 174.244 0.013 1 69 16 16 SER CA C 56.474 0.016 1 70 16 16 SER CB C 65.796 0.031 1 71 16 16 SER N N 119.642 0.112 1 72 17 17 TYR H H 8.957 0.013 1 73 17 17 TYR C C 176.105 0.005 1 74 17 17 TYR CA C 61.486 0.012 1 75 17 17 TYR CB C 37.876 0.018 1 76 17 17 TYR N N 122.070 0.111 1 77 18 18 GLU H H 8.860 0.014 1 78 18 18 GLU C C 179.081 0.004 1 79 18 18 GLU CA C 59.477 0.015 1 80 18 18 GLU CB C 28.183 0.018 1 81 18 18 GLU N N 116.898 0.104 1 82 19 19 ASP H H 7.520 0.014 1 83 19 19 ASP C C 177.956 0.029 1 84 19 19 ASP CA C 57.377 0.022 1 85 19 19 ASP CB C 41.277 0.037 1 86 19 19 ASP N N 117.755 0.107 1 87 20 20 PHE H H 7.435 0.016 1 88 20 20 PHE C C 177.391 0.007 1 89 20 20 PHE CA C 62.326 0.017 1 90 20 20 PHE CB C 38.795 0.016 1 91 20 20 PHE N N 116.066 0.117 1 92 21 21 GLN H H 8.846 0.014 1 93 21 21 GLN C C 177.779 0.004 1 94 21 21 GLN CA C 57.333 0.02 1 95 21 21 GLN CB C 27.123 0.019 1 96 21 21 GLN N N 121.601 0.11 1 97 22 22 LYS H H 7.389 0.015 1 98 22 22 LYS C C 178.933 . 1 99 22 22 LYS CA C 59.767 . 1 100 22 22 LYS CB C 31.244 . 1 101 22 22 LYS N N 119.498 0.111 1 102 24 24 TYR CA C 60.424 . 1 103 24 24 TYR CB C 36.473 0.028 1 104 25 25 ASN H H 8.756 0.025 1 105 25 25 ASN C C 176.836 . 1 106 25 25 ASN CA C 54.902 0.027 1 107 25 25 ASN CB C 36.196 . 1 108 25 25 ASN N N 117.717 0.152 1 109 26 26 ALA H H 7.842 0.017 1 110 26 26 ALA CB C 18.481 . 1 111 26 26 ALA N N 123.090 0.174 1 112 27 27 ILE C C 177.010 . 1 113 27 27 ILE CA C 65.163 . 1 114 27 27 ILE CB C 37.086 . 1 115 28 28 ALA H H 9.125 0.018 1 116 28 28 ALA C C 180.688 . 1 117 28 28 ALA CA C 54.949 0.068 1 118 28 28 ALA CB C 18.558 0.045 1 119 28 28 ALA N N 122.232 0.159 1 120 29 29 LEU H H 9.322 0.019 1 121 29 29 LEU C C 179.609 . 1 122 29 29 LEU CA C 57.324 . 1 123 29 29 LEU CB C 40.674 0.051 1 124 29 29 LEU N N 121.657 0.168 1 125 30 30 LYS H H 7.578 0.021 1 126 30 30 LYS C C 178.610 0.038 1 127 30 30 LYS CA C 59.259 0.007 1 128 30 30 LYS CB C 35.504 . 1 129 30 30 LYS N N 123.293 0.126 1 130 31 31 LEU H H 8.730 0.016 1 131 31 31 LEU C C 180.091 0.023 1 132 31 31 LEU CA C 56.989 0.066 1 133 31 31 LEU CB C 41.490 0.031 1 134 31 31 LEU N N 120.584 0.149 1 135 32 32 ARG H H 7.476 0.016 1 136 32 32 ARG C C 177.808 0.015 1 137 32 32 ARG CA C 58.168 0.032 1 138 32 32 ARG CB C 30.809 0.038 1 139 32 32 ARG N N 117.585 0.128 1 140 33 33 GLU H H 7.921 0.014 1 141 33 33 GLU C C 177.907 0.015 1 142 33 33 GLU CA C 58.132 0.003 1 143 33 33 GLU CB C 29.954 0.024 1 144 33 33 GLU N N 118.246 0.129 1 145 34 34 ASP H H 8.680 0.013 1 146 34 34 ASP C C 177.559 0.001 1 147 34 34 ASP CA C 52.732 0.005 1 148 34 34 ASP CB C 37.899 0.029 1 149 34 34 ASP N N 123.019 0.122 1 150 35 35 ASP H H 8.327 0.02 1 151 35 35 ASP C C 176.478 0.016 1 152 35 35 ASP CA C 54.572 0.037 1 153 35 35 ASP CB C 39.295 0.053 1 154 35 35 ASP N N 119.591 0.104 1 155 36 36 GLU H H 8.365 0.013 1 156 36 36 GLU C C 177.277 0.04 1 157 36 36 GLU CA C 56.696 0.01 1 158 36 36 GLU CB C 28.830 0.016 1 159 36 36 GLU N N 117.859 0.122 1 160 37 37 TYR H H 6.896 0.014 1 161 37 37 TYR C C 174.229 0.004 1 162 37 37 TYR CA C 58.658 0.012 1 163 37 37 TYR CB C 40.354 0.024 1 164 37 37 TYR N N 121.377 0.114 1 165 38 38 ASP H H 8.181 0.012 1 166 38 38 ASP C C 175.642 0.007 1 167 38 38 ASP CA C 53.281 0.007 1 168 38 38 ASP CB C 38.606 0.03 1 169 38 38 ASP N N 128.139 0.116 1 170 39 39 ASN H H 8.534 0.013 1 171 39 39 ASN C C 175.052 0.003 1 172 39 39 ASN CA C 54.560 0.013 1 173 39 39 ASN CB C 36.742 0.045 1 174 39 39 ASN N N 114.984 0.117 1 175 40 40 TYR H H 7.516 0.013 1 176 40 40 TYR C C 176.986 0.008 1 177 40 40 TYR CA C 60.139 0.05 1 178 40 40 TYR CB C 33.037 0.009 1 179 40 40 TYR N N 109.089 0.129 1 180 41 41 ILE H H 8.000 0.013 1 181 41 41 ILE C C 179.193 0.003 1 182 41 41 ILE CA C 65.886 0.019 1 183 41 41 ILE CB C 38.442 0.019 1 184 41 41 ILE N N 124.278 0.114 1 185 42 42 GLY H H 8.786 0.015 1 186 42 42 GLY C C 173.706 0.012 1 187 42 42 GLY CA C 44.455 0.028 1 188 42 42 GLY N N 107.557 0.126 1 189 43 43 TYR H H 9.686 0.011 1 190 43 43 TYR C C 175.524 0.012 1 191 43 43 TYR CA C 60.265 0.019 1 192 43 43 TYR CB C 38.925 0.017 1 193 43 43 TYR N N 116.071 0.092 1 194 44 44 GLY H H 9.814 0.014 1 195 44 44 GLY C C 174.904 . 1 196 44 44 GLY CA C 48.825 . 1 197 44 44 GLY N N 109.621 0.133 1 198 48 48 VAL C C 176.081 0.015 1 199 48 48 VAL CA C 61.901 . 1 200 48 48 VAL CB C 30.092 . 1 201 49 49 ARG H H 9.191 0.012 1 202 49 49 ARG C C 173.049 0.027 1 203 49 49 ARG CA C 56.766 0.042 1 204 49 49 ARG CB C 31.906 0.085 1 205 49 49 ARG N N 124.868 0.144 1 206 50 50 LEU H H 7.935 0.017 1 207 50 50 LEU C C 171.959 0.017 1 208 50 50 LEU CA C 52.900 0.019 1 209 50 50 LEU CB C 33.511 0.037 1 210 50 50 LEU N N 126.643 0.117 1 211 51 51 ALA H H 6.625 0.012 1 212 51 51 ALA C C 176.852 . 1 213 51 51 ALA CA C 49.628 . 1 214 51 51 ALA CB C 22.243 . 1 215 51 51 ALA N N 121.389 0.108 1 216 53 53 HIS CA C 57.130 . 1 217 53 53 HIS CB C 27.993 . 1 218 54 54 THR H H 7.719 0.015 1 219 54 54 THR CB C 69.067 . 1 220 54 54 THR N N 117.584 0.142 1 221 57 57 THR C C 173.576 0.097 1 222 57 57 THR CA C 59.632 0.011 1 223 57 57 THR CB C 69.198 . 1 224 58 58 TRP H H 6.721 0.015 1 225 58 58 TRP C C 173.693 0.005 1 226 58 58 TRP CA C 58.685 0.012 1 227 58 58 TRP CB C 27.641 0.031 1 228 58 58 TRP N N 121.686 0.115 1 229 59 59 ASP H H 7.339 0.012 1 230 59 59 ASP C C 175.021 0.004 1 231 59 59 ASP CA C 52.059 0.019 1 232 59 59 ASP CB C 42.039 0.015 1 233 59 59 ASP N N 125.694 0.138 1 234 60 60 LYS H H 6.811 0.016 1 235 60 60 LYS C C 177.262 0.013 1 236 60 60 LYS CA C 56.491 0.021 1 237 60 60 LYS CB C 31.406 0.015 1 238 60 60 LYS N N 122.736 0.112 1 239 61 61 HIS H H 8.842 0.015 1 240 61 61 HIS C C 175.595 0.007 1 241 61 61 HIS CA C 58.419 0.021 1 242 61 61 HIS CB C 27.197 0.026 1 243 61 61 HIS N N 119.000 0.111 1 244 62 62 ASP H H 6.846 0.015 1 245 62 62 ASP C C 176.082 0.025 1 246 62 62 ASP CA C 51.909 0.017 1 247 62 62 ASP CB C 40.880 0.038 1 248 62 62 ASP N N 114.272 0.114 1 249 63 63 ASN H H 8.285 0.017 1 250 63 63 ASN C C 174.450 0.023 1 251 63 63 ASN CA C 53.144 0.026 1 252 63 63 ASN CB C 38.017 0.042 1 253 63 63 ASN N N 117.501 0.108 1 254 64 64 THR H H 7.557 0.014 1 255 64 64 THR C C 175.582 0.027 1 256 64 64 THR CA C 60.530 0.011 1 257 64 64 THR CB C 71.469 0.042 1 258 64 64 THR N N 108.356 0.128 1 259 65 65 GLY H H 8.348 0.015 1 260 65 65 GLY C C 175.879 0.011 1 261 65 65 GLY CA C 44.259 0.048 1 262 65 65 GLY N N 105.385 0.13 1 263 66 66 GLY H H 7.816 0.015 1 264 66 66 GLY C C 172.947 0.03 1 265 66 66 GLY CA C 43.572 0.026 1 266 66 66 GLY N N 107.555 0.1 1 267 67 67 SER H H 8.473 0.014 1 268 67 67 SER C C 177.479 0.029 1 269 67 67 SER CA C 59.524 0.015 1 270 67 67 SER CB C 63.516 0.058 1 271 67 67 SER N N 111.724 0.104 1 272 68 68 TYR H H 8.350 0.013 1 273 68 68 TYR C C 175.409 0.003 1 274 68 68 TYR CA C 62.471 0.011 1 275 68 68 TYR CB C 37.328 0.023 1 276 68 68 TYR N N 122.348 0.113 1 277 69 69 GLY H H 8.315 0.013 1 278 69 69 GLY C C 175.932 0.014 1 279 69 69 GLY CA C 45.921 0.016 1 280 69 69 GLY N N 98.827 . 1 281 70 70 GLY H H 7.608 0.011 1 282 70 70 GLY C C 177.638 . 1 283 70 70 GLY CA C 46.846 0.045 1 284 70 70 GLY N N 109.689 0.015 1 285 71 71 THR H H 7.433 0.014 1 286 71 71 THR C C 174.076 0.035 1 287 71 71 THR CA C 64.025 0.041 1 288 71 71 THR CB C 66.952 0.082 1 289 71 71 THR N N 111.991 0.107 1 290 72 72 TYR H H 8.061 0.015 1 291 72 72 TYR C C 170.818 0.006 1 292 72 72 TYR CA C 59.163 0.097 1 293 72 72 TYR CB C 38.278 0.033 1 294 72 72 TYR N N 124.191 0.119 1 295 73 73 ARG H H 6.509 0.016 1 296 73 73 ARG C C 175.991 0.01 1 297 73 73 ARG CA C 55.450 0.015 1 298 73 73 ARG CB C 28.358 0.038 1 299 73 73 ARG N N 107.928 0.118 1 300 74 74 PHE H H 7.964 0.016 1 301 74 74 PHE C C 176.267 0.007 1 302 74 74 PHE CA C 57.094 0.024 1 303 74 74 PHE CB C 37.732 0.044 1 304 74 74 PHE N N 123.354 0.127 1 305 75 75 LYS H H 8.605 0.014 1 306 75 75 LYS C C 176.804 0.003 1 307 75 75 LYS CA C 58.628 0.053 1 308 75 75 LYS CB C 31.487 0.025 1 309 75 75 LYS N N 121.961 0.114 1 310 76 76 LYS H H 8.349 0.015 1 311 76 76 LYS C C 177.243 0.001 1 312 76 76 LYS CA C 59.408 . 1 313 76 76 LYS CB C 31.447 . 1 314 76 76 LYS N N 117.336 0.121 1 315 77 77 GLU H H 6.289 0.004 1 316 77 77 GLU C C 178.752 0.017 1 317 77 77 GLU CA C 57.071 0.033 1 318 77 77 GLU CB C 29.372 0.039 1 319 77 77 GLU N N 118.446 0.013 1 320 78 78 PHE H H 8.027 0.013 1 321 78 78 PHE C C 177.459 0.121 1 322 78 78 PHE CA C 59.974 0.01 1 323 78 78 PHE CB C 37.126 0.024 1 324 78 78 PHE N N 124.214 0.132 1 325 79 79 ASN H H 7.436 0.016 1 326 79 79 ASN C C 174.046 0.003 1 327 79 79 ASN CA C 52.007 0.004 1 328 79 79 ASN CB C 37.531 0.043 1 329 79 79 ASN N N 112.004 0.122 1 330 80 80 ASP H H 6.702 0.02 1 331 80 80 ASP C C 177.233 . 1 332 80 80 ASP CB C 40.925 . 1 333 80 80 ASP N N 123.926 0.116 1 334 82 82 SER C C 170.372 0.03 1 335 82 82 SER CA C 57.193 0.005 1 336 82 82 SER CB C 62.578 0.049 1 337 83 83 ASN H H 8.288 0.012 1 338 83 83 ASN C C 181.281 . 1 339 83 83 ASN CA C 57.861 . 1 340 83 83 ASN CB C 32.523 . 1 341 83 83 ASN N N 127.402 0.104 1 342 84 84 ALA C C 177.548 0.0 1 343 84 84 ALA CA C 54.364 0.011 1 344 84 84 ALA CB C 17.306 0.001 1 345 85 85 GLY H H 8.260 0.017 1 346 85 85 GLY CA C 44.546 . 1 347 85 85 GLY N N 114.422 0.125 1 348 86 86 LEU C C 177.877 0.011 1 349 86 86 LEU CA C 55.552 0.016 1 350 86 86 LEU CB C 38.518 0.04 1 351 87 87 GLN H H 9.236 0.015 1 352 87 87 GLN C C 178.261 0.042 1 353 87 87 GLN CA C 58.559 0.021 1 354 87 87 GLN CB C 25.675 0.013 1 355 87 87 GLN N N 121.848 0.119 1 356 88 88 ASN H H 7.311 0.014 1 357 88 88 ASN C C 178.356 . 1 358 88 88 ASN CA C 56.018 0.023 1 359 88 88 ASN CB C 38.068 0.041 1 360 88 88 ASN N N 116.394 0.112 1 361 89 89 GLY H H 7.428 0.017 1 362 89 89 GLY C C 173.513 0.004 1 363 89 89 GLY CA C 46.418 0.038 1 364 89 89 GLY N N 107.234 0.134 1 365 90 90 PHE H H 7.812 0.012 1 366 90 90 PHE C C 177.472 0.005 1 367 90 90 PHE CA C 61.738 0.019 1 368 90 90 PHE CB C 39.042 0.033 1 369 90 90 PHE N N 122.809 0.1 1 370 91 91 LYS H H 8.450 0.015 1 371 91 91 LYS C C 178.976 0.016 1 372 91 91 LYS CA C 58.321 0.015 1 373 91 91 LYS CB C 31.174 0.028 1 374 91 91 LYS N N 117.732 0.115 1 375 92 92 PHE H H 7.129 0.015 1 376 92 92 PHE C C 175.713 0.004 1 377 92 92 PHE CA C 60.471 0.018 1 378 92 92 PHE CB C 37.851 0.034 1 379 92 92 PHE N N 121.115 0.115 1 380 93 93 LEU H H 7.152 0.014 1 381 93 93 LEU C C 178.488 0.036 1 382 93 93 LEU CA C 55.009 0.017 1 383 93 93 LEU CB C 41.812 0.018 1 384 93 93 LEU N N 114.081 0.119 1 385 94 94 GLU H H 7.633 0.014 1 386 94 94 GLU C C 175.909 . 1 387 94 94 GLU CA C 61.266 . 1 388 94 94 GLU CB C 26.634 . 1 389 94 94 GLU N N 122.907 0.118 1 390 95 95 PRO C C 179.871 0.011 1 391 95 95 PRO CA C 64.866 0.023 1 392 95 95 PRO CB C 29.915 0.039 1 393 96 96 ILE H H 6.620 0.015 1 394 96 96 ILE C C 177.542 0.021 1 395 96 96 ILE CA C 62.961 0.024 1 396 96 96 ILE CB C 35.525 0.044 1 397 96 96 ILE N N 119.115 0.113 1 398 97 97 HIS H H 8.170 0.012 1 399 97 97 HIS C C 177.560 0.001 1 400 97 97 HIS CA C 55.289 0.015 1 401 97 97 HIS CB C 28.464 0.031 1 402 97 97 HIS N N 120.955 0.116 1 403 98 98 LYS H H 7.582 0.013 1 404 98 98 LYS C C 177.811 0.012 1 405 98 98 LYS CA C 57.988 0.047 1 406 98 98 LYS CB C 31.151 0.024 1 407 98 98 LYS N N 115.270 0.127 1 408 99 99 GLU H H 7.064 0.014 1 409 99 99 GLU C C 175.751 0.058 1 410 99 99 GLU CA C 57.178 0.039 1 411 99 99 GLU CB C 28.517 0.014 1 412 99 99 GLU N N 119.319 0.116 1 413 100 100 PHE H H 7.349 0.018 1 414 100 100 PHE CA C 53.458 . 1 415 100 100 PHE CB C 38.089 . 1 416 100 100 PHE N N 116.778 0.123 1 417 101 101 PRO C C 175.814 0.006 1 418 101 101 PRO CA C 64.486 0.047 1 419 101 101 PRO CB C 30.536 0.011 1 420 102 102 TRP H H 6.639 0.014 1 421 102 102 TRP C C 177.092 0.027 1 422 102 102 TRP CA C 53.665 0.02 1 423 102 102 TRP CB C 28.948 0.025 1 424 102 102 TRP N N 114.335 0.11 1 425 103 103 ILE H H 6.861 0.015 1 426 103 103 ILE C C 173.890 . 1 427 103 103 ILE CA C 61.684 . 1 428 103 103 ILE CB C 37.998 . 1 429 103 103 ILE N N 125.423 0.111 1 430 104 104 SER C C 174.929 0.001 1 431 104 104 SER CA C 57.251 0.023 1 432 104 104 SER CB C 64.322 0.063 1 433 105 105 SER H H 10.096 0.014 1 434 105 105 SER C C 174.195 0.006 1 435 105 105 SER CA C 63.290 0.036 1 436 105 105 SER CB C 61.355 0.007 1 437 105 105 SER N N 120.281 0.115 1 438 106 106 GLY H H 9.368 0.014 1 439 106 106 GLY C C 178.740 0.022 1 440 106 106 GLY CA C 45.675 0.002 1 441 106 106 GLY N N 108.932 0.14 1 442 107 107 ASP H H 7.549 0.015 1 443 107 107 ASP C C 176.087 . 1 444 107 107 ASP CB C 38.069 . 1 445 107 107 ASP N N 124.499 0.114 1 446 108 108 LEU H H 7.785 0.011 1 447 108 108 LEU C C 178.224 . 1 448 108 108 LEU CA C 57.763 0.065 1 449 108 108 LEU N N 122.050 0.136 1 450 109 109 PHE H H 8.565 0.02 1 451 109 109 PHE CA C 57.284 . 1 452 109 109 PHE N N 116.071 0.104 1 453 110 110 SER H H 7.775 0.003 1 454 110 110 SER C C 176.038 . 1 455 110 110 SER CA C 61.313 0.091 1 456 110 110 SER N N 112.572 0.057 1 457 111 111 LEU H H 8.688 0.015 1 458 111 111 LEU C C 180.830 . 1 459 111 111 LEU CA C 57.031 0.053 1 460 111 111 LEU CB C 40.541 0.031 1 461 111 111 LEU N N 127.411 0.126 1 462 112 112 GLY H H 8.783 0.015 1 463 112 112 GLY CA C 47.657 0.068 1 464 112 112 GLY N N 109.236 0.229 1 465 113 113 GLY H H 7.258 0.011 1 466 113 113 GLY C C 174.703 0.087 1 467 113 113 GLY CA C 47.397 . 1 468 113 113 GLY N N 105.446 0.122 1 469 115 115 THR C C 176.026 . 1 470 115 115 THR CA C 65.999 . 1 471 115 115 THR CB C 67.945 . 1 472 116 116 ALA H H 8.021 0.015 1 473 116 116 ALA C C 178.660 . 1 474 116 116 ALA CA C 55.954 . 1 475 116 116 ALA CB C 19.561 . 1 476 116 116 ALA N N 121.310 0.144 1 477 117 117 VAL C C 178.906 . 1 478 117 117 VAL CB C 31.334 0.052 1 479 118 118 GLN H H 8.275 0.015 1 480 118 118 GLN C C 181.440 0.022 1 481 118 118 GLN CA C 59.420 0.038 1 482 118 118 GLN CB C 27.708 . 1 483 118 118 GLN N N 115.040 0.107 1 484 119 119 GLU H H 9.352 0.015 1 485 119 119 GLU CA C 57.989 0.01 1 486 119 119 GLU CB C 28.543 0.023 1 487 119 119 GLU N N 119.836 0.115 1 488 120 120 MET H H 7.849 0.016 1 489 120 120 MET C C 173.677 0.004 1 490 120 120 MET CA C 56.462 0.063 1 491 120 120 MET CB C 31.182 0.025 1 492 120 120 MET N N 120.304 0.23 1 493 121 121 GLN H H 7.683 0.014 1 494 121 121 GLN C C 176.180 0.037 1 495 121 121 GLN CA C 57.204 0.052 1 496 121 121 GLN CB C 24.258 0.028 1 497 121 121 GLN N N 109.002 0.119 1 498 122 122 GLY H H 8.297 0.017 1 499 122 122 GLY CA C 44.542 . 1 500 122 122 GLY N N 106.061 0.142 1 501 123 123 PRO C C 174.283 0.0 1 502 123 123 PRO CA C 61.299 0.013 1 503 123 123 PRO CB C 31.236 0.045 1 504 124 124 LYS H H 7.900 0.013 1 505 124 124 LYS C C 178.845 0.041 1 506 124 124 LYS CA C 54.344 0.043 1 507 124 124 LYS N N 112.581 0.121 1 508 125 125 ILE H H 8.835 0.014 1 509 125 125 ILE C C 172.337 . 1 510 125 125 ILE CA C 56.220 . 1 511 125 125 ILE CB C 38.182 . 1 512 125 125 ILE N N 125.702 0.117 1 513 127 127 TRP C C 178.306 . 1 514 127 127 TRP CA C 61.566 . 1 515 127 127 TRP CB C 30.123 . 1 516 128 128 ARG H H 8.148 0.005 1 517 128 128 ARG C C 175.970 . 1 518 128 128 ARG CA C 56.327 . 1 519 128 128 ARG CB C 32.826 . 1 520 128 128 ARG N N 126.997 0.015 1 521 129 129 ALA H H 7.928 0.014 1 522 129 129 ALA CB C 19.561 . 1 523 129 129 ALA N N 129.919 0.174 1 524 131 131 ARG C C 175.330 . 1 525 131 131 ARG CA C 58.934 . 1 526 131 131 ARG CB C 28.056 . 1 527 132 132 VAL H H 7.022 0.02 1 528 132 132 VAL C C 172.095 0.0 1 529 132 132 VAL CA C 60.495 0.035 1 530 132 132 VAL CB C 33.780 0.025 1 531 132 132 VAL N N 117.126 0.133 1 532 133 133 ASP H H 8.066 0.012 1 533 133 133 ASP C C 177.664 0.005 1 534 133 133 ASP CA C 54.479 0.01 1 535 133 133 ASP CB C 38.044 0.022 1 536 133 133 ASP N N 123.966 0.128 1 537 134 134 THR H H 8.534 0.015 1 538 134 134 THR C C 173.971 . 1 539 134 134 THR CA C 59.150 . 1 540 134 134 THR CB C 67.658 . 1 541 134 134 THR N N 116.895 0.112 1 542 135 135 PRO C C 177.561 0.0 1 543 135 135 PRO CA C 62.646 0.005 1 544 135 135 PRO CB C 32.114 0.017 1 545 136 136 GLU H H 8.584 0.013 1 546 136 136 GLU C C 178.728 0.007 1 547 136 136 GLU CA C 59.603 0.025 1 548 136 136 GLU CB C 28.124 0.03 1 549 136 136 GLU N N 124.180 0.119 1 550 137 137 ASP H H 8.383 0.013 1 551 137 137 ASP C C 176.447 0.011 1 552 137 137 ASP CA C 55.006 0.07 1 553 137 137 ASP CB C 38.487 0.053 1 554 137 137 ASP N N 117.766 0.119 1 555 138 138 THR H H 7.862 0.013 1 556 138 138 THR C C 174.374 0.001 1 557 138 138 THR CA C 61.619 0.029 1 558 138 138 THR CB C 69.512 0.056 1 559 138 138 THR N N 110.419 0.116 1 560 139 139 THR H H 7.370 0.015 1 561 139 139 THR C C 172.629 . 1 562 139 139 THR N N 123.714 0.149 1 563 140 140 PRO C C 175.721 0.032 1 564 140 140 PRO CA C 61.727 0.001 1 565 140 140 PRO CB C 30.121 0.023 1 566 141 141 ASP H H 8.082 0.013 1 567 141 141 ASP C C 175.667 0.0 1 568 141 141 ASP CA C 53.909 0.014 1 569 141 141 ASP CB C 39.759 0.025 1 570 141 141 ASP N N 119.715 0.124 1 571 142 142 ASN H H 8.394 0.014 1 572 142 142 ASN C C 174.578 0.017 1 573 142 142 ASN CA C 52.927 0.006 1 574 142 142 ASN CB C 38.359 0.012 1 575 142 142 ASN N N 117.068 0.117 1 576 143 143 GLY H H 7.692 0.018 1 577 143 143 GLY C C 175.847 0.007 1 578 143 143 GLY CA C 44.622 0.038 1 579 143 143 GLY N N 110.438 0.116 1 580 144 144 ARG H H 8.556 0.014 1 581 144 144 ARG C C 175.791 0.005 1 582 144 144 ARG CA C 55.784 0.002 1 583 144 144 ARG CB C 29.521 0.056 1 584 144 144 ARG N N 119.809 0.102 1 585 145 145 LEU H H 7.089 0.025 1 586 145 145 LEU C C 174.962 . 1 587 145 145 LEU CA C 50.962 . 1 588 145 145 LEU N N 120.704 0.162 1 589 148 148 ALA C C 179.205 . 1 590 148 148 ALA CA C 55.121 . 1 591 149 149 ASP H H 9.708 0.008 1 592 149 149 ASP C C 177.079 0.004 1 593 149 149 ASP CA C 53.427 0.022 1 594 149 149 ASP CB C 39.749 0.08 1 595 149 149 ASP N N 117.491 0.114 1 596 150 150 LYS H H 7.248 0.012 1 597 150 150 LYS C C 173.358 0.011 1 598 150 150 LYS CA C 54.236 0.005 1 599 150 150 LYS CB C 36.084 0.04 1 600 150 150 LYS N N 119.318 0.124 1 601 151 151 ASP H H 7.596 0.013 1 602 151 151 ASP C C 176.939 0.006 1 603 151 151 ASP CA C 51.721 0.016 1 604 151 151 ASP CB C 42.668 0.025 1 605 151 151 ASP N N 116.469 0.118 1 606 152 152 ALA H H 8.808 0.013 1 607 152 152 ALA C C 179.637 . 1 608 152 152 ALA CA C 55.525 0.004 1 609 152 152 ALA CB C 19.069 0.017 1 610 152 152 ALA N N 120.137 0.108 1 611 153 153 ASP H H 8.094 0.014 1 612 153 153 ASP C C 179.551 0.054 1 613 153 153 ASP CA C 57.168 0.009 1 614 153 153 ASP CB C 40.286 0.007 1 615 153 153 ASP N N 115.742 0.122 1 616 154 154 TYR H H 8.361 0.014 1 617 154 154 TYR C C 177.978 0.026 1 618 154 154 TYR CA C 61.852 0.058 1 619 154 154 TYR CB C 38.132 0.021 1 620 154 154 TYR N N 122.286 0.12 1 621 155 155 VAL H H 9.016 0.014 1 622 155 155 VAL C C 178.178 0.051 1 623 155 155 VAL CA C 68.741 0.027 1 624 155 155 VAL CB C 32.347 0.035 1 625 155 155 VAL N N 123.800 0.126 1 626 156 156 ARG H H 9.401 0.013 1 627 156 156 ARG C C 181.030 0.006 1 628 156 156 ARG CA C 60.389 0.017 1 629 156 156 ARG CB C 29.294 0.03 1 630 156 156 ARG N N 122.263 0.117 1 631 157 157 THR H H 8.645 0.014 1 632 157 157 THR C C 177.610 0.013 1 633 157 157 THR CA C 66.538 0.024 1 634 157 157 THR CB C 68.645 0.083 1 635 157 157 THR N N 116.578 0.123 1 636 158 158 PHE H H 9.744 0.014 1 637 158 158 PHE C C 178.609 0.031 1 638 158 158 PHE CA C 62.077 0.022 1 639 158 158 PHE CB C 38.719 0.033 1 640 158 158 PHE N N 126.691 0.122 1 641 159 159 PHE H H 9.132 0.014 1 642 159 159 PHE C C 179.902 0.004 1 643 159 159 PHE CA C 62.709 0.012 1 644 159 159 PHE CB C 39.939 0.019 1 645 159 159 PHE N N 115.064 0.122 1 646 160 160 GLN H H 8.257 0.014 1 647 160 160 GLN C C 180.535 0.006 1 648 160 160 GLN CA C 59.278 0.025 1 649 160 160 GLN CB C 26.990 0.027 1 650 160 160 GLN N N 122.308 0.112 1 651 161 161 ARG H H 7.800 0.015 1 652 161 161 ARG C C 175.100 0.018 1 653 161 161 ARG CA C 58.127 0.022 1 654 161 161 ARG CB C 29.810 0.028 1 655 161 161 ARG N N 123.947 0.115 1 656 162 162 LEU H H 6.989 0.014 1 657 162 162 LEU C C 176.011 0.013 1 658 162 162 LEU CA C 53.680 0.042 1 659 162 162 LEU CB C 43.012 0.019 1 660 162 162 LEU N N 112.577 0.103 1 661 163 163 ASN H H 8.163 0.016 1 662 163 163 ASN C C 174.324 0.008 1 663 163 163 ASN CA C 53.661 0.041 1 664 163 163 ASN CB C 37.551 0.018 1 665 163 163 ASN N N 113.695 0.114 1 666 164 164 MET H H 7.942 0.014 1 667 164 164 MET C C 176.803 0.005 1 668 164 164 MET CA C 52.935 0.023 1 669 164 164 MET CB C 33.498 0.067 1 670 164 164 MET N N 114.332 0.114 1 671 165 165 ASN H H 10.298 0.012 1 672 165 165 ASN C C 174.735 0.01 1 673 165 165 ASN CA C 50.698 0.007 1 674 165 165 ASN CB C 38.611 0.015 1 675 165 165 ASN N N 126.783 0.127 1 676 166 166 ASP H H 8.293 0.012 1 677 166 166 ASP C C 177.127 0.019 1 678 166 166 ASP CA C 57.771 0.024 1 679 166 166 ASP CB C 40.265 0.029 1 680 166 166 ASP N N 114.883 0.11 1 681 167 167 ARG H H 7.823 0.014 1 682 167 167 ARG C C 177.463 0.011 1 683 167 167 ARG CA C 60.207 0.035 1 684 167 167 ARG CB C 29.421 0.025 1 685 167 167 ARG N N 118.115 0.125 1 686 168 168 GLU H H 8.107 0.013 1 687 168 168 GLU C C 178.611 0.034 1 688 168 168 GLU CA C 59.485 0.027 1 689 168 168 GLU CB C 30.136 0.031 1 690 168 168 GLU N N 117.655 0.129 1 691 169 169 VAL H H 8.761 0.013 1 692 169 169 VAL C C 177.681 0.013 1 693 169 169 VAL CA C 67.756 0.072 1 694 169 169 VAL CB C 31.295 . 1 695 169 169 VAL N N 118.643 0.118 1 696 170 170 VAL H H 8.276 0.012 1 697 170 170 VAL C C 179.987 0.025 1 698 170 170 VAL CA C 66.733 0.067 1 699 170 170 VAL CB C 30.866 0.031 1 700 170 170 VAL N N 117.491 0.115 1 701 171 171 ALA H H 9.102 0.017 1 702 171 171 ALA CA C 55.398 . 1 703 171 171 ALA CB C 16.064 . 1 704 171 171 ALA N N 123.264 0.119 1 705 174 174 GLY H H 7.174 0.002 1 706 174 174 GLY CA C 44.224 . 1 707 174 174 GLY N N 114.635 0.07 1 708 176 176 HIS C C 181.208 . 1 709 176 176 HIS CB C 24.293 0.114 1 710 177 177 ALA H H 7.053 0.017 1 711 177 177 ALA CB C 14.577 . 1 712 177 177 ALA N N 113.613 0.124 1 713 180 180 LYS C C 176.438 . 1 714 180 180 LYS CA C 55.624 . 1 715 180 180 LYS CB C 31.935 0.067 1 716 181 181 THR H H 7.994 0.018 1 717 181 181 THR C C 176.886 . 1 718 181 181 THR CA C 61.492 . 1 719 181 181 THR CB C 69.307 . 1 720 181 181 THR N N 116.936 0.139 1 721 182 182 HIS H H 7.970 0.001 1 722 182 182 HIS C C 178.007 0.006 1 723 182 182 HIS CA C 55.314 0.034 1 724 182 182 HIS CB C 30.427 0.004 1 725 182 182 HIS N N 122.260 0.003 1 726 183 183 LEU H H 9.457 0.014 1 727 183 183 LEU C C 181.166 0.01 1 728 183 183 LEU CA C 59.942 0.022 1 729 183 183 LEU CB C 42.346 0.027 1 730 183 183 LEU N N 132.497 0.114 1 731 184 184 LYS H H 9.251 0.012 1 732 184 184 LYS C C 177.360 0.003 1 733 184 184 LYS CA C 57.807 0.051 1 734 184 184 LYS CB C 31.316 0.034 1 735 184 184 LYS N N 114.477 0.125 1 736 185 185 ASN H H 8.442 0.013 1 737 185 185 ASN C C 176.467 . 1 738 185 185 ASN CA C 54.038 . 1 739 185 185 ASN CB C 38.152 . 1 740 185 185 ASN N N 116.224 0.116 1 741 186 186 SER C C 176.606 . 1 742 186 186 SER CA C 59.403 0.032 1 743 186 186 SER CB C 70.199 . 1 744 187 187 GLY H H 8.958 0.017 1 745 187 187 GLY C C 172.341 0.01 1 746 187 187 GLY CA C 45.699 0.026 1 747 187 187 GLY N N 111.409 0.136 1 748 188 188 TYR H H 8.551 0.014 1 749 188 188 TYR C C 171.634 . 1 750 188 188 TYR CA C 59.009 0.016 1 751 188 188 TYR CB C 41.032 0.083 1 752 188 188 TYR N N 120.452 0.119 1 753 189 189 GLU H H 8.252 0.013 1 754 189 189 GLU C C 176.529 0.027 1 755 189 189 GLU CA C 55.254 0.055 1 756 189 189 GLU CB C 33.351 0.015 1 757 189 189 GLU N N 118.550 0.114 1 758 190 190 GLY H H 7.679 0.015 1 759 190 190 GLY CA C 42.992 . 1 760 190 190 GLY N N 118.230 0.133 1 761 193 193 GLY C C 171.870 0.01 1 762 193 193 GLY CA C 43.879 0.002 1 763 194 194 ALA H H 9.201 0.021 1 764 194 194 ALA C C 178.925 0.022 1 765 194 194 ALA CA C 52.454 0.008 1 766 194 194 ALA CB C 19.632 0.047 1 767 194 194 ALA N N 122.380 0.088 1 768 195 195 ALA H H 8.262 0.015 1 769 195 195 ALA C C 177.390 0.007 1 770 195 195 ALA CA C 50.904 0.02 1 771 195 195 ALA CB C 16.538 0.019 1 772 195 195 ALA N N 124.383 0.144 1 773 196 196 ASN H H 8.058 0.014 1 774 196 196 ASN C C 175.980 0.006 1 775 196 196 ASN CA C 54.300 0.012 1 776 196 196 ASN CB C 38.181 0.047 1 777 196 196 ASN N N 113.595 0.118 1 778 197 197 ASN H H 8.023 0.017 1 779 197 197 ASN C C 173.497 0.011 1 780 197 197 ASN CA C 51.831 0.031 1 781 197 197 ASN CB C 37.143 0.042 1 782 197 197 ASN N N 115.195 0.118 1 783 198 198 VAL H H 7.463 0.014 1 784 198 198 VAL C C 173.740 0.008 1 785 198 198 VAL CA C 60.789 0.011 1 786 198 198 VAL CB C 34.095 0.019 1 787 198 198 VAL N N 117.049 0.12 1 788 199 199 PHE H H 9.239 0.014 1 789 199 199 PHE C C 173.370 0.01 1 790 199 199 PHE CA C 59.088 0.05 1 791 199 199 PHE CB C 38.844 0.04 1 792 199 199 PHE N N 128.588 0.115 1 793 200 200 THR H H 6.481 0.017 1 794 200 200 THR C C 172.973 0.003 1 795 200 200 THR CA C 59.844 0.025 1 796 200 200 THR CB C 72.560 0.022 1 797 200 200 THR N N 117.305 0.117 1 798 201 201 ASN H H 8.499 0.014 1 799 201 201 ASN C C 175.237 0.013 1 800 201 201 ASN CA C 52.212 0.013 1 801 201 201 ASN CB C 36.307 0.05 1 802 201 201 ASN N N 116.121 0.113 1 803 202 202 GLU H H 7.927 0.017 1 804 202 202 GLU C C 174.992 0.021 1 805 202 202 GLU CA C 59.162 0.266 1 806 202 202 GLU CB C 27.907 0.083 1 807 202 202 GLU N N 118.919 0.123 1 808 203 203 PHE H H 6.573 0.017 1 809 203 203 PHE C C 173.988 . 1 810 203 203 PHE CA C 59.911 . 1 811 203 203 PHE CB C 36.344 . 1 812 203 203 PHE N N 116.454 0.128 1 813 204 204 TYR C C 177.343 . 1 814 204 204 TYR CB C 36.284 0.032 1 815 205 205 LEU H H 6.371 0.011 1 816 205 205 LEU C C 178.417 0.093 1 817 205 205 LEU CA C 56.897 0.08 1 818 205 205 LEU CB C 40.209 0.106 1 819 205 205 LEU N N 115.714 0.102 1 820 206 206 ASN H H 7.925 0.018 1 821 206 206 ASN C C 177.623 0.002 1 822 206 206 ASN CA C 54.233 0.015 1 823 206 206 ASN CB C 33.900 0.001 1 824 206 206 ASN N N 118.237 0.13 1 825 207 207 LEU H H 6.975 0.018 1 826 207 207 LEU C C 177.488 0.018 1 827 207 207 LEU CA C 57.405 0.039 1 828 207 207 LEU CB C 39.704 0.036 1 829 207 207 LEU N N 122.330 0.118 1 830 208 208 LEU H H 6.512 0.017 1 831 208 208 LEU C C 178.928 0.007 1 832 208 208 LEU CA C 55.730 0.041 1 833 208 208 LEU CB C 41.745 0.024 1 834 208 208 LEU N N 111.997 0.122 1 835 209 209 ASN H H 7.921 0.015 1 836 209 209 ASN C C 176.696 0.005 1 837 209 209 ASN CA C 53.947 0.012 1 838 209 209 ASN CB C 39.246 0.038 1 839 209 209 ASN N N 114.069 0.114 1 840 210 210 GLU H H 7.237 0.015 1 841 210 210 GLU C C 173.431 0.005 1 842 210 210 GLU CA C 54.528 0.011 1 843 210 210 GLU CB C 28.754 0.021 1 844 210 210 GLU N N 118.469 0.115 1 845 211 211 ASP H H 7.798 0.014 1 846 211 211 ASP C C 174.988 0.01 1 847 211 211 ASP CA C 52.143 0.014 1 848 211 211 ASP CB C 40.053 0.021 1 849 211 211 ASP N N 119.480 0.111 1 850 212 212 TRP H H 7.569 0.013 1 851 212 212 TRP C C 176.446 0.006 1 852 212 212 TRP CA C 55.797 0.015 1 853 212 212 TRP CB C 32.217 0.031 1 854 212 212 TRP N N 124.419 0.116 1 855 213 213 LYS H H 8.980 0.015 1 856 213 213 LYS C C 173.965 0.005 1 857 213 213 LYS CA C 54.645 0.012 1 858 213 213 LYS CB C 34.980 0.015 1 859 213 213 LYS N N 124.004 0.113 1 860 214 214 LEU H H 8.011 0.013 1 861 214 214 LEU C C 176.309 0.01 1 862 214 214 LEU CA C 54.450 0.015 1 863 214 214 LEU CB C 39.245 0.056 1 864 214 214 LEU N N 131.006 0.139 1 865 215 215 GLU H H 8.878 0.015 1 866 215 215 GLU C C 174.270 0.003 1 867 215 215 GLU CA C 54.042 0.033 1 868 215 215 GLU CB C 31.642 0.026 1 869 215 215 GLU N N 127.183 0.116 1 870 216 216 LYS H H 8.305 0.014 1 871 216 216 LYS C C 177.085 0.006 1 872 216 216 LYS CA C 55.219 0.022 1 873 216 216 LYS CB C 32.705 0.026 1 874 216 216 LYS N N 119.927 0.114 1 875 217 217 ASN H H 8.629 0.012 1 876 217 217 ASN C C 178.296 0.03 1 877 217 217 ASN CA C 50.696 0.01 1 878 217 217 ASN CB C 38.875 0.038 1 879 217 217 ASN N N 122.963 0.106 1 880 218 218 ASP H H 8.906 0.011 1 881 218 218 ASP C C 176.885 0.005 1 882 218 218 ASP CA C 56.621 0.019 1 883 218 218 ASP CB C 39.967 0.042 1 884 218 218 ASP N N 117.614 0.108 1 885 219 219 ALA H H 8.362 0.014 1 886 219 219 ALA C C 176.076 0.013 1 887 219 219 ALA CA C 51.290 0.014 1 888 219 219 ALA CB C 17.840 0.01 1 889 219 219 ALA N N 122.733 0.119 1 890 220 220 ASN H H 8.378 0.015 1 891 220 220 ASN C C 174.005 0.017 1 892 220 220 ASN CA C 54.509 0.017 1 893 220 220 ASN CB C 37.001 0.035 1 894 220 220 ASN N N 112.952 0.115 1 895 221 221 ASN H H 7.705 0.013 1 896 221 221 ASN C C 174.655 0.006 1 897 221 221 ASN CA C 51.548 0.014 1 898 221 221 ASN CB C 40.076 0.025 1 899 221 221 ASN N N 115.820 0.112 1 900 222 222 GLU H H 8.550 0.012 1 901 222 222 GLU C C 175.480 0.004 1 902 222 222 GLU CA C 55.637 0.01 1 903 222 222 GLU CB C 29.415 0.029 1 904 222 222 GLU N N 120.093 0.118 1 905 223 223 GLN H H 8.892 0.013 1 906 223 223 GLN C C 171.936 0.025 1 907 223 223 GLN CA C 53.737 0.019 1 908 223 223 GLN N N 117.593 0.082 1 909 224 224 TRP H H 8.032 0.013 1 910 224 224 TRP C C 174.406 0.008 1 911 224 224 TRP CA C 55.505 0.01 1 912 224 224 TRP CB C 28.440 0.029 1 913 224 224 TRP N N 123.231 0.119 1 914 225 225 ASP H H 9.282 0.014 1 915 225 225 ASP C C 176.274 0.007 1 916 225 225 ASP CA C 51.679 0.01 1 917 225 225 ASP CB C 42.179 0.029 1 918 225 225 ASP N N 119.977 0.113 1 919 226 226 SER H H 8.545 0.015 1 920 226 226 SER C C 176.789 0.009 1 921 226 226 SER CA C 54.522 0.005 1 922 226 226 SER CB C 64.897 0.092 1 923 226 226 SER N N 118.467 0.122 1 924 227 227 LYS H H 8.489 0.015 1 925 227 227 LYS C C 177.442 0.01 1 926 227 227 LYS CA C 57.695 0.04 1 927 227 227 LYS CB C 30.429 0.028 1 928 227 227 LYS N N 124.718 0.111 1 929 228 228 SER H H 7.160 0.016 1 930 228 228 SER C C 172.913 0.013 1 931 228 228 SER CA C 57.260 0.038 1 932 228 228 SER CB C 61.332 0.1 1 933 228 228 SER N N 112.755 0.107 1 934 229 229 GLY H H 7.383 0.016 1 935 229 229 GLY C C 173.835 . 1 936 229 229 GLY CA C 43.986 . 1 937 229 229 GLY N N 106.274 0.136 1 938 230 230 TYR C C 174.270 0.005 1 939 230 230 TYR CA C 51.921 0.003 1 940 230 230 TYR CB C 38.408 0.005 1 941 231 231 MET H H 8.357 0.016 1 942 231 231 MET C C 171.408 0.018 1 943 231 231 MET CA C 52.511 0.026 1 944 231 231 MET CB C 36.247 0.009 1 945 231 231 MET N N 123.312 0.117 1 946 232 232 MET H H 7.857 0.017 1 947 232 232 MET C C 175.689 . 1 948 232 232 MET CA C 51.728 . 1 949 232 232 MET CB C 34.064 . 1 950 232 232 MET N N 111.730 0.114 1 951 235 235 THR C C 178.068 . 1 952 236 236 ASP H H 8.378 0.001 1 953 236 236 ASP C C 175.675 . 1 954 236 236 ASP CA C 55.840 0.027 1 955 236 236 ASP CB C 44.140 . 1 956 236 236 ASP N N 115.042 0.02 1 957 237 237 TYR H H 7.044 0.017 1 958 237 237 TYR C C 176.886 0.003 1 959 237 237 TYR CA C 59.478 0.034 1 960 237 237 TYR CB C 38.281 0.044 1 961 237 237 TYR N N 118.129 0.121 1 962 238 238 SER H H 7.423 0.019 1 963 238 238 SER C C 175.356 . 1 964 238 238 SER CA C 61.479 . 1 965 238 238 SER CB C 62.328 0.005 1 966 238 238 SER N N 113.419 0.142 1 967 239 239 LEU H H 6.977 0.018 1 968 239 239 LEU C C 176.123 0.017 1 969 239 239 LEU CA C 55.693 0.002 1 970 239 239 LEU CB C 39.502 0.036 1 971 239 239 LEU N N 119.968 0.132 1 972 240 240 ILE H H 6.671 0.018 1 973 240 240 ILE C C 176.961 0.011 1 974 240 240 ILE CA C 59.186 0.009 1 975 240 240 ILE CB C 36.601 0.006 1 976 240 240 ILE N N 129.904 10.599 1 977 241 241 GLN H H 7.005 0.014 1 978 241 241 GLN C C 175.814 0.008 1 979 241 241 GLN CA C 55.766 0.022 1 980 241 241 GLN CB C 29.136 0.043 1 981 241 241 GLN N N 120.586 0.117 1 982 242 242 ASP H H 7.222 0.013 1 983 242 242 ASP C C 173.799 . 1 984 242 242 ASP CA C 50.403 . 1 985 242 242 ASP CB C 43.910 . 1 986 242 242 ASP N N 122.782 0.117 1 987 243 243 PRO C C 179.402 0.003 1 988 243 243 PRO CA C 64.588 0.015 1 989 243 243 PRO CB C 31.323 0.05 1 990 244 244 LYS H H 7.439 0.015 1 991 244 244 LYS C C 180.297 0.011 1 992 244 244 LYS CA C 58.184 0.015 1 993 244 244 LYS CB C 30.673 0.028 1 994 244 244 LYS N N 118.647 0.106 1 995 245 245 TYR H H 8.464 0.014 1 996 245 245 TYR C C 178.787 0.002 1 997 245 245 TYR CA C 57.246 0.029 1 998 245 245 TYR CB C 36.756 0.027 1 999 245 245 TYR N N 121.059 0.118 1 1000 246 246 LEU H H 8.555 0.013 1 1001 246 246 LEU C C 178.019 0.004 1 1002 246 246 LEU CA C 57.775 0.004 1 1003 246 246 LEU CB C 40.318 0.021 1 1004 246 246 LEU N N 121.919 0.116 1 1005 247 247 SER H H 6.906 0.013 1 1006 247 247 SER C C 176.421 0.042 1 1007 247 247 SER CA C 61.026 0.025 1 1008 247 247 SER CB C 62.717 0.022 1 1009 247 247 SER N N 109.766 0.123 1 1010 248 248 ILE H H 7.086 0.016 1 1011 248 248 ILE C C 176.529 0.007 1 1012 248 248 ILE CA C 63.830 0.044 1 1013 248 248 ILE CB C 37.191 0.016 1 1014 248 248 ILE N N 123.299 0.105 1 1015 249 249 VAL H H 8.151 0.015 1 1016 249 249 VAL C C 177.966 0.007 1 1017 249 249 VAL CA C 65.929 0.051 1 1018 249 249 VAL CB C 30.236 0.015 1 1019 249 249 VAL N N 121.811 0.113 1 1020 250 250 LYS H H 7.761 0.015 1 1021 250 250 LYS C C 178.776 0.014 1 1022 250 250 LYS CA C 59.390 0.024 1 1023 250 250 LYS CB C 31.603 0.022 1 1024 250 250 LYS N N 115.171 0.117 1 1025 251 251 GLU H H 6.935 0.015 1 1026 251 251 GLU C C 179.845 0.024 1 1027 251 251 GLU CA C 58.782 0.039 1 1028 251 251 GLU CB C 28.899 0.022 1 1029 251 251 GLU N N 120.168 0.16 1 1030 252 252 TYR H H 7.378 0.015 1 1031 252 252 TYR C C 178.439 0.003 1 1032 252 252 TYR CA C 55.120 0.014 1 1033 252 252 TYR CB C 34.921 0.018 1 1034 252 252 TYR N N 119.499 0.116 1 1035 253 253 ALA H H 8.091 0.015 1 1036 253 253 ALA C C 177.255 0.006 1 1037 253 253 ALA CA C 53.937 0.02 1 1038 253 253 ALA CB C 17.521 0.021 1 1039 253 253 ALA N N 121.345 0.119 1 1040 254 254 ASN H H 6.934 0.015 1 1041 254 254 ASN C C 174.839 0.024 1 1042 254 254 ASN CA C 53.534 0.011 1 1043 254 254 ASN CB C 39.550 0.018 1 1044 254 254 ASN N N 111.975 0.118 1 1045 255 255 ASP H H 7.436 0.013 1 1046 255 255 ASP C C 174.088 0.016 1 1047 255 255 ASP CA C 52.604 0.028 1 1048 255 255 ASP CB C 41.041 0.014 1 1049 255 255 ASP N N 120.151 0.099 1 1050 256 256 GLN H H 8.935 0.009 1 1051 256 256 GLN C C 176.686 0.008 1 1052 256 256 GLN CA C 59.145 0.006 1 1053 256 256 GLN CB C 29.436 0.019 1 1054 256 256 GLN N N 125.685 0.1 1 1055 257 257 ASP H H 8.019 0.014 1 1056 257 257 ASP C C 178.372 0.011 1 1057 257 257 ASP CA C 57.432 0.01 1 1058 257 257 ASP CB C 40.244 0.017 1 1059 257 257 ASP N N 118.676 0.116 1 1060 258 258 LYS H H 7.526 0.014 1 1061 258 258 LYS C C 177.980 0.039 1 1062 258 258 LYS CA C 58.222 0.007 1 1063 258 258 LYS CB C 31.377 0.015 1 1064 258 258 LYS N N 121.816 0.115 1 1065 259 259 PHE H H 7.288 0.015 1 1066 259 259 PHE C C 175.954 0.025 1 1067 259 259 PHE CA C 58.271 0.021 1 1068 259 259 PHE CB C 36.812 0.066 1 1069 259 259 PHE N N 118.395 0.122 1 1070 260 260 PHE H H 8.906 0.014 1 1071 260 260 PHE C C 178.295 0.019 1 1072 260 260 PHE CA C 59.717 0.03 1 1073 260 260 PHE CB C 36.662 . 1 1074 260 260 PHE N N 121.045 0.123 1 1075 261 261 LYS H H 7.915 0.015 1 1076 261 261 LYS C C 179.899 0.039 1 1077 261 261 LYS CB C 31.768 0.081 1 1078 261 261 LYS N N 118.876 0.124 1 1079 262 262 ASP H H 8.405 0.015 1 1080 262 262 ASP C C 180.053 0.02 1 1081 262 262 ASP CA C 56.866 0.014 1 1082 262 262 ASP CB C 38.495 0.034 1 1083 262 262 ASP N N 121.816 0.123 1 1084 263 263 PHE H H 9.931 0.016 1 1085 263 263 PHE C C 176.659 0.034 1 1086 263 263 PHE CA C 63.003 0.034 1 1087 263 263 PHE CB C 38.375 0.064 1 1088 263 263 PHE N N 123.675 0.123 1 1089 264 264 SER H H 8.436 0.014 1 1090 264 264 SER C C 176.723 0.024 1 1091 264 264 SER CA C 61.481 0.011 1 1092 264 264 SER CB C 62.493 0.031 1 1093 264 264 SER N N 112.992 0.177 1 1094 265 265 LYS H H 7.311 0.014 1 1095 265 265 LYS C C 179.655 0.041 1 1096 265 265 LYS CA C 58.738 0.083 1 1097 265 265 LYS CB C 32.270 0.044 1 1098 265 265 LYS N N 117.411 0.111 1 1099 266 266 ALA H H 8.336 0.014 1 1100 266 266 ALA C C 179.140 0.042 1 1101 266 266 ALA CA C 55.196 0.035 1 1102 266 266 ALA CB C 17.716 0.036 1 1103 266 266 ALA N N 123.287 0.114 1 1104 267 267 PHE H H 9.782 0.018 1 1105 267 267 PHE C C 177.863 0.025 1 1106 267 267 PHE CA C 60.333 0.05 1 1107 267 267 PHE CB C 39.237 0.035 1 1108 267 267 PHE N N 120.724 0.13 1 1109 268 268 GLU H H 8.199 0.015 1 1110 268 268 GLU C C 177.340 0.006 1 1111 268 268 GLU CA C 59.917 0.074 1 1112 268 268 GLU CB C 25.874 0.056 1 1113 268 268 GLU N N 117.849 0.129 1 1114 269 269 LYS H H 7.829 0.013 1 1115 269 269 LYS C C 179.039 0.038 1 1116 269 269 LYS CA C 59.428 0.056 1 1117 269 269 LYS CB C 32.320 0.037 1 1118 269 269 LYS N N 118.977 0.12 1 1119 270 270 LEU H H 8.703 0.013 1 1120 270 270 LEU C C 179.842 . 1 1121 270 270 LEU CB C 42.343 . 1 1122 270 270 LEU N N 120.151 0.144 1 1123 271 271 LEU C C 178.182 . 1 1124 271 271 LEU CA C 56.258 . 1 1125 271 271 LEU CB C 40.407 . 1 1126 272 272 GLU H H 7.757 0.019 1 1127 272 272 GLU C C 176.213 0.016 1 1128 272 272 GLU CA C 55.197 0.038 1 1129 272 272 GLU CB C 29.437 0.028 1 1130 272 272 GLU N N 119.870 0.129 1 1131 273 273 ASN H H 7.280 0.014 1 1132 273 273 ASN C C 176.482 0.003 1 1133 273 273 ASN CA C 53.045 0.011 1 1134 273 273 ASN CB C 36.867 0.025 1 1135 273 273 ASN N N 123.292 0.113 1 1136 274 274 GLY H H 8.365 0.014 1 1137 274 274 GLY C C 174.591 0.008 1 1138 274 274 GLY CA C 45.327 0.021 1 1139 274 274 GLY N N 109.970 0.125 1 1140 275 275 ILE H H 7.614 0.012 1 1141 275 275 ILE C C 175.229 0.017 1 1142 275 275 ILE CA C 60.960 0.053 1 1143 275 275 ILE CB C 37.642 0.022 1 1144 275 275 ILE N N 121.810 0.088 1 1145 276 276 THR H H 8.750 0.015 1 1146 276 276 THR C C 172.626 0.005 1 1147 276 276 THR CA C 61.466 0.039 1 1148 276 276 THR CB C 69.299 0.025 1 1149 276 276 THR N N 124.956 0.113 1 1150 277 277 PHE H H 9.136 0.012 1 1151 277 277 PHE C C 173.731 . 1 1152 277 277 PHE CA C 55.495 . 1 1153 277 277 PHE CB C 38.082 . 1 1154 277 277 PHE N N 129.216 0.117 1 1155 278 278 PRO C C 177.144 0.005 1 1156 278 278 PRO CA C 61.921 0.006 1 1157 278 278 PRO CB C 32.191 0.006 1 1158 279 279 LYS H H 8.802 0.013 1 1159 279 279 LYS C C 176.810 0.004 1 1160 279 279 LYS CA C 58.441 0.006 1 1161 279 279 LYS CB C 31.168 0.024 1 1162 279 279 LYS N N 121.813 0.12 1 1163 280 280 ASP H H 8.178 0.014 1 1164 280 280 ASP C C 175.820 0.009 1 1165 280 280 ASP CA C 52.544 0.017 1 1166 280 280 ASP CB C 38.937 0.03 1 1167 280 280 ASP N N 115.041 0.112 1 1168 281 281 ALA H H 7.518 0.014 1 1169 281 281 ALA C C 175.356 . 1 1170 281 281 ALA CA C 50.503 . 1 1171 281 281 ALA CB C 16.996 . 1 1172 281 281 ALA N N 124.144 0.113 1 1173 282 282 PRO C C 176.880 0.002 1 1174 282 282 PRO CA C 62.125 0.013 1 1175 282 282 PRO CB C 31.008 0.019 1 1176 283 283 SER H H 8.343 0.012 1 1177 283 283 SER C C 171.205 . 1 1178 283 283 SER CA C 57.865 . 1 1179 283 283 SER CB C 60.929 . 1 1180 283 283 SER N N 119.147 0.121 1 1181 284 284 PRO C C 175.702 0.004 1 1182 284 284 PRO CA C 62.976 0.01 1 1183 284 284 PRO CB C 31.533 0.016 1 1184 285 285 PHE H H 9.055 0.014 1 1185 285 285 PHE C C 174.919 0.004 1 1186 285 285 PHE CA C 54.245 0.032 1 1187 285 285 PHE CB C 39.561 0.028 1 1188 285 285 PHE N N 124.455 0.119 1 1189 286 286 ILE H H 7.913 0.012 1 1190 286 286 ILE C C 176.811 0.046 1 1191 286 286 ILE CA C 58.908 0.063 1 1192 286 286 ILE CB C 36.928 . 1 1193 286 286 ILE N N 120.307 0.112 1 1194 287 287 PHE H H 10.001 0.014 1 1195 287 287 PHE C C 177.228 0.002 1 1196 287 287 PHE CA C 58.935 0.025 1 1197 287 287 PHE CB C 38.986 0.037 1 1198 287 287 PHE N N 130.181 0.11 1 1199 288 288 LYS H H 8.782 0.015 1 1200 288 288 LYS C C 176.622 0.039 1 1201 288 288 LYS CA C 54.827 0.018 1 1202 288 288 LYS CB C 33.493 0.064 1 1203 288 288 LYS N N 123.827 0.117 1 1204 289 289 THR H H 8.615 0.021 1 1205 289 289 THR C C 179.242 0.031 1 1206 289 289 THR CA C 59.812 0.048 1 1207 289 289 THR CB C 70.422 0.035 1 1208 289 289 THR N N 109.584 0.126 1 1209 290 290 LEU H H 9.606 0.016 1 1210 290 290 LEU C C 180.551 0.006 1 1211 290 290 LEU CA C 59.115 . 1 1212 290 290 LEU CB C 39.008 0.035 1 1213 290 290 LEU N N 122.591 0.115 1 1214 291 291 GLU H H 8.927 0.017 1 1215 291 291 GLU C C 180.957 0.008 1 1216 291 291 GLU CA C 59.001 . 1 1217 291 291 GLU CB C 28.603 0.023 1 1218 291 291 GLU N N 120.222 0.117 1 1219 292 292 GLU H H 8.057 0.014 1 1220 292 292 GLU C C 178.655 0.004 1 1221 292 292 GLU CA C 58.384 0.024 1 1222 292 292 GLU CB C 29.642 0.023 1 1223 292 292 GLU N N 120.428 0.121 1 1224 293 293 GLN H H 7.603 0.015 1 1225 293 293 GLN C C 175.808 0.001 1 1226 293 293 GLN CA C 55.721 0.007 1 1227 293 293 GLN CB C 32.790 0.044 1 1228 293 293 GLN N N 116.385 0.098 1 1229 294 294 GLY H H 7.978 0.015 1 1230 294 294 GLY C C 174.129 0.008 1 1231 294 294 GLY CA C 45.831 0.015 1 1232 294 294 GLY N N 110.269 0.118 1 1233 295 295 LEU H H 7.734 0.011 1 1234 295 295 LEU C C 182.344 . 1 1235 295 295 LEU CA C 54.851 . 1 1236 295 295 LEU CB C 44.267 . 1 1237 295 295 LEU N N 126.104 0.088 1 stop_ save_