data_25237 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR Structure of Maltose-binding protein from Escherichia coli, Northeast Structural Genomics Consortium (NESG) Target ER690 ; _BMRB_accession_number 25237 _BMRB_flat_file_name bmr25237.str _Entry_type original _Submission_date 2014-09-18 _Accession_date 2014-09-18 _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 Rossi Paolo . . 2 Lange Oliver F. . 3 Sgourakis Nikolaos G. . 4 Song Yifan . . 5 Lee Hsiau-Wei . . 6 Aramini James M. . 7 Ertekin Asli . . 8 Xiao Rong . . 9 Acton Thomas B. . 10 Baker David . . 11 Montelione Gaetano T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 464 "13C chemical shifts" 1137 "15N chemical shifts" 340 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-12-08 original author . stop_ _Original_release_date 2014-12-08 save_ ############################# # Citation for this entry # ############################# save_citations _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution NMR Structure of Maltose-binding protein from Escherichia coli, Northeast Structural Genomics Consortium (NESG) Target ER690' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rossi Paolo . . 2 Lange Oliver F. . 3 Sgourakis Nikolaos G. . 4 Song Yifan . . 5 Lee Hsiau-Wei . . 6 Aramini James M. . 7 Ertekin Asli . . 8 Xiao Rong . . 9 Acton Thomas B. . 10 Montelione Gaetano T. . 11 Baker David . . stop_ _Journal_abbreviation 'To be published' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name MBP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MBP $ER690 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ER690 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common ER690 _Molecular_mass 40724.547 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 370 _Mol_residue_sequence ; KIEEGKLVIWINGDKGYNGL AEVGKKFEKDTGIKVTVEHP DKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEIT PDKAFQDKLYPFTWDAVRYN GKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELK AKGKSALMFNLQEPYFTWPL IAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIK NKHMNADTDYSIAEAAFNKG ETAMTINGPRAWSNIDTSKV NYGVTVLPTFKGQPSKPFVG VLSAGINAASPNKELAKEFL ENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAAT MENAQKGEIMPNIPQMSAFW YAVRTAVINAASGRQTVDEA LKDAQTRITK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 LYS 2 2 ILE 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 ARG 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 2015-11-25 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4354 "E. coli maltose binding protein" 100.00 370 99.46 99.46 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 99.46 99.46 0.00e+00 PDB 1EZP "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin Using Peptide Orientations From Dipolar Couplings" 100.00 370 99.46 99.46 0.00e+00 PDB 1FQA "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.73 370 99.73 99.73 0.00e+00 PDB 1FQB "Structure Of Maltotriotol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.73 370 99.73 99.73 0.00e+00 PDB 1FQC "Crystal Structure Of Maltotriotol Bound To Closed-Form Maltodextrin Binding Protein" 99.73 370 99.73 99.73 0.00e+00 PDB 1FQD "Crystal Structure Of Maltotetraitol Bound To Closed-Form Maltodextrin Binding Protein" 99.73 370 99.73 99.73 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 98.90 98.90 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)" 100.00 370 100.00 100.00 0.00e+00 PDB 1MPC "Maltodextrin-binding Protein (maltose-binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (trp-230-arg)" 100.00 370 100.00 100.00 0.00e+00 PDB 1MPD "Maltodextrin-Binding Protein (Maltose-Binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (Trp-230-Arg)" 100.00 370 100.00 100.00 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 99.45 99.45 0.00e+00 PDB 1T0K "Joint X-ray And Nmr Refinement Of Yeast L30e-mrna Complex" 98.92 381 99.45 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 99.46 99.46 0.00e+00 PDB 2KLF "Pere Nmr Structure Of Maltodextrin-Binding Protein" 100.00 370 99.46 99.46 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 2N44 "Ec-nmr Structure Of Escherichia Coli Maltose-binding Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr" 100.00 370 99.73 99.73 0.00e+00 PDB 2N45 "Ec-nmr Structure Of Escherichia Coli Maltose-binding Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr" 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 99.73 99.73 0.00e+00 PDB 2OK2 "Muts C-Terminal Domain Fused To Maltose Binding Protein" 99.19 402 99.18 99.46 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 99.73 99.73 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 99.73 99.73 0.00e+00 PDB 3CSG "Crystal Structure Of Monobody Ys1(Mbp-74)MALTOSE BINDING Protein Fusion Complex" 98.92 461 99.73 99.73 0.00e+00 PDB 3D4C "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form I)" 98.92 481 98.63 98.63 0.00e+00 PDB 3D4G "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Ii)" 98.92 481 98.63 98.63 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 98.63 98.63 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" 99.19 393 98.64 98.64 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 3J9P "Structure Of The Trpa1 Ion Channel Determined By Electron Cryo- Microscopy" 98.92 1528 99.73 99.73 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 99.73 99.73 0.00e+00 PDB 3LBS "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Bound Form)" 97.84 384 99.45 99.72 0.00e+00 PDB 3LC8 "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Free Form)" 97.84 384 99.45 99.72 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)" 98.65 581 98.90 98.90 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" 99.19 378 99.46 99.46 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" 99.19 378 99.46 99.46 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 3WOA "Crystal Structure Of Lambda Repressor (1-45) Fused With Maltose- Binding Protein" 98.92 417 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 98.63 98.63 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 98.63 98.63 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 98.63 98.63 0.00e+00 PDB 4BLB "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli1p Complex" 98.92 753 98.09 98.09 0.00e+00 PDB 4BLD "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli3p Complex" 98.92 753 98.09 98.09 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 4QSZ "Crystal Structure Of Mouse Jmjd7 Fused With Maltose-binding Protein" 98.92 687 99.18 99.18 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 4RG5 "Crystal Structure Of S. Pombe Smn Yg-dimer" 99.73 401 99.73 99.73 0.00e+00 PDB 4RWF "Crystal Structure Of The Clr:ramp2 Extracellular Domain Heterodimer With Bound Adrenomedullin" 98.92 591 99.73 99.73 0.00e+00 PDB 4RWG "Crystal Structure Of The Clr:ramp1 Extracellular Domain Heterodimer With Bound High Affinity Cgrp Analog" 98.92 593 99.73 99.73 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 PDB 4WMS "Structure Of Apo Mbp-mcl1 At 1.9a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMT "Structure Of Mbp-mcl1 Bound To Ligand 1 At 2.35a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMU "Structure Of Mbp-mcl1 Bound To Ligand 2 At 1.55a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMV "Structure Of Mbp-mcl1 Bound To Ligand 4 At 2.4a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMW "The Structure Of Mbp-mcl1 Bound To Ligand 5 At 1.9a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMX "The Structure Of Mbp-mcl1 Bound To Ligand 6 At 2.0a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WVG "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb)" 97.30 542 99.44 99.72 0.00e+00 PDB 4WVH "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb) In Complex With A Substrate Peptide (pep1)." 97.30 533 98.61 98.89 0.00e+00 PDB 4WVI "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb) In Complex With A Substrate Peptide (pep2)." 97.30 533 98.61 98.89 0.00e+00 PDB 4WVJ "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb) In Complex With An Inhibitor Peptide (pep3)" 97.30 533 98.61 98.89 0.00e+00 PDB 4XAI "Crystal Structure Of Red Flour Beetle Nr2e1/tlx" 98.92 573 99.73 99.73 0.00e+00 PDB 4XAJ "Crystal Structure Of Human Nr2e1/tlx" 98.92 576 99.73 99.73 0.00e+00 PDB 5C7R "Revealing Surface Waters On An Antifreeze Protein By Fusion Protein Crystallography" 98.92 444 98.91 98.91 0.00e+00 PDB 5CL1 "Complex Structure Of Norrin With Human Frizzled 4" 98.92 483 99.73 99.73 0.00e+00 PDB 5DFM "Structure Of Tetrahymena Telomerase P19 Fused To Mbp" 98.92 534 98.91 98.91 0.00e+00 PDB 5DIS "Crystal Structure Of A Crm1-rangtp-spn1 Export Complex Bound To A 113 Amino Acid Fg-repeat Containing Fragment Of Nup214" 97.84 479 98.90 98.90 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. K12 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 99.73 99.73 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_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 WP_000367925 "hypothetical protein [Escherichia coli]" 50.81 188 98.94 99.47 1.26e-125 REF WP_000695369 "MULTISPECIES: sugar ABC transporter substrate-binding protein [Enterobacteriaceae]" 100.00 396 99.73 99.73 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 _Gene_mnemonic $ER690 'E. coli' 562 bacteria . Escherichia coli 'b4034, JW3994' 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 $ER690 'recombinant technology' . Escherichia coli BL21(DE3)pMgK pET21_NESG stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1.05 mM ER690.005, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ER690 1.05 mM 'natural abundance' H20 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task 'refinemen,structure solution,geometry optimization' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'refinement,geometry optimization,structure solution' stop_ _Details . save_ save_AutoStructure _Saveframe_category software _Name AutoStructure _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Huang, Tejero, Powers and Montelione' . . stop_ loop_ _Task 'data analysis,refinement' stop_ _Details . save_ save_AutoAssign _Saveframe_category software _Name AutoAssign _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Zimmerman, Moseley, Kulikowski and Montelione' . . stop_ loop_ _Task 'data analysis,chemical shift assignment' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'data analysis,peak picking,chemical shift assignment' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_VNMRJ _Saveframe_category software _Name VNMRJ _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_PINE _Saveframe_category software _Name PINE _Version . loop_ _Vendor _Address _Electronic_address 'Bahrami, Markley, Assadi, and Eghbalnia' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_TALOS+ _Saveframe_category software _Name TALOS+ _Version . loop_ _Vendor _Address _Electronic_address 'Shen, Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_PALES _Saveframe_category software _Name PALES _Version . loop_ _Vendor _Address _Electronic_address 'PALES (Zweckstetter, Bax)' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_REDCAT _Saveframe_category software _Name REDCAT _Version . loop_ _Vendor _Address _Electronic_address 'Valafar, Prestegard' . . stop_ loop_ _Task 'geometry optimization' stop_ _Details . save_ save_PSVS _Saveframe_category software _Name PSVS _Version . loop_ _Vendor _Address _Electronic_address 'Bhattacharya, Montelione' . . stop_ loop_ _Task 'structure validation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_(h)CCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (h)CCH-TOCSY' _Sample_label $sample_1 save_ save_3D_(h)NNH_HSQC-NOESY-HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (h)NNH HSQC-NOESY-HSQC' _Sample_label $sample_1 save_ save_3D_(h)CCH_HSQC-NOESY-HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (h)CCH HSQC-NOESY-HSQC' _Sample_label $sample_1 save_ save_3D_(h)CNH_HSQC-NOESY-HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (h)CNH HSQC-NOESY-HSQC' _Sample_label $sample_1 save_ save_3D_(h)NCH_HSQC-NOESY-HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (h)NCH HSQC-NOESY-HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 . pH pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $AutoAssign $NMRPipe $XEASY $PINE $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HNCO' '3D CBCA(CO)NH' '3D HNCACB' '3D 1H-13C NOESY' '3D 1H-15N NOESY' '3D (h)CCH-TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 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 C C 176.453 0.400 1 2 1 1 LYS CA C 56.408 0.400 1 3 1 1 LYS CB C 32.880 0.400 1 4 2 2 ILE H H 7.988 0.020 1 5 2 2 ILE HD1 H 0.402 0.020 1 6 2 2 ILE C C 176.016 0.400 1 7 2 2 ILE CA C 62.458 0.400 1 8 2 2 ILE CB C 38.298 0.400 1 9 2 2 ILE CD1 C 13.054 0.400 1 10 2 2 ILE N N 123.415 0.400 1 11 3 3 GLU H H 8.640 0.020 1 12 3 3 GLU C C 176.438 0.400 1 13 3 3 GLU CA C 56.417 0.400 1 14 3 3 GLU CB C 31.187 0.400 1 15 3 3 GLU N N 126.626 0.400 1 16 4 4 GLU H H 8.633 0.020 1 17 4 4 GLU C C 177.433 0.400 1 18 4 4 GLU CA C 56.989 0.400 1 19 4 4 GLU CB C 30.024 0.400 1 20 4 4 GLU N N 124.204 0.400 1 21 5 5 GLY H H 8.983 0.020 1 22 5 5 GLY C C 172.261 0.400 1 23 5 5 GLY CA C 45.937 0.400 1 24 5 5 GLY N N 111.365 0.400 1 25 6 6 LYS H H 7.582 0.020 1 26 6 6 LYS C C 173.108 0.400 1 27 6 6 LYS CA C 54.965 0.400 1 28 6 6 LYS CB C 35.109 0.400 1 29 6 6 LYS N N 118.910 0.400 1 30 7 7 LEU H H 8.237 0.020 1 31 7 7 LEU HD1 H 0.267 0.020 2 32 7 7 LEU HD2 H 0.615 0.020 2 33 7 7 LEU C C 175.788 0.400 1 34 7 7 LEU CA C 53.365 0.400 1 35 7 7 LEU CB C 46.699 0.400 1 36 7 7 LEU CD1 C 25.203 0.400 1 37 7 7 LEU CD2 C 24.064 0.400 1 38 7 7 LEU N N 116.121 0.400 1 39 8 8 VAL H H 10.153 0.020 1 40 8 8 VAL HG1 H 0.876 0.020 2 41 8 8 VAL HG2 H 0.923 0.020 2 42 8 8 VAL C C 176.033 0.400 1 43 8 8 VAL CA C 61.918 0.400 1 44 8 8 VAL CB C 33.845 0.400 1 45 8 8 VAL CG1 C 20.962 0.400 1 46 8 8 VAL CG2 C 21.211 0.400 1 47 8 8 VAL N N 125.470 0.400 1 48 9 9 ILE H H 9.117 0.020 1 49 9 9 ILE HD1 H 0.346 0.020 1 50 9 9 ILE C C 174.901 0.400 1 51 9 9 ILE CA C 59.974 0.400 1 52 9 9 ILE CB C 40.926 0.400 1 53 9 9 ILE CD1 C 14.523 0.400 1 54 9 9 ILE N N 128.221 0.400 1 55 10 10 TRP H H 9.032 0.020 1 56 10 10 TRP HE1 H 10.610 0.020 1 57 10 10 TRP C C 174.116 0.400 1 58 10 10 TRP CA C 54.451 0.400 1 59 10 10 TRP CB C 32.669 0.400 1 60 10 10 TRP N N 126.710 0.400 1 61 10 10 TRP NE1 N 129.337 0.400 1 62 11 11 ILE H H 8.700 0.020 1 63 11 11 ILE HD1 H 0.107 0.020 1 64 11 11 ILE C C 171.286 0.400 1 65 11 11 ILE CA C 59.976 0.400 1 66 11 11 ILE CB C 41.304 0.400 1 67 11 11 ILE CD1 C 13.105 0.400 1 68 11 11 ILE N N 122.081 0.400 1 69 12 12 ASN H H 8.922 0.020 1 70 12 12 ASN C C 177.503 0.400 1 71 12 12 ASN CA C 54.628 0.400 1 72 12 12 ASN CB C 39.936 0.400 1 73 12 12 ASN N N 122.990 0.400 1 74 13 13 GLY H H 8.287 0.020 1 75 13 13 GLY C C 173.365 0.400 1 76 13 13 GLY CA C 46.560 0.400 1 77 13 13 GLY N N 106.791 0.400 1 78 14 14 ASP H H 7.990 0.020 1 79 14 14 ASP C C 176.544 0.400 1 80 14 14 ASP CA C 53.217 0.400 1 81 14 14 ASP CB C 39.635 0.400 1 82 14 14 ASP N N 117.008 0.400 1 83 15 15 LYS H H 7.576 0.020 1 84 15 15 LYS C C 177.640 0.400 1 85 15 15 LYS CA C 53.230 0.400 1 86 15 15 LYS CB C 32.784 0.400 1 87 15 15 LYS N N 118.724 0.400 1 88 16 16 GLY H H 8.739 0.020 1 89 16 16 GLY C C 175.872 0.400 1 90 16 16 GLY CA C 48.203 0.400 1 91 16 16 GLY N N 108.204 0.400 1 92 17 17 TYR H H 8.287 0.020 1 93 17 17 TYR C C 177.234 0.400 1 94 17 17 TYR CA C 59.803 0.400 1 95 17 17 TYR CB C 37.646 0.400 1 96 17 17 TYR N N 120.664 0.400 1 97 18 18 ASN H H 8.109 0.020 1 98 18 18 ASN C C 179.208 0.400 1 99 18 18 ASN CA C 56.445 0.400 1 100 18 18 ASN CB C 37.499 0.400 1 101 18 18 ASN N N 123.757 0.400 1 102 19 19 GLY H H 9.023 0.020 1 103 19 19 GLY C C 176.074 0.400 1 104 19 19 GLY CA C 47.490 0.400 1 105 19 19 GLY N N 111.780 0.400 1 106 20 20 LEU H H 8.336 0.020 1 107 20 20 LEU HD1 H 0.876 0.020 2 108 20 20 LEU HD2 H 0.638 0.020 2 109 20 20 LEU C C 178.845 0.400 1 110 20 20 LEU CA C 57.821 0.400 1 111 20 20 LEU CB C 41.221 0.400 1 112 20 20 LEU CD1 C 24.725 0.400 1 113 20 20 LEU CD2 C 26.879 0.400 1 114 20 20 LEU N N 121.835 0.400 1 115 21 21 ALA H H 8.143 0.020 1 116 21 21 ALA C C 180.845 0.400 1 117 21 21 ALA CA C 55.317 0.400 1 118 21 21 ALA CB C 17.478 0.400 1 119 21 21 ALA N N 121.302 0.400 1 120 22 22 GLU H H 7.825 0.020 1 121 22 22 GLU C C 180.280 0.400 1 122 22 22 GLU CA C 59.876 0.400 1 123 22 22 GLU CB C 28.487 0.400 1 124 22 22 GLU N N 120.559 0.400 1 125 23 23 VAL H H 7.842 0.020 1 126 23 23 VAL HG1 H 0.823 0.020 2 127 23 23 VAL HG2 H 1.252 0.020 2 128 23 23 VAL C C 179.592 0.400 1 129 23 23 VAL CA C 66.874 0.400 1 130 23 23 VAL CB C 31.497 0.400 1 131 23 23 VAL CG1 C 22.314 0.400 1 132 23 23 VAL CG2 C 23.403 0.400 1 133 23 23 VAL N N 123.306 0.400 1 134 24 24 GLY H H 8.723 0.020 1 135 24 24 GLY C C 175.393 0.400 1 136 24 24 GLY CA C 47.698 0.400 1 137 24 24 GLY N N 106.853 0.400 1 138 25 25 LYS H H 8.342 0.020 1 139 25 25 LYS C C 179.664 0.400 1 140 25 25 LYS CA C 59.448 0.400 1 141 25 25 LYS CB C 31.663 0.400 1 142 25 25 LYS N N 122.996 0.400 1 143 26 26 LYS H H 7.690 0.020 1 144 26 26 LYS C C 178.246 0.400 1 145 26 26 LYS CA C 59.777 0.400 1 146 26 26 LYS CB C 31.838 0.400 1 147 26 26 LYS N N 123.048 0.400 1 148 27 27 PHE H H 8.129 0.020 1 149 27 27 PHE C C 179.166 0.400 1 150 27 27 PHE CA C 61.492 0.400 1 151 27 27 PHE CB C 39.203 0.400 1 152 27 27 PHE N N 120.127 0.400 1 153 28 28 GLU H H 8.864 0.020 1 154 28 28 GLU C C 180.031 0.400 1 155 28 28 GLU CA C 59.297 0.400 1 156 28 28 GLU CB C 29.547 0.400 1 157 28 28 GLU N N 124.241 0.400 1 158 29 29 LYS H H 8.152 0.020 1 159 29 29 LYS CA C 59.596 0.400 1 160 29 29 LYS CB C 31.171 0.400 1 161 29 29 LYS N N 122.179 0.400 1 162 30 30 ASP H H 7.615 0.020 1 163 30 30 ASP C C 178.471 0.400 1 164 30 30 ASP CA C 56.840 0.400 1 165 30 30 ASP CB C 41.001 0.400 1 166 30 30 ASP N N 116.490 0.400 1 167 31 31 THR H H 7.930 0.020 1 168 31 31 THR C C 176.383 0.400 1 169 31 31 THR CA C 62.830 0.400 1 170 31 31 THR CB C 72.293 0.400 1 171 31 31 THR N N 107.255 0.400 1 172 32 32 GLY H H 8.600 0.020 1 173 32 32 GLY C C 173.645 0.400 1 174 32 32 GLY CA C 45.563 0.400 1 175 32 32 GLY N N 112.891 0.400 1 176 33 33 ILE H H 7.752 0.020 1 177 33 33 ILE HD1 H 0.574 0.020 1 178 33 33 ILE C C 173.715 0.400 1 179 33 33 ILE CA C 59.048 0.400 1 180 33 33 ILE CB C 35.660 0.400 1 181 33 33 ILE CD1 C 10.138 0.400 1 182 33 33 ILE N N 124.535 0.400 1 183 34 34 LYS H H 7.920 0.020 1 184 34 34 LYS C C 175.675 0.400 1 185 34 34 LYS CA C 56.969 0.400 1 186 34 34 LYS CB C 32.694 0.400 1 187 34 34 LYS N N 125.011 0.400 1 188 35 35 VAL H H 8.348 0.020 1 189 35 35 VAL HG1 H 0.331 0.020 2 190 35 35 VAL HG2 H 0.760 0.020 2 191 35 35 VAL C C 175.898 0.400 1 192 35 35 VAL CA C 61.064 0.400 1 193 35 35 VAL CB C 33.372 0.400 1 194 35 35 VAL CG1 C 20.685 0.400 1 195 35 35 VAL CG2 C 22.360 0.400 1 196 35 35 VAL N N 124.422 0.400 1 197 36 36 THR H H 9.176 0.020 1 198 36 36 THR C C 172.762 0.400 1 199 36 36 THR CA C 61.594 0.400 1 200 36 36 THR CB C 70.974 0.400 1 201 36 36 THR N N 125.315 0.400 1 202 37 37 VAL H H 8.920 0.020 1 203 37 37 VAL HG1 H 0.951 0.020 2 204 37 37 VAL HG2 H 0.766 0.020 2 205 37 37 VAL C C 175.348 0.400 1 206 37 37 VAL CA C 61.689 0.400 1 207 37 37 VAL CB C 32.431 0.400 1 208 37 37 VAL CG1 C 22.840 0.400 1 209 37 37 VAL CG2 C 20.673 0.400 1 210 37 37 VAL N N 127.530 0.400 1 211 38 38 GLU H H 9.643 0.020 1 212 38 38 GLU C C 173.567 0.400 1 213 38 38 GLU CA C 54.475 0.400 1 214 38 38 GLU CB C 33.046 0.400 1 215 38 38 GLU N N 127.167 0.400 1 216 39 39 HIS H H 8.297 0.020 1 217 39 39 HIS CA C 51.527 0.400 1 218 39 39 HIS CB C 28.597 0.400 1 219 39 39 HIS N N 115.302 0.400 1 220 40 40 PRO C C 176.926 0.400 1 221 40 40 PRO CA C 62.226 0.400 1 222 40 40 PRO CB C 30.665 0.400 1 223 41 41 ASP H H 8.215 0.020 1 224 41 41 ASP C C 176.581 0.400 1 225 41 41 ASP CA C 54.829 0.400 1 226 41 41 ASP CB C 41.029 0.400 1 227 41 41 ASP N N 121.163 0.400 1 228 42 42 LYS H H 8.774 0.020 1 229 42 42 LYS C C 178.612 0.400 1 230 42 42 LYS CA C 56.642 0.400 1 231 42 42 LYS CB C 29.442 0.400 1 232 42 42 LYS N N 119.241 0.400 1 233 43 43 LEU H H 7.385 0.020 1 234 43 43 LEU HD1 H 1.101 0.020 2 235 43 43 LEU HD2 H 1.133 0.020 2 236 43 43 LEU C C 175.961 0.400 1 237 43 43 LEU CA C 59.806 0.400 1 238 43 43 LEU CB C 40.897 0.400 1 239 43 43 LEU CD1 C 26.677 0.400 1 240 43 43 LEU CD2 C 26.431 0.400 1 241 43 43 LEU N N 120.020 0.400 1 242 44 44 GLU H H 10.448 0.020 1 243 44 44 GLU C C 178.284 0.400 1 244 44 44 GLU CA C 57.383 0.400 1 245 44 44 GLU CB C 24.597 0.400 1 246 44 44 GLU N N 123.847 0.400 1 247 45 45 GLU H H 7.326 0.020 1 248 45 45 GLU C C 178.462 0.400 1 249 45 45 GLU CA C 56.456 0.400 1 250 45 45 GLU CB C 29.961 0.400 1 251 45 45 GLU N N 120.295 0.400 1 252 46 46 LYS H H 8.285 0.020 1 253 46 46 LYS C C 179.121 0.400 1 254 46 46 LYS CA C 58.611 0.400 1 255 46 46 LYS CB C 33.277 0.400 1 256 46 46 LYS N N 120.581 0.400 1 257 47 47 PHE H H 8.657 0.020 1 258 47 47 PHE CA C 63.747 0.400 1 259 47 47 PHE CB C 36.001 0.400 1 260 47 47 PHE N N 116.931 0.400 1 261 48 48 PRO C C 178.106 0.400 1 262 48 48 PRO CA C 65.499 0.400 1 263 48 48 PRO CB C 30.015 0.400 1 264 49 49 GLN H H 6.833 0.020 1 265 49 49 GLN C C 178.513 0.400 1 266 49 49 GLN CA C 58.331 0.400 1 267 49 49 GLN CB C 28.541 0.400 1 268 49 49 GLN N N 115.257 0.400 1 269 50 50 VAL H H 7.730 0.020 1 270 50 50 VAL HG1 H 0.967 0.020 2 271 50 50 VAL HG2 H 0.906 0.020 2 272 50 50 VAL C C 178.512 0.400 1 273 50 50 VAL CA C 62.603 0.400 1 274 50 50 VAL CB C 32.167 0.400 1 275 50 50 VAL CG1 C 21.260 0.400 1 276 50 50 VAL CG2 C 19.894 0.400 1 277 50 50 VAL N N 111.081 0.400 1 278 51 51 ALA H H 8.347 0.020 1 279 51 51 ALA C C 180.521 0.400 1 280 51 51 ALA CA C 54.700 0.400 1 281 51 51 ALA CB C 17.566 0.400 1 282 51 51 ALA N N 125.689 0.400 1 283 52 52 ALA H H 7.395 0.020 1 284 52 52 ALA C C 178.618 0.400 1 285 52 52 ALA CA C 53.841 0.400 1 286 52 52 ALA CB C 18.146 0.400 1 287 52 52 ALA N N 118.252 0.400 1 288 53 53 THR H H 7.229 0.020 1 289 53 53 THR C C 175.138 0.400 1 290 53 53 THR CA C 61.307 0.400 1 291 53 53 THR CB C 69.750 0.400 1 292 53 53 THR N N 106.054 0.400 1 293 54 54 GLY H H 7.751 0.020 1 294 54 54 GLY C C 172.610 0.400 1 295 54 54 GLY CA C 45.722 0.400 1 296 54 54 GLY N N 109.258 0.400 1 297 55 55 ASP H H 7.395 0.020 1 298 55 55 ASP C C 174.814 0.400 1 299 55 55 ASP CA C 52.778 0.400 1 300 55 55 ASP CB C 43.412 0.400 1 301 55 55 ASP N N 119.703 0.400 1 302 56 56 GLY H H 8.332 0.020 1 303 56 56 GLY CA C 43.790 0.400 1 304 56 56 GLY N N 105.503 0.400 1 305 57 57 PRO C C 175.448 0.400 1 306 57 57 PRO CA C 61.575 0.400 1 307 57 57 PRO CB C 30.658 0.400 1 308 58 58 ASP H H 8.698 0.020 1 309 58 58 ASP C C 176.037 0.400 1 310 58 58 ASP CA C 58.668 0.400 1 311 58 58 ASP CB C 43.983 0.400 1 312 58 58 ASP N N 117.791 0.400 1 313 59 59 ILE H H 7.631 0.020 1 314 59 59 ILE HD1 H 0.735 0.020 1 315 59 59 ILE C C 173.696 0.400 1 316 59 59 ILE CA C 58.982 0.400 1 317 59 59 ILE CB C 42.695 0.400 1 318 59 59 ILE CD1 C 13.790 0.400 1 319 59 59 ILE N N 114.107 0.400 1 320 60 60 ILE H H 8.897 0.020 1 321 60 60 ILE HD1 H 0.452 0.020 1 322 60 60 ILE C C 172.929 0.400 1 323 60 60 ILE CA C 58.076 0.400 1 324 60 60 ILE CB C 41.343 0.400 1 325 60 60 ILE CD1 C 14.568 0.400 1 326 60 60 ILE N N 124.531 0.400 1 327 61 61 PHE H H 8.602 0.020 1 328 61 61 PHE C C 176.742 0.400 1 329 61 61 PHE CA C 55.839 0.400 1 330 61 61 PHE CB C 41.950 0.400 1 331 61 61 PHE N N 126.191 0.400 1 332 62 62 TRP H H 9.180 0.020 1 333 62 62 TRP HE1 H 10.321 0.020 1 334 62 62 TRP C C 173.771 0.400 1 335 62 62 TRP CA C 57.786 0.400 1 336 62 62 TRP CB C 31.813 0.400 1 337 62 62 TRP N N 121.352 0.400 1 338 62 62 TRP NE1 N 129.552 0.400 1 339 63 63 ALA H H 6.297 0.020 1 340 63 63 ALA C C 179.957 0.400 1 341 63 63 ALA CA C 54.068 0.400 1 342 63 63 ALA CB C 18.639 0.400 1 343 63 63 ALA N N 125.965 0.400 1 344 64 64 HIS H H 7.999 0.020 1 345 64 64 HIS HE2 H 13.180 0.020 1 346 64 64 HIS C C 178.490 0.400 1 347 64 64 HIS CA C 60.167 0.400 1 348 64 64 HIS CB C 30.244 0.400 1 349 64 64 HIS N N 115.783 0.400 1 350 64 64 HIS NE2 N 133.600 0.400 1 351 65 65 ASP H H 7.721 0.020 1 352 65 65 ASP C C 177.968 0.400 1 353 65 65 ASP CA C 57.074 0.400 1 354 65 65 ASP CB C 39.500 0.400 1 355 65 65 ASP N N 119.219 0.400 1 356 66 66 ARG H H 6.911 0.020 1 357 66 66 ARG C C 177.663 0.400 1 358 66 66 ARG CA C 55.042 0.400 1 359 66 66 ARG CB C 29.530 0.400 1 360 66 66 ARG N N 116.099 0.400 1 361 67 67 PHE H H 7.687 0.020 1 362 67 67 PHE C C 177.883 0.400 1 363 67 67 PHE CA C 58.703 0.400 1 364 67 67 PHE CB C 36.331 0.400 1 365 67 67 PHE N N 116.978 0.400 1 366 68 68 GLY H H 7.273 0.020 1 367 68 68 GLY C C 175.810 0.400 1 368 68 68 GLY CA C 47.517 0.400 1 369 68 68 GLY N N 107.291 0.400 1 370 69 69 GLY H H 7.650 0.020 1 371 69 69 GLY C C 177.239 0.400 1 372 69 69 GLY CA C 47.089 0.400 1 373 69 69 GLY N N 107.542 0.400 1 374 70 70 TYR H H 6.974 0.020 1 375 70 70 TYR C C 178.454 0.400 1 376 70 70 TYR CA C 57.372 0.400 1 377 70 70 TYR CB C 35.758 0.400 1 378 70 70 TYR N N 119.254 0.400 1 379 71 71 ALA H H 8.625 0.020 1 380 71 71 ALA C C 182.277 0.400 1 381 71 71 ALA CA C 54.487 0.400 1 382 71 71 ALA CB C 18.040 0.400 1 383 71 71 ALA N N 122.642 0.400 1 384 72 72 GLN H H 8.710 0.020 1 385 72 72 GLN C C 177.850 0.400 1 386 72 72 GLN CA C 58.635 0.400 1 387 72 72 GLN CB C 27.562 0.400 1 388 72 72 GLN N N 122.857 0.400 1 389 73 73 SER H H 7.362 0.020 1 390 73 73 SER C C 173.702 0.400 1 391 73 73 SER CA C 59.274 0.400 1 392 73 73 SER CB C 64.148 0.400 1 393 73 73 SER N N 112.177 0.400 1 394 74 74 GLY H H 8.083 0.020 1 395 74 74 GLY C C 176.186 0.400 1 396 74 74 GLY CA C 46.341 0.400 1 397 74 74 GLY N N 109.400 0.400 1 398 75 75 LEU H H 7.814 0.020 1 399 75 75 LEU HD1 H 0.638 0.020 2 400 75 75 LEU HD2 H 0.538 0.020 2 401 75 75 LEU C C 177.608 0.400 1 402 75 75 LEU CA C 55.677 0.400 1 403 75 75 LEU CB C 42.483 0.400 1 404 75 75 LEU CD1 C 25.725 0.400 1 405 75 75 LEU CD2 C 20.664 0.400 1 406 75 75 LEU N N 113.934 0.400 1 407 76 76 LEU H H 7.432 0.020 1 408 76 76 LEU HD1 H 0.897 0.020 2 409 76 76 LEU HD2 H 0.538 0.020 2 410 76 76 LEU C C 176.782 0.400 1 411 76 76 LEU CA C 52.794 0.400 1 412 76 76 LEU CB C 43.798 0.400 1 413 76 76 LEU CD1 C 27.430 0.400 1 414 76 76 LEU CD2 C 21.891 0.400 1 415 76 76 LEU N N 115.904 0.400 1 416 77 77 ALA H H 9.006 0.020 1 417 77 77 ALA C C 176.398 0.400 1 418 77 77 ALA CA C 51.102 0.400 1 419 77 77 ALA CB C 19.120 0.400 1 420 77 77 ALA N N 125.955 0.400 1 421 78 78 GLU H H 8.229 0.020 1 422 78 78 GLU C C 176.784 0.400 1 423 78 78 GLU CA C 56.426 0.400 1 424 78 78 GLU CB C 29.286 0.400 1 425 78 78 GLU N N 120.937 0.400 1 426 79 79 ILE H H 8.176 0.020 1 427 79 79 ILE HD1 H 0.161 0.020 1 428 79 79 ILE C C 175.746 0.400 1 429 79 79 ILE CA C 59.839 0.400 1 430 79 79 ILE CB C 38.941 0.400 1 431 79 79 ILE CD1 C 12.313 0.400 1 432 79 79 ILE N N 122.869 0.400 1 433 80 80 THR H H 8.786 0.020 1 434 80 80 THR CA C 57.984 0.400 1 435 80 80 THR CB C 69.327 0.400 1 436 80 80 THR N N 112.789 0.400 1 437 81 81 PRO C C 177.695 0.400 1 438 81 81 PRO CA C 62.548 0.400 1 439 81 81 PRO CB C 31.586 0.400 1 440 82 82 ASP H H 9.117 0.020 1 441 82 82 ASP CA C 53.594 0.400 1 442 82 82 ASP CB C 41.513 0.400 1 443 82 82 ASP N N 123.842 0.400 1 444 83 83 LYS C C 177.708 0.400 1 445 83 83 LYS CA C 59.912 0.400 1 446 83 83 LYS CB C 31.752 0.400 1 447 84 84 ALA H H 8.192 0.020 1 448 84 84 ALA C C 180.452 0.400 1 449 84 84 ALA CA C 54.875 0.400 1 450 84 84 ALA CB C 17.553 0.400 1 451 84 84 ALA N N 119.536 0.400 1 452 85 85 PHE H H 7.959 0.020 1 453 85 85 PHE C C 178.439 0.400 1 454 85 85 PHE CA C 62.571 0.400 1 455 85 85 PHE CB C 39.035 0.400 1 456 85 85 PHE N N 118.632 0.400 1 457 86 86 GLN H H 8.512 0.020 1 458 86 86 GLN C C 180.140 0.400 1 459 86 86 GLN CA C 59.616 0.400 1 460 86 86 GLN CB C 28.073 0.400 1 461 86 86 GLN N N 117.282 0.400 1 462 87 87 ASP H H 8.052 0.020 1 463 87 87 ASP C C 176.576 0.400 1 464 87 87 ASP CA C 56.177 0.400 1 465 87 87 ASP CB C 40.956 0.400 1 466 87 87 ASP N N 116.918 0.400 1 467 88 88 LYS H H 7.815 0.020 1 468 88 88 LYS C C 176.797 0.400 1 469 88 88 LYS CA C 58.402 0.400 1 470 88 88 LYS CB C 31.855 0.400 1 471 88 88 LYS N N 117.287 0.400 1 472 89 89 LEU H H 7.661 0.020 1 473 89 89 LEU HD1 H 0.526 0.020 2 474 89 89 LEU HD2 H 0.484 0.020 2 475 89 89 LEU C C 176.725 0.400 1 476 89 89 LEU CA C 53.550 0.400 1 477 89 89 LEU CB C 42.609 0.400 1 478 89 89 LEU CD1 C 26.152 0.400 1 479 89 89 LEU CD2 C 25.298 0.400 1 480 89 89 LEU N N 120.004 0.400 1 481 90 90 TYR H H 7.620 0.020 1 482 90 90 TYR CA C 59.276 0.400 1 483 90 90 TYR CB C 38.921 0.400 1 484 90 90 TYR N N 116.751 0.400 1 485 91 91 PRO C C 179.472 0.400 1 486 91 91 PRO CA C 66.902 0.400 1 487 91 91 PRO CB C 31.380 0.400 1 488 92 92 PHE H H 8.010 0.020 1 489 92 92 PHE C C 176.471 0.400 1 490 92 92 PHE CA C 59.517 0.400 1 491 92 92 PHE CB C 36.630 0.400 1 492 92 92 PHE N N 112.620 0.400 1 493 93 93 THR H H 7.100 0.020 1 494 93 93 THR C C 176.347 0.400 1 495 93 93 THR CA C 64.755 0.400 1 496 93 93 THR CB C 67.099 0.400 1 497 93 93 THR N N 111.501 0.400 1 498 94 94 TRP H H 6.595 0.020 1 499 94 94 TRP HE1 H 10.570 0.020 1 500 94 94 TRP C C 178.465 0.400 1 501 94 94 TRP CA C 58.672 0.400 1 502 94 94 TRP CB C 29.411 0.400 1 503 94 94 TRP N N 120.085 0.400 1 504 94 94 TRP NE1 N 129.101 0.400 1 505 95 95 ASP H H 7.311 0.020 1 506 95 95 ASP C C 178.700 0.400 1 507 95 95 ASP CA C 57.436 0.400 1 508 95 95 ASP CB C 39.916 0.400 1 509 95 95 ASP N N 115.560 0.400 1 510 96 96 ALA H H 6.989 0.020 1 511 96 96 ALA C C 177.085 0.400 1 512 96 96 ALA CA C 54.000 0.400 1 513 96 96 ALA CB C 17.727 0.400 1 514 96 96 ALA N N 118.728 0.400 1 515 97 97 VAL H H 7.002 0.020 1 516 97 97 VAL HG1 H 0.578 0.020 2 517 97 97 VAL HG2 H 1.347 0.020 2 518 97 97 VAL C C 172.577 0.400 1 519 97 97 VAL CA C 59.857 0.400 1 520 97 97 VAL CB C 30.785 0.400 1 521 97 97 VAL CG1 C 22.085 0.400 1 522 97 97 VAL CG2 C 19.363 0.400 1 523 97 97 VAL N N 106.208 0.400 1 524 98 98 ARG H H 7.048 0.020 1 525 98 98 ARG C C 176.565 0.400 1 526 98 98 ARG CA C 55.065 0.400 1 527 98 98 ARG CB C 31.357 0.400 1 528 98 98 ARG N N 121.682 0.400 1 529 99 99 TYR H H 9.706 0.020 1 530 99 99 TYR CA C 58.493 0.400 1 531 99 99 TYR CB C 41.936 0.400 1 532 99 99 TYR N N 127.480 0.400 1 533 100 100 ASN C C 175.400 0.400 1 534 100 100 ASN CA C 53.907 0.400 1 535 100 100 ASN CB C 37.221 0.400 1 536 101 101 GLY H H 8.648 0.020 1 537 101 101 GLY C C 173.987 0.400 1 538 101 101 GLY CA C 45.638 0.400 1 539 101 101 GLY N N 102.271 0.400 1 540 102 102 LYS H H 7.760 0.020 1 541 102 102 LYS C C 175.208 0.400 1 542 102 102 LYS CA C 54.578 0.400 1 543 102 102 LYS CB C 34.731 0.400 1 544 102 102 LYS N N 121.247 0.400 1 545 103 103 LEU H H 8.966 0.020 1 546 103 103 LEU HD1 H 0.490 0.020 2 547 103 103 LEU HD2 H 0.972 0.020 2 548 103 103 LEU C C 178.524 0.400 1 549 103 103 LEU CA C 55.200 0.400 1 550 103 103 LEU CB C 42.179 0.400 1 551 103 103 LEU CD1 C 24.748 0.400 1 552 103 103 LEU CD2 C 24.100 0.400 1 553 103 103 LEU N N 123.231 0.400 1 554 104 104 ILE H H 8.774 0.020 1 555 104 104 ILE HG2 H 0.889 0.020 1 556 104 104 ILE HD1 H 0.845 0.020 1 557 104 104 ILE C C 175.468 0.400 1 558 104 104 ILE CA C 59.655 0.400 1 559 104 104 ILE CB C 39.029 0.400 1 560 104 104 ILE CG2 C 19.739 0.400 1 561 104 104 ILE CD1 C 14.779 0.400 1 562 104 104 ILE N N 112.821 0.400 1 563 105 105 ALA H H 7.668 0.020 1 564 105 105 ALA C C 173.871 0.400 1 565 105 105 ALA CA C 52.152 0.400 1 566 105 105 ALA CB C 22.111 0.400 1 567 105 105 ALA N N 117.404 0.400 1 568 106 106 TYR H H 8.976 0.020 1 569 106 106 TYR CA C 56.214 0.400 1 570 106 106 TYR CB C 39.931 0.400 1 571 106 106 TYR N N 113.914 0.400 1 572 107 107 PRO C C 174.609 0.400 1 573 107 107 PRO CA C 62.281 0.400 1 574 107 107 PRO CB C 32.783 0.400 1 575 108 108 ILE H H 8.516 0.020 1 576 108 108 ILE HD1 H 0.637 0.020 1 577 108 108 ILE C C 176.711 0.400 1 578 108 108 ILE CA C 60.276 0.400 1 579 108 108 ILE CB C 37.612 0.400 1 580 108 108 ILE CD1 C 9.981 0.400 1 581 108 108 ILE N N 115.372 0.400 1 582 109 109 ALA H H 7.855 0.020 1 583 109 109 ALA C C 174.628 0.400 1 584 109 109 ALA CA C 50.761 0.400 1 585 109 109 ALA CB C 23.471 0.400 1 586 109 109 ALA N N 118.152 0.400 1 587 110 110 VAL H H 8.781 0.020 1 588 110 110 VAL HG1 H 0.767 0.020 2 589 110 110 VAL HG2 H 0.476 0.020 2 590 110 110 VAL C C 173.634 0.400 1 591 110 110 VAL CA C 62.167 0.400 1 592 110 110 VAL CB C 34.093 0.400 1 593 110 110 VAL CG1 C 20.954 0.400 1 594 110 110 VAL CG2 C 20.424 0.400 1 595 110 110 VAL N N 121.414 0.400 1 596 111 111 GLU H H 9.596 0.020 1 597 111 111 GLU C C 173.917 0.400 1 598 111 111 GLU CA C 54.847 0.400 1 599 111 111 GLU CB C 32.976 0.400 1 600 111 111 GLU N N 123.136 0.400 1 601 112 112 ALA H H 6.355 0.020 1 602 112 112 ALA C C 176.641 0.400 1 603 112 112 ALA CA C 50.959 0.400 1 604 112 112 ALA CB C 22.076 0.400 1 605 112 112 ALA N N 117.074 0.400 1 606 113 113 LEU H H 8.456 0.020 1 607 113 113 LEU HD1 H 0.691 0.020 2 608 113 113 LEU HD2 H 0.854 0.020 2 609 113 113 LEU C C 173.598 0.400 1 610 113 113 LEU CA C 55.257 0.400 1 611 113 113 LEU CB C 43.367 0.400 1 612 113 113 LEU CD1 C 26.792 0.400 1 613 113 113 LEU CD2 C 23.625 0.400 1 614 113 113 LEU N N 123.255 0.400 1 615 114 114 SER H H 7.494 0.020 1 616 114 114 SER C C 172.040 0.400 1 617 114 114 SER CA C 57.265 0.400 1 618 114 114 SER CB C 67.447 0.400 1 619 114 114 SER N N 108.167 0.400 1 620 115 115 LEU H H 7.308 0.020 1 621 115 115 LEU HD1 H 0.684 0.020 2 622 115 115 LEU HD2 H 0.587 0.020 2 623 115 115 LEU C C 174.244 0.400 1 624 115 115 LEU CA C 54.482 0.400 1 625 115 115 LEU CB C 43.729 0.400 1 626 115 115 LEU CD1 C 22.828 0.400 1 627 115 115 LEU CD2 C 24.597 0.400 1 628 115 115 LEU N N 122.337 0.400 1 629 116 116 ILE H H 8.666 0.020 1 630 116 116 ILE HD1 H 0.459 0.020 1 631 116 116 ILE C C 174.596 0.400 1 632 116 116 ILE CA C 60.103 0.400 1 633 116 116 ILE CB C 38.153 0.400 1 634 116 116 ILE CD1 C 13.706 0.400 1 635 116 116 ILE N N 129.613 0.400 1 636 117 117 TYR H H 9.061 0.020 1 637 117 117 TYR C C 172.945 0.400 1 638 117 117 TYR CA C 54.610 0.400 1 639 117 117 TYR CB C 42.250 0.400 1 640 117 117 TYR N N 121.829 0.400 1 641 118 118 ASN H H 9.303 0.020 1 642 118 118 ASN C C 175.772 0.400 1 643 118 118 ASN CA C 52.211 0.400 1 644 118 118 ASN CB C 37.620 0.400 1 645 118 118 ASN N N 121.191 0.400 1 646 119 119 LYS H H 8.805 0.020 1 647 119 119 LYS C C 177.723 0.400 1 648 119 119 LYS CA C 58.733 0.400 1 649 119 119 LYS CB C 32.435 0.400 1 650 119 119 LYS N N 125.523 0.400 1 651 120 120 ASP H H 8.153 0.020 1 652 120 120 ASP C C 177.651 0.400 1 653 120 120 ASP CA C 56.643 0.400 1 654 120 120 ASP CB C 40.325 0.400 1 655 120 120 ASP N N 115.406 0.400 1 656 121 121 LEU H H 7.121 0.020 1 657 121 121 LEU HD1 H 0.665 0.020 2 658 121 121 LEU HD2 H 0.779 0.020 2 659 121 121 LEU C C 176.749 0.400 1 660 121 121 LEU CA C 55.765 0.400 1 661 121 121 LEU CB C 44.134 0.400 1 662 121 121 LEU CD1 C 24.729 0.400 1 663 121 121 LEU CD2 C 22.791 0.400 1 664 121 121 LEU N N 117.839 0.400 1 665 122 122 LEU H H 8.337 0.020 1 666 122 122 LEU HD1 H 0.930 0.020 2 667 122 122 LEU HD2 H 0.937 0.020 2 668 122 122 LEU CA C 51.732 0.400 1 669 122 122 LEU CB C 44.118 0.400 1 670 122 122 LEU CD1 C 25.548 0.400 1 671 122 122 LEU CD2 C 26.848 0.400 1 672 122 122 LEU N N 119.986 0.400 1 673 126 126 PRO C C 176.075 0.400 1 674 126 126 PRO CA C 62.495 0.400 1 675 126 126 PRO CB C 31.066 0.400 1 676 127 127 LYS H H 8.137 0.020 1 677 127 127 LYS C C 177.427 0.400 1 678 127 127 LYS CA C 56.778 0.400 1 679 127 127 LYS CB C 33.055 0.400 1 680 127 127 LYS N N 118.456 0.400 1 681 128 128 THR H H 7.870 0.020 1 682 128 128 THR C C 174.604 0.400 1 683 128 128 THR CA C 60.211 0.400 1 684 128 128 THR CB C 71.920 0.400 1 685 128 128 THR N N 108.742 0.400 1 686 129 129 TRP H H 10.181 0.020 1 687 129 129 TRP HE1 H 9.198 0.020 1 688 129 129 TRP C C 179.925 0.400 1 689 129 129 TRP CA C 60.871 0.400 1 690 129 129 TRP CB C 28.480 0.400 1 691 129 129 TRP N N 123.949 0.400 1 692 129 129 TRP NE1 N 126.198 0.400 1 693 130 130 GLU H H 10.581 0.020 1 694 130 130 GLU C C 178.604 0.400 1 695 130 130 GLU CA C 61.701 0.400 1 696 130 130 GLU CB C 28.126 0.400 1 697 130 130 GLU N N 118.044 0.400 1 698 131 131 GLU H H 7.606 0.020 1 699 131 131 GLU C C 176.985 0.400 1 700 131 131 GLU CA C 57.205 0.400 1 701 131 131 GLU CB C 31.200 0.400 1 702 131 131 GLU N N 116.717 0.400 1 703 132 132 ILE H H 8.202 0.020 1 704 132 132 ILE HD1 H 0.560 0.020 1 705 132 132 ILE CA C 66.928 0.400 1 706 132 132 ILE CB C 33.966 0.400 1 707 132 132 ILE CD1 C 12.360 0.400 1 708 132 132 ILE N N 121.570 0.400 1 709 133 133 PRO C C 177.795 0.400 1 710 133 133 PRO CA C 67.059 0.400 1 711 133 133 PRO CB C 30.467 0.400 1 712 134 134 ALA H H 7.847 0.020 1 713 134 134 ALA C C 181.280 0.400 1 714 134 134 ALA CA C 55.458 0.400 1 715 134 134 ALA CB C 17.944 0.400 1 716 134 134 ALA N N 118.138 0.400 1 717 135 135 LEU H H 7.598 0.020 1 718 135 135 LEU HD1 H 0.888 0.020 2 719 135 135 LEU HD2 H 0.882 0.020 2 720 135 135 LEU C C 179.093 0.400 1 721 135 135 LEU CA C 57.396 0.400 1 722 135 135 LEU CB C 42.001 0.400 1 723 135 135 LEU CD1 C 24.040 0.400 1 724 135 135 LEU CD2 C 24.317 0.400 1 725 135 135 LEU N N 120.079 0.400 1 726 136 136 ASP H H 8.838 0.020 1 727 136 136 ASP C C 177.411 0.400 1 728 136 136 ASP CA C 58.901 0.400 1 729 136 136 ASP CB C 41.752 0.400 1 730 136 136 ASP N N 118.575 0.400 1 731 137 137 LYS H H 8.043 0.020 1 732 137 137 LYS C C 179.894 0.400 1 733 137 137 LYS CA C 60.252 0.400 1 734 137 137 LYS CB C 31.951 0.400 1 735 137 137 LYS N N 117.346 0.400 1 736 138 138 GLU H H 7.482 0.020 1 737 138 138 GLU C C 179.799 0.400 1 738 138 138 GLU CA C 59.454 0.400 1 739 138 138 GLU CB C 29.298 0.400 1 740 138 138 GLU N N 118.649 0.400 1 741 139 139 LEU H H 8.415 0.020 1 742 139 139 LEU HD1 H 0.787 0.020 2 743 139 139 LEU HD2 H 0.852 0.020 2 744 139 139 LEU C C 180.721 0.400 1 745 139 139 LEU CA C 58.317 0.400 1 746 139 139 LEU CB C 40.311 0.400 1 747 139 139 LEU CD1 C 25.914 0.400 1 748 139 139 LEU CD2 C 22.927 0.400 1 749 139 139 LEU N N 121.275 0.400 1 750 140 140 LYS H H 9.261 0.020 1 751 140 140 LYS C C 181.621 0.400 1 752 140 140 LYS CA C 58.851 0.400 1 753 140 140 LYS CB C 31.840 0.400 1 754 140 140 LYS N N 124.200 0.400 1 755 141 141 ALA H H 7.262 0.020 1 756 141 141 ALA C C 178.627 0.400 1 757 141 141 ALA CA C 54.521 0.400 1 758 141 141 ALA CB C 17.803 0.400 1 759 141 141 ALA N N 122.088 0.400 1 760 142 142 LYS H H 7.643 0.020 1 761 142 142 LYS C C 176.787 0.400 1 762 142 142 LYS CA C 55.093 0.400 1 763 142 142 LYS CB C 32.237 0.400 1 764 142 142 LYS N N 115.807 0.400 1 765 143 143 GLY H H 7.876 0.020 1 766 143 143 GLY C C 174.318 0.400 1 767 143 143 GLY CA C 46.128 0.400 1 768 143 143 GLY N N 107.843 0.400 1 769 144 144 LYS H H 7.859 0.020 1 770 144 144 LYS C C 173.812 0.400 1 771 144 144 LYS CA C 53.440 0.400 1 772 144 144 LYS CB C 35.010 0.400 1 773 144 144 LYS N N 119.918 0.400 1 774 145 145 SER H H 7.568 0.020 1 775 145 145 SER C C 174.656 0.400 1 776 145 145 SER CA C 56.884 0.400 1 777 145 145 SER CB C 66.549 0.400 1 778 145 145 SER N N 109.466 0.400 1 779 146 146 ALA H H 9.566 0.020 1 780 146 146 ALA C C 175.894 0.400 1 781 146 146 ALA CA C 55.960 0.400 1 782 146 146 ALA CB C 17.973 0.400 1 783 146 146 ALA N N 122.802 0.400 1 784 147 147 LEU H H 8.697 0.020 1 785 147 147 LEU HD1 H 0.683 0.020 2 786 147 147 LEU HD2 H 0.936 0.020 2 787 147 147 LEU C C 175.050 0.400 1 788 147 147 LEU CA C 54.604 0.400 1 789 147 147 LEU CB C 45.575 0.400 1 790 147 147 LEU CD1 C 22.500 0.400 1 791 147 147 LEU CD2 C 27.555 0.400 1 792 147 147 LEU N N 116.872 0.400 1 793 148 148 MET H H 8.178 0.020 1 794 148 148 MET C C 174.325 0.400 1 795 148 148 MET CA C 55.800 0.400 1 796 148 148 MET CB C 37.724 0.400 1 797 148 148 MET N N 121.716 0.400 1 798 149 149 PHE H H 8.611 0.020 1 799 149 149 PHE C C 171.590 0.400 1 800 149 149 PHE CA C 55.826 0.400 1 801 149 149 PHE CB C 41.587 0.400 1 802 149 149 PHE N N 120.235 0.400 1 803 150 150 ASN H H 8.671 0.020 1 804 150 150 ASN C C 172.549 0.400 1 805 150 150 ASN CA C 53.341 0.400 1 806 150 150 ASN CB C 37.305 0.400 1 807 150 150 ASN N N 116.069 0.400 1 808 151 151 LEU H H 7.287 0.020 1 809 151 151 LEU HD1 H 0.744 0.020 2 810 151 151 LEU HD2 H 0.135 0.020 2 811 151 151 LEU C C 177.963 0.400 1 812 151 151 LEU CA C 54.594 0.400 1 813 151 151 LEU CB C 41.878 0.400 1 814 151 151 LEU CD1 C 26.232 0.400 1 815 151 151 LEU CD2 C 23.579 0.400 1 816 151 151 LEU N N 122.969 0.400 1 817 152 152 GLN H H 7.940 0.020 1 818 152 152 GLN C C 176.073 0.400 1 819 152 152 GLN CA C 55.678 0.400 1 820 152 152 GLN CB C 28.252 0.400 1 821 152 152 GLN N N 113.114 0.400 1 822 153 153 GLU H H 6.404 0.020 1 823 153 153 GLU CA C 51.537 0.400 1 824 153 153 GLU CB C 32.958 0.400 1 825 153 153 GLU N N 113.572 0.400 1 826 154 154 PRO C C 176.855 0.400 1 827 154 154 PRO CA C 63.731 0.400 1 828 154 154 PRO CB C 31.966 0.400 1 829 155 155 TYR H H 7.823 0.020 1 830 155 155 TYR C C 176.001 0.400 1 831 155 155 TYR CA C 62.679 0.400 1 832 155 155 TYR CB C 40.447 0.400 1 833 155 155 TYR N N 117.652 0.400 1 834 156 156 PHE H H 8.045 0.020 1 835 156 156 PHE C C 176.222 0.400 1 836 156 156 PHE CA C 60.847 0.400 1 837 156 156 PHE CB C 41.587 0.400 1 838 156 156 PHE N N 112.213 0.400 1 839 157 157 THR H H 7.590 0.020 1 840 157 157 THR C C 176.039 0.400 1 841 157 157 THR CA C 63.074 0.400 1 842 157 157 THR CB C 69.290 0.400 1 843 157 157 THR N N 106.110 0.400 1 844 158 158 TRP H H 8.368 0.020 1 845 158 158 TRP HE1 H 9.461 0.020 1 846 158 158 TRP CA C 60.968 0.400 1 847 158 158 TRP CB C 28.509 0.400 1 848 158 158 TRP N N 124.174 0.400 1 849 158 158 TRP NE1 N 130.629 0.400 1 850 159 159 PRO C C 178.142 0.400 1 851 159 159 PRO CA C 65.931 0.400 1 852 159 159 PRO CB C 30.052 0.400 1 853 160 160 LEU H H 6.439 0.020 1 854 160 160 LEU HD1 H -1.003 0.020 2 855 160 160 LEU HD2 H -0.302 0.020 2 856 160 160 LEU C C 176.867 0.400 1 857 160 160 LEU CA C 56.069 0.400 1 858 160 160 LEU CB C 42.223 0.400 1 859 160 160 LEU CD1 C 19.602 0.400 1 860 160 160 LEU CD2 C 25.084 0.400 1 861 160 160 LEU N N 111.643 0.400 1 862 161 161 ILE H H 6.956 0.020 1 863 161 161 ILE HD1 H 0.760 0.020 1 864 161 161 ILE C C 175.677 0.400 1 865 161 161 ILE CA C 65.625 0.400 1 866 161 161 ILE CB C 37.395 0.400 1 867 161 161 ILE CD1 C 13.081 0.400 1 868 161 161 ILE N N 119.710 0.400 1 869 162 162 ALA H H 8.001 0.020 1 870 162 162 ALA C C 179.724 0.400 1 871 162 162 ALA CA C 52.320 0.400 1 872 162 162 ALA CB C 18.354 0.400 1 873 162 162 ALA N N 115.255 0.400 1 874 163 163 ALA H H 6.669 0.020 1 875 163 163 ALA C C 178.286 0.400 1 876 163 163 ALA CA C 56.425 0.400 1 877 163 163 ALA CB C 19.604 0.400 1 878 163 163 ALA N N 120.835 0.400 1 879 164 164 ASP H H 9.570 0.020 1 880 164 164 ASP C C 176.695 0.400 1 881 164 164 ASP CA C 53.440 0.400 1 882 164 164 ASP CB C 42.538 0.400 1 883 164 164 ASP N N 114.996 0.400 1 884 165 165 GLY H H 7.468 0.020 1 885 165 165 GLY C C 175.607 0.400 1 886 165 165 GLY CA C 45.694 0.400 1 887 165 165 GLY N N 103.621 0.400 1 888 166 166 GLY H H 7.382 0.020 1 889 166 166 GLY C C 172.227 0.400 1 890 166 166 GLY CA C 45.592 0.400 1 891 166 166 GLY N N 108.121 0.400 1 892 167 167 TYR H H 8.328 0.020 1 893 167 167 TYR C C 173.273 0.400 1 894 167 167 TYR CA C 57.657 0.400 1 895 167 167 TYR CB C 39.169 0.400 1 896 167 167 TYR N N 115.906 0.400 1 897 168 168 ALA H H 10.208 0.020 1 898 168 168 ALA C C 173.012 0.400 1 899 168 168 ALA CA C 53.124 0.400 1 900 168 168 ALA CB C 16.475 0.400 1 901 168 168 ALA N N 124.003 0.400 1 902 169 169 PHE H H 6.324 0.020 1 903 169 169 PHE C C 176.744 0.400 1 904 169 169 PHE CA C 55.752 0.400 1 905 169 169 PHE CB C 42.514 0.400 1 906 169 169 PHE N N 108.343 0.400 1 907 170 170 LYS H H 8.863 0.020 1 908 170 170 LYS C C 174.716 0.400 1 909 170 170 LYS CA C 57.027 0.400 1 910 170 170 LYS CB C 32.355 0.400 1 911 170 170 LYS N N 125.705 0.400 1 912 171 171 TYR H H 8.599 0.020 1 913 171 171 TYR C C 175.029 0.400 1 914 171 171 TYR CA C 56.200 0.400 1 915 171 171 TYR CB C 39.896 0.400 1 916 171 171 TYR N N 129.711 0.400 1 917 172 172 GLU H H 8.241 0.020 1 918 172 172 GLU CA C 55.981 0.400 1 919 172 172 GLU CB C 32.477 0.400 1 920 172 172 GLU N N 126.805 0.400 1 921 173 173 ASN C C 175.432 0.400 1 922 173 173 ASN CA C 54.334 0.400 1 923 173 173 ASN CB C 37.411 0.400 1 924 174 174 GLY H H 7.520 0.020 1 925 174 174 GLY C C 173.294 0.400 1 926 174 174 GLY CA C 45.705 0.400 1 927 174 174 GLY N N 102.080 0.400 1 928 175 175 LYS H H 7.107 0.020 1 929 175 175 LYS C C 174.739 0.400 1 930 175 175 LYS CA C 54.619 0.400 1 931 175 175 LYS CB C 35.233 0.400 1 932 175 175 LYS N N 118.703 0.400 1 933 176 176 TYR H H 8.731 0.020 1 934 176 176 TYR C C 176.262 0.400 1 935 176 176 TYR CA C 58.920 0.400 1 936 176 176 TYR CB C 39.696 0.400 1 937 176 176 TYR N N 120.130 0.400 1 938 177 177 ASP H H 9.043 0.020 1 939 177 177 ASP C C 177.455 0.400 1 940 177 177 ASP CA C 52.944 0.400 1 941 177 177 ASP CB C 41.216 0.400 1 942 177 177 ASP N N 124.057 0.400 1 943 178 178 ILE H H 7.730 0.020 1 944 178 178 ILE HD1 H 0.853 0.020 1 945 178 178 ILE C C 175.849 0.400 1 946 178 178 ILE CA C 63.627 0.400 1 947 178 178 ILE CB C 36.684 0.400 1 948 178 178 ILE CD1 C 13.905 0.400 1 949 178 178 ILE N N 117.048 0.400 1 950 179 179 LYS H H 8.300 0.020 1 951 179 179 LYS C C 176.528 0.400 1 952 179 179 LYS CA C 54.706 0.400 1 953 179 179 LYS CB C 31.878 0.400 1 954 179 179 LYS N N 116.085 0.400 1 955 180 180 ASP H H 7.755 0.020 1 956 180 180 ASP C C 172.993 0.400 1 957 180 180 ASP CA C 53.425 0.400 1 958 180 180 ASP CB C 40.826 0.400 1 959 180 180 ASP N N 123.266 0.400 1 960 181 181 VAL H H 7.492 0.020 1 961 181 181 VAL HG1 H 0.823 0.020 2 962 181 181 VAL HG2 H 0.711 0.020 2 963 181 181 VAL C C 176.899 0.400 1 964 181 181 VAL CA C 59.481 0.400 1 965 181 181 VAL CB C 35.024 0.400 1 966 181 181 VAL CG1 C 21.539 0.400 1 967 181 181 VAL CG2 C 22.538 0.400 1 968 181 181 VAL N N 122.888 0.400 1 969 182 182 GLY H H 7.065 0.020 1 970 182 182 GLY C C 174.259 0.400 1 971 182 182 GLY CA C 46.411 0.400 1 972 182 182 GLY N N 120.861 0.400 1 973 183 183 VAL H H 6.758 0.020 1 974 183 183 VAL HG1 H 0.882 0.020 2 975 183 183 VAL HG2 H 0.841 0.020 2 976 183 183 VAL C C 173.292 0.400 1 977 183 183 VAL CA C 63.489 0.400 1 978 183 183 VAL CB C 32.783 0.400 1 979 183 183 VAL CG1 C 22.416 0.400 1 980 183 183 VAL CG2 C 22.420 0.400 1 981 183 183 VAL N N 114.254 0.400 1 982 184 184 ASP H H 7.835 0.020 1 983 184 184 ASP C C 176.249 0.400 1 984 184 184 ASP CA C 51.670 0.400 1 985 184 184 ASP CB C 39.755 0.400 1 986 184 184 ASP N N 114.847 0.400 1 987 185 185 ASN H H 6.891 0.020 1 988 185 185 ASN CA C 51.688 0.400 1 989 185 185 ASN CB C 39.263 0.400 1 990 185 185 ASN N N 116.303 0.400 1 991 186 186 ALA C C 180.525 0.400 1 992 186 186 ALA CA C 55.672 0.400 1 993 186 186 ALA CB C 18.220 0.400 1 994 187 187 GLY H H 8.385 0.020 1 995 187 187 GLY C C 176.046 0.400 1 996 187 187 GLY CA C 47.366 0.400 1 997 187 187 GLY N N 109.507 0.400 1 998 188 188 ALA H H 8.074 0.020 1 999 188 188 ALA C C 180.829 0.400 1 1000 188 188 ALA CA C 54.062 0.400 1 1001 188 188 ALA CB C 18.399 0.400 1 1002 188 188 ALA N N 127.735 0.400 1 1003 189 189 LYS H H 7.977 0.020 1 1004 189 189 LYS C C 180.343 0.400 1 1005 189 189 LYS CA C 59.830 0.400 1 1006 189 189 LYS CB C 31.728 0.400 1 1007 189 189 LYS N N 115.246 0.400 1 1008 190 190 ALA H H 8.224 0.020 1 1009 190 190 ALA C C 181.347 0.400 1 1010 190 190 ALA CA C 55.835 0.400 1 1011 190 190 ALA CB C 17.890 0.400 1 1012 190 190 ALA N N 124.675 0.400 1 1013 191 191 GLY H H 8.207 0.020 1 1014 191 191 GLY C C 174.985 0.400 1 1015 191 191 GLY CA C 47.937 0.400 1 1016 191 191 GLY N N 107.567 0.400 1 1017 192 192 LEU H H 8.647 0.020 1 1018 192 192 LEU HD1 H 1.085 0.020 2 1019 192 192 LEU HD2 H 0.845 0.020 2 1020 192 192 LEU C C 178.412 0.400 1 1021 192 192 LEU CA C 57.325 0.400 1 1022 192 192 LEU CB C 40.218 0.400 1 1023 192 192 LEU CD1 C 24.249 0.400 1 1024 192 192 LEU CD2 C 25.330 0.400 1 1025 192 192 LEU N N 121.237 0.400 1 1026 193 193 THR H H 8.544 0.020 1 1027 193 193 THR C C 175.230 0.400 1 1028 193 193 THR CA C 67.423 0.400 1 1029 193 193 THR CB C 69.081 0.400 1 1030 193 193 THR N N 116.495 0.400 1 1031 194 194 PHE H H 7.651 0.020 1 1032 194 194 PHE C C 177.467 0.400 1 1033 194 194 PHE CA C 62.485 0.400 1 1034 194 194 PHE CB C 39.196 0.400 1 1035 194 194 PHE N N 122.073 0.400 1 1036 195 195 LEU H H 7.712 0.020 1 1037 195 195 LEU HD1 H 0.893 0.020 2 1038 195 195 LEU HD2 H 0.845 0.020 2 1039 195 195 LEU C C 178.132 0.400 1 1040 195 195 LEU CA C 58.694 0.400 1 1041 195 195 LEU CB C 41.352 0.400 1 1042 195 195 LEU CD1 C 23.706 0.400 1 1043 195 195 LEU CD2 C 25.191 0.400 1 1044 195 195 LEU N N 119.614 0.400 1 1045 196 196 VAL H H 8.589 0.020 1 1046 196 196 VAL HG1 H 0.969 0.020 2 1047 196 196 VAL HG2 H 0.856 0.020 2 1048 196 196 VAL C C 178.464 0.400 1 1049 196 196 VAL CA C 67.271 0.400 1 1050 196 196 VAL CB C 31.053 0.400 1 1051 196 196 VAL CG1 C 21.649 0.400 1 1052 196 196 VAL CG2 C 23.319 0.400 1 1053 196 196 VAL N N 117.533 0.400 1 1054 197 197 ASP H H 8.581 0.020 1 1055 197 197 ASP C C 179.361 0.400 1 1056 197 197 ASP CA C 58.171 0.400 1 1057 197 197 ASP CB C 39.828 0.400 1 1058 197 197 ASP N N 122.944 0.400 1 1059 198 198 LEU H H 7.875 0.020 1 1060 198 198 LEU HD1 H 1.018 0.020 2 1061 198 198 LEU HD2 H 0.813 0.020 2 1062 198 198 LEU C C 179.126 0.400 1 1063 198 198 LEU CA C 58.599 0.400 1 1064 198 198 LEU CB C 42.167 0.400 1 1065 198 198 LEU CD1 C 25.598 0.400 1 1066 198 198 LEU CD2 C 23.461 0.400 1 1067 198 198 LEU N N 120.212 0.400 1 1068 199 199 ILE H H 7.434 0.020 1 1069 199 199 ILE HD1 H 0.743 0.020 1 1070 199 199 ILE C C 181.156 0.400 1 1071 199 199 ILE CA C 63.317 0.400 1 1072 199 199 ILE CB C 38.209 0.400 1 1073 199 199 ILE CD1 C 14.222 0.400 1 1074 199 199 ILE N N 119.976 0.400 1 1075 200 200 LYS H H 9.392 0.020 1 1076 200 200 LYS C C 178.834 0.400 1 1077 200 200 LYS CA C 59.943 0.400 1 1078 200 200 LYS CB C 32.127 0.400 1 1079 200 200 LYS N N 124.564 0.400 1 1080 201 201 ASN H H 8.003 0.020 1 1081 201 201 ASN C C 173.244 0.400 1 1082 201 201 ASN CA C 53.732 0.400 1 1083 201 201 ASN CB C 38.686 0.400 1 1084 201 201 ASN N N 113.965 0.400 1 1085 202 202 LYS H H 7.933 0.020 1 1086 202 202 LYS C C 175.847 0.400 1 1087 202 202 LYS CA C 57.479 0.400 1 1088 202 202 LYS CB C 27.266 0.400 1 1089 202 202 LYS N N 111.501 0.400 1 1090 203 203 HIS H H 8.353 0.020 1 1091 203 203 HIS C C 175.643 0.400 1 1092 203 203 HIS CA C 57.268 0.400 1 1093 203 203 HIS CB C 28.529 0.400 1 1094 203 203 HIS N N 116.245 0.400 1 1095 204 204 MET H H 7.476 0.020 1 1096 204 204 MET C C 173.186 0.400 1 1097 204 204 MET CA C 54.646 0.400 1 1098 204 204 MET CB C 37.454 0.400 1 1099 204 204 MET N N 114.045 0.400 1 1100 205 205 ASN H H 8.710 0.020 1 1101 205 205 ASN C C 176.088 0.400 1 1102 205 205 ASN CA C 52.185 0.400 1 1103 205 205 ASN CB C 40.287 0.400 1 1104 205 205 ASN N N 118.497 0.400 1 1105 206 206 ALA H H 9.082 0.020 1 1106 206 206 ALA C C 176.403 0.400 1 1107 206 206 ALA CA C 54.814 0.400 1 1108 206 206 ALA CB C 18.252 0.400 1 1109 206 206 ALA N N 125.067 0.400 1 1110 207 207 ASP H H 8.171 0.020 1 1111 207 207 ASP C C 176.539 0.400 1 1112 207 207 ASP CA C 53.950 0.400 1 1113 207 207 ASP CB C 39.943 0.400 1 1114 207 207 ASP N N 112.749 0.400 1 1115 208 208 THR H H 7.342 0.020 1 1116 208 208 THR C C 173.305 0.400 1 1117 208 208 THR CA C 66.760 0.400 1 1118 208 208 THR CB C 69.073 0.400 1 1119 208 208 THR N N 116.633 0.400 1 1120 209 209 ASP H H 6.979 0.020 1 1121 209 209 ASP C C 175.818 0.400 1 1122 209 209 ASP CA C 51.852 0.400 1 1123 209 209 ASP CB C 42.062 0.400 1 1124 209 209 ASP N N 130.962 0.400 1 1125 210 210 TYR H H 7.858 0.020 1 1126 210 210 TYR C C 178.370 0.400 1 1127 210 210 TYR CA C 63.648 0.400 1 1128 210 210 TYR CB C 39.077 0.400 1 1129 210 210 TYR N N 117.493 0.400 1 1130 211 211 SER H H 8.201 0.020 1 1131 211 211 SER C C 177.629 0.400 1 1132 211 211 SER CA C 61.419 0.400 1 1133 211 211 SER CB C 63.042 0.400 1 1134 211 211 SER N N 114.684 0.400 1 1135 212 212 ILE H H 8.959 0.020 1 1136 212 212 ILE HD1 H 0.867 0.020 1 1137 212 212 ILE C C 179.021 0.400 1 1138 212 212 ILE CA C 65.023 0.400 1 1139 212 212 ILE CB C 38.613 0.400 1 1140 212 212 ILE CD1 C 13.110 0.400 1 1141 212 212 ILE N N 124.464 0.400 1 1142 213 213 ALA H H 7.620 0.020 1 1143 213 213 ALA C C 177.865 0.400 1 1144 213 213 ALA CA C 55.567 0.400 1 1145 213 213 ALA CB C 17.072 0.400 1 1146 213 213 ALA N N 120.745 0.400 1 1147 214 214 GLU H H 7.872 0.020 1 1148 214 214 GLU C C 178.115 0.400 1 1149 214 214 GLU CA C 58.941 0.400 1 1150 214 214 GLU CB C 29.652 0.400 1 1151 214 214 GLU N N 117.544 0.400 1 1152 215 215 ALA H H 7.951 0.020 1 1153 215 215 ALA C C 179.783 0.400 1 1154 215 215 ALA CA C 54.696 0.400 1 1155 215 215 ALA CB C 18.034 0.400 1 1156 215 215 ALA N N 119.687 0.400 1 1157 216 216 ALA H H 7.796 0.020 1 1158 216 216 ALA C C 180.736 0.400 1 1159 216 216 ALA CA C 55.247 0.400 1 1160 216 216 ALA CB C 19.732 0.400 1 1161 216 216 ALA N N 117.585 0.400 1 1162 217 217 PHE H H 8.339 0.020 1 1163 217 217 PHE CA C 62.919 0.400 1 1164 217 217 PHE CB C 38.072 0.400 1 1165 217 217 PHE N N 119.437 0.400 1 1166 218 218 ASN C C 176.867 0.400 1 1167 218 218 ASN CA C 55.368 0.400 1 1168 218 218 ASN CB C 36.484 0.400 1 1169 219 219 LYS H H 7.713 0.020 1 1170 219 219 LYS C C 177.780 0.400 1 1171 219 219 LYS CA C 56.131 0.400 1 1172 219 219 LYS CB C 32.853 0.400 1 1173 219 219 LYS N N 116.748 0.400 1 1174 220 220 GLY H H 7.718 0.020 1 1175 220 220 GLY C C 175.309 0.400 1 1176 220 220 GLY CA C 46.152 0.400 1 1177 220 220 GLY N N 108.762 0.400 1 1178 221 221 GLU H H 8.382 0.020 1 1179 221 221 GLU C C 175.803 0.400 1 1180 221 221 GLU CA C 57.326 0.400 1 1181 221 221 GLU CB C 30.469 0.400 1 1182 221 221 GLU N N 116.381 0.400 1 1183 222 222 THR H H 6.856 0.020 1 1184 222 222 THR C C 172.722 0.400 1 1185 222 222 THR CA C 58.169 0.400 1 1186 222 222 THR CB C 70.566 0.400 1 1187 222 222 THR N N 110.520 0.400 1 1188 223 223 ALA H H 8.684 0.020 1 1189 223 223 ALA C C 176.461 0.400 1 1190 223 223 ALA CA C 54.727 0.400 1 1191 223 223 ALA CB C 20.427 0.400 1 1192 223 223 ALA N N 127.377 0.400 1 1193 224 224 MET H H 8.075 0.020 1 1194 224 224 MET C C 173.936 0.400 1 1195 224 224 MET CA C 54.542 0.400 1 1196 224 224 MET CB C 40.062 0.400 1 1197 224 224 MET N N 114.198 0.400 1 1198 225 225 THR H H 9.152 0.020 1 1199 225 225 THR C C 171.424 0.400 1 1200 225 225 THR CA C 59.728 0.400 1 1201 225 225 THR CB C 71.023 0.400 1 1202 225 225 THR N N 113.328 0.400 1 1203 226 226 ILE H H 7.139 0.020 1 1204 226 226 ILE HD1 H 0.060 0.020 1 1205 226 226 ILE C C 174.820 0.400 1 1206 226 226 ILE CA C 60.308 0.400 1 1207 226 226 ILE CB C 40.344 0.400 1 1208 226 226 ILE CD1 C 11.775 0.400 1 1209 226 226 ILE N N 122.719 0.400 1 1210 227 227 ASN H H 8.472 0.020 1 1211 227 227 ASN C C 175.514 0.400 1 1212 227 227 ASN CA C 52.466 0.400 1 1213 227 227 ASN CB C 42.842 0.400 1 1214 227 227 ASN N N 121.902 0.400 1 1215 228 228 GLY H H 8.192 0.020 1 1216 228 228 GLY CA C 42.270 0.400 1 1217 228 228 GLY N N 110.667 0.400 1 1218 229 229 PRO CA C 62.755 0.400 1 1219 229 229 PRO CB C 29.552 0.400 1 1220 231 231 ALA H H 6.971 0.020 1 1221 231 231 ALA CA C 52.168 0.400 1 1222 231 231 ALA CB C 19.110 0.400 1 1223 231 231 ALA N N 125.512 0.400 1 1224 232 232 TRP H H 7.197 0.020 1 1225 232 232 TRP HE1 H 10.508 0.020 1 1226 232 232 TRP CA C 58.678 0.400 1 1227 232 232 TRP CB C 28.673 0.400 1 1228 232 232 TRP N N 118.541 0.400 1 1229 232 232 TRP NE1 N 128.275 0.400 1 1230 235 235 ILE HD1 H 0.310 0.020 1 1231 235 235 ILE CD1 C 13.800 0.400 1 1232 240 240 VAL HG1 H 0.585 0.020 2 1233 240 240 VAL HG2 H 0.788 0.020 2 1234 240 240 VAL CG1 C 20.890 0.400 1 1235 240 240 VAL CG2 C 21.830 0.400 1 1236 241 241 ASN CB C 37.371 0.400 1 1237 242 242 TYR H H 7.872 0.020 1 1238 242 242 TYR C C 174.489 0.400 1 1239 242 242 TYR CA C 54.853 0.400 1 1240 242 242 TYR CB C 41.485 0.400 1 1241 242 242 TYR N N 121.813 0.400 1 1242 243 243 GLY H H 8.493 0.020 1 1243 243 243 GLY C C 171.154 0.400 1 1244 243 243 GLY CA C 42.935 0.400 1 1245 243 243 GLY N N 107.512 0.400 1 1246 244 244 VAL H H 8.228 0.020 1 1247 244 244 VAL HG1 H 1.072 0.020 2 1248 244 244 VAL HG2 H 0.636 0.020 2 1249 244 244 VAL C C 174.872 0.400 1 1250 244 244 VAL CA C 61.547 0.400 1 1251 244 244 VAL CB C 34.455 0.400 1 1252 244 244 VAL CG1 C 22.083 0.400 1 1253 244 244 VAL CG2 C 21.606 0.400 1 1254 244 244 VAL N N 120.877 0.400 1 1255 245 245 THR H H 9.515 0.020 1 1256 245 245 THR C C 174.234 0.400 1 1257 245 245 THR CA C 59.071 0.400 1 1258 245 245 THR CB C 71.559 0.400 1 1259 245 245 THR N N 119.803 0.400 1 1260 246 246 VAL H H 8.158 0.020 1 1261 246 246 VAL HG1 H 0.969 0.020 2 1262 246 246 VAL HG2 H 0.983 0.020 2 1263 246 246 VAL C C 175.040 0.400 1 1264 246 246 VAL CA C 62.433 0.400 1 1265 246 246 VAL CB C 32.412 0.400 1 1266 246 246 VAL CG1 C 20.441 0.400 1 1267 246 246 VAL CG2 C 21.596 0.400 1 1268 246 246 VAL N N 123.611 0.400 1 1269 247 247 LEU H H 8.649 0.020 1 1270 247 247 LEU HD1 H 0.663 0.020 2 1271 247 247 LEU HD2 H 0.645 0.020 2 1272 247 247 LEU CA C 54.498 0.400 1 1273 247 247 LEU CB C 40.229 0.400 1 1274 247 247 LEU CD1 C 25.833 0.400 1 1275 247 247 LEU CD2 C 23.824 0.400 1 1276 247 247 LEU N N 125.537 0.400 1 1277 248 248 PRO C C 175.498 0.400 1 1278 248 248 PRO CA C 61.842 0.400 1 1279 248 248 PRO CB C 30.183 0.400 1 1280 249 249 THR H H 8.815 0.020 1 1281 249 249 THR C C 174.599 0.400 1 1282 249 249 THR CA C 61.157 0.400 1 1283 249 249 THR CB C 71.441 0.400 1 1284 249 249 THR N N 111.705 0.400 1 1285 250 250 PHE H H 9.579 0.020 1 1286 250 250 PHE C C 174.684 0.400 1 1287 250 250 PHE CA C 56.938 0.400 1 1288 250 250 PHE CB C 41.787 0.400 1 1289 250 250 PHE N N 121.915 0.400 1 1290 251 251 LYS H H 10.570 0.020 1 1291 251 251 LYS C C 177.723 0.400 1 1292 251 251 LYS CA C 57.416 0.400 1 1293 251 251 LYS CB C 28.138 0.400 1 1294 251 251 LYS N N 129.702 0.400 1 1295 252 252 GLY H H 9.030 0.020 1 1296 252 252 GLY C C 173.912 0.400 1 1297 252 252 GLY CA C 45.086 0.400 1 1298 252 252 GLY N N 103.626 0.400 1 1299 253 253 GLN H H 8.244 0.020 1 1300 253 253 GLN CA C 52.486 0.400 1 1301 253 253 GLN CB C 29.298 0.400 1 1302 253 253 GLN N N 122.357 0.400 1 1303 254 254 PRO C C 178.676 0.400 1 1304 254 254 PRO CA C 62.977 0.400 1 1305 254 254 PRO CB C 31.093 0.400 1 1306 255 255 SER H H 8.002 0.020 1 1307 255 255 SER C C 173.658 0.400 1 1308 255 255 SER CA C 62.323 0.400 1 1309 255 255 SER CB C 64.942 0.400 1 1310 255 255 SER N N 117.976 0.400 1 1311 256 256 LYS H H 7.639 0.020 1 1312 256 256 LYS CA C 53.191 0.400 1 1313 256 256 LYS CB C 33.307 0.400 1 1314 256 256 LYS N N 123.449 0.400 1 1315 257 257 PRO C C 177.147 0.400 1 1316 257 257 PRO CA C 62.452 0.400 1 1317 257 257 PRO CB C 31.379 0.400 1 1318 258 258 PHE H H 9.265 0.020 1 1319 258 258 PHE C C 177.449 0.400 1 1320 258 258 PHE CA C 58.534 0.400 1 1321 258 258 PHE CB C 40.121 0.400 1 1322 258 258 PHE N N 118.347 0.400 1 1323 259 259 VAL H H 8.776 0.020 1 1324 259 259 VAL HG1 H 0.925 0.020 2 1325 259 259 VAL HG2 H 0.980 0.020 2 1326 259 259 VAL C C 176.569 0.400 1 1327 259 259 VAL CA C 62.078 0.400 1 1328 259 259 VAL CB C 33.876 0.400 1 1329 259 259 VAL CG1 C 21.509 0.400 1 1330 259 259 VAL CG2 C 22.697 0.400 1 1331 259 259 VAL N N 121.972 0.400 1 1332 260 260 GLY H H 8.961 0.020 1 1333 260 260 GLY C C 171.463 0.400 1 1334 260 260 GLY CA C 44.790 0.400 1 1335 260 260 GLY N N 116.162 0.400 1 1336 261 261 VAL H H 11.174 0.020 1 1337 261 261 VAL HG1 H 0.679 0.020 2 1338 261 261 VAL HG2 H 0.565 0.020 2 1339 261 261 VAL C C 179.695 0.400 1 1340 261 261 VAL CA C 60.241 0.400 1 1341 261 261 VAL CB C 32.821 0.400 1 1342 261 261 VAL CG1 C 20.308 0.400 1 1343 261 261 VAL CG2 C 20.936 0.400 1 1344 261 261 VAL N N 128.975 0.400 1 1345 262 262 LEU H H 8.835 0.020 1 1346 262 262 LEU HD1 H 0.806 0.020 2 1347 262 262 LEU HD2 H 0.885 0.020 2 1348 262 262 LEU C C 175.254 0.400 1 1349 262 262 LEU CA C 56.739 0.400 1 1350 262 262 LEU CB C 41.091 0.400 1 1351 262 262 LEU CD1 C 22.681 0.400 1 1352 262 262 LEU CD2 C 25.314 0.400 1 1353 262 262 LEU N N 134.069 0.400 1 1354 263 263 SER H H 8.769 0.020 1 1355 263 263 SER C C 170.638 0.400 1 1356 263 263 SER CA C 58.853 0.400 1 1357 263 263 SER CB C 66.154 0.400 1 1358 263 263 SER N N 126.737 0.400 1 1359 264 264 ALA H H 9.143 0.020 1 1360 264 264 ALA C C 176.219 0.400 1 1361 264 264 ALA CA C 49.918 0.400 1 1362 264 264 ALA CB C 20.730 0.400 1 1363 264 264 ALA N N 123.799 0.400 1 1364 265 265 GLY H H 9.417 0.020 1 1365 265 265 GLY C C 171.119 0.400 1 1366 265 265 GLY CA C 42.908 0.400 1 1367 265 265 GLY N N 110.747 0.400 1 1368 266 266 ILE H H 10.297 0.020 1 1369 266 266 ILE HD1 H 0.915 0.020 1 1370 266 266 ILE C C 175.264 0.400 1 1371 266 266 ILE CA C 59.829 0.400 1 1372 266 266 ILE CB C 39.519 0.400 1 1373 266 266 ILE CD1 C 13.882 0.400 1 1374 266 266 ILE N N 123.632 0.400 1 1375 267 267 ASN H H 8.250 0.020 1 1376 267 267 ASN C C 177.436 0.400 1 1377 267 267 ASN CA C 53.657 0.400 1 1378 267 267 ASN CB C 38.767 0.400 1 1379 267 267 ASN N N 125.881 0.400 1 1380 268 268 ALA H H 8.845 0.020 1 1381 268 268 ALA C C 178.479 0.400 1 1382 268 268 ALA CA C 55.511 0.400 1 1383 268 268 ALA CB C 17.854 0.400 1 1384 268 268 ALA N N 131.136 0.400 1 1385 269 269 ALA H H 8.158 0.020 1 1386 269 269 ALA C C 178.117 0.400 1 1387 269 269 ALA CA C 51.541 0.400 1 1388 269 269 ALA CB C 18.592 0.400 1 1389 269 269 ALA N N 117.810 0.400 1 1390 270 270 SER H H 7.619 0.020 1 1391 270 270 SER CA C 56.356 0.400 1 1392 270 270 SER CB C 64.366 0.400 1 1393 270 270 SER N N 112.930 0.400 1 1394 271 271 PRO C C 175.683 0.400 1 1395 271 271 PRO CA C 63.726 0.400 1 1396 271 271 PRO CB C 30.878 0.400 1 1397 272 272 ASN H H 8.881 0.020 1 1398 272 272 ASN C C 176.555 0.400 1 1399 272 272 ASN CA C 52.889 0.400 1 1400 272 272 ASN CB C 40.445 0.400 1 1401 272 272 ASN N N 119.718 0.400 1 1402 273 273 LYS H H 7.806 0.020 1 1403 273 273 LYS C C 179.093 0.400 1 1404 273 273 LYS CA C 61.823 0.400 1 1405 273 273 LYS CB C 31.497 0.400 1 1406 273 273 LYS N N 119.362 0.400 1 1407 274 274 GLU H H 8.836 0.020 1 1408 274 274 GLU C C 179.758 0.400 1 1409 274 274 GLU CA C 59.973 0.400 1 1410 274 274 GLU CB C 27.918 0.400 1 1411 274 274 GLU N N 118.293 0.400 1 1412 275 275 LEU H H 7.385 0.020 1 1413 275 275 LEU HD1 H 0.933 0.020 2 1414 275 275 LEU HD2 H 0.947 0.020 2 1415 275 275 LEU C C 178.403 0.400 1 1416 275 275 LEU CA C 57.369 0.400 1 1417 275 275 LEU CB C 42.076 0.400 1 1418 275 275 LEU CD1 C 25.202 0.400 1 1419 275 275 LEU CD2 C 22.493 0.400 1 1420 275 275 LEU N N 120.650 0.400 1 1421 276 276 ALA H H 8.405 0.020 1 1422 276 276 ALA C C 178.528 0.400 1 1423 276 276 ALA CA C 55.495 0.400 1 1424 276 276 ALA CB C 17.894 0.400 1 1425 276 276 ALA N N 120.289 0.400 1 1426 277 277 LYS H H 7.851 0.020 1 1427 277 277 LYS C C 177.189 0.400 1 1428 277 277 LYS CA C 60.263 0.400 1 1429 277 277 LYS CB C 32.345 0.400 1 1430 277 277 LYS N N 118.272 0.400 1 1431 278 278 GLU H H 7.592 0.020 1 1432 278 278 GLU C C 179.240 0.400 1 1433 278 278 GLU CA C 59.619 0.400 1 1434 278 278 GLU CB C 29.066 0.400 1 1435 278 278 GLU N N 118.645 0.400 1 1436 279 279 PHE H H 8.368 0.020 1 1437 279 279 PHE C C 177.602 0.400 1 1438 279 279 PHE CA C 61.633 0.400 1 1439 279 279 PHE CB C 38.567 0.400 1 1440 279 279 PHE N N 118.379 0.400 1 1441 280 280 LEU H H 8.444 0.020 1 1442 280 280 LEU HD1 H 0.672 0.020 2 1443 280 280 LEU HD2 H 0.710 0.020 2 1444 280 280 LEU C C 177.138 0.400 1 1445 280 280 LEU CA C 58.444 0.400 1 1446 280 280 LEU CB C 40.671 0.400 1 1447 280 280 LEU CD1 C 25.779 0.400 1 1448 280 280 LEU CD2 C 23.405 0.400 1 1449 280 280 LEU N N 120.026 0.400 1 1450 281 281 GLU H H 8.415 0.020 1 1451 281 281 GLU C C 177.096 0.400 1 1452 281 281 GLU CA C 59.622 0.400 1 1453 281 281 GLU CB C 29.368 0.400 1 1454 281 281 GLU N N 112.879 0.400 1 1455 282 282 ASN H H 7.684 0.020 1 1456 282 282 ASN C C 175.250 0.400 1 1457 282 282 ASN CA C 53.164 0.400 1 1458 282 282 ASN CB C 38.992 0.400 1 1459 282 282 ASN N N 108.801 0.400 1 1460 283 283 TYR H H 7.164 0.020 1 1461 283 283 TYR C C 176.349 0.400 1 1462 283 283 TYR CA C 59.857 0.400 1 1463 283 283 TYR CB C 38.052 0.400 1 1464 283 283 TYR N N 116.367 0.400 1 1465 284 284 LEU H H 8.101 0.020 1 1466 284 284 LEU HD1 H 0.843 0.020 2 1467 284 284 LEU HD2 H 1.039 0.020 2 1468 284 284 LEU C C 176.848 0.400 1 1469 284 284 LEU CA C 58.416 0.400 1 1470 284 284 LEU CB C 41.002 0.400 1 1471 284 284 LEU CD1 C 23.945 0.400 1 1472 284 284 LEU CD2 C 27.398 0.400 1 1473 284 284 LEU N N 121.495 0.400 1 1474 285 285 LEU H H 7.831 0.020 1 1475 285 285 LEU HD1 H 1.052 0.020 2 1476 285 285 LEU HD2 H 1.119 0.020 2 1477 285 285 LEU C C 174.944 0.400 1 1478 285 285 LEU CA C 54.472 0.400 1 1479 285 285 LEU CB C 38.472 0.400 1 1480 285 285 LEU CD1 C 25.695 0.400 1 1481 285 285 LEU CD2 C 24.003 0.400 1 1482 285 285 LEU N N 119.213 0.400 1 1483 286 286 THR H H 8.542 0.020 1 1484 286 286 THR C C 174.320 0.400 1 1485 286 286 THR CA C 59.007 0.400 1 1486 286 286 THR CB C 73.569 0.400 1 1487 286 286 THR N N 108.729 0.400 1 1488 287 287 ASP H H 8.528 0.020 1 1489 287 287 ASP C C 177.870 0.400 1 1490 287 287 ASP CA C 58.734 0.400 1 1491 287 287 ASP CB C 39.534 0.400 1 1492 287 287 ASP N N 122.214 0.400 1 1493 288 288 GLU H H 8.443 0.020 1 1494 288 288 GLU C C 180.161 0.400 1 1495 288 288 GLU CA C 59.339 0.400 1 1496 288 288 GLU CB C 29.115 0.400 1 1497 288 288 GLU N N 115.695 0.400 1 1498 289 289 GLY H H 8.327 0.020 1 1499 289 289 GLY C C 175.256 0.400 1 1500 289 289 GLY CA C 46.992 0.400 1 1501 289 289 GLY N N 112.930 0.400 1 1502 290 290 LEU H H 8.208 0.020 1 1503 290 290 LEU HD1 H 1.074 0.020 2 1504 290 290 LEU HD2 H 0.792 0.020 2 1505 290 290 LEU C C 179.873 0.400 1 1506 290 290 LEU CA C 57.262 0.400 1 1507 290 290 LEU CB C 41.642 0.400 1 1508 290 290 LEU CD1 C 27.886 0.400 1 1509 290 290 LEU CD2 C 21.864 0.400 1 1510 290 290 LEU N N 119.524 0.400 1 1511 291 291 GLU H H 7.744 0.020 1 1512 291 291 GLU C C 178.136 0.400 1 1513 291 291 GLU CA C 59.656 0.400 1 1514 291 291 GLU CB C 29.033 0.400 1 1515 291 291 GLU N N 120.812 0.400 1 1516 292 292 ALA H H 7.193 0.020 1 1517 292 292 ALA C C 180.822 0.400 1 1518 292 292 ALA CA C 55.495 0.400 1 1519 292 292 ALA CB C 17.683 0.400 1 1520 292 292 ALA N N 119.831 0.400 1 1521 293 293 VAL H H 7.243 0.020 1 1522 293 293 VAL HG1 H 1.004 0.020 2 1523 293 293 VAL HG2 H 0.901 0.020 2 1524 293 293 VAL C C 177.079 0.400 1 1525 293 293 VAL CA C 67.318 0.400 1 1526 293 293 VAL CB C 32.055 0.400 1 1527 293 293 VAL CG1 C 21.422 0.400 1 1528 293 293 VAL CG2 C 22.246 0.400 1 1529 293 293 VAL N N 115.882 0.400 1 1530 294 294 ASN H H 8.758 0.020 1 1531 294 294 ASN C C 176.450 0.400 1 1532 294 294 ASN CA C 56.199 0.400 1 1533 294 294 ASN CB C 40.911 0.400 1 1534 294 294 ASN N N 117.481 0.400 1 1535 295 295 LYS H H 8.338 0.020 1 1536 295 295 LYS C C 177.444 0.400 1 1537 295 295 LYS CA C 58.561 0.400 1 1538 295 295 LYS CB C 31.978 0.400 1 1539 295 295 LYS N N 115.909 0.400 1 1540 296 296 ASP H H 7.251 0.020 1 1541 296 296 ASP C C 176.142 0.400 1 1542 296 296 ASP CA C 56.212 0.400 1 1543 296 296 ASP CB C 41.922 0.400 1 1544 296 296 ASP N N 118.993 0.400 1 1545 297 297 LYS H H 7.653 0.020 1 1546 297 297 LYS CA C 52.627 0.400 1 1547 297 297 LYS CB C 34.952 0.400 1 1548 297 297 LYS N N 115.617 0.400 1 1549 298 298 PRO C C 178.549 0.400 1 1550 298 298 PRO CA C 63.219 0.400 1 1551 298 298 PRO CB C 31.663 0.400 1 1552 299 299 LEU H H 8.530 0.020 1 1553 299 299 LEU HD1 H 0.893 0.020 2 1554 299 299 LEU HD2 H 0.813 0.020 2 1555 299 299 LEU C C 177.573 0.400 1 1556 299 299 LEU CA C 55.710 0.400 1 1557 299 299 LEU CB C 43.852 0.400 1 1558 299 299 LEU CD1 C 26.581 0.400 1 1559 299 299 LEU CD2 C 22.958 0.400 1 1560 299 299 LEU N N 121.742 0.400 1 1561 300 300 GLY H H 8.134 0.020 1 1562 300 300 GLY C C 174.043 0.400 1 1563 300 300 GLY CA C 44.458 0.400 1 1564 300 300 GLY N N 103.347 0.400 1 1565 301 301 ALA H H 7.522 0.020 1 1566 301 301 ALA C C 177.667 0.400 1 1567 301 301 ALA CA C 51.558 0.400 1 1568 301 301 ALA CB C 19.844 0.400 1 1569 301 301 ALA N N 123.838 0.400 1 1570 302 302 VAL H H 8.045 0.020 1 1571 302 302 VAL HG1 H 1.059 0.020 2 1572 302 302 VAL HG2 H 1.262 0.020 2 1573 302 302 VAL C C 174.034 0.400 1 1574 302 302 VAL CA C 59.900 0.400 1 1575 302 302 VAL CB C 35.614 0.400 1 1576 302 302 VAL CG1 C 22.153 0.400 1 1577 302 302 VAL CG2 C 19.070 0.400 1 1578 302 302 VAL N N 110.167 0.400 1 1579 303 303 ALA H H 7.689 0.020 1 1580 303 303 ALA C C 175.560 0.400 1 1581 303 303 ALA CA C 53.039 0.400 1 1582 303 303 ALA CB C 19.491 0.400 1 1583 303 303 ALA N N 117.959 0.400 1 1584 304 304 LEU H H 6.348 0.020 1 1585 304 304 LEU HD1 H 0.848 0.020 2 1586 304 304 LEU HD2 H 0.702 0.020 2 1587 304 304 LEU C C 175.458 0.400 1 1588 304 304 LEU CA C 54.335 0.400 1 1589 304 304 LEU CB C 44.147 0.400 1 1590 304 304 LEU CD1 C 24.263 0.400 1 1591 304 304 LEU CD2 C 26.586 0.400 1 1592 304 304 LEU N N 114.829 0.400 1 1593 305 305 LYS H H 8.043 0.020 1 1594 305 305 LYS C C 178.455 0.400 1 1595 305 305 LYS CA C 60.428 0.400 1 1596 305 305 LYS CB C 31.715 0.400 1 1597 305 305 LYS N N 129.635 0.400 1 1598 306 306 SER H H 8.684 0.020 1 1599 306 306 SER C C 176.963 0.400 1 1600 306 306 SER CA C 61.989 0.400 1 1601 306 306 SER CB C 60.391 0.400 1 1602 306 306 SER N N 111.863 0.400 1 1603 307 307 TYR H H 6.641 0.020 1 1604 307 307 TYR C C 177.811 0.400 1 1605 307 307 TYR CA C 58.904 0.400 1 1606 307 307 TYR CB C 38.656 0.400 1 1607 307 307 TYR N N 122.102 0.400 1 1608 308 308 GLU H H 8.473 0.020 1 1609 308 308 GLU C C 177.652 0.400 1 1610 308 308 GLU CA C 58.466 0.400 1 1611 308 308 GLU CB C 26.173 0.400 1 1612 308 308 GLU N N 122.650 0.400 1 1613 309 309 GLU H H 7.813 0.020 1 1614 309 309 GLU C C 178.002 0.400 1 1615 309 309 GLU CA C 58.922 0.400 1 1616 309 309 GLU CB C 28.862 0.400 1 1617 309 309 GLU N N 114.966 0.400 1 1618 310 310 GLU H H 7.088 0.020 1 1619 310 310 GLU C C 178.868 0.400 1 1620 310 310 GLU CA C 57.536 0.400 1 1621 310 310 GLU CB C 29.333 0.400 1 1622 310 310 GLU N N 116.959 0.400 1 1623 311 311 LEU H H 8.020 0.020 1 1624 311 311 LEU HD1 H 0.870 0.020 2 1625 311 311 LEU HD2 H 0.797 0.020 2 1626 311 311 LEU C C 179.536 0.400 1 1627 311 311 LEU CA C 57.324 0.400 1 1628 311 311 LEU CB C 41.926 0.400 1 1629 311 311 LEU CD1 C 26.326 0.400 1 1630 311 311 LEU CD2 C 22.652 0.400 1 1631 311 311 LEU N N 120.859 0.400 1 1632 312 312 ALA H H 8.191 0.020 1 1633 312 312 ALA C C 174.696 0.400 1 1634 312 312 ALA CA C 54.037 0.400 1 1635 312 312 ALA CB C 17.699 0.400 1 1636 312 312 ALA N N 114.676 0.400 1 1637 313 313 LYS H H 6.993 0.020 1 1638 313 313 LYS C C 177.970 0.400 1 1639 313 313 LYS CA C 58.418 0.400 1 1640 313 313 LYS CB C 31.727 0.400 1 1641 313 313 LYS N N 119.326 0.400 1 1642 314 314 ASP H H 8.311 0.020 1 1643 314 314 ASP CA C 50.784 0.400 1 1644 314 314 ASP CB C 41.334 0.400 1 1645 314 314 ASP N N 121.733 0.400 1 1646 315 315 PRO C C 179.227 0.400 1 1647 315 315 PRO CA C 64.525 0.400 1 1648 315 315 PRO CB C 32.168 0.400 1 1649 316 316 ARG H H 8.502 0.020 1 1650 316 316 ARG C C 179.821 0.400 1 1651 316 316 ARG CA C 58.813 0.400 1 1652 316 316 ARG CB C 29.263 0.400 1 1653 316 316 ARG N N 116.914 0.400 1 1654 317 317 ILE H H 7.702 0.020 1 1655 317 317 ILE HD1 H 1.118 0.020 1 1656 317 317 ILE C C 178.067 0.400 1 1657 317 317 ILE CA C 64.418 0.400 1 1658 317 317 ILE CB C 35.853 0.400 1 1659 317 317 ILE CD1 C 12.483 0.400 1 1660 317 317 ILE N N 123.536 0.400 1 1661 318 318 ALA H H 7.906 0.020 1 1662 318 318 ALA C C 181.157 0.400 1 1663 318 318 ALA CA C 56.138 0.400 1 1664 318 318 ALA CB C 17.268 0.400 1 1665 318 318 ALA N N 123.331 0.400 1 1666 319 319 ALA H H 8.086 0.020 1 1667 319 319 ALA C C 178.916 0.400 1 1668 319 319 ALA CA C 55.519 0.400 1 1669 319 319 ALA CB C 17.969 0.400 1 1670 319 319 ALA N N 118.981 0.400 1 1671 320 320 THR H H 7.357 0.020 1 1672 320 320 THR C C 175.479 0.400 1 1673 320 320 THR CA C 67.517 0.400 1 1674 320 320 THR CB C 69.151 0.400 1 1675 320 320 THR N N 114.576 0.400 1 1676 321 321 MET H H 8.186 0.020 1 1677 321 321 MET C C 177.825 0.400 1 1678 321 321 MET CA C 56.766 0.400 1 1679 321 321 MET CB C 30.864 0.400 1 1680 321 321 MET N N 118.790 0.400 1 1681 322 322 GLU H H 8.267 0.020 1 1682 322 322 GLU C C 179.547 0.400 1 1683 322 322 GLU CA C 59.926 0.400 1 1684 322 322 GLU CB C 28.863 0.400 1 1685 322 322 GLU N N 122.177 0.400 1 1686 323 323 ASN H H 8.207 0.020 1 1687 323 323 ASN CA C 57.124 0.400 1 1688 323 323 ASN CB C 39.313 0.400 1 1689 323 323 ASN N N 115.260 0.400 1 1690 324 324 ALA H H 8.199 0.020 1 1691 324 324 ALA C C 180.381 0.400 1 1692 324 324 ALA CA C 54.780 0.400 1 1693 324 324 ALA CB C 17.528 0.400 1 1694 324 324 ALA N N 119.875 0.400 1 1695 325 325 GLN H H 8.250 0.020 1 1696 325 325 GLN C C 177.826 0.400 1 1697 325 325 GLN CA C 58.414 0.400 1 1698 325 325 GLN CB C 27.963 0.400 1 1699 325 325 GLN N N 116.348 0.400 1 1700 326 326 LYS H H 7.079 0.020 1 1701 326 326 LYS C C 176.163 0.400 1 1702 326 326 LYS CA C 56.011 0.400 1 1703 326 326 LYS CB C 32.560 0.400 1 1704 326 326 LYS N N 117.706 0.400 1 1705 327 327 GLY H H 7.292 0.020 1 1706 327 327 GLY C C 172.587 0.400 1 1707 327 327 GLY CA C 44.518 0.400 1 1708 327 327 GLY N N 106.643 0.400 1 1709 328 328 GLU H H 8.442 0.020 1 1710 328 328 GLU C C 176.702 0.400 1 1711 328 328 GLU CA C 54.153 0.400 1 1712 328 328 GLU CB C 32.974 0.400 1 1713 328 328 GLU N N 121.098 0.400 1 1714 329 329 ILE H H 9.146 0.020 1 1715 329 329 ILE HD1 H 0.821 0.020 1 1716 329 329 ILE C C 178.106 0.400 1 1717 329 329 ILE CA C 62.150 0.400 1 1718 329 329 ILE CB C 37.812 0.400 1 1719 329 329 ILE CD1 C 12.362 0.400 1 1720 329 329 ILE N N 127.521 0.400 1 1721 330 330 MET H H 8.501 0.020 1 1722 330 330 MET CA C 56.700 0.400 1 1723 330 330 MET CB C 34.295 0.400 1 1724 330 330 MET N N 124.382 0.400 1 1725 331 331 PRO C C 175.327 0.400 1 1726 331 331 PRO CA C 63.503 0.400 1 1727 331 331 PRO CB C 31.138 0.400 1 1728 332 332 ASN H H 7.579 0.020 1 1729 332 332 ASN C C 175.698 0.400 1 1730 332 332 ASN CA C 51.443 0.400 1 1731 332 332 ASN CB C 38.656 0.400 1 1732 332 332 ASN N N 117.308 0.400 1 1733 333 333 ILE H H 6.383 0.020 1 1734 333 333 ILE HD1 H -0.138 0.020 1 1735 333 333 ILE CA C 59.976 0.400 1 1736 333 333 ILE CB C 36.320 0.400 1 1737 333 333 ILE CD1 C 12.253 0.400 1 1738 333 333 ILE N N 108.582 0.400 1 1739 334 334 PRO C C 178.686 0.400 1 1740 334 334 PRO CA C 65.485 0.400 1 1741 334 334 PRO CB C 31.199 0.400 1 1742 335 335 GLN H H 8.368 0.020 1 1743 335 335 GLN C C 177.018 0.400 1 1744 335 335 GLN CA C 59.566 0.400 1 1745 335 335 GLN CB C 26.389 0.400 1 1746 335 335 GLN N N 116.301 0.400 1 1747 336 336 MET H H 7.898 0.020 1 1748 336 336 MET C C 177.650 0.400 1 1749 336 336 MET CA C 56.084 0.400 1 1750 336 336 MET CB C 30.289 0.400 1 1751 336 336 MET N N 118.456 0.400 1 1752 337 337 SER H H 7.922 0.020 1 1753 337 337 SER C C 177.115 0.400 1 1754 337 337 SER CA C 62.431 0.400 1 1755 337 337 SER CB C 60.579 0.400 1 1756 337 337 SER N N 113.543 0.400 1 1757 338 338 ALA H H 7.349 0.020 1 1758 338 338 ALA C C 180.158 0.400 1 1759 338 338 ALA CA C 54.699 0.400 1 1760 338 338 ALA CB C 18.545 0.400 1 1761 338 338 ALA N N 122.864 0.400 1 1762 339 339 PHE H H 7.541 0.020 1 1763 339 339 PHE C C 176.472 0.400 1 1764 339 339 PHE CA C 61.758 0.400 1 1765 339 339 PHE CB C 38.827 0.400 1 1766 339 339 PHE N N 118.848 0.400 1 1767 340 340 TRP H H 8.855 0.020 1 1768 340 340 TRP HE1 H 10.424 0.020 1 1769 340 340 TRP C C 179.128 0.400 1 1770 340 340 TRP CA C 59.877 0.400 1 1771 340 340 TRP CB C 30.212 0.400 1 1772 340 340 TRP N N 118.274 0.400 1 1773 340 340 TRP NE1 N 130.128 0.400 1 1774 341 341 TYR H H 7.514 0.020 1 1775 341 341 TYR C C 178.712 0.400 1 1776 341 341 TYR CA C 61.558 0.400 1 1777 341 341 TYR CB C 38.306 0.400 1 1778 341 341 TYR N N 114.829 0.400 1 1779 342 342 ALA H H 8.402 0.020 1 1780 342 342 ALA C C 180.891 0.400 1 1781 342 342 ALA CA C 55.063 0.400 1 1782 342 342 ALA CB C 19.012 0.400 1 1783 342 342 ALA N N 121.918 0.400 1 1784 343 343 VAL H H 8.630 0.020 1 1785 343 343 VAL HG1 H 0.863 0.020 2 1786 343 343 VAL HG2 H 0.168 0.020 2 1787 343 343 VAL C C 177.082 0.400 1 1788 343 343 VAL CA C 66.924 0.400 1 1789 343 343 VAL CB C 31.022 0.400 1 1790 343 343 VAL CG1 C 21.297 0.400 1 1791 343 343 VAL CG2 C 23.236 0.400 1 1792 343 343 VAL N N 118.565 0.400 1 1793 344 344 ARG H H 8.191 0.020 1 1794 344 344 ARG C C 178.506 0.400 1 1795 344 344 ARG CA C 60.236 0.400 1 1796 344 344 ARG CB C 29.926 0.400 1 1797 344 344 ARG N N 120.767 0.400 1 1798 345 345 THR H H 7.565 0.020 1 1799 345 345 THR C C 175.055 0.400 1 1800 345 345 THR CA C 66.564 0.400 1 1801 345 345 THR CB C 69.297 0.400 1 1802 345 345 THR N N 113.734 0.400 1 1803 346 346 ALA H H 7.804 0.020 1 1804 346 346 ALA C C 179.234 0.400 1 1805 346 346 ALA CA C 55.734 0.400 1 1806 346 346 ALA CB C 18.537 0.400 1 1807 346 346 ALA N N 122.931 0.400 1 1808 347 347 VAL H H 8.157 0.020 1 1809 347 347 VAL HG1 H 0.918 0.020 2 1810 347 347 VAL HG2 H 1.043 0.020 2 1811 347 347 VAL C C 178.034 0.400 1 1812 347 347 VAL CA C 67.494 0.400 1 1813 347 347 VAL CB C 31.336 0.400 1 1814 347 347 VAL CG1 C 20.468 0.400 1 1815 347 347 VAL CG2 C 22.282 0.400 1 1816 347 347 VAL N N 115.982 0.400 1 1817 348 348 ILE H H 7.771 0.020 1 1818 348 348 ILE HD1 H 0.869 0.020 1 1819 348 348 ILE C C 180.338 0.400 1 1820 348 348 ILE CA C 65.054 0.400 1 1821 348 348 ILE CB C 37.334 0.400 1 1822 348 348 ILE CD1 C 12.965 0.400 1 1823 348 348 ILE N N 118.391 0.400 1 1824 349 349 ASN H H 8.830 0.020 1 1825 349 349 ASN C C 178.073 0.400 1 1826 349 349 ASN CA C 55.948 0.400 1 1827 349 349 ASN CB C 37.166 0.400 1 1828 349 349 ASN N N 121.104 0.400 1 1829 350 350 ALA H H 8.519 0.020 1 1830 350 350 ALA C C 181.189 0.400 1 1831 350 350 ALA CA C 54.159 0.400 1 1832 350 350 ALA CB C 17.998 0.400 1 1833 350 350 ALA N N 122.788 0.400 1 1834 351 351 ALA H H 9.165 0.020 1 1835 351 351 ALA C C 178.326 0.400 1 1836 351 351 ALA CA C 55.635 0.400 1 1837 351 351 ALA CB C 18.028 0.400 1 1838 351 351 ALA N N 121.117 0.400 1 1839 352 352 SER H H 7.879 0.020 1 1840 352 352 SER C C 175.715 0.400 1 1841 352 352 SER CA C 58.960 0.400 1 1842 352 352 SER CB C 64.440 0.400 1 1843 352 352 SER N N 108.006 0.400 1 1844 353 353 GLY H H 7.614 0.020 1 1845 353 353 GLY C C 174.546 0.400 1 1846 353 353 GLY CA C 45.785 0.400 1 1847 353 353 GLY N N 109.918 0.400 1 1848 354 354 ARG H H 8.227 0.020 1 1849 354 354 ARG C C 176.819 0.400 1 1850 354 354 ARG CA C 58.578 0.400 1 1851 354 354 ARG CB C 30.613 0.400 1 1852 354 354 ARG N N 121.091 0.400 1 1853 355 355 GLN H H 7.330 0.020 1 1854 355 355 GLN C C 176.068 0.400 1 1855 355 355 GLN CA C 54.391 0.400 1 1856 355 355 GLN CB C 36.304 0.400 1 1857 355 355 GLN N N 113.628 0.400 1 1858 356 356 THR H H 8.567 0.020 1 1859 356 356 THR C C 174.887 0.400 1 1860 356 356 THR CA C 61.464 0.400 1 1861 356 356 THR CB C 70.567 0.400 1 1862 356 356 THR N N 111.810 0.400 1 1863 357 357 VAL H H 8.731 0.020 1 1864 357 357 VAL HG1 H 0.991 0.020 2 1865 357 357 VAL HG2 H 1.045 0.020 2 1866 357 357 VAL C C 177.155 0.400 1 1867 357 357 VAL CA C 67.861 0.400 1 1868 357 357 VAL CB C 31.562 0.400 1 1869 357 357 VAL CG1 C 21.315 0.400 1 1870 357 357 VAL CG2 C 23.401 0.400 1 1871 357 357 VAL N N 121.378 0.400 1 1872 358 358 ASP H H 8.121 0.020 1 1873 358 358 ASP C C 178.907 0.400 1 1874 358 358 ASP CA C 57.822 0.400 1 1875 358 358 ASP CB C 40.961 0.400 1 1876 358 358 ASP N N 115.258 0.400 1 1877 359 359 GLU H H 7.605 0.020 1 1878 359 359 GLU C C 178.618 0.400 1 1879 359 359 GLU CA C 58.759 0.400 1 1880 359 359 GLU CB C 29.969 0.400 1 1881 359 359 GLU N N 118.661 0.400 1 1882 360 360 ALA H H 8.697 0.020 1 1883 360 360 ALA C C 181.584 0.400 1 1884 360 360 ALA CA C 54.768 0.400 1 1885 360 360 ALA CB C 18.270 0.400 1 1886 360 360 ALA N N 121.539 0.400 1 1887 361 361 LEU H H 8.077 0.020 1 1888 361 361 LEU HD1 H 0.892 0.020 2 1889 361 361 LEU HD2 H 0.722 0.020 2 1890 361 361 LEU C C 178.899 0.400 1 1891 361 361 LEU CA C 57.465 0.400 1 1892 361 361 LEU CB C 39.897 0.400 1 1893 361 361 LEU CD1 C 25.264 0.400 1 1894 361 361 LEU CD2 C 19.605 0.400 1 1895 361 361 LEU N N 116.237 0.400 1 1896 362 362 LYS H H 7.701 0.020 1 1897 362 362 LYS C C 179.903 0.400 1 1898 362 362 LYS CA C 59.792 0.400 1 1899 362 362 LYS CB C 31.531 0.400 1 1900 362 362 LYS N N 121.554 0.400 1 1901 363 363 ASP H H 8.148 0.020 1 1902 363 363 ASP C C 178.938 0.400 1 1903 363 363 ASP CA C 57.231 0.400 1 1904 363 363 ASP CB C 40.438 0.400 1 1905 363 363 ASP N N 120.036 0.400 1 1906 364 364 ALA H H 7.736 0.020 1 1907 364 364 ALA C C 178.422 0.400 1 1908 364 364 ALA CA C 55.445 0.400 1 1909 364 364 ALA CB C 17.847 0.400 1 1910 364 364 ALA N N 121.437 0.400 1 1911 365 365 GLN H H 8.240 0.020 1 1912 365 365 GLN C C 179.207 0.400 1 1913 365 365 GLN CA C 60.224 0.400 1 1914 365 365 GLN CB C 27.280 0.400 1 1915 365 365 GLN N N 118.228 0.400 1 1916 366 366 THR H H 8.154 0.020 1 1917 366 366 THR C C 175.969 0.400 1 1918 366 366 THR CA C 66.157 0.400 1 1919 366 366 THR CB C 69.063 0.400 1 1920 366 366 THR N N 115.346 0.400 1 1921 367 367 ARG H H 7.974 0.020 1 1922 367 367 ARG C C 178.725 0.400 1 1923 367 367 ARG CA C 58.985 0.400 1 1924 367 367 ARG CB C 29.725 0.400 1 1925 367 367 ARG N N 120.129 0.400 1 1926 368 368 ILE H H 8.005 0.020 1 1927 368 368 ILE HD1 H 0.693 0.020 1 1928 368 368 ILE C C 177.188 0.400 1 1929 368 368 ILE CA C 65.050 0.400 1 1930 368 368 ILE CB C 38.613 0.400 1 1931 368 368 ILE CD1 C 15.285 0.400 1 1932 368 368 ILE N N 117.405 0.400 1 1933 369 369 THR H H 7.633 0.020 1 1934 369 369 THR C C 174.309 0.400 1 1935 369 369 THR CA C 62.641 0.400 1 1936 369 369 THR CB C 70.438 0.400 1 1937 369 369 THR N N 107.054 0.400 1 1938 370 370 LYS H H 7.400 0.020 1 1939 370 370 LYS CA C 59.013 0.400 1 1940 370 370 LYS CB C 32.391 0.400 1 1941 370 370 LYS N N 128.247 0.400 1 stop_ save_