data_4987 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H,13C and 15N chemical shift assignment for the maltotriose-bound state of 2H,13C,15N-labeled maltodextrin-binding protein ; _BMRB_accession_number 4987 _BMRB_flat_file_name bmr4987.str _Entry_type original _Submission_date 2001-04-11 _Accession_date 2001-04-17 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Assignment of the deuterated protein' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Evenas Johan . . 2 Tugarinov Vitali . . 3 Skrynnikov Nikolai R. . 4 Goto Natalie K. . 5 Muhandiram Ranjith . . 6 Kay Lewis E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 341 "13C chemical shifts" 1043 "15N chemical shifts" 341 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-09-12 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4986 'ligand-free state' stop_ _Original_release_date 2001-09-12 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Ligand-induced Structural changes to Maltodextrin-binding Protein as Studied by Solution NMR Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21293199 _PubMed_ID 11399072 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Evenas Johan . . 2 Tugarinov Vitali . . 3 Skrynnikov Nikolai R. . 4 Goto Natalie K. . 5 Muhandiram Ranjith . . 6 Kay Lewis E. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 309 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 961 _Page_last 974 _Year 2001 _Details . loop_ _Keyword 'chemical shift assignment' 'dipolar couplings' 'maltodextrin binding protein' 'protein domains' 'solution conformation' stop_ save_ ################################## # Molecular system description # ################################## save_system_MBP _Saveframe_category molecular_system _Mol_system_name 'maltodextrin-binding protein' _Abbreviation_common MBP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'maltodextrin-binding protein' $MBP maltotriose $MLR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'maltodextrin-binding protein' _Abbreviation_common MBP _Molecular_mass 40694 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 370 _Mol_residue_sequence ; KTEEGKLVIWINGDKGYNGL AEVGKKFEKDTGIKVTVEHP DKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEIT PDKAFQDKLYPFTWDAVRYN GKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELK AKGKSALMFNLQEPYFTWPL IAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIK NKHMNADTDYSIAEAAFNKG ETAMTINGPWAWSNIDTSKV NYGVTVLPTFKGQPSKPFVG VLSAGINAASPNKELAKEFL ENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAAT MENAQKGEIMPNIPQMSAFW YAVRTAVINAASGRQTVDEA LKDAQTRITK ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 THR 3 GLU 4 GLU 5 GLY 6 LYS 7 LEU 8 VAL 9 ILE 10 TRP 11 ILE 12 ASN 13 GLY 14 ASP 15 LYS 16 GLY 17 TYR 18 ASN 19 GLY 20 LEU 21 ALA 22 GLU 23 VAL 24 GLY 25 LYS 26 LYS 27 PHE 28 GLU 29 LYS 30 ASP 31 THR 32 GLY 33 ILE 34 LYS 35 VAL 36 THR 37 VAL 38 GLU 39 HIS 40 PRO 41 ASP 42 LYS 43 LEU 44 GLU 45 GLU 46 LYS 47 PHE 48 PRO 49 GLN 50 VAL 51 ALA 52 ALA 53 THR 54 GLY 55 ASP 56 GLY 57 PRO 58 ASP 59 ILE 60 ILE 61 PHE 62 TRP 63 ALA 64 HIS 65 ASP 66 ARG 67 PHE 68 GLY 69 GLY 70 TYR 71 ALA 72 GLN 73 SER 74 GLY 75 LEU 76 LEU 77 ALA 78 GLU 79 ILE 80 THR 81 PRO 82 ASP 83 LYS 84 ALA 85 PHE 86 GLN 87 ASP 88 LYS 89 LEU 90 TYR 91 PRO 92 PHE 93 THR 94 TRP 95 ASP 96 ALA 97 VAL 98 ARG 99 TYR 100 ASN 101 GLY 102 LYS 103 LEU 104 ILE 105 ALA 106 TYR 107 PRO 108 ILE 109 ALA 110 VAL 111 GLU 112 ALA 113 LEU 114 SER 115 LEU 116 ILE 117 TYR 118 ASN 119 LYS 120 ASP 121 LEU 122 LEU 123 PRO 124 ASN 125 PRO 126 PRO 127 LYS 128 THR 129 TRP 130 GLU 131 GLU 132 ILE 133 PRO 134 ALA 135 LEU 136 ASP 137 LYS 138 GLU 139 LEU 140 LYS 141 ALA 142 LYS 143 GLY 144 LYS 145 SER 146 ALA 147 LEU 148 MET 149 PHE 150 ASN 151 LEU 152 GLN 153 GLU 154 PRO 155 TYR 156 PHE 157 THR 158 TRP 159 PRO 160 LEU 161 ILE 162 ALA 163 ALA 164 ASP 165 GLY 166 GLY 167 TYR 168 ALA 169 PHE 170 LYS 171 TYR 172 GLU 173 ASN 174 GLY 175 LYS 176 TYR 177 ASP 178 ILE 179 LYS 180 ASP 181 VAL 182 GLY 183 VAL 184 ASP 185 ASN 186 ALA 187 GLY 188 ALA 189 LYS 190 ALA 191 GLY 192 LEU 193 THR 194 PHE 195 LEU 196 VAL 197 ASP 198 LEU 199 ILE 200 LYS 201 ASN 202 LYS 203 HIS 204 MET 205 ASN 206 ALA 207 ASP 208 THR 209 ASP 210 TYR 211 SER 212 ILE 213 ALA 214 GLU 215 ALA 216 ALA 217 PHE 218 ASN 219 LYS 220 GLY 221 GLU 222 THR 223 ALA 224 MET 225 THR 226 ILE 227 ASN 228 GLY 229 PRO 230 TRP 231 ALA 232 TRP 233 SER 234 ASN 235 ILE 236 ASP 237 THR 238 SER 239 LYS 240 VAL 241 ASN 242 TYR 243 GLY 244 VAL 245 THR 246 VAL 247 LEU 248 PRO 249 THR 250 PHE 251 LYS 252 GLY 253 GLN 254 PRO 255 SER 256 LYS 257 PRO 258 PHE 259 VAL 260 GLY 261 VAL 262 LEU 263 SER 264 ALA 265 GLY 266 ILE 267 ASN 268 ALA 269 ALA 270 SER 271 PRO 272 ASN 273 LYS 274 GLU 275 LEU 276 ALA 277 LYS 278 GLU 279 PHE 280 LEU 281 GLU 282 ASN 283 TYR 284 LEU 285 LEU 286 THR 287 ASP 288 GLU 289 GLY 290 LEU 291 GLU 292 ALA 293 VAL 294 ASN 295 LYS 296 ASP 297 LYS 298 PRO 299 LEU 300 GLY 301 ALA 302 VAL 303 ALA 304 LEU 305 LYS 306 SER 307 TYR 308 GLU 309 GLU 310 GLU 311 LEU 312 ALA 313 LYS 314 ASP 315 PRO 316 ARG 317 ILE 318 ALA 319 ALA 320 THR 321 MET 322 GLU 323 ASN 324 ALA 325 GLN 326 LYS 327 GLY 328 GLU 329 ILE 330 MET 331 PRO 332 ASN 333 ILE 334 PRO 335 GLN 336 MET 337 SER 338 ALA 339 PHE 340 TRP 341 TYR 342 ALA 343 VAL 344 ARG 345 THR 346 ALA 347 VAL 348 ILE 349 ASN 350 ALA 351 ALA 352 SER 353 GLY 354 ARG 355 GLN 356 THR 357 VAL 358 ASP 359 GLU 360 ALA 361 LEU 362 LYS 363 ASP 364 ALA 365 GLN 366 THR 367 ARG 368 ILE 369 THR 370 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 25237 ER690 100.00 370 99.46 99.46 0.00e+00 BMRB 4354 MBP 100.00 370 100.00 100.00 0.00e+00 BMRB 4986 MBP 100.00 370 100.00 100.00 0.00e+00 BMRB 6807 MBP 100.00 370 99.73 99.73 0.00e+00 BMRB 7114 MBP 100.00 370 100.00 100.00 0.00e+00 PDB 1A7L "Dominant B-Cell Epitope From The Pres2 Region Of Hepatitis B Virus In The Form Of An Inserted Peptide Segment In Maltodextrin-B" 98.65 389 99.18 99.18 0.00e+00 PDB 1ANF "Maltodextrin Binding Protein With Bound Maltose" 100.00 370 99.73 99.73 0.00e+00 PDB 1DMB "Refined 1.8 Angstroms Structure Reveals The Mechanism Of Binding Of A Cyclic Sugar, Beta-Cyclodextrin, To The Maltodextrin Bind" 100.00 370 99.73 99.73 0.00e+00 PDB 1EZ9 "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P1 Crystal Form" 100.00 370 99.73 99.73 0.00e+00 PDB 1EZO "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 100.00 100.00 0.00e+00 PDB 1EZP "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin Using Peptide Orientations From Dipolar Couplings" 100.00 370 100.00 100.00 0.00e+00 PDB 1FQA "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQB "Structure Of Maltotriotol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQC "Crystal Structure Of Maltotriotol Bound To Closed-Form Maltodextrin Binding Protein" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQD "Crystal Structure Of Maltotetraitol Bound To Closed-Form Maltodextrin Binding Protein" 99.46 370 100.00 100.00 0.00e+00 PDB 1HSJ "Sarr Mbp Fusion Structure" 98.92 487 99.18 99.18 0.00e+00 PDB 1JVX "Maltodextrin-Binding Protein Variant D207cA301GSP316C Cross-Linked In Crystal" 100.27 372 98.65 98.92 0.00e+00 PDB 1JVY "Maltodextrin-Binding Protein Variant D207cA301GSP316C With Beta-Mercaptoethanol Mixed Disulfides" 100.27 372 98.65 98.92 0.00e+00 PDB 1JW4 "Structure Of Ligand-Free Maltodextrin-Binding Protein" 100.00 370 99.73 99.73 0.00e+00 PDB 1JW5 "Structure Of Maltose Bound To Open-Form Maltodextrin- Binding Protein In P1 Crystal" 100.00 370 99.73 99.73 0.00e+00 PDB 1LAX "Crystal Structure Of Male31, A Defective Folding Mutant Of Maltose-Binding Protein" 100.00 370 99.19 99.19 0.00e+00 PDB 1LLS "Crystal Structure Of Unliganded Maltose Binding Protein With Xenon" 100.00 370 99.73 99.73 0.00e+00 PDB 1MDP "Refined Structures Of Two Insertion(Slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.00 363 97.30 97.30 0.00e+00 PDB 1MDQ "Refined Structures Of Two Insertion(slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.27 371 99.19 99.46 0.00e+00 PDB 1MG1 "Htlv-1 Gp21 EctodomainMALTOSE-Binding Protein Chimera" 97.84 450 99.17 99.17 0.00e+00 PDB 1MH3 "Maltose Binding-A1 Homeodomain Protein Chimera, Crystal Form I" 98.92 421 98.91 98.91 0.00e+00 PDB 1MH4 "Maltose Binding-A1 Homeodomain Protein Chimera, Crystal Form Ii" 98.92 421 98.91 98.91 0.00e+00 PDB 1MPB "Maltodextrin-Binding Protein (Maltose-Binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (Trp-230-Arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1MPC "Maltodextrin-binding Protein (maltose-binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (trp-230-arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1MPD "Maltodextrin-Binding Protein (Maltose-Binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (Trp-230-Arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1N3W "Engineered High-affinity Maltose-binding Protein" 100.00 366 98.38 98.38 0.00e+00 PDB 1N3X "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 98.38 98.38 0.00e+00 PDB 1NL5 "Engineered High-affinity Maltose-binding Protein" 100.00 366 97.84 97.84 0.00e+00 PDB 1NMU Mbp-L30 98.92 382 99.73 99.73 0.00e+00 PDB 1OMP "Crystallographic Evidence Of A Large Ligand-Induced Hinge- Twist Motion Between The Two Domains Of The Maltodextrin- Binding Pr" 100.00 370 99.73 99.73 0.00e+00 PDB 1PEB "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 97.84 97.84 0.00e+00 PDB 1R6Z "The Crystal Structure Of The Argonaute2 Paz Domain (as A Mbp Fusion)" 98.92 509 99.73 99.73 0.00e+00 PDB 1SVX "Crystal Structure Of A Designed Selected Ankyrin Repeat Protein In Complex With The Maltose Binding Protein" 98.92 395 100.00 100.00 0.00e+00 PDB 1T0K "Joint X-ray And Nmr Refinement Of Yeast L30e-mrna Complex" 98.92 381 99.73 99.73 0.00e+00 PDB 1Y4C "Designed Helical Protein Fusion Mbp" 98.92 494 99.73 99.73 0.00e+00 PDB 1YTV "Maltose-binding Protein Fusion To A C-terminal Fragment Of The V1a Vasopressin Receptor" 98.92 366 99.73 99.73 0.00e+00 PDB 1ZIU "Crystal Structure Of Nickel-bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZJL "Crystal Structure Of Zinc-Bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZKB "Zinc-Free Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZMG "Crystal Structure Of Copper-Bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 2D21 "Nmr Structure Of Stereo-Array Isotope Labelled (Sail) Maltodextrin-Binding Protein (Mbp)" 100.00 370 99.73 99.73 0.00e+00 PDB 2H25 "Solution Structure Of Maltose Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 100.00 100.00 0.00e+00 PDB 2KLF "Pere Nmr Structure Of Maltodextrin-Binding Protein" 100.00 370 100.00 100.00 0.00e+00 PDB 2MV0 "Solution Nmr Structure Of Maltose-binding Protein From Escherichia Coli, Northeast Structural Genomics Consortium (nesg) Target" 100.00 370 99.73 99.73 0.00e+00 PDB 2NVU "Structure Of Appbp1-Uba3~nedd8-Nedd8-Mgatp-Ubc12(C111a), A Trapped Ubiquitin-Like Protein Activation Complex" 98.92 805 98.91 98.91 0.00e+00 PDB 2OBG "Crystal Structure Of Monobody Mbp-74MALTOSE BINDING PROTEIN FUSION Complex" 98.92 461 100.00 100.00 0.00e+00 PDB 2OK2 "Muts C-Terminal Domain Fused To Maltose Binding Protein" 98.92 402 99.45 99.73 0.00e+00 PDB 2R6G "The Crystal Structure Of The E. Coli Maltose Transporter" 100.00 370 99.73 99.73 0.00e+00 PDB 2V93 "Equillibrium Mixture Of Open And Partially-Closed Species In The Apo State Of Maltodextrin-Binding Protein By Paramagnetic Rela" 100.00 370 99.19 99.19 0.00e+00 PDB 2VGQ "Crystal Structure Of Human Ips-1 Card" 98.92 477 99.73 99.73 0.00e+00 PDB 2XZ3 "Blv Tm Hairpin" 98.92 463 98.91 98.91 0.00e+00 PDB 2ZXT "Crystal Structure Of Tim40/mia40, A Disulfide Relay System In Mitochondria, Solved As Mbp Fusion Protein" 98.92 465 99.73 99.73 0.00e+00 PDB 3A3C "Crystal Structure Of Tim40/mia40 Fusing Mbp, C296s And C298s Mutant" 98.38 451 100.00 100.00 0.00e+00 PDB 3C4M "Structure Of Human Parathyroid Hormone In Complex With The Extracellular Domain Of Its G-Protein-Coupled Receptor (Pth1r)" 98.92 539 99.73 99.73 0.00e+00 PDB 3CSB "Crystal Structure Of Monobody Ysx1MALTOSE BINDING PROTEIN Fusion Complex" 98.92 465 100.00 100.00 0.00e+00 PDB 3CSG "Crystal Structure Of Monobody Ys1(Mbp-74)MALTOSE BINDING Protein Fusion Complex" 98.92 461 100.00 100.00 0.00e+00 PDB 3D4C "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form I)" 98.92 481 99.18 99.18 0.00e+00 PDB 3D4G "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Ii)" 98.92 481 99.18 99.18 0.00e+00 PDB 3DM0 "Maltose Binding Protein Fusion With Rack1 From A. Thaliana" 98.92 694 98.09 98.09 0.00e+00 PDB 3EF7 "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Iii)" 98.92 481 99.18 99.18 0.00e+00 PDB 3EHS "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (Crfr1)" 98.92 476 99.73 99.73 0.00e+00 PDB 3EHT "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (crfr1) In Complex With C" 98.92 476 99.45 99.45 0.00e+00 PDB 3EHU "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (crfr1) In Complex With C" 98.92 476 99.45 99.45 0.00e+00 PDB 3F5F "Crystal Structure Of Heparan Sulfate 2-O-Sulfotransferase From Gallus Gallus As A Maltose Binding Protein Fusion" 98.92 658 98.91 98.91 0.00e+00 PDB 3G7V "Islet Amyloid Polypeptide (iapp Or Amylin) Fused To Maltose Binding Protein" 99.19 408 98.64 98.64 0.00e+00 PDB 3G7W "Islet Amyloid Polypeptide (Iapp Or Amylin) Residues 1 To 22 Fused To Maltose Binding Protein" 98.92 393 98.91 98.91 0.00e+00 PDB 3H3G "Crystal Structure Of The Extracellular Domain Of The Human Parathyroid Hormone Receptor (Pth1r) In Complex With Parathyroid Hor" 98.92 539 99.73 99.73 0.00e+00 PDB 3H4Z "Crystal Structure Of An Mbp-Der P 7 Fusion Protein" 98.92 568 97.54 97.54 0.00e+00 PDB 3HPI "Crystal Structure Of Maltose-Binding Protein Mutant With Bound Sucrose" 100.00 372 98.65 98.92 0.00e+00 PDB 3HST "N-Terminal Rnase H Domain Of Rv2228c From Mycobacterium Tuberculosis As A Fusion Protein With Maltose Binding Protein" 99.19 387 99.46 99.46 0.00e+00 PDB 3IO4 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C90" 98.92 449 98.91 98.91 0.00e+00 PDB 3IO6 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-A" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOR "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C95" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOT "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-B" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOU "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C94" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOV "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C99" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOW "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C99-Hg" 98.92 449 98.91 98.91 0.00e+00 PDB 3KJT "Stimulation Of The Maltose Transporter By A Mutant Sucrose B Protein Gives Insights Into Abc Transporter Coupling" 100.00 372 98.65 98.92 0.00e+00 PDB 3L2J "Dimeric Structure Of The Ligand-Free Extracellular Domain Of Parathyroid Hormone Receptor (Pth1r)" 98.38 535 100.00 100.00 0.00e+00 PDB 3LBS "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Bound Form)" 98.38 384 99.45 100.00 0.00e+00 PDB 3LC8 "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Free Form)" 98.38 384 99.45 100.00 0.00e+00 PDB 3MBP "Maltodextrin-Binding Protein With Bound Maltotriose" 100.00 370 99.73 99.73 0.00e+00 PDB 3MP1 "Complex Structure Of Sgf29 And Trimethylated H3k4" 98.92 522 99.18 99.18 0.00e+00 PDB 3MP6 "Complex Structure Of Sgf29 And Dimethylated H3k4" 98.92 522 99.18 99.18 0.00e+00 PDB 3MP8 "Crystal Structure Of Sgf29 Tudor Domain" 98.92 522 99.18 99.18 0.00e+00 PDB 3MQ9 "Crystal Structure Of Ectodomain Mutant Of Bst-2TETHERINCD317 FUSED To Mbp" 99.73 471 99.73 99.73 0.00e+00 PDB 3N93 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 3" 98.92 482 99.73 99.73 0.00e+00 PDB 3N94 "Crystal Structure Of Human Pituitary Adenylate Cyclase 1 Receptor- Short N-Terminal Extracellular Domain" 98.92 475 99.73 99.73 0.00e+00 PDB 3N95 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 2" 98.92 482 99.73 99.73 0.00e+00 PDB 3N96 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 1" 98.92 482 99.73 99.73 0.00e+00 PDB 3O3U "Crystal Structure Of Human Receptor For Advanced Glycation Endproducts (Rage)" 98.38 581 99.18 99.18 0.00e+00 PDB 3OAI "Crystal Structure Of The Extra-Cellular Domain Of Human Myelin Protein Zero" 99.19 507 99.46 99.46 0.00e+00 PDB 3OB4 "Mbp-Fusion Protein Of The Major Peanut Allergen Ara H 2" 98.92 500 97.54 97.54 0.00e+00 PDB 3PGF "Crystal Structure Of Maltose Bound Mbp With A Conformationally Specific Synthetic Antigen Binder (Sab)" 99.19 398 99.46 99.46 0.00e+00 PDB 3PUV "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Vo4" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUW "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Alf4" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUX "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Bef3" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUY "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Amp-Pnp After Crystal Soaking Of The Pretranslo" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUZ "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Bound To Amp-Pnp" 100.00 370 99.19 99.19 0.00e+00 PDB 3PV0 "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Without Nucleotide" 100.00 370 99.19 99.19 0.00e+00 PDB 3PY7 "Crystal Structure Of Full-length Bovine Papillomavirus Oncoprotein E6 In Complex With Ld1 Motif Of Paxillin At 2.3a Resolution" 98.92 523 98.09 98.09 0.00e+00 PDB 3Q25 "Crystal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 99.73 99.73 0.00e+00 PDB 3Q26 "Cyrstal Structure Of Human Alpha-Synuclein (10-42) Fused To Maltose Binding Protein (Mbp)" 98.92 404 99.73 99.73 0.00e+00 PDB 3Q27 "Cyrstal Structure Of Human Alpha-Synuclein (32-57) Fused To Maltose Binding Protein (Mbp)" 98.92 397 99.73 99.73 0.00e+00 PDB 3Q28 "Cyrstal Structure Of Human Alpha-Synuclein (58-79) Fused To Maltose Binding Protein (Mbp)" 99.19 393 99.46 99.46 0.00e+00 PDB 3Q29 "Cyrstal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 99.73 99.73 0.00e+00 PDB 3RLF "Crystal Structure Of The Maltose-Binding ProteinMALTOSE TRANSPORTER Complex In An Outward-Facing Conformation Bound To Mgamppnp" 100.00 380 99.73 99.73 0.00e+00 PDB 3RUM "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" 98.92 378 99.73 99.73 0.00e+00 PDB 3SER "Zn-Mediated Polymer Of Maltose-Binding Protein K26hK30H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SES "Cu-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SET "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form I)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEU "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Iii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEV "Zn-Mediated Trimer Of Maltose-Binding Protein E310hK314H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEW "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form I)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEX "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form Ii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEY "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Ii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3VD8 "Crystal Structure Of Human Aim2 Pyd Domain With Mbp Fusion" 98.92 489 97.54 97.54 0.00e+00 PDB 3VFJ "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Mbp As A Ligand Carrier" 98.92 378 99.73 99.73 0.00e+00 PDB 3W15 "Structure Of Peroxisomal Targeting Signal 2 (pts2) Of Saccharomyces Cerevisiae 3-ketoacyl-coa Thiolase In Complex With Pex7p An" 100.00 389 99.73 99.73 0.00e+00 PDB 3WAI "Crystal Structure Of The C-terminal Globular Domain Of Oligosaccharyltransferase (afaglb-l, O29867_arcfu) From Archaeoglobus Fu" 98.92 739 99.73 99.73 0.00e+00 PDB 4B3N "Crystal Structure Of Rhesus Trim5alpha PrySPRY DOMAIN" 100.00 602 99.19 99.73 0.00e+00 PDB 4BL8 "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu)" 98.92 831 99.18 99.18 0.00e+00 PDB 4BL9 "Crystal Structure Of Full-length Human Suppressor Of Fused ( Sufu) Mutant Lacking A Regulatory Subdomain (crystal Form I)" 98.92 756 99.18 99.18 0.00e+00 PDB 4BLA "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu) Mutant Lacking A Regulatory Subdomain (crystal Form Ii)" 98.92 756 99.18 99.18 0.00e+00 PDB 4BLB "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli1p Complex" 98.92 753 98.63 98.63 0.00e+00 PDB 4BLD "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli3p Complex" 98.92 753 98.63 98.63 0.00e+00 PDB 4EDQ "Mbp-fusion Protein Of Myosin-binding Protein C Residues 149-269" 98.92 492 98.91 98.91 0.00e+00 PDB 4EGC "Crystal Structure Of Mbp-fused Human Six1 Bound To Human Eya2 Eya Domain" 98.92 559 98.36 98.36 0.00e+00 PDB 4EXK "A Chimera Protein Containing Mbp Fused To The C-Terminal Domain Of The Uncharacterized Protein Stm14_2015 From Salmonella Enter" 98.92 487 97.54 97.54 0.00e+00 PDB 4FE8 "Crystal Structure Of Htt36q3h-ex1-x1-c1(alpha)" 98.92 452 98.91 98.91 0.00e+00 PDB 4FEB "Crystal Structure Of Htt36q3h-ex1-x1-c2(beta)" 98.92 452 98.91 98.91 0.00e+00 PDB 4FEC "Crystal Structure Of Htt36q3h" 98.92 452 98.91 98.91 0.00e+00 PDB 4FED "Crystal Structure Of Htt36q3h" 98.92 452 98.91 98.91 0.00e+00 PDB 4GIZ "Crystal Structure Of Full-length Human Papillomavirus Oncoprotein E6 In Complex With Lxxll Peptide Of Ubiquitin Ligase E6ap At " 98.92 382 98.09 98.09 0.00e+00 PDB 4GLI "Crystal Structure Of Human Smn Yg-Dimer" 99.73 401 99.73 99.73 0.00e+00 PDB 4H1G "Structure Of Candida Albicans Kar3 Motor Domain Fused To Maltose- Binding Protein" 98.92 715 98.91 98.91 0.00e+00 PDB 4IFP "X-ray Crystal Structure Of Human Nlrp1 Card Domain" 98.92 466 97.54 97.54 0.00e+00 PDB 4JBZ "Structure Of Mcm10 Coiled-coil Region" 98.92 403 97.54 97.54 0.00e+00 PDB 4JKM "Crystal Structure Of Clostridium Perfringens Beta-glucuronidase" 99.19 400 99.18 99.18 0.00e+00 PDB 4KEG "Crystal Structure Of Mbp Fused Human Splunc1" 98.92 584 99.18 99.18 0.00e+00 PDB 4KHZ "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Pre-translocation Conformation Bound To Malt" 100.00 380 99.73 99.73 0.00e+00 PDB 4KI0 "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Outward-facing Conformation Bound To Maltohe" 100.00 380 99.73 99.73 0.00e+00 PDB 4KV3 "Ubiquitin-like Domain Of The Mycobacterium Tuberculosis Type Vii Secretion System Protein Eccd1 As Maltose-binding Protein Fusi" 98.92 461 98.91 98.91 0.00e+00 PDB 4KYC "Structure Of The C-terminal Domain Of The Menangle Virus Phosphoprotein, Fused To Mbp" 98.92 420 98.36 98.36 0.00e+00 PDB 4KYD "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp." 98.92 420 98.36 98.36 0.00e+00 PDB 4KYE "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp" 98.92 420 98.36 98.36 0.00e+00 PDB 4LOG "The Crystal Structure Of The Orphan Nuclear Receptor Pnr Ligand Binding Domain Fused With Mbp" 98.92 574 99.73 99.73 0.00e+00 PDB 4MBP "Maltodextrin Binding Protein With Bound Maltetrose" 100.00 370 99.73 99.73 0.00e+00 PDB 4MY2 "Crystal Structure Of Norrin In Fusion With Maltose Binding Protein" 98.92 477 99.73 99.73 0.00e+00 PDB 4N4X "Crystal Structure Of The Mbp Fused Human Splunc1 (native Form)" 98.92 584 99.18 99.18 0.00e+00 PDB 4NDZ "Structure Of Maltose Binding Protein Fusion To 2-o-sulfotransferase With Bound Heptasaccharide And Pap" 98.92 658 98.91 98.91 0.00e+00 PDB 4NUF "Crystal Structure Of Shp/eid1" 98.92 580 99.73 99.73 0.00e+00 PDB 4O4B "Crystal Structure Of An Inositol Hexakisphosphate Kinase Ehip6ka As A Fusion Protein With Maltose Binding Protein" 98.92 396 99.73 99.73 0.00e+00 PDB 4OGM "Mbp-fusion Protein Of Pila1 Residues 26-159" 99.19 520 97.28 97.28 0.00e+00 PDB 4OZQ "Crystal Structure Of The Mouse Kif14 Motor Domain" 98.92 720 98.91 98.91 0.00e+00 PDB 4PE2 "Mbp Pila1 Cd160" 99.19 516 99.46 99.46 0.00e+00 PDB 4PQK "C-terminal Domain Of Dna Binding Protein" 99.19 487 99.46 99.46 0.00e+00 PDB 4QVH "Crystal Structure Of The Essential Mycobacterium Tuberculosis Phosphopantetheinyl Transferase Pptt, Solved As A Fusion Protein " 98.92 598 98.36 98.36 0.00e+00 PDB 4R0Y "Structure Of Maltose-binding Protein Fusion With The C-terminal Gh1 Domain Of Guanylate Kinase-associated Protein From Rattus N" 97.57 501 99.72 99.72 0.00e+00 PDB 4TSM "Mbp-fusion Protein Of Pila1 From C. Difficile R20291 Residues 26-166" 99.19 520 97.28 97.28 0.00e+00 PDB 4WGI "A Single Diastereomer Of A Macrolactam Core Binds Specifically To Myeloid Cell Leukemia 1 (mcl1)" 98.92 518 99.73 99.73 0.00e+00 PDB 4WJV "Crystal Structure Of Rsa4 In Complex With The Nsa2 Binding Peptide" 99.19 381 97.82 97.82 0.00e+00 DBJ BAB38440 "periplasmic maltose-binding protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAE78036 "maltose transporter subunit [Escherichia coli str. K-12 substr. W3110]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAG79849 "maltose ABC transporter substrate binding component [Escherichia coli SE11]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAI28296 "periplasmic maltose-binding protein MalE [Escherichia coli O26:H11 str. 11368]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAI33473 "periplasmic maltose-binding protein MalE [Escherichia coli O103:H2 str. 12009]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAP78494 "Maltose-binding periplasmic protein [Escherichia coli LF82]" 100.00 396 98.65 99.46 0.00e+00 EMBL CAQ34383 "malE, subunit of maltose ABC transporter [Escherichia coli BL21(DE3)]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAR01012 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli IAI1]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAR05669 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli S88]" 100.00 396 98.65 99.46 0.00e+00 EMBL CAR10711 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli ED1a]" 100.00 396 98.65 99.46 0.00e+00 GB AAB59056 "periplasmic maltose-binding protein [Escherichia coli]" 100.00 396 99.73 99.73 0.00e+00 GB AAB86559 "maltose binding protein-lacZ alpha peptide fusion protein precursor [Shuttle vector pMAL-pIII]" 98.92 482 99.73 99.73 0.00e+00 GB AAB87675 "maltose binding protein-lacZ-alpha fusion protein [Expression vector pMal-X]" 98.38 496 100.00 100.00 0.00e+00 GB AAC43128 "periplasmic maltose-binding protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 GB AAC77004 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 REF NP_290668 "maltose ABC transporter substrate-binding protein [Escherichia coli O157:H7 str. EDL933]" 100.00 396 99.73 99.73 0.00e+00 REF NP_313044 "maltose ABC transporter periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 99.73 99.73 0.00e+00 REF NP_418458 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 REF NP_709885 "maltose ABC transporter substrate-binding protein [Shigella flexneri 2a str. 301]" 100.00 396 99.46 99.46 0.00e+00 REF NP_756856 "maltose ABC transporter periplasmic protein [Escherichia coli CFT073]" 100.00 396 98.65 99.46 0.00e+00 SP P0AEX9 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 99.73 99.73 0.00e+00 SP P0AEY0 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 99.73 99.73 0.00e+00 stop_ save_ ############# # Ligands # ############# save_MLR _Saveframe_category ligand _Mol_type non-polymer _Name_common "MLR (MALTOTRIOSE)" _BMRB_code . _PDB_code MLR _Molecular_mass 504.437 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 16 11:45:20 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1A C1A C . 0 . ? C2A C2A C . 0 . ? C3A C3A C . 0 . ? C4A C4A C . 0 . ? C5A C5A C . 0 . ? C6A C6A C . 0 . ? O1X O1X O . 0 . ? O2A O2A O . 0 . ? O3A O3A O . 0 . ? O4A O4A O . 0 . ? O5A O5A O . 0 . ? O6A O6A O . 0 . ? C1B C1B C . 0 . ? C2B C2B C . 0 . ? C3B C3B C . 0 . ? C4B C4B C . 0 . ? C5B C5B C . 0 . ? C6B C6B C . 0 . ? O2B O2B O . 0 . ? O3B O3B O . 0 . ? O4B O4B O . 0 . ? O5B O5B O . 0 . ? O6B O6B O . 0 . ? C1C C1C C . 0 . ? C2C C2C C . 0 . ? C3C C3C C . 0 . ? C4C C4C C . 0 . ? C5C C5C C . 0 . ? C6C C6C C . 0 . ? O2C O2C O . 0 . ? O3C O3C O . 0 . ? O4C O4C O . 0 . ? O5C O5C O . 0 . ? O6C O6C O . 0 . ? H1A H1A H . 0 . ? H2A H2A H . 0 . ? H3A H3A H . 0 . ? H4A H4A H . 0 . ? H5A H5A H . 0 . ? H6A1 H6A1 H . 0 . ? H6A2 H6A2 H . 0 . ? H1X H1X H . 0 . ? HOA2 HOA2 H . 0 . ? HOA3 HOA3 H . 0 . ? HOA6 HOA6 H . 0 . ? H1B H1B H . 0 . ? H2B H2B H . 0 . ? H3B H3B H . 0 . ? H4B H4B H . 0 . ? H5B H5B H . 0 . ? H6B1 H6B1 H . 0 . ? H6B2 H6B2 H . 0 . ? HOB2 HOB2 H . 0 . ? HOB3 HOB3 H . 0 . ? HOB6 HOB6 H . 0 . ? H1C H1C H . 0 . ? H2C H2C H . 0 . ? H3C H3C H . 0 . ? H4C H4C H . 0 . ? H5C H5C H . 0 . ? H6C1 H6C1 H . 0 . ? H6C2 H6C2 H . 0 . ? HOC2 HOC2 H . 0 . ? HOC3 HOC3 H . 0 . ? HOC4 HOC4 H . 0 . ? HOC6 HOC6 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1A C2A ? ? SING C1A O1X ? ? SING C1A O5A ? ? SING C1A H1A ? ? SING C2A C3A ? ? SING C2A O2A ? ? SING C2A H2A ? ? SING C3A C4A ? ? SING C3A O3A ? ? SING C3A H3A ? ? SING C4A C5A ? ? SING C4A O4A ? ? SING C4A H4A ? ? SING C5A C6A ? ? SING C5A O5A ? ? SING C5A H5A ? ? SING C6A O6A ? ? SING C6A H6A1 ? ? SING C6A H6A2 ? ? SING O1X H1X ? ? SING O2A HOA2 ? ? SING O3A HOA3 ? ? SING O4A C1B ? ? SING O6A HOA6 ? ? SING C1B C2B ? ? SING C1B O5B ? ? SING C1B H1B ? ? SING C2B C3B ? ? SING C2B O2B ? ? SING C2B H2B ? ? SING C3B C4B ? ? SING C3B O3B ? ? SING C3B H3B ? ? SING C4B C5B ? ? SING C4B O4B ? ? SING C4B H4B ? ? SING C5B C6B ? ? SING C5B O5B ? ? SING C5B H5B ? ? SING C6B O6B ? ? SING C6B H6B1 ? ? SING C6B H6B2 ? ? SING O2B HOB2 ? ? SING O3B HOB3 ? ? SING O4B C1C ? ? SING O6B HOB6 ? ? SING C1C C2C ? ? SING C1C O5C ? ? SING C1C H1C ? ? SING C2C C3C ? ? SING C2C O2C ? ? SING C2C H2C ? ? SING C3C C4C ? ? SING C3C O3C ? ? SING C3C H3C ? ? SING C4C C5C ? ? SING C4C O4C ? ? SING C4C H4C ? ? SING C5C C6C ? ? SING C5C O5C ? ? SING C5C H5C ? ? SING C6C O6C ? ? SING C6C H6C1 ? ? SING C6C H6C2 ? ? SING O2C HOC2 ? ? SING O3C HOC3 ? ? SING O4C HOC4 ? ? SING O6C HOC6 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MBP 'E. coli' 562 Bacteria . Escherichia coli stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $MBP 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $MBP 1.3 mM '[U-2H; U-15N; U-13C]' $MLR 1.3 mM . stop_ save_ ############################ # Computer software used # ############################ save_nmrview _Saveframe_category software _Name NMRView _Version 4.1 loop_ _Task 'semi-automatic assignment using CACB module' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_TROSY-versions_were_used_of_all_experiments_listed._1 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY-versions were used of all experiments listed.' _Sample_label $sample_1 save_ save_All_non-exchangeable_hydrogens_are_deuterons_so_all_2 _Saveframe_category NMR_applied_experiment _Experiment_name 'All non-exchangeable hydrogens are deuterons so all' _Sample_label $sample_1 save_ save_triple-resonance_experiments_are_2H-decoupled._3 _Saveframe_category NMR_applied_experiment _Experiment_name 'triple-resonance experiments are 2H-decoupled.' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__0_1 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__0_2 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__0_3 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__1_1 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_2 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__1_2 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__1_3 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__1_3 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__2_1 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_2 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__2_2 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__2_3 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__2_3 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__3_1 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_2 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__3_2 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__3_3 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__3_3 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__4_1 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_2 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__4_2 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__4_3 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__4_3 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_1 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__5_1 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_2 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__5_2 _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__5_3 _Saveframe_category NMR_applied_experiment _Experiment_name NMR_spec_expt__5_3 _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_mltrmbp_std _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 7.2 0.1 n/a temperature 310 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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_citation_label _Correction_value_citation_label 'sodium acetate' C 13 methyl ppm 25.87 external direct cylindrical external parallel $entry_citation $entry_citation H2O H 1 H2O ppm 4.658 internal direct cylindrical internal parallel $entry_citation $entry_citation urea N 15 methyl ppm 79.0 external direct cylindrical external parallel $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; Note that the protein is fully deuterated with the exception of exchangeable hydrogens which are protonated (2H-isotope effects are not corrected here). ; loop_ _Experiment_label 'TROSY-versions were used of all experiments listed.' 'All non-exchangeable hydrogens are deuterons so all' 'triple-resonance experiments are 2H-decoupled.' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $mltrmbp_std _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'maltodextrin-binding protein' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 LYS CA C 55.800 0.05 1 2 . 1 LYS CB C 32.200 0.05 1 3 . 1 LYS C C 176.400 0.05 1 4 . 2 THR N N 116.100 0.05 1 5 . 2 THR H H 8.200 0.005 1 6 . 2 THR CA C 61.600 0.05 1 7 . 2 THR CB C 69.100 0.05 1 8 . 2 THR C C 174.300 0.05 1 9 . 3 GLU N N 122.500 0.05 1 10 . 3 GLU H H 8.540 0.005 1 11 . 3 GLU CA C 55.600 0.05 1 12 . 3 GLU CB C 30.400 0.05 1 13 . 3 GLU C C 176.000 0.05 1 14 . 4 GLU N N 122.300 0.05 1 15 . 4 GLU H H 8.510 0.005 1 16 . 4 GLU CA C 56.300 0.05 1 17 . 4 GLU CB C 29.500 0.05 1 18 . 4 GLU C C 176.900 0.05 1 19 . 5 GLY N N 110.400 0.05 1 20 . 5 GLY H H 8.620 0.005 1 21 . 5 GLY CA C 45.200 0.05 1 22 . 5 GLY C C 172.200 0.05 1 23 . 6 LYS N N 119.100 0.05 1 24 . 6 LYS H H 7.710 0.005 1 25 . 6 LYS CA C 54.500 0.05 1 26 . 6 LYS CB C 34.500 0.05 1 27 . 6 LYS C C 173.500 0.05 1 28 . 7 LEU N N 118.500 0.05 1 29 . 7 LEU H H 8.420 0.005 1 30 . 7 LEU CA C 52.900 0.05 1 31 . 7 LEU CB C 45.500 0.05 1 32 . 7 LEU C C 175.200 0.05 1 33 . 8 VAL N N 125.400 0.05 1 34 . 8 VAL H H 10.010 0.005 1 35 . 8 VAL CA C 61.300 0.05 1 36 . 8 VAL CB C 32.800 0.05 1 37 . 8 VAL C C 175.700 0.05 1 38 . 9 ILE N N 128.200 0.05 1 39 . 9 ILE H H 9.100 0.005 1 40 . 9 ILE CA C 59.500 0.05 1 41 . 9 ILE CB C 40.400 0.05 1 42 . 9 ILE C C 174.700 0.05 1 43 . 10 TRP N N 126.500 0.05 1 44 . 10 TRP H H 8.820 0.005 1 45 . 10 TRP CA C 53.500 0.05 1 46 . 10 TRP CB C 32.400 0.05 1 47 . 10 TRP C C 173.900 0.05 1 48 . 11 ILE N N 122.000 0.05 1 49 . 11 ILE H H 8.760 0.005 1 50 . 11 ILE CA C 59.300 0.05 1 51 . 11 ILE CB C 40.500 0.05 1 52 . 11 ILE C C 170.900 0.05 1 53 . 12 ASN N N 122.000 0.05 1 54 . 12 ASN H H 9.260 0.005 1 55 . 12 ASN CA C 53.900 0.05 1 56 . 12 ASN CB C 39.600 0.05 1 57 . 12 ASN C C 177.400 0.05 1 58 . 13 GLY N N 105.200 0.05 1 59 . 13 GLY H H 7.950 0.005 1 60 . 13 GLY CA C 45.700 0.05 1 61 . 13 GLY C C 173.000 0.05 1 62 . 14 ASP N N 115.500 0.05 1 63 . 14 ASP H H 7.140 0.005 1 64 . 14 ASP CA C 52.100 0.05 1 65 . 14 ASP CB C 38.000 0.05 1 66 . 14 ASP C C 174.700 0.05 1 67 . 15 LYS N N 114.800 0.05 1 68 . 15 LYS H H 7.340 0.005 1 69 . 15 LYS CA C 51.600 0.05 1 70 . 15 LYS CB C 33.100 0.05 1 71 . 15 LYS C C 179.000 0.05 1 72 . 16 GLY N N 109.400 0.05 1 73 . 16 GLY H H 9.410 0.005 1 74 . 16 GLY CA C 47.900 0.05 1 75 . 16 GLY C C 175.400 0.05 1 76 . 17 TYR N N 120.700 0.05 1 77 . 17 TYR H H 8.310 0.005 1 78 . 17 TYR CA C 58.800 0.05 1 79 . 17 TYR CB C 36.500 0.05 1 80 . 17 TYR C C 177.600 0.05 1 81 . 18 ASN N N 124.300 0.05 1 82 . 18 ASN H H 7.990 0.005 1 83 . 18 ASN CA C 55.800 0.05 1 84 . 18 ASN CB C 36.700 0.05 1 85 . 18 ASN C C 179.000 0.05 1 86 . 19 GLY N N 112.500 0.05 1 87 . 19 GLY H H 9.250 0.005 1 88 . 19 GLY CA C 47.100 0.05 1 89 . 19 GLY C C 176.000 0.05 1 90 . 20 LEU N N 121.500 0.05 1 91 . 20 LEU H H 8.380 0.005 1 92 . 20 LEU CA C 57.100 0.05 1 93 . 20 LEU CB C 40.600 0.05 1 94 . 20 LEU C C 178.600 0.05 1 95 . 21 ALA N N 120.900 0.05 1 96 . 21 ALA H H 8.030 0.005 1 97 . 21 ALA CA C 54.600 0.05 1 98 . 21 ALA CB C 16.900 0.05 1 99 . 21 ALA C C 180.500 0.05 1 100 . 22 GLU N N 120.200 0.05 1 101 . 22 GLU H H 7.780 0.005 1 102 . 22 GLU CA C 59.200 0.05 1 103 . 22 GLU CB C 27.900 0.05 1 104 . 22 GLU C C 180.100 0.05 1 105 . 23 VAL N N 123.000 0.05 1 106 . 23 VAL H H 7.740 0.005 1 107 . 23 VAL CA C 66.200 0.05 1 108 . 23 VAL CB C 30.500 0.05 1 109 . 23 VAL C C 179.400 0.05 1 110 . 24 GLY N N 106.400 0.05 1 111 . 24 GLY H H 8.640 0.005 1 112 . 24 GLY CA C 47.200 0.05 1 113 . 24 GLY C C 175.100 0.05 1 114 . 25 LYS N N 122.500 0.05 1 115 . 25 LYS H H 8.310 0.005 1 116 . 25 LYS CA C 58.800 0.05 1 117 . 25 LYS CB C 31.200 0.05 1 118 . 25 LYS C C 179.400 0.05 1 119 . 26 LYS N N 122.600 0.05 1 120 . 26 LYS H H 7.640 0.005 1 121 . 26 LYS CA C 59.200 0.05 1 122 . 26 LYS CB C 31.300 0.05 1 123 . 26 LYS C C 178.100 0.05 1 124 . 27 PHE N N 120.000 0.05 1 125 . 27 PHE H H 8.060 0.005 1 126 . 27 PHE CA C 60.900 0.05 1 127 . 27 PHE CB C 38.600 0.05 1 128 . 27 PHE C C 178.900 0.05 1 129 . 28 GLU N N 124.000 0.05 1 130 . 28 GLU H H 8.880 0.005 1 131 . 28 GLU CA C 58.600 0.05 1 132 . 28 GLU CB C 29.200 0.05 1 133 . 28 GLU C C 179.800 0.05 1 134 . 29 LYS N N 121.800 0.05 1 135 . 29 LYS H H 8.100 0.005 1 136 . 29 LYS CA C 58.800 0.05 1 137 . 29 LYS CB C 30.700 0.05 1 138 . 29 LYS C C 178.300 0.05 1 139 . 30 ASP N N 116.200 0.05 1 140 . 30 ASP H H 7.580 0.005 1 141 . 30 ASP CA C 56.000 0.05 1 142 . 30 ASP CB C 40.400 0.05 1 143 . 30 ASP C C 178.200 0.05 1 144 . 31 THR N N 107.000 0.05 1 145 . 31 THR H H 7.910 0.005 1 146 . 31 THR CA C 62.200 0.05 1 147 . 31 THR CB C 71.600 0.05 1 148 . 31 THR C C 176.200 0.05 1 149 . 32 GLY N N 112.500 0.05 1 150 . 32 GLY H H 8.590 0.005 1 151 . 32 GLY CA C 44.900 0.05 1 152 . 32 GLY C C 173.400 0.05 1 153 . 33 ILE N N 124.100 0.05 1 154 . 33 ILE H H 7.750 0.005 1 155 . 33 ILE CA C 58.300 0.05 1 156 . 33 ILE CB C 35.100 0.05 1 157 . 33 ILE C C 173.700 0.05 1 158 . 34 LYS N N 124.500 0.05 1 159 . 34 LYS H H 7.710 0.005 1 160 . 34 LYS CA C 56.100 0.05 1 161 . 34 LYS CB C 32.100 0.05 1 162 . 34 LYS C C 175.600 0.05 1 163 . 35 VAL N N 124.800 0.05 1 164 . 35 VAL H H 8.450 0.005 1 165 . 35 VAL CA C 60.500 0.05 1 166 . 35 VAL CB C 32.200 0.05 1 167 . 35 VAL C C 175.700 0.05 1 168 . 36 THR N N 125.000 0.05 1 169 . 36 THR H H 9.100 0.005 1 170 . 36 THR CA C 60.900 0.05 1 171 . 36 THR CB C 70.300 0.05 1 172 . 36 THR C C 172.600 0.05 1 173 . 37 VAL N N 127.300 0.05 1 174 . 37 VAL H H 8.880 0.005 1 175 . 37 VAL CA C 61.100 0.05 1 176 . 37 VAL CB C 31.600 0.05 1 177 . 37 VAL C C 175.300 0.05 1 178 . 38 GLU N N 127.100 0.05 1 179 . 38 GLU H H 9.610 0.005 1 180 . 38 GLU CA C 53.700 0.05 1 181 . 38 GLU CB C 32.500 0.05 1 182 . 38 GLU C C 173.500 0.05 1 183 . 39 HIS N N 115.400 0.05 1 184 . 39 HIS H H 8.370 0.005 1 185 . 39 HIS CA C 50.700 0.05 1 186 . 39 HIS CB C 28.100 0.05 1 187 . 40 PRO CA C 61.600 0.05 1 188 . 40 PRO CB C 29.900 0.05 1 189 . 40 PRO C C 176.900 0.05 1 190 . 41 ASP N N 121.800 0.05 1 191 . 41 ASP H H 8.250 0.005 1 192 . 41 ASP CA C 54.500 0.05 1 193 . 41 ASP CB C 40.400 0.05 1 194 . 41 ASP C C 176.400 0.05 1 195 . 42 LYS N N 119.400 0.05 1 196 . 42 LYS H H 8.670 0.005 1 197 . 42 LYS CA C 55.600 0.05 1 198 . 42 LYS CB C 28.000 0.05 1 199 . 42 LYS C C 178.600 0.05 1 200 . 43 LEU N N 119.600 0.05 1 201 . 43 LEU H H 7.380 0.005 1 202 . 43 LEU CA C 58.400 0.05 1 203 . 43 LEU CB C 39.500 0.05 1 204 . 43 LEU C C 175.300 0.05 1 205 . 44 GLU N N 125.000 0.05 1 206 . 44 GLU H H 10.720 0.005 1 207 . 44 GLU CA C 56.500 0.05 1 208 . 44 GLU CB C 24.000 0.05 1 209 . 44 GLU C C 178.400 0.05 1 210 . 45 GLU N N 119.800 0.05 1 211 . 45 GLU H H 7.090 0.005 1 212 . 45 GLU CA C 56.400 0.05 1 213 . 45 GLU CB C 29.900 0.05 1 214 . 45 GLU C C 178.600 0.05 1 215 . 46 LYS N N 120.000 0.05 1 216 . 46 LYS H H 8.150 0.005 1 217 . 46 LYS CA C 58.000 0.05 1 218 . 46 LYS CB C 32.600 0.05 1 219 . 46 LYS C C 179.000 0.05 1 220 . 47 PHE N N 117.400 0.05 1 221 . 47 PHE H H 8.620 0.005 1 222 . 47 PHE CA C 62.900 0.05 1 223 . 47 PHE CB C 35.700 0.05 1 224 . 48 PRO CA C 64.900 0.05 1 225 . 48 PRO CB C 29.600 0.05 1 226 . 48 PRO C C 177.700 0.05 1 227 . 49 GLN N N 114.500 0.05 1 228 . 49 GLN H H 7.030 0.005 1 229 . 49 GLN CA C 57.300 0.05 1 230 . 49 GLN CB C 28.100 0.05 1 231 . 49 GLN C C 178.200 0.05 1 232 . 50 VAL N N 110.100 0.05 1 233 . 50 VAL H H 7.570 0.005 1 234 . 50 VAL CA C 61.200 0.05 1 235 . 50 VAL CB C 31.600 0.05 1 236 . 50 VAL C C 178.000 0.05 1 237 . 51 ALA N N 124.600 0.05 1 238 . 51 ALA H H 8.090 0.005 1 239 . 51 ALA CA C 54.500 0.05 1 240 . 51 ALA CB C 17.300 0.05 1 241 . 51 ALA C C 179.800 0.05 1 242 . 52 ALA N N 117.400 0.05 1 243 . 52 ALA H H 7.740 0.005 1 244 . 52 ALA CA C 52.700 0.05 1 245 . 52 ALA CB C 17.600 0.05 1 246 . 52 ALA C C 178.400 0.05 1 247 . 53 THR N N 106.100 0.05 1 248 . 53 THR H H 7.260 0.005 1 249 . 53 THR CA C 61.000 0.05 1 250 . 53 THR CB C 69.300 0.05 1 251 . 53 THR C C 175.200 0.05 1 252 . 54 GLY N N 108.800 0.05 1 253 . 54 GLY H H 7.810 0.005 1 254 . 54 GLY CA C 45.100 0.05 1 255 . 54 GLY C C 173.500 0.05 1 256 . 55 ASP N N 119.000 0.05 1 257 . 55 ASP H H 7.550 0.005 1 258 . 55 ASP CA C 53.000 0.05 1 259 . 55 ASP CB C 41.600 0.05 1 260 . 55 ASP C C 175.100 0.05 1 261 . 56 GLY N N 106.300 0.05 1 262 . 56 GLY H H 8.160 0.005 1 263 . 56 GLY CA C 43.500 0.05 1 264 . 57 PRO CA C 61.300 0.05 1 265 . 57 PRO CB C 30.000 0.05 1 266 . 57 PRO C C 174.900 0.05 1 267 . 58 ASP N N 118.100 0.05 1 268 . 58 ASP H H 8.660 0.005 1 269 . 58 ASP CA C 57.700 0.05 1 270 . 58 ASP CB C 43.100 0.05 1 271 . 58 ASP C C 175.400 0.05 1 272 . 59 ILE N N 114.200 0.05 1 273 . 59 ILE H H 7.610 0.005 1 274 . 59 ILE CA C 58.400 0.05 1 275 . 59 ILE CB C 41.700 0.05 1 276 . 59 ILE C C 173.600 0.05 1 277 . 60 ILE N N 124.500 0.05 1 278 . 60 ILE H H 8.810 0.005 1 279 . 60 ILE CA C 57.100 0.05 1 280 . 60 ILE CB C 40.400 0.05 1 281 . 60 ILE C C 172.600 0.05 1 282 . 61 PHE N N 125.700 0.05 1 283 . 61 PHE H H 8.860 0.005 1 284 . 61 PHE CA C 55.300 0.05 1 285 . 61 PHE CB C 41.300 0.05 1 286 . 61 PHE C C 177.200 0.05 1 287 . 62 TRP N N 119.900 0.05 1 288 . 62 TRP H H 9.280 0.005 1 289 . 62 TRP CA C 55.800 0.05 1 290 . 62 TRP CB C 29.500 0.05 1 291 . 62 TRP C C 174.200 0.05 1 292 . 63 ALA N N 125.600 0.05 1 293 . 63 ALA H H 6.120 0.005 1 294 . 63 ALA CA C 53.000 0.05 1 295 . 63 ALA CB C 18.000 0.05 1 296 . 63 ALA C C 179.000 0.05 1 297 . 64 HIS N N 117.100 0.05 1 298 . 64 HIS H H 8.250 0.005 1 299 . 64 HIS CA C 59.400 0.05 1 300 . 64 HIS CB C 29.700 0.05 1 301 . 64 HIS C C 177.100 0.05 1 302 . 65 ASP N N 117.300 0.05 1 303 . 65 ASP H H 8.000 0.005 1 304 . 65 ASP CA C 55.700 0.05 1 305 . 65 ASP CB C 41.400 0.05 1 306 . 65 ASP C C 177.700 0.05 1 307 . 66 ARG N N 115.400 0.05 1 308 . 66 ARG H H 6.910 0.005 1 309 . 66 ARG CA C 55.400 0.05 1 310 . 66 ARG CB C 33.100 0.05 1 311 . 66 ARG C C 177.900 0.05 1 312 . 67 PHE N N 116.600 0.05 1 313 . 67 PHE H H 7.790 0.005 1 314 . 67 PHE CA C 61.200 0.05 1 315 . 67 PHE CB C 36.700 0.05 1 316 . 67 PHE C C 177.400 0.05 1 317 . 68 GLY N N 109.000 0.05 1 318 . 68 GLY H H 7.300 0.005 1 319 . 68 GLY CA C 46.700 0.05 1 320 . 68 GLY C C 176.200 0.05 1 321 . 69 GLY N N 106.900 0.05 1 322 . 69 GLY H H 8.130 0.005 1 323 . 69 GLY CA C 46.400 0.05 1 324 . 69 GLY C C 176.500 0.05 1 325 . 70 TYR N N 118.800 0.05 1 326 . 70 TYR H H 6.690 0.005 1 327 . 70 TYR CA C 56.600 0.05 1 328 . 70 TYR CB C 35.100 0.05 1 329 . 70 TYR C C 178.100 0.05 1 330 . 71 ALA N N 122.300 0.05 1 331 . 71 ALA H H 8.620 0.005 1 332 . 71 ALA CA C 53.800 0.05 1 333 . 71 ALA CB C 17.800 0.05 1 334 . 71 ALA C C 182.100 0.05 1 335 . 72 GLN N N 122.200 0.05 1 336 . 72 GLN H H 8.890 0.005 1 337 . 72 GLN CA C 58.000 0.05 1 338 . 72 GLN CB C 27.400 0.05 1 339 . 72 GLN C C 177.600 0.05 1 340 . 73 SER N N 111.800 0.05 1 341 . 73 SER H H 7.300 0.005 1 342 . 73 SER CA C 58.700 0.05 1 343 . 73 SER CB C 63.500 0.05 1 344 . 73 SER C C 173.500 0.05 1 345 . 74 GLY N N 109.200 0.05 1 346 . 74 GLY H H 8.110 0.005 1 347 . 74 GLY CA C 45.800 0.05 1 348 . 74 GLY C C 176.000 0.05 1 349 . 75 LEU N N 113.600 0.05 1 350 . 75 LEU H H 7.770 0.005 1 351 . 75 LEU CA C 54.900 0.05 1 352 . 75 LEU CB C 41.900 0.05 1 353 . 75 LEU C C 177.500 0.05 1 354 . 76 LEU N N 116.100 0.05 1 355 . 76 LEU H H 7.630 0.005 1 356 . 76 LEU CA C 52.100 0.05 1 357 . 76 LEU CB C 43.000 0.05 1 358 . 76 LEU C C 176.800 0.05 1 359 . 77 ALA N N 125.900 0.05 1 360 . 77 ALA H H 9.010 0.005 1 361 . 77 ALA CA C 50.400 0.05 1 362 . 77 ALA CB C 18.200 0.05 1 363 . 77 ALA C C 176.400 0.05 1 364 . 78 GLU N N 121.400 0.05 1 365 . 78 GLU H H 8.300 0.005 1 366 . 78 GLU CA C 56.100 0.05 1 367 . 78 GLU CB C 28.700 0.05 1 368 . 78 GLU C C 176.100 0.05 1 369 . 79 ILE N N 124.700 0.05 1 370 . 79 ILE H H 8.160 0.005 1 371 . 79 ILE CA C 58.700 0.05 1 372 . 79 ILE CB C 37.000 0.05 1 373 . 79 ILE C C 175.600 0.05 1 374 . 80 THR N N 114.500 0.05 1 375 . 80 THR H H 8.720 0.005 1 376 . 80 THR CA C 57.000 0.05 1 377 . 80 THR CB C 68.700 0.05 1 378 . 81 PRO CA C 61.600 0.05 1 379 . 81 PRO CB C 31.100 0.05 1 380 . 81 PRO C C 177.400 0.05 1 381 . 82 ASP N N 123.300 0.05 1 382 . 82 ASP H H 9.070 0.005 1 383 . 82 ASP CA C 53.100 0.05 1 384 . 82 ASP CB C 40.900 0.05 1 385 . 83 LYS N N 123.000 0.05 1 386 . 83 LYS H H 8.570 0.005 1 387 . 83 LYS CA C 59.300 0.05 1 388 . 83 LYS CB C 31.100 0.05 1 389 . 83 LYS C C 177.500 0.05 1 390 . 84 ALA N N 119.100 0.05 1 391 . 84 ALA H H 8.210 0.005 1 392 . 84 ALA CA C 54.200 0.05 1 393 . 84 ALA CB C 17.000 0.05 1 394 . 84 ALA C C 180.100 0.05 1 395 . 85 PHE N N 118.300 0.05 1 396 . 85 PHE H H 7.920 0.005 1 397 . 85 PHE CA C 61.700 0.05 1 398 . 85 PHE CB C 38.500 0.05 1 399 . 85 PHE C C 178.200 0.05 1 400 . 86 GLN N N 117.300 0.05 1 401 . 86 GLN H H 8.560 0.005 1 402 . 86 GLN CA C 59.200 0.05 1 403 . 86 GLN CB C 27.700 0.05 1 404 . 86 GLN C C 179.900 0.05 1 405 . 87 ASP N N 116.400 0.05 1 406 . 87 ASP H H 8.070 0.005 1 407 . 87 ASP CA C 55.500 0.05 1 408 . 87 ASP CB C 40.300 0.05 1 409 . 87 ASP C C 176.400 0.05 1 410 . 88 LYS N N 117.100 0.05 1 411 . 88 LYS H H 7.790 0.005 1 412 . 88 LYS CA C 57.700 0.05 1 413 . 88 LYS CB C 31.400 0.05 1 414 . 88 LYS C C 176.700 0.05 1 415 . 89 LEU N N 119.000 0.05 1 416 . 89 LEU H H 7.600 0.005 1 417 . 89 LEU CA C 52.600 0.05 1 418 . 89 LEU CB C 41.600 0.05 1 419 . 89 LEU C C 176.700 0.05 1 420 . 90 TYR N N 116.500 0.05 1 421 . 90 TYR H H 7.700 0.005 1 422 . 90 TYR CA C 58.400 0.05 1 423 . 90 TYR CB C 38.300 0.05 1 424 . 91 PRO CA C 66.200 0.05 1 425 . 91 PRO CB C 30.900 0.05 1 426 . 91 PRO C C 178.800 0.05 1 427 . 92 PHE N N 111.900 0.05 1 428 . 92 PHE H H 7.940 0.005 1 429 . 92 PHE CA C 58.800 0.05 1 430 . 92 PHE CB C 36.200 0.05 1 431 . 92 PHE C C 177.100 0.05 1 432 . 93 THR N N 112.800 0.05 1 433 . 93 THR H H 7.190 0.005 1 434 . 93 THR CA C 64.200 0.05 1 435 . 93 THR CB C 66.600 0.05 1 436 . 93 THR C C 175.900 0.05 1 437 . 94 TRP N N 120.200 0.05 1 438 . 94 TRP H H 6.560 0.005 1 439 . 94 TRP CA C 58.200 0.05 1 440 . 94 TRP CB C 29.000 0.05 1 441 . 94 TRP C C 178.300 0.05 1 442 . 95 ASP N N 114.700 0.05 1 443 . 95 ASP H H 7.460 0.005 1 444 . 95 ASP CA C 56.700 0.05 1 445 . 95 ASP CB C 39.500 0.05 1 446 . 95 ASP C C 178.500 0.05 1 447 . 96 ALA N N 119.300 0.05 1 448 . 96 ALA H H 6.940 0.005 1 449 . 96 ALA CA C 53.600 0.05 1 450 . 96 ALA CB C 16.600 0.05 1 451 . 96 ALA C C 177.300 0.05 1 452 . 97 VAL N N 106.400 0.05 1 453 . 97 VAL H H 7.050 0.005 1 454 . 97 VAL CA C 59.000 0.05 1 455 . 97 VAL CB C 29.700 0.05 1 456 . 97 VAL C C 172.300 0.05 1 457 . 98 ARG N N 121.500 0.05 1 458 . 98 ARG H H 7.020 0.005 1 459 . 98 ARG CA C 54.400 0.05 1 460 . 98 ARG CB C 30.400 0.05 1 461 . 98 ARG C C 176.300 0.05 1 462 . 99 TYR N N 127.400 0.05 1 463 . 99 TYR H H 9.590 0.005 1 464 . 99 TYR CA C 57.500 0.05 1 465 . 99 TYR CB C 41.400 0.05 1 466 . 99 TYR C C 175.500 0.05 1 467 . 100 ASN N N 128.600 0.05 1 468 . 100 ASN H H 8.740 0.005 1 469 . 100 ASN CA C 53.000 0.05 1 470 . 100 ASN CB C 36.300 0.05 1 471 . 100 ASN C C 175.200 0.05 1 472 . 101 GLY N N 102.000 0.05 1 473 . 101 GLY H H 8.590 0.005 1 474 . 101 GLY CA C 44.900 0.05 1 475 . 101 GLY C C 173.800 0.05 1 476 . 102 LYS N N 120.700 0.05 1 477 . 102 LYS H H 7.690 0.005 1 478 . 102 LYS CA C 54.000 0.05 1 479 . 102 LYS CB C 34.400 0.05 1 480 . 102 LYS C C 174.900 0.05 1 481 . 103 LEU N N 122.600 0.05 1 482 . 103 LEU H H 8.910 0.005 1 483 . 103 LEU CA C 54.500 0.05 1 484 . 103 LEU CB C 41.100 0.05 1 485 . 103 LEU C C 178.200 0.05 1 486 . 104 ILE N N 113.200 0.05 1 487 . 104 ILE H H 8.600 0.005 1 488 . 104 ILE CA C 59.500 0.05 1 489 . 104 ILE CB C 37.900 0.05 1 490 . 104 ILE C C 174.700 0.05 1 491 . 105 ALA N N 118.400 0.05 1 492 . 105 ALA H H 7.730 0.005 1 493 . 105 ALA CA C 51.100 0.05 1 494 . 105 ALA CB C 21.300 0.05 1 495 . 105 ALA C C 173.800 0.05 1 496 . 106 TYR N N 113.600 0.05 1 497 . 106 TYR H H 8.880 0.005 1 498 . 106 TYR CA C 55.300 0.05 1 499 . 106 TYR CB C 39.000 0.05 1 500 . 107 PRO CA C 61.400 0.05 1 501 . 107 PRO CB C 31.800 0.05 1 502 . 107 PRO C C 174.400 0.05 1 503 . 108 ILE N N 113.800 0.05 1 504 . 108 ILE H H 8.920 0.005 1 505 . 108 ILE CA C 60.300 0.05 1 506 . 108 ILE CB C 37.000 0.05 1 507 . 108 ILE C C 177.600 0.05 1 508 . 109 ALA N N 116.900 0.05 1 509 . 109 ALA H H 7.490 0.005 1 510 . 109 ALA CA C 51.300 0.05 1 511 . 109 ALA CB C 23.000 0.05 1 512 . 109 ALA C C 173.600 0.05 1 513 . 110 VAL N N 122.300 0.05 1 514 . 110 VAL H H 9.120 0.005 1 515 . 110 VAL CA C 62.300 0.05 1 516 . 110 VAL CB C 31.700 0.05 1 517 . 110 VAL C C 173.600 0.05 1 518 . 111 GLU N N 123.800 0.05 1 519 . 111 GLU H H 9.470 0.005 1 520 . 111 GLU CA C 54.200 0.05 1 521 . 111 GLU CB C 32.500 0.05 1 522 . 111 GLU C C 174.200 0.05 1 523 . 112 ALA N N 115.500 0.05 1 524 . 112 ALA H H 6.120 0.005 1 525 . 112 ALA CA C 49.600 0.05 1 526 . 112 ALA CB C 21.900 0.05 1 527 . 112 ALA C C 176.800 0.05 1 528 . 113 LEU N N 123.100 0.05 1 529 . 113 LEU H H 7.670 0.005 1 530 . 113 LEU CA C 54.200 0.05 1 531 . 113 LEU CB C 43.600 0.05 1 532 . 113 LEU C C 173.700 0.05 1 533 . 114 SER N N 107.700 0.05 1 534 . 114 SER H H 7.410 0.005 1 535 . 114 SER CA C 56.500 0.05 1 536 . 114 SER CB C 66.600 0.05 1 537 . 114 SER C C 171.900 0.05 1 538 . 115 LEU N N 121.700 0.05 1 539 . 115 LEU H H 7.280 0.005 1 540 . 115 LEU CA C 53.600 0.05 1 541 . 115 LEU CB C 43.100 0.05 1 542 . 115 LEU C C 174.100 0.05 1 543 . 116 ILE N N 129.700 0.05 1 544 . 116 ILE H H 8.640 0.005 1 545 . 116 ILE CA C 59.500 0.05 1 546 . 116 ILE CB C 37.700 0.05 1 547 . 116 ILE C C 174.500 0.05 1 548 . 117 TYR N N 121.500 0.05 1 549 . 117 TYR H H 9.000 0.005 1 550 . 117 TYR CA C 54.000 0.05 1 551 . 117 TYR CB C 41.700 0.05 1 552 . 117 TYR C C 172.700 0.05 1 553 . 118 ASN N N 120.900 0.05 1 554 . 118 ASN H H 9.280 0.005 1 555 . 118 ASN CA C 51.600 0.05 1 556 . 118 ASN CB C 37.100 0.05 1 557 . 118 ASN C C 175.500 0.05 1 558 . 119 LYS N N 125.400 0.05 1 559 . 119 LYS H H 8.800 0.005 1 560 . 119 LYS CA C 58.000 0.05 1 561 . 119 LYS CB C 32.000 0.05 1 562 . 119 LYS C C 177.500 0.05 1 563 . 120 ASP N N 115.600 0.05 1 564 . 120 ASP H H 8.180 0.005 1 565 . 120 ASP CA C 55.800 0.05 1 566 . 120 ASP CB C 39.800 0.05 1 567 . 120 ASP C C 177.500 0.05 1 568 . 121 LEU N N 117.700 0.05 1 569 . 121 LEU H H 7.120 0.005 1 570 . 121 LEU CA C 54.900 0.05 1 571 . 121 LEU CB C 43.300 0.05 1 572 . 121 LEU C C 176.500 0.05 1 573 . 122 LEU N N 119.600 0.05 1 574 . 122 LEU H H 8.320 0.005 1 575 . 122 LEU CA C 51.100 0.05 1 576 . 122 LEU CB C 43.300 0.05 1 577 . 123 PRO CA C 64.200 0.05 1 578 . 123 PRO CB C 31.100 0.05 1 579 . 123 PRO C C 177.200 0.05 1 580 . 124 ASN N N 112.500 0.05 1 581 . 124 ASN H H 7.500 0.005 1 582 . 124 ASN CA C 49.100 0.05 1 583 . 124 ASN CB C 39.400 0.05 1 584 . 126 PRO CA C 61.800 0.05 1 585 . 126 PRO CB C 30.500 0.05 1 586 . 126 PRO C C 175.900 0.05 1 587 . 127 LYS N N 118.600 0.05 1 588 . 127 LYS H H 8.140 0.005 1 589 . 127 LYS CA C 56.000 0.05 1 590 . 127 LYS CB C 32.600 0.05 1 591 . 127 LYS C C 177.300 0.05 1 592 . 128 THR N N 108.500 0.05 1 593 . 128 THR H H 7.900 0.005 1 594 . 128 THR CA C 59.500 0.05 1 595 . 128 THR CB C 71.300 0.05 1 596 . 128 THR C C 174.400 0.05 1 597 . 129 TRP N N 123.700 0.05 1 598 . 129 TRP H H 10.170 0.005 1 599 . 129 TRP CA C 60.400 0.05 1 600 . 129 TRP CB C 27.800 0.05 1 601 . 129 TRP C C 179.700 0.05 1 602 . 130 GLU N N 117.800 0.05 1 603 . 130 GLU H H 10.580 0.005 1 604 . 130 GLU CA C 61.200 0.05 1 605 . 130 GLU CB C 27.600 0.05 1 606 . 130 GLU C C 178.400 0.05 1 607 . 131 GLU N N 116.500 0.05 1 608 . 131 GLU H H 7.630 0.005 1 609 . 131 GLU CA C 56.500 0.05 1 610 . 131 GLU CB C 30.600 0.05 1 611 . 131 GLU C C 176.700 0.05 1 612 . 132 ILE N N 121.600 0.05 1 613 . 132 ILE H H 8.230 0.005 1 614 . 132 ILE CA C 66.500 0.05 1 615 . 132 ILE CB C 33.500 0.05 1 616 . 133 PRO CA C 66.500 0.05 1 617 . 133 PRO CB C 29.800 0.05 1 618 . 133 PRO C C 177.500 0.05 1 619 . 134 ALA N N 117.900 0.05 1 620 . 134 ALA H H 7.800 0.005 1 621 . 134 ALA CA C 54.600 0.05 1 622 . 134 ALA CB C 17.300 0.05 1 623 . 134 ALA C C 181.000 0.05 1 624 . 135 LEU N N 119.900 0.05 1 625 . 135 LEU H H 7.620 0.005 1 626 . 135 LEU CA C 56.800 0.05 1 627 . 135 LEU CB C 41.300 0.05 1 628 . 135 LEU C C 179.100 0.05 1 629 . 136 ASP N N 118.300 0.05 1 630 . 136 ASP H H 8.860 0.005 1 631 . 136 ASP CA C 58.400 0.05 1 632 . 136 ASP CB C 41.200 0.05 1 633 . 136 ASP C C 177.200 0.05 1 634 . 137 LYS N N 117.100 0.05 1 635 . 137 LYS H H 8.050 0.005 1 636 . 137 LYS CA C 59.800 0.05 1 637 . 137 LYS CB C 31.400 0.05 1 638 . 137 LYS C C 179.600 0.05 1 639 . 138 GLU N N 118.500 0.05 1 640 . 138 GLU H H 7.490 0.005 1 641 . 138 GLU CA C 58.700 0.05 1 642 . 138 GLU CB C 28.800 0.05 1 643 . 138 GLU C C 179.600 0.05 1 644 . 139 LEU N N 121.100 0.05 1 645 . 139 LEU H H 8.410 0.005 1 646 . 139 LEU CA C 57.400 0.05 1 647 . 139 LEU CB C 39.700 0.05 1 648 . 139 LEU C C 180.400 0.05 1 649 . 140 LYS N N 124.100 0.05 1 650 . 140 LYS H H 9.260 0.005 1 651 . 140 LYS CA C 58.300 0.05 1 652 . 140 LYS CB C 31.300 0.05 1 653 . 140 LYS C C 181.400 0.05 1 654 . 141 ALA N N 121.900 0.05 1 655 . 141 ALA H H 7.270 0.005 1 656 . 141 ALA CA C 53.800 0.05 1 657 . 141 ALA CB C 17.200 0.05 1 658 . 141 ALA C C 178.400 0.05 1 659 . 142 LYS N N 115.600 0.05 1 660 . 142 LYS H H 7.660 0.005 1 661 . 142 LYS CA C 54.400 0.05 1 662 . 142 LYS CB C 31.800 0.05 1 663 . 142 LYS C C 176.500 0.05 1 664 . 143 GLY N N 107.600 0.05 1 665 . 143 GLY H H 7.880 0.005 1 666 . 143 GLY CA C 45.600 0.05 1 667 . 143 GLY C C 174.100 0.05 1 668 . 144 LYS N N 119.900 0.05 1 669 . 144 LYS H H 7.870 0.005 1 670 . 144 LYS CA C 52.800 0.05 1 671 . 144 LYS CB C 34.600 0.05 1 672 . 144 LYS C C 173.600 0.05 1 673 . 145 SER N N 109.300 0.05 1 674 . 145 SER H H 7.680 0.005 1 675 . 145 SER CA C 56.000 0.05 1 676 . 145 SER CB C 66.000 0.05 1 677 . 145 SER C C 174.500 0.05 1 678 . 146 ALA N N 122.700 0.05 1 679 . 146 ALA H H 9.610 0.005 1 680 . 146 ALA CA C 55.100 0.05 1 681 . 146 ALA CB C 17.400 0.05 1 682 . 146 ALA C C 175.800 0.05 1 683 . 147 LEU N N 116.800 0.05 1 684 . 147 LEU H H 8.650 0.005 1 685 . 147 LEU CA C 53.900 0.05 1 686 . 147 LEU CB C 44.900 0.05 1 687 . 147 LEU C C 174.900 0.05 1 688 . 148 MET N N 121.300 0.05 1 689 . 148 MET H H 8.180 0.005 1 690 . 148 MET CA C 55.400 0.05 1 691 . 148 MET CB C 37.500 0.05 1 692 . 148 MET C C 174.000 0.05 1 693 . 149 PHE N N 119.400 0.05 1 694 . 149 PHE H H 8.370 0.005 1 695 . 149 PHE CA C 55.300 0.05 1 696 . 149 PHE CB C 40.500 0.05 1 697 . 149 PHE C C 171.500 0.05 1 698 . 150 ASN N N 115.600 0.05 1 699 . 150 ASN H H 8.650 0.005 1 700 . 150 ASN CA C 52.900 0.05 1 701 . 150 ASN CB C 36.500 0.05 1 702 . 150 ASN C C 172.800 0.05 1 703 . 151 LEU N N 124.000 0.05 1 704 . 151 LEU H H 7.340 0.005 1 705 . 151 LEU CA C 54.200 0.05 1 706 . 151 LEU CB C 41.300 0.05 1 707 . 151 LEU C C 178.000 0.05 1 708 . 152 GLN N N 113.600 0.05 1 709 . 152 GLN H H 8.090 0.005 1 710 . 152 GLN CA C 54.700 0.05 1 711 . 152 GLN CB C 27.600 0.05 1 712 . 152 GLN C C 175.900 0.05 1 713 . 153 GLU N N 114.000 0.05 1 714 . 153 GLU H H 6.410 0.005 1 715 . 153 GLU CA C 50.900 0.05 1 716 . 153 GLU CB C 31.400 0.05 1 717 . 154 PRO CA C 63.200 0.05 1 718 . 154 PRO CB C 31.500 0.05 1 719 . 154 PRO C C 176.300 0.05 1 720 . 155 TYR N N 121.500 0.05 1 721 . 155 TYR H H 8.080 0.005 1 722 . 155 TYR CA C 61.400 0.05 1 723 . 155 TYR CB C 39.300 0.05 1 724 . 155 TYR C C 175.900 0.05 1 725 . 156 PHE N N 109.800 0.05 1 726 . 156 PHE H H 7.780 0.005 1 727 . 156 PHE CA C 59.800 0.05 1 728 . 156 PHE CB C 39.800 0.05 1 729 . 156 PHE C C 175.400 0.05 1 730 . 157 THR N N 107.400 0.05 1 731 . 157 THR H H 7.320 0.005 1 732 . 157 THR CA C 62.500 0.05 1 733 . 157 THR CB C 68.900 0.05 1 734 . 157 THR C C 175.700 0.05 1 735 . 158 TRP N N 123.900 0.05 1 736 . 158 TRP H H 8.580 0.005 1 737 . 158 TRP CA C 60.700 0.05 1 738 . 158 TRP CB C 27.100 0.05 1 739 . 159 PRO CA C 65.300 0.05 1 740 . 159 PRO CB C 29.900 0.05 1 741 . 159 PRO C C 177.900 0.05 1 742 . 160 LEU N N 112.800 0.05 1 743 . 160 LEU H H 6.690 0.005 1 744 . 160 LEU CA C 55.600 0.05 1 745 . 160 LEU CB C 41.400 0.05 1 746 . 160 LEU C C 176.800 0.05 1 747 . 161 ILE N N 120.800 0.05 1 748 . 161 ILE H H 6.910 0.005 1 749 . 161 ILE CA C 64.700 0.05 1 750 . 161 ILE CB C 36.300 0.05 1 751 . 161 ILE C C 175.700 0.05 1 752 . 162 ALA N N 115.600 0.05 1 753 . 162 ALA H H 7.680 0.005 1 754 . 162 ALA CA C 51.600 0.05 1 755 . 162 ALA CB C 18.700 0.05 1 756 . 162 ALA C C 180.200 0.05 1 757 . 163 ALA N N 120.800 0.05 1 758 . 163 ALA H H 6.780 0.005 1 759 . 163 ALA CA C 55.800 0.05 1 760 . 163 ALA CB C 19.000 0.05 1 761 . 163 ALA C C 177.900 0.05 1 762 . 164 ASP N N 114.400 0.05 1 763 . 164 ASP H H 9.510 0.005 1 764 . 164 ASP CA C 52.600 0.05 1 765 . 164 ASP CB C 42.400 0.05 1 766 . 164 ASP C C 176.800 0.05 1 767 . 165 GLY N N 102.400 0.05 1 768 . 165 GLY H H 7.370 0.005 1 769 . 165 GLY CA C 45.000 0.05 1 770 . 165 GLY C C 175.500 0.05 1 771 . 166 GLY N N 107.900 0.05 1 772 . 166 GLY H H 7.100 0.005 1 773 . 166 GLY CA C 45.600 0.05 1 774 . 166 GLY C C 171.800 0.05 1 775 . 167 TYR N N 116.300 0.05 1 776 . 167 TYR H H 8.200 0.005 1 777 . 167 TYR CA C 56.500 0.05 1 778 . 167 TYR CB C 39.000 0.05 1 779 . 167 TYR C C 172.500 0.05 1 780 . 168 ALA N N 122.000 0.05 1 781 . 168 ALA H H 8.720 0.005 1 782 . 168 ALA CA C 52.300 0.05 1 783 . 168 ALA CB C 16.100 0.05 1 784 . 168 ALA C C 172.400 0.05 1 785 . 169 PHE N N 109.200 0.05 1 786 . 169 PHE H H 6.660 0.005 1 787 . 169 PHE CA C 54.500 0.05 1 788 . 169 PHE CB C 41.500 0.05 1 789 . 169 PHE C C 176.600 0.05 1 790 . 170 LYS N N 126.000 0.05 1 791 . 170 LYS H H 8.840 0.005 1 792 . 170 LYS CA C 56.400 0.05 1 793 . 170 LYS CB C 31.900 0.05 1 794 . 170 LYS C C 174.500 0.05 1 795 . 171 TYR N N 129.100 0.05 1 796 . 171 TYR H H 8.500 0.005 1 797 . 171 TYR CA C 55.700 0.05 1 798 . 171 TYR CB C 39.100 0.05 1 799 . 171 TYR C C 174.700 0.05 1 800 . 172 GLU N N 126.700 0.05 1 801 . 172 GLU H H 8.270 0.005 1 802 . 172 GLU CA C 55.200 0.05 1 803 . 172 GLU CB C 31.900 0.05 1 804 . 173 ASN CA C 53.600 0.05 1 805 . 173 ASN CB C 36.700 0.05 1 806 . 173 ASN C C 175.200 0.05 1 807 . 174 GLY N N 101.900 0.05 1 808 . 174 GLY H H 7.480 0.005 1 809 . 174 GLY CA C 45.000 0.05 1 810 . 174 GLY C C 173.100 0.05 1 811 . 175 LYS N N 118.500 0.05 1 812 . 175 LYS H H 7.130 0.005 1 813 . 175 LYS CA C 53.900 0.05 1 814 . 175 LYS CB C 34.600 0.05 1 815 . 175 LYS C C 174.400 0.05 1 816 . 176 TYR N N 119.500 0.05 1 817 . 176 TYR H H 8.590 0.005 1 818 . 176 TYR CA C 58.000 0.05 1 819 . 176 TYR CB C 38.800 0.05 1 820 . 176 TYR C C 175.900 0.05 1 821 . 177 ASP N N 124.100 0.05 1 822 . 177 ASP H H 9.120 0.005 1 823 . 177 ASP CA C 52.300 0.05 1 824 . 177 ASP CB C 40.600 0.05 1 825 . 177 ASP C C 177.200 0.05 1 826 . 178 ILE N N 116.500 0.05 1 827 . 178 ILE H H 7.700 0.005 1 828 . 178 ILE CA C 62.700 0.05 1 829 . 178 ILE CB C 36.000 0.05 1 830 . 178 ILE C C 175.700 0.05 1 831 . 179 LYS N N 116.000 0.05 1 832 . 179 LYS H H 8.270 0.005 1 833 . 179 LYS CA C 54.300 0.05 1 834 . 179 LYS CB C 31.200 0.05 1 835 . 179 LYS C C 176.300 0.05 1 836 . 180 ASP N N 123.400 0.05 1 837 . 180 ASP H H 7.750 0.005 1 838 . 180 ASP CA C 52.700 0.05 1 839 . 180 ASP CB C 40.200 0.05 1 840 . 180 ASP C C 172.800 0.05 1 841 . 181 VAL N N 122.500 0.05 1 842 . 181 VAL H H 7.510 0.005 1 843 . 181 VAL CA C 58.600 0.05 1 844 . 181 VAL CB C 34.000 0.05 1 845 . 181 VAL C C 177.200 0.05 1 846 . 182 GLY N N 120.000 0.05 1 847 . 182 GLY H H 6.920 0.005 1 848 . 182 GLY CA C 45.600 0.05 1 849 . 182 GLY C C 174.800 0.05 1 850 . 183 VAL N N 112.900 0.05 1 851 . 183 VAL H H 6.750 0.005 1 852 . 183 VAL CA C 62.500 0.05 1 853 . 183 VAL CB C 31.500 0.05 1 854 . 183 VAL C C 172.800 0.05 1 855 . 184 ASP N N 114.500 0.05 1 856 . 184 ASP H H 7.780 0.005 1 857 . 184 ASP CA C 50.800 0.05 1 858 . 184 ASP CB C 39.500 0.05 1 859 . 184 ASP C C 176.100 0.05 1 860 . 185 ASN N N 115.800 0.05 1 861 . 185 ASN H H 6.740 0.005 1 862 . 185 ASN CA C 51.000 0.05 1 863 . 185 ASN CB C 38.400 0.05 1 864 . 185 ASN C C 174.600 0.05 1 865 . 186 ALA N N 119.700 0.05 1 866 . 186 ALA H H 8.410 0.005 1 867 . 186 ALA CA C 54.900 0.05 1 868 . 186 ALA CB C 17.600 0.05 1 869 . 186 ALA C C 180.400 0.05 1 870 . 187 GLY N N 108.900 0.05 1 871 . 187 GLY H H 8.310 0.005 1 872 . 187 GLY CA C 46.700 0.05 1 873 . 187 GLY C C 175.900 0.05 1 874 . 188 ALA N N 127.400 0.05 1 875 . 188 ALA H H 8.220 0.005 1 876 . 188 ALA CA C 53.800 0.05 1 877 . 188 ALA CB C 18.000 0.05 1 878 . 188 ALA C C 180.400 0.05 1 879 . 189 LYS N N 114.600 0.05 1 880 . 189 LYS H H 8.040 0.005 1 881 . 189 LYS CA C 59.000 0.05 1 882 . 189 LYS CB C 31.400 0.05 1 883 . 189 LYS C C 180.100 0.05 1 884 . 190 ALA N N 124.400 0.05 1 885 . 190 ALA H H 8.320 0.005 1 886 . 190 ALA CA C 55.200 0.05 1 887 . 190 ALA CB C 17.300 0.05 1 888 . 190 ALA C C 181.100 0.05 1 889 . 191 GLY N N 106.500 0.05 1 890 . 191 GLY H H 8.030 0.005 1 891 . 191 GLY CA C 47.100 0.05 1 892 . 191 GLY C C 174.500 0.05 1 893 . 192 LEU N N 120.700 0.05 1 894 . 192 LEU H H 8.390 0.005 1 895 . 192 LEU CA C 56.600 0.05 1 896 . 192 LEU CB C 39.800 0.05 1 897 . 192 LEU C C 178.200 0.05 1 898 . 193 THR N N 116.200 0.05 1 899 . 193 THR H H 8.640 0.005 1 900 . 193 THR CA C 67.300 0.05 1 901 . 193 THR CB C 68.000 0.05 1 902 . 193 THR C C 175.000 0.05 1 903 . 194 PHE N N 121.800 0.05 1 904 . 194 PHE H H 7.620 0.005 1 905 . 194 PHE CA C 61.800 0.05 1 906 . 194 PHE CB C 38.500 0.05 1 907 . 194 PHE C C 177.300 0.05 1 908 . 195 LEU N N 119.100 0.05 1 909 . 195 LEU H H 7.520 0.005 1 910 . 195 LEU CA C 57.800 0.05 1 911 . 195 LEU CB C 40.600 0.05 1 912 . 195 LEU C C 178.000 0.05 1 913 . 196 VAL N N 117.800 0.05 1 914 . 196 VAL H H 8.520 0.005 1 915 . 196 VAL CA C 66.700 0.05 1 916 . 196 VAL CB C 30.100 0.05 1 917 . 196 VAL C C 178.300 0.05 1 918 . 197 ASP N N 122.600 0.05 1 919 . 197 ASP H H 8.600 0.005 1 920 . 197 ASP CA C 57.400 0.05 1 921 . 197 ASP CB C 39.300 0.05 1 922 . 197 ASP C C 179.200 0.05 1 923 . 198 LEU N N 120.100 0.05 1 924 . 198 LEU H H 7.840 0.005 1 925 . 198 LEU CA C 57.900 0.05 1 926 . 198 LEU CB C 41.300 0.05 1 927 . 198 LEU C C 179.000 0.05 1 928 . 199 ILE N N 120.000 0.05 1 929 . 199 ILE H H 7.500 0.005 1 930 . 199 ILE CA C 62.800 0.05 1 931 . 199 ILE CB C 37.500 0.05 1 932 . 199 ILE C C 181.000 0.05 1 933 . 200 LYS N N 124.300 0.05 1 934 . 200 LYS H H 9.380 0.005 1 935 . 200 LYS CA C 59.300 0.05 1 936 . 200 LYS CB C 31.500 0.05 1 937 . 200 LYS C C 178.600 0.05 1 938 . 201 ASN N N 113.800 0.05 1 939 . 201 ASN H H 7.930 0.005 1 940 . 201 ASN CA C 53.000 0.05 1 941 . 201 ASN CB C 38.200 0.05 1 942 . 201 ASN C C 173.000 0.05 1 943 . 202 LYS N N 111.300 0.05 1 944 . 202 LYS H H 7.950 0.005 1 945 . 202 LYS CA C 56.900 0.05 1 946 . 202 LYS CB C 26.700 0.05 1 947 . 202 LYS C C 175.600 0.05 1 948 . 203 HIS N N 115.800 0.05 1 949 . 203 HIS H H 8.420 0.005 1 950 . 203 HIS CA C 56.500 0.05 1 951 . 203 HIS CB C 28.000 0.05 1 952 . 203 HIS C C 175.300 0.05 1 953 . 204 MET N N 114.200 0.05 1 954 . 204 MET H H 7.460 0.005 1 955 . 204 MET CA C 54.200 0.05 1 956 . 204 MET CB C 36.800 0.05 1 957 . 204 MET C C 172.900 0.05 1 958 . 205 ASN N N 118.500 0.05 1 959 . 205 ASN H H 8.680 0.005 1 960 . 205 ASN CA C 51.600 0.05 1 961 . 205 ASN CB C 39.700 0.05 1 962 . 205 ASN C C 175.900 0.05 1 963 . 206 ALA N N 124.900 0.05 1 964 . 206 ALA H H 9.070 0.005 1 965 . 206 ALA CA C 54.100 0.05 1 966 . 206 ALA CB C 17.700 0.05 1 967 . 206 ALA C C 176.200 0.05 1 968 . 207 ASP N N 112.600 0.05 1 969 . 207 ASP H H 8.170 0.005 1 970 . 207 ASP CA C 53.200 0.05 1 971 . 207 ASP CB C 39.300 0.05 1 972 . 207 ASP C C 176.300 0.05 1 973 . 208 THR N N 116.400 0.05 1 974 . 208 THR H H 7.310 0.005 1 975 . 208 THR CA C 66.100 0.05 1 976 . 208 THR CB C 68.500 0.05 1 977 . 208 THR C C 173.200 0.05 1 978 . 209 ASP N N 130.500 0.05 1 979 . 209 ASP H H 6.990 0.005 1 980 . 209 ASP CA C 51.200 0.05 1 981 . 209 ASP CB C 41.500 0.05 1 982 . 209 ASP C C 175.600 0.05 1 983 . 210 TYR N N 117.400 0.05 1 984 . 210 TYR H H 7.870 0.005 1 985 . 210 TYR CA C 62.700 0.05 1 986 . 210 TYR CB C 38.600 0.05 1 987 . 210 TYR C C 178.200 0.05 1 988 . 211 SER N N 114.400 0.05 1 989 . 211 SER H H 8.220 0.005 1 990 . 211 SER CA C 61.200 0.05 1 991 . 211 SER CB C 62.200 0.05 1 992 . 211 SER C C 177.400 0.05 1 993 . 212 ILE N N 124.200 0.05 1 994 . 212 ILE H H 8.950 0.005 1 995 . 212 ILE CA C 64.300 0.05 1 996 . 212 ILE CB C 37.900 0.05 1 997 . 212 ILE C C 178.700 0.05 1 998 . 213 ALA N N 120.500 0.05 1 999 . 213 ALA H H 7.620 0.005 1 1000 . 213 ALA CA C 54.800 0.05 1 1001 . 213 ALA CB C 16.400 0.05 1 1002 . 213 ALA C C 177.700 0.05 1 1003 . 214 GLU N N 117.100 0.05 1 1004 . 214 GLU H H 7.910 0.005 1 1005 . 214 GLU CA C 58.400 0.05 1 1006 . 214 GLU CB C 29.300 0.05 1 1007 . 214 GLU C C 178.000 0.05 1 1008 . 215 ALA N N 119.500 0.05 1 1009 . 215 ALA H H 8.030 0.005 1 1010 . 215 ALA CA C 54.200 0.05 1 1011 . 215 ALA CB C 17.200 0.05 1 1012 . 215 ALA C C 179.600 0.05 1 1013 . 216 ALA N N 117.600 0.05 1 1014 . 216 ALA H H 7.820 0.005 1 1015 . 216 ALA CA C 54.400 0.05 1 1016 . 216 ALA CB C 19.100 0.05 1 1017 . 216 ALA C C 180.500 0.05 1 1018 . 217 PHE N N 119.400 0.05 1 1019 . 217 PHE H H 8.310 0.005 1 1020 . 217 PHE CA C 62.300 0.05 1 1021 . 217 PHE CB C 37.500 0.05 1 1022 . 217 PHE C C 178.900 0.05 1 1023 . 218 ASN N N 119.700 0.05 1 1024 . 218 ASN H H 8.550 0.005 1 1025 . 218 ASN CA C 55.000 0.05 1 1026 . 218 ASN CB C 35.800 0.05 1 1027 . 218 ASN C C 176.600 0.05 1 1028 . 219 LYS N N 116.600 0.05 1 1029 . 219 LYS H H 7.740 0.005 1 1030 . 219 LYS CA C 55.500 0.05 1 1031 . 219 LYS CB C 32.200 0.05 1 1032 . 219 LYS C C 177.500 0.05 1 1033 . 220 GLY N N 108.600 0.05 1 1034 . 220 GLY H H 7.730 0.005 1 1035 . 220 GLY CA C 45.500 0.05 1 1036 . 220 GLY C C 174.900 0.05 1 1037 . 221 GLU N N 116.300 0.05 1 1038 . 221 GLU H H 8.360 0.005 1 1039 . 221 GLU CA C 56.800 0.05 1 1040 . 221 GLU CB C 29.800 0.05 1 1041 . 221 GLU C C 175.600 0.05 1 1042 . 222 THR N N 110.500 0.05 1 1043 . 222 THR H H 6.850 0.005 1 1044 . 222 THR CA C 57.500 0.05 1 1045 . 222 THR CB C 70.000 0.05 1 1046 . 222 THR C C 172.600 0.05 1 1047 . 223 ALA N N 126.900 0.05 1 1048 . 223 ALA H H 8.650 0.005 1 1049 . 223 ALA CA C 54.000 0.05 1 1050 . 223 ALA CB C 19.800 0.05 1 1051 . 223 ALA C C 176.300 0.05 1 1052 . 224 MET N N 114.400 0.05 1 1053 . 224 MET H H 8.070 0.005 1 1054 . 224 MET CA C 54.100 0.05 1 1055 . 224 MET CB C 39.600 0.05 1 1056 . 224 MET C C 173.700 0.05 1 1057 . 225 THR N N 113.000 0.05 1 1058 . 225 THR H H 9.100 0.005 1 1059 . 225 THR CA C 59.100 0.05 1 1060 . 225 THR CB C 70.300 0.05 1 1061 . 225 THR C C 171.100 0.05 1 1062 . 226 ILE N N 122.600 0.05 1 1063 . 226 ILE H H 7.080 0.005 1 1064 . 226 ILE CA C 59.900 0.05 1 1065 . 226 ILE CB C 40.200 0.05 1 1066 . 226 ILE C C 174.400 0.05 1 1067 . 227 ASN N N 121.400 0.05 1 1068 . 227 ASN H H 8.300 0.005 1 1069 . 227 ASN CA C 51.400 0.05 1 1070 . 227 ASN CB C 42.200 0.05 1 1071 . 227 ASN C C 175.300 0.05 1 1072 . 228 GLY N N 110.500 0.05 1 1073 . 228 GLY H H 8.820 0.005 1 1074 . 228 GLY CA C 41.600 0.05 1 1075 . 229 PRO CA C 62.100 0.05 1 1076 . 229 PRO CB C 29.500 0.05 1 1077 . 229 PRO C C 174.700 0.05 1 1078 . 230 TRP N N 110.200 0.05 1 1079 . 230 TRP H H 5.810 0.005 1 1080 . 230 TRP CA C 58.900 0.05 1 1081 . 230 TRP CB C 25.100 0.05 1 1082 . 230 TRP C C 177.000 0.05 1 1083 . 231 ALA N N 123.600 0.05 1 1084 . 231 ALA H H 6.470 0.005 1 1085 . 231 ALA CA C 51.900 0.05 1 1086 . 231 ALA CB C 17.800 0.05 1 1087 . 231 ALA C C 180.200 0.05 1 1088 . 232 TRP N N 116.700 0.05 1 1089 . 232 TRP H H 7.680 0.005 1 1090 . 232 TRP CA C 57.800 0.05 1 1091 . 232 TRP CB C 28.700 0.05 1 1092 . 232 TRP C C 177.800 0.05 1 1093 . 233 SER N N 108.800 0.05 1 1094 . 233 SER H H 6.870 0.005 1 1095 . 233 SER CA C 60.800 0.05 1 1096 . 233 SER CB C 61.900 0.05 1 1097 . 237 THR CA C 64.900 0.05 1 1098 . 237 THR CB C 68.300 0.05 1 1099 . 237 THR C C 175.700 0.05 1 1100 . 238 SER N N 118.000 0.05 1 1101 . 238 SER H H 7.680 0.005 1 1102 . 238 SER CA C 60.200 0.05 1 1103 . 238 SER CB C 63.400 0.05 1 1104 . 239 LYS CA C 57.000 0.05 1 1105 . 239 LYS CB C 27.900 0.05 1 1106 . 239 LYS C C 176.000 0.05 1 1107 . 240 VAL N N 120.100 0.05 1 1108 . 240 VAL H H 7.260 0.005 1 1109 . 240 VAL CA C 62.700 0.05 1 1110 . 240 VAL CB C 32.000 0.05 1 1111 . 241 ASN CA C 51.500 0.05 1 1112 . 241 ASN CB C 36.800 0.05 1 1113 . 241 ASN C C 173.200 0.05 1 1114 . 242 TYR N N 121.400 0.05 1 1115 . 242 TYR H H 7.870 0.005 1 1116 . 242 TYR CA C 54.100 0.05 1 1117 . 242 TYR CB C 41.000 0.05 1 1118 . 242 TYR C C 174.200 0.05 1 1119 . 243 GLY N N 106.800 0.05 1 1120 . 243 GLY H H 8.400 0.005 1 1121 . 243 GLY CA C 42.500 0.05 1 1122 . 243 GLY C C 170.800 0.05 1 1123 . 244 VAL N N 120.600 0.05 1 1124 . 244 VAL H H 8.000 0.005 1 1125 . 244 VAL CA C 61.000 0.05 1 1126 . 244 VAL CB C 33.100 0.05 1 1127 . 244 VAL C C 175.000 0.05 1 1128 . 245 THR N N 120.300 0.05 1 1129 . 245 THR H H 9.570 0.005 1 1130 . 245 THR CA C 58.400 0.05 1 1131 . 245 THR CB C 70.700 0.05 1 1132 . 245 THR C C 173.900 0.05 1 1133 . 246 VAL N N 123.700 0.05 1 1134 . 246 VAL H H 8.190 0.005 1 1135 . 246 VAL CA C 61.300 0.05 1 1136 . 246 VAL CB C 31.500 0.05 1 1137 . 246 VAL C C 174.800 0.05 1 1138 . 247 LEU N N 125.100 0.05 1 1139 . 247 LEU H H 8.600 0.005 1 1140 . 247 LEU CA C 53.800 0.05 1 1141 . 247 LEU CB C 39.700 0.05 1 1142 . 248 PRO CA C 61.400 0.05 1 1143 . 248 PRO CB C 29.700 0.05 1 1144 . 248 PRO C C 175.400 0.05 1 1145 . 249 THR N N 111.600 0.05 1 1146 . 249 THR H H 8.870 0.005 1 1147 . 249 THR CA C 60.400 0.05 1 1148 . 249 THR CB C 70.700 0.05 1 1149 . 249 THR C C 174.300 0.05 1 1150 . 250 PHE N N 121.700 0.05 1 1151 . 250 PHE H H 9.580 0.005 1 1152 . 250 PHE CA C 56.100 0.05 1 1153 . 250 PHE CB C 41.300 0.05 1 1154 . 250 PHE C C 174.500 0.05 1 1155 . 251 LYS N N 129.600 0.05 1 1156 . 251 LYS H H 10.600 0.005 1 1157 . 251 LYS CA C 56.700 0.05 1 1158 . 251 LYS CB C 27.600 0.05 1 1159 . 251 LYS C C 177.500 0.05 1 1160 . 252 GLY N N 103.400 0.05 1 1161 . 252 GLY H H 9.060 0.005 1 1162 . 252 GLY CA C 44.500 0.05 1 1163 . 252 GLY C C 173.800 0.05 1 1164 . 253 GLN N N 122.000 0.05 1 1165 . 253 GLN H H 8.210 0.005 1 1166 . 253 GLN CA C 51.800 0.05 1 1167 . 253 GLN CB C 29.200 0.05 1 1168 . 254 PRO CA C 62.700 0.05 1 1169 . 254 PRO CB C 30.700 0.05 1 1170 . 254 PRO C C 178.300 0.05 1 1171 . 255 SER N N 117.700 0.05 1 1172 . 255 SER H H 8.050 0.005 1 1173 . 255 SER CA C 61.500 0.05 1 1174 . 255 SER CB C 63.900 0.05 1 1175 . 255 SER C C 174.100 0.05 1 1176 . 256 LYS N N 122.700 0.05 1 1177 . 256 LYS H H 7.420 0.005 1 1178 . 256 LYS CA C 52.800 0.05 1 1179 . 256 LYS CB C 33.100 0.05 1 1180 . 257 PRO CA C 62.500 0.05 1 1181 . 257 PRO CB C 30.500 0.05 1 1182 . 257 PRO C C 176.000 0.05 1 1183 . 258 PHE N N 122.300 0.05 1 1184 . 258 PHE H H 8.610 0.005 1 1185 . 258 PHE CA C 54.900 0.05 1 1186 . 258 PHE CB C 38.600 0.05 1 1187 . 258 PHE C C 176.900 0.05 1 1188 . 259 VAL N N 126.700 0.05 1 1189 . 259 VAL H H 9.330 0.005 1 1190 . 259 VAL CA C 62.200 0.05 1 1191 . 259 VAL CB C 32.200 0.05 1 1192 . 259 VAL C C 176.200 0.05 1 1193 . 260 GLY N N 116.500 0.05 1 1194 . 260 GLY H H 8.580 0.005 1 1195 . 260 GLY CA C 44.200 0.05 1 1196 . 260 GLY C C 170.900 0.05 1 1197 . 261 VAL N N 126.700 0.05 1 1198 . 261 VAL H H 10.980 0.005 1 1199 . 261 VAL CA C 59.800 0.05 1 1200 . 261 VAL CB C 30.900 0.05 1 1201 . 261 VAL C C 179.600 0.05 1 1202 . 262 LEU N N 133.200 0.05 1 1203 . 262 LEU H H 9.020 0.005 1 1204 . 262 LEU CA C 56.800 0.05 1 1205 . 262 LEU CB C 39.400 0.05 1 1206 . 262 LEU C C 175.000 0.05 1 1207 . 263 SER N N 125.900 0.05 1 1208 . 263 SER H H 8.960 0.005 1 1209 . 263 SER CA C 58.300 0.05 1 1210 . 263 SER CB C 65.400 0.05 1 1211 . 263 SER C C 170.400 0.05 1 1212 . 264 ALA N N 122.900 0.05 1 1213 . 264 ALA H H 8.930 0.005 1 1214 . 264 ALA CA C 49.200 0.05 1 1215 . 264 ALA CB C 20.600 0.05 1 1216 . 264 ALA C C 176.200 0.05 1 1217 . 265 GLY N N 109.600 0.05 1 1218 . 265 GLY H H 9.370 0.005 1 1219 . 265 GLY CA C 42.300 0.05 1 1220 . 265 GLY C C 171.200 0.05 1 1221 . 266 ILE N N 122.500 0.05 1 1222 . 266 ILE H H 10.050 0.005 1 1223 . 266 ILE CA C 59.400 0.05 1 1224 . 266 ILE CB C 39.100 0.05 1 1225 . 266 ILE C C 175.000 0.05 1 1226 . 267 ASN N N 125.500 0.05 1 1227 . 267 ASN H H 8.200 0.005 1 1228 . 267 ASN CA C 52.900 0.05 1 1229 . 267 ASN CB C 38.200 0.05 1 1230 . 267 ASN C C 177.000 0.05 1 1231 . 268 ALA N N 130.800 0.05 1 1232 . 268 ALA H H 8.930 0.005 1 1233 . 268 ALA CA C 54.600 0.05 1 1234 . 268 ALA CB C 17.300 0.05 1 1235 . 268 ALA C C 178.200 0.05 1 1236 . 269 ALA N N 117.900 0.05 1 1237 . 269 ALA H H 8.190 0.005 1 1238 . 269 ALA CA C 50.700 0.05 1 1239 . 269 ALA CB C 17.900 0.05 1 1240 . 269 ALA C C 177.900 0.05 1 1241 . 270 SER N N 113.500 0.05 1 1242 . 270 SER H H 7.520 0.005 1 1243 . 270 SER CA C 55.600 0.05 1 1244 . 270 SER CB C 63.800 0.05 1 1245 . 271 PRO CA C 63.000 0.05 1 1246 . 271 PRO CB C 30.600 0.05 1 1247 . 271 PRO C C 175.800 0.05 1 1248 . 272 ASN N N 119.300 0.05 1 1249 . 272 ASN H H 8.790 0.005 1 1250 . 272 ASN CA C 52.100 0.05 1 1251 . 272 ASN CB C 39.900 0.05 1 1252 . 272 ASN C C 176.100 0.05 1 1253 . 273 LYS N N 119.100 0.05 1 1254 . 273 LYS H H 7.820 0.005 1 1255 . 273 LYS CA C 61.100 0.05 1 1256 . 273 LYS CB C 31.200 0.05 1 1257 . 273 LYS C C 178.700 0.05 1 1258 . 274 GLU N N 118.100 0.05 1 1259 . 274 GLU H H 8.810 0.005 1 1260 . 274 GLU CA C 59.400 0.05 1 1261 . 274 GLU CB C 27.400 0.05 1 1262 . 274 GLU C C 179.600 0.05 1 1263 . 275 LEU N N 120.500 0.05 1 1264 . 275 LEU H H 7.450 0.005 1 1265 . 275 LEU CA C 56.800 0.05 1 1266 . 275 LEU CB C 41.500 0.05 1 1267 . 275 LEU C C 178.200 0.05 1 1268 . 276 ALA N N 120.200 0.05 1 1269 . 276 ALA H H 8.320 0.005 1 1270 . 276 ALA CA C 54.800 0.05 1 1271 . 276 ALA CB C 17.200 0.05 1 1272 . 276 ALA C C 178.400 0.05 1 1273 . 277 LYS N N 118.100 0.05 1 1274 . 277 LYS H H 7.810 0.005 1 1275 . 277 LYS CA C 59.600 0.05 1 1276 . 277 LYS CB C 31.800 0.05 1 1277 . 277 LYS C C 177.100 0.05 1 1278 . 278 GLU N N 118.700 0.05 1 1279 . 278 GLU H H 7.620 0.005 1 1280 . 278 GLU CA C 59.000 0.05 1 1281 . 278 GLU CB C 28.600 0.05 1 1282 . 278 GLU C C 179.100 0.05 1 1283 . 279 PHE N N 118.300 0.05 1 1284 . 279 PHE H H 8.420 0.005 1 1285 . 279 PHE CA C 61.000 0.05 1 1286 . 279 PHE CB C 37.800 0.05 1 1287 . 279 PHE C C 177.300 0.05 1 1288 . 280 LEU N N 119.800 0.05 1 1289 . 280 LEU H H 8.310 0.005 1 1290 . 280 LEU CA C 57.700 0.05 1 1291 . 280 LEU CB C 40.100 0.05 1 1292 . 280 LEU C C 176.900 0.05 1 1293 . 281 GLU N N 112.700 0.05 1 1294 . 281 GLU H H 8.380 0.005 1 1295 . 281 GLU CA C 58.900 0.05 1 1296 . 281 GLU CB C 28.900 0.05 1 1297 . 281 GLU C C 176.800 0.05 1 1298 . 282 ASN N N 108.800 0.05 1 1299 . 282 ASN H H 7.760 0.005 1 1300 . 282 ASN CA C 52.500 0.05 1 1301 . 282 ASN CB C 38.400 0.05 1 1302 . 282 ASN C C 175.000 0.05 1 1303 . 283 TYR N N 116.200 0.05 1 1304 . 283 TYR H H 7.170 0.005 1 1305 . 283 TYR CA C 59.300 0.05 1 1306 . 283 TYR CB C 37.400 0.05 1 1307 . 283 TYR C C 176.100 0.05 1 1308 . 284 LEU N N 120.900 0.05 1 1309 . 284 LEU H H 8.090 0.005 1 1310 . 284 LEU CA C 57.800 0.05 1 1311 . 284 LEU CB C 40.300 0.05 1 1312 . 284 LEU C C 176.700 0.05 1 1313 . 285 LEU N N 118.800 0.05 1 1314 . 285 LEU H H 7.760 0.005 1 1315 . 285 LEU CA C 54.000 0.05 1 1316 . 285 LEU CB C 37.800 0.05 1 1317 . 285 LEU C C 174.700 0.05 1 1318 . 286 THR N N 108.300 0.05 1 1319 . 286 THR H H 8.530 0.005 1 1320 . 286 THR CA C 58.400 0.05 1 1321 . 286 THR CB C 72.900 0.05 1 1322 . 286 THR C C 174.200 0.05 1 1323 . 287 ASP N N 121.700 0.05 1 1324 . 287 ASP H H 8.500 0.005 1 1325 . 287 ASP CA C 57.900 0.05 1 1326 . 287 ASP CB C 39.100 0.05 1 1327 . 287 ASP C C 177.700 0.05 1 1328 . 288 GLU N N 115.300 0.05 1 1329 . 288 GLU H H 8.450 0.005 1 1330 . 288 GLU CA C 58.600 0.05 1 1331 . 288 GLU CB C 28.600 0.05 1 1332 . 288 GLU C C 179.900 0.05 1 1333 . 289 GLY N N 112.900 0.05 1 1334 . 289 GLY H H 8.320 0.005 1 1335 . 289 GLY CA C 46.300 0.05 1 1336 . 289 GLY C C 175.000 0.05 1 1337 . 290 LEU N N 119.200 0.05 1 1338 . 290 LEU H H 8.240 0.005 1 1339 . 290 LEU CA C 56.800 0.05 1 1340 . 290 LEU CB C 40.600 0.05 1 1341 . 290 LEU C C 179.600 0.05 1 1342 . 291 GLU N N 120.000 0.05 1 1343 . 291 GLU H H 7.730 0.005 1 1344 . 291 GLU CA C 58.900 0.05 1 1345 . 291 GLU CB C 28.500 0.05 1 1346 . 291 GLU C C 177.800 0.05 1 1347 . 292 ALA N N 119.400 0.05 1 1348 . 292 ALA H H 7.190 0.005 1 1349 . 292 ALA CA C 54.600 0.05 1 1350 . 292 ALA CB C 17.100 0.05 1 1351 . 292 ALA C C 180.300 0.05 1 1352 . 293 VAL N N 116.000 0.05 1 1353 . 293 VAL H H 7.180 0.005 1 1354 . 293 VAL CA C 66.900 0.05 1 1355 . 293 VAL CB C 31.000 0.05 1 1356 . 293 VAL C C 177.000 0.05 1 1357 . 294 ASN N N 118.000 0.05 1 1358 . 294 ASN H H 8.830 0.005 1 1359 . 294 ASN CA C 55.600 0.05 1 1360 . 294 ASN CB C 40.500 0.05 1 1361 . 294 ASN C C 176.500 0.05 1 1362 . 295 LYS N N 114.500 0.05 1 1363 . 295 LYS H H 8.140 0.005 1 1364 . 295 LYS CA C 57.600 0.05 1 1365 . 295 LYS CB C 31.600 0.05 1 1366 . 295 LYS C C 176.900 0.05 1 1367 . 296 ASP N N 118.900 0.05 1 1368 . 296 ASP H H 7.420 0.005 1 1369 . 296 ASP CA C 55.200 0.05 1 1370 . 296 ASP CB C 41.300 0.05 1 1371 . 296 ASP C C 175.900 0.05 1 1372 . 297 LYS N N 114.600 0.05 1 1373 . 297 LYS H H 7.460 0.005 1 1374 . 297 LYS CA C 51.700 0.05 1 1375 . 297 LYS CB C 34.400 0.05 1 1376 . 298 PRO CA C 62.800 0.05 1 1377 . 298 PRO CB C 30.700 0.05 1 1378 . 298 PRO C C 177.200 0.05 1 1379 . 299 LEU N N 120.900 0.05 1 1380 . 299 LEU H H 8.300 0.005 1 1381 . 299 LEU CA C 55.000 0.05 1 1382 . 299 LEU CB C 44.100 0.05 1 1383 . 299 LEU C C 177.500 0.05 1 1384 . 300 GLY N N 101.300 0.05 1 1385 . 300 GLY H H 8.080 0.005 1 1386 . 300 GLY CA C 43.200 0.05 1 1387 . 300 GLY C C 173.500 0.05 1 1388 . 301 ALA N N 124.800 0.05 1 1389 . 301 ALA H H 7.890 0.005 1 1390 . 301 ALA CA C 50.500 0.05 1 1391 . 301 ALA CB C 18.700 0.05 1 1392 . 301 ALA C C 177.800 0.05 1 1393 . 302 VAL N N 117.600 0.05 1 1394 . 302 VAL H H 7.670 0.005 1 1395 . 302 VAL CA C 61.000 0.05 1 1396 . 302 VAL CB C 33.100 0.05 1 1397 . 302 VAL C C 174.800 0.05 1 1398 . 303 ALA N N 119.800 0.05 1 1399 . 303 ALA H H 8.280 0.005 1 1400 . 303 ALA CA C 52.900 0.05 1 1401 . 303 ALA CB C 18.500 0.05 1 1402 . 303 ALA C C 175.400 0.05 1 1403 . 304 LEU N N 113.900 0.05 1 1404 . 304 LEU H H 6.230 0.005 1 1405 . 304 LEU CA C 53.600 0.05 1 1406 . 304 LEU CB C 43.500 0.05 1 1407 . 304 LEU C C 175.300 0.05 1 1408 . 305 LYS N N 129.300 0.05 1 1409 . 305 LYS H H 8.010 0.005 1 1410 . 305 LYS CA C 59.700 0.05 1 1411 . 305 LYS CB C 31.200 0.05 1 1412 . 305 LYS C C 178.300 0.05 1 1413 . 306 SER N N 111.700 0.05 1 1414 . 306 SER H H 8.580 0.005 1 1415 . 306 SER CA C 60.800 0.05 1 1416 . 306 SER CB C 60.100 0.05 1 1417 . 306 SER C C 176.600 0.05 1 1418 . 307 TYR N N 122.200 0.05 1 1419 . 307 TYR H H 6.700 0.005 1 1420 . 307 TYR CA C 57.300 0.05 1 1421 . 307 TYR CB C 38.100 0.05 1 1422 . 307 TYR C C 177.300 0.05 1 1423 . 308 GLU N N 121.100 0.05 1 1424 . 308 GLU H H 8.390 0.005 1 1425 . 308 GLU CA C 57.200 0.05 1 1426 . 308 GLU CB C 25.800 0.05 1 1427 . 308 GLU C C 177.900 0.05 1 1428 . 309 GLU N N 115.800 0.05 1 1429 . 309 GLU H H 7.840 0.005 1 1430 . 309 GLU CA C 58.700 0.05 1 1431 . 309 GLU CB C 28.500 0.05 1 1432 . 309 GLU C C 178.700 0.05 1 1433 . 310 GLU N N 116.300 0.05 1 1434 . 310 GLU H H 7.170 0.005 1 1435 . 310 GLU CA C 57.200 0.05 1 1436 . 310 GLU CB C 28.600 0.05 1 1437 . 310 GLU C C 179.200 0.05 1 1438 . 311 LEU N N 120.800 0.05 1 1439 . 311 LEU H H 7.730 0.005 1 1440 . 311 LEU CA C 56.700 0.05 1 1441 . 311 LEU CB C 40.500 0.05 1 1442 . 311 LEU C C 178.500 0.05 1 1443 . 312 ALA N N 117.200 0.05 1 1444 . 312 ALA H H 8.360 0.005 1 1445 . 312 ALA CA C 53.600 0.05 1 1446 . 312 ALA CB C 17.300 0.05 1 1447 . 312 ALA C C 177.700 0.05 1 1448 . 313 LYS N N 114.100 0.05 1 1449 . 313 LYS H H 7.100 0.005 1 1450 . 313 LYS CA C 56.600 0.05 1 1451 . 313 LYS CB C 31.500 0.05 1 1452 . 313 LYS C C 176.800 0.05 1 1453 . 314 ASP N N 123.200 0.05 1 1454 . 314 ASP H H 8.180 0.005 1 1455 . 314 ASP CA C 50.500 0.05 1 1456 . 314 ASP CB C 41.500 0.05 1 1457 . 315 PRO CA C 64.100 0.05 1 1458 . 315 PRO CB C 31.400 0.05 1 1459 . 315 PRO C C 179.300 0.05 1 1460 . 316 ARG N N 118.100 0.05 1 1461 . 316 ARG H H 8.810 0.005 1 1462 . 316 ARG CA C 58.100 0.05 1 1463 . 316 ARG CB C 28.100 0.05 1 1464 . 316 ARG C C 180.300 0.05 1 1465 . 317 ILE N N 123.800 0.05 1 1466 . 317 ILE H H 7.620 0.005 1 1467 . 317 ILE CA C 61.900 0.05 1 1468 . 317 ILE CB C 34.200 0.05 1 1469 . 317 ILE C C 178.000 0.05 1 1470 . 318 ALA N N 124.500 0.05 1 1471 . 318 ALA H H 7.960 0.005 1 1472 . 318 ALA CA C 55.300 0.05 1 1473 . 318 ALA CB C 16.600 0.05 1 1474 . 318 ALA C C 181.100 0.05 1 1475 . 319 ALA N N 119.700 0.05 1 1476 . 319 ALA H H 7.950 0.005 1 1477 . 319 ALA CA C 54.700 0.05 1 1478 . 319 ALA CB C 17.600 0.05 1 1479 . 319 ALA C C 179.000 0.05 1 1480 . 320 THR N N 115.100 0.05 1 1481 . 320 THR H H 7.490 0.005 1 1482 . 320 THR CA C 67.300 0.05 1 1483 . 320 THR CB C 68.300 0.05 1 1484 . 320 THR C C 175.700 0.05 1 1485 . 321 MET N N 118.200 0.05 1 1486 . 321 MET H H 8.360 0.005 1 1487 . 321 MET CA C 55.800 0.05 1 1488 . 321 MET CB C 29.600 0.05 1 1489 . 321 MET C C 178.500 0.05 1 1490 . 322 GLU N N 123.300 0.05 1 1491 . 322 GLU H H 8.230 0.005 1 1492 . 322 GLU CA C 59.300 0.05 1 1493 . 322 GLU CB C 28.300 0.05 1 1494 . 322 GLU C C 179.300 0.05 1 1495 . 323 ASN N N 115.700 0.05 1 1496 . 323 ASN H H 8.070 0.005 1 1497 . 323 ASN CA C 56.900 0.05 1 1498 . 323 ASN CB C 39.300 0.05 1 1499 . 323 ASN C C 177.200 0.05 1 1500 . 324 ALA N N 120.000 0.05 1 1501 . 324 ALA H H 8.460 0.005 1 1502 . 324 ALA CA C 54.100 0.05 1 1503 . 324 ALA CB C 16.700 0.05 1 1504 . 324 ALA C C 179.900 0.05 1 1505 . 325 GLN N N 115.900 0.05 1 1506 . 325 GLN H H 8.100 0.005 1 1507 . 325 GLN CA C 57.300 0.05 1 1508 . 325 GLN CB C 27.600 0.05 1 1509 . 325 GLN C C 177.900 0.05 1 1510 . 326 LYS N N 117.100 0.05 1 1511 . 326 LYS H H 7.280 0.005 1 1512 . 326 LYS CA C 56.200 0.05 1 1513 . 326 LYS CB C 32.200 0.05 1 1514 . 326 LYS C C 176.500 0.05 1 1515 . 327 GLY N N 106.400 0.05 1 1516 . 327 GLY H H 7.350 0.005 1 1517 . 327 GLY CA C 43.200 0.05 1 1518 . 327 GLY C C 171.700 0.05 1 1519 . 328 GLU N N 117.900 0.05 1 1520 . 328 GLU H H 8.160 0.005 1 1521 . 328 GLU CA C 54.000 0.05 1 1522 . 328 GLU CB C 32.900 0.05 1 1523 . 328 GLU C C 176.200 0.05 1 1524 . 329 ILE N N 127.300 0.05 1 1525 . 329 ILE H H 9.050 0.005 1 1526 . 329 ILE CA C 60.800 0.05 1 1527 . 329 ILE CB C 36.600 0.05 1 1528 . 329 ILE C C 177.000 0.05 1 1529 . 330 MET N N 124.100 0.05 1 1530 . 330 MET H H 8.500 0.005 1 1531 . 330 MET CA C 56.100 0.05 1 1532 . 330 MET CB C 31.900 0.05 1 1533 . 331 PRO CA C 62.400 0.05 1 1534 . 331 PRO CB C 31.300 0.05 1 1535 . 331 PRO C C 175.100 0.05 1 1536 . 332 ASN N N 114.300 0.05 1 1537 . 332 ASN H H 8.060 0.005 1 1538 . 332 ASN CA C 50.100 0.05 1 1539 . 332 ASN CB C 38.800 0.05 1 1540 . 332 ASN C C 175.800 0.05 1 1541 . 333 ILE N N 107.500 0.05 1 1542 . 333 ILE H H 6.280 0.005 1 1543 . 333 ILE CA C 60.600 0.05 1 1544 . 333 ILE CB C 35.000 0.05 1 1545 . 334 PRO CA C 65.200 0.05 1 1546 . 334 PRO CB C 30.900 0.05 1 1547 . 334 PRO C C 177.200 0.05 1 1548 . 335 GLN N N 113.400 0.05 1 1549 . 335 GLN H H 8.160 0.005 1 1550 . 335 GLN CA C 58.400 0.05 1 1551 . 335 GLN CB C 26.300 0.05 1 1552 . 335 GLN C C 176.100 0.05 1 1553 . 336 MET N N 118.100 0.05 1 1554 . 336 MET H H 8.000 0.005 1 1555 . 336 MET CA C 56.100 0.05 1 1556 . 336 MET CB C 29.000 0.05 1 1557 . 336 MET C C 178.100 0.05 1 1558 . 337 SER N N 113.100 0.05 1 1559 . 337 SER H H 7.690 0.005 1 1560 . 337 SER CA C 62.400 0.05 1 1561 . 337 SER CB C 60.700 0.05 1 1562 . 337 SER C C 175.000 0.05 1 1563 . 338 ALA N N 124.000 0.05 1 1564 . 338 ALA H H 7.320 0.005 1 1565 . 338 ALA CA C 54.800 0.05 1 1566 . 338 ALA CB C 17.400 0.05 1 1567 . 338 ALA C C 180.900 0.05 1 1568 . 339 PHE N N 118.200 0.05 1 1569 . 339 PHE H H 8.070 0.005 1 1570 . 339 PHE CA C 60.300 0.05 1 1571 . 339 PHE CB C 37.200 0.05 1 1572 . 339 PHE C C 175.400 0.05 1 1573 . 340 TRP N N 120.400 0.05 1 1574 . 340 TRP H H 8.520 0.005 1 1575 . 340 TRP CA C 59.100 0.05 1 1576 . 340 TRP CB C 30.100 0.05 1 1577 . 340 TRP C C 179.600 0.05 1 1578 . 341 TYR N N 115.600 0.05 1 1579 . 341 TYR H H 8.590 0.005 1 1580 . 341 TYR CA C 62.000 0.05 1 1581 . 341 TYR CB C 37.300 0.05 1 1582 . 341 TYR C C 179.200 0.05 1 1583 . 342 ALA N N 120.500 0.05 1 1584 . 342 ALA H H 7.960 0.005 1 1585 . 342 ALA CA C 54.500 0.05 1 1586 . 342 ALA CB C 18.100 0.05 1 1587 . 342 ALA C C 180.800 0.05 1 1588 . 343 VAL N N 118.500 0.05 1 1589 . 343 VAL H H 8.480 0.005 1 1590 . 343 VAL CA C 66.200 0.05 1 1591 . 343 VAL CB C 30.400 0.05 1 1592 . 343 VAL C C 177.000 0.05 1 1593 . 344 ARG N N 121.100 0.05 1 1594 . 344 ARG H H 8.790 0.005 1 1595 . 344 ARG CA C 59.800 0.05 1 1596 . 344 ARG CB C 28.600 0.05 1 1597 . 344 ARG C C 177.900 0.05 1 1598 . 345 THR N N 113.600 0.05 1 1599 . 345 THR H H 7.490 0.005 1 1600 . 345 THR CA C 65.900 0.05 1 1601 . 345 THR CB C 68.800 0.05 1 1602 . 345 THR C C 174.900 0.05 1 1603 . 346 ALA N N 122.500 0.05 1 1604 . 346 ALA H H 7.710 0.005 1 1605 . 346 ALA CA C 54.900 0.05 1 1606 . 346 ALA CB C 18.000 0.05 1 1607 . 346 ALA C C 178.900 0.05 1 1608 . 347 VAL N N 116.000 0.05 1 1609 . 347 VAL H H 8.420 0.005 1 1610 . 347 VAL CA C 66.900 0.05 1 1611 . 347 VAL CB C 30.500 0.05 1 1612 . 347 VAL C C 178.000 0.05 1 1613 . 348 ILE N N 117.800 0.05 1 1614 . 348 ILE H H 7.980 0.005 1 1615 . 348 ILE CA C 64.600 0.05 1 1616 . 348 ILE CB C 37.000 0.05 1 1617 . 348 ILE C C 180.200 0.05 1 1618 . 349 ASN N N 120.900 0.05 1 1619 . 349 ASN H H 8.890 0.005 1 1620 . 349 ASN CA C 55.300 0.05 1 1621 . 349 ASN CB C 36.400 0.05 1 1622 . 349 ASN C C 177.800 0.05 1 1623 . 350 ALA N N 122.400 0.05 1 1624 . 350 ALA H H 8.490 0.005 1 1625 . 350 ALA CA C 53.400 0.05 1 1626 . 350 ALA CB C 17.300 0.05 1 1627 . 350 ALA C C 181.000 0.05 1 1628 . 351 ALA N N 121.000 0.05 1 1629 . 351 ALA H H 9.190 0.005 1 1630 . 351 ALA CA C 55.100 0.05 1 1631 . 351 ALA CB C 17.300 0.05 1 1632 . 351 ALA C C 178.100 0.05 1 1633 . 352 SER N N 107.400 0.05 1 1634 . 352 SER H H 7.920 0.005 1 1635 . 352 SER CA C 58.400 0.05 1 1636 . 352 SER CB C 63.700 0.05 1 1637 . 352 SER C C 175.500 0.05 1 1638 . 353 GLY N N 109.600 0.05 1 1639 . 353 GLY H H 7.620 0.005 1 1640 . 353 GLY CA C 45.200 0.05 1 1641 . 353 GLY C C 174.400 0.05 1 1642 . 354 ARG N N 121.000 0.05 1 1643 . 354 ARG H H 8.220 0.005 1 1644 . 354 ARG CA C 57.900 0.05 1 1645 . 354 ARG CB C 30.100 0.05 1 1646 . 354 ARG C C 176.600 0.05 1 1647 . 355 GLN N N 113.400 0.05 1 1648 . 355 GLN H H 7.370 0.005 1 1649 . 355 GLN CA C 53.600 0.05 1 1650 . 355 GLN CB C 35.900 0.05 1 1651 . 355 GLN C C 175.900 0.05 1 1652 . 356 THR N N 111.500 0.05 1 1653 . 356 THR H H 8.570 0.005 1 1654 . 356 THR CA C 60.800 0.05 1 1655 . 356 THR CB C 69.900 0.05 1 1656 . 356 THR C C 174.700 0.05 1 1657 . 357 VAL N N 121.200 0.05 1 1658 . 357 VAL H H 8.710 0.005 1 1659 . 357 VAL CA C 67.300 0.05 1 1660 . 357 VAL CB C 30.600 0.05 1 1661 . 357 VAL C C 177.000 0.05 1 1662 . 358 ASP N N 115.000 0.05 1 1663 . 358 ASP H H 8.110 0.005 1 1664 . 358 ASP CA C 57.100 0.05 1 1665 . 358 ASP CB C 40.300 0.05 1 1666 . 358 ASP C C 178.700 0.05 1 1667 . 359 GLU N N 118.500 0.05 1 1668 . 359 GLU H H 7.600 0.005 1 1669 . 359 GLU CA C 58.200 0.05 1 1670 . 359 GLU CB C 29.600 0.05 1 1671 . 359 GLU C C 178.400 0.05 1 1672 . 360 ALA N N 121.300 0.05 1 1673 . 360 ALA H H 8.720 0.005 1 1674 . 360 ALA CA C 54.200 0.05 1 1675 . 360 ALA CB C 17.900 0.05 1 1676 . 360 ALA C C 181.500 0.05 1 1677 . 361 LEU N N 116.200 0.05 1 1678 . 361 LEU H H 8.160 0.005 1 1679 . 361 LEU CA C 56.900 0.05 1 1680 . 361 LEU CB C 38.900 0.05 1 1681 . 361 LEU C C 178.800 0.05 1 1682 . 362 LYS N N 121.500 0.05 1 1683 . 362 LYS H H 7.750 0.005 1 1684 . 362 LYS CA C 59.100 0.05 1 1685 . 362 LYS CB C 30.900 0.05 1 1686 . 362 LYS C C 179.700 0.05 1 1687 . 363 ASP N N 119.900 0.05 1 1688 . 363 ASP H H 8.150 0.005 1 1689 . 363 ASP CA C 56.700 0.05 1 1690 . 363 ASP CB C 39.700 0.05 1 1691 . 363 ASP C C 178.700 0.05 1 1692 . 364 ALA N N 121.400 0.05 1 1693 . 364 ALA H H 7.680 0.005 1 1694 . 364 ALA CA C 54.700 0.05 1 1695 . 364 ALA CB C 17.200 0.05 1 1696 . 364 ALA C C 178.100 0.05 1 1697 . 365 GLN N N 118.400 0.05 1 1698 . 365 GLN H H 8.260 0.005 1 1699 . 365 GLN CA C 59.800 0.05 1 1700 . 365 GLN CB C 26.700 0.05 1 1701 . 365 GLN C C 179.100 0.05 1 1702 . 366 THR N N 115.200 0.05 1 1703 . 366 THR H H 8.230 0.005 1 1704 . 366 THR CA C 65.500 0.05 1 1705 . 366 THR CB C 68.400 0.05 1 1706 . 366 THR C C 175.800 0.05 1 1707 . 367 ARG N N 120.100 0.05 1 1708 . 367 ARG H H 8.030 0.005 1 1709 . 367 ARG CA C 58.400 0.05 1 1710 . 367 ARG CB C 29.300 0.05 1 1711 . 367 ARG C C 178.800 0.05 1 1712 . 368 ILE N N 117.200 0.05 1 1713 . 368 ILE H H 8.050 0.005 1 1714 . 368 ILE CA C 64.400 0.05 1 1715 . 368 ILE CB C 37.900 0.05 1 1716 . 368 ILE C C 177.100 0.05 1 1717 . 369 THR N N 107.200 0.05 1 1718 . 369 THR H H 7.640 0.005 1 1719 . 369 THR CA C 62.000 0.05 1 1720 . 369 THR CB C 69.800 0.05 1 1721 . 369 THR C C 174.200 0.05 1 1722 . 370 LYS N N 128.100 0.05 1 1723 . 370 LYS H H 7.430 0.005 1 1724 . 370 LYS CA C 58.300 0.05 1 1725 . 370 LYS CB C 31.900 0.05 1 stop_ save_