data_7114 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N chemical shift assignment of Escherichia coli Maltose Binding Protein complexed with Beta-Cyclodextrin ; _BMRB_accession_number 7114 _BMRB_flat_file_name bmr7114.str _Entry_type original _Submission_date 2006-05-17 _Accession_date 2006-05-17 _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 Xu Yingqi . . 2 Lin Zhi . . 3 Zheng Yu . . 4 Yang Daiwen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1981 "13C chemical shifts" 1605 "15N chemical shifts" 373 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-11-01 original author . stop_ _Original_release_date 2006-11-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'A new strategy for structure determination of large proteins in solution without deuteration' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17060917 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu Yingqi . . 2 Zheng Yu . . 3 Fan JS . . 4 Yang Daiwen . . stop_ _Journal_abbreviation 'Nature Methods' _Journal_volume 3 _Journal_issue 11 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 931 _Page_last 937 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'E. coli maltose binding protein' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MBP $MBP beta-cyclodextrin $BCD stop_ _System_molecular_weight 42000 _System_physical_state native _System_oligomer_state 'protein-ligand system' _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'maltose binding protein' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 370 _Mol_residue_sequence ; KTEEGKLVIWINGDKGYNGL AEVGKKFEKDTGIKVTVEHP DKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEIT PDKAFQDKLYPFTWDAVRYN GKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELK AKGKSALMFNLQEPYFTWPL IAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIK NKHMNADTDYSIAEAAFNKG ETAMTINGPWAWSNIDTSKV NYGVTVLPTFKGQPSKPFVG VLSAGINAASPNKELAKEFL ENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAAT MENAQKGEIMPNIPQMSAFW YAVRTAVINAASGRQTVDEA LKDAQTRITK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 LYS 2 2 THR 3 3 GLU 4 4 GLU 5 5 GLY 6 6 LYS 7 7 LEU 8 8 VAL 9 9 ILE 10 10 TRP 11 11 ILE 12 12 ASN 13 13 GLY 14 14 ASP 15 15 LYS 16 16 GLY 17 17 TYR 18 18 ASN 19 19 GLY 20 20 LEU 21 21 ALA 22 22 GLU 23 23 VAL 24 24 GLY 25 25 LYS 26 26 LYS 27 27 PHE 28 28 GLU 29 29 LYS 30 30 ASP 31 31 THR 32 32 GLY 33 33 ILE 34 34 LYS 35 35 VAL 36 36 THR 37 37 VAL 38 38 GLU 39 39 HIS 40 40 PRO 41 41 ASP 42 42 LYS 43 43 LEU 44 44 GLU 45 45 GLU 46 46 LYS 47 47 PHE 48 48 PRO 49 49 GLN 50 50 VAL 51 51 ALA 52 52 ALA 53 53 THR 54 54 GLY 55 55 ASP 56 56 GLY 57 57 PRO 58 58 ASP 59 59 ILE 60 60 ILE 61 61 PHE 62 62 TRP 63 63 ALA 64 64 HIS 65 65 ASP 66 66 ARG 67 67 PHE 68 68 GLY 69 69 GLY 70 70 TYR 71 71 ALA 72 72 GLN 73 73 SER 74 74 GLY 75 75 LEU 76 76 LEU 77 77 ALA 78 78 GLU 79 79 ILE 80 80 THR 81 81 PRO 82 82 ASP 83 83 LYS 84 84 ALA 85 85 PHE 86 86 GLN 87 87 ASP 88 88 LYS 89 89 LEU 90 90 TYR 91 91 PRO 92 92 PHE 93 93 THR 94 94 TRP 95 95 ASP 96 96 ALA 97 97 VAL 98 98 ARG 99 99 TYR 100 100 ASN 101 101 GLY 102 102 LYS 103 103 LEU 104 104 ILE 105 105 ALA 106 106 TYR 107 107 PRO 108 108 ILE 109 109 ALA 110 110 VAL 111 111 GLU 112 112 ALA 113 113 LEU 114 114 SER 115 115 LEU 116 116 ILE 117 117 TYR 118 118 ASN 119 119 LYS 120 120 ASP 121 121 LEU 122 122 LEU 123 123 PRO 124 124 ASN 125 125 PRO 126 126 PRO 127 127 LYS 128 128 THR 129 129 TRP 130 130 GLU 131 131 GLU 132 132 ILE 133 133 PRO 134 134 ALA 135 135 LEU 136 136 ASP 137 137 LYS 138 138 GLU 139 139 LEU 140 140 LYS 141 141 ALA 142 142 LYS 143 143 GLY 144 144 LYS 145 145 SER 146 146 ALA 147 147 LEU 148 148 MET 149 149 PHE 150 150 ASN 151 151 LEU 152 152 GLN 153 153 GLU 154 154 PRO 155 155 TYR 156 156 PHE 157 157 THR 158 158 TRP 159 159 PRO 160 160 LEU 161 161 ILE 162 162 ALA 163 163 ALA 164 164 ASP 165 165 GLY 166 166 GLY 167 167 TYR 168 168 ALA 169 169 PHE 170 170 LYS 171 171 TYR 172 172 GLU 173 173 ASN 174 174 GLY 175 175 LYS 176 176 TYR 177 177 ASP 178 178 ILE 179 179 LYS 180 180 ASP 181 181 VAL 182 182 GLY 183 183 VAL 184 184 ASP 185 185 ASN 186 186 ALA 187 187 GLY 188 188 ALA 189 189 LYS 190 190 ALA 191 191 GLY 192 192 LEU 193 193 THR 194 194 PHE 195 195 LEU 196 196 VAL 197 197 ASP 198 198 LEU 199 199 ILE 200 200 LYS 201 201 ASN 202 202 LYS 203 203 HIS 204 204 MET 205 205 ASN 206 206 ALA 207 207 ASP 208 208 THR 209 209 ASP 210 210 TYR 211 211 SER 212 212 ILE 213 213 ALA 214 214 GLU 215 215 ALA 216 216 ALA 217 217 PHE 218 218 ASN 219 219 LYS 220 220 GLY 221 221 GLU 222 222 THR 223 223 ALA 224 224 MET 225 225 THR 226 226 ILE 227 227 ASN 228 228 GLY 229 229 PRO 230 230 TRP 231 231 ALA 232 232 TRP 233 233 SER 234 234 ASN 235 235 ILE 236 236 ASP 237 237 THR 238 238 SER 239 239 LYS 240 240 VAL 241 241 ASN 242 242 TYR 243 243 GLY 244 244 VAL 245 245 THR 246 246 VAL 247 247 LEU 248 248 PRO 249 249 THR 250 250 PHE 251 251 LYS 252 252 GLY 253 253 GLN 254 254 PRO 255 255 SER 256 256 LYS 257 257 PRO 258 258 PHE 259 259 VAL 260 260 GLY 261 261 VAL 262 262 LEU 263 263 SER 264 264 ALA 265 265 GLY 266 266 ILE 267 267 ASN 268 268 ALA 269 269 ALA 270 270 SER 271 271 PRO 272 272 ASN 273 273 LYS 274 274 GLU 275 275 LEU 276 276 ALA 277 277 LYS 278 278 GLU 279 279 PHE 280 280 LEU 281 281 GLU 282 282 ASN 283 283 TYR 284 284 LEU 285 285 LEU 286 286 THR 287 287 ASP 288 288 GLU 289 289 GLY 290 290 LEU 291 291 GLU 292 292 ALA 293 293 VAL 294 294 ASN 295 295 LYS 296 296 ASP 297 297 LYS 298 298 PRO 299 299 LEU 300 300 GLY 301 301 ALA 302 302 VAL 303 303 ALA 304 304 LEU 305 305 LYS 306 306 SER 307 307 TYR 308 308 GLU 309 309 GLU 310 310 GLU 311 311 LEU 312 312 ALA 313 313 LYS 314 314 ASP 315 315 PRO 316 316 ARG 317 317 ILE 318 318 ALA 319 319 ALA 320 320 THR 321 321 MET 322 322 GLU 323 323 ASN 324 324 ALA 325 325 GLN 326 326 LYS 327 327 GLY 328 328 GLU 329 329 ILE 330 330 MET 331 331 PRO 332 332 ASN 333 333 ILE 334 334 PRO 335 335 GLN 336 336 MET 337 337 SER 338 338 ALA 339 339 PHE 340 340 TRP 341 341 TYR 342 342 ALA 343 343 VAL 344 344 ARG 345 345 THR 346 346 ALA 347 347 VAL 348 348 ILE 349 349 ASN 350 350 ALA 351 351 ALA 352 352 SER 353 353 GLY 354 354 ARG 355 355 GLN 356 356 THR 357 357 VAL 358 358 ASP 359 359 GLU 360 360 ALA 361 361 LEU 362 362 LYS 363 363 ASP 364 364 ALA 365 365 GLN 366 366 THR 367 367 ARG 368 368 ILE 369 369 THR 370 370 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 25237 ER690 100.00 370 99.46 99.46 0.00e+00 BMRB 4354 MBP 100.00 370 100.00 100.00 0.00e+00 BMRB 4986 MBP 100.00 370 100.00 100.00 0.00e+00 BMRB 4987 "maltodextrin-binding protein" 100.00 370 100.00 100.00 0.00e+00 BMRB 6807 MBP 100.00 370 99.73 99.73 0.00e+00 PDB 1A7L "Dominant B-Cell Epitope From The Pres2 Region Of Hepatitis B Virus In The Form Of An Inserted Peptide Segment In Maltodextrin-B" 98.65 389 99.18 99.18 0.00e+00 PDB 1ANF "Maltodextrin Binding Protein With Bound Maltose" 100.00 370 99.73 99.73 0.00e+00 PDB 1DMB "Refined 1.8 Angstroms Structure Reveals The Mechanism Of Binding Of A Cyclic Sugar, Beta-Cyclodextrin, To The Maltodextrin Bind" 100.00 370 99.73 99.73 0.00e+00 PDB 1EZ9 "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P1 Crystal Form" 100.00 370 99.73 99.73 0.00e+00 PDB 1EZO "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 100.00 100.00 0.00e+00 PDB 1EZP "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin Using Peptide Orientations From Dipolar Couplings" 100.00 370 100.00 100.00 0.00e+00 PDB 1FQA "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQB "Structure Of Maltotriotol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQC "Crystal Structure Of Maltotriotol Bound To Closed-Form Maltodextrin Binding Protein" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQD "Crystal Structure Of Maltotetraitol Bound To Closed-Form Maltodextrin Binding Protein" 99.46 370 100.00 100.00 0.00e+00 PDB 1HSJ "Sarr Mbp Fusion Structure" 98.92 487 99.18 99.18 0.00e+00 PDB 1JVX "Maltodextrin-Binding Protein Variant D207cA301GSP316C Cross-Linked In Crystal" 100.27 372 98.65 98.92 0.00e+00 PDB 1JVY "Maltodextrin-Binding Protein Variant D207cA301GSP316C With Beta-Mercaptoethanol Mixed Disulfides" 100.27 372 98.65 98.92 0.00e+00 PDB 1JW4 "Structure Of Ligand-Free Maltodextrin-Binding Protein" 100.00 370 99.73 99.73 0.00e+00 PDB 1JW5 "Structure Of Maltose Bound To Open-Form Maltodextrin- Binding Protein In P1 Crystal" 100.00 370 99.73 99.73 0.00e+00 PDB 1LAX "Crystal Structure Of Male31, A Defective Folding Mutant Of Maltose-Binding Protein" 100.00 370 99.19 99.19 0.00e+00 PDB 1LLS "Crystal Structure Of Unliganded Maltose Binding Protein With Xenon" 100.00 370 99.73 99.73 0.00e+00 PDB 1MDP "Refined Structures Of Two Insertion(Slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.00 363 97.30 97.30 0.00e+00 PDB 1MDQ "Refined Structures Of Two Insertion(slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.27 371 99.19 99.46 0.00e+00 PDB 1MG1 "Htlv-1 Gp21 EctodomainMALTOSE-Binding Protein Chimera" 97.84 450 99.17 99.17 0.00e+00 PDB 1MH3 "Maltose Binding-A1 Homeodomain Protein Chimera, Crystal Form I" 98.92 421 98.91 98.91 0.00e+00 PDB 1MH4 "Maltose Binding-A1 Homeodomain Protein Chimera, Crystal Form Ii" 98.92 421 98.91 98.91 0.00e+00 PDB 1MPB "Maltodextrin-Binding Protein (Maltose-Binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (Trp-230-Arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1MPC "Maltodextrin-binding Protein (maltose-binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (trp-230-arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1MPD "Maltodextrin-Binding Protein (Maltose-Binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (Trp-230-Arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1N3W "Engineered High-affinity Maltose-binding Protein" 100.00 366 98.38 98.38 0.00e+00 PDB 1N3X "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 98.38 98.38 0.00e+00 PDB 1NL5 "Engineered High-affinity Maltose-binding Protein" 100.00 366 97.84 97.84 0.00e+00 PDB 1NMU Mbp-L30 98.92 382 99.73 99.73 0.00e+00 PDB 1OMP "Crystallographic Evidence Of A Large Ligand-Induced Hinge- Twist Motion Between The Two Domains Of The Maltodextrin- Binding Pr" 100.00 370 99.73 99.73 0.00e+00 PDB 1PEB "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 97.84 97.84 0.00e+00 PDB 1R6Z "The Crystal Structure Of The Argonaute2 Paz Domain (as A Mbp Fusion)" 98.92 509 99.73 99.73 0.00e+00 PDB 1SVX "Crystal Structure Of A Designed Selected Ankyrin Repeat Protein In Complex With The Maltose Binding Protein" 98.92 395 100.00 100.00 0.00e+00 PDB 1T0K "Joint X-ray And Nmr Refinement Of Yeast L30e-mrna Complex" 98.92 381 99.73 99.73 0.00e+00 PDB 1Y4C "Designed Helical Protein Fusion Mbp" 98.92 494 99.73 99.73 0.00e+00 PDB 1YTV "Maltose-binding Protein Fusion To A C-terminal Fragment Of The V1a Vasopressin Receptor" 98.92 366 99.73 99.73 0.00e+00 PDB 1ZIU "Crystal Structure Of Nickel-bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZJL "Crystal Structure Of Zinc-Bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZKB "Zinc-Free Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZMG "Crystal Structure Of Copper-Bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 2D21 "Nmr Structure Of Stereo-Array Isotope Labelled (Sail) Maltodextrin-Binding Protein (Mbp)" 100.00 370 99.73 99.73 0.00e+00 PDB 2H25 "Solution Structure Of Maltose Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 100.00 100.00 0.00e+00 PDB 2KLF "Pere Nmr Structure Of Maltodextrin-Binding Protein" 100.00 370 100.00 100.00 0.00e+00 PDB 2MV0 "Solution Nmr Structure Of Maltose-binding Protein From Escherichia Coli, Northeast Structural Genomics Consortium (nesg) Target" 100.00 370 99.73 99.73 0.00e+00 PDB 2NVU "Structure Of Appbp1-Uba3~nedd8-Nedd8-Mgatp-Ubc12(C111a), A Trapped Ubiquitin-Like Protein Activation Complex" 98.92 805 98.91 98.91 0.00e+00 PDB 2OBG "Crystal Structure Of Monobody Mbp-74MALTOSE BINDING PROTEIN FUSION Complex" 98.92 461 100.00 100.00 0.00e+00 PDB 2OK2 "Muts C-Terminal Domain Fused To Maltose Binding Protein" 98.92 402 99.45 99.73 0.00e+00 PDB 2R6G "The Crystal Structure Of The E. Coli Maltose Transporter" 100.00 370 99.73 99.73 0.00e+00 PDB 2V93 "Equillibrium Mixture Of Open And Partially-Closed Species In The Apo State Of Maltodextrin-Binding Protein By Paramagnetic Rela" 100.00 370 99.19 99.19 0.00e+00 PDB 2VGQ "Crystal Structure Of Human Ips-1 Card" 98.92 477 99.73 99.73 0.00e+00 PDB 2XZ3 "Blv Tm Hairpin" 98.92 463 98.91 98.91 0.00e+00 PDB 2ZXT "Crystal Structure Of Tim40/mia40, A Disulfide Relay System In Mitochondria, Solved As Mbp Fusion Protein" 98.92 465 99.73 99.73 0.00e+00 PDB 3A3C "Crystal Structure Of Tim40/mia40 Fusing Mbp, C296s And C298s Mutant" 98.38 451 100.00 100.00 0.00e+00 PDB 3C4M "Structure Of Human Parathyroid Hormone In Complex With The Extracellular Domain Of Its G-Protein-Coupled Receptor (Pth1r)" 98.92 539 99.73 99.73 0.00e+00 PDB 3CSB "Crystal Structure Of Monobody Ysx1MALTOSE BINDING PROTEIN Fusion Complex" 98.92 465 100.00 100.00 0.00e+00 PDB 3CSG "Crystal Structure Of Monobody Ys1(Mbp-74)MALTOSE BINDING Protein Fusion Complex" 98.92 461 100.00 100.00 0.00e+00 PDB 3D4C "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form I)" 98.92 481 99.18 99.18 0.00e+00 PDB 3D4G "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Ii)" 98.92 481 99.18 99.18 0.00e+00 PDB 3DM0 "Maltose Binding Protein Fusion With Rack1 From A. Thaliana" 98.92 694 98.09 98.09 0.00e+00 PDB 3EF7 "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Iii)" 98.92 481 99.18 99.18 0.00e+00 PDB 3EHS "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (Crfr1)" 98.92 476 99.73 99.73 0.00e+00 PDB 3EHT "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (crfr1) In Complex With C" 98.92 476 99.45 99.45 0.00e+00 PDB 3EHU "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (crfr1) In Complex With C" 98.92 476 99.45 99.45 0.00e+00 PDB 3F5F "Crystal Structure Of Heparan Sulfate 2-O-Sulfotransferase From Gallus Gallus As A Maltose Binding Protein Fusion" 98.92 658 98.91 98.91 0.00e+00 PDB 3G7V "Islet Amyloid Polypeptide (iapp Or Amylin) Fused To Maltose Binding Protein" 99.19 408 98.64 98.64 0.00e+00 PDB 3G7W "Islet Amyloid Polypeptide (Iapp Or Amylin) Residues 1 To 22 Fused To Maltose Binding Protein" 98.92 393 98.91 98.91 0.00e+00 PDB 3H3G "Crystal Structure Of The Extracellular Domain Of The Human Parathyroid Hormone Receptor (Pth1r) In Complex With Parathyroid Hor" 98.92 539 99.73 99.73 0.00e+00 PDB 3H4Z "Crystal Structure Of An Mbp-Der P 7 Fusion Protein" 98.92 568 97.54 97.54 0.00e+00 PDB 3HPI "Crystal Structure Of Maltose-Binding Protein Mutant With Bound Sucrose" 100.00 372 98.65 98.92 0.00e+00 PDB 3HST "N-Terminal Rnase H Domain Of Rv2228c From Mycobacterium Tuberculosis As A Fusion Protein With Maltose Binding Protein" 99.19 387 99.46 99.46 0.00e+00 PDB 3IO4 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C90" 98.92 449 98.91 98.91 0.00e+00 PDB 3IO6 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-A" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOR "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C95" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOT "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-B" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOU "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C94" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOV "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C99" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOW "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C99-Hg" 98.92 449 98.91 98.91 0.00e+00 PDB 3KJT "Stimulation Of The Maltose Transporter By A Mutant Sucrose B Protein Gives Insights Into Abc Transporter Coupling" 100.00 372 98.65 98.92 0.00e+00 PDB 3L2J "Dimeric Structure Of The Ligand-Free Extracellular Domain Of Parathyroid Hormone Receptor (Pth1r)" 98.38 535 100.00 100.00 0.00e+00 PDB 3LBS "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Bound Form)" 98.38 384 99.45 100.00 0.00e+00 PDB 3LC8 "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Free Form)" 98.38 384 99.45 100.00 0.00e+00 PDB 3MBP "Maltodextrin-Binding Protein With Bound Maltotriose" 100.00 370 99.73 99.73 0.00e+00 PDB 3MP1 "Complex Structure Of Sgf29 And Trimethylated H3k4" 98.92 522 99.18 99.18 0.00e+00 PDB 3MP6 "Complex Structure Of Sgf29 And Dimethylated H3k4" 98.92 522 99.18 99.18 0.00e+00 PDB 3MP8 "Crystal Structure Of Sgf29 Tudor Domain" 98.92 522 99.18 99.18 0.00e+00 PDB 3MQ9 "Crystal Structure Of Ectodomain Mutant Of Bst-2TETHERINCD317 FUSED To Mbp" 99.73 471 99.73 99.73 0.00e+00 PDB 3N93 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 3" 98.92 482 99.73 99.73 0.00e+00 PDB 3N94 "Crystal Structure Of Human Pituitary Adenylate Cyclase 1 Receptor- Short N-Terminal Extracellular Domain" 98.92 475 99.73 99.73 0.00e+00 PDB 3N95 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 2" 98.92 482 99.73 99.73 0.00e+00 PDB 3N96 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 1" 98.92 482 99.73 99.73 0.00e+00 PDB 3O3U "Crystal Structure Of Human Receptor For Advanced Glycation Endproducts (Rage)" 98.38 581 99.18 99.18 0.00e+00 PDB 3OAI "Crystal Structure Of The Extra-Cellular Domain Of Human Myelin Protein Zero" 99.19 507 99.46 99.46 0.00e+00 PDB 3OB4 "Mbp-Fusion Protein Of The Major Peanut Allergen Ara H 2" 98.92 500 97.54 97.54 0.00e+00 PDB 3PGF "Crystal Structure Of Maltose Bound Mbp With A Conformationally Specific Synthetic Antigen Binder (Sab)" 99.19 398 99.46 99.46 0.00e+00 PDB 3PUV "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Vo4" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUW "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Alf4" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUX "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Bef3" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUY "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Amp-Pnp After Crystal Soaking Of The Pretranslo" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUZ "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Bound To Amp-Pnp" 100.00 370 99.19 99.19 0.00e+00 PDB 3PV0 "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Without Nucleotide" 100.00 370 99.19 99.19 0.00e+00 PDB 3PY7 "Crystal Structure Of Full-length Bovine Papillomavirus Oncoprotein E6 In Complex With Ld1 Motif Of Paxillin At 2.3a Resolution" 98.92 523 98.09 98.09 0.00e+00 PDB 3Q25 "Crystal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 99.73 99.73 0.00e+00 PDB 3Q26 "Cyrstal Structure Of Human Alpha-Synuclein (10-42) Fused To Maltose Binding Protein (Mbp)" 98.92 404 99.73 99.73 0.00e+00 PDB 3Q27 "Cyrstal Structure Of Human Alpha-Synuclein (32-57) Fused To Maltose Binding Protein (Mbp)" 98.92 397 99.73 99.73 0.00e+00 PDB 3Q28 "Cyrstal Structure Of Human Alpha-Synuclein (58-79) Fused To Maltose Binding Protein (Mbp)" 99.19 393 99.46 99.46 0.00e+00 PDB 3Q29 "Cyrstal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 99.73 99.73 0.00e+00 PDB 3RLF "Crystal Structure Of The Maltose-Binding ProteinMALTOSE TRANSPORTER Complex In An Outward-Facing Conformation Bound To Mgamppnp" 100.00 380 99.73 99.73 0.00e+00 PDB 3RUM "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" 98.92 378 99.73 99.73 0.00e+00 PDB 3SER "Zn-Mediated Polymer Of Maltose-Binding Protein K26hK30H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SES "Cu-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SET "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form I)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEU "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Iii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEV "Zn-Mediated Trimer Of Maltose-Binding Protein E310hK314H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEW "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form I)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEX "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form Ii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEY "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Ii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3VD8 "Crystal Structure Of Human Aim2 Pyd Domain With Mbp Fusion" 98.92 489 97.54 97.54 0.00e+00 PDB 3VFJ "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Mbp As A Ligand Carrier" 98.92 378 99.73 99.73 0.00e+00 PDB 3W15 "Structure Of Peroxisomal Targeting Signal 2 (pts2) Of Saccharomyces Cerevisiae 3-ketoacyl-coa Thiolase In Complex With Pex7p An" 100.00 389 99.73 99.73 0.00e+00 PDB 3WAI "Crystal Structure Of The C-terminal Globular Domain Of Oligosaccharyltransferase (afaglb-l, O29867_arcfu) From Archaeoglobus Fu" 98.92 739 99.73 99.73 0.00e+00 PDB 4B3N "Crystal Structure Of Rhesus Trim5alpha PrySPRY DOMAIN" 100.00 602 99.19 99.73 0.00e+00 PDB 4BL8 "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu)" 98.92 831 99.18 99.18 0.00e+00 PDB 4BL9 "Crystal Structure Of Full-length Human Suppressor Of Fused ( Sufu) Mutant Lacking A Regulatory Subdomain (crystal Form I)" 98.92 756 99.18 99.18 0.00e+00 PDB 4BLA "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu) Mutant Lacking A Regulatory Subdomain (crystal Form Ii)" 98.92 756 99.18 99.18 0.00e+00 PDB 4BLB "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli1p Complex" 98.92 753 98.63 98.63 0.00e+00 PDB 4BLD "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli3p Complex" 98.92 753 98.63 98.63 0.00e+00 PDB 4EDQ "Mbp-fusion Protein Of Myosin-binding Protein C Residues 149-269" 98.92 492 98.91 98.91 0.00e+00 PDB 4EGC "Crystal Structure Of Mbp-fused Human Six1 Bound To Human Eya2 Eya Domain" 98.92 559 98.36 98.36 0.00e+00 PDB 4EXK "A Chimera Protein Containing Mbp Fused To The C-Terminal Domain Of The Uncharacterized Protein Stm14_2015 From Salmonella Enter" 98.92 487 97.54 97.54 0.00e+00 PDB 4FE8 "Crystal Structure Of Htt36q3h-ex1-x1-c1(alpha)" 98.92 452 98.91 98.91 0.00e+00 PDB 4FEB "Crystal Structure Of Htt36q3h-ex1-x1-c2(beta)" 98.92 452 98.91 98.91 0.00e+00 PDB 4FEC "Crystal Structure Of Htt36q3h" 98.92 452 98.91 98.91 0.00e+00 PDB 4FED "Crystal Structure Of Htt36q3h" 98.92 452 98.91 98.91 0.00e+00 PDB 4GIZ "Crystal Structure Of Full-length Human Papillomavirus Oncoprotein E6 In Complex With Lxxll Peptide Of Ubiquitin Ligase E6ap At " 98.92 382 98.09 98.09 0.00e+00 PDB 4GLI "Crystal Structure Of Human Smn Yg-Dimer" 99.73 401 99.73 99.73 0.00e+00 PDB 4H1G "Structure Of Candida Albicans Kar3 Motor Domain Fused To Maltose- Binding Protein" 98.92 715 98.91 98.91 0.00e+00 PDB 4IFP "X-ray Crystal Structure Of Human Nlrp1 Card Domain" 98.92 466 97.54 97.54 0.00e+00 PDB 4JBZ "Structure Of Mcm10 Coiled-coil Region" 98.92 403 97.54 97.54 0.00e+00 PDB 4JKM "Crystal Structure Of Clostridium Perfringens Beta-glucuronidase" 99.19 400 99.18 99.18 0.00e+00 PDB 4KEG "Crystal Structure Of Mbp Fused Human Splunc1" 98.92 584 99.18 99.18 0.00e+00 PDB 4KHZ "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Pre-translocation Conformation Bound To Malt" 100.00 380 99.73 99.73 0.00e+00 PDB 4KI0 "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Outward-facing Conformation Bound To Maltohe" 100.00 380 99.73 99.73 0.00e+00 PDB 4KV3 "Ubiquitin-like Domain Of The Mycobacterium Tuberculosis Type Vii Secretion System Protein Eccd1 As Maltose-binding Protein Fusi" 98.92 461 98.91 98.91 0.00e+00 PDB 4KYC "Structure Of The C-terminal Domain Of The Menangle Virus Phosphoprotein, Fused To Mbp" 98.92 420 98.36 98.36 0.00e+00 PDB 4KYD "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp." 98.92 420 98.36 98.36 0.00e+00 PDB 4KYE "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp" 98.92 420 98.36 98.36 0.00e+00 PDB 4LOG "The Crystal Structure Of The Orphan Nuclear Receptor Pnr Ligand Binding Domain Fused With Mbp" 98.92 574 99.73 99.73 0.00e+00 PDB 4MBP "Maltodextrin Binding Protein With Bound Maltetrose" 100.00 370 99.73 99.73 0.00e+00 PDB 4MY2 "Crystal Structure Of Norrin In Fusion With Maltose Binding Protein" 98.92 477 99.73 99.73 0.00e+00 PDB 4N4X "Crystal Structure Of The Mbp Fused Human Splunc1 (native Form)" 98.92 584 99.18 99.18 0.00e+00 PDB 4NDZ "Structure Of Maltose Binding Protein Fusion To 2-o-sulfotransferase With Bound Heptasaccharide And Pap" 98.92 658 98.91 98.91 0.00e+00 PDB 4NUF "Crystal Structure Of Shp/eid1" 98.92 580 99.73 99.73 0.00e+00 PDB 4O4B "Crystal Structure Of An Inositol Hexakisphosphate Kinase Ehip6ka As A Fusion Protein With Maltose Binding Protein" 98.92 396 99.73 99.73 0.00e+00 PDB 4OGM "Mbp-fusion Protein Of Pila1 Residues 26-159" 99.19 520 97.28 97.28 0.00e+00 PDB 4OZQ "Crystal Structure Of The Mouse Kif14 Motor Domain" 98.92 720 98.91 98.91 0.00e+00 PDB 4PE2 "Mbp Pila1 Cd160" 99.19 516 99.46 99.46 0.00e+00 PDB 4PQK "C-terminal Domain Of Dna Binding Protein" 99.19 487 99.46 99.46 0.00e+00 PDB 4QVH "Crystal Structure Of The Essential Mycobacterium Tuberculosis Phosphopantetheinyl Transferase Pptt, Solved As A Fusion Protein " 98.92 598 98.36 98.36 0.00e+00 PDB 4R0Y "Structure Of Maltose-binding Protein Fusion With The C-terminal Gh1 Domain Of Guanylate Kinase-associated Protein From Rattus N" 97.57 501 99.72 99.72 0.00e+00 PDB 4TSM "Mbp-fusion Protein Of Pila1 From C. Difficile R20291 Residues 26-166" 99.19 520 97.28 97.28 0.00e+00 PDB 4WGI "A Single Diastereomer Of A Macrolactam Core Binds Specifically To Myeloid Cell Leukemia 1 (mcl1)" 98.92 518 99.73 99.73 0.00e+00 PDB 4WJV "Crystal Structure Of Rsa4 In Complex With The Nsa2 Binding Peptide" 99.19 381 97.82 97.82 0.00e+00 DBJ BAB38440 "periplasmic maltose-binding protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAE78036 "maltose transporter subunit [Escherichia coli str. K-12 substr. W3110]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAG79849 "maltose ABC transporter substrate binding component [Escherichia coli SE11]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAI28296 "periplasmic maltose-binding protein MalE [Escherichia coli O26:H11 str. 11368]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAI33473 "periplasmic maltose-binding protein MalE [Escherichia coli O103:H2 str. 12009]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAP78494 "Maltose-binding periplasmic protein [Escherichia coli LF82]" 100.00 396 98.65 99.46 0.00e+00 EMBL CAQ34383 "malE, subunit of maltose ABC transporter [Escherichia coli BL21(DE3)]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAR01012 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli IAI1]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAR05669 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli S88]" 100.00 396 98.65 99.46 0.00e+00 EMBL CAR10711 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli ED1a]" 100.00 396 98.65 99.46 0.00e+00 GB AAB59056 "periplasmic maltose-binding protein [Escherichia coli]" 100.00 396 99.73 99.73 0.00e+00 GB AAB86559 "maltose binding protein-lacZ alpha peptide fusion protein precursor [Shuttle vector pMAL-pIII]" 98.92 482 99.73 99.73 0.00e+00 GB AAB87675 "maltose binding protein-lacZ-alpha fusion protein [Expression vector pMal-X]" 98.38 496 100.00 100.00 0.00e+00 GB AAC43128 "periplasmic maltose-binding protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 GB AAC77004 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 REF NP_290668 "maltose ABC transporter substrate-binding protein [Escherichia coli O157:H7 str. EDL933]" 100.00 396 99.73 99.73 0.00e+00 REF NP_313044 "maltose ABC transporter periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 99.73 99.73 0.00e+00 REF NP_418458 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 REF NP_709885 "maltose ABC transporter substrate-binding protein [Shigella flexneri 2a str. 301]" 100.00 396 99.46 99.46 0.00e+00 REF NP_756856 "maltose ABC transporter periplasmic protein [Escherichia coli CFT073]" 100.00 396 98.65 99.46 0.00e+00 SP P0AEX9 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 99.73 99.73 0.00e+00 SP P0AEY0 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 99.73 99.73 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 $MBP 'E. coli' 562 Bacteria . Escherichia coli 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 $MBP 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MBP 1.2 mM . $BCD . mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address UCSF . . stop_ loop_ _Task 'peak assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model . _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_4D-15N,13C-edited_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '4D-15N,13C-edited NOESY' _Sample_label $sample_1 save_ save_3D-CCH-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-CCH-TOCSY _Sample_label $sample_1 save_ save_TROSY-HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label $sample_1 save_ save_4D-13C,13C-edited_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '4D-13C,13C-edited NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7 0.2 pH temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label H2O H 1 protons ppm 4.724 internal direct . . . 1.0 $entry_citation $entry_citation 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '4D-15N,13C-edited NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name MBP _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 LYS HA H 4.46 0.02 1 2 1 1 LYS HB2 H 1.84 0.02 2 3 1 1 LYS HB3 H 1.78 0.02 2 4 1 1 LYS HG2 H 1.43 0.02 1 5 1 1 LYS HG3 H 1.43 0.02 1 6 1 1 LYS HD2 H 1.68 0.02 1 7 1 1 LYS HD3 H 1.68 0.02 1 8 1 1 LYS HE2 H 2.99 0.02 1 9 1 1 LYS HE3 H 2.99 0.02 1 10 1 1 LYS C C 176.47 0.20 1 11 1 1 LYS CA C 56.31 0.10 1 12 1 1 LYS CB C 33.34 0.10 1 13 1 1 LYS CG C 24.63 0.10 1 14 1 1 LYS CD C 29.03 0.10 1 15 1 1 LYS CE C 42.11 0.10 1 16 2 2 THR H H 8.23 0.02 1 17 2 2 THR HA H 4.25 0.02 1 18 2 2 THR HB H 4.11 0.02 1 19 2 2 THR HG2 H 1.16 0.02 1 20 2 2 THR C C 174.34 0.20 1 21 2 2 THR CA C 62.15 0.10 1 22 2 2 THR CB C 69.75 0.10 1 23 2 2 THR CG2 C 21.94 0.10 1 24 2 2 THR N N 116.33 0.10 1 25 3 3 GLU H H 8.58 0.02 1 26 3 3 GLU HA H 4.36 0.02 1 27 3 3 GLU HB2 H 1.89 0.02 2 28 3 3 GLU HB3 H 2.01 0.02 2 29 3 3 GLU HG2 H 2.22 0.02 1 30 3 3 GLU HG3 H 2.22 0.02 1 31 3 3 GLU C C 176.04 0.20 1 32 3 3 GLU CA C 56.13 0.10 1 33 3 3 GLU CB C 31.48 0.10 1 34 3 3 GLU CG C 36.31 0.10 1 35 3 3 GLU N N 122.69 0.10 1 36 4 4 GLU H H 8.56 0.02 1 37 4 4 GLU HA H 4.36 0.02 1 38 4 4 GLU HB2 H 1.95 0.02 2 39 4 4 GLU HB3 H 2.03 0.02 2 40 4 4 GLU HG2 H 2.24 0.02 1 41 4 4 GLU HG3 H 2.24 0.02 1 42 4 4 GLU C C 176.97 0.20 1 43 4 4 GLU CA C 56.82 0.10 1 44 4 4 GLU CB C 30.46 0.10 1 45 4 4 GLU CG C 36.51 0.10 1 46 4 4 GLU N N 122.59 0.10 1 47 5 5 GLY H H 8.67 0.02 1 48 5 5 GLY HA2 H 3.86 0.02 2 49 5 5 GLY HA3 H 3.93 0.02 2 50 5 5 GLY C C 172.21 0.20 1 51 5 5 GLY CA C 45.79 0.10 1 52 5 5 GLY N N 110.60 0.10 1 53 6 6 LYS H H 7.70 0.02 1 54 6 6 LYS HA H 4.93 0.02 1 55 6 6 LYS HB2 H 1.69 0.03 2 56 6 6 LYS HB3 H 1.61 0.02 2 57 6 6 LYS HG2 H 1.21 0.02 1 58 6 6 LYS HG3 H 1.21 0.02 1 59 6 6 LYS HD2 H 1.53 0.02 1 60 6 6 LYS HD3 H 1.53 0.02 1 61 6 6 LYS HE2 H 2.86 0.02 1 62 6 6 LYS HE3 H 2.86 0.02 1 63 6 6 LYS C C 173.48 0.20 1 64 6 6 LYS CA C 54.93 0.10 1 65 6 6 LYS CB C 35.59 0.10 1 66 6 6 LYS CG C 23.77 0.10 1 67 6 6 LYS CD C 29.51 0.10 1 68 6 6 LYS CE C 42.24 0.10 1 69 6 6 LYS N N 118.99 0.10 1 70 7 7 LEU H H 8.36 0.02 1 71 7 7 LEU HA H 4.84 0.02 1 72 7 7 LEU HB2 H 0.96 0.02 2 73 7 7 LEU HB3 H 1.35 0.02 2 74 7 7 LEU HG H 1.23 0.02 1 75 7 7 LEU HD1 H 0.34 0.02 1 76 7 7 LEU HD2 H 0.56 0.02 1 77 7 7 LEU C C 175.36 0.20 1 78 7 7 LEU CA C 53.31 0.10 1 79 7 7 LEU CB C 46.88 0.10 1 80 7 7 LEU CG C 26.57 0.10 1 81 7 7 LEU CD1 C 25.39 0.10 1 82 7 7 LEU CD2 C 24.56 0.10 1 83 7 7 LEU N N 118.11 0.10 1 84 8 8 VAL H H 10.02 0.02 1 85 8 8 VAL HA H 4.80 0.02 1 86 8 8 VAL HB H 1.82 0.02 1 87 8 8 VAL HG1 H 0.89 0.02 1 88 8 8 VAL HG2 H 0.93 0.02 1 89 8 8 VAL C C 175.90 0.20 1 90 8 8 VAL CA C 61.76 0.10 1 91 8 8 VAL CB C 33.98 0.10 1 92 8 8 VAL CG1 C 21.18 0.10 1 93 8 8 VAL CG2 C 21.46 0.10 1 94 8 8 VAL N N 125.39 0.10 1 95 9 9 ILE H H 9.13 0.02 1 96 9 9 ILE HA H 5.02 0.02 1 97 9 9 ILE HB H 1.76 0.02 1 98 9 9 ILE HG12 H 0.88 0.02 2 99 9 9 ILE HG13 H 1.42 0.02 2 100 9 9 ILE HG2 H 1.03 0.02 1 101 9 9 ILE HD1 H 0.34 0.02 1 102 9 9 ILE C C 174.65 0.20 1 103 9 9 ILE CA C 59.97 0.10 1 104 9 9 ILE CB C 41.43 0.10 1 105 9 9 ILE CG1 C 27.62 0.10 1 106 9 9 ILE CG2 C 18.97 0.10 1 107 9 9 ILE CD1 C 14.89 0.10 1 108 9 9 ILE N N 128.32 0.10 1 109 10 10 TRP H H 9.04 0.02 1 110 10 10 TRP HA H 6.15 0.02 1 111 10 10 TRP HB2 H 3.29 0.02 2 112 10 10 TRP HB3 H 3.27 0.02 2 113 10 10 TRP HD1 H 7.21 0.02 1 114 10 10 TRP HE1 H 10.62 0.02 1 115 10 10 TRP HE3 H 8.33 0.02 1 116 10 10 TRP HZ2 H 7.56 0.02 1 117 10 10 TRP HH2 H 7.07 0.02 1 118 10 10 TRP C C 174.05 0.20 1 119 10 10 TRP CA C 54.15 0.10 1 120 10 10 TRP CB C 33.08 0.10 1 121 10 10 TRP CD1 C 124.32 0.10 1 122 10 10 TRP CE3 C 122.10 0.10 1 123 10 10 TRP CZ2 C 115.58 0.10 1 124 10 10 TRP CH2 C 124.59 0.10 1 125 10 10 TRP N N 126.84 0.10 1 126 10 10 TRP NE1 N 129.14 0.10 1 127 11 11 ILE H H 8.72 0.02 1 128 11 11 ILE HA H 4.79 0.02 1 129 11 11 ILE HB H 1.42 0.02 1 130 11 11 ILE HG12 H 1.39 0.02 2 131 11 11 ILE HG13 H 1.76 0.04 2 132 11 11 ILE HG2 H 0.68 0.02 1 133 11 11 ILE HD1 H 0.13 0.02 1 134 11 11 ILE C C 171.01 0.20 1 135 11 11 ILE CA C 59.87 0.10 1 136 11 11 ILE CB C 41.77 0.10 1 137 11 11 ILE CG1 C 28.86 0.10 1 138 11 11 ILE CG2 C 15.10 0.10 1 139 11 11 ILE CD1 C 13.56 0.10 1 140 11 11 ILE N N 122.05 0.10 1 141 12 12 ASN H H 8.89 0.02 1 142 12 12 ASN HA H 4.72 0.02 1 143 12 12 ASN HB2 H 2.72 0.02 2 144 12 12 ASN HB3 H 3.00 0.02 2 145 12 12 ASN HD21 H 7.49 0.02 2 146 12 12 ASN C C 177.40 0.20 1 147 12 12 ASN CA C 54.40 0.10 1 148 12 12 ASN CB C 39.98 0.10 1 149 12 12 ASN N N 122.53 0.10 1 150 12 12 ASN ND2 N 115.28 0.10 1 151 13 13 GLY H H 8.22 0.02 1 152 13 13 GLY HA2 H 3.62 0.02 2 153 13 13 GLY HA3 H 3.90 0.02 2 154 13 13 GLY C C 173.16 0.20 1 155 13 13 GLY CA C 46.51 0.10 1 156 13 13 GLY N N 106.27 0.10 1 157 14 14 ASP H H 7.89 0.02 1 158 14 14 ASP HA H 4.75 0.02 1 159 14 14 ASP HB2 H 2.61 0.02 2 160 14 14 ASP HB3 H 2.96 0.02 2 161 14 14 ASP C C 176.10 0.20 1 162 14 14 ASP CA C 52.97 0.10 1 163 14 14 ASP CB C 39.83 0.10 1 164 14 14 ASP N N 116.55 0.10 1 165 15 15 LYS H H 7.57 0.02 1 166 15 15 LYS HA H 4.52 0.02 1 167 15 15 LYS HB2 H 2.02 0.02 2 168 15 15 LYS HB3 H 1.56 0.02 2 169 15 15 LYS HG2 H 1.41 0.02 2 170 15 15 LYS HD2 H 1.39 0.02 2 171 15 15 LYS HD3 H 1.47 0.02 2 172 15 15 LYS HE2 H 2.98 0.03 2 173 15 15 LYS C C 177.58 0.20 1 174 15 15 LYS CA C 52.88 0.10 1 175 15 15 LYS CB C 33.55 0.10 1 176 15 15 LYS CG C 24.38 0.10 1 177 15 15 LYS CD C 27.70 0.10 1 178 15 15 LYS CE C 42.58 0.10 1 179 15 15 LYS N N 118.55 0.10 1 180 16 16 GLY H H 8.85 0.02 1 181 16 16 GLY HA2 H 3.60 0.02 2 182 16 16 GLY HA3 H 4.17 0.02 2 183 16 16 GLY C C 175.65 0.20 1 184 16 16 GLY CA C 48.23 0.10 1 185 16 16 GLY N N 108.25 0.10 1 186 17 17 TYR H H 8.22 0.02 1 187 17 17 TYR HA H 3.99 0.02 1 188 17 17 TYR HB2 H 2.47 0.02 2 189 17 17 TYR HB3 H 3.01 0.02 2 190 17 17 TYR HD1 H 6.89 0.02 1 191 17 17 TYR HD2 H 6.89 0.02 1 192 17 17 TYR HE1 H 6.82 0.02 1 193 17 17 TYR HE2 H 6.82 0.02 1 194 17 17 TYR C C 177.16 0.20 1 195 17 17 TYR CA C 59.74 0.10 1 196 17 17 TYR CB C 37.94 0.10 1 197 17 17 TYR CD1 C 133.70 0.10 1 198 17 17 TYR CD2 C 133.70 0.10 1 199 17 17 TYR CE1 C 118.37 0.10 1 200 17 17 TYR CE2 C 118.37 0.10 1 201 17 17 TYR N N 120.55 0.10 1 202 18 18 ASN H H 8.08 0.02 1 203 18 18 ASN HA H 4.62 0.02 1 204 18 18 ASN HB2 H 2.55 0.02 2 205 18 18 ASN HB3 H 2.71 0.02 2 206 18 18 ASN HD21 H 7.81 0.02 2 207 18 18 ASN HD22 H 6.70 0.02 2 208 18 18 ASN C C 179.03 0.20 1 209 18 18 ASN CA C 56.17 0.10 1 210 18 18 ASN CB C 37.55 0.10 1 211 18 18 ASN N N 123.69 0.10 1 212 18 18 ASN ND2 N 115.36 0.10 1 213 19 19 GLY H H 8.98 0.02 1 214 19 19 GLY HA2 H 3.85 0.02 1 215 19 19 GLY HA3 H 3.85 0.02 1 216 19 19 GLY C C 175.95 0.20 1 217 19 19 GLY CA C 47.54 0.10 1 218 19 19 GLY N N 111.81 0.10 1 219 20 20 LEU H H 8.33 0.02 1 220 20 20 LEU HA H 4.00 0.02 1 221 20 20 LEU HB2 H 1.32 0.02 2 222 20 20 LEU HB3 H 1.90 0.02 2 223 20 20 LEU HG H 1.56 0.02 1 224 20 20 LEU HD1 H 0.88 0.02 1 225 20 20 LEU HD2 H 0.64 0.02 1 226 20 20 LEU C C 178.68 0.20 1 227 20 20 LEU CA C 57.62 0.10 1 228 20 20 LEU CB C 41.77 0.10 1 229 20 20 LEU CG C 27.03 0.10 1 230 20 20 LEU CD1 C 25.10 0.10 1 231 20 20 LEU CD2 C 27.22 0.10 1 232 20 20 LEU N N 121.70 0.10 1 233 21 21 ALA H H 8.09 0.02 1 234 21 21 ALA HA H 4.05 0.02 1 235 21 21 ALA HB H 1.68 0.02 1 236 21 21 ALA C C 180.59 0.20 1 237 21 21 ALA CA C 55.22 0.10 1 238 21 21 ALA CB C 17.77 0.10 1 239 21 21 ALA N N 121.14 0.10 1 240 22 22 GLU H H 7.80 0.02 1 241 22 22 GLU HA H 4.12 0.02 1 242 22 22 GLU HB2 H 2.27 0.02 2 243 22 22 GLU HB3 H 2.45 0.02 2 244 22 22 GLU HG2 H 2.40 0.02 2 245 22 22 GLU HG3 H 2.43 0.02 2 246 22 22 GLU C C 180.12 0.20 1 247 22 22 GLU CA C 59.77 0.10 1 248 22 22 GLU CB C 28.90 0.10 1 249 22 22 GLU CG C 35.97 0.10 1 250 22 22 GLU N N 120.41 0.10 1 251 23 23 VAL H H 7.82 0.02 1 252 23 23 VAL HA H 3.75 0.02 1 253 23 23 VAL HB H 2.44 0.02 1 254 23 23 VAL HG1 H 0.83 0.02 1 255 23 23 VAL HG2 H 1.27 0.02 1 256 23 23 VAL C C 179.42 0.20 1 257 23 23 VAL CA C 66.87 0.10 1 258 23 23 VAL CB C 31.56 0.10 1 259 23 23 VAL CG1 C 22.62 0.10 1 260 23 23 VAL CG2 C 23.76 0.10 1 261 23 23 VAL N N 123.14 0.10 1 262 24 24 GLY H H 8.69 0.02 1 263 24 24 GLY HA2 H 3.81 0.02 2 264 24 24 GLY HA3 H 3.75 0.02 2 265 24 24 GLY C C 175.13 0.20 1 266 24 24 GLY CA C 47.80 0.10 1 267 24 24 GLY N N 106.67 0.10 1 268 25 25 LYS H H 8.30 0.02 1 269 25 25 LYS HA H 4.23 0.02 1 270 25 25 LYS HB2 H 2.03 0.02 2 271 25 25 LYS HG2 H 1.68 0.02 2 272 25 25 LYS HD2 H 1.75 0.04 2 273 25 25 LYS HE2 H 2.98 0.04 2 274 25 25 LYS C C 179.43 0.20 1 275 25 25 LYS CA C 59.40 0.10 1 276 25 25 LYS CB C 32.23 0.10 1 277 25 25 LYS CG C 25.50 0.10 1 278 25 25 LYS CD C 29.22 0.10 1 279 25 25 LYS CE C 42.19 0.10 1 280 25 25 LYS N N 122.72 0.10 1 281 26 26 LYS H H 7.65 0.02 1 282 26 26 LYS HA H 4.15 0.02 1 283 26 26 LYS HB2 H 2.31 0.02 2 284 26 26 LYS HB3 H 2.21 0.02 2 285 26 26 LYS HG2 H 1.75 0.02 2 286 26 26 LYS HG3 H 1.62 0.03 2 287 26 26 LYS HD2 H 1.84 0.02 2 288 26 26 LYS HE2 H 3.04 0.02 2 289 26 26 LYS C C 178.07 0.20 1 290 26 26 LYS CA C 59.75 0.10 1 291 26 26 LYS CB C 32.44 0.10 1 292 26 26 LYS CG C 25.59 0.10 1 293 26 26 LYS CD C 29.57 0.10 1 294 26 26 LYS CE C 42.38 0.10 1 295 26 26 LYS N N 122.81 0.10 1 296 27 27 PHE H H 8.11 0.02 1 297 27 27 PHE HA H 3.74 0.02 1 298 27 27 PHE HB2 H 2.58 0.02 2 299 27 27 PHE HB3 H 3.27 0.02 2 300 27 27 PHE HD1 H 6.21 0.02 1 301 27 27 PHE HD2 H 6.21 0.02 1 302 27 27 PHE HE1 H 6.88 0.02 1 303 27 27 PHE HE2 H 6.88 0.02 1 304 27 27 PHE HZ H 7.18 0.02 1 305 27 27 PHE C C 178.98 0.20 1 306 27 27 PHE CA C 61.48 0.10 1 307 27 27 PHE CB C 39.57 0.10 1 308 27 27 PHE CD1 C 132.06 0.10 1 309 27 27 PHE CD2 C 132.06 0.10 1 310 27 27 PHE CE1 C 130.86 0.10 1 311 27 27 PHE CE2 C 130.86 0.10 1 312 27 27 PHE CZ C 129.93 0.10 1 313 27 27 PHE N N 120.05 0.10 1 314 28 28 GLU H H 8.90 0.02 1 315 28 28 GLU HA H 3.98 0.02 1 316 28 28 GLU HB2 H 2.04 0.02 2 317 28 28 GLU HB3 H 2.44 0.02 2 318 28 28 GLU HG2 H 1.98 0.02 2 319 28 28 GLU HG3 H 1.89 0.02 2 320 28 28 GLU C C 179.82 0.20 1 321 28 28 GLU CA C 59.20 0.10 1 322 28 28 GLU CB C 30.10 0.10 1 323 28 28 GLU CG C 35.40 0.10 1 324 28 28 GLU N N 124.11 0.10 1 325 29 29 LYS H H 8.11 0.02 1 326 29 29 LYS HA H 3.98 0.02 1 327 29 29 LYS HB2 H 2.01 0.03 2 328 29 29 LYS HB3 H 2.10 0.02 2 329 29 29 LYS HG2 H 1.55 0.02 2 330 29 29 LYS HG3 H 1.52 0.02 2 331 29 29 LYS HD2 H 1.74 0.02 2 332 29 29 LYS HE2 H 3.01 0.04 2 333 29 29 LYS C C 178.31 0.20 1 334 29 29 LYS CA C 59.38 0.10 1 335 29 29 LYS CB C 31.84 0.10 1 336 29 29 LYS CG C 24.71 0.10 1 337 29 29 LYS CD C 29.24 0.10 1 338 29 29 LYS CE C 42.19 0.10 1 339 29 29 LYS N N 122.03 0.10 1 340 30 30 ASP H H 7.58 0.02 1 341 30 30 ASP HA H 4.54 0.02 1 342 30 30 ASP HB2 H 2.73 0.04 2 343 30 30 ASP C C 178.29 0.20 1 344 30 30 ASP CA C 56.50 0.10 1 345 30 30 ASP CB C 41.11 0.10 1 346 30 30 ASP N N 116.31 0.10 1 347 31 31 THR H H 7.92 0.02 1 348 31 31 THR HA H 4.34 0.02 1 349 31 31 THR HB H 3.79 0.02 1 350 31 31 THR HG2 H 0.50 0.02 1 351 31 31 THR C C 176.20 0.20 1 352 31 31 THR CA C 62.69 0.10 1 353 31 31 THR CB C 72.31 0.10 1 354 31 31 THR CG2 C 19.94 0.10 1 355 31 31 THR N N 107.06 0.10 1 356 32 32 GLY H H 8.62 0.02 1 357 32 32 GLY HA2 H 3.71 0.02 2 358 32 32 GLY HA3 H 4.20 0.02 2 359 32 32 GLY C C 173.49 0.20 1 360 32 32 GLY CA C 45.45 0.10 1 361 32 32 GLY N N 112.68 0.10 1 362 33 33 ILE H H 7.75 0.02 1 363 33 33 ILE HA H 3.89 0.02 1 364 33 33 ILE HB H 1.95 0.02 1 365 33 33 ILE HG12 H 1.14 0.02 2 366 33 33 ILE HG2 H 0.68 0.02 1 367 33 33 ILE HD1 H 0.59 0.02 1 368 33 33 ILE C C 173.69 0.20 1 369 33 33 ILE CA C 58.75 0.10 1 370 33 33 ILE CB C 36.06 0.10 1 371 33 33 ILE CG1 C 26.02 0.10 1 372 33 33 ILE CG2 C 16.87 0.10 1 373 33 33 ILE CD1 C 10.49 0.10 1 374 33 33 ILE N N 124.18 0.10 1 375 34 34 LYS H H 7.78 0.02 1 376 34 34 LYS HA H 3.97 0.02 1 377 34 34 LYS HB2 H 1.69 0.02 2 378 34 34 LYS HG2 H 1.43 0.02 2 379 34 34 LYS HG3 H 1.34 0.02 2 380 34 34 LYS HD2 H 1.62 0.02 2 381 34 34 LYS C C 175.60 0.20 1 382 34 34 LYS CA C 56.66 0.10 1 383 34 34 LYS CB C 33.30 0.10 1 384 34 34 LYS CG C 24.98 0.10 1 385 34 34 LYS CD C 29.09 0.10 1 386 34 34 LYS CE C 42.09 0.10 1 387 34 34 LYS N N 124.81 0.10 1 388 35 35 VAL H H 8.47 0.02 1 389 35 35 VAL HA H 4.72 0.02 1 390 35 35 VAL HB H 1.76 0.02 1 391 35 35 VAL HG1 H 0.36 0.02 1 392 35 35 VAL HG2 H 0.79 0.02 1 393 35 35 VAL C C 175.70 0.20 1 394 35 35 VAL CA C 61.02 0.10 1 395 35 35 VAL CB C 33.35 0.10 1 396 35 35 VAL CG1 C 21.02 0.10 1 397 35 35 VAL CG2 C 22.74 0.10 1 398 35 35 VAL N N 124.78 0.10 1 399 36 36 THR H H 9.12 0.02 1 400 36 36 THR HA H 4.56 0.02 1 401 36 36 THR HB H 4.01 0.02 1 402 36 36 THR HG2 H 1.25 0.02 1 403 36 36 THR C C 172.63 0.20 1 404 36 36 THR CA C 61.45 0.10 1 405 36 36 THR CB C 71.03 0.10 1 406 36 36 THR CG2 C 21.92 0.10 1 407 36 36 THR N N 125.18 0.10 1 408 37 37 VAL H H 8.93 0.02 1 409 37 37 VAL HA H 4.75 0.02 1 410 37 37 VAL HB H 2.12 0.02 1 411 37 37 VAL HG1 H 0.97 0.02 1 412 37 37 VAL HG2 H 0.78 0.02 1 413 37 37 VAL C C 175.32 0.20 1 414 37 37 VAL CA C 61.55 0.10 1 415 37 37 VAL CB C 32.63 0.10 1 416 37 37 VAL CG1 C 23.16 0.10 1 417 37 37 VAL CG2 C 20.97 0.10 1 418 37 37 VAL N N 127.44 0.10 1 419 38 38 GLU H H 9.64 0.02 1 420 38 38 GLU HA H 4.59 0.02 1 421 38 38 GLU HB2 H 2.02 0.02 2 422 38 38 GLU HB3 H 1.81 0.02 2 423 38 38 GLU HG2 H 2.20 0.03 2 424 38 38 GLU HG3 H 2.09 0.02 2 425 38 38 GLU C C 173.39 0.20 1 426 38 38 GLU CA C 54.23 0.10 1 427 38 38 GLU CB C 33.56 0.10 1 428 38 38 GLU CG C 36.39 0.10 1 429 38 38 GLU N N 127.06 0.10 1 430 39 39 HIS H H 8.36 0.02 1 431 39 39 HIS HA H 5.67 0.02 1 432 39 39 HIS HB2 H 2.48 0.02 2 433 39 39 HIS HB3 H 2.83 0.02 2 434 39 39 HIS HD2 H 6.10 0.02 1 435 39 39 HIS HE1 H 8.20 0.02 1 436 39 39 HIS CA C 51.27 0.10 1 437 39 39 HIS CB C 28.73 0.10 1 438 39 39 HIS CD2 C 121.24 0.10 1 439 39 39 HIS CE1 C 135.68 0.10 1 440 39 39 HIS N N 115.17 0.10 1 441 40 40 PRO HA H 4.02 0.02 1 442 40 40 PRO HB2 H 1.72 0.02 2 443 40 40 PRO HB3 H 0.94 0.02 2 444 40 40 PRO HG2 H 0.33 0.02 2 445 40 40 PRO HG3 H 0.06 0.02 2 446 40 40 PRO HD2 H 2.66 0.02 2 447 40 40 PRO HD3 H 2.72 0.02 2 448 40 40 PRO C C 176.64 0.20 1 449 40 40 PRO CA C 62.22 0.10 1 450 40 40 PRO CB C 31.14 0.10 1 451 40 40 PRO CG C 25.33 0.10 1 452 40 40 PRO CD C 49.21 0.10 1 453 41 41 ASP H H 8.27 0.02 1 454 41 41 ASP HA H 4.45 0.02 1 455 41 41 ASP HB2 H 2.47 0.02 2 456 41 41 ASP C C 176.40 0.20 1 457 41 41 ASP CA C 54.83 0.10 1 458 41 41 ASP CB C 41.20 0.10 1 459 41 41 ASP N N 121.26 0.10 1 460 42 42 LYS H H 8.79 0.02 1 461 42 42 LYS HA H 4.16 0.02 1 462 42 42 LYS HB2 H 1.76 0.02 2 463 42 42 LYS HG2 H 1.35 0.02 2 464 42 42 LYS HD2 H 1.57 0.02 2 465 42 42 LYS HE2 H 2.94 0.03 2 466 42 42 LYS C C 178.38 0.20 1 467 42 42 LYS CA C 56.47 0.10 1 468 42 42 LYS CB C 29.85 0.10 1 469 42 42 LYS CG C 25.09 0.10 1 470 42 42 LYS CD C 29.32 0.10 1 471 42 42 LYS CE C 42.33 0.10 1 472 42 42 LYS N N 119.29 0.10 1 473 43 43 LEU H H 7.44 0.02 1 474 43 43 LEU HA H 3.46 0.02 1 475 43 43 LEU HB2 H 1.73 0.02 2 476 43 43 LEU HB3 H 1.77 0.02 2 477 43 43 LEU HG H 1.95 0.02 1 478 43 43 LEU HD1 H 1.12 0.02 1 479 43 43 LEU HD2 H 1.13 0.02 1 480 43 43 LEU C C 175.83 0.20 1 481 43 43 LEU CA C 59.53 0.10 1 482 43 43 LEU CB C 41.20 0.10 1 483 43 43 LEU CG C 26.49 0.10 1 484 43 43 LEU CD1 C 26.90 0.10 1 485 43 43 LEU CD2 C 26.87 0.10 1 486 43 43 LEU N N 120.03 0.10 1 487 44 44 GLU H H 10.49 0.02 1 488 44 44 GLU HA H 3.88 0.02 1 489 44 44 GLU HB2 H -0.22 0.04 2 490 44 44 GLU HB3 H 0.83 0.04 2 491 44 44 GLU C C 178.45 0.20 1 492 44 44 GLU CA C 57.15 0.10 1 493 44 44 GLU CB C 25.02 0.10 1 494 44 44 GLU N N 123.98 0.10 1 495 45 45 GLU H H 7.33 0.02 1 496 45 45 GLU HA H 4.45 0.02 1 497 45 45 GLU HB2 H 1.86 0.02 2 498 45 45 GLU HB3 H 2.14 0.02 2 499 45 45 GLU HG2 H 2.08 0.02 2 500 45 45 GLU C C 178.23 0.20 1 501 45 45 GLU CA C 56.55 0.10 1 502 45 45 GLU CB C 30.29 0.10 1 503 45 45 GLU CG C 36.17 0.10 1 504 45 45 GLU N N 120.60 0.10 1 505 46 46 LYS H H 8.20 0.02 1 506 46 46 LYS HA H 4.19 0.02 1 507 46 46 LYS HB2 H 1.83 0.02 2 508 46 46 LYS HB3 H 1.92 0.02 2 509 46 46 LYS HG2 H 1.53 0.03 2 510 46 46 LYS HG3 H 1.44 0.02 2 511 46 46 LYS HD2 H 1.48 0.02 2 512 46 46 LYS HD3 H 1.40 0.02 2 513 46 46 LYS HE2 H 2.92 0.04 2 514 46 46 LYS C C 179.02 0.20 1 515 46 46 LYS CA C 58.50 0.10 1 516 46 46 LYS CB C 33.87 0.10 1 517 46 46 LYS CG C 25.63 0.10 1 518 46 46 LYS CD C 28.96 0.10 1 519 46 46 LYS CE C 42.37 0.20 1 520 46 46 LYS N N 120.23 0.10 1 521 47 47 PHE H H 8.61 0.02 1 522 47 47 PHE HA H 4.26 0.02 1 523 47 47 PHE HB2 H 2.68 0.02 2 524 47 47 PHE HB3 H 3.21 0.02 2 525 47 47 PHE HD1 H 5.91 0.02 1 526 47 47 PHE HD2 H 5.91 0.02 1 527 47 47 PHE CA C 63.62 0.10 1 528 47 47 PHE CB C 36.44 0.10 1 529 47 47 PHE CD1 C 131.06 0.10 1 530 47 47 PHE CD2 C 131.06 0.10 1 531 47 47 PHE N N 117.08 0.10 1 532 48 48 PRO HA H 3.71 0.02 1 533 48 48 PRO HB2 H 1.83 0.02 2 534 48 48 PRO HB3 H 2.06 0.02 2 535 48 48 PRO HG2 H 1.97 0.02 2 536 48 48 PRO HG3 H 2.19 0.02 2 537 48 48 PRO HD2 H 3.33 0.02 2 538 48 48 PRO HD3 H 3.66 0.02 2 539 48 48 PRO C C 177.77 0.20 1 540 48 48 PRO CA C 65.48 0.10 1 541 48 48 PRO CB C 30.48 0.10 1 542 48 48 PRO CG C 28.49 0.10 1 543 48 48 PRO CD C 49.56 0.10 1 544 49 49 GLN H H 6.95 0.02 1 545 49 49 GLN HA H 4.13 0.02 1 546 49 49 GLN HB2 H 2.17 0.02 2 547 49 49 GLN HB3 H 2.24 0.03 2 548 49 49 GLN HG2 H 2.49 0.02 2 549 49 49 GLN HG3 H 2.35 0.02 2 550 49 49 GLN HE21 H 7.33 0.02 2 551 49 49 GLN HE22 H 6.77 0.02 2 552 49 49 GLN C C 178.32 0.20 1 553 49 49 GLN CA C 57.94 0.10 1 554 49 49 GLN CB C 28.91 0.10 1 555 49 49 GLN CG C 33.76 0.10 1 556 49 49 GLN N N 114.72 0.10 1 557 49 49 GLN NE2 N 111.22 0.10 1 558 50 50 VAL H H 7.58 0.02 1 559 50 50 VAL HA H 4.42 0.02 1 560 50 50 VAL HB H 2.00 0.02 1 561 50 50 VAL HG1 H 0.97 0.02 1 562 50 50 VAL HG2 H 0.86 0.02 1 563 50 50 VAL C C 178.03 0.20 1 564 50 50 VAL CA C 61.77 0.10 1 565 50 50 VAL CB C 32.62 0.10 1 566 50 50 VAL CG1 C 21.40 0.10 1 567 50 50 VAL CG2 C 19.94 0.10 1 568 50 50 VAL N N 110.00 0.10 1 569 51 51 ALA H H 8.10 0.02 1 570 51 51 ALA HA H 3.68 0.02 1 571 51 51 ALA HB H 0.57 0.02 1 572 51 51 ALA C C 179.86 0.20 1 573 51 51 ALA CA C 55.07 0.10 1 574 51 51 ALA CB C 18.14 0.10 1 575 51 51 ALA N N 124.92 0.10 1 576 52 52 ALA H H 7.73 0.02 1 577 52 52 ALA HA H 4.15 0.02 1 578 52 52 ALA HB H 1.35 0.02 1 579 52 52 ALA C C 178.44 0.20 1 580 52 52 ALA CA C 53.19 0.10 1 581 52 52 ALA CB C 18.56 0.10 1 582 52 52 ALA N N 117.56 0.10 1 583 53 53 THR H H 7.25 0.02 1 584 53 53 THR HA H 4.42 0.02 1 585 53 53 THR HB H 4.50 0.02 1 586 53 53 THR HG2 H 1.16 0.02 1 587 53 53 THR C C 175.22 0.20 1 588 53 53 THR CA C 61.51 0.10 1 589 53 53 THR CB C 69.98 0.10 1 590 53 53 THR CG2 C 21.65 0.10 1 591 53 53 THR N N 106.12 0.10 1 592 54 54 GLY H H 7.84 0.02 1 593 54 54 GLY HA2 H 3.64 0.02 2 594 54 54 GLY HA3 H 4.23 0.02 2 595 54 54 GLY C C 173.54 0.20 1 596 54 54 GLY CA C 45.61 0.10 1 597 54 54 GLY N N 108.93 0.10 1 598 55 55 ASP H H 7.55 0.02 1 599 55 55 ASP HA H 4.92 0.02 1 600 55 55 ASP HB2 H 2.32 0.02 2 601 55 55 ASP HB3 H 2.78 0.02 2 602 55 55 ASP C C 175.17 0.20 1 603 55 55 ASP CA C 53.41 0.10 1 604 55 55 ASP CB C 42.41 0.10 1 605 55 55 ASP N N 119.07 0.10 1 606 56 56 GLY H H 8.19 0.02 1 607 56 56 GLY HA2 H 3.16 0.02 2 608 56 56 GLY HA3 H 3.55 0.02 2 609 56 56 GLY CA C 44.12 0.10 1 610 56 56 GLY N N 106.49 0.10 1 611 57 57 PRO HA H 3.94 0.02 1 612 57 57 PRO HB2 H 1.71 0.02 2 613 57 57 PRO C C 174.89 0.20 1 614 57 57 PRO CA C 61.82 0.10 1 615 57 57 PRO CB C 31.04 0.10 1 616 58 58 ASP H H 8.72 0.02 1 617 58 58 ASP HA H 4.48 0.02 1 618 58 58 ASP HB2 H 2.52 0.02 2 619 58 58 ASP HB3 H 2.58 0.02 2 620 58 58 ASP C C 175.56 0.20 1 621 58 58 ASP CA C 58.29 0.10 1 622 58 58 ASP CB C 44.03 0.10 1 623 58 58 ASP N N 117.82 0.10 1 624 59 59 ILE H H 7.61 0.02 1 625 59 59 ILE HA H 5.27 0.02 1 626 59 59 ILE HB H 1.60 0.02 1 627 59 59 ILE HG12 H 0.87 0.02 2 628 59 59 ILE HG13 H 1.42 0.02 2 629 59 59 ILE HG2 H 0.87 0.02 1 630 59 59 ILE HD1 H 0.77 0.02 1 631 59 59 ILE C C 173.60 0.20 1 632 59 59 ILE CA C 58.87 0.10 1 633 59 59 ILE CB C 43.13 0.10 1 634 59 59 ILE CG1 C 27.67 0.10 1 635 59 59 ILE CG2 C 19.12 0.10 1 636 59 59 ILE CD1 C 14.20 0.10 1 637 59 59 ILE N N 114.32 0.10 1 638 60 60 ILE H H 8.90 0.02 1 639 60 60 ILE HA H 5.38 0.02 1 640 60 60 ILE HB H 1.08 0.02 1 641 60 60 ILE HG12 H 0.84 0.02 2 642 60 60 ILE HG13 H 1.48 0.02 2 643 60 60 ILE HG2 H 0.09 0.02 1 644 60 60 ILE HD1 H 0.44 0.02 1 645 60 60 ILE C C 172.75 0.20 1 646 60 60 ILE CA C 57.92 0.10 1 647 60 60 ILE CB C 41.88 0.10 1 648 60 60 ILE CG1 C 29.33 0.10 1 649 60 60 ILE CG2 C 14.05 0.10 1 650 60 60 ILE CD1 C 15.14 0.10 1 651 60 60 ILE N N 124.41 0.10 1 652 61 61 PHE H H 8.66 0.02 1 653 61 61 PHE HA H 6.34 0.02 1 654 61 61 PHE HB2 H 3.50 0.02 2 655 61 61 PHE HB3 H 2.73 0.03 2 656 61 61 PHE HD1 H 7.21 0.02 1 657 61 61 PHE HD2 H 7.21 0.02 1 658 61 61 PHE HE1 H 7.10 0.02 1 659 61 61 PHE HE2 H 7.10 0.02 1 660 61 61 PHE HZ H 7.00 0.02 1 661 61 61 PHE C C 176.56 0.20 1 662 61 61 PHE CA C 55.65 0.10 1 663 61 61 PHE CB C 42.41 0.10 1 664 61 61 PHE CD1 C 131.51 0.10 1 665 61 61 PHE CD2 C 131.51 0.10 1 666 61 61 PHE CE1 C 130.78 0.10 1 667 61 61 PHE CE2 C 130.78 0.10 1 668 61 61 PHE CZ C 128.09 0.10 1 669 61 61 PHE N N 126.25 0.10 1 670 62 62 TRP H H 9.17 0.02 1 671 62 62 TRP HA H 4.27 0.02 1 672 62 62 TRP HB2 H 2.89 0.02 2 673 62 62 TRP HB3 H 3.58 0.02 2 674 62 62 TRP HD1 H 7.60 0.02 1 675 62 62 TRP HE1 H 10.34 0.02 1 676 62 62 TRP HZ2 H 7.42 0.02 1 677 62 62 TRP HZ3 H 7.13 0.02 1 678 62 62 TRP HH2 H 7.22 0.02 1 679 62 62 TRP C C 173.42 0.20 1 680 62 62 TRP CA C 57.29 0.10 1 681 62 62 TRP CB C 31.90 0.10 1 682 62 62 TRP CD1 C 128.13 0.10 1 683 62 62 TRP CZ2 C 114.47 0.10 1 684 62 62 TRP CZ3 C 121.61 0.10 1 685 62 62 TRP CH2 C 125.94 0.10 1 686 62 62 TRP N N 121.36 0.10 1 687 62 62 TRP NE1 N 129.08 0.10 1 688 63 63 ALA H H 6.44 0.02 1 689 63 63 ALA HA H 4.09 0.02 1 690 63 63 ALA HB H 1.12 0.02 1 691 63 63 ALA C C 179.50 0.20 1 692 63 63 ALA CA C 53.91 0.10 1 693 63 63 ALA CB C 19.21 0.10 1 694 63 63 ALA N N 126.31 0.10 1 695 64 64 HIS H H 8.14 0.02 1 696 64 64 HIS HA H 3.74 0.02 1 697 64 64 HIS HB2 H 3.45 0.02 2 698 64 64 HIS HB3 H 3.06 0.02 2 699 64 64 HIS HD2 H 7.24 0.02 1 700 64 64 HIS HE1 H 8.96 0.02 1 701 64 64 HIS C C 178.25 0.20 1 702 64 64 HIS CA C 60.22 0.10 1 703 64 64 HIS CB C 30.29 0.10 1 704 64 64 HIS CD2 C 119.81 0.10 1 705 64 64 HIS CE1 C 138.36 0.10 1 706 64 64 HIS N N 116.31 0.10 1 707 65 65 ASP H H 7.71 0.02 1 708 65 65 ASP HA H 3.71 0.02 1 709 65 65 ASP HB2 H 1.85 0.02 2 710 65 65 ASP HB3 H 2.69 0.02 2 711 65 65 ASP C C 177.70 0.20 1 712 65 65 ASP CA C 56.59 0.10 1 713 65 65 ASP CB C 39.12 0.10 1 714 65 65 ASP N N 119.23 0.10 1 715 66 66 ARG H H 7.04 0.02 1 716 66 66 ARG HA H 4.17 0.02 1 717 66 66 ARG HB2 H 1.65 0.02 2 718 66 66 ARG HB3 H 1.59 0.02 2 719 66 66 ARG HG2 H 1.35 0.02 2 720 66 66 ARG HG3 H 1.40 0.02 2 721 66 66 ARG HD2 H 3.08 0.02 2 722 66 66 ARG HD3 H 2.98 0.02 2 723 66 66 ARG C C 177.37 0.20 1 724 66 66 ARG CA C 54.78 0.10 1 725 66 66 ARG CB C 30.34 0.10 1 726 66 66 ARG CG C 26.64 0.10 1 727 66 66 ARG CD C 41.12 0.10 1 728 66 66 ARG N N 117.29 0.10 1 729 67 67 PHE H H 7.62 0.02 1 730 67 67 PHE HA H 4.13 0.02 1 731 67 67 PHE HB2 H 3.04 0.02 2 732 67 67 PHE HB3 H 3.54 0.02 2 733 67 67 PHE HD1 H 6.94 0.02 1 734 67 67 PHE HD2 H 6.94 0.02 1 735 67 67 PHE HE1 H 7.08 0.02 1 736 67 67 PHE HE2 H 7.08 0.02 1 737 67 67 PHE HZ H 7.43 0.02 1 738 67 67 PHE C C 177.82 0.20 1 739 67 67 PHE CA C 57.94 0.10 1 740 67 67 PHE CB C 36.78 0.10 1 741 67 67 PHE CD1 C 129.05 0.10 1 742 67 67 PHE CD2 C 129.05 0.10 1 743 67 67 PHE CE1 C 131.23 0.10 1 744 67 67 PHE CE2 C 131.23 0.10 1 745 67 67 PHE CZ C 130.17 0.10 1 746 67 67 PHE N N 116.53 0.10 1 747 68 68 GLY H H 7.37 0.02 1 748 68 68 GLY HA2 H 3.18 0.02 2 749 68 68 GLY HA3 H 4.41 0.02 2 750 68 68 GLY C C 175.75 0.20 1 751 68 68 GLY CA C 47.61 0.10 1 752 68 68 GLY N N 107.47 0.10 1 753 69 69 GLY H H 7.78 0.02 1 754 69 69 GLY HA2 H 3.83 0.02 2 755 69 69 GLY C C 177.21 0.20 1 756 69 69 GLY CA C 46.98 0.10 1 757 69 69 GLY N N 107.65 0.10 1 758 70 70 TYR H H 6.88 0.02 1 759 70 70 TYR HA H 4.66 0.02 1 760 70 70 TYR HB2 H 3.27 0.02 2 761 70 70 TYR HB3 H 3.04 0.02 2 762 70 70 TYR HD1 H 6.75 0.02 1 763 70 70 TYR HD2 H 6.75 0.02 1 764 70 70 TYR HE1 H 6.54 0.02 1 765 70 70 TYR HE2 H 6.54 0.02 1 766 70 70 TYR CA C 57.03 0.10 1 767 70 70 TYR CB C 36.17 0.10 1 768 70 70 TYR CD1 C 131.24 0.10 1 769 70 70 TYR CD2 C 131.24 0.10 1 770 70 70 TYR CE1 C 118.37 0.10 1 771 70 70 TYR CE2 C 118.37 0.10 1 772 70 70 TYR N N 118.98 0.10 1 773 71 71 ALA H H 8.59 0.02 1 774 71 71 ALA HA H 4.47 0.02 1 775 71 71 ALA HB H 1.28 0.02 1 776 71 71 ALA C C 182.01 0.20 1 777 71 71 ALA CA C 54.33 0.10 1 778 71 71 ALA CB C 18.32 0.10 1 779 71 71 ALA N N 122.79 0.10 1 780 72 72 GLN H H 8.64 0.02 1 781 72 72 GLN HA H 4.12 0.02 1 782 72 72 GLN HB2 H 2.28 0.02 2 783 72 72 GLN HB3 H 2.38 0.02 2 784 72 72 GLN HG2 H 2.54 0.02 2 785 72 72 GLN HG3 H 2.56 0.02 2 786 72 72 GLN HE21 H 7.67 0.02 2 787 72 72 GLN HE22 H 7.02 0.02 2 788 72 72 GLN C C 177.68 0.20 1 789 72 72 GLN CA C 58.61 0.10 1 790 72 72 GLN CB C 27.92 0.10 1 791 72 72 GLN CG C 33.41 0.10 1 792 72 72 GLN N N 122.64 0.10 1 793 72 72 GLN NE2 N 113.07 0.10 1 794 73 73 SER H H 7.31 0.02 1 795 73 73 SER HA H 4.57 0.02 1 796 73 73 SER HB2 H 3.91 0.02 2 797 73 73 SER HB3 H 4.15 0.02 2 798 73 73 SER C C 173.59 0.20 1 799 73 73 SER CA C 59.08 0.10 1 800 73 73 SER CB C 64.24 0.10 1 801 73 73 SER N N 112.05 0.10 1 802 74 74 GLY H H 8.05 0.02 1 803 74 74 GLY HA2 H 4.04 0.02 2 804 74 74 GLY C C 176.15 0.20 1 805 74 74 GLY CA C 46.36 0.10 1 806 74 74 GLY N N 109.30 0.10 1 807 75 75 LEU H H 7.85 0.02 1 808 75 75 LEU HA H 4.17 0.02 1 809 75 75 LEU HB2 H 1.42 0.02 2 810 75 75 LEU HG H 1.54 0.02 1 811 75 75 LEU HD1 H 0.65 0.02 1 812 75 75 LEU HD2 H 0.53 0.02 1 813 75 75 LEU C C 177.62 0.20 1 814 75 75 LEU CA C 55.57 0.10 1 815 75 75 LEU CB C 43.08 0.10 1 816 75 75 LEU CG C 26.27 0.10 1 817 75 75 LEU CD1 C 26.00 0.10 1 818 75 75 LEU CD2 C 20.94 0.10 1 819 75 75 LEU N N 113.64 0.10 1 820 76 76 LEU H H 7.44 0.02 1 821 76 76 LEU HA H 5.21 0.02 1 822 76 76 LEU HB2 H 1.50 0.02 2 823 76 76 LEU HB3 H 1.92 0.02 2 824 76 76 LEU HG H 1.31 0.02 1 825 76 76 LEU HD1 H 0.85 0.02 1 826 76 76 LEU HD2 H 0.51 0.02 1 827 76 76 LEU C C 176.56 0.20 1 828 76 76 LEU CA C 52.49 0.10 1 829 76 76 LEU CB C 43.96 0.10 1 830 76 76 LEU CG C 27.29 0.10 1 831 76 76 LEU CD1 C 27.41 0.10 1 832 76 76 LEU CD2 C 22.09 0.10 1 833 76 76 LEU N N 116.05 0.10 1 834 77 77 ALA H H 9.05 0.02 1 835 77 77 ALA HA H 4.26 0.02 1 836 77 77 ALA HB H 1.19 0.02 1 837 77 77 ALA C C 176.28 0.20 1 838 77 77 ALA CA C 51.03 0.10 1 839 77 77 ALA CB C 19.36 0.10 1 840 77 77 ALA N N 126.09 0.10 1 841 78 78 GLU H H 8.23 0.02 1 842 78 78 GLU HA H 4.57 0.02 1 843 78 78 GLU HB2 H 1.94 0.02 2 844 78 78 GLU HG2 H 2.52 0.02 2 845 78 78 GLU HG3 H 2.22 0.02 2 846 78 78 GLU C C 176.76 0.20 1 847 78 78 GLU CA C 56.30 0.10 1 848 78 78 GLU CB C 29.82 0.10 1 849 78 78 GLU CG C 36.29 0.10 1 850 78 78 GLU N N 120.96 0.10 1 851 79 79 ILE H H 8.17 0.02 1 852 79 79 ILE HA H 4.54 0.02 1 853 79 79 ILE HB H 1.62 0.02 1 854 79 79 ILE HG12 H 1.00 0.02 2 855 79 79 ILE HG13 H 0.68 0.02 2 856 79 79 ILE HG2 H 0.71 0.02 1 857 79 79 ILE HD1 H 0.17 0.02 1 858 79 79 ILE C C 175.55 0.20 1 859 79 79 ILE CA C 59.70 0.10 1 860 79 79 ILE CB C 39.54 0.10 1 861 79 79 ILE CG1 C 26.54 0.10 1 862 79 79 ILE CG2 C 18.54 0.10 1 863 79 79 ILE CD1 C 12.80 0.10 1 864 79 79 ILE N N 122.63 0.10 1 865 80 80 THR H H 8.80 0.02 1 866 80 80 THR HA H 4.65 0.02 1 867 80 80 THR HB H 4.36 0.02 1 868 80 80 THR HG2 H 0.99 0.02 1 869 80 80 THR CA C 57.89 0.10 1 870 80 80 THR CB C 69.25 0.10 1 871 80 80 THR CG2 C 20.97 0.10 1 872 80 80 THR N N 112.27 0.10 1 873 81 81 PRO HA H 4.71 0.02 1 874 81 81 PRO HB2 H 1.98 0.02 2 875 81 81 PRO HB3 H 2.34 0.02 2 876 81 81 PRO HG2 H 1.60 0.02 2 877 81 81 PRO HG3 H 1.56 0.02 2 878 81 81 PRO HD2 H 3.20 0.02 2 879 81 81 PRO HD3 H 3.27 0.02 2 880 81 81 PRO C C 177.45 0.20 1 881 81 81 PRO CA C 62.37 0.10 1 882 81 81 PRO CB C 32.10 0.10 1 883 81 81 PRO CG C 27.13 0.10 1 884 81 81 PRO CD C 49.81 0.10 1 885 82 82 ASP H H 9.09 0.02 1 886 82 82 ASP HA H 4.51 0.02 1 887 82 82 ASP HB2 H 2.81 0.02 2 888 82 82 ASP HB3 H 3.05 0.02 2 889 82 82 ASP CA C 53.34 0.10 1 890 82 82 ASP CB C 41.56 0.10 1 891 82 82 ASP N N 123.81 0.10 1 892 83 83 LYS H H 8.56 0.02 1 893 83 83 LYS HA H 3.71 0.02 1 894 83 83 LYS HB2 H 1.80 0.02 2 895 83 83 LYS HB3 H 1.83 0.02 2 896 83 83 LYS HG2 H 1.42 0.02 2 897 83 83 LYS HD2 H 1.57 0.02 2 898 83 83 LYS HD3 H 1.65 0.02 2 899 83 83 LYS C C 177.50 0.20 1 900 83 83 LYS CA C 59.79 0.10 1 901 83 83 LYS CB C 32.18 0.10 1 902 83 83 LYS CG C 24.76 0.10 1 903 83 83 LYS CD C 28.66 0.10 1 904 83 83 LYS N N 122.71 0.10 1 905 84 84 ALA H H 8.19 0.02 1 906 84 84 ALA HA H 4.11 0.02 1 907 84 84 ALA HB H 1.45 0.02 1 908 84 84 ALA C C 180.22 0.20 1 909 84 84 ALA CA C 54.85 0.10 1 910 84 84 ALA CB C 17.86 0.10 1 911 84 84 ALA N N 119.40 0.10 1 912 85 85 PHE H H 7.96 0.02 1 913 85 85 PHE HA H 4.06 0.02 1 914 85 85 PHE HB2 H 3.13 0.02 2 915 85 85 PHE HB3 H 3.39 0.02 2 916 85 85 PHE HD1 H 7.34 0.02 1 917 85 85 PHE HD2 H 7.34 0.02 1 918 85 85 PHE HE1 H 7.76 0.02 1 919 85 85 PHE HE2 H 7.76 0.02 1 920 85 85 PHE HZ H 7.55 0.02 1 921 85 85 PHE C C 178.21 0.20 1 922 85 85 PHE CA C 62.39 0.10 1 923 85 85 PHE CB C 39.38 0.10 1 924 85 85 PHE CD1 C 131.94 0.10 1 925 85 85 PHE CD2 C 131.94 0.10 1 926 85 85 PHE CE1 C 130.80 0.10 1 927 85 85 PHE CE2 C 130.80 0.10 1 928 85 85 PHE CZ C 129.48 0.10 1 929 85 85 PHE N N 118.46 0.10 1 930 86 86 GLN H H 8.52 0.02 1 931 86 86 GLN HA H 4.21 0.02 1 932 86 86 GLN HB2 H 1.74 0.02 2 933 86 86 GLN HB3 H 1.86 0.03 2 934 86 86 GLN HG2 H 0.96 0.02 2 935 86 86 GLN HG3 H 1.93 0.02 2 936 86 86 GLN HE21 H 6.58 0.02 2 937 86 86 GLN HE22 H 6.37 0.02 2 938 86 86 GLN C C 179.97 0.20 1 939 86 86 GLN CA C 59.71 0.10 1 940 86 86 GLN CB C 28.65 0.10 1 941 86 86 GLN CG C 33.99 0.10 1 942 86 86 GLN N N 117.22 0.10 1 943 86 86 GLN NE2 N 110.40 0.10 1 944 87 87 ASP H H 8.10 0.02 1 945 87 87 ASP HA H 4.61 0.02 1 946 87 87 ASP HB2 H 2.70 0.02 2 947 87 87 ASP C C 176.41 0.20 1 948 87 87 ASP CA C 56.04 0.10 1 949 87 87 ASP CB C 41.06 0.10 1 950 87 87 ASP N N 116.90 0.10 1 951 88 88 LYS H H 7.82 0.02 1 952 88 88 LYS HA H 4.09 0.02 1 953 88 88 LYS HB2 H 1.72 0.03 2 954 88 88 LYS HG2 H 1.33 0.02 2 955 88 88 LYS HG3 H 1.75 0.02 2 956 88 88 LYS HD2 H 1.61 0.02 2 957 88 88 LYS HD3 H 1.57 0.02 2 958 88 88 LYS HE2 H 2.90 0.02 2 959 88 88 LYS C C 176.64 0.20 1 960 88 88 LYS CA C 58.17 0.10 1 961 88 88 LYS CB C 32.37 0.10 1 962 88 88 LYS CG C 25.86 0.10 1 963 88 88 LYS CD C 29.86 0.10 1 964 88 88 LYS CE C 42.21 0.10 1 965 88 88 LYS N N 117.15 0.10 1 966 89 89 LEU H H 7.68 0.02 1 967 89 89 LEU HA H 5.27 0.02 1 968 89 89 LEU HB2 H 1.17 0.02 2 969 89 89 LEU HB3 H 1.46 0.02 2 970 89 89 LEU HG H 1.34 0.02 1 971 89 89 LEU HD1 H 0.57 0.02 1 972 89 89 LEU HD2 H 0.52 0.02 1 973 89 89 LEU C C 176.56 0.20 1 974 89 89 LEU CA C 53.46 0.10 1 975 89 89 LEU CB C 43.15 0.10 1 976 89 89 LEU CG C 29.01 0.10 1 977 89 89 LEU CD1 C 26.43 0.10 1 978 89 89 LEU CD2 C 25.69 0.10 1 979 89 89 LEU N N 120.22 0.10 1 980 90 90 TYR H H 7.73 0.02 1 981 90 90 TYR HA H 4.26 0.02 1 982 90 90 TYR HB2 H 3.05 0.02 2 983 90 90 TYR HB3 H 2.26 0.02 2 984 90 90 TYR HD1 H 7.23 0.02 1 985 90 90 TYR HD2 H 7.23 0.02 1 986 90 90 TYR HE1 H 6.83 0.02 1 987 90 90 TYR HE2 H 6.83 0.02 1 988 90 90 TYR CA C 59.16 0.10 1 989 90 90 TYR CB C 39.43 0.10 1 990 90 90 TYR CD1 C 133.33 0.10 1 991 90 90 TYR CD2 C 133.33 0.10 1 992 90 90 TYR CE1 C 119.31 0.10 1 993 90 90 TYR CE2 C 119.31 0.10 1 994 90 90 TYR N N 117.03 0.10 1 995 91 91 PRO HA H 4.59 0.02 1 996 91 91 PRO HB2 H 2.61 0.02 2 997 91 91 PRO HB3 H 2.33 0.02 2 998 91 91 PRO HG2 H 2.40 0.02 2 999 91 91 PRO HD2 H 4.20 0.02 2 1000 91 91 PRO C C 179.51 0.20 1 1001 91 91 PRO CA C 66.77 0.10 1 1002 91 91 PRO CB C 31.84 0.10 1 1003 91 91 PRO CG C 27.46 0.10 1 1004 91 91 PRO CD C 51.53 0.10 1 1005 92 92 PHE H H 8.08 0.02 1 1006 92 92 PHE HA H 4.70 0.02 1 1007 92 92 PHE HB2 H 3.34 0.02 2 1008 92 92 PHE HB3 H 3.27 0.02 2 1009 92 92 PHE HD1 H 7.24 0.02 1 1010 92 92 PHE HD2 H 7.24 0.02 1 1011 92 92 PHE HE1 H 6.85 0.02 1 1012 92 92 PHE HE2 H 6.85 0.02 1 1013 92 92 PHE HZ H 6.85 0.02 1 1014 92 92 PHE C C 176.21 0.20 1 1015 92 92 PHE CA C 59.28 0.10 1 1016 92 92 PHE CB C 37.00 0.10 1 1017 92 92 PHE CD1 C 132.50 0.10 1 1018 92 92 PHE CD2 C 132.50 0.10 1 1019 92 92 PHE CE1 C 130.49 0.10 1 1020 92 92 PHE CE2 C 130.49 0.10 1 1021 92 92 PHE CZ C 128.88 0.10 1 1022 92 92 PHE N N 112.86 0.10 1 1023 93 93 THR H H 7.09 0.02 1 1024 93 93 THR HA H 3.42 0.02 1 1025 93 93 THR HB H 3.47 0.02 1 1026 93 93 THR HG2 H 0.23 0.02 1 1027 93 93 THR C C 176.33 0.20 1 1028 93 93 THR CA C 64.73 0.10 1 1029 93 93 THR CB C 67.21 0.10 1 1030 93 93 THR CG2 C 23.12 0.10 1 1031 93 93 THR N N 110.76 0.10 1 1032 94 94 TRP H H 6.68 0.02 1 1033 94 94 TRP HA H 4.60 0.02 1 1034 94 94 TRP HB2 H 3.22 0.02 2 1035 94 94 TRP HB3 H 3.24 0.02 2 1036 94 94 TRP HD1 H 7.17 0.02 1 1037 94 94 TRP HE1 H 10.48 0.02 1 1038 94 94 TRP HE3 H 7.72 0.02 1 1039 94 94 TRP HZ2 H 7.47 0.02 1 1040 94 94 TRP C C 178.10 0.20 1 1041 94 94 TRP CA C 58.52 0.10 1 1042 94 94 TRP CB C 29.61 0.10 1 1043 94 94 TRP CD1 C 127.89 0.10 1 1044 94 94 TRP CE3 C 123.20 0.10 1 1045 94 94 TRP CZ2 C 114.30 0.10 1 1046 94 94 TRP N N 119.80 0.10 1 1047 94 94 TRP NE1 N 128.55 0.10 1 1048 95 95 ASP H H 7.24 0.02 1 1049 95 95 ASP HA H 4.46 0.02 1 1050 95 95 ASP HB2 H 2.89 0.02 2 1051 95 95 ASP HB3 H 2.62 0.02 2 1052 95 95 ASP C C 178.23 0.20 1 1053 95 95 ASP CA C 57.15 0.10 1 1054 95 95 ASP CB C 40.03 0.10 1 1055 95 95 ASP N N 115.36 0.10 1 1056 96 96 ALA H H 7.01 0.02 1 1057 96 96 ALA HA H 3.95 0.02 1 1058 96 96 ALA HB H 0.77 0.02 1 1059 96 96 ALA C C 176.67 0.20 1 1060 96 96 ALA CA C 53.62 0.10 1 1061 96 96 ALA CB C 18.25 0.10 1 1062 96 96 ALA N N 118.65 0.10 1 1063 97 97 VAL H H 6.97 0.02 1 1064 97 97 VAL HA H 4.50 0.02 1 1065 97 97 VAL HB H 2.71 0.02 1 1066 97 97 VAL HG1 H 0.59 0.02 1 1067 97 97 VAL HG2 H 1.36 0.02 1 1068 97 97 VAL C C 172.57 0.20 1 1069 97 97 VAL CA C 59.59 0.10 1 1070 97 97 VAL CB C 30.88 0.10 1 1071 97 97 VAL CG1 C 22.52 0.10 1 1072 97 97 VAL CG2 C 19.79 0.10 1 1073 97 97 VAL N N 105.85 0.10 1 1074 98 98 ARG H H 7.04 0.02 1 1075 98 98 ARG HA H 5.33 0.02 1 1076 98 98 ARG HB2 H 1.84 0.03 2 1077 98 98 ARG HB3 H 1.95 0.02 2 1078 98 98 ARG HG2 H 1.68 0.02 2 1079 98 98 ARG HG3 H 1.43 0.02 2 1080 98 98 ARG C C 176.58 0.20 1 1081 98 98 ARG CA C 54.70 0.10 1 1082 98 98 ARG CB C 32.20 0.10 1 1083 98 98 ARG CG C 28.58 0.10 1 1084 98 98 ARG N N 120.97 0.10 1 1085 99 99 TYR H H 9.69 0.02 1 1086 99 99 TYR HA H 4.92 0.02 1 1087 99 99 TYR HB2 H 2.81 0.03 2 1088 99 99 TYR HD1 H 7.17 0.02 1 1089 99 99 TYR HD2 H 7.17 0.02 1 1090 99 99 TYR HE1 H 6.80 0.02 1 1091 99 99 TYR HE2 H 6.80 0.02 1 1092 99 99 TYR CA C 58.37 0.10 1 1093 99 99 TYR CB C 42.27 0.10 1 1094 99 99 TYR CD1 C 133.45 0.10 1 1095 99 99 TYR CD2 C 133.45 0.10 1 1096 99 99 TYR CE1 C 118.30 0.10 1 1097 99 99 TYR CE2 C 118.30 0.10 1 1098 99 99 TYR N N 126.47 0.10 1 1099 100 100 ASN HA H 4.23 0.02 1 1100 100 100 ASN HB2 H 2.31 0.02 2 1101 100 100 ASN HB3 H 3.08 0.02 2 1102 100 100 ASN HD21 H 7.38 0.02 2 1103 100 100 ASN HD22 H 6.76 0.02 2 1104 100 100 ASN C C 175.22 0.20 1 1105 100 100 ASN CA C 53.72 0.10 1 1106 100 100 ASN CB C 37.22 0.10 1 1107 100 100 ASN ND2 N 111.20 0.10 1 1108 101 101 GLY H H 8.63 0.02 1 1109 101 101 GLY HA2 H 3.60 0.02 2 1110 101 101 GLY HA3 H 4.22 0.02 2 1111 101 101 GLY C C 173.91 0.20 1 1112 101 101 GLY CA C 45.55 0.10 1 1113 101 101 GLY N N 102.14 0.10 1 1114 102 102 LYS H H 7.77 0.02 1 1115 102 102 LYS HA H 4.64 0.02 1 1116 102 102 LYS HB2 H 1.68 0.02 2 1117 102 102 LYS HB3 H 1.92 0.02 2 1118 102 102 LYS HG2 H 1.44 0.02 2 1119 102 102 LYS HD2 H 1.67 0.02 2 1120 102 102 LYS HE2 H 3.04 0.02 2 1121 102 102 LYS C C 175.15 0.20 1 1122 102 102 LYS CA C 54.58 0.10 1 1123 102 102 LYS CB C 35.22 0.10 1 1124 102 102 LYS CG C 24.78 0.10 1 1125 102 102 LYS CD C 29.10 0.10 1 1126 102 102 LYS CE C 42.39 0.10 1 1127 102 102 LYS N N 121.18 0.10 1 1128 103 103 LEU H H 8.99 0.02 1 1129 103 103 LEU HA H 5.03 0.02 1 1130 103 103 LEU HB2 H 2.23 0.02 2 1131 103 103 LEU HG H 1.72 0.02 1 1132 103 103 LEU HD1 H 0.54 0.02 1 1133 103 103 LEU HD2 H 1.01 0.02 1 1134 103 103 LEU C C 178.36 0.20 1 1135 103 103 LEU CA C 55.15 0.10 1 1136 103 103 LEU CB C 42.84 0.10 1 1137 103 103 LEU CG C 26.73 0.10 1 1138 103 103 LEU CD1 C 25.15 0.10 1 1139 103 103 LEU CD2 C 24.63 0.10 1 1140 103 103 LEU N N 123.48 0.10 1 1141 104 104 ILE H H 8.83 0.02 1 1142 104 104 ILE HA H 4.89 0.02 1 1143 104 104 ILE HB H 2.56 0.02 1 1144 104 104 ILE HG12 H 1.21 0.02 2 1145 104 104 ILE HG13 H 1.45 0.02 2 1146 104 104 ILE HG2 H 0.92 0.02 1 1147 104 104 ILE HD1 H 0.88 0.02 1 1148 104 104 ILE C C 175.42 0.20 1 1149 104 104 ILE CA C 59.52 0.10 1 1150 104 104 ILE CB C 39.53 0.10 1 1151 104 104 ILE CG1 C 27.92 0.10 1 1152 104 104 ILE CG2 C 20.73 0.10 1 1153 104 104 ILE CD1 C 15.03 0.10 1 1154 104 104 ILE N N 112.43 0.10 1 1155 105 105 ALA H H 7.67 0.02 1 1156 105 105 ALA HA H 4.60 0.02 1 1157 105 105 ALA HB H 1.45 0.02 1 1158 105 105 ALA C C 173.56 0.20 1 1159 105 105 ALA CA C 52.09 0.10 1 1160 105 105 ALA CB C 22.41 0.10 1 1161 105 105 ALA N N 116.99 0.10 1 1162 106 106 TYR H H 8.99 0.02 1 1163 106 106 TYR HA H 4.82 0.02 1 1164 106 106 TYR HB2 H 2.74 0.04 2 1165 106 106 TYR HD1 H 7.14 0.02 1 1166 106 106 TYR HD2 H 7.14 0.02 1 1167 106 106 TYR HE1 H 6.61 0.02 1 1168 106 106 TYR HE2 H 6.61 0.02 1 1169 106 106 TYR CA C 56.01 0.10 1 1170 106 106 TYR CB C 40.33 0.10 1 1171 106 106 TYR CD1 C 133.27 0.10 1 1172 106 106 TYR CD2 C 133.27 0.10 1 1173 106 106 TYR CE1 C 118.66 0.10 1 1174 106 106 TYR CE2 C 118.66 0.10 1 1175 106 106 TYR N N 113.70 0.10 1 1176 107 107 PRO HA H 4.07 0.02 1 1177 107 107 PRO HB2 H 1.14 0.02 2 1178 107 107 PRO HB3 H 1.56 0.02 2 1179 107 107 PRO HG2 H 0.82 0.02 2 1180 107 107 PRO HG3 H 0.98 0.02 2 1181 107 107 PRO HD2 H 2.49 0.02 2 1182 107 107 PRO HD3 H 3.54 0.02 2 1183 107 107 PRO C C 174.46 0.20 1 1184 107 107 PRO CA C 62.35 0.10 1 1185 107 107 PRO CB C 33.21 0.10 1 1186 107 107 PRO CG C 26.14 0.10 1 1187 107 107 PRO CD C 50.94 0.10 1 1188 108 108 ILE H H 8.55 0.02 1 1189 108 108 ILE HA H 4.36 0.02 1 1190 108 108 ILE HB H 1.98 0.02 1 1191 108 108 ILE HG12 H 1.30 0.02 2 1192 108 108 ILE HG13 H 1.84 0.02 2 1193 108 108 ILE HG2 H 0.90 0.02 1 1194 108 108 ILE HD1 H 0.67 0.02 1 1195 108 108 ILE C C 176.42 0.20 1 1196 108 108 ILE CA C 60.84 0.10 1 1197 108 108 ILE CB C 38.07 0.10 1 1198 108 108 ILE CG1 C 26.25 0.10 1 1199 108 108 ILE CG2 C 16.84 0.10 1 1200 108 108 ILE CD1 C 10.26 0.10 1 1201 108 108 ILE N N 115.34 0.10 1 1202 109 109 ALA H H 7.88 0.02 1 1203 109 109 ALA HA H 5.21 0.02 1 1204 109 109 ALA HB H 1.55 0.02 1 1205 109 109 ALA C C 174.61 0.20 1 1206 109 109 ALA CA C 50.65 0.10 1 1207 109 109 ALA CB C 23.58 0.10 1 1208 109 109 ALA N N 118.39 0.10 1 1209 110 110 VAL H H 8.72 0.02 1 1210 110 110 VAL HA H 4.49 0.02 1 1211 110 110 VAL HB H 1.60 0.02 1 1212 110 110 VAL HG1 H 0.76 0.02 1 1213 110 110 VAL HG2 H 0.51 0.02 1 1214 110 110 VAL C C 173.68 0.20 1 1215 110 110 VAL CA C 61.78 0.10 1 1216 110 110 VAL CB C 34.70 0.10 1 1217 110 110 VAL CG1 C 21.48 0.10 1 1218 110 110 VAL CG2 C 21.09 0.10 1 1219 110 110 VAL N N 120.59 0.10 1 1220 111 111 GLU H H 9.54 0.02 1 1221 111 111 GLU HA H 4.49 0.02 1 1222 111 111 GLU HB2 H 2.10 0.02 2 1223 111 111 GLU HG2 H 2.34 0.02 2 1224 111 111 GLU HG3 H 2.30 0.02 2 1225 111 111 GLU C C 173.60 0.20 1 1226 111 111 GLU CA C 54.94 0.10 1 1227 111 111 GLU CB C 33.70 0.10 1 1228 111 111 GLU CG C 35.49 0.10 1 1229 111 111 GLU N N 123.51 0.10 1 1230 112 112 ALA H H 6.43 0.02 1 1231 112 112 ALA HA H 5.04 0.02 1 1232 112 112 ALA HB H 1.37 0.02 1 1233 112 112 ALA C C 176.30 0.20 1 1234 112 112 ALA CA C 50.83 0.10 1 1235 112 112 ALA CB C 22.56 0.10 1 1236 112 112 ALA N N 117.64 0.10 1 1237 113 113 LEU H H 8.46 0.02 1 1238 113 113 LEU HA H 3.90 0.02 1 1239 113 113 LEU HG H 1.87 0.02 1 1240 113 113 LEU HD1 H 0.73 0.02 1 1241 113 113 LEU HD2 H 0.88 0.02 1 1242 113 113 LEU C C 173.42 0.20 1 1243 113 113 LEU CA C 55.14 0.10 1 1244 113 113 LEU CB C 44.09 0.20 1 1245 113 113 LEU CG C 25.83 0.10 1 1246 113 113 LEU CD1 C 27.12 0.10 1 1247 113 113 LEU CD2 C 23.96 0.10 1 1248 113 113 LEU N N 122.92 0.10 1 1249 114 114 SER H H 7.46 0.02 1 1250 114 114 SER HA H 4.82 0.02 1 1251 114 114 SER HB2 H 4.17 0.02 2 1252 114 114 SER HB3 H 3.72 0.02 2 1253 114 114 SER C C 171.83 0.20 1 1254 114 114 SER CA C 57.05 0.10 1 1255 114 114 SER CB C 67.60 0.10 1 1256 114 114 SER N N 107.92 0.10 1 1257 115 115 LEU H H 7.28 0.02 1 1258 115 115 LEU HA H 4.50 0.02 1 1259 115 115 LEU HG H 1.29 0.02 1 1260 115 115 LEU HD1 H 0.70 0.02 1 1261 115 115 LEU HD2 H 0.59 0.02 1 1262 115 115 LEU C C 174.04 0.20 1 1263 115 115 LEU CA C 54.33 0.10 1 1264 115 115 LEU CB C 44.29 0.10 1 1265 115 115 LEU CG C 27.40 0.10 1 1266 115 115 LEU CD1 C 23.02 0.10 1 1267 115 115 LEU CD2 C 24.92 0.10 1 1268 115 115 LEU N N 121.96 0.10 1 1269 116 116 ILE H H 8.65 0.02 1 1270 116 116 ILE HA H 5.16 0.02 1 1271 116 116 ILE HB H 1.07 0.02 1 1272 116 116 ILE HG12 H 1.54 0.02 2 1273 116 116 ILE HG13 H 0.86 0.02 2 1274 116 116 ILE HG2 H 0.50 0.02 1 1275 116 116 ILE HD1 H 0.47 0.02 1 1276 116 116 ILE C C 174.43 0.20 1 1277 116 116 ILE CA C 60.03 0.10 1 1278 116 116 ILE CB C 38.62 0.10 1 1279 116 116 ILE CG1 C 27.48 0.10 1 1280 116 116 ILE CG2 C 18.10 0.10 1 1281 116 116 ILE CD1 C 14.10 0.10 1 1282 116 116 ILE N N 129.51 0.10 1 1283 117 117 TYR H H 9.07 0.02 1 1284 117 117 TYR HA H 6.11 0.02 1 1285 117 117 TYR HB2 H 2.62 0.04 2 1286 117 117 TYR C C 172.79 0.20 1 1287 117 117 TYR CA C 54.45 0.10 1 1288 117 117 TYR CB C 42.72 0.10 1 1289 117 117 TYR N N 121.83 0.10 1 1290 118 118 ASN H H 9.30 0.02 1 1291 118 118 ASN HA H 4.56 0.02 1 1292 118 118 ASN HB2 H 2.98 0.02 2 1293 118 118 ASN C C 175.58 0.20 1 1294 118 118 ASN CA C 52.04 0.10 1 1295 118 118 ASN CB C 37.91 0.14 1 1296 118 118 ASN N N 121.11 0.10 1 1297 119 119 LYS H H 8.81 0.02 1 1298 119 119 LYS HA H 4.06 0.02 1 1299 119 119 LYS HB2 H 1.80 0.02 2 1300 119 119 LYS HB3 H 1.41 0.02 2 1301 119 119 LYS HG2 H 1.27 0.02 2 1302 119 119 LYS HG3 H 0.94 0.02 2 1303 119 119 LYS HD2 H 1.32 0.02 2 1304 119 119 LYS HD3 H 1.36 0.02 2 1305 119 119 LYS C C 177.51 0.20 1 1306 119 119 LYS CA C 58.72 0.10 1 1307 119 119 LYS CB C 33.14 0.10 1 1308 119 119 LYS CG C 26.20 0.10 1 1309 119 119 LYS CD C 29.76 0.10 1 1310 119 119 LYS N N 125.41 0.10 1 1311 120 120 ASP H H 8.16 0.02 1 1312 120 120 ASP HA H 4.54 0.02 1 1313 120 120 ASP HB2 H 2.72 0.02 2 1314 120 120 ASP C C 177.52 0.20 1 1315 120 120 ASP CA C 56.29 0.10 1 1316 120 120 ASP CB C 40.53 0.10 1 1317 120 120 ASP N N 115.52 0.10 1 1318 121 121 LEU H H 7.11 0.02 1 1319 121 121 LEU HA H 4.35 0.02 1 1320 121 121 LEU HB2 H 1.33 0.02 2 1321 121 121 LEU HB3 H 1.63 0.02 2 1322 121 121 LEU HG H 1.53 0.02 1 1323 121 121 LEU HD1 H 0.68 0.02 1 1324 121 121 LEU HD2 H 0.79 0.02 1 1325 121 121 LEU C C 176.62 0.20 1 1326 121 121 LEU CA C 55.30 0.10 1 1327 121 121 LEU CB C 44.60 0.10 1 1328 121 121 LEU CG C 26.77 0.10 1 1329 121 121 LEU CD1 C 25.05 0.10 1 1330 121 121 LEU CD2 C 23.08 0.10 1 1331 121 121 LEU N N 117.71 0.10 1 1332 122 122 LEU H H 8.34 0.02 1 1333 122 122 LEU HA H 4.73 0.02 1 1334 122 122 LEU HB2 H 1.92 0.02 2 1335 122 122 LEU HB3 H 1.23 0.02 2 1336 122 122 LEU HG H 1.34 0.02 1 1337 122 122 LEU HD1 H 0.94 0.02 1 1338 122 122 LEU HD2 H 0.96 0.02 1 1339 122 122 LEU CA C 51.66 0.10 1 1340 122 122 LEU CB C 44.57 0.10 1 1341 122 122 LEU CG C 26.81 0.10 1 1342 122 122 LEU CD1 C 25.89 0.10 1 1343 122 122 LEU CD2 C 27.17 0.10 1 1344 122 122 LEU N N 119.82 0.10 1 1345 123 123 PRO HA H 4.43 0.02 1 1346 123 123 PRO HB2 H 1.87 0.02 2 1347 123 123 PRO HB3 H 2.41 0.02 2 1348 123 123 PRO HG2 H 2.01 0.02 2 1349 123 123 PRO HG3 H 2.05 0.02 2 1350 123 123 PRO HD2 H 3.75 0.02 2 1351 123 123 PRO HD3 H 3.37 0.02 2 1352 123 123 PRO C C 177.12 0.20 1 1353 123 123 PRO CA C 64.66 0.10 1 1354 123 123 PRO CB C 32.14 0.10 1 1355 123 123 PRO CG C 27.25 0.10 1 1356 123 123 PRO CD C 49.55 0.10 1 1357 124 124 ASN H H 7.54 0.02 1 1358 124 124 ASN HA H 5.13 0.02 1 1359 124 124 ASN HB2 H 2.52 0.02 1 1360 124 124 ASN HB3 H 2.52 0.02 1 1361 124 124 ASN HD21 H 7.56 0.02 2 1362 124 124 ASN HD22 H 6.84 0.02 2 1363 124 124 ASN CA C 49.52 0.10 1 1364 124 124 ASN CB C 40.03 0.10 1 1365 124 124 ASN N N 112.81 0.10 1 1366 124 124 ASN ND2 N 114.09 0.10 1 1367 125 125 PRO HA H 3.98 0.02 1 1368 125 125 PRO HB2 H 0.80 0.02 2 1369 125 125 PRO HB3 H 1.31 0.02 2 1370 125 125 PRO HG2 H 1.50 0.02 2 1371 125 125 PRO HG3 H 0.85 0.02 2 1372 125 125 PRO HD2 H 2.95 0.02 2 1373 125 125 PRO HD3 H 3.58 0.02 2 1374 125 125 PRO CA C 60.73 0.10 1 1375 125 125 PRO CB C 29.98 0.10 1 1376 125 125 PRO CG C 26.00 0.10 1 1377 125 125 PRO CD C 50.10 0.10 1 1378 126 126 PRO HA H 4.30 0.02 1 1379 126 126 PRO HB2 H 1.91 0.02 2 1380 126 126 PRO HG2 H 1.66 0.02 2 1381 126 126 PRO HG3 H 1.48 0.02 2 1382 126 126 PRO HD2 H 3.31 0.02 2 1383 126 126 PRO HD3 H 3.39 0.02 2 1384 126 126 PRO C C 175.94 0.20 1 1385 126 126 PRO CA C 62.26 0.10 1 1386 126 126 PRO CB C 31.63 0.10 1 1387 126 126 PRO CG C 27.15 0.10 1 1388 126 126 PRO CD C 50.66 0.10 1 1389 127 127 LYS H H 8.15 0.02 1 1390 127 127 LYS HA H 4.14 0.02 1 1391 127 127 LYS HB2 H 1.86 0.02 2 1392 127 127 LYS HB3 H 1.80 0.02 2 1393 127 127 LYS HG2 H 1.45 0.02 2 1394 127 127 LYS HG3 H 1.50 0.04 2 1395 127 127 LYS HD2 H 1.59 0.02 2 1396 127 127 LYS HE2 H 2.94 0.02 2 1397 127 127 LYS C C 177.26 0.20 1 1398 127 127 LYS CA C 56.51 0.10 1 1399 127 127 LYS CB C 33.69 0.10 1 1400 127 127 LYS CG C 25.24 0.10 1 1401 127 127 LYS CD C 28.52 0.10 1 1402 127 127 LYS CE C 42.15 0.10 1 1403 127 127 LYS N N 118.36 0.10 1 1404 128 128 THR H H 7.86 0.02 1 1405 128 128 THR HA H 5.12 0.02 1 1406 128 128 THR HB H 4.82 0.02 1 1407 128 128 THR HG2 H 1.04 0.02 1 1408 128 128 THR C C 174.42 0.20 1 1409 128 128 THR CA C 59.90 0.10 1 1410 128 128 THR CB C 71.78 0.10 1 1411 128 128 THR CG2 C 21.47 0.10 1 1412 128 128 THR N N 108.51 0.10 1 1413 129 129 TRP H H 10.17 0.02 1 1414 129 129 TRP HA H 4.06 0.02 1 1415 129 129 TRP HB2 H 2.89 0.02 2 1416 129 129 TRP HD1 H 6.71 0.02 1 1417 129 129 TRP HE1 H 9.20 0.02 1 1418 129 129 TRP HZ2 H 6.76 0.02 1 1419 129 129 TRP HZ3 H 6.78 0.02 1 1420 129 129 TRP HH2 H 6.63 0.02 1 1421 129 129 TRP C C 179.71 0.20 1 1422 129 129 TRP CA C 60.98 0.10 1 1423 129 129 TRP CB C 28.84 0.10 1 1424 129 129 TRP CD1 C 127.46 0.10 1 1425 129 129 TRP CZ2 C 112.63 0.10 1 1426 129 129 TRP CZ3 C 120.83 0.10 1 1427 129 129 TRP CH2 C 123.93 0.10 1 1428 129 129 TRP N N 123.90 0.10 1 1429 129 129 TRP NE1 N 126.05 0.10 1 1430 130 130 GLU H H 10.59 0.02 1 1431 130 130 GLU HA H 4.15 0.02 1 1432 130 130 GLU HB2 H 2.10 0.02 2 1433 130 130 GLU HG2 H 2.15 0.02 2 1434 130 130 GLU HG3 H 2.75 0.02 2 1435 130 130 GLU C C 178.45 0.20 1 1436 130 130 GLU CA C 61.85 0.10 1 1437 130 130 GLU CB C 28.49 0.10 1 1438 130 130 GLU CG C 38.53 0.10 1 1439 130 130 GLU N N 118.03 0.10 1 1440 131 131 GLU H H 7.59 0.02 1 1441 131 131 GLU HA H 4.40 0.02 1 1442 131 131 GLU HB2 H 2.39 0.02 2 1443 131 131 GLU HB3 H 1.91 0.04 2 1444 131 131 GLU HG2 H 1.98 0.02 2 1445 131 131 GLU HG3 H 2.60 0.04 2 1446 131 131 GLU C C 176.85 0.20 1 1447 131 131 GLU CA C 57.09 0.10 1 1448 131 131 GLU CB C 31.67 0.10 1 1449 131 131 GLU CG C 37.03 0.10 1 1450 131 131 GLU N N 116.60 0.10 1 1451 132 132 ILE H H 8.20 0.02 1 1452 132 132 ILE HA H 3.75 0.02 1 1453 132 132 ILE HB H 2.60 0.02 1 1454 132 132 ILE HG12 H 1.02 0.02 2 1455 132 132 ILE HG13 H 1.98 0.02 2 1456 132 132 ILE HG2 H 0.83 0.02 1 1457 132 132 ILE HD1 H 0.59 0.02 1 1458 132 132 ILE CA C 67.08 0.10 1 1459 132 132 ILE CB C 34.47 0.10 1 1460 132 132 ILE CG1 C 30.75 0.10 1 1461 132 132 ILE CG2 C 16.97 0.10 1 1462 132 132 ILE CD1 C 12.83 0.10 1 1463 132 132 ILE N N 121.45 0.10 1 1464 133 133 PRO HA H 2.90 0.02 1 1465 133 133 PRO HB2 H 1.80 0.02 2 1466 133 133 PRO HB3 H 2.23 0.02 2 1467 133 133 PRO HG2 H 2.23 0.02 2 1468 133 133 PRO HG3 H 1.56 0.02 2 1469 133 133 PRO HD2 H 3.69 0.02 2 1470 133 133 PRO HD3 H 3.98 0.02 2 1471 133 133 PRO C C 177.50 0.20 1 1472 133 133 PRO CA C 67.13 0.10 1 1473 133 133 PRO CB C 30.83 0.10 1 1474 133 133 PRO CG C 28.37 0.10 1 1475 133 133 PRO CD C 49.03 0.10 1 1476 134 134 ALA H H 7.87 0.02 1 1477 134 134 ALA HA H 4.06 0.02 1 1478 134 134 ALA HB H 1.47 0.02 1 1479 134 134 ALA C C 181.09 0.20 1 1480 134 134 ALA CA C 55.23 0.10 1 1481 134 134 ALA CB C 18.24 0.10 1 1482 134 134 ALA N N 118.12 0.10 1 1483 135 135 LEU H H 7.59 0.02 1 1484 135 135 LEU HA H 4.23 0.02 1 1485 135 135 LEU HB2 H 1.58 0.02 2 1486 135 135 LEU HB3 H 1.84 0.02 2 1487 135 135 LEU HG H 1.72 0.02 1 1488 135 135 LEU HD1 H 0.90 0.02 1 1489 135 135 LEU HD2 H 0.91 0.02 1 1490 135 135 LEU C C 179.03 0.20 1 1491 135 135 LEU CA C 57.34 0.10 1 1492 135 135 LEU CB C 42.50 0.10 1 1493 135 135 LEU CG C 26.97 0.10 1 1494 135 135 LEU CD1 C 24.37 0.10 1 1495 135 135 LEU CD2 C 24.43 0.10 1 1496 135 135 LEU N N 119.92 0.10 1 1497 136 136 ASP H H 8.84 0.02 1 1498 136 136 ASP HA H 4.38 0.02 1 1499 136 136 ASP HB2 H 2.59 0.02 2 1500 136 136 ASP C C 177.22 0.20 1 1501 136 136 ASP CA C 59.00 0.10 1 1502 136 136 ASP CB C 42.01 0.10 1 1503 136 136 ASP N N 118.48 0.10 1 1504 137 137 LYS H H 8.04 0.02 1 1505 137 137 LYS HA H 4.08 0.02 1 1506 137 137 LYS HB2 H 2.02 0.02 2 1507 137 137 LYS HG2 H 1.60 0.02 2 1508 137 137 LYS HG3 H 1.80 0.02 2 1509 137 137 LYS HD2 H 1.79 0.02 2 1510 137 137 LYS HE2 H 2.97 0.04 2 1511 137 137 LYS HE3 H 3.07 0.04 2 1512 137 137 LYS C C 179.68 0.20 1 1513 137 137 LYS CA C 60.36 0.10 1 1514 137 137 LYS CB C 32.54 0.10 1 1515 137 137 LYS CG C 25.59 0.10 1 1516 137 137 LYS CD C 29.66 0.10 1 1517 137 137 LYS CE C 42.29 0.10 1 1518 137 137 LYS N N 117.28 0.10 1 1519 138 138 GLU H H 7.48 0.02 1 1520 138 138 GLU HA H 4.13 0.02 1 1521 138 138 GLU HB2 H 2.20 0.02 2 1522 138 138 GLU HB3 H 2.25 0.02 2 1523 138 138 GLU HG2 H 2.26 0.02 2 1524 138 138 GLU HG3 H 2.42 0.02 2 1525 138 138 GLU C C 179.57 0.20 1 1526 138 138 GLU CA C 59.28 0.10 1 1527 138 138 GLU CB C 29.77 0.10 1 1528 138 138 GLU CG C 36.15 0.10 1 1529 138 138 GLU N N 118.58 0.10 1 1530 139 139 LEU H H 8.41 0.02 1 1531 139 139 LEU HA H 4.00 0.02 1 1532 139 139 LEU HB2 H 1.72 0.02 2 1533 139 139 LEU HB3 H 1.11 0.02 2 1534 139 139 LEU HG H 1.77 0.02 1 1535 139 139 LEU HD1 H 0.80 0.02 1 1536 139 139 LEU HD2 H 0.86 0.02 1 1537 139 139 LEU C C 180.48 0.20 1 1538 139 139 LEU CA C 57.96 0.10 1 1539 139 139 LEU CB C 40.84 0.10 1 1540 139 139 LEU CG C 28.04 0.10 1 1541 139 139 LEU CD1 C 26.25 0.10 1 1542 139 139 LEU CD2 C 23.33 0.10 1 1543 139 139 LEU N N 121.25 0.10 1 1544 140 140 LYS H H 9.28 0.02 1 1545 140 140 LYS HA H 4.54 0.02 1 1546 140 140 LYS HB2 H 1.71 0.02 2 1547 140 140 LYS HB3 H 2.16 0.02 2 1548 140 140 LYS HG2 H 1.67 0.02 2 1549 140 140 LYS HG3 H 1.74 0.02 2 1550 140 140 LYS HD2 H 1.68 0.03 2 1551 140 140 LYS HD3 H 1.83 0.02 2 1552 140 140 LYS HE2 H 3.17 0.02 2 1553 140 140 LYS C C 181.40 0.20 1 1554 140 140 LYS CA C 58.82 0.10 1 1555 140 140 LYS CB C 32.33 0.10 1 1556 140 140 LYS CG C 25.86 0.10 1 1557 140 140 LYS CD C 28.67 0.10 1 1558 140 140 LYS CE C 42.77 0.10 1 1559 140 140 LYS N N 124.17 0.10 1 1560 141 141 ALA H H 7.25 0.02 1 1561 141 141 ALA HA H 4.33 0.02 1 1562 141 141 ALA HB H 1.59 0.02 1 1563 141 141 ALA C C 178.43 0.20 1 1564 141 141 ALA CA C 54.37 0.10 1 1565 141 141 ALA CB C 18.09 0.10 1 1566 141 141 ALA N N 122.00 0.10 1 1567 142 142 LYS H H 7.63 0.02 1 1568 142 142 LYS HA H 4.62 0.02 1 1569 142 142 LYS HB2 H 1.84 0.02 2 1570 142 142 LYS HB3 H 2.13 0.02 2 1571 142 142 LYS HG2 H 1.51 0.02 2 1572 142 142 LYS HD2 H 1.72 0.02 2 1573 142 142 LYS HD3 H 1.66 0.02 2 1574 142 142 LYS C C 176.56 0.20 1 1575 142 142 LYS CA C 54.93 0.10 1 1576 142 142 LYS CB C 32.78 0.10 1 1577 142 142 LYS CG C 24.87 0.10 1 1578 142 142 LYS CD C 29.52 0.10 1 1579 142 142 LYS N N 115.69 0.10 1 1580 143 143 GLY H H 7.87 0.02 1 1581 143 143 GLY HA2 H 3.87 0.02 2 1582 143 143 GLY HA3 H 4.17 0.02 2 1583 143 143 GLY C C 174.19 0.20 1 1584 143 143 GLY CA C 46.12 0.10 1 1585 143 143 GLY N N 107.62 0.10 1 1586 144 144 LYS H H 7.86 0.02 1 1587 144 144 LYS HA H 4.98 0.02 1 1588 144 144 LYS HB2 H 1.68 0.02 2 1589 144 144 LYS HG2 H 1.32 0.02 2 1590 144 144 LYS HD2 H 1.76 0.02 2 1591 144 144 LYS HD3 H 1.60 0.02 2 1592 144 144 LYS HE2 H 3.03 0.02 2 1593 144 144 LYS HE3 H 2.94 0.04 2 1594 144 144 LYS C C 173.61 0.20 1 1595 144 144 LYS CA C 53.20 0.10 1 1596 144 144 LYS CB C 35.73 0.10 1 1597 144 144 LYS CG C 24.93 0.10 1 1598 144 144 LYS CD C 28.38 0.10 1 1599 144 144 LYS CE C 42.81 0.10 1 1600 144 144 LYS N N 119.74 0.10 1 1601 145 145 SER H H 7.55 0.02 1 1602 145 145 SER HA H 4.98 0.02 1 1603 145 145 SER HB2 H 3.99 0.02 2 1604 145 145 SER HB3 H 4.15 0.02 2 1605 145 145 SER C C 174.48 0.20 1 1606 145 145 SER CA C 56.50 0.10 1 1607 145 145 SER CB C 66.63 0.10 1 1608 145 145 SER N N 109.31 0.10 1 1609 146 146 ALA H H 9.55 0.02 1 1610 146 146 ALA HA H 4.24 0.02 1 1611 146 146 ALA HB H 1.32 0.02 1 1612 146 146 ALA C C 175.74 0.20 1 1613 146 146 ALA CA C 55.70 0.10 1 1614 146 146 ALA CB C 18.31 0.10 1 1615 146 146 ALA N N 122.70 0.10 1 1616 147 147 LEU H H 8.71 0.02 1 1617 147 147 LEU HA H 5.07 0.02 1 1618 147 147 LEU HB2 H 1.12 0.02 2 1619 147 147 LEU HB3 H 1.65 0.02 2 1620 147 147 LEU HG H 1.59 0.02 1 1621 147 147 LEU HD1 H 0.70 0.02 1 1622 147 147 LEU HD2 H 0.96 0.02 1 1623 147 147 LEU C C 174.96 0.20 1 1624 147 147 LEU CA C 54.29 0.10 1 1625 147 147 LEU CB C 46.07 0.10 1 1626 147 147 LEU CG C 28.19 0.12 1 1627 147 147 LEU CD1 C 22.82 0.10 1 1628 147 147 LEU CD2 C 27.91 0.10 1 1629 147 147 LEU N N 116.74 0.10 1 1630 148 148 MET H H 8.20 0.02 1 1631 148 148 MET HA H 4.96 0.02 1 1632 148 148 MET HB2 H 1.92 0.02 2 1633 148 148 MET HB3 H 2.13 0.02 2 1634 148 148 MET HG2 H 2.69 0.02 2 1635 148 148 MET HE H 2.02 0.02 1 1636 148 148 MET C C 174.09 0.20 1 1637 148 148 MET CA C 55.74 0.10 1 1638 148 148 MET CB C 38.26 0.10 1 1639 148 148 MET CG C 32.39 0.10 1 1640 148 148 MET CE C 17.59 0.10 1 1641 148 148 MET N N 121.65 0.10 1 1642 149 149 PHE H H 8.61 0.02 1 1643 149 149 PHE HA H 4.84 0.02 1 1644 149 149 PHE HD1 H 7.13 0.02 1 1645 149 149 PHE HD2 H 7.13 0.02 1 1646 149 149 PHE HE1 H 7.28 0.02 1 1647 149 149 PHE HE2 H 7.28 0.02 1 1648 149 149 PHE HZ H 7.04 0.02 1 1649 149 149 PHE C C 171.43 0.20 1 1650 149 149 PHE CA C 55.65 0.10 1 1651 149 149 PHE CD1 C 132.86 0.10 1 1652 149 149 PHE CD2 C 132.86 0.10 1 1653 149 149 PHE CE1 C 131.50 0.10 1 1654 149 149 PHE CE2 C 131.50 0.10 1 1655 149 149 PHE CZ C 128.69 0.10 1 1656 149 149 PHE N N 120.09 0.10 1 1657 150 150 ASN H H 8.72 0.02 1 1658 150 150 ASN HA H 3.76 0.02 1 1659 150 150 ASN HB2 H 1.84 0.02 2 1660 150 150 ASN HB3 H 2.19 0.02 2 1661 150 150 ASN C C 172.48 0.20 1 1662 150 150 ASN CA C 53.36 0.10 1 1663 150 150 ASN CB C 37.38 0.10 1 1664 150 150 ASN N N 116.06 0.10 1 1665 151 151 LEU H H 7.31 0.02 1 1666 151 151 LEU HA H 4.05 0.02 1 1667 151 151 LEU HB2 H 1.29 0.02 2 1668 151 151 LEU HB3 H 1.57 0.02 2 1669 151 151 LEU HG H 1.47 0.02 1 1670 151 151 LEU HD1 H 0.77 0.02 1 1671 151 151 LEU HD2 H 0.12 0.02 1 1672 151 151 LEU C C 177.99 0.20 1 1673 151 151 LEU CA C 54.31 0.10 1 1674 151 151 LEU CB C 42.30 0.10 1 1675 151 151 LEU CG C 26.47 0.10 1 1676 151 151 LEU CD1 C 26.55 0.10 1 1677 151 151 LEU CD2 C 23.81 0.10 1 1678 151 151 LEU N N 122.75 0.10 1 1679 152 152 GLN H H 7.97 0.02 1 1680 152 152 GLN HA H 4.09 0.02 1 1681 152 152 GLN HB2 H 2.49 0.02 2 1682 152 152 GLN HB3 H 2.13 0.02 2 1683 152 152 GLN HG2 H 2.51 0.02 2 1684 152 152 GLN HE21 H 6.99 0.02 2 1685 152 152 GLN HE22 H 6.86 0.02 2 1686 152 152 GLN C C 175.99 0.20 1 1687 152 152 GLN CA C 55.52 0.10 1 1688 152 152 GLN CB C 28.76 0.10 1 1689 152 152 GLN CG C 33.22 0.10 1 1690 152 152 GLN N N 113.03 0.10 1 1691 152 152 GLN NE2 N 114.10 0.10 1 1692 153 153 GLU H H 6.44 0.02 1 1693 153 153 GLU HA H 5.23 0.02 1 1694 153 153 GLU HB2 H 2.02 0.04 2 1695 153 153 GLU HB3 H 2.33 0.04 2 1696 153 153 GLU HG2 H 2.33 0.02 2 1697 153 153 GLU HG3 H 2.43 0.04 2 1698 153 153 GLU CA C 51.27 0.10 1 1699 153 153 GLU CB C 33.49 0.10 1 1700 153 153 GLU CG C 36.15 0.10 1 1701 153 153 GLU N N 113.64 0.10 1 1702 154 154 PRO HA H 4.96 0.02 1 1703 154 154 PRO HB2 H 2.26 0.02 2 1704 154 154 PRO HB3 H 2.31 0.02 2 1705 154 154 PRO HG2 H 2.52 0.02 2 1706 154 154 PRO HG3 H 2.60 0.02 2 1707 154 154 PRO C C 176.64 0.20 1 1708 154 154 PRO CA C 63.49 0.10 1 1709 154 154 PRO CB C 32.53 0.10 1 1710 154 154 PRO CG C 28.07 0.10 1 1711 154 154 PRO CD C 51.28 0.10 1 1712 155 155 TYR H H 7.95 0.02 1 1713 155 155 TYR HA H 4.48 0.02 1 1714 155 155 TYR HB2 H 2.60 0.02 2 1715 155 155 TYR HB3 H 3.46 0.02 2 1716 155 155 TYR C C 175.61 0.20 1 1717 155 155 TYR CA C 62.59 0.10 1 1718 155 155 TYR CB C 40.47 0.10 1 1719 155 155 TYR N N 117.73 0.10 1 1720 156 156 PHE H H 8.05 0.02 1 1721 156 156 PHE HA H 4.48 0.02 1 1722 156 156 PHE HB2 H 3.59 0.02 2 1723 156 156 PHE HB3 H 3.99 0.02 2 1724 156 156 PHE HD1 H 7.64 0.02 1 1725 156 156 PHE HD2 H 7.64 0.02 1 1726 156 156 PHE C C 175.91 0.20 1 1727 156 156 PHE CA C 60.58 0.10 1 1728 156 156 PHE CB C 41.91 0.13 1 1729 156 156 PHE CD1 C 132.63 0.10 1 1730 156 156 PHE CD2 C 132.63 0.10 1 1731 156 156 PHE N N 111.86 0.10 1 1732 157 157 THR H H 7.58 0.02 1 1733 157 157 THR HA H 4.44 0.02 1 1734 157 157 THR HB H 4.27 0.02 1 1735 157 157 THR HG2 H 1.43 0.02 1 1736 157 157 THR C C 175.83 0.20 1 1737 157 157 THR CA C 62.85 0.10 1 1738 157 157 THR CB C 69.33 0.10 1 1739 157 157 THR CG2 C 24.46 0.10 1 1740 157 157 THR N N 105.66 0.10 1 1741 158 158 TRP H H 8.39 0.02 1 1742 158 158 TRP HA H 4.48 0.02 1 1743 158 158 TRP HB2 H 3.73 0.02 2 1744 158 158 TRP HB3 H 2.83 0.02 2 1745 158 158 TRP HD1 H 5.98 0.02 1 1746 158 158 TRP HE1 H 9.60 0.02 1 1747 158 158 TRP HE3 H 7.29 0.02 1 1748 158 158 TRP HZ2 H 6.99 0.02 1 1749 158 158 TRP HZ3 H 6.72 0.02 1 1750 158 158 TRP HH2 H 6.78 0.02 1 1751 158 158 TRP CA C 60.71 0.10 1 1752 158 158 TRP CB C 28.79 0.10 1 1753 158 158 TRP CD1 C 128.39 0.10 1 1754 158 158 TRP CE3 C 118.85 0.10 1 1755 158 158 TRP CZ2 C 114.30 0.10 1 1756 158 158 TRP CZ3 C 120.47 0.10 1 1757 158 158 TRP CH2 C 122.10 0.10 1 1758 158 158 TRP N N 124.17 0.10 1 1759 158 158 TRP NE1 N 130.99 0.10 1 1760 159 159 PRO HA H 3.87 0.02 1 1761 159 159 PRO HB2 H 1.68 0.04 2 1762 159 159 PRO HB3 H 1.72 0.02 2 1763 159 159 PRO HD2 H 3.65 0.02 2 1764 159 159 PRO C C 177.94 0.20 1 1765 159 159 PRO CA C 65.77 0.10 1 1766 159 159 PRO CB C 30.48 0.10 1 1767 159 159 PRO CD C 49.64 0.10 1 1768 160 160 LEU H H 6.40 0.02 1 1769 160 160 LEU HA H 3.72 0.02 1 1770 160 160 LEU HB2 H 0.50 0.02 2 1771 160 160 LEU HB3 H 1.08 0.02 2 1772 160 160 LEU HG H 0.54 0.02 1 1773 160 160 LEU HD1 H -1.02 0.02 1 1774 160 160 LEU HD2 H -0.27 0.02 1 1775 160 160 LEU C C 176.56 0.20 1 1776 160 160 LEU CA C 55.89 0.10 1 1777 160 160 LEU CB C 42.70 0.10 1 1778 160 160 LEU CG C 26.27 0.10 1 1779 160 160 LEU CD1 C 19.72 0.10 1 1780 160 160 LEU CD2 C 25.48 0.10 1 1781 160 160 LEU N N 111.32 0.10 1 1782 161 161 ILE H H 6.98 0.02 1 1783 161 161 ILE HA H 2.94 0.02 1 1784 161 161 ILE HB H 1.19 0.02 1 1785 161 161 ILE HG12 H 0.58 0.02 2 1786 161 161 ILE HG13 H 1.53 0.02 2 1787 161 161 ILE HG2 H 0.54 0.02 1 1788 161 161 ILE HD1 H 0.79 0.02 1 1789 161 161 ILE C C 175.38 0.20 1 1790 161 161 ILE CA C 65.79 0.10 1 1791 161 161 ILE CB C 37.91 0.10 1 1792 161 161 ILE CG1 C 29.05 0.10 1 1793 161 161 ILE CG2 C 16.86 0.10 1 1794 161 161 ILE CD1 C 13.69 0.10 1 1795 161 161 ILE N N 119.26 0.10 1 1796 162 162 ALA H H 8.01 0.02 1 1797 162 162 ALA HA H 3.46 0.02 1 1798 162 162 ALA HB H 0.34 0.02 1 1799 162 162 ALA C C 179.39 0.20 1 1800 162 162 ALA CA C 52.30 0.10 1 1801 162 162 ALA CB C 18.68 0.10 1 1802 162 162 ALA N N 114.94 0.10 1 1803 163 163 ALA H H 6.63 0.02 1 1804 163 163 ALA HA H 4.02 0.02 1 1805 163 163 ALA HB H 1.58 0.02 1 1806 163 163 ALA C C 178.15 0.20 1 1807 163 163 ALA CA C 56.37 0.10 1 1808 163 163 ALA CB C 20.18 0.10 1 1809 163 163 ALA N N 120.63 0.10 1 1810 164 164 ASP H H 9.62 0.02 1 1811 164 164 ASP HA H 4.97 0.02 1 1812 164 164 ASP HB2 H 2.14 0.02 2 1813 164 164 ASP HB3 H 2.84 0.02 2 1814 164 164 ASP C C 176.38 0.20 1 1815 164 164 ASP CA C 53.31 0.10 1 1816 164 164 ASP CB C 42.62 0.10 1 1817 164 164 ASP N N 114.85 0.10 1 1818 165 165 GLY H H 7.50 0.02 1 1819 165 165 GLY HA2 H 3.79 0.02 2 1820 165 165 GLY HA3 H 4.54 0.02 2 1821 165 165 GLY C C 175.60 0.20 1 1822 165 165 GLY CA C 45.72 0.10 1 1823 165 165 GLY N N 103.56 0.10 1 1824 166 166 GLY H H 7.42 0.02 1 1825 166 166 GLY HA2 H 3.12 0.02 2 1826 166 166 GLY HA3 H 4.63 0.02 2 1827 166 166 GLY C C 172.05 0.20 1 1828 166 166 GLY CA C 45.35 0.10 1 1829 166 166 GLY N N 107.97 0.10 1 1830 167 167 TYR H H 8.27 0.02 1 1831 167 167 TYR HA H 5.42 0.02 1 1832 167 167 TYR HB2 H 2.98 0.02 2 1833 167 167 TYR HB3 H 3.34 0.02 2 1834 167 167 TYR HE1 H 6.70 0.02 1 1835 167 167 TYR HE2 H 6.70 0.02 1 1836 167 167 TYR C C 173.28 0.20 1 1837 167 167 TYR CA C 57.55 0.10 1 1838 167 167 TYR CB C 39.37 0.10 1 1839 167 167 TYR CE1 C 117.92 0.10 1 1840 167 167 TYR CE2 C 117.92 0.10 1 1841 167 167 TYR N N 115.29 0.10 1 1842 168 168 ALA H H 10.65 0.02 1 1843 168 168 ALA HA H 4.20 0.02 1 1844 168 168 ALA HB H 0.48 0.02 1 1845 168 168 ALA C C 172.95 0.20 1 1846 168 168 ALA CA C 53.31 0.10 1 1847 168 168 ALA CB C 16.96 0.10 1 1848 168 168 ALA N N 124.50 0.10 1 1849 169 169 PHE H H 6.29 0.02 1 1850 169 169 PHE HA H 5.53 0.02 1 1851 169 169 PHE HB2 H 2.44 0.02 2 1852 169 169 PHE HB3 H 3.14 0.02 2 1853 169 169 PHE HD1 H 7.00 0.02 1 1854 169 169 PHE HD2 H 7.00 0.02 1 1855 169 169 PHE HE1 H 6.99 0.02 1 1856 169 169 PHE HE2 H 6.99 0.02 1 1857 169 169 PHE HZ H 6.87 0.02 1 1858 169 169 PHE C C 176.52 0.20 1 1859 169 169 PHE CA C 55.50 0.10 1 1860 169 169 PHE CB C 43.20 0.10 1 1861 169 169 PHE CD1 C 132.69 0.10 1 1862 169 169 PHE CD2 C 132.69 0.10 1 1863 169 169 PHE CE1 C 130.64 0.10 1 1864 169 169 PHE CE2 C 130.64 0.10 1 1865 169 169 PHE CZ C 128.96 0.10 1 1866 169 169 PHE N N 107.55 0.10 1 1867 170 170 LYS H H 8.88 0.02 1 1868 170 170 LYS HA H 3.99 0.02 1 1869 170 170 LYS HB2 H 1.77 0.02 2 1870 170 170 LYS HB3 H 2.08 0.02 2 1871 170 170 LYS HG2 H 1.18 0.02 2 1872 170 170 LYS HG3 H 1.44 0.02 2 1873 170 170 LYS HD2 H 1.51 0.02 2 1874 170 170 LYS HD3 H 1.43 0.02 2 1875 170 170 LYS HE2 H 2.69 0.02 2 1876 170 170 LYS C C 174.51 0.20 1 1877 170 170 LYS CA C 56.95 0.10 1 1878 170 170 LYS CB C 32.91 0.10 1 1879 170 170 LYS CG C 24.05 0.10 1 1880 170 170 LYS CD C 27.74 0.10 1 1881 170 170 LYS CE C 41.56 0.10 1 1882 170 170 LYS N N 125.58 0.10 1 1883 171 171 TYR H H 8.64 0.02 1 1884 171 171 TYR HA H 4.81 0.02 1 1885 171 171 TYR HB2 H 2.70 0.02 2 1886 171 171 TYR HB3 H 2.93 0.02 2 1887 171 171 TYR HD1 H 6.00 0.02 1 1888 171 171 TYR HD2 H 6.00 0.02 1 1889 171 171 TYR HE1 H 6.41 0.02 1 1890 171 171 TYR HE2 H 6.41 0.02 1 1891 171 171 TYR C C 174.76 0.20 1 1892 171 171 TYR CA C 56.24 0.10 1 1893 171 171 TYR CB C 40.20 0.10 1 1894 171 171 TYR CD1 C 133.05 0.10 1 1895 171 171 TYR CD2 C 133.05 0.10 1 1896 171 171 TYR CE1 C 117.38 0.10 1 1897 171 171 TYR CE2 C 117.38 0.10 1 1898 171 171 TYR N N 129.91 0.10 1 1899 172 172 GLU H H 8.23 0.02 1 1900 172 172 GLU HA H 4.22 0.02 1 1901 172 172 GLU HB2 H 1.81 0.02 2 1902 172 172 GLU HG2 H 2.08 0.02 2 1903 172 172 GLU CA C 55.70 0.10 1 1904 172 172 GLU CB C 32.95 0.10 1 1905 172 172 GLU CG C 36.20 0.10 1 1906 172 172 GLU N N 126.69 0.10 1 1907 173 173 ASN HA H 4.19 0.02 1 1908 173 173 ASN HB2 H 2.62 0.02 1 1909 173 173 ASN HB3 H 2.91 0.02 1 1910 173 173 ASN HD21 H 7.59 0.02 2 1911 173 173 ASN HD22 H 6.85 0.02 2 1912 173 173 ASN C C 175.33 0.20 1 1913 173 173 ASN CA C 53.97 0.10 1 1914 173 173 ASN CB C 37.35 0.10 1 1915 173 173 ASN ND2 N 113.49 0.10 1 1916 174 174 GLY H H 7.52 0.02 1 1917 174 174 GLY HA2 H 3.50 0.02 2 1918 174 174 GLY HA3 H 3.86 0.02 2 1919 174 174 GLY C C 173.08 0.20 1 1920 174 174 GLY CA C 45.69 0.10 1 1921 174 174 GLY N N 101.91 0.10 1 1922 175 175 LYS H H 7.07 0.02 1 1923 175 175 LYS HA H 4.63 0.02 1 1924 175 175 LYS HB2 H 1.66 0.03 2 1925 175 175 LYS HB3 H 1.74 0.02 2 1926 175 175 LYS HG2 H 1.24 0.02 2 1927 175 175 LYS HD2 H 1.60 0.02 2 1928 175 175 LYS HE2 H 2.94 0.02 2 1929 175 175 LYS C C 174.56 0.20 1 1930 175 175 LYS CA C 54.47 0.10 1 1931 175 175 LYS CB C 35.90 0.10 1 1932 175 175 LYS CG C 23.82 0.10 1 1933 175 175 LYS CD C 29.25 0.10 1 1934 175 175 LYS CE C 42.20 0.10 1 1935 175 175 LYS N N 118.28 0.10 1 1936 176 176 TYR H H 8.76 0.02 1 1937 176 176 TYR HA H 5.29 0.02 1 1938 176 176 TYR HB2 H 2.58 0.02 2 1939 176 176 TYR HB3 H 2.83 0.02 2 1940 176 176 TYR HD1 H 7.30 0.02 1 1941 176 176 TYR HD2 H 7.30 0.02 1 1942 176 176 TYR HE1 H 7.08 0.02 1 1943 176 176 TYR HE2 H 7.08 0.02 1 1944 176 176 TYR C C 176.16 0.20 1 1945 176 176 TYR CA C 58.80 0.10 1 1946 176 176 TYR CB C 40.22 0.10 1 1947 176 176 TYR CD1 C 133.97 0.10 1 1948 176 176 TYR CD2 C 133.97 0.10 1 1949 176 176 TYR CE1 C 118.20 0.10 1 1950 176 176 TYR CE2 C 118.20 0.10 1 1951 176 176 TYR N N 119.86 0.10 1 1952 177 177 ASP H H 8.98 0.02 1 1953 177 177 ASP HA H 4.86 0.02 1 1954 177 177 ASP HB2 H 2.68 0.02 2 1955 177 177 ASP HB3 H 3.20 0.04 2 1956 177 177 ASP C C 177.38 0.20 1 1957 177 177 ASP CA C 52.73 0.10 1 1958 177 177 ASP CB C 41.49 0.10 1 1959 177 177 ASP N N 123.68 0.10 1 1960 178 178 ILE H H 7.76 0.02 1 1961 178 178 ILE HA H 4.22 0.02 1 1962 178 178 ILE HB H 2.02 0.02 1 1963 178 178 ILE HG12 H 1.33 0.02 2 1964 178 178 ILE HG13 H 1.27 0.02 2 1965 178 178 ILE HG2 H 0.69 0.02 1 1966 178 178 ILE HD1 H 0.89 0.02 1 1967 178 178 ILE C C 175.68 0.20 1 1968 178 178 ILE CA C 63.64 0.10 1 1969 178 178 ILE CB C 37.25 0.10 1 1970 178 178 ILE CG1 C 25.95 0.10 1 1971 178 178 ILE CG2 C 18.36 0.10 1 1972 178 178 ILE CD1 C 14.33 0.10 1 1973 178 178 ILE N N 116.83 0.10 1 1974 179 179 LYS H H 8.30 0.02 1 1975 179 179 LYS HA H 4.61 0.02 1 1976 179 179 LYS HB2 H 2.06 0.03 2 1977 179 179 LYS HG2 H 1.46 0.03 2 1978 179 179 LYS HG3 H 1.58 0.02 2 1979 179 179 LYS HD2 H 1.75 0.02 2 1980 179 179 LYS C C 176.35 0.20 1 1981 179 179 LYS CA C 54.53 0.10 1 1982 179 179 LYS CB C 32.45 0.10 1 1983 179 179 LYS CG C 24.85 0.10 1 1984 179 179 LYS CD C 28.55 0.10 1 1985 179 179 LYS N N 115.93 0.10 1 1986 180 180 ASP H H 7.76 0.02 1 1987 180 180 ASP HA H 4.89 0.02 1 1988 180 180 ASP HB2 H 2.35 0.02 2 1989 180 180 ASP HB3 H 3.20 0.02 2 1990 180 180 ASP C C 172.87 0.20 1 1991 180 180 ASP CA C 53.15 0.10 1 1992 180 180 ASP CB C 41.14 0.10 1 1993 180 180 ASP N N 123.13 0.10 1 1994 181 181 VAL H H 7.50 0.02 1 1995 181 181 VAL HA H 4.97 0.02 1 1996 181 181 VAL HB H 1.71 0.02 1 1997 181 181 VAL HG1 H 0.83 0.02 1 1998 181 181 VAL HG2 H 0.71 0.02 1 1999 181 181 VAL C C 176.70 0.20 1 2000 181 181 VAL CA C 59.21 0.10 1 2001 181 181 VAL CB C 35.22 0.10 1 2002 181 181 VAL CG1 C 21.78 0.10 1 2003 181 181 VAL CG2 C 22.98 0.10 1 2004 181 181 VAL N N 122.94 0.10 1 2005 182 182 GLY H H 7.05 0.02 1 2006 182 182 GLY HA2 H 3.96 0.02 2 2007 182 182 GLY HA3 H 1.50 0.02 2 2008 182 182 GLY C C 173.95 0.20 1 2009 182 182 GLY CA C 46.39 0.10 1 2010 182 182 GLY N N 120.92 0.10 1 2011 183 183 VAL H H 6.71 0.02 1 2012 183 183 VAL HA H 4.06 0.02 1 2013 183 183 VAL HB H 2.06 0.02 1 2014 183 183 VAL HG1 H 0.88 0.02 1 2015 183 183 VAL HG2 H 0.85 0.02 1 2016 183 183 VAL C C 173.10 0.20 1 2017 183 183 VAL CA C 63.33 0.10 1 2018 183 183 VAL CB C 32.97 0.10 1 2019 183 183 VAL CG1 C 22.76 0.10 1 2020 183 183 VAL CG2 C 22.82 0.10 1 2021 183 183 VAL N N 113.93 0.10 1 2022 184 184 ASP H H 7.84 0.02 1 2023 184 184 ASP HA H 4.78 0.02 1 2024 184 184 ASP HB2 H 2.39 0.02 2 2025 184 184 ASP HB3 H 2.35 0.02 2 2026 184 184 ASP C C 176.10 0.20 1 2027 184 184 ASP CA C 51.43 0.10 1 2028 184 184 ASP CB C 40.04 0.10 1 2029 184 184 ASP N N 114.59 0.10 1 2030 185 185 ASN H H 6.87 0.02 1 2031 185 185 ASN HA H 4.59 0.02 1 2032 185 185 ASN HB2 H 2.82 0.02 2 2033 185 185 ASN HB3 H 3.11 0.02 2 2034 185 185 ASN HD21 H 7.36 0.02 2 2035 185 185 ASN HD22 H 6.43 0.02 2 2036 185 185 ASN C C 174.66 0.20 1 2037 185 185 ASN CA C 51.48 0.10 1 2038 185 185 ASN CB C 39.35 0.10 1 2039 185 185 ASN N N 116.12 0.10 1 2040 185 185 ASN ND2 N 109.64 0.10 1 2041 186 186 ALA H H 8.52 0.02 1 2042 186 186 ALA HA H 3.94 0.02 1 2043 186 186 ALA HB H 1.44 0.02 1 2044 186 186 ALA C C 180.34 0.20 1 2045 186 186 ALA CA C 55.50 0.10 1 2046 186 186 ALA CB C 18.55 0.10 1 2047 186 186 ALA N N 120.37 0.10 1 2048 187 187 GLY H H 8.38 0.02 1 2049 187 187 GLY HA2 H 3.41 0.02 2 2050 187 187 GLY HA3 H 3.99 0.02 2 2051 187 187 GLY C C 175.80 0.20 1 2052 187 187 GLY CA C 47.31 0.10 1 2053 187 187 GLY N N 109.38 0.10 1 2054 188 188 ALA H H 8.06 0.02 1 2055 188 188 ALA HA H 4.72 0.02 1 2056 188 188 ALA HB H 1.24 0.02 1 2057 188 188 ALA C C 180.66 0.20 1 2058 188 188 ALA CA C 53.84 0.10 1 2059 188 188 ALA CB C 18.66 0.10 1 2060 188 188 ALA N N 127.63 0.10 1 2061 189 189 LYS H H 7.99 0.02 1 2062 189 189 LYS HA H 3.68 0.02 1 2063 189 189 LYS HB2 H 1.81 0.02 2 2064 189 189 LYS HG2 H 1.22 0.02 2 2065 189 189 LYS HG3 H 1.47 0.02 2 2066 189 189 LYS HD2 H 1.49 0.02 2 2067 189 189 LYS HD3 H 1.72 0.04 2 2068 189 189 LYS HE2 H 2.86 0.02 2 2069 189 189 LYS C C 180.15 0.20 1 2070 189 189 LYS CA C 59.66 0.10 1 2071 189 189 LYS CB C 32.39 0.10 1 2072 189 189 LYS CG C 26.93 0.10 1 2073 189 189 LYS CD C 29.79 0.10 1 2074 189 189 LYS CE C 42.37 0.10 1 2075 189 189 LYS N N 115.12 0.10 1 2076 190 190 ALA H H 8.22 0.02 1 2077 190 190 ALA HA H 4.23 0.02 1 2078 190 190 ALA HB H 1.77 0.02 1 2079 190 190 ALA C C 181.18 0.20 1 2080 190 190 ALA CA C 55.72 0.10 1 2081 190 190 ALA CB C 18.22 0.10 1 2082 190 190 ALA N N 124.58 0.10 1 2083 191 191 GLY H H 8.24 0.02 1 2084 191 191 GLY HA2 H 3.58 0.04 2 2085 191 191 GLY HA3 H 3.14 0.02 2 2086 191 191 GLY C C 174.89 0.20 1 2087 191 191 GLY CA C 47.92 0.10 1 2088 191 191 GLY N N 107.59 0.10 1 2089 192 192 LEU H H 8.69 0.02 1 2090 192 192 LEU HA H 4.14 0.02 1 2091 192 192 LEU HB2 H 1.98 0.02 2 2092 192 192 LEU HB3 H 1.27 0.04 2 2093 192 192 LEU HD1 H 1.10 0.02 1 2094 192 192 LEU HD2 H 0.87 0.02 1 2095 192 192 LEU C C 178.22 0.20 1 2096 192 192 LEU CA C 57.22 0.10 1 2097 192 192 LEU CB C 40.64 0.10 1 2098 192 192 LEU CG C 26.98 0.20 1 2099 192 192 LEU CD1 C 24.60 0.10 1 2100 192 192 LEU CD2 C 25.61 0.10 1 2101 192 192 LEU N N 121.13 0.10 1 2102 193 193 THR H H 8.53 0.02 1 2103 193 193 THR HA H 3.79 0.02 1 2104 193 193 THR HB H 4.42 0.02 1 2105 193 193 THR HG2 H 1.29 0.02 1 2106 193 193 THR C C 175.04 0.20 1 2107 193 193 THR CA C 68.06 0.10 1 2108 193 193 THR CB C 68.64 0.10 1 2109 193 193 THR CG2 C 21.14 0.10 1 2110 193 193 THR N N 116.36 0.10 1 2111 194 194 PHE H H 7.66 0.02 1 2112 194 194 PHE HA H 4.21 0.02 1 2113 194 194 PHE HB2 H 2.72 0.02 2 2114 194 194 PHE HB3 H 3.15 0.02 2 2115 194 194 PHE HD1 H 7.13 0.02 1 2116 194 194 PHE HD2 H 7.13 0.02 1 2117 194 194 PHE HE1 H 7.51 0.02 1 2118 194 194 PHE HE2 H 7.51 0.02 1 2119 194 194 PHE HZ H 7.46 0.02 1 2120 194 194 PHE C C 177.33 0.20 1 2121 194 194 PHE CA C 62.33 0.10 1 2122 194 194 PHE CB C 39.49 0.10 1 2123 194 194 PHE CD1 C 132.69 0.10 1 2124 194 194 PHE CD2 C 132.69 0.10 1 2125 194 194 PHE CE1 C 131.14 0.10 1 2126 194 194 PHE CE2 C 131.14 0.10 1 2127 194 194 PHE CZ C 129.41 0.10 1 2128 194 194 PHE N N 121.93 0.10 1 2129 195 195 LEU H H 7.74 0.02 1 2130 195 195 LEU HA H 3.77 0.02 1 2131 195 195 LEU HB2 H 1.49 0.02 2 2132 195 195 LEU HB3 H 2.07 0.02 2 2133 195 195 LEU HG H 1.54 0.02 1 2134 195 195 LEU HD1 H 0.91 0.02 1 2135 195 195 LEU HD2 H 0.87 0.02 1 2136 195 195 LEU C C 177.89 0.20 1 2137 195 195 LEU CA C 58.70 0.10 1 2138 195 195 LEU CB C 41.75 0.10 1 2139 195 195 LEU CG C 27.29 0.10 1 2140 195 195 LEU CD1 C 24.05 0.10 1 2141 195 195 LEU CD2 C 25.49 0.10 1 2142 195 195 LEU N N 119.51 0.10 1 2143 196 196 VAL H H 8.61 0.02 1 2144 196 196 VAL HA H 3.47 0.02 1 2145 196 196 VAL HB H 2.21 0.02 1 2146 196 196 VAL HG1 H 0.97 0.02 1 2147 196 196 VAL HG2 H 0.87 0.02 1 2148 196 196 VAL C C 178.27 0.20 1 2149 196 196 VAL CA C 67.28 0.10 1 2150 196 196 VAL CB C 31.16 0.10 1 2151 196 196 VAL CG1 C 21.92 0.10 1 2152 196 196 VAL CG2 C 23.70 0.10 1 2153 196 196 VAL N N 117.47 0.10 1 2154 197 197 ASP H H 8.59 0.02 1 2155 197 197 ASP HA H 4.49 0.02 1 2156 197 197 ASP HB2 H 2.44 0.02 2 2157 197 197 ASP HB3 H 2.73 0.02 2 2158 197 197 ASP C C 179.08 0.20 1 2159 197 197 ASP CA C 57.93 0.10 1 2160 197 197 ASP CB C 39.95 0.10 1 2161 197 197 ASP N N 122.89 0.10 1 2162 198 198 LEU H H 7.87 0.02 1 2163 198 198 LEU HA H 4.16 0.02 1 2164 198 198 LEU HB2 H 2.52 0.02 2 2165 198 198 LEU HB3 H 1.22 0.02 2 2166 198 198 LEU HG H 1.68 0.02 1 2167 198 198 LEU HD1 H 1.03 0.02 1 2168 198 198 LEU HD2 H 0.83 0.02 1 2169 198 198 LEU C C 178.92 0.20 1 2170 198 198 LEU CA C 58.49 0.10 1 2171 198 198 LEU CB C 42.64 0.10 1 2172 198 198 LEU CG C 26.07 0.10 1 2173 198 198 LEU CD1 C 25.92 0.10 1 2174 198 198 LEU CD2 C 23.69 0.10 1 2175 198 198 LEU N N 120.08 0.10 1 2176 199 199 ILE H H 7.42 0.02 1 2177 199 199 ILE HA H 4.28 0.02 1 2178 199 199 ILE HB H 2.15 0.02 1 2179 199 199 ILE HG12 H 0.71 0.02 2 2180 199 199 ILE HG13 H 1.68 0.02 2 2181 199 199 ILE HG2 H 1.03 0.02 1 2182 199 199 ILE HD1 H 0.78 0.02 1 2183 199 199 ILE C C 180.88 0.20 1 2184 199 199 ILE CA C 63.30 0.10 1 2185 199 199 ILE CB C 38.71 0.10 1 2186 199 199 ILE CG1 C 29.09 0.10 1 2187 199 199 ILE CG2 C 17.89 0.10 1 2188 199 199 ILE CD1 C 14.73 0.10 1 2189 199 199 ILE N N 119.78 0.10 1 2190 200 200 LYS H H 9.40 0.02 1 2191 200 200 LYS HA H 4.03 0.02 1 2192 200 200 LYS HB2 H 1.91 0.02 2 2193 200 200 LYS HG2 H 1.45 0.02 2 2194 200 200 LYS HG3 H 1.68 0.02 2 2195 200 200 LYS HD2 H 1.70 0.02 2 2196 200 200 LYS HD3 H 1.74 0.02 2 2197 200 200 LYS HE2 H 2.96 0.02 2 2198 200 200 LYS C C 178.67 0.20 1 2199 200 200 LYS CA C 59.92 0.10 1 2200 200 200 LYS CB C 32.66 0.10 1 2201 200 200 LYS CG C 25.38 0.10 1 2202 200 200 LYS CD C 29.40 0.10 1 2203 200 200 LYS CE C 42.01 0.10 1 2204 200 200 LYS N N 124.54 0.10 1 2205 201 201 ASN H H 8.04 0.02 1 2206 201 201 ASN HA H 4.66 0.02 1 2207 201 201 ASN HB2 H 2.81 0.02 2 2208 201 201 ASN HB3 H 2.87 0.04 2 2209 201 201 ASN HD21 H 7.86 0.02 2 2210 201 201 ASN HD22 H 7.01 0.02 2 2211 201 201 ASN C C 173.10 0.20 1 2212 201 201 ASN CA C 53.40 0.10 1 2213 201 201 ASN CB C 38.74 0.10 1 2214 201 201 ASN N N 113.85 0.10 1 2215 201 201 ASN ND2 N 115.32 0.10 1 2216 202 202 LYS H H 7.93 0.02 1 2217 202 202 LYS HA H 3.91 0.02 1 2218 202 202 LYS HB2 H 1.97 0.02 2 2219 202 202 LYS HG2 H 1.32 0.02 2 2220 202 202 LYS HD2 H 1.70 0.02 2 2221 202 202 LYS HD3 H 1.64 0.02 2 2222 202 202 LYS HE2 H 3.01 0.04 2 2223 202 202 LYS C C 175.57 0.20 1 2224 202 202 LYS CA C 57.49 0.10 1 2225 202 202 LYS CB C 27.74 0.10 1 2226 202 202 LYS CG C 25.01 0.10 1 2227 202 202 LYS CD C 28.94 0.10 1 2228 202 202 LYS CE C 42.38 0.10 1 2229 202 202 LYS N N 111.25 0.10 1 2230 203 203 HIS H H 8.36 0.02 1 2231 203 203 HIS HA H 4.79 0.02 1 2232 203 203 HIS HB2 H 3.09 0.02 2 2233 203 203 HIS HE1 H 7.71 0.02 1 2234 203 203 HIS C C 175.45 0.20 1 2235 203 203 HIS CA C 57.12 0.10 1 2236 203 203 HIS CB C 28.73 0.10 1 2237 203 203 HIS CE1 C 139.47 0.10 1 2238 203 203 HIS N N 115.99 0.10 1 2239 204 204 MET H H 7.48 0.02 1 2240 204 204 MET HA H 4.67 0.02 1 2241 204 204 MET HB2 H 1.64 0.02 2 2242 204 204 MET HB3 H 2.02 0.02 2 2243 204 204 MET HG2 H 2.49 0.02 2 2244 204 204 MET HG3 H 2.80 0.02 2 2245 204 204 MET HE H 2.05 0.02 1 2246 204 204 MET C C 172.99 0.20 1 2247 204 204 MET CA C 54.53 0.10 1 2248 204 204 MET CB C 37.91 0.10 1 2249 204 204 MET CG C 32.12 0.10 1 2250 204 204 MET CE C 17.08 0.10 1 2251 204 204 MET N N 113.90 0.10 1 2252 205 205 ASN H H 8.73 0.02 1 2253 205 205 ASN HA H 4.93 0.02 1 2254 205 205 ASN HB2 H 2.68 0.02 2 2255 205 205 ASN HB3 H 2.87 0.02 2 2256 205 205 ASN HD21 H 7.61 0.02 2 2257 205 205 ASN HD22 H 6.91 0.02 2 2258 205 205 ASN C C 175.95 0.20 1 2259 205 205 ASN CA C 51.91 0.10 1 2260 205 205 ASN CB C 40.41 0.10 1 2261 205 205 ASN N N 118.47 0.10 1 2262 205 205 ASN ND2 N 113.36 0.10 1 2263 206 206 ALA H H 9.09 0.02 1 2264 206 206 ALA HA H 3.81 0.02 1 2265 206 206 ALA HB H 1.35 0.02 1 2266 206 206 ALA C C 176.24 0.20 1 2267 206 206 ALA CA C 54.67 0.10 1 2268 206 206 ALA CB C 18.64 0.10 1 2269 206 206 ALA N N 124.97 0.10 1 2270 207 207 ASP H H 8.17 0.02 1 2271 207 207 ASP HA H 4.43 0.02 1 2272 207 207 ASP HB2 H 2.68 0.03 2 2273 207 207 ASP HB3 H 2.58 0.02 2 2274 207 207 ASP C C 176.38 0.20 1 2275 207 207 ASP CA C 53.65 0.10 1 2276 207 207 ASP CB C 40.07 0.10 1 2277 207 207 ASP N N 112.63 0.10 1 2278 208 208 THR H H 7.36 0.02 1 2279 208 208 THR HA H 3.52 0.02 1 2280 208 208 THR HB H 4.05 0.02 1 2281 208 208 THR HG2 H 1.21 0.02 1 2282 208 208 THR C C 173.16 0.20 1 2283 208 208 THR CA C 66.80 0.10 1 2284 208 208 THR CB C 69.06 0.10 1 2285 208 208 THR CG2 C 23.81 0.10 1 2286 208 208 THR N N 116.53 0.10 1 2287 209 209 ASP H H 6.98 0.02 1 2288 209 209 ASP HA H 5.28 0.02 1 2289 209 209 ASP HB2 H 2.56 0.02 2 2290 209 209 ASP HB3 H 3.24 0.02 2 2291 209 209 ASP C C 175.67 0.20 1 2292 209 209 ASP CA C 51.69 0.10 1 2293 209 209 ASP CB C 42.26 0.10 1 2294 209 209 ASP N N 131.03 0.10 1 2295 210 210 TYR H H 7.88 0.02 1 2296 210 210 TYR HA H 3.50 0.02 1 2297 210 210 TYR HB2 H 3.03 0.02 2 2298 210 210 TYR HB3 H 2.90 0.04 2 2299 210 210 TYR HD1 H 6.88 0.02 1 2300 210 210 TYR HD2 H 6.88 0.02 1 2301 210 210 TYR HE1 H 7.30 0.02 1 2302 210 210 TYR HE2 H 7.30 0.02 1 2303 210 210 TYR C C 178.26 0.20 1 2304 210 210 TYR CA C 63.40 0.10 1 2305 210 210 TYR CB C 39.39 0.10 1 2306 210 210 TYR CD1 C 133.91 0.10 1 2307 210 210 TYR CD2 C 133.91 0.10 1 2308 210 210 TYR CE1 C 118.01 0.10 1 2309 210 210 TYR CE2 C 118.01 0.10 1 2310 210 210 TYR N N 117.26 0.10 1 2311 211 211 SER H H 8.23 0.02 1 2312 211 211 SER HA H 4.37 0.02 1 2313 211 211 SER HB2 H 4.04 0.02 2 2314 211 211 SER C C 177.39 0.20 1 2315 211 211 SER CA C 61.85 0.10 1 2316 211 211 SER CB C 62.99 0.10 1 2317 211 211 SER N N 114.72 0.10 1 2318 212 212 ILE H H 9.03 0.02 1 2319 212 212 ILE HA H 3.76 0.02 1 2320 212 212 ILE HB H 1.63 0.02 1 2321 212 212 ILE HG12 H 1.11 0.02 2 2322 212 212 ILE HG13 H 1.93 0.02 2 2323 212 212 ILE HG2 H 0.99 0.02 1 2324 212 212 ILE HD1 H 0.89 0.02 1 2325 212 212 ILE C C 178.84 0.20 1 2326 212 212 ILE CA C 64.99 0.10 1 2327 212 212 ILE CB C 39.15 0.10 1 2328 212 212 ILE CG1 C 29.77 0.10 1 2329 212 212 ILE CG2 C 17.66 0.10 1 2330 212 212 ILE CD1 C 13.50 0.10 1 2331 212 212 ILE N N 124.37 0.10 1 2332 213 213 ALA H H 7.64 0.02 1 2333 213 213 ALA HA H 3.95 0.02 1 2334 213 213 ALA HB H 1.13 0.02 1 2335 213 213 ALA C C 177.60 0.20 1 2336 213 213 ALA CA C 55.44 0.10 1 2337 213 213 ALA CB C 17.46 0.10 1 2338 213 213 ALA N N 120.67 0.10 1 2339 214 214 GLU H H 7.88 0.02 1 2340 214 214 GLU HA H 4.05 0.02 1 2341 214 214 GLU HB2 H 1.62 0.02 2 2342 214 214 GLU HB3 H 2.03 0.02 2 2343 214 214 GLU HG2 H 2.08 0.04 2 2344 214 214 GLU C C 177.86 0.20 1 2345 214 214 GLU CA C 58.96 0.10 1 2346 214 214 GLU CB C 30.32 0.10 1 2347 214 214 GLU CG C 36.48 0.20 1 2348 214 214 GLU N N 117.20 0.10 1 2349 215 215 ALA H H 7.97 0.02 1 2350 215 215 ALA HA H 4.09 0.02 1 2351 215 215 ALA HB H 1.43 0.02 1 2352 215 215 ALA CA C 54.72 0.10 1 2353 215 215 ALA CB C 18.16 0.10 1 2354 215 215 ALA N N 119.50 0.10 1 2355 216 216 ALA H H 7.77 0.02 1 2356 216 216 ALA HA H 4.07 0.02 1 2357 216 216 ALA HB H 1.52 0.02 1 2358 216 216 ALA C C 180.52 0.20 1 2359 216 216 ALA CA C 54.97 0.10 1 2360 216 216 ALA CB C 20.25 0.10 1 2361 216 216 ALA N N 117.45 0.10 1 2362 217 217 PHE H H 8.36 0.02 1 2363 217 217 PHE HA H 4.02 0.02 1 2364 217 217 PHE HB2 H 2.77 0.02 2 2365 217 217 PHE HB3 H 3.03 0.02 2 2366 217 217 PHE C C 178.91 0.20 1 2367 217 217 PHE CA C 62.97 0.10 1 2368 217 217 PHE CB C 38.40 0.10 1 2369 217 217 PHE N N 119.30 0.10 1 2370 218 218 ASN H H 8.56 0.02 1 2371 218 218 ASN HA H 4.44 0.02 1 2372 218 218 ASN HB2 H 2.88 0.02 2 2373 218 218 ASN HB3 H 2.92 0.04 2 2374 218 218 ASN CA C 55.45 0.10 1 2375 218 218 ASN CB C 36.30 0.10 1 2376 218 218 ASN N N 119.99 0.10 1 2377 219 219 LYS H H 7.71 0.02 1 2378 219 219 LYS HA H 4.34 0.02 1 2379 219 219 LYS HB2 H 1.77 0.04 2 2380 219 219 LYS HB3 H 2.01 0.02 2 2381 219 219 LYS HG2 H 1.49 0.02 2 2382 219 219 LYS HG3 H 1.64 0.02 2 2383 219 219 LYS HD2 H 1.63 0.02 2 2384 219 219 LYS HE2 H 2.92 0.02 2 2385 219 219 LYS C C 177.57 0.20 1 2386 219 219 LYS CA C 56.05 0.10 1 2387 219 219 LYS CB C 33.34 0.10 1 2388 219 219 LYS CG C 25.61 0.10 1 2389 219 219 LYS CD C 29.29 0.10 1 2390 219 219 LYS CE C 42.00 0.10 1 2391 219 219 LYS N N 116.78 0.10 1 2392 220 220 GLY H H 7.73 0.02 1 2393 220 220 GLY HA2 H 3.87 0.02 2 2394 220 220 GLY HA3 H 4.22 0.04 2 2395 220 220 GLY C C 175.08 0.20 1 2396 220 220 GLY CA C 46.10 0.10 1 2397 220 220 GLY N N 108.65 0.10 1 2398 221 221 GLU H H 8.37 0.02 1 2399 221 221 GLU HA H 4.21 0.02 1 2400 221 221 GLU HB2 H 2.17 0.02 2 2401 221 221 GLU HB3 H 1.91 0.02 2 2402 221 221 GLU HG2 H 2.19 0.02 2 2403 221 221 GLU C C 175.63 0.20 1 2404 221 221 GLU CA C 57.36 0.10 1 2405 221 221 GLU CB C 30.80 0.10 1 2406 221 221 GLU CG C 36.49 0.10 1 2407 221 221 GLU N N 116.17 0.10 1 2408 222 222 THR H H 6.85 0.02 1 2409 222 222 THR HA H 5.26 0.02 1 2410 222 222 THR HB H 3.70 0.02 1 2411 222 222 THR HG2 H 1.15 0.02 1 2412 222 222 THR C C 172.51 0.20 1 2413 222 222 THR CA C 57.94 0.10 1 2414 222 222 THR CB C 70.62 0.10 1 2415 222 222 THR CG2 C 19.55 0.10 1 2416 222 222 THR N N 110.49 0.10 1 2417 223 223 ALA H H 8.67 0.02 1 2418 223 223 ALA HA H 4.26 0.02 1 2419 223 223 ALA HB H 1.73 0.02 1 2420 223 223 ALA C C 176.28 0.20 1 2421 223 223 ALA CA C 54.66 0.10 1 2422 223 223 ALA CB C 20.88 0.10 1 2423 223 223 ALA N N 127.45 0.10 1 2424 224 224 MET H H 8.06 0.02 1 2425 224 224 MET HA H 5.82 0.02 1 2426 224 224 MET HB2 H 1.92 0.02 2 2427 224 224 MET HB3 H 2.56 0.02 2 2428 224 224 MET HG2 H 2.57 0.02 2 2429 224 224 MET HE H 1.84 0.02 1 2430 224 224 MET C C 173.81 0.20 1 2431 224 224 MET CA C 54.52 0.10 1 2432 224 224 MET CB C 40.65 0.10 1 2433 224 224 MET CG C 33.21 0.10 1 2434 224 224 MET CE C 17.20 0.10 1 2435 224 224 MET N N 114.20 0.10 1 2436 225 225 THR H H 9.14 0.02 1 2437 225 225 THR HA H 4.89 0.02 1 2438 225 225 THR HB H 4.00 0.02 1 2439 225 225 THR HG2 H 0.19 0.02 1 2440 225 225 THR C C 171.28 0.20 1 2441 225 225 THR CA C 59.42 0.10 1 2442 225 225 THR CB C 71.03 0.10 1 2443 225 225 THR CG2 C 17.65 0.10 1 2444 225 225 THR N N 113.13 0.10 1 2445 226 226 ILE H H 7.16 0.02 1 2446 226 226 ILE HA H 4.95 0.02 1 2447 226 226 ILE HB H 1.40 0.02 1 2448 226 226 ILE HG12 H 0.60 0.02 2 2449 226 226 ILE HG13 H 1.12 0.02 2 2450 226 226 ILE HG2 H 0.89 0.02 1 2451 226 226 ILE HD1 H 0.07 0.02 1 2452 226 226 ILE C C 174.56 0.20 1 2453 226 226 ILE CA C 60.28 0.10 1 2454 226 226 ILE CB C 40.92 0.10 1 2455 226 226 ILE CG1 C 28.03 0.10 1 2456 226 226 ILE CG2 C 18.53 0.10 1 2457 226 226 ILE CD1 C 12.16 0.10 1 2458 226 226 ILE N N 122.45 0.10 1 2459 227 227 ASN H H 8.42 0.02 1 2460 227 227 ASN HA H 5.16 0.02 1 2461 227 227 ASN HB2 H 2.51 0.02 2 2462 227 227 ASN C C 175.43 0.20 1 2463 227 227 ASN CA C 52.33 0.10 1 2464 227 227 ASN CB C 43.03 0.11 1 2465 227 227 ASN N N 121.86 0.10 1 2466 228 228 GLY H H 8.29 0.02 1 2467 228 228 GLY HA2 H 1.52 0.04 2 2468 228 228 GLY CA C 42.37 0.10 1 2469 228 228 GLY N N 110.77 0.10 1 2470 229 229 PRO HA H 1.23 0.02 1 2471 229 229 PRO HB2 H 1.21 0.02 2 2472 229 229 PRO HB3 H 0.61 0.04 2 2473 229 229 PRO HG2 H 1.60 0.02 2 2474 229 229 PRO HG3 H 1.98 0.02 2 2475 229 229 PRO HD2 H 2.93 0.02 2 2476 229 229 PRO HD3 H 3.27 0.02 2 2477 229 229 PRO C C 176.23 0.20 1 2478 229 229 PRO CA C 62.63 0.10 1 2479 229 229 PRO CB C 30.13 0.10 1 2480 229 229 PRO CG C 27.73 0.10 1 2481 229 229 PRO CD C 48.49 0.10 1 2482 230 230 TRP H H 5.99 0.02 1 2483 230 230 TRP HA H 4.34 0.02 1 2484 230 230 TRP HB2 H 3.32 0.03 2 2485 230 230 TRP HB3 H 3.21 0.02 2 2486 230 230 TRP HD1 H 7.17 0.02 1 2487 230 230 TRP HE1 H 10.67 0.02 1 2488 230 230 TRP HE3 H 7.65 0.02 1 2489 230 230 TRP HZ2 H 7.83 0.02 1 2490 230 230 TRP HZ3 H 6.95 0.02 1 2491 230 230 TRP HH2 H 7.45 0.02 1 2492 230 230 TRP C C 176.23 0.20 1 2493 230 230 TRP CA C 59.02 0.10 1 2494 230 230 TRP CB C 26.66 0.10 1 2495 230 230 TRP CD1 C 129.57 0.10 1 2496 230 230 TRP CE3 C 120.94 0.10 1 2497 230 230 TRP CZ2 C 114.70 0.10 1 2498 230 230 TRP CZ3 C 122.73 0.10 1 2499 230 230 TRP CH2 C 124.53 0.10 1 2500 230 230 TRP N N 111.88 0.10 1 2501 230 230 TRP NE1 N 134.64 0.10 1 2502 231 231 ALA H H 7.00 0.02 1 2503 231 231 ALA HA H 4.78 0.02 1 2504 231 231 ALA HB H 1.36 0.02 1 2505 231 231 ALA C C 179.19 0.20 1 2506 231 231 ALA CA C 52.02 0.10 1 2507 231 231 ALA CB C 19.32 0.10 1 2508 231 231 ALA N N 125.27 0.10 1 2509 232 232 TRP H H 7.16 0.02 1 2510 232 232 TRP HA H 4.25 0.02 1 2511 232 232 TRP HB2 H 3.46 0.02 2 2512 232 232 TRP HB3 H 3.25 0.02 2 2513 232 232 TRP HD1 H 6.30 0.02 1 2514 232 232 TRP HE1 H 10.50 0.02 1 2515 232 232 TRP HE3 H 7.55 0.02 1 2516 232 232 TRP HZ2 H 6.98 0.02 1 2517 232 232 TRP HZ3 H 6.92 0.02 1 2518 232 232 TRP HH2 H 6.70 0.02 1 2519 232 232 TRP C C 177.63 0.20 1 2520 232 232 TRP CA C 58.57 0.10 1 2521 232 232 TRP CB C 28.76 0.12 1 2522 232 232 TRP CD1 C 122.45 0.10 1 2523 232 232 TRP CE3 C 122.22 0.10 1 2524 232 232 TRP CZ2 C 113.40 0.10 1 2525 232 232 TRP CZ3 C 120.88 0.10 1 2526 232 232 TRP CH2 C 124.47 0.10 1 2527 232 232 TRP N N 118.36 0.10 1 2528 232 232 TRP NE1 N 128.16 0.10 1 2529 233 233 SER H H 8.80 0.02 1 2530 233 233 SER HA H 4.40 0.02 1 2531 233 233 SER HB2 H 4.05 0.02 2 2532 233 233 SER CA C 62.40 0.10 1 2533 233 233 SER CB C 62.27 0.10 1 2534 233 233 SER N N 113.85 0.10 1 2535 234 234 ASN H H 8.19 0.02 1 2536 234 234 ASN HA H 4.64 0.02 1 2537 234 234 ASN HB2 H 3.00 0.02 2 2538 234 234 ASN HB3 H 2.71 0.02 2 2539 234 234 ASN HD21 H 8.07 0.04 2 2540 234 234 ASN HD22 H 6.90 0.02 2 2541 234 234 ASN CA C 55.10 0.10 1 2542 234 234 ASN CB C 37.27 0.10 1 2543 234 234 ASN N N 119.48 0.10 1 2544 234 234 ASN ND2 N 111.41 0.10 1 2545 235 235 ILE HA H 4.09 0.04 1 2546 235 235 ILE HB H 1.35 0.04 1 2547 235 235 ILE HG2 H 0.41 0.02 1 2548 235 235 ILE HD1 H 0.33 0.02 1 2549 235 235 ILE CA C 59.75 0.10 1 2550 235 235 ILE CB C 37.13 0.10 1 2551 235 235 ILE CG1 C 26.68 0.20 1 2552 235 235 ILE CG2 C 20.33 0.10 1 2553 235 235 ILE CD1 C 14.18 0.10 1 2554 237 237 THR HA H 4.09 0.02 1 2555 237 237 THR HB H 4.36 0.02 1 2556 237 237 THR HG2 H 1.34 0.02 1 2557 237 237 THR C C 175.65 0.20 1 2558 237 237 THR CA C 65.33 0.10 1 2559 237 237 THR CB C 69.01 0.10 1 2560 237 237 THR CG2 C 22.18 0.10 1 2561 238 238 SER H H 7.66 0.02 1 2562 238 238 SER HA H 4.37 0.02 1 2563 238 238 SER HB2 H 4.06 0.02 2 2564 238 238 SER HB3 H 4.30 0.02 2 2565 238 238 SER C C 173.95 0.20 1 2566 238 238 SER CA C 60.81 0.10 1 2567 238 238 SER CB C 64.31 0.10 1 2568 238 238 SER N N 118.29 0.10 1 2569 239 239 LYS H H 7.75 0.02 1 2570 239 239 LYS HA H 4.06 0.02 1 2571 239 239 LYS HG2 H 1.43 0.02 2 2572 239 239 LYS HG3 H 1.48 0.02 2 2573 239 239 LYS HD2 H 1.71 0.04 2 2574 239 239 LYS C C 176.07 0.20 1 2575 239 239 LYS CA C 57.70 0.10 1 2576 239 239 LYS CG C 24.79 0.10 1 2577 239 239 LYS CD C 28.84 0.20 1 2578 239 239 LYS N N 113.73 0.10 1 2579 240 240 VAL H H 7.38 0.02 1 2580 240 240 VAL HA H 3.68 0.02 1 2581 240 240 VAL HB H 1.73 0.02 1 2582 240 240 VAL HG1 H 0.60 0.02 1 2583 240 240 VAL HG2 H 0.80 0.02 1 2584 240 240 VAL C C 176.04 0.20 1 2585 240 240 VAL CA C 63.54 0.10 1 2586 240 240 VAL CB C 32.92 0.10 1 2587 240 240 VAL CG1 C 21.20 0.10 1 2588 240 240 VAL CG2 C 22.19 0.10 1 2589 240 240 VAL N N 120.41 0.10 1 2590 241 241 ASN H H 9.10 0.02 1 2591 241 241 ASN HA H 4.82 0.02 1 2592 241 241 ASN HB2 H 2.75 0.02 2 2593 241 241 ASN HB3 H 2.81 0.02 2 2594 241 241 ASN HD22 H 6.77 0.02 2 2595 241 241 ASN C C 173.20 0.20 1 2596 241 241 ASN CA C 51.93 0.10 1 2597 241 241 ASN CB C 37.46 0.10 1 2598 241 241 ASN N N 127.44 0.10 1 2599 241 241 ASN ND2 N 112.99 0.10 1 2600 242 242 TYR H H 7.88 0.02 1 2601 242 242 TYR HA H 5.83 0.02 1 2602 242 242 TYR HB2 H 2.63 0.02 2 2603 242 242 TYR HB3 H 2.97 0.03 2 2604 242 242 TYR HD1 H 6.90 0.02 1 2605 242 242 TYR HD2 H 6.90 0.02 1 2606 242 242 TYR HE1 H 6.38 0.02 1 2607 242 242 TYR HE2 H 6.38 0.02 1 2608 242 242 TYR C C 174.28 0.20 1 2609 242 242 TYR CA C 54.64 0.10 1 2610 242 242 TYR CB C 41.84 0.12 1 2611 242 242 TYR CD1 C 133.78 0.10 1 2612 242 242 TYR CD2 C 133.78 0.10 1 2613 242 242 TYR CE1 C 117.33 0.10 1 2614 242 242 TYR CE2 C 117.33 0.10 1 2615 242 242 TYR N N 121.82 0.10 1 2616 243 243 GLY H H 8.51 0.02 1 2617 243 243 GLY HA2 H 2.83 0.02 2 2618 243 243 GLY HA3 H 4.19 0.02 2 2619 243 243 GLY C C 171.00 0.20 1 2620 243 243 GLY CA C 42.97 0.10 1 2621 243 243 GLY N N 107.48 0.10 1 2622 244 244 VAL H H 8.26 0.02 1 2623 244 244 VAL HA H 4.96 0.02 1 2624 244 244 VAL HB H 1.58 0.02 1 2625 244 244 VAL HG1 H 1.08 0.02 1 2626 244 244 VAL HG2 H 0.61 0.02 1 2627 244 244 VAL C C 174.71 0.20 1 2628 244 244 VAL CA C 61.34 0.10 1 2629 244 244 VAL CB C 34.75 0.10 1 2630 244 244 VAL CG1 C 22.26 0.10 1 2631 244 244 VAL CG2 C 21.75 0.10 1 2632 244 244 VAL N N 120.53 0.10 1 2633 245 245 THR H H 9.49 0.02 1 2634 245 245 THR HA H 4.91 0.02 1 2635 245 245 THR HB H 4.06 0.02 1 2636 245 245 THR HG2 H 1.12 0.02 1 2637 245 245 THR C C 174.00 0.20 1 2638 245 245 THR CA C 58.87 0.10 1 2639 245 245 THR CB C 71.58 0.10 1 2640 245 245 THR CG2 C 19.00 0.10 1 2641 245 245 THR N N 119.47 0.10 1 2642 246 246 VAL H H 8.13 0.02 1 2643 246 246 VAL HA H 4.01 0.02 1 2644 246 246 VAL HB H 1.95 0.02 1 2645 246 246 VAL HG1 H 0.98 0.02 1 2646 246 246 VAL HG2 H 0.99 0.02 1 2647 246 246 VAL C C 174.91 0.20 1 2648 246 246 VAL CA C 62.28 0.10 1 2649 246 246 VAL CB C 32.51 0.10 1 2650 246 246 VAL CG1 C 20.70 0.10 1 2651 246 246 VAL CG2 C 21.95 0.10 1 2652 246 246 VAL N N 123.51 0.10 1 2653 247 247 LEU H H 8.61 0.02 1 2654 247 247 LEU HA H 4.09 0.02 1 2655 247 247 LEU HB2 H 1.86 0.04 2 2656 247 247 LEU HG H 1.63 0.02 1 2657 247 247 LEU HD1 H 0.67 0.02 1 2658 247 247 LEU HD2 H 0.66 0.02 1 2659 247 247 LEU CA C 54.47 0.10 1 2660 247 247 LEU CB C 40.80 0.10 1 2661 247 247 LEU CG C 28.51 0.10 1 2662 247 247 LEU CD1 C 26.18 0.10 1 2663 247 247 LEU CD2 C 24.25 0.10 1 2664 247 247 LEU N N 125.72 0.10 1 2665 248 248 PRO HA H 4.27 0.02 1 2666 248 248 PRO HB2 H 1.12 0.02 2 2667 248 248 PRO HB3 H 1.37 0.02 2 2668 248 248 PRO HG2 H 0.24 0.02 2 2669 248 248 PRO HG3 H 0.93 0.02 2 2670 248 248 PRO HD2 H 2.70 0.02 2 2671 248 248 PRO HD3 H 3.26 0.02 2 2672 248 248 PRO C C 175.34 0.20 1 2673 248 248 PRO CA C 61.83 0.10 1 2674 248 248 PRO CB C 30.67 0.10 1 2675 248 248 PRO CG C 25.87 0.10 1 2676 248 248 PRO CD C 49.20 0.10 1 2677 249 249 THR H H 8.81 0.02 1 2678 249 249 THR HA H 4.80 0.02 1 2679 249 249 THR HB H 3.89 0.02 1 2680 249 249 THR HG2 H 1.05 0.02 1 2681 249 249 THR C C 174.48 0.20 1 2682 249 249 THR CA C 60.84 0.10 1 2683 249 249 THR CB C 71.38 0.10 1 2684 249 249 THR CG2 C 21.15 0.10 1 2685 249 249 THR N N 111.58 0.10 1 2686 250 250 PHE H H 9.55 0.02 1 2687 250 250 PHE HA H 5.26 0.02 1 2688 250 250 PHE HB2 H 2.73 0.02 2 2689 250 250 PHE HB3 H 2.41 0.02 2 2690 250 250 PHE HD1 H 6.63 0.02 1 2691 250 250 PHE HD2 H 6.63 0.02 1 2692 250 250 PHE HE1 H 6.74 0.02 1 2693 250 250 PHE HE2 H 6.74 0.02 1 2694 250 250 PHE HZ H 6.95 0.02 1 2695 250 250 PHE C C 174.50 0.20 1 2696 250 250 PHE CA C 56.66 0.10 1 2697 250 250 PHE CB C 42.11 0.12 1 2698 250 250 PHE CD1 C 131.22 0.10 1 2699 250 250 PHE CD2 C 131.22 0.10 1 2700 250 250 PHE CE1 C 130.79 0.10 1 2701 250 250 PHE CE2 C 130.79 0.10 1 2702 250 250 PHE CZ C 128.99 0.10 1 2703 250 250 PHE N N 121.78 0.10 1 2704 251 251 LYS H H 10.59 0.02 1 2705 251 251 LYS HA H 3.26 0.02 1 2706 251 251 LYS HB2 H 1.64 0.02 2 2707 251 251 LYS HB3 H 1.13 0.04 2 2708 251 251 LYS HG2 H -0.28 0.02 2 2709 251 251 LYS HG3 H 0.49 0.02 2 2710 251 251 LYS HD2 H 1.29 0.02 2 2711 251 251 LYS HD3 H 0.93 0.02 2 2712 251 251 LYS C C 177.50 0.20 1 2713 251 251 LYS CA C 57.31 0.10 1 2714 251 251 LYS CB C 28.68 0.10 1 2715 251 251 LYS CG C 24.07 0.10 1 2716 251 251 LYS CD C 29.53 0.10 1 2717 251 251 LYS CE C 41.80 0.10 1 2718 251 251 LYS N N 129.49 0.10 1 2719 252 252 GLY H H 9.02 0.02 1 2720 252 252 GLY HA2 H 3.42 0.02 2 2721 252 252 GLY HA3 H 4.05 0.02 2 2722 252 252 GLY C C 173.76 0.20 1 2723 252 252 GLY CA C 45.05 0.10 1 2724 252 252 GLY N N 103.32 0.10 1 2725 253 253 GLN H H 8.24 0.02 1 2726 253 253 GLN HA H 4.79 0.02 1 2727 253 253 GLN HB2 H 1.93 0.02 2 2728 253 253 GLN HB3 H 2.34 0.02 2 2729 253 253 GLN HG2 H 2.21 0.02 2 2730 253 253 GLN HG3 H 2.49 0.02 2 2731 253 253 GLN HE22 H 7.26 0.02 2 2732 253 253 GLN CA C 52.28 0.10 1 2733 253 253 GLN CB C 29.71 0.10 1 2734 253 253 GLN CG C 33.22 0.10 1 2735 253 253 GLN N N 122.26 0.10 1 2736 253 253 GLN NE2 N 112.41 0.10 1 2737 254 254 PRO HA H 4.42 0.02 1 2738 254 254 PRO HB2 H 2.21 0.02 2 2739 254 254 PRO HB3 H 1.91 0.02 2 2740 254 254 PRO HG2 H 2.04 0.02 2 2741 254 254 PRO HG3 H 2.14 0.02 2 2742 254 254 PRO HD2 H 3.81 0.02 2 2743 254 254 PRO HD3 H 3.86 0.02 2 2744 254 254 PRO C C 178.45 0.20 1 2745 254 254 PRO CA C 63.17 0.10 1 2746 254 254 PRO CB C 31.64 0.10 1 2747 254 254 PRO CG C 27.50 0.10 1 2748 254 254 PRO CD C 50.16 0.10 1 2749 255 255 SER H H 7.98 0.02 1 2750 255 255 SER HA H 4.36 0.02 1 2751 255 255 SER HB2 H 3.37 0.02 2 2752 255 255 SER HB3 H 3.71 0.02 2 2753 255 255 SER C C 173.38 0.20 1 2754 255 255 SER CA C 62.15 0.10 1 2755 255 255 SER CB C 65.14 0.10 1 2756 255 255 SER N N 117.96 0.10 1 2757 256 256 LYS H H 7.70 0.02 1 2758 256 256 LYS HA H 4.95 0.02 1 2759 256 256 LYS HB2 H 1.45 0.02 2 2760 256 256 LYS HB3 H 1.53 0.02 2 2761 256 256 LYS HG2 H 1.39 0.02 2 2762 256 256 LYS HG3 H 1.48 0.02 2 2763 256 256 LYS HD2 H 1.71 0.02 2 2764 256 256 LYS HE2 H 2.98 0.03 2 2765 256 256 LYS CA C 52.95 0.10 1 2766 256 256 LYS CB C 33.78 0.10 1 2767 256 256 LYS CG C 23.98 0.10 1 2768 256 256 LYS CD C 29.36 0.10 1 2769 256 256 LYS CE C 42.28 0.10 1 2770 256 256 LYS N N 123.15 0.10 1 2771 257 257 PRO HA H 4.27 0.02 1 2772 257 257 PRO HD2 H 3.65 0.04 2 2773 257 257 PRO HD3 H 3.03 0.02 2 2774 257 257 PRO C C 176.93 0.20 1 2775 257 257 PRO CA C 62.13 0.10 1 2776 257 257 PRO CD C 50.29 0.10 1 2777 258 258 PHE H H 9.40 0.02 1 2778 258 258 PHE HA H 5.69 0.02 1 2779 258 258 PHE HD1 H 7.36 0.02 1 2780 258 258 PHE HD2 H 7.36 0.02 1 2781 258 258 PHE HE1 H 6.62 0.02 1 2782 258 258 PHE HE2 H 6.62 0.02 1 2783 258 258 PHE C C 177.58 0.20 1 2784 258 258 PHE CA C 58.44 0.10 1 2785 258 258 PHE CB C 40.43 0.20 1 2786 258 258 PHE CD1 C 130.06 0.10 1 2787 258 258 PHE CD2 C 130.06 0.10 1 2788 258 258 PHE CE1 C 130.93 0.10 1 2789 258 258 PHE CE2 C 130.93 0.10 1 2790 258 258 PHE N N 118.36 0.10 1 2791 259 259 VAL H H 8.73 0.02 1 2792 259 259 VAL HA H 4.79 0.02 1 2793 259 259 VAL HB H 1.86 0.02 1 2794 259 259 VAL HG1 H 0.95 0.02 1 2795 259 259 VAL HG2 H 1.03 0.02 1 2796 259 259 VAL C C 176.30 0.20 1 2797 259 259 VAL CA C 61.81 0.10 1 2798 259 259 VAL CB C 34.30 0.10 1 2799 259 259 VAL CG1 C 21.98 0.10 1 2800 259 259 VAL CG2 C 23.04 0.10 1 2801 259 259 VAL N N 121.64 0.10 1 2802 260 260 GLY H H 8.81 0.02 1 2803 260 260 GLY HA2 H 4.21 0.02 2 2804 260 260 GLY C C 171.55 0.20 1 2805 260 260 GLY CA C 44.89 0.10 1 2806 260 260 GLY N N 115.83 0.10 1 2807 261 261 VAL H H 10.96 0.02 1 2808 261 261 VAL HA H 5.23 0.02 1 2809 261 261 VAL HB H 1.85 0.02 1 2810 261 261 VAL HG1 H 0.71 0.02 1 2811 261 261 VAL HG2 H 0.56 0.02 1 2812 261 261 VAL C C 179.12 0.20 1 2813 261 261 VAL CA C 60.08 0.10 1 2814 261 261 VAL CB C 33.26 0.10 1 2815 261 261 VAL CG1 C 20.58 0.10 1 2816 261 261 VAL CG2 C 21.34 0.10 1 2817 261 261 VAL N N 128.94 0.10 1 2818 262 262 LEU H H 8.78 0.02 1 2819 262 262 LEU HA H 4.04 0.02 1 2820 262 262 LEU HB2 H 1.52 0.02 2 2821 262 262 LEU HB3 H 1.78 0.02 2 2822 262 262 LEU HG H 1.52 0.02 1 2823 262 262 LEU HD1 H 0.81 0.02 1 2824 262 262 LEU HD2 H 0.89 0.02 1 2825 262 262 LEU C C 175.03 0.20 1 2826 262 262 LEU CA C 56.59 0.10 1 2827 262 262 LEU CB C 41.53 0.10 1 2828 262 262 LEU CG C 27.67 0.10 1 2829 262 262 LEU CD1 C 22.93 0.10 1 2830 262 262 LEU CD2 C 25.53 0.10 1 2831 262 262 LEU N N 134.40 0.10 1 2832 263 263 SER H H 8.76 0.02 1 2833 263 263 SER HA H 5.33 0.02 1 2834 263 263 SER HB2 H 3.31 0.02 2 2835 263 263 SER HB3 H 3.15 0.02 2 2836 263 263 SER C C 170.57 0.20 1 2837 263 263 SER CA C 58.72 0.10 1 2838 263 263 SER CB C 66.46 0.10 1 2839 263 263 SER N N 126.59 0.10 1 2840 264 264 ALA H H 9.14 0.02 1 2841 264 264 ALA HA H 5.09 0.02 1 2842 264 264 ALA HB H 0.55 0.02 1 2843 264 264 ALA C C 176.01 0.20 1 2844 264 264 ALA CA C 49.77 0.10 1 2845 264 264 ALA CB C 21.26 0.10 1 2846 264 264 ALA N N 123.64 0.10 1 2847 265 265 GLY H H 9.43 0.02 1 2848 265 265 GLY HA2 H 3.15 0.02 2 2849 265 265 GLY HA3 H 4.75 0.02 2 2850 265 265 GLY C C 170.97 0.20 1 2851 265 265 GLY CA C 42.88 0.10 1 2852 265 265 GLY N N 110.75 0.10 1 2853 266 266 ILE H H 10.34 0.02 1 2854 266 266 ILE HA H 4.65 0.02 1 2855 266 266 ILE HB H 1.57 0.02 1 2856 266 266 ILE HG12 H 1.68 0.02 2 2857 266 266 ILE HG13 H 0.71 0.02 2 2858 266 266 ILE HG2 H 0.85 0.02 1 2859 266 266 ILE HD1 H 0.95 0.02 1 2860 266 266 ILE C C 175.08 0.20 1 2861 266 266 ILE CA C 59.75 0.10 1 2862 266 266 ILE CB C 40.01 0.10 1 2863 266 266 ILE CG1 C 28.23 0.10 1 2864 266 266 ILE CG2 C 16.64 0.10 1 2865 266 266 ILE CD1 C 14.27 0.10 1 2866 266 266 ILE N N 123.50 0.10 1 2867 267 267 ASN H H 8.20 0.02 1 2868 267 267 ASN HA H 4.47 0.02 1 2869 267 267 ASN HB2 H 2.92 0.04 2 2870 267 267 ASN C C 177.14 0.20 1 2871 267 267 ASN CA C 53.43 0.10 1 2872 267 267 ASN CB C 39.06 0.10 1 2873 267 267 ASN N N 125.71 0.10 1 2874 268 268 ALA H H 8.86 0.02 1 2875 268 268 ALA HA H 3.80 0.02 1 2876 268 268 ALA HB H 1.22 0.02 1 2877 268 268 ALA C C 178.23 0.20 1 2878 268 268 ALA CA C 55.32 0.10 1 2879 268 268 ALA CB C 18.23 0.10 1 2880 268 268 ALA N N 131.06 0.10 1 2881 269 269 ALA H H 8.17 0.02 1 2882 269 269 ALA HA H 4.36 0.02 1 2883 269 269 ALA HB H 1.30 0.02 1 2884 269 269 ALA C C 177.96 0.20 1 2885 269 269 ALA CA C 51.27 0.10 1 2886 269 269 ALA CB C 18.93 0.10 1 2887 269 269 ALA N N 118.04 0.10 1 2888 270 270 SER H H 7.57 0.02 1 2889 270 270 SER HA H 4.56 0.02 1 2890 270 270 SER HB2 H 3.98 0.02 2 2891 270 270 SER HB3 H 4.21 0.02 2 2892 270 270 SER CA C 56.17 0.10 1 2893 270 270 SER CB C 64.75 0.10 1 2894 270 270 SER N N 113.61 0.10 1 2895 271 271 PRO HA H 4.92 0.02 1 2896 271 271 PRO HB2 H 2.15 0.02 2 2897 271 271 PRO HB3 H 2.23 0.02 2 2898 271 271 PRO HG2 H 2.06 0.02 2 2899 271 271 PRO HG3 H 1.85 0.02 2 2900 271 271 PRO HD2 H 3.89 0.04 2 2901 271 271 PRO C C 175.72 0.20 1 2902 271 271 PRO CA C 63.42 0.10 1 2903 271 271 PRO CB C 31.51 0.10 1 2904 271 271 PRO CG C 26.11 0.10 1 2905 271 271 PRO CD C 50.62 0.10 1 2906 272 272 ASN H H 8.79 0.02 1 2907 272 272 ASN HA H 5.41 0.02 1 2908 272 272 ASN HB2 H 2.29 0.02 2 2909 272 272 ASN HB3 H 2.92 0.02 2 2910 272 272 ASN C C 176.17 0.20 1 2911 272 272 ASN CA C 52.50 0.10 1 2912 272 272 ASN CB C 40.76 0.10 1 2913 272 272 ASN N N 119.60 0.10 1 2914 273 273 LYS H H 7.91 0.02 1 2915 273 273 LYS HA H 3.71 0.02 1 2916 273 273 LYS HB2 H 1.79 0.02 2 2917 273 273 LYS HB3 H 1.85 0.02 2 2918 273 273 LYS HG2 H 1.20 0.02 2 2919 273 273 LYS HG3 H 1.92 0.02 2 2920 273 273 LYS HD2 H 1.67 0.04 2 2921 273 273 LYS HD3 H 1.77 0.03 2 2922 273 273 LYS HE2 H 3.21 0.02 2 2923 273 273 LYS HE3 H 3.14 0.02 2 2924 273 273 LYS C C 178.81 0.20 1 2925 273 273 LYS CA C 61.78 0.10 1 2926 273 273 LYS CB C 32.25 0.10 1 2927 273 273 LYS CG C 26.03 0.10 1 2928 273 273 LYS CD C 29.37 0.10 1 2929 273 273 LYS CE C 42.69 0.10 1 2930 273 273 LYS N N 119.18 0.10 1 2931 274 274 GLU H H 8.86 0.02 1 2932 274 274 GLU HA H 4.11 0.02 1 2933 274 274 GLU HB2 H 2.08 0.02 2 2934 274 274 GLU HG2 H 2.42 0.02 2 2935 274 274 GLU HG3 H 2.37 0.02 2 2936 274 274 GLU C C 179.60 0.20 1 2937 274 274 GLU CA C 59.96 0.10 1 2938 274 274 GLU CB C 28.34 0.10 1 2939 274 274 GLU CG C 36.73 0.10 1 2940 274 274 GLU N N 118.31 0.10 1 2941 275 275 LEU H H 7.48 0.02 1 2942 275 275 LEU HA H 4.29 0.02 1 2943 275 275 LEU HB2 H 1.40 0.02 2 2944 275 275 LEU HB3 H 1.91 0.02 2 2945 275 275 LEU HG H 1.87 0.02 1 2946 275 275 LEU HD1 H 0.96 0.02 1 2947 275 275 LEU HD2 H 0.98 0.02 1 2948 275 275 LEU C C 178.23 0.20 1 2949 275 275 LEU CA C 57.32 0.10 1 2950 275 275 LEU CB C 42.71 0.10 1 2951 275 275 LEU CG C 26.97 0.10 1 2952 275 275 LEU CD1 C 25.71 0.10 1 2953 275 275 LEU CD2 C 22.95 0.10 1 2954 275 275 LEU N N 120.82 0.10 1 2955 276 276 ALA H H 8.35 0.02 1 2956 276 276 ALA HA H 3.81 0.02 1 2957 276 276 ALA HB H 1.32 0.02 1 2958 276 276 ALA C C 178.38 0.20 1 2959 276 276 ALA CA C 55.45 0.10 1 2960 276 276 ALA CB C 18.22 0.10 1 2961 276 276 ALA N N 120.32 0.10 1 2962 277 277 LYS H H 7.83 0.02 1 2963 277 277 LYS HA H 3.74 0.02 1 2964 277 277 LYS HB2 H 1.95 0.02 2 2965 277 277 LYS HG2 H 1.14 0.02 2 2966 277 277 LYS HG3 H 1.55 0.04 2 2967 277 277 LYS HD2 H 1.66 0.04 2 2968 277 277 LYS HE2 H 3.00 0.04 2 2969 277 277 LYS C C 177.01 0.20 1 2970 277 277 LYS CA C 60.19 0.10 1 2971 277 277 LYS CB C 32.88 0.10 1 2972 277 277 LYS CG C 24.43 0.10 1 2973 277 277 LYS CD C 30.13 0.20 1 2974 277 277 LYS CE C 42.39 0.20 1 2975 277 277 LYS N N 118.16 0.10 1 2976 278 278 GLU H H 7.60 0.02 1 2977 278 278 GLU HA H 4.01 0.02 1 2978 278 278 GLU HB2 H 2.35 0.02 2 2979 278 278 GLU HB3 H 2.37 0.02 2 2980 278 278 GLU HG2 H 2.54 0.02 2 2981 278 278 GLU C C 179.05 0.20 1 2982 278 278 GLU CA C 59.67 0.10 1 2983 278 278 GLU CB C 29.66 0.10 1 2984 278 278 GLU CG C 35.90 0.10 1 2985 278 278 GLU N N 118.70 0.10 1 2986 279 279 PHE H H 8.42 0.02 1 2987 279 279 PHE HA H 3.61 0.02 1 2988 279 279 PHE HB2 H 1.80 0.02 2 2989 279 279 PHE HB3 H 2.56 0.02 2 2990 279 279 PHE HD1 H 6.23 0.02 1 2991 279 279 PHE HD2 H 6.23 0.02 1 2992 279 279 PHE HE1 H 6.83 0.02 1 2993 279 279 PHE HE2 H 6.83 0.02 1 2994 279 279 PHE HZ H 6.83 0.02 1 2995 279 279 PHE C C 177.41 0.20 1 2996 279 279 PHE CA C 61.67 0.10 1 2997 279 279 PHE CB C 38.80 0.10 1 2998 279 279 PHE CD1 C 131.31 0.10 1 2999 279 279 PHE CD2 C 131.31 0.10 1 3000 279 279 PHE CE1 C 130.16 0.10 1 3001 279 279 PHE CE2 C 130.16 0.10 1 3002 279 279 PHE CZ C 127.74 0.10 1 3003 279 279 PHE N N 118.25 0.10 1 3004 280 280 LEU H H 8.38 0.02 1 3005 280 280 LEU HA H 3.57 0.02 1 3006 280 280 LEU HB2 H 0.38 0.02 2 3007 280 280 LEU HB3 H 1.36 0.02 2 3008 280 280 LEU HG H 1.89 0.02 1 3009 280 280 LEU HD1 H 0.69 0.02 1 3010 280 280 LEU HD2 H 0.74 0.02 1 3011 280 280 LEU C C 176.95 0.20 1 3012 280 280 LEU CA C 58.27 0.10 1 3013 280 280 LEU CB C 41.22 0.10 1 3014 280 280 LEU CG C 27.71 0.10 1 3015 280 280 LEU CD1 C 26.06 0.10 1 3016 280 280 LEU CD2 C 23.76 0.10 1 3017 280 280 LEU N N 119.95 0.10 1 3018 281 281 GLU H H 8.43 0.02 1 3019 281 281 GLU HA H 3.72 0.02 1 3020 281 281 GLU HB2 H 1.54 0.02 2 3021 281 281 GLU HG2 H 2.06 0.04 2 3022 281 281 GLU HG3 H 0.97 0.04 2 3023 281 281 GLU C C 176.91 0.20 1 3024 281 281 GLU CA C 59.54 0.10 1 3025 281 281 GLU CB C 29.83 0.10 1 3026 281 281 GLU CG C 36.02 0.10 1 3027 281 281 GLU N N 112.80 0.10 1 3028 282 282 ASN H H 7.72 0.02 1 3029 282 282 ASN HA H 4.84 0.02 1 3030 282 282 ASN HB2 H 2.69 0.02 2 3031 282 282 ASN HB3 H 3.08 0.02 2 3032 282 282 ASN HD21 H 7.78 0.02 2 3033 282 282 ASN HD22 H 6.92 0.02 2 3034 282 282 ASN C C 175.16 0.20 1 3035 282 282 ASN CA C 52.91 0.10 1 3036 282 282 ASN CB C 39.11 0.10 1 3037 282 282 ASN N N 108.78 0.10 1 3038 282 282 ASN ND2 N 113.24 0.10 1 3039 283 283 TYR H H 7.16 0.02 1 3040 283 283 TYR HA H 4.30 0.02 1 3041 283 283 TYR HB2 H 3.08 0.02 2 3042 283 283 TYR HB3 H 2.26 0.02 2 3043 283 283 TYR HD1 H 7.21 0.02 1 3044 283 283 TYR HD2 H 7.21 0.02 1 3045 283 283 TYR HE1 H 6.96 0.02 1 3046 283 283 TYR HE2 H 6.96 0.02 1 3047 283 283 TYR C C 176.18 0.20 1 3048 283 283 TYR CA C 59.73 0.10 1 3049 283 283 TYR CB C 38.29 0.10 1 3050 283 283 TYR CD1 C 132.69 0.10 1 3051 283 283 TYR CD2 C 132.69 0.10 1 3052 283 283 TYR CE1 C 118.04 0.10 1 3053 283 283 TYR CE2 C 118.04 0.10 1 3054 283 283 TYR N N 116.30 0.10 1 3055 284 284 LEU H H 8.11 0.02 1 3056 284 284 LEU HA H 4.04 0.02 1 3057 284 284 LEU HB2 H 0.69 0.02 2 3058 284 284 LEU HD1 H 0.86 0.02 1 3059 284 284 LEU HD2 H 1.06 0.02 1 3060 284 284 LEU C C 176.78 0.20 1 3061 284 284 LEU CA C 58.12 0.10 1 3062 284 284 LEU CB C 41.49 0.10 1 3063 284 284 LEU CD1 C 24.23 0.10 1 3064 284 284 LEU CD2 C 27.68 0.10 1 3065 284 284 LEU N N 121.30 0.10 1 3066 285 285 LEU H H 7.82 0.02 1 3067 285 285 LEU HA H 4.41 0.02 1 3068 285 285 LEU HB2 H 1.81 0.02 2 3069 285 285 LEU HB3 H 2.25 0.02 2 3070 285 285 LEU HG H 1.53 0.02 1 3071 285 285 LEU HD1 H 1.07 0.02 1 3072 285 285 LEU HD2 H 1.14 0.02 1 3073 285 285 LEU C C 174.81 0.20 1 3074 285 285 LEU CA C 54.42 0.10 1 3075 285 285 LEU CB C 38.91 0.10 1 3076 285 285 LEU CG C 28.26 0.10 1 3077 285 285 LEU CD1 C 26.02 0.10 1 3078 285 285 LEU CD2 C 24.39 0.10 1 3079 285 285 LEU N N 119.28 0.10 1 3080 286 286 THR H H 8.56 0.02 1 3081 286 286 THR HA H 4.44 0.02 1 3082 286 286 THR HB H 4.31 0.02 1 3083 286 286 THR HG2 H 0.83 0.02 1 3084 286 286 THR C C 174.10 0.20 1 3085 286 286 THR CA C 58.79 0.10 1 3086 286 286 THR CB C 73.56 0.10 1 3087 286 286 THR CG2 C 21.09 0.10 1 3088 286 286 THR N N 108.64 0.10 1 3089 287 287 ASP H H 8.56 0.02 1 3090 287 287 ASP HA H 3.75 0.02 1 3091 287 287 ASP HB2 H 2.47 0.02 2 3092 287 287 ASP C C 177.67 0.20 1 3093 287 287 ASP CA C 58.39 0.10 1 3094 287 287 ASP CB C 39.75 0.10 1 3095 287 287 ASP N N 122.26 0.10 1 3096 288 288 GLU H H 8.46 0.02 1 3097 288 288 GLU HA H 3.88 0.02 1 3098 288 288 GLU HB2 H 1.91 0.02 2 3099 288 288 GLU HB3 H 1.94 0.02 2 3100 288 288 GLU HG2 H 2.31 0.02 2 3101 288 288 GLU C C 179.98 0.20 1 3102 288 288 GLU CA C 59.31 0.10 1 3103 288 288 GLU CB C 29.48 0.10 1 3104 288 288 GLU CG C 36.68 0.10 1 3105 288 288 GLU N N 115.65 0.10 1 3106 289 289 GLY H H 8.34 0.02 1 3107 289 289 GLY HA2 H 3.75 0.02 2 3108 289 289 GLY HA3 H 4.40 0.02 2 3109 289 289 GLY C C 175.07 0.20 1 3110 289 289 GLY CA C 46.91 0.10 1 3111 289 289 GLY N N 113.01 0.10 1 3112 290 290 LEU H H 8.20 0.02 1 3113 290 290 LEU HA H 4.02 0.02 1 3114 290 290 LEU HB2 H 1.14 0.02 2 3115 290 290 LEU HB3 H 1.68 0.02 2 3116 290 290 LEU HG H 2.47 0.02 1 3117 290 290 LEU HD1 H 1.10 0.02 1 3118 290 290 LEU HD2 H 0.81 0.02 1 3119 290 290 LEU C C 179.67 0.20 1 3120 290 290 LEU CA C 57.25 0.10 1 3121 290 290 LEU CB C 42.16 0.10 1 3122 290 290 LEU CG C 26.01 0.10 1 3123 290 290 LEU CD1 C 28.24 0.10 1 3124 290 290 LEU CD2 C 22.10 0.10 1 3125 290 290 LEU N N 119.43 0.10 1 3126 291 291 GLU H H 7.73 0.02 1 3127 291 291 GLU HA H 4.21 0.02 1 3128 291 291 GLU HB2 H 1.92 0.02 2 3129 291 291 GLU HG2 H 2.14 0.02 2 3130 291 291 GLU HG3 H 2.27 0.04 2 3131 291 291 GLU C C 177.97 0.20 1 3132 291 291 GLU CA C 59.40 0.10 1 3133 291 291 GLU CB C 29.41 0.10 1 3134 291 291 GLU CG C 36.38 0.10 1 3135 291 291 GLU N N 120.66 0.10 1 3136 292 292 ALA H H 7.16 0.02 1 3137 292 292 ALA HA H 3.98 0.02 1 3138 292 292 ALA HB H 1.47 0.02 1 3139 292 292 ALA C C 180.61 0.20 1 3140 292 292 ALA CA C 55.31 0.10 1 3141 292 292 ALA CB C 18.00 0.10 1 3142 292 292 ALA N N 119.82 0.10 1 3143 293 293 VAL H H 7.23 0.02 1 3144 293 293 VAL HA H 3.52 0.02 1 3145 293 293 VAL HB H 2.10 0.02 1 3146 293 293 VAL HG1 H 1.01 0.02 1 3147 293 293 VAL HG2 H 0.90 0.02 1 3148 293 293 VAL C C 176.87 0.20 1 3149 293 293 VAL CA C 67.34 0.10 1 3150 293 293 VAL CB C 32.17 0.10 1 3151 293 293 VAL CG1 C 21.69 0.10 1 3152 293 293 VAL CG2 C 22.56 0.10 1 3153 293 293 VAL N N 115.84 0.10 1 3154 294 294 ASN H H 8.75 0.02 1 3155 294 294 ASN HA H 4.60 0.02 1 3156 294 294 ASN HB2 H 3.05 0.02 2 3157 294 294 ASN HB3 H 2.78 0.02 2 3158 294 294 ASN HD21 H 8.17 0.02 2 3159 294 294 ASN HD22 H 7.09 0.02 2 3160 294 294 ASN C C 176.28 0.20 1 3161 294 294 ASN CA C 56.16 0.10 1 3162 294 294 ASN CB C 41.21 0.10 1 3163 294 294 ASN N N 117.44 0.10 1 3164 294 294 ASN ND2 N 117.30 0.10 1 3165 295 295 LYS H H 8.29 0.02 1 3166 295 295 LYS HA H 3.97 0.02 1 3167 295 295 LYS HB2 H 1.87 0.02 2 3168 295 295 LYS HB3 H 1.81 0.02 2 3169 295 295 LYS HG2 H 1.64 0.02 2 3170 295 295 LYS HG3 H 1.52 0.02 2 3171 295 295 LYS HD2 H 1.69 0.02 2 3172 295 295 LYS HE2 H 2.99 0.02 2 3173 295 295 LYS C C 177.23 0.20 1 3174 295 295 LYS CA C 58.32 0.10 1 3175 295 295 LYS CB C 32.65 0.10 1 3176 295 295 LYS CG C 25.53 0.10 1 3177 295 295 LYS CD C 29.49 0.10 1 3178 295 295 LYS CE C 42.07 0.10 1 3179 295 295 LYS N N 115.74 0.10 1 3180 296 296 ASP H H 7.26 0.02 1 3181 296 296 ASP HA H 4.55 0.02 1 3182 296 296 ASP HB2 H 2.54 0.02 2 3183 296 296 ASP HB3 H 3.02 0.02 2 3184 296 296 ASP C C 175.93 0.20 1 3185 296 296 ASP CA C 56.02 0.10 1 3186 296 296 ASP CB C 42.29 0.10 1 3187 296 296 ASP N N 118.68 0.10 1 3188 297 297 LYS H H 7.63 0.02 1 3189 297 297 LYS HA H 4.73 0.02 1 3190 297 297 LYS HB2 H 1.39 0.02 2 3191 297 297 LYS HB3 H 1.59 0.02 2 3192 297 297 LYS HG2 H 1.19 0.02 2 3193 297 297 LYS HG3 H 1.23 0.02 2 3194 297 297 LYS HD2 H 1.51 0.02 2 3195 297 297 LYS HD3 H 1.78 0.02 2 3196 297 297 LYS CA C 52.47 0.10 1 3197 297 297 LYS CB C 35.20 0.10 1 3198 297 297 LYS CG C 24.05 0.10 1 3199 297 297 LYS CD C 28.59 0.10 1 3200 297 297 LYS CE C 42.46 0.10 1 3201 297 297 LYS N N 115.72 0.10 1 3202 298 298 PRO HA H 4.54 0.02 1 3203 298 298 PRO HB2 H 1.92 0.02 2 3204 298 298 PRO HB3 H 2.46 0.02 2 3205 298 298 PRO HG2 H 2.27 0.02 2 3206 298 298 PRO HD2 H 3.70 0.02 2 3207 298 298 PRO HD3 H 3.84 0.02 2 3208 298 298 PRO C C 178.81 0.20 1 3209 298 298 PRO CA C 63.09 0.10 1 3210 298 298 PRO CB C 31.99 0.10 1 3211 298 298 PRO CG C 27.70 0.10 1 3212 298 298 PRO CD C 50.73 0.10 1 3213 299 299 LEU H H 8.66 0.02 1 3214 299 299 LEU HA H 4.08 0.02 1 3215 299 299 LEU HB2 H 1.47 0.02 2 3216 299 299 LEU HB3 H 1.39 0.04 2 3217 299 299 LEU HG H 1.72 0.02 1 3218 299 299 LEU HD1 H 0.93 0.02 1 3219 299 299 LEU HD2 H 0.83 0.02 1 3220 299 299 LEU C C 177.32 0.20 1 3221 299 299 LEU CA C 55.64 0.10 1 3222 299 299 LEU CB C 44.34 0.10 1 3223 299 299 LEU CG C 27.22 0.10 1 3224 299 299 LEU CD1 C 27.12 0.10 1 3225 299 299 LEU CD2 C 23.30 0.10 1 3226 299 299 LEU N N 122.87 0.10 1 3227 300 300 GLY H H 8.20 0.02 1 3228 300 300 GLY HA2 H 3.17 0.02 2 3229 300 300 GLY HA3 H 4.47 0.02 2 3230 300 300 GLY C C 173.74 0.20 1 3231 300 300 GLY CA C 44.35 0.10 1 3232 300 300 GLY N N 104.57 0.10 1 3233 301 301 ALA H H 7.53 0.02 1 3234 301 301 ALA HA H 4.88 0.02 1 3235 301 301 ALA HB H 1.38 0.02 1 3236 301 301 ALA C C 177.51 0.20 1 3237 301 301 ALA CA C 51.40 0.10 1 3238 301 301 ALA CB C 19.73 0.10 1 3239 301 301 ALA N N 124.06 0.10 1 3240 302 302 VAL H H 8.16 0.02 1 3241 302 302 VAL HA H 5.17 0.02 1 3242 302 302 VAL HB H 2.53 0.02 1 3243 302 302 VAL HG1 H 1.07 0.02 1 3244 302 302 VAL HG2 H 1.26 0.02 1 3245 302 302 VAL C C 173.44 0.20 1 3246 302 302 VAL CA C 59.47 0.10 1 3247 302 302 VAL CB C 35.73 0.10 1 3248 302 302 VAL CG1 C 22.62 0.10 1 3249 302 302 VAL CG2 C 19.23 0.10 1 3250 302 302 VAL N N 109.98 0.10 1 3251 303 303 ALA H H 7.62 0.02 1 3252 303 303 ALA HA H 3.99 0.02 1 3253 303 303 ALA HB H 1.01 0.02 1 3254 303 303 ALA C C 175.62 0.20 1 3255 303 303 ALA CA C 53.07 0.10 1 3256 303 303 ALA CB C 19.92 0.10 1 3257 303 303 ALA N N 117.05 0.10 1 3258 304 304 LEU H H 6.40 0.02 1 3259 304 304 LEU HA H 4.22 0.02 1 3260 304 304 LEU HB2 H 1.92 0.02 2 3261 304 304 LEU HG H 1.69 0.02 1 3262 304 304 LEU HD1 H 0.87 0.02 1 3263 304 304 LEU HD2 H 0.72 0.02 1 3264 304 304 LEU C C 175.33 0.20 1 3265 304 304 LEU CA C 54.25 0.10 1 3266 304 304 LEU CB C 44.58 0.10 1 3267 304 304 LEU CG C 27.04 0.10 1 3268 304 304 LEU CD1 C 24.59 0.10 1 3269 304 304 LEU CD2 C 26.80 0.10 1 3270 304 304 LEU N N 114.94 0.10 1 3271 305 305 LYS H H 8.07 0.02 1 3272 305 305 LYS HA H 3.74 0.02 1 3273 305 305 LYS HB2 H 1.63 0.02 2 3274 305 305 LYS HG2 H 0.63 0.02 2 3275 305 305 LYS HG3 H -0.06 0.02 2 3276 305 305 LYS HD2 H 1.31 0.02 2 3277 305 305 LYS HE2 H 2.60 0.02 2 3278 305 305 LYS HE3 H 2.62 0.02 2 3279 305 305 LYS C C 178.44 0.20 1 3280 305 305 LYS CA C 60.52 0.10 1 3281 305 305 LYS CB C 32.29 0.10 1 3282 305 305 LYS CG C 24.14 0.10 1 3283 305 305 LYS CD C 29.95 0.10 1 3284 305 305 LYS CE C 41.64 0.10 1 3285 305 305 LYS N N 129.47 0.10 1 3286 306 306 SER H H 8.75 0.02 1 3287 306 306 SER HA H 4.00 0.02 1 3288 306 306 SER HB2 H 3.74 0.02 2 3289 306 306 SER HB3 H 4.15 0.04 2 3290 306 306 SER C C 176.97 0.20 1 3291 306 306 SER CA C 61.40 0.10 1 3292 306 306 SER CB C 60.64 0.10 1 3293 306 306 SER N N 112.27 0.10 1 3294 307 307 TYR H H 6.62 0.02 1 3295 307 307 TYR HA H 4.85 0.02 1 3296 307 307 TYR HB2 H 2.65 0.02 2 3297 307 307 TYR HB3 H 3.62 0.02 2 3298 307 307 TYR HD1 H 7.10 0.02 1 3299 307 307 TYR HD2 H 7.10 0.02 1 3300 307 307 TYR HE1 H 6.64 0.02 1 3301 307 307 TYR HE2 H 6.64 0.02 1 3302 307 307 TYR C C 177.24 0.20 1 3303 307 307 TYR CA C 59.03 0.10 1 3304 307 307 TYR CB C 38.90 0.10 1 3305 307 307 TYR CD1 C 132.59 0.10 1 3306 307 307 TYR CD2 C 132.59 0.10 1 3307 307 307 TYR CE1 C 117.73 0.10 1 3308 307 307 TYR CE2 C 117.73 0.10 1 3309 307 307 TYR N N 122.24 0.10 1 3310 308 308 GLU H H 8.51 0.02 1 3311 308 308 GLU HA H 4.17 0.02 1 3312 308 308 GLU HB2 H 2.54 0.02 2 3313 308 308 GLU HB3 H 2.29 0.02 2 3314 308 308 GLU HG2 H 2.91 0.02 2 3315 308 308 GLU C C 177.59 0.20 1 3316 308 308 GLU CA C 57.95 0.10 1 3317 308 308 GLU CB C 26.15 0.10 1 3318 308 308 GLU CG C 33.40 0.10 1 3319 308 308 GLU N N 121.29 0.10 1 3320 309 309 GLU H H 7.76 0.02 1 3321 309 309 GLU HA H 3.95 0.02 1 3322 309 309 GLU HB2 H 2.03 0.02 2 3323 309 309 GLU HG2 H 2.33 0.02 2 3324 309 309 GLU HG3 H 2.52 0.02 2 3325 309 309 GLU C C 178.63 0.20 1 3326 309 309 GLU CA C 59.23 0.10 1 3327 309 309 GLU CB C 29.33 0.10 1 3328 309 309 GLU CG C 36.52 0.10 1 3329 309 309 GLU N N 115.52 0.10 1 3330 310 310 GLU H H 6.87 0.02 1 3331 310 310 GLU HA H 4.20 0.02 1 3332 310 310 GLU HB2 H 2.02 0.02 2 3333 310 310 GLU HG2 H 2.21 0.02 2 3334 310 310 GLU HG3 H 2.43 0.02 2 3335 310 310 GLU C C 179.06 0.20 1 3336 310 310 GLU CA C 57.84 0.10 1 3337 310 310 GLU CB C 29.52 0.10 1 3338 310 310 GLU CG C 34.94 0.10 1 3339 310 310 GLU N N 117.47 0.10 1 3340 311 311 LEU H H 8.23 0.02 1 3341 311 311 LEU HA H 3.97 0.02 1 3342 311 311 LEU HB2 H 1.51 0.03 2 3343 311 311 LEU HB3 H 1.60 0.03 2 3344 311 311 LEU HG H 1.03 0.02 1 3345 311 311 LEU HD1 H 0.89 0.02 1 3346 311 311 LEU HD2 H 0.79 0.02 1 3347 311 311 LEU C C 179.55 0.20 1 3348 311 311 LEU CA C 57.08 0.10 1 3349 311 311 LEU CB C 42.37 0.10 1 3350 311 311 LEU CG C 25.79 0.10 1 3351 311 311 LEU CD1 C 26.72 0.10 1 3352 311 311 LEU CD2 C 22.81 0.10 1 3353 311 311 LEU N N 120.84 0.10 1 3354 312 312 ALA H H 8.62 0.02 1 3355 312 312 ALA HA H 3.94 0.02 1 3356 312 312 ALA HB H 1.43 0.02 1 3357 312 312 ALA C C 176.44 0.20 1 3358 312 312 ALA CA C 53.99 0.10 1 3359 312 312 ALA CB C 17.39 0.10 1 3360 312 312 ALA N N 118.05 0.10 1 3361 313 313 LYS H H 7.10 0.02 1 3362 313 313 LYS HA H 4.00 0.02 1 3363 313 313 LYS HB2 H 1.74 0.04 2 3364 313 313 LYS HB3 H 1.94 0.04 2 3365 313 313 LYS HG2 H 1.61 0.02 2 3366 313 313 LYS HG3 H 1.47 0.02 2 3367 313 313 LYS HD2 H 1.73 0.02 2 3368 313 313 LYS HE2 H 3.00 0.02 2 3369 313 313 LYS C C 177.97 0.20 1 3370 313 313 LYS CA C 58.87 0.10 1 3371 313 313 LYS CB C 32.38 0.10 1 3372 313 313 LYS CG C 25.99 0.10 1 3373 313 313 LYS CD C 29.42 0.10 1 3374 313 313 LYS CE C 42.43 0.10 1 3375 313 313 LYS N N 117.50 0.10 1 3376 314 314 ASP H H 8.29 0.02 1 3377 314 314 ASP HA H 4.96 0.02 1 3378 314 314 ASP HB2 H 2.70 0.02 2 3379 314 314 ASP HB3 H 3.32 0.02 2 3380 314 314 ASP CA C 50.46 0.10 1 3381 314 314 ASP CB C 41.50 0.10 1 3382 314 314 ASP N N 120.90 0.10 1 3383 315 315 PRO HA H 4.38 0.02 1 3384 315 315 PRO HB2 H 2.08 0.02 2 3385 315 315 PRO HB3 H 2.46 0.02 2 3386 315 315 PRO HG2 H 2.01 0.02 2 3387 315 315 PRO HG3 H 2.07 0.02 2 3388 315 315 PRO HD2 H 4.00 0.03 2 3389 315 315 PRO HD3 H 4.14 0.02 2 3390 315 315 PRO C C 178.93 0.20 1 3391 315 315 PRO CA C 64.38 0.10 1 3392 315 315 PRO CB C 32.50 0.10 1 3393 315 315 PRO CG C 27.25 0.10 1 3394 315 315 PRO CD C 51.47 0.10 1 3395 316 316 ARG H H 8.44 0.02 1 3396 316 316 ARG HA H 3.79 0.02 1 3397 316 316 ARG HB2 H 1.12 0.04 2 3398 316 316 ARG C C 179.72 0.20 1 3399 316 316 ARG CA C 58.41 0.10 1 3400 316 316 ARG CB C 29.95 0.10 1 3401 316 316 ARG N N 116.89 0.10 1 3402 317 317 ILE H H 7.51 0.02 1 3403 317 317 ILE HA H 3.73 0.02 1 3404 317 317 ILE HB H 2.29 0.02 1 3405 317 317 ILE HG12 H 1.32 0.02 2 3406 317 317 ILE HG13 H 1.69 0.02 2 3407 317 317 ILE HG2 H 0.98 0.02 1 3408 317 317 ILE HD1 H 1.12 0.02 1 3409 317 317 ILE C C 177.73 0.20 1 3410 317 317 ILE CA C 64.49 0.10 1 3411 317 317 ILE CB C 36.88 0.10 1 3412 317 317 ILE CG1 C 29.95 0.10 1 3413 317 317 ILE CG2 C 17.97 0.10 1 3414 317 317 ILE CD1 C 12.87 0.10 1 3415 317 317 ILE N N 122.79 0.10 1 3416 318 318 ALA H H 7.83 0.02 1 3417 318 318 ALA HA H 4.03 0.02 1 3418 318 318 ALA HB H 1.65 0.02 1 3419 318 318 ALA C C 181.13 0.20 1 3420 318 318 ALA CA C 55.80 0.10 1 3421 318 318 ALA CB C 17.68 0.10 1 3422 318 318 ALA N N 122.50 0.10 1 3423 319 319 ALA H H 8.14 0.02 1 3424 319 319 ALA HA H 4.10 0.02 1 3425 319 319 ALA HB H 1.32 0.02 1 3426 319 319 ALA C C 178.61 0.20 1 3427 319 319 ALA CA C 55.21 0.10 1 3428 319 319 ALA CB C 18.28 0.10 1 3429 319 319 ALA N N 118.73 0.10 1 3430 320 320 THR H H 7.34 0.02 1 3431 320 320 THR HA H 3.70 0.02 1 3432 320 320 THR HB H 4.84 0.02 1 3433 320 320 THR HG2 H 1.39 0.02 1 3434 320 320 THR C C 175.17 0.20 1 3435 320 320 THR CA C 68.06 0.10 1 3436 320 320 THR CB C 68.90 0.10 1 3437 320 320 THR CG2 C 20.68 0.10 1 3438 320 320 THR N N 114.63 0.10 1 3439 321 321 MET H H 8.15 0.02 1 3440 321 321 MET HA H 4.25 0.02 1 3441 321 321 MET HB2 H 2.13 0.02 2 3442 321 321 MET HG2 H 2.48 0.02 2 3443 321 321 MET HE H 1.56 0.02 1 3444 321 321 MET C C 177.04 0.20 1 3445 321 321 MET CA C 57.05 0.10 1 3446 321 321 MET CB C 31.80 0.10 1 3447 321 321 MET CG C 33.09 0.10 1 3448 321 321 MET CE C 18.22 0.10 1 3449 321 321 MET N N 119.18 0.10 1 3450 322 322 GLU H H 8.22 0.02 1 3451 322 322 GLU HA H 3.94 0.02 1 3452 322 322 GLU HB2 H 1.93 0.02 2 3453 322 322 GLU HB3 H 2.00 0.03 2 3454 322 322 GLU HG2 H 2.06 0.02 2 3455 322 322 GLU HG3 H 2.25 0.02 2 3456 322 322 GLU C C 179.21 0.20 1 3457 322 322 GLU CA C 59.88 0.10 1 3458 322 322 GLU CB C 29.27 0.10 1 3459 322 322 GLU CG C 36.25 0.10 1 3460 322 322 GLU N N 121.36 0.10 1 3461 323 323 ASN H H 8.29 0.02 1 3462 323 323 ASN HA H 4.36 0.02 1 3463 323 323 ASN HB2 H 2.54 0.04 2 3464 323 323 ASN HB3 H 2.73 0.02 2 3465 323 323 ASN C C 176.84 0.20 1 3466 323 323 ASN CA C 56.82 0.10 1 3467 323 323 ASN CB C 39.26 0.10 1 3468 323 323 ASN N N 115.17 0.10 1 3469 324 324 ALA H H 8.09 0.02 1 3470 324 324 ALA HA H 3.75 0.02 1 3471 324 324 ALA HB H 1.30 0.02 1 3472 324 324 ALA C C 180.07 0.20 1 3473 324 324 ALA CA C 54.43 0.10 1 3474 324 324 ALA CB C 18.12 0.10 1 3475 324 324 ALA N N 119.62 0.10 1 3476 325 325 GLN H H 8.28 0.02 1 3477 325 325 GLN HA H 3.41 0.02 1 3478 325 325 GLN HB2 H 1.97 0.02 2 3479 325 325 GLN HB3 H 2.04 0.02 2 3480 325 325 GLN HG2 H 1.90 0.02 2 3481 325 325 GLN HG3 H 2.38 0.02 2 3482 325 325 GLN HE21 H 6.70 0.02 2 3483 325 325 GLN HE22 H 6.59 0.02 2 3484 325 325 GLN C C 177.63 0.20 1 3485 325 325 GLN CA C 58.39 0.10 1 3486 325 325 GLN CB C 28.29 0.10 1 3487 325 325 GLN CG C 35.28 0.10 1 3488 325 325 GLN N N 116.33 0.10 1 3489 325 325 GLN NE2 N 109.43 0.10 1 3490 326 326 LYS H H 7.04 0.02 1 3491 326 326 LYS HA H 4.31 0.02 1 3492 326 326 LYS HB2 H 2.16 0.02 2 3493 326 326 LYS HG2 H 1.50 0.02 2 3494 326 326 LYS HD2 H 1.64 0.04 2 3495 326 326 LYS HE2 H 2.96 0.04 2 3496 326 326 LYS C C 175.90 0.20 1 3497 326 326 LYS CA C 56.10 0.10 1 3498 326 326 LYS CB C 33.13 0.10 1 3499 326 326 LYS CG C 26.16 0.10 1 3500 326 326 LYS CD C 29.36 0.20 1 3501 326 326 LYS CE C 42.61 0.20 1 3502 326 326 LYS N N 117.80 0.10 1 3503 327 327 GLY H H 7.25 0.02 1 3504 327 327 GLY HA2 H 4.17 0.02 2 3505 327 327 GLY HA3 H 3.85 0.02 2 3506 327 327 GLY C C 172.51 0.20 1 3507 327 327 GLY CA C 44.65 0.10 1 3508 327 327 GLY N N 106.34 0.10 1 3509 328 328 GLU H H 8.56 0.02 1 3510 328 328 GLU HA H 4.78 0.02 1 3511 328 328 GLU HB2 H 1.72 0.02 2 3512 328 328 GLU HB3 H 1.96 0.02 2 3513 328 328 GLU HG2 H 2.29 0.02 2 3514 328 328 GLU HG3 H 2.35 0.02 2 3515 328 328 GLU C C 176.54 0.20 1 3516 328 328 GLU CA C 53.82 0.10 1 3517 328 328 GLU CB C 33.26 0.10 1 3518 328 328 GLU CG C 35.35 0.10 1 3519 328 328 GLU N N 121.92 0.10 1 3520 329 329 ILE H H 9.23 0.02 1 3521 329 329 ILE HA H 4.13 0.02 1 3522 329 329 ILE HB H 1.85 0.02 1 3523 329 329 ILE HG12 H 1.20 0.02 2 3524 329 329 ILE HG13 H 1.72 0.02 2 3525 329 329 ILE HG2 H 0.85 0.02 1 3526 329 329 ILE HD1 H 0.85 0.02 1 3527 329 329 ILE C C 178.07 0.20 1 3528 329 329 ILE CA C 62.35 0.10 1 3529 329 329 ILE CB C 38.14 0.10 1 3530 329 329 ILE CG1 C 28.08 0.10 1 3531 329 329 ILE CG2 C 17.62 0.10 1 3532 329 329 ILE CD1 C 12.76 0.10 1 3533 329 329 ILE N N 128.31 0.10 1 3534 330 330 MET H H 8.52 0.02 1 3535 330 330 MET HB2 H 1.80 0.02 2 3536 330 330 MET HB3 H 2.19 0.02 2 3537 330 330 MET HG2 H 2.09 0.02 2 3538 330 330 MET HG3 H 2.58 0.02 2 3539 330 330 MET HE H 2.09 0.02 1 3540 330 330 MET CA C 56.41 0.10 1 3541 330 330 MET CB C 34.84 0.10 1 3542 330 330 MET CG C 32.82 0.10 1 3543 330 330 MET CE C 17.42 0.10 1 3544 330 330 MET N N 125.42 0.10 1 3545 331 331 PRO HA H 4.36 0.02 1 3546 331 331 PRO HB2 H 0.86 0.04 2 3547 331 331 PRO HB3 H 1.59 0.04 2 3548 331 331 PRO C C 175.36 0.20 1 3549 331 331 PRO CA C 63.53 0.10 1 3550 331 331 PRO CB C 31.62 0.10 1 3551 332 332 ASN H H 7.64 0.02 1 3552 332 332 ASN HA H 4.86 0.02 1 3553 332 332 ASN HB2 H 2.97 0.02 2 3554 332 332 ASN HB3 H 3.29 0.02 2 3555 332 332 ASN C C 175.50 0.20 1 3556 332 332 ASN CA C 51.48 0.10 1 3557 332 332 ASN CB C 38.57 0.10 1 3558 332 332 ASN N N 118.53 0.10 1 3559 333 333 ILE H H 6.38 0.02 1 3560 333 333 ILE HA H 4.61 0.02 1 3561 333 333 ILE HB H 2.31 0.02 1 3562 333 333 ILE HG12 H 0.35 0.02 2 3563 333 333 ILE HG13 H 0.88 0.02 2 3564 333 333 ILE HG2 H 1.20 0.02 1 3565 333 333 ILE HD1 H -0.14 0.02 1 3566 333 333 ILE CA C 59.49 0.10 1 3567 333 333 ILE CB C 37.04 0.10 1 3568 333 333 ILE CG1 C 25.68 0.10 1 3569 333 333 ILE CG2 C 19.94 0.10 1 3570 333 333 ILE CD1 C 12.68 0.10 1 3571 333 333 ILE N N 108.34 0.10 1 3572 334 334 PRO HA H 4.33 0.02 1 3573 334 334 PRO HB2 H 1.93 0.02 2 3574 334 334 PRO HB3 H 2.37 0.02 2 3575 334 334 PRO HG2 H 1.95 0.02 2 3576 334 334 PRO HG3 H 2.14 0.02 2 3577 334 334 PRO HD2 H 3.91 0.02 2 3578 334 334 PRO C C 178.58 0.20 1 3579 334 334 PRO CA C 65.33 0.10 1 3580 334 334 PRO CB C 31.75 0.10 1 3581 334 334 PRO CG C 27.77 0.10 1 3582 334 334 PRO CD C 51.08 0.10 1 3583 335 335 GLN H H 8.36 0.02 1 3584 335 335 GLN HA H 4.27 0.02 1 3585 335 335 GLN HB2 H 1.54 0.02 2 3586 335 335 GLN HB3 H 2.19 0.02 2 3587 335 335 GLN HG2 H 2.64 0.02 2 3588 335 335 GLN HG3 H 2.82 0.02 2 3589 335 335 GLN HE21 H 7.79 0.02 2 3590 335 335 GLN HE22 H 6.87 0.02 2 3591 335 335 GLN C C 176.84 0.20 1 3592 335 335 GLN CA C 59.46 0.10 1 3593 335 335 GLN CB C 26.82 0.10 1 3594 335 335 GLN CG C 35.16 0.10 1 3595 335 335 GLN N N 116.48 0.10 1 3596 335 335 GLN NE2 N 111.34 0.10 1 3597 336 336 MET H H 7.80 0.02 1 3598 336 336 MET HA H 4.47 0.02 1 3599 336 336 MET HB2 H 1.94 0.02 2 3600 336 336 MET HG2 H 2.40 0.02 2 3601 336 336 MET HE H 0.27 0.02 1 3602 336 336 MET C C 177.32 0.20 1 3603 336 336 MET CA C 55.96 0.10 1 3604 336 336 MET CB C 30.61 0.10 1 3605 336 336 MET CG C 33.26 0.10 1 3606 336 336 MET CE C 17.51 0.10 1 3607 336 336 MET N N 118.28 0.10 1 3608 337 337 SER H H 7.96 0.02 1 3609 337 337 SER HA H 4.52 0.02 1 3610 337 337 SER HB2 H 4.08 0.02 1 3611 337 337 SER HB3 H 4.08 0.02 1 3612 337 337 SER C C 177.13 0.20 1 3613 337 337 SER CA C 62.10 0.10 1 3614 337 337 SER CB C 62.48 0.10 1 3615 337 337 SER N N 113.62 0.10 1 3616 338 338 ALA H H 7.35 0.02 1 3617 338 338 ALA HA H 4.40 0.02 1 3618 338 338 ALA HB H 1.69 0.02 1 3619 338 338 ALA CA C 54.62 0.10 1 3620 338 338 ALA CB C 18.96 0.10 1 3621 338 338 ALA N N 122.94 0.10 1 3622 339 339 PHE H H 7.51 0.02 1 3623 339 339 PHE HA H 3.90 0.02 1 3624 339 339 PHE HB2 H 2.65 0.02 2 3625 339 339 PHE HB3 H 3.48 0.02 2 3626 339 339 PHE HD1 H 6.13 0.02 1 3627 339 339 PHE HD2 H 6.13 0.02 1 3628 339 339 PHE HE1 H 6.38 0.02 1 3629 339 339 PHE HE2 H 6.38 0.02 1 3630 339 339 PHE C C 176.41 0.20 1 3631 339 339 PHE CA C 61.76 0.10 1 3632 339 339 PHE CB C 39.35 0.10 1 3633 339 339 PHE CD1 C 131.57 0.10 1 3634 339 339 PHE CD2 C 131.57 0.10 1 3635 339 339 PHE CE1 C 130.21 0.10 1 3636 339 339 PHE CE2 C 130.21 0.10 1 3637 339 339 PHE N N 118.76 0.10 1 3638 340 340 TRP H H 8.75 0.02 1 3639 340 340 TRP HA H 4.56 0.02 1 3640 340 340 TRP HB2 H 3.35 0.02 2 3641 340 340 TRP HD1 H 7.29 0.02 1 3642 340 340 TRP HE1 H 10.68 0.02 1 3643 340 340 TRP HE3 H 7.59 0.02 1 3644 340 340 TRP HZ2 H 7.16 0.02 1 3645 340 340 TRP HH2 H 6.32 0.02 1 3646 340 340 TRP C C 178.80 0.20 1 3647 340 340 TRP CA C 59.99 0.10 1 3648 340 340 TRP CB C 30.60 0.10 1 3649 340 340 TRP CD1 C 130.87 0.10 1 3650 340 340 TRP CE3 C 120.22 0.10 1 3651 340 340 TRP CZ2 C 115.92 0.10 1 3652 340 340 TRP CH2 C 124.72 0.10 1 3653 340 340 TRP N N 118.02 0.10 1 3654 340 340 TRP NE1 N 130.60 0.10 1 3655 341 341 TYR H H 7.41 0.02 1 3656 341 341 TYR HA H 4.26 0.02 1 3657 341 341 TYR HB2 H 3.18 0.03 2 3658 341 341 TYR HB3 H 3.12 0.02 2 3659 341 341 TYR HD1 H 7.25 0.02 1 3660 341 341 TYR HD2 H 7.25 0.02 1 3661 341 341 TYR HE1 H 6.83 0.02 1 3662 341 341 TYR HE2 H 6.83 0.02 1 3663 341 341 TYR C C 178.44 0.20 1 3664 341 341 TYR CA C 61.35 0.10 1 3665 341 341 TYR CB C 38.80 0.10 1 3666 341 341 TYR CD1 C 133.26 0.10 1 3667 341 341 TYR CD2 C 133.26 0.10 1 3668 341 341 TYR CE1 C 118.28 0.10 1 3669 341 341 TYR CE2 C 118.28 0.10 1 3670 341 341 TYR N N 114.47 0.10 1 3671 342 342 ALA H H 8.45 0.02 1 3672 342 342 ALA HA H 3.99 0.02 1 3673 342 342 ALA HB H 1.49 0.02 1 3674 342 342 ALA C C 180.72 0.20 1 3675 342 342 ALA CA C 54.91 0.10 1 3676 342 342 ALA CB C 19.53 0.10 1 3677 342 342 ALA N N 121.70 0.10 1 3678 343 343 VAL H H 8.69 0.02 1 3679 343 343 VAL HA H 3.39 0.02 1 3680 343 343 VAL HB H 1.50 0.02 1 3681 343 343 VAL HG1 H 0.86 0.02 1 3682 343 343 VAL HG2 H 0.13 0.02 1 3683 343 343 VAL C C 176.86 0.20 1 3684 343 343 VAL CA C 66.97 0.10 1 3685 343 343 VAL CB C 31.09 0.10 1 3686 343 343 VAL CG1 C 21.55 0.10 1 3687 343 343 VAL CG2 C 23.56 0.10 1 3688 343 343 VAL N N 118.42 0.10 1 3689 344 344 ARG H H 8.10 0.02 1 3690 344 344 ARG HA H 3.91 0.02 1 3691 344 344 ARG HB2 H 2.04 0.02 2 3692 344 344 ARG C C 178.39 0.20 1 3693 344 344 ARG CA C 60.27 0.10 1 3694 344 344 ARG CB C 30.41 0.10 1 3695 344 344 ARG N N 120.77 0.10 1 3696 345 345 THR H H 7.52 0.02 1 3697 345 345 THR HA H 3.74 0.02 1 3698 345 345 THR HB H 4.09 0.02 1 3699 345 345 THR HG2 H 1.15 0.02 1 3700 345 345 THR C C 174.86 0.20 1 3701 345 345 THR CA C 66.44 0.10 1 3702 345 345 THR CB C 69.31 0.10 1 3703 345 345 THR CG2 C 21.65 0.10 1 3704 345 345 THR N N 113.67 0.10 1 3705 346 346 ALA H H 7.79 0.02 1 3706 346 346 ALA HA H 4.18 0.02 1 3707 346 346 ALA HB H 1.29 0.02 1 3708 346 346 ALA C C 179.01 0.20 1 3709 346 346 ALA CA C 55.48 0.10 1 3710 346 346 ALA CB C 19.07 0.10 1 3711 346 346 ALA N N 122.76 0.10 1 3712 347 347 VAL H H 8.14 0.02 1 3713 347 347 VAL HA H 3.47 0.02 1 3714 347 347 VAL HB H 2.16 0.02 1 3715 347 347 VAL HG1 H 0.93 0.02 1 3716 347 347 VAL HG2 H 1.05 0.02 1 3717 347 347 VAL C C 177.80 0.20 1 3718 347 347 VAL CA C 67.51 0.10 1 3719 347 347 VAL CB C 31.42 0.10 1 3720 347 347 VAL CG1 C 20.78 0.10 1 3721 347 347 VAL CG2 C 22.62 0.10 1 3722 347 347 VAL N N 115.79 0.10 1 3723 348 348 ILE H H 7.73 0.02 1 3724 348 348 ILE HA H 3.77 0.02 1 3725 348 348 ILE HB H 1.90 0.02 1 3726 348 348 ILE HG12 H 1.29 0.02 2 3727 348 348 ILE HG13 H 1.70 0.02 2 3728 348 348 ILE HG2 H 0.95 0.02 1 3729 348 348 ILE HD1 H 0.89 0.02 1 3730 348 348 ILE C C 180.10 0.20 1 3731 348 348 ILE CA C 64.93 0.10 1 3732 348 348 ILE CB C 37.90 0.10 1 3733 348 348 ILE CG1 C 29.27 0.10 1 3734 348 348 ILE CG2 C 17.05 0.10 1 3735 348 348 ILE CD1 C 13.38 0.10 1 3736 348 348 ILE N N 118.33 0.10 1 3737 349 349 ASN H H 8.82 0.02 1 3738 349 349 ASN HA H 4.36 0.02 1 3739 349 349 ASN HB2 H 2.45 0.02 2 3740 349 349 ASN HB3 H 3.12 0.02 2 3741 349 349 ASN HD21 H 7.40 0.02 2 3742 349 349 ASN HD22 H 6.77 0.02 2 3743 349 349 ASN C C 177.84 0.20 1 3744 349 349 ASN CA C 55.77 0.10 1 3745 349 349 ASN CB C 37.26 0.10 1 3746 349 349 ASN N N 121.08 0.10 1 3747 349 349 ASN ND2 N 109.64 0.10 1 3748 350 350 ALA H H 8.53 0.02 1 3749 350 350 ALA HA H 4.70 0.02 1 3750 350 350 ALA HB H 1.31 0.02 1 3751 350 350 ALA C C 180.95 0.20 1 3752 350 350 ALA CA C 53.96 0.10 1 3753 350 350 ALA CB C 18.32 0.10 1 3754 350 350 ALA N N 122.75 0.10 1 3755 351 351 ALA H H 9.15 0.02 1 3756 351 351 ALA HA H 3.99 0.02 1 3757 351 351 ALA HB H 1.45 0.02 1 3758 351 351 ALA C C 178.13 0.20 1 3759 351 351 ALA CA C 55.55 0.10 1 3760 351 351 ALA CB C 18.36 0.10 1 3761 351 351 ALA N N 120.97 0.10 1 3762 352 352 SER H H 7.88 0.02 1 3763 352 352 SER HA H 4.36 0.02 1 3764 352 352 SER HB2 H 4.02 0.02 2 3765 352 352 SER HB3 H 4.05 0.02 2 3766 352 352 SER C C 175.58 0.20 1 3767 352 352 SER CA C 58.78 0.10 1 3768 352 352 SER CB C 64.52 0.10 1 3769 352 352 SER N N 107.88 0.10 1 3770 353 353 GLY H H 7.61 0.02 1 3771 353 353 GLY HA2 H 4.21 0.02 2 3772 353 353 GLY HA3 H 3.84 0.04 2 3773 353 353 GLY C C 174.39 0.20 1 3774 353 353 GLY CA C 45.72 0.10 1 3775 353 353 GLY N N 109.78 0.10 1 3776 354 354 ARG H H 8.23 0.02 1 3777 354 354 ARG HA H 4.09 0.02 1 3778 354 354 ARG HB2 H 1.72 0.02 2 3779 354 354 ARG HB3 H 1.76 0.02 2 3780 354 354 ARG HG2 H 1.67 0.03 2 3781 354 354 ARG HG3 H 1.58 0.03 2 3782 354 354 ARG HD2 H 3.14 0.02 2 3783 354 354 ARG HD3 H 3.21 0.02 2 3784 354 354 ARG C C 176.67 0.20 1 3785 354 354 ARG CA C 58.49 0.10 1 3786 354 354 ARG CB C 31.24 0.10 1 3787 354 354 ARG CG C 28.25 0.10 1 3788 354 354 ARG CD C 43.26 0.10 1 3789 354 354 ARG N N 121.04 0.10 1 3790 355 355 GLN H H 7.33 0.02 1 3791 355 355 GLN HA H 4.70 0.02 1 3792 355 355 GLN HB2 H 2.18 0.02 2 3793 355 355 GLN HB3 H 1.48 0.02 2 3794 355 355 GLN HG2 H 1.97 0.02 2 3795 355 355 GLN HG3 H 2.43 0.02 2 3796 355 355 GLN HE21 H 7.51 0.02 2 3797 355 355 GLN HE22 H 6.87 0.02 2 3798 355 355 GLN C C 175.89 0.20 1 3799 355 355 GLN CA C 54.12 0.10 1 3800 355 355 GLN CB C 36.85 0.10 1 3801 355 355 GLN CG C 36.11 0.10 1 3802 355 355 GLN N N 113.46 0.10 1 3803 355 355 GLN NE2 N 112.17 0.10 1 3804 356 356 THR H H 8.56 0.02 1 3805 356 356 THR HA H 4.30 0.02 1 3806 356 356 THR HB H 4.72 0.02 1 3807 356 356 THR HG2 H 1.33 0.02 1 3808 356 356 THR C C 174.71 0.20 1 3809 356 356 THR CA C 61.26 0.10 1 3810 356 356 THR CB C 70.51 0.10 1 3811 356 356 THR CG2 C 22.12 0.10 1 3812 356 356 THR N N 111.63 0.10 1 3813 357 357 VAL H H 8.74 0.02 1 3814 357 357 VAL HA H 3.33 0.02 1 3815 357 357 VAL HB H 2.03 0.02 1 3816 357 357 VAL HG1 H 1.00 0.02 1 3817 357 357 VAL HG2 H 1.06 0.02 1 3818 357 357 VAL C C 176.96 0.20 1 3819 357 357 VAL CA C 67.91 0.10 1 3820 357 357 VAL CB C 31.65 0.10 1 3821 357 357 VAL CG1 C 21.55 0.10 1 3822 357 357 VAL CG2 C 23.70 0.10 1 3823 357 357 VAL N N 121.41 0.10 1 3824 358 358 ASP H H 8.13 0.02 1 3825 358 358 ASP HA H 4.07 0.02 1 3826 358 358 ASP HB2 H 2.53 0.02 1 3827 358 358 ASP HB3 H 2.53 0.02 1 3828 358 358 ASP C C 178.76 0.20 1 3829 358 358 ASP CA C 57.62 0.10 1 3830 358 358 ASP CB C 41.03 0.10 1 3831 358 358 ASP N N 115.20 0.10 1 3832 359 359 GLU H H 7.60 0.02 1 3833 359 359 GLU HA H 3.84 0.02 1 3834 359 359 GLU HB2 H 1.98 0.03 2 3835 359 359 GLU HB3 H 2.07 0.02 2 3836 359 359 GLU HG2 H 2.24 0.02 2 3837 359 359 GLU C C 178.41 0.20 1 3838 359 359 GLU CA C 58.77 0.10 1 3839 359 359 GLU CB C 30.52 0.10 1 3840 359 359 GLU CG C 36.81 0.10 1 3841 359 359 GLU N N 118.63 0.10 1 3842 360 360 ALA H H 8.70 0.02 1 3843 360 360 ALA HA H 4.00 0.02 1 3844 360 360 ALA HB H 1.41 0.02 1 3845 360 360 ALA C C 181.38 0.20 1 3846 360 360 ALA CA C 54.79 0.10 1 3847 360 360 ALA CB C 18.66 0.10 1 3848 360 360 ALA N N 121.41 0.10 1 3849 361 361 LEU H H 8.08 0.02 1 3850 361 361 LEU HA H 4.02 0.02 1 3851 361 361 LEU HG H 1.74 0.02 1 3852 361 361 LEU HD1 H 0.90 0.02 1 3853 361 361 LEU HD2 H 0.73 0.02 1 3854 361 361 LEU C C 178.73 0.20 1 3855 361 361 LEU CA C 57.39 0.10 1 3856 361 361 LEU CB C 40.24 0.10 1 3857 361 361 LEU CG C 26.80 0.11 1 3858 361 361 LEU CD1 C 25.56 0.10 1 3859 361 361 LEU CD2 C 19.85 0.10 1 3860 361 361 LEU N N 116.12 0.10 1 3861 362 362 LYS H H 7.71 0.02 1 3862 362 362 LYS HA H 4.08 0.02 1 3863 362 362 LYS HB2 H 1.90 0.02 2 3864 362 362 LYS HG2 H 1.43 0.02 2 3865 362 362 LYS HD2 H 1.67 0.02 2 3866 362 362 LYS HE2 H 2.94 0.02 2 3867 362 362 LYS C C 179.69 0.20 1 3868 362 362 LYS CA C 59.75 0.10 1 3869 362 362 LYS CB C 32.11 0.10 1 3870 362 362 LYS CG C 24.54 0.10 1 3871 362 362 LYS CD C 28.93 0.10 1 3872 362 362 LYS CE C 42.05 0.10 1 3873 362 362 LYS N N 121.45 0.10 1 3874 363 363 ASP H H 8.13 0.02 1 3875 363 363 ASP HA H 4.35 0.02 1 3876 363 363 ASP HB2 H 2.67 0.02 2 3877 363 363 ASP HB3 H 2.86 0.02 2 3878 363 363 ASP CA C 57.13 0.10 1 3879 363 363 ASP CB C 40.52 0.10 1 3880 363 363 ASP N N 119.91 0.10 1 3881 364 364 ALA H H 7.72 0.02 1 3882 364 364 ALA HA H 4.10 0.02 1 3883 364 364 ALA HB H 1.26 0.02 1 3884 364 364 ALA C C 178.20 0.20 1 3885 364 364 ALA CA C 55.24 0.10 1 3886 364 364 ALA CB C 18.16 0.10 1 3887 364 364 ALA N N 121.42 0.10 1 3888 365 365 GLN H H 8.26 0.02 1 3889 365 365 GLN HA H 3.54 0.02 1 3890 365 365 GLN HB2 H 2.21 0.02 2 3891 365 365 GLN HG2 H 2.21 0.02 2 3892 365 365 GLN HG3 H 2.58 0.02 2 3893 365 365 GLN HE21 H 7.34 0.02 2 3894 365 365 GLN HE22 H 6.98 0.02 2 3895 365 365 GLN C C 179.06 0.20 1 3896 365 365 GLN CA C 60.39 0.10 1 3897 365 365 GLN CB C 27.63 0.10 1 3898 365 365 GLN CG C 31.92 0.10 1 3899 365 365 GLN N N 118.19 0.10 1 3900 365 365 GLN NE2 N 110.56 0.10 1 3901 366 366 THR H H 8.17 0.02 1 3902 366 366 THR HA H 3.85 0.02 1 3903 366 366 THR HB H 4.35 0.02 1 3904 366 366 THR HG2 H 1.26 0.02 1 3905 366 366 THR C C 175.76 0.20 1 3906 366 366 THR CA C 66.12 0.10 1 3907 366 366 THR CB C 68.98 0.10 1 3908 366 366 THR CG2 C 21.76 0.10 1 3909 366 366 THR N N 115.29 0.10 1 3910 367 367 ARG H H 7.95 0.02 1 3911 367 367 ARG HA H 4.09 0.02 1 3912 367 367 ARG HB2 H 1.99 0.02 2 3913 367 367 ARG HG2 H 1.84 0.02 2 3914 367 367 ARG HG3 H 1.75 0.02 2 3915 367 367 ARG HD2 H 3.21 0.02 2 3916 367 367 ARG HD3 H 3.25 0.02 2 3917 367 367 ARG C C 178.58 0.20 1 3918 367 367 ARG CA C 58.84 0.10 1 3919 367 367 ARG CB C 30.30 0.10 1 3920 367 367 ARG CG C 28.16 0.10 1 3921 367 367 ARG CD C 43.42 0.10 1 3922 367 367 ARG N N 119.96 0.10 1 3923 368 368 ILE H H 8.03 0.02 1 3924 368 368 ILE HA H 3.72 0.02 1 3925 368 368 ILE HB H 1.71 0.02 1 3926 368 368 ILE HG12 H 1.99 0.02 2 3927 368 368 ILE HG13 H 0.58 0.02 2 3928 368 368 ILE HG2 H 1.06 0.02 1 3929 368 368 ILE HD1 H 0.70 0.02 1 3930 368 368 ILE C C 177.05 0.20 1 3931 368 368 ILE CA C 64.95 0.10 1 3932 368 368 ILE CB C 39.10 0.10 1 3933 368 368 ILE CG1 C 29.49 0.10 1 3934 368 368 ILE CG2 C 20.30 0.10 1 3935 368 368 ILE CD1 C 15.69 0.10 1 3936 368 368 ILE N N 117.34 0.10 1 3937 369 369 THR H H 7.63 0.02 1 3938 369 369 THR HA H 4.47 0.02 1 3939 369 369 THR HB H 4.60 0.02 1 3940 369 369 THR HG2 H 1.38 0.02 1 3941 369 369 THR C C 174.11 0.20 1 3942 369 369 THR CA C 62.39 0.10 1 3943 369 369 THR CB C 70.34 0.10 1 3944 369 369 THR CG2 C 22.18 0.10 1 3945 369 369 THR N N 106.84 0.10 1 3946 370 370 LYS H H 7.37 0.02 1 3947 370 370 LYS HA H 4.11 0.02 1 3948 370 370 LYS HB2 H 1.92 0.02 2 3949 370 370 LYS HB3 H 1.87 0.02 2 3950 370 370 LYS HG2 H 1.55 0.02 2 3951 370 370 LYS HG3 H 1.51 0.02 2 3952 370 370 LYS HD2 H 1.71 0.02 2 3953 370 370 LYS HE2 H 3.02 0.02 2 3954 370 370 LYS CA C 58.95 0.10 1 3955 370 370 LYS CB C 32.96 0.10 1 3956 370 370 LYS CG C 24.83 0.10 1 3957 370 370 LYS CD C 29.36 0.10 1 3958 370 370 LYS CE C 42.26 0.10 1 3959 370 370 LYS N N 128.09 0.10 1 stop_ save_