data_6807 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N chemical shift assignments for stereo-array isotope labelled (SAIL) maltodextrin-binding protein (MBP) ; _BMRB_accession_number 6807 _BMRB_flat_file_name bmr6807.str _Entry_type original _Submission_date 2005-09-02 _Accession_date 2005-09-02 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kainosho Masatsune . . 2 Torizawa Takuya . . 3 Iwashita Yuki . . 4 Terauchi Tsutomu . . 5 Ono Akira Mei . 6 Guntert Peter . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1433 "13C chemical shifts" 1035 "15N chemical shifts" 360 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-04-25 original author . stop_ _Original_release_date 2006-04-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Optimal isotope labelling for NMR protein structure determination' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16511487 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kainosho Masatsune . . 2 Torizawa Takuya . . 3 Iwashita Yuki . . 4 Terauchi Tsutomu . . 5 'Mei Ono' Akira . . 6 Guntert Peter . . stop_ _Journal_abbreviation Nature _Journal_volume 440 _Journal_issue 7080 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 52 _Page_last 57 _Year 2006 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Maltodextrin-binding protein (MBP)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Maltodextrin-binding protein' $MBP beta-cyclodextrin $BCD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _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' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 370 _Mol_residue_sequence ; KIEEGKLVIWINGDKGYNGL AEVGKKFEKDTGIKVTVEHP DKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEIT PDKAFQDKLYPFTWDAVRYN GKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELK AKGKSALMFNLQEPYFTWPL IAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIK NKHMNADTDYSIAEAAFNKG ETAMTINGPWAWSNIDTSKV NYGVTVLPTFKGQPSKPFVG VLSAGINAASPNKELAKEFL ENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAAT MENAQKGEIMPNIPQMSAFW YAVRTAVINAASGRQTVDEA LKDAQTRITK ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 ILE 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 99.73 99.73 0.00e+00 BMRB 4354 MBP 100.00 370 99.73 99.73 0.00e+00 BMRB 4986 MBP 100.00 370 99.73 99.73 0.00e+00 BMRB 4987 "maltodextrin-binding protein" 100.00 370 99.73 99.73 0.00e+00 BMRB 7114 MBP 100.00 370 99.73 99.73 0.00e+00 PDB 1A7L "Dominant B-Cell Epitope From The Pres2 Region Of Hepatitis B Virus In The Form Of An Inserted Peptide Segment In Maltodextrin-B" 98.65 389 99.45 99.45 0.00e+00 PDB 1ANF "Maltodextrin Binding Protein With Bound Maltose" 100.00 370 100.00 100.00 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" 100.00 370 100.00 100.00 0.00e+00 PDB 1EZ9 "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P1 Crystal Form" 100.00 370 100.00 100.00 0.00e+00 PDB 1EZO "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 99.73 99.73 0.00e+00 PDB 1EZP "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin Using Peptide Orientations From Dipolar Couplings" 100.00 370 99.73 99.73 0.00e+00 PDB 1FQA "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.73 370 100.00 100.00 0.00e+00 PDB 1FQB "Structure Of Maltotriotol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.73 370 100.00 100.00 0.00e+00 PDB 1FQC "Crystal Structure Of Maltotriotol Bound To Closed-Form Maltodextrin Binding Protein" 99.73 370 100.00 100.00 0.00e+00 PDB 1FQD "Crystal Structure Of Maltotetraitol Bound To Closed-Form Maltodextrin Binding Protein" 99.73 370 100.00 100.00 0.00e+00 PDB 1HSJ "Sarr Mbp Fusion Structure" 98.92 487 99.45 99.45 0.00e+00 PDB 1JVX "Maltodextrin-Binding Protein Variant D207cA301GSP316C Cross-Linked In Crystal" 100.27 372 98.92 99.19 0.00e+00 PDB 1JVY "Maltodextrin-Binding Protein Variant D207cA301GSP316C With Beta-Mercaptoethanol Mixed Disulfides" 100.27 372 98.92 99.19 0.00e+00 PDB 1JW4 "Structure Of Ligand-Free Maltodextrin-Binding Protein" 100.00 370 100.00 100.00 0.00e+00 PDB 1JW5 "Structure Of Maltose Bound To Open-Form Maltodextrin- Binding Protein In P1 Crystal" 100.00 370 100.00 100.00 0.00e+00 PDB 1LAX "Crystal Structure Of Male31, A Defective Folding Mutant Of Maltose-Binding Protein" 100.00 370 99.46 99.46 0.00e+00 PDB 1LLS "Crystal Structure Of Unliganded Maltose Binding Protein With Xenon" 100.00 370 100.00 100.00 0.00e+00 PDB 1MDP "Refined Structures Of Two Insertion(Slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.00 363 97.57 97.57 0.00e+00 PDB 1MDQ "Refined Structures Of Two Insertion(slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.27 371 99.46 99.73 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 99.18 99.18 0.00e+00 PDB 1MH4 "Maltose Binding-A1 Homeodomain Protein Chimera, Crystal Form Ii" 98.92 421 99.18 99.18 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 99.73 99.73 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 99.73 99.73 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 99.73 99.73 0.00e+00 PDB 1N3W "Engineered High-affinity Maltose-binding Protein" 100.00 366 98.65 98.65 0.00e+00 PDB 1N3X "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 98.65 98.65 0.00e+00 PDB 1NL5 "Engineered High-affinity Maltose-binding Protein" 100.00 366 98.11 98.11 0.00e+00 PDB 1NMU Mbp-L30 98.92 382 100.00 100.00 0.00e+00 PDB 1OMP "Crystallographic Evidence Of A Large Ligand-Induced Hinge- Twist Motion Between The Two Domains Of The Maltodextrin- Binding Pr" 100.00 370 100.00 100.00 0.00e+00 PDB 1PEB "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 98.11 98.11 0.00e+00 PDB 1R6Z "The Crystal Structure Of The Argonaute2 Paz Domain (as A Mbp Fusion)" 98.92 509 100.00 100.00 0.00e+00 PDB 1SVX "Crystal Structure Of A Designed Selected Ankyrin Repeat Protein In Complex With The Maltose Binding Protein" 98.92 395 99.73 99.73 0.00e+00 PDB 1T0K "Joint X-ray And Nmr Refinement Of Yeast L30e-mrna Complex" 98.92 381 99.73 100.00 0.00e+00 PDB 1Y4C "Designed Helical Protein Fusion Mbp" 98.92 494 100.00 100.00 0.00e+00 PDB 1YTV "Maltose-binding Protein Fusion To A C-terminal Fragment Of The V1a Vasopressin Receptor" 98.92 366 100.00 100.00 0.00e+00 PDB 1ZIU "Crystal Structure Of Nickel-bound Engineered Maltose Binding Protein" 100.00 370 98.65 98.65 0.00e+00 PDB 1ZJL "Crystal Structure Of Zinc-Bound Engineered Maltose Binding Protein" 100.00 370 98.65 98.65 0.00e+00 PDB 1ZKB "Zinc-Free Engineered Maltose Binding Protein" 100.00 370 98.65 98.65 0.00e+00 PDB 1ZMG "Crystal Structure Of Copper-Bound Engineered Maltose Binding Protein" 100.00 370 98.65 98.65 0.00e+00 PDB 2D21 "Nmr Structure Of Stereo-Array Isotope Labelled (Sail) Maltodextrin-Binding Protein (Mbp)" 100.00 370 100.00 100.00 0.00e+00 PDB 2H25 "Solution Structure Of Maltose Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 99.73 99.73 0.00e+00 PDB 2KLF "Pere Nmr Structure Of Maltodextrin-Binding Protein" 100.00 370 99.73 99.73 0.00e+00 PDB 2MV0 "Solution Nmr Structure Of Maltose-binding Protein From Escherichia Coli, Northeast Structural Genomics Consortium (nesg) Target" 100.00 370 100.00 100.00 0.00e+00 PDB 2NVU "Structure Of Appbp1-Uba3~nedd8-Nedd8-Mgatp-Ubc12(C111a), A Trapped Ubiquitin-Like Protein Activation Complex" 98.92 805 99.18 99.18 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" 99.19 402 99.46 99.73 0.00e+00 PDB 2R6G "The Crystal Structure Of The E. Coli Maltose Transporter" 100.00 370 100.00 100.00 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 99.46 99.46 0.00e+00 PDB 2VGQ "Crystal Structure Of Human Ips-1 Card" 98.92 477 100.00 100.00 0.00e+00 PDB 2XZ3 "Blv Tm Hairpin" 98.92 463 99.18 99.18 0.00e+00 PDB 2ZXT "Crystal Structure Of Tim40/mia40, A Disulfide Relay System In Mitochondria, Solved As Mbp Fusion Protein" 98.92 465 100.00 100.00 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)" 98.92 539 100.00 100.00 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 98.91 98.91 0.00e+00 PDB 3D4G "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Ii)" 98.92 481 98.91 98.91 0.00e+00 PDB 3DM0 "Maltose Binding Protein Fusion With Rack1 From A. Thaliana" 98.92 694 98.36 98.36 0.00e+00 PDB 3EF7 "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Iii)" 98.92 481 98.91 98.91 0.00e+00 PDB 3EHS "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (Crfr1)" 98.92 476 100.00 100.00 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 99.73 99.73 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 99.73 99.73 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 99.18 99.18 0.00e+00 PDB 3G7V "Islet Amyloid Polypeptide (iapp Or Amylin) Fused To Maltose Binding Protein" 99.19 408 98.91 98.91 0.00e+00 PDB 3G7W "Islet Amyloid Polypeptide (Iapp Or Amylin) Residues 1 To 22 Fused To Maltose Binding Protein" 98.92 393 99.18 99.18 0.00e+00 PDB 3H3G "Crystal Structure Of The Extracellular Domain Of The Human Parathyroid Hormone Receptor (Pth1r) In Complex With Parathyroid Hor" 98.92 539 100.00 100.00 0.00e+00 PDB 3H4Z "Crystal Structure Of An Mbp-Der P 7 Fusion Protein" 98.92 568 97.81 97.81 0.00e+00 PDB 3HPI "Crystal Structure Of Maltose-Binding Protein Mutant With Bound Sucrose" 100.00 372 98.92 99.19 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 99.73 99.73 0.00e+00 PDB 3IO4 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C90" 98.92 449 99.18 99.18 0.00e+00 PDB 3IO6 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-A" 98.92 449 99.18 99.18 0.00e+00 PDB 3IOR "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C95" 98.92 449 99.18 99.18 0.00e+00 PDB 3IOT "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-B" 98.92 449 99.18 99.18 0.00e+00 PDB 3IOU "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C94" 98.92 449 99.18 99.18 0.00e+00 PDB 3IOV "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C99" 98.92 449 99.18 99.18 0.00e+00 PDB 3IOW "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C99-Hg" 98.92 449 99.18 99.18 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 98.92 99.19 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)" 97.84 384 99.72 100.00 0.00e+00 PDB 3LC8 "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Free Form)" 97.84 384 99.72 100.00 0.00e+00 PDB 3MBP "Maltodextrin-Binding Protein With Bound Maltotriose" 100.00 370 100.00 100.00 0.00e+00 PDB 3MP1 "Complex Structure Of Sgf29 And Trimethylated H3k4" 98.92 522 99.45 99.45 0.00e+00 PDB 3MP6 "Complex Structure Of Sgf29 And Dimethylated H3k4" 98.92 522 99.45 99.45 0.00e+00 PDB 3MP8 "Crystal Structure Of Sgf29 Tudor Domain" 98.92 522 99.45 99.45 0.00e+00 PDB 3MQ9 "Crystal Structure Of Ectodomain Mutant Of Bst-2TETHERINCD317 FUSED To Mbp" 99.73 471 100.00 100.00 0.00e+00 PDB 3N93 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 3" 98.92 482 100.00 100.00 0.00e+00 PDB 3N94 "Crystal Structure Of Human Pituitary Adenylate Cyclase 1 Receptor- Short N-Terminal Extracellular Domain" 98.92 475 100.00 100.00 0.00e+00 PDB 3N95 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 2" 98.92 482 100.00 100.00 0.00e+00 PDB 3N96 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 1" 98.92 482 100.00 100.00 0.00e+00 PDB 3O3U "Crystal Structure Of Human Receptor For Advanced Glycation Endproducts (Rage)" 98.65 581 99.18 99.18 0.00e+00 PDB 3OAI "Crystal Structure Of The Extra-Cellular Domain Of Human Myelin Protein Zero" 99.19 507 99.73 99.73 0.00e+00 PDB 3OB4 "Mbp-Fusion Protein Of The Major Peanut Allergen Ara H 2" 98.92 500 97.81 97.81 0.00e+00 PDB 3PGF "Crystal Structure Of Maltose Bound Mbp With A Conformationally Specific Synthetic Antigen Binder (Sab)" 99.19 398 99.73 99.73 0.00e+00 PDB 3PUV "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Vo4" 100.00 378 100.00 100.00 0.00e+00 PDB 3PUW "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Alf4" 100.00 378 100.00 100.00 0.00e+00 PDB 3PUX "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Bef3" 100.00 378 100.00 100.00 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" 100.00 378 100.00 100.00 0.00e+00 PDB 3PUZ "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Bound To Amp-Pnp" 100.00 370 99.46 99.46 0.00e+00 PDB 3PV0 "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Without Nucleotide" 100.00 370 99.46 99.46 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 98.36 98.36 0.00e+00 PDB 3Q25 "Crystal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 100.00 100.00 0.00e+00 PDB 3Q26 "Cyrstal Structure Of Human Alpha-Synuclein (10-42) Fused To Maltose Binding Protein (Mbp)" 98.92 404 100.00 100.00 0.00e+00 PDB 3Q27 "Cyrstal Structure Of Human Alpha-Synuclein (32-57) Fused To Maltose Binding Protein (Mbp)" 98.92 397 100.00 100.00 0.00e+00 PDB 3Q28 "Cyrstal Structure Of Human Alpha-Synuclein (58-79) Fused To Maltose Binding Protein (Mbp)" 99.19 393 99.73 99.73 0.00e+00 PDB 3Q29 "Cyrstal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 100.00 100.00 0.00e+00 PDB 3RLF "Crystal Structure Of The Maltose-Binding ProteinMALTOSE TRANSPORTER Complex In An Outward-Facing Conformation Bound To Mgamppnp" 100.00 380 100.00 100.00 0.00e+00 PDB 3RUM "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" 99.19 378 99.73 99.73 0.00e+00 PDB 3SER "Zn-Mediated Polymer Of Maltose-Binding Protein K26hK30H BY SYNTHETIC Symmetrization" 99.19 372 98.37 98.37 0.00e+00 PDB 3SES "Cu-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization" 99.19 372 98.37 98.37 0.00e+00 PDB 3SET "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form I)" 99.19 372 98.37 98.37 0.00e+00 PDB 3SEU "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Iii)" 99.19 372 98.37 98.37 0.00e+00 PDB 3SEV "Zn-Mediated Trimer Of Maltose-Binding Protein E310hK314H BY SYNTHETIC Symmetrization" 99.19 372 98.37 98.37 0.00e+00 PDB 3SEW "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form I)" 99.19 372 98.37 98.37 0.00e+00 PDB 3SEX "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form Ii)" 99.19 372 98.37 98.37 0.00e+00 PDB 3SEY "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Ii)" 99.19 372 98.37 98.37 0.00e+00 PDB 3VD8 "Crystal Structure Of Human Aim2 Pyd Domain With Mbp Fusion" 98.92 489 97.81 97.81 0.00e+00 PDB 3VFJ "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Mbp As A Ligand Carrier" 99.19 378 99.73 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" 100.00 389 100.00 100.00 0.00e+00 PDB 3WAI "Crystal Structure Of The C-terminal Globular Domain Of Oligosaccharyltransferase (afaglb-l, O29867_arcfu) From Archaeoglobus Fu" 98.92 739 100.00 100.00 0.00e+00 PDB 4B3N "Crystal Structure Of Rhesus Trim5alpha PrySPRY DOMAIN" 100.00 602 99.46 100.00 0.00e+00 PDB 4BL8 "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu)" 98.92 831 98.91 98.91 0.00e+00 PDB 4BL9 "Crystal Structure Of Full-length Human Suppressor Of Fused ( Sufu) Mutant Lacking A Regulatory Subdomain (crystal Form I)" 98.92 756 98.91 98.91 0.00e+00 PDB 4BLA "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu) Mutant Lacking A Regulatory Subdomain (crystal Form Ii)" 98.92 756 98.91 98.91 0.00e+00 PDB 4BLB "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli1p Complex" 98.92 753 98.36 98.36 0.00e+00 PDB 4BLD "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli3p Complex" 98.92 753 98.36 98.36 0.00e+00 PDB 4EDQ "Mbp-fusion Protein Of Myosin-binding Protein C Residues 149-269" 98.92 492 99.18 99.18 0.00e+00 PDB 4EGC "Crystal Structure Of Mbp-fused Human Six1 Bound To Human Eya2 Eya Domain" 98.92 559 98.63 98.63 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 97.81 97.81 0.00e+00 PDB 4FE8 "Crystal Structure Of Htt36q3h-ex1-x1-c1(alpha)" 98.92 452 99.18 99.18 0.00e+00 PDB 4FEB "Crystal Structure Of Htt36q3h-ex1-x1-c2(beta)" 98.92 452 99.18 99.18 0.00e+00 PDB 4FEC "Crystal Structure Of Htt36q3h" 98.92 452 99.18 99.18 0.00e+00 PDB 4FED "Crystal Structure Of Htt36q3h" 98.92 452 99.18 99.18 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 98.36 98.36 0.00e+00 PDB 4GLI "Crystal Structure Of Human Smn Yg-Dimer" 99.73 401 100.00 100.00 0.00e+00 PDB 4H1G "Structure Of Candida Albicans Kar3 Motor Domain Fused To Maltose- Binding Protein" 98.92 715 99.18 99.18 0.00e+00 PDB 4IFP "X-ray Crystal Structure Of Human Nlrp1 Card Domain" 98.92 466 97.81 97.81 0.00e+00 PDB 4JBZ "Structure Of Mcm10 Coiled-coil Region" 98.92 403 97.81 97.81 0.00e+00 PDB 4JKM "Crystal Structure Of Clostridium Perfringens Beta-glucuronidase" 99.19 400 99.46 99.46 0.00e+00 PDB 4KEG "Crystal Structure Of Mbp Fused Human Splunc1" 98.92 584 99.45 99.45 0.00e+00 PDB 4KHZ "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Pre-translocation Conformation Bound To Malt" 100.00 380 100.00 100.00 0.00e+00 PDB 4KI0 "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Outward-facing Conformation Bound To Maltohe" 100.00 380 100.00 100.00 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 99.18 99.18 0.00e+00 PDB 4KYC "Structure Of The C-terminal Domain Of The Menangle Virus Phosphoprotein, Fused To Mbp" 98.92 420 98.63 98.63 0.00e+00 PDB 4KYD "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp." 98.92 420 98.63 98.63 0.00e+00 PDB 4KYE "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp" 98.92 420 98.63 98.63 0.00e+00 PDB 4LOG "The Crystal Structure Of The Orphan Nuclear Receptor Pnr Ligand Binding Domain Fused With Mbp" 98.92 574 100.00 100.00 0.00e+00 PDB 4MBP "Maltodextrin Binding Protein With Bound Maltetrose" 100.00 370 100.00 100.00 0.00e+00 PDB 4MY2 "Crystal Structure Of Norrin In Fusion With Maltose Binding Protein" 98.92 477 100.00 100.00 0.00e+00 PDB 4N4X "Crystal Structure Of The Mbp Fused Human Splunc1 (native Form)" 98.92 584 99.45 99.45 0.00e+00 PDB 4NDZ "Structure Of Maltose Binding Protein Fusion To 2-o-sulfotransferase With Bound Heptasaccharide And Pap" 98.92 658 99.18 99.18 0.00e+00 PDB 4NUF "Crystal Structure Of Shp/eid1" 98.92 580 100.00 100.00 0.00e+00 PDB 4O4B "Crystal Structure Of An Inositol Hexakisphosphate Kinase Ehip6ka As A Fusion Protein With Maltose Binding Protein" 98.92 396 100.00 100.00 0.00e+00 PDB 4OGM "Mbp-fusion Protein Of Pila1 Residues 26-159" 99.19 520 97.55 97.55 0.00e+00 PDB 4OZQ "Crystal Structure Of The Mouse Kif14 Motor Domain" 98.92 720 99.18 99.18 0.00e+00 PDB 4PE2 "Mbp Pila1 Cd160" 99.19 516 99.73 99.73 0.00e+00 PDB 4PQK "C-terminal Domain Of Dna Binding Protein" 99.19 487 99.73 99.73 0.00e+00 PDB 4QVH "Crystal Structure Of The Essential Mycobacterium Tuberculosis Phosphopantetheinyl Transferase Pptt, Solved As A Fusion Protein " 98.92 598 98.63 98.63 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" 97.57 501 100.00 100.00 0.00e+00 PDB 4TSM "Mbp-fusion Protein Of Pila1 From C. Difficile R20291 Residues 26-166" 99.19 520 97.55 97.55 0.00e+00 PDB 4WGI "A Single Diastereomer Of A Macrolactam Core Binds Specifically To Myeloid Cell Leukemia 1 (mcl1)" 98.92 518 100.00 100.00 0.00e+00 PDB 4WJV "Crystal Structure Of Rsa4 In Complex With The Nsa2 Binding Peptide" 99.19 381 98.09 98.09 0.00e+00 DBJ BAB38440 "periplasmic maltose-binding protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 100.00 100.00 0.00e+00 DBJ BAE78036 "maltose transporter subunit [Escherichia coli str. K-12 substr. W3110]" 100.00 396 100.00 100.00 0.00e+00 DBJ BAG79849 "maltose ABC transporter substrate binding component [Escherichia coli SE11]" 100.00 396 100.00 100.00 0.00e+00 DBJ BAI28296 "periplasmic maltose-binding protein MalE [Escherichia coli O26:H11 str. 11368]" 100.00 396 100.00 100.00 0.00e+00 DBJ BAI33473 "periplasmic maltose-binding protein MalE [Escherichia coli O103:H2 str. 12009]" 100.00 396 100.00 100.00 0.00e+00 EMBL CAP78494 "Maltose-binding periplasmic protein [Escherichia coli LF82]" 100.00 396 98.92 99.73 0.00e+00 EMBL CAQ34383 "malE, subunit of maltose ABC transporter [Escherichia coli BL21(DE3)]" 100.00 396 100.00 100.00 0.00e+00 EMBL CAR01012 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli IAI1]" 100.00 396 100.00 100.00 0.00e+00 EMBL CAR05669 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli S88]" 100.00 396 98.92 99.73 0.00e+00 EMBL CAR10711 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli ED1a]" 100.00 396 98.92 99.73 0.00e+00 GB AAB59056 "periplasmic maltose-binding protein [Escherichia coli]" 100.00 396 100.00 100.00 0.00e+00 GB AAB86559 "maltose binding protein-lacZ alpha peptide fusion protein precursor [Shuttle vector pMAL-pIII]" 98.92 482 100.00 100.00 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]" 100.00 396 100.00 100.00 0.00e+00 GB AAC77004 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 100.00 100.00 0.00e+00 REF NP_290668 "maltose ABC transporter substrate-binding protein [Escherichia coli O157:H7 str. EDL933]" 100.00 396 100.00 100.00 0.00e+00 REF NP_313044 "maltose ABC transporter periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 100.00 100.00 0.00e+00 REF NP_418458 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 100.00 100.00 0.00e+00 REF NP_709885 "maltose ABC transporter substrate-binding protein [Shigella flexneri 2a str. 301]" 100.00 396 99.73 99.73 0.00e+00 REF NP_756856 "maltose ABC transporter periplasmic protein [Escherichia coli CFT073]" 100.00 396 98.92 99.73 0.00e+00 SP P0AEX9 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 100.00 100.00 0.00e+00 SP P0AEY0 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 100.00 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_BCD _Saveframe_category ligand _Mol_type "non-polymer (SACCHARIDE)" _Name_common "BCD (BETA-CYCLODEXTRIN)" _BMRB_code . _PDB_code BCD _Molecular_mass 1134.984 _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 Mon Aug 29 11:27:42 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C11 C11 C . 0 . ? C21 C21 C . 0 . ? O21 O21 O . 0 . ? C31 C31 C . 0 . ? O31 O31 O . 0 . ? C41 C41 C . 0 . ? O41 O41 O . 0 . ? C51 C51 C . 0 . ? O51 O51 O . 0 . ? C61 C61 C . 0 . ? O61 O61 O . 0 . ? C12 C12 C . 0 . ? C22 C22 C . 0 . ? O22 O22 O . 0 . ? C32 C32 C . 0 . ? O32 O32 O . 0 . ? C42 C42 C . 0 . ? O42 O42 O . 0 . ? C52 C52 C . 0 . ? O52 O52 O . 0 . ? C62 C62 C . 0 . ? O62 O62 O . 0 . ? C13 C13 C . 0 . ? C23 C23 C . 0 . ? O23 O23 O . 0 . ? C33 C33 C . 0 . ? O33 O33 O . 0 . ? C43 C43 C . 0 . ? O43 O43 O . 0 . ? C53 C53 C . 0 . ? O53 O53 O . 0 . ? C63 C63 C . 0 . ? O63 O63 O . 0 . ? C14 C14 C . 0 . ? C24 C24 C . 0 . ? O24 O24 O . 0 . ? C34 C34 C . 0 . ? O34 O34 O . 0 . ? C44 C44 C . 0 . ? O44 O44 O . 0 . ? C54 C54 C . 0 . ? O54 O54 O . 0 . ? C64 C64 C . 0 . ? O64 O64 O . 0 . ? C15 C15 C . 0 . ? C25 C25 C . 0 . ? O25 O25 O . 0 . ? C35 C35 C . 0 . ? O35 O35 O . 0 . ? C45 C45 C . 0 . ? O45 O45 O . 0 . ? C55 C55 C . 0 . ? O55 O55 O . 0 . ? C65 C65 C . 0 . ? O65 O65 O . 0 . ? C16 C16 C . 0 . ? C26 C26 C . 0 . ? O26 O26 O . 0 . ? C36 C36 C . 0 . ? O36 O36 O . 0 . ? C46 C46 C . 0 . ? O46 O46 O . 0 . ? C56 C56 C . 0 . ? O56 O56 O . 0 . ? C66 C66 C . 0 . ? O66 O66 O . 0 . ? C17 C17 C . 0 . ? C27 C27 C . 0 . ? O27 O27 O . 0 . ? C37 C37 C . 0 . ? O37 O37 O . 0 . ? C47 C47 C . 0 . ? O47 O47 O . 0 . ? C57 C57 C . 0 . ? O57 O57 O . 0 . ? C67 C67 C . 0 . ? O67 O67 O . 0 . ? H11 H11 H . 0 . ? H21 H21 H . 0 . ? HO21 HO21 H . 0 . ? H31 H31 H . 0 . ? HO31 HO31 H . 0 . ? H41 H41 H . 0 . ? H51 H51 H . 0 . ? H611 H611 H . 0 . ? H612 H612 H . 0 . ? HO61 HO61 H . 0 . ? H12 H12 H . 0 . ? H22 H22 H . 0 . ? HO22 HO22 H . 0 . ? H32 H32 H . 0 . ? HO32 HO32 H . 0 . ? H42 H42 H . 0 . ? H52 H52 H . 0 . ? H621 H621 H . 0 . ? H622 H622 H . 0 . ? HO62 HO62 H . 0 . ? H13 H13 H . 0 . ? H23 H23 H . 0 . ? HO23 HO23 H . 0 . ? H33 H33 H . 0 . ? HO33 HO33 H . 0 . ? H43 H43 H . 0 . ? H53 H53 H . 0 . ? H631 H631 H . 0 . ? H632 H632 H . 0 . ? HO63 HO63 H . 0 . ? H14 H14 H . 0 . ? H24 H24 H . 0 . ? HO24 HO24 H . 0 . ? H34 H34 H . 0 . ? HO34 HO34 H . 0 . ? H44 H44 H . 0 . ? H54 H54 H . 0 . ? H641 H641 H . 0 . ? H642 H642 H . 0 . ? HO64 HO64 H . 0 . ? H15 H15 H . 0 . ? H25 H25 H . 0 . ? HO25 HO25 H . 0 . ? H35 H35 H . 0 . ? HO35 HO35 H . 0 . ? H45 H45 H . 0 . ? H55 H55 H . 0 . ? H651 H651 H . 0 . ? H652 H652 H . 0 . ? HO65 HO65 H . 0 . ? H16 H16 H . 0 . ? H26 H26 H . 0 . ? HO26 HO26 H . 0 . ? H36 H36 H . 0 . ? HO36 HO36 H . 0 . ? H46 H46 H . 0 . ? H56 H56 H . 0 . ? H661 H661 H . 0 . ? H662 H662 H . 0 . ? HO66 HO66 H . 0 . ? H17 H17 H . 0 . ? H27 H27 H . 0 . ? HO27 HO27 H . 0 . ? H37 H37 H . 0 . ? HO37 HO37 H . 0 . ? H47 H47 H . 0 . ? H57 H57 H . 0 . ? H671 H671 H . 0 . ? H672 H672 H . 0 . ? HO67 HO67 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 C11 C21 ? ? SING C11 O51 ? ? SING C11 O47 ? ? SING C11 H11 ? ? SING C21 O21 ? ? SING C21 C31 ? ? SING C21 H21 ? ? SING O21 HO21 ? ? SING C31 O31 ? ? SING C31 C41 ? ? SING C31 H31 ? ? SING O31 HO31 ? ? SING C41 O41 ? ? SING C41 C51 ? ? SING C41 H41 ? ? SING O41 C12 ? ? SING C51 O51 ? ? SING C51 C61 ? ? SING C51 H51 ? ? SING C61 O61 ? ? SING C61 H611 ? ? SING C61 H612 ? ? SING O61 HO61 ? ? SING C12 C22 ? ? SING C12 O52 ? ? SING C12 H12 ? ? SING C22 O22 ? ? SING C22 C32 ? ? SING C22 H22 ? ? SING O22 HO22 ? ? SING C32 O32 ? ? SING C32 C42 ? ? SING C32 H32 ? ? SING O32 HO32 ? ? SING C42 O42 ? ? SING C42 C52 ? ? SING C42 H42 ? ? SING O42 C13 ? ? SING C52 O52 ? ? SING C52 C62 ? ? SING C52 H52 ? ? SING C62 O62 ? ? SING C62 H621 ? ? SING C62 H622 ? ? SING O62 HO62 ? ? SING C13 C23 ? ? SING C13 O53 ? ? SING C13 H13 ? ? SING C23 O23 ? ? SING C23 C33 ? ? SING C23 H23 ? ? SING O23 HO23 ? ? SING C33 O33 ? ? SING C33 C43 ? ? SING C33 H33 ? ? SING O33 HO33 ? ? SING C43 O43 ? ? SING C43 C53 ? ? SING C43 H43 ? ? SING O43 C14 ? ? SING C53 O53 ? ? SING C53 C63 ? ? SING C53 H53 ? ? SING C63 O63 ? ? SING C63 H631 ? ? SING C63 H632 ? ? SING O63 HO63 ? ? SING C14 C24 ? ? SING C14 O54 ? ? SING C14 H14 ? ? SING C24 O24 ? ? SING C24 C34 ? ? SING C24 H24 ? ? SING O24 HO24 ? ? SING C34 O34 ? ? SING C34 C44 ? ? SING C34 H34 ? ? SING O34 HO34 ? ? SING C44 O44 ? ? SING C44 C54 ? ? SING C44 H44 ? ? SING O44 C15 ? ? SING C54 O54 ? ? SING C54 C64 ? ? SING C54 H54 ? ? SING C64 O64 ? ? SING C64 H641 ? ? SING C64 H642 ? ? SING O64 HO64 ? ? SING C15 C25 ? ? SING C15 O55 ? ? SING C15 H15 ? ? SING C25 O25 ? ? SING C25 C35 ? ? SING C25 H25 ? ? SING O25 HO25 ? ? SING C35 O35 ? ? SING C35 C45 ? ? SING C35 H35 ? ? SING O35 HO35 ? ? SING C45 O45 ? ? SING C45 C55 ? ? SING C45 H45 ? ? SING O45 C16 ? ? SING C55 O55 ? ? SING C55 C65 ? ? SING C55 H55 ? ? SING C65 O65 ? ? SING C65 H651 ? ? SING C65 H652 ? ? SING O65 HO65 ? ? SING C16 C26 ? ? SING C16 O56 ? ? SING C16 H16 ? ? SING C26 O26 ? ? SING C26 C36 ? ? SING C26 H26 ? ? SING O26 HO26 ? ? SING C36 O36 ? ? SING C36 C46 ? ? SING C36 H36 ? ? SING O36 HO36 ? ? SING C46 O46 ? ? SING C46 C56 ? ? SING C46 H46 ? ? SING O46 C17 ? ? SING C56 O56 ? ? SING C56 C66 ? ? SING C56 H56 ? ? SING C66 O66 ? ? SING C66 H661 ? ? SING C66 H662 ? ? SING O66 HO66 ? ? SING C17 C27 ? ? SING C17 O57 ? ? SING C17 H17 ? ? SING C27 O27 ? ? SING C27 C37 ? ? SING C27 H27 ? ? SING O27 HO27 ? ? SING C37 O37 ? ? SING C37 C47 ? ? SING C37 H37 ? ? SING O37 HO37 ? ? SING C47 O47 ? ? SING C47 C57 ? ? SING C47 H47 ? ? SING C57 O57 ? ? SING C57 C67 ? ? SING C57 H57 ? ? SING C67 O67 ? ? SING C67 H671 ? ? SING C67 H672 ? ? SING O67 HO67 ? ? 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 'chemical synthesis' . . . . . 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 0.9 mM . $BCD 3.3 mM . 'sodium phosphate' 20 mM . NaN3 3 mM . 'CompleteMini protease inhibitor mix' . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_800MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_unknown_1 _Saveframe_category NMR_applied_experiment _Experiment_name unknown _Sample_label $sample_1 save_ save_NMR_spec_expt _Saveframe_category NMR_applied_experiment _Experiment_name unknown _BMRB_pulse_sequence_accession_number . _Details 'experiment information not available' save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.1 pH temperature 310 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label unknown stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _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 1 LYS H H 8.284 0.020 1 2 1 1 LYS HA H 4.381 0.020 1 3 1 1 LYS HB3 H 1.818 0.020 1 4 1 1 LYS HG3 H 1.387 0.020 1 5 1 1 LYS HE2 H 3.009 0.020 1 6 1 1 LYS CA C 56.270 0.200 1 7 1 1 LYS CB C 32.935 0.200 1 8 1 1 LYS CG C 24.207 0.200 1 9 1 1 LYS CE C 41.966 0.200 1 10 1 1 LYS N N 122.149 0.200 1 11 2 2 ILE H H 7.914 0.020 1 12 2 2 ILE HA H 4.061 0.020 1 13 2 2 ILE HB H 1.667 0.020 1 14 2 2 ILE HG12 H 1.127 0.020 1 15 2 2 ILE HG2 H 0.903 0.020 1 16 2 2 ILE HD1 H 0.541 0.020 1 17 2 2 ILE CA C 61.917 0.200 1 18 2 2 ILE CB C 38.755 0.200 1 19 2 2 ILE CG1 C 27.113 0.200 1 20 2 2 ILE CG2 C 17.588 0.200 1 21 2 2 ILE CD1 C 12.719 0.200 1 22 2 2 ILE N N 122.752 0.200 1 23 3 3 GLU H H 8.582 0.020 1 24 3 3 GLU HA H 4.270 0.020 1 25 3 3 GLU HB2 H 1.895 0.020 1 26 3 3 GLU HG2 H 2.223 0.020 1 27 3 3 GLU CA C 56.629 0.200 1 28 3 3 GLU CB C 30.799 0.200 1 29 3 3 GLU CG C 36.164 0.200 1 30 3 3 GLU N N 126.156 0.200 1 31 4 4 GLU H H 8.536 0.020 1 32 4 4 GLU HA H 4.457 0.020 1 33 4 4 GLU HB2 H 1.968 0.020 1 34 4 4 GLU HG2 H 2.235 0.020 1 35 4 4 GLU CA C 56.643 0.200 1 36 4 4 GLU CB C 30.422 0.200 1 37 4 4 GLU CG C 36.456 0.200 1 38 4 4 GLU N N 123.446 0.200 1 39 5 5 GLY H H 8.857 0.020 1 40 5 5 GLY HA3 H 3.973 0.020 1 41 5 5 GLY CA C 45.749 0.200 1 42 5 5 GLY N N 110.665 0.200 1 43 6 6 LYS H H 7.658 0.020 1 44 6 6 LYS HA H 4.854 0.020 1 45 6 6 LYS HB3 H 1.751 0.020 1 46 6 6 LYS HG3 H 1.217 0.020 1 47 6 6 LYS HD3 H 1.544 0.020 1 48 6 6 LYS HE2 H 2.857 0.020 1 49 6 6 LYS CA C 54.811 0.200 1 50 6 6 LYS CB C 35.132 0.200 1 51 6 6 LYS CG C 23.115 0.200 1 52 6 6 LYS CD C 29.041 0.200 1 53 6 6 LYS CE C 41.987 0.200 1 54 6 6 LYS N N 118.841 0.200 1 55 7 7 LEU H H 8.247 0.020 1 56 7 7 LEU HA H 4.932 0.020 1 57 7 7 LEU HB3 H 0.906 0.020 1 58 7 7 LEU HG H 1.249 0.020 1 59 7 7 LEU HD1 H 0.307 0.020 1 60 7 7 LEU CA C 53.293 0.200 1 61 7 7 LEU CB C 46.621 0.200 1 62 7 7 LEU CG C 26.065 0.200 1 63 7 7 LEU CD1 C 24.832 0.200 1 64 7 7 LEU N N 116.554 0.200 1 65 8 8 VAL H H 10.141 0.020 1 66 8 8 VAL HA H 4.826 0.020 1 67 8 8 VAL HB H 1.881 0.020 1 68 8 8 VAL HG2 H 0.970 0.020 1 69 8 8 VAL CA C 61.865 0.200 1 70 8 8 VAL CB C 33.538 0.200 1 71 8 8 VAL CG2 C 21.009 0.200 1 72 8 8 VAL N N 125.483 0.200 1 73 9 9 ILE H H 9.162 0.020 1 74 9 9 ILE HA H 5.090 0.020 1 75 9 9 ILE HB H 1.791 0.020 1 76 9 9 ILE HG12 H 0.911 0.020 1 77 9 9 ILE HG2 H 1.048 0.020 1 78 9 9 ILE HD1 H 0.364 0.020 1 79 9 9 ILE CA C 60.036 0.200 1 80 9 9 ILE CB C 41.275 0.200 1 81 9 9 ILE CG1 C 27.200 0.200 1 82 9 9 ILE CG2 C 18.472 0.200 1 83 9 9 ILE CD1 C 14.224 0.200 1 84 9 9 ILE N N 128.156 0.200 1 85 10 10 TRP H H 9.064 0.020 1 86 10 10 TRP HA H 6.177 0.020 1 87 10 10 TRP HB3 H 3.279 0.020 1 88 10 10 TRP HD1 H 7.278 0.020 1 89 10 10 TRP HE1 H 10.651 0.020 1 90 10 10 TRP HE3 H 7.471 0.020 1 91 10 10 TRP HH2 H 7.099 0.020 1 92 10 10 TRP CA C 54.154 0.200 1 93 10 10 TRP CB C 32.648 0.200 1 94 10 10 TRP CD1 C 127.406 0.200 1 95 10 10 TRP CE3 C 120.482 0.200 1 96 10 10 TRP CH2 C 124.408 0.200 1 97 10 10 TRP N N 126.723 0.200 1 98 10 10 TRP NE1 N 129.095 0.200 1 99 11 11 ILE H H 8.761 0.020 1 100 11 11 ILE HA H 4.837 0.020 1 101 11 11 ILE HB H 1.460 0.020 1 102 11 11 ILE HG2 H 0.145 0.020 1 103 11 11 ILE HD1 H 0.706 0.020 1 104 11 11 ILE CA C 59.938 0.200 1 105 11 11 ILE CB C 41.608 0.200 1 106 11 11 ILE CG2 C 12.958 0.200 1 107 11 11 ILE CD1 C 14.608 0.200 1 108 11 11 ILE N N 122.045 0.200 1 109 12 12 ASN H H 8.924 0.020 1 110 12 12 ASN HA H 4.768 0.020 1 111 12 12 ASN HB2 H 3.016 0.020 1 112 12 12 ASN CA C 54.201 0.200 1 113 12 12 ASN CB C 39.761 0.200 1 114 12 12 ASN N N 122.679 0.200 1 115 13 13 GLY H H 8.266 0.020 1 116 13 13 GLY HA3 H 3.875 0.020 1 117 13 13 GLY CA C 46.341 0.200 1 118 13 13 GLY N N 106.270 0.200 1 119 14 14 ASP H H 7.955 0.020 1 120 14 14 ASP HA H 4.797 0.020 1 121 14 14 ASP HB2 H 2.995 0.020 1 122 14 14 ASP CA C 53.078 0.200 1 123 14 14 ASP CB C 39.736 0.200 1 124 14 14 ASP N N 116.657 0.200 1 125 15 15 LYS H H 7.605 0.020 1 126 15 15 LYS HA H 4.563 0.020 1 127 15 15 LYS HB3 H 1.607 0.020 1 128 15 15 LYS HG3 H 1.332 0.020 1 129 15 15 LYS HD3 H 1.528 0.020 1 130 15 15 LYS HE2 H 2.750 0.020 1 131 15 15 LYS CA C 52.984 0.200 1 132 15 15 LYS CB C 33.033 0.200 1 133 15 15 LYS CG C 23.951 0.200 1 134 15 15 LYS CD C 27.268 0.200 1 135 15 15 LYS CE C 42.049 0.200 1 136 15 15 LYS N N 118.560 0.200 1 137 16 16 GLY H H 8.792 0.020 1 138 16 16 GLY HA3 H 3.671 0.020 1 139 16 16 GLY CA C 48.036 0.200 1 140 16 16 GLY N N 107.836 0.200 1 141 17 17 TYR H H 8.254 0.020 1 142 17 17 TYR HA H 4.044 0.020 1 143 17 17 TYR HB3 H 2.529 0.020 1 144 17 17 TYR CA C 59.880 0.200 1 145 17 17 TYR CB C 37.681 0.200 1 146 17 17 TYR N N 120.527 0.200 1 147 18 18 ASN H H 8.139 0.020 1 148 18 18 ASN HA H 4.650 0.020 1 149 18 18 ASN HB2 H 2.739 0.020 1 150 18 18 ASN HD21 H 7.832 0.020 2 151 18 18 ASN HD22 H 6.712 0.020 2 152 18 18 ASN CA C 56.136 0.200 1 153 18 18 ASN CB C 37.445 0.200 1 154 18 18 ASN N N 123.423 0.200 1 155 18 18 ASN ND2 N 115.263 0.200 1 156 19 19 GLY H H 8.964 0.020 1 157 19 19 GLY HA3 H 3.884 0.020 1 158 19 19 GLY CA C 47.366 0.200 1 159 19 19 GLY N N 111.405 0.200 1 160 20 20 LEU H H 8.366 0.020 1 161 20 20 LEU HA H 4.044 0.020 1 162 20 20 LEU HB3 H 1.904 0.020 1 163 20 20 LEU HG H 1.578 0.020 1 164 20 20 LEU HD1 H 0.884 0.020 1 165 20 20 LEU CA C 57.695 0.200 1 166 20 20 LEU CB C 41.380 0.200 1 167 20 20 LEU CG C 27.279 0.200 1 168 20 20 LEU CD1 C 24.423 0.200 1 169 20 20 LEU N N 121.802 0.200 1 170 21 21 ALA H H 8.141 0.020 1 171 21 21 ALA HA H 4.088 0.020 1 172 21 21 ALA HB H 1.687 0.020 1 173 21 21 ALA CA C 55.217 0.200 1 174 21 21 ALA CB C 17.323 0.200 1 175 21 21 ALA N N 121.067 0.200 1 176 22 22 GLU H H 7.841 0.020 1 177 22 22 GLU HA H 4.176 0.020 1 178 22 22 GLU HB2 H 2.459 0.020 1 179 22 22 GLU HG2 H 2.412 0.020 1 180 22 22 GLU CA C 59.836 0.200 1 181 22 22 GLU CB C 28.645 0.200 1 182 22 22 GLU CG C 35.676 0.200 1 183 22 22 GLU N N 120.409 0.200 1 184 23 23 VAL H H 7.873 0.020 1 185 23 23 VAL HA H 3.803 0.020 1 186 23 23 VAL HB H 2.449 0.020 1 187 23 23 VAL HG2 H 1.269 0.020 1 188 23 23 VAL CA C 66.910 0.200 1 189 23 23 VAL CB C 31.275 0.200 1 190 23 23 VAL CG2 C 23.137 0.200 1 191 23 23 VAL N N 123.089 0.200 1 192 24 24 GLY H H 8.748 0.020 1 193 24 24 GLY HA3 H 3.778 0.020 1 194 24 24 GLY CA C 47.579 0.200 1 195 24 24 GLY N N 106.603 0.200 1 196 25 25 LYS H H 8.349 0.020 1 197 25 25 LYS HA H 4.277 0.020 1 198 25 25 LYS HB3 H 1.993 0.020 1 199 25 25 LYS HG3 H 1.733 0.020 1 200 25 25 LYS HD3 H 1.801 0.020 1 201 25 25 LYS HE2 H 3.022 0.020 1 202 25 25 LYS CA C 59.382 0.200 1 203 25 25 LYS CB C 31.844 0.200 1 204 25 25 LYS CG C 24.924 0.200 1 205 25 25 LYS CD C 28.621 0.200 1 206 25 25 LYS CE C 41.980 0.200 1 207 25 25 LYS N N 122.700 0.200 1 208 26 26 LYS H H 7.711 0.020 1 209 26 26 LYS HA H 4.192 0.020 1 210 26 26 LYS HB3 H 2.346 0.020 1 211 26 26 LYS HG3 H 1.770 0.020 1 212 26 26 LYS HD3 H 1.832 0.020 1 213 26 26 LYS HE2 H 3.108 0.020 1 214 26 26 LYS CA C 59.818 0.200 1 215 26 26 LYS CB C 32.111 0.200 1 216 26 26 LYS CG C 25.086 0.200 1 217 26 26 LYS CD C 29.111 0.200 1 218 26 26 LYS CE C 42.126 0.200 1 219 26 26 LYS N N 122.772 0.200 1 220 27 27 PHE H H 8.152 0.020 1 221 27 27 PHE HA H 3.784 0.020 1 222 27 27 PHE HB3 H 3.301 0.020 1 223 27 27 PHE HE1 H 6.929 0.020 1 224 27 27 PHE HE2 H 6.929 0.020 1 225 27 27 PHE CA C 61.542 0.200 1 226 27 27 PHE CB C 39.211 0.200 1 227 27 27 PHE CE1 C 130.783 0.200 1 228 27 27 PHE N N 120.075 0.200 1 229 28 28 GLU H H 8.922 0.020 1 230 28 28 GLU HA H 4.024 0.020 1 231 28 28 GLU HB2 H 2.464 0.020 1 232 28 28 GLU HG2 H 2.032 0.020 1 233 28 28 GLU CA C 58.999 0.200 1 234 28 28 GLU CB C 29.815 0.200 1 235 28 28 GLU CG C 35.110 0.200 1 236 28 28 GLU N N 124.100 0.200 1 237 29 29 LYS H H 8.171 0.020 1 238 29 29 LYS HA H 4.018 0.020 1 239 29 29 LYS HB3 H 2.115 0.020 1 240 29 29 LYS HG3 H 1.588 0.020 1 241 29 29 LYS HD3 H 1.727 0.020 1 242 29 29 LYS HE2 H 3.045 0.020 1 243 29 29 LYS CA C 59.423 0.200 1 244 29 29 LYS CB C 31.431 0.200 1 245 29 29 LYS CG C 24.262 0.200 1 246 29 29 LYS CD C 29.624 0.200 1 247 29 29 LYS CE C 42.073 0.200 1 248 29 29 LYS N N 121.988 0.200 1 249 30 30 ASP H H 7.641 0.020 1 250 30 30 ASP HA H 4.584 0.020 1 251 30 30 ASP HB2 H 2.821 0.020 1 252 30 30 ASP CA C 56.579 0.200 1 253 30 30 ASP CB C 40.940 0.200 1 254 30 30 ASP N N 116.464 0.200 1 255 31 31 THR H H 7.956 0.020 1 256 31 31 THR HA H 4.387 0.020 1 257 31 31 THR HB H 3.833 0.020 1 258 31 31 THR HG2 H 0.542 0.020 1 259 31 31 THR CA C 62.769 0.200 1 260 31 31 THR CB C 72.298 0.200 1 261 31 31 THR CG2 C 19.733 0.200 1 262 31 31 THR N N 107.078 0.200 1 263 32 32 GLY H H 8.637 0.020 1 264 32 32 GLY HA3 H 4.228 0.020 1 265 32 32 GLY CA C 45.328 0.200 1 266 32 32 GLY N N 112.604 0.200 1 267 33 33 ILE H H 7.787 0.020 1 268 33 33 ILE HA H 3.930 0.020 1 269 33 33 ILE HB H 1.977 0.020 1 270 33 33 ILE HG12 H 1.132 0.020 1 271 33 33 ILE HG2 H 0.699 0.020 1 272 33 33 ILE HD1 H 0.609 0.020 1 273 33 33 ILE CA C 58.942 0.200 1 274 33 33 ILE CB C 35.992 0.200 1 275 33 33 ILE CG1 C 25.544 0.200 1 276 33 33 ILE CG2 C 16.367 0.200 1 277 33 33 ILE CD1 C 10.017 0.200 1 278 33 33 ILE N N 124.244 0.200 1 279 34 34 LYS H H 7.916 0.020 1 280 34 34 LYS HA H 4.012 0.020 1 281 34 34 LYS HB3 H 1.699 0.020 1 282 34 34 LYS HG3 H 1.455 0.020 1 283 34 34 LYS HD3 H 1.644 0.020 1 284 34 34 LYS HE2 H 3.002 0.020 1 285 34 34 LYS CA C 56.764 0.200 1 286 34 34 LYS CB C 32.874 0.200 1 287 34 34 LYS CG C 24.479 0.200 1 288 34 34 LYS CD C 28.526 0.200 1 289 34 34 LYS CE C 41.810 0.200 1 290 34 34 LYS N N 124.837 0.200 1 291 35 35 VAL H H 8.392 0.020 1 292 35 35 VAL HA H 4.796 0.020 1 293 35 35 VAL HB H 1.768 0.020 1 294 35 35 VAL HG2 H 0.784 0.020 1 295 35 35 VAL CA C 60.957 0.200 1 296 35 35 VAL CB C 33.149 0.200 1 297 35 35 VAL CG2 C 22.073 0.200 1 298 35 35 VAL N N 124.409 0.200 1 299 36 36 THR H H 9.199 0.020 1 300 36 36 THR HA H 4.625 0.020 1 301 36 36 THR HB H 4.060 0.020 1 302 36 36 THR HG2 H 1.278 0.020 1 303 36 36 THR CA C 61.494 0.200 1 304 36 36 THR CB C 71.094 0.200 1 305 36 36 THR CG2 C 21.475 0.200 1 306 36 36 THR N N 125.117 0.200 1 307 37 37 VAL H H 8.922 0.020 1 308 37 37 VAL HA H 4.774 0.020 1 309 37 37 VAL HB H 2.115 0.020 1 310 37 37 VAL HG2 H 0.779 0.020 1 311 37 37 VAL CA C 61.608 0.200 1 312 37 37 VAL CB C 32.243 0.200 1 313 37 37 VAL CG2 C 20.370 0.200 1 314 37 37 VAL N N 127.333 0.200 1 315 38 38 GLU H H 9.672 0.020 1 316 38 38 GLU HA H 4.633 0.020 1 317 38 38 GLU HB2 H 2.011 0.020 1 318 38 38 GLU HG2 H 2.130 0.020 1 319 38 38 GLU CA C 54.216 0.200 1 320 38 38 GLU CB C 33.331 0.200 1 321 38 38 GLU CG C 36.025 0.200 1 322 38 38 GLU N N 127.098 0.200 1 323 39 39 HIS H H 8.384 0.020 1 324 39 39 HIS HA H 5.735 0.020 1 325 39 39 HIS HB3 H 2.535 0.020 1 326 39 39 HIS HD2 H 6.130 0.020 1 327 39 39 HIS CA C 51.284 0.200 1 328 39 39 HIS CB C 28.568 0.200 1 329 39 39 HIS CD2 C 121.353 0.200 1 330 39 39 HIS N N 115.041 0.200 1 331 40 40 PRO HA H 4.082 0.020 1 332 40 40 PRO HB2 H 0.969 0.020 1 333 40 40 PRO HG2 H 0.099 0.020 1 334 40 40 PRO HD3 H 2.787 0.020 1 335 40 40 PRO CA C 62.323 0.200 1 336 40 40 PRO CB C 30.826 0.200 1 337 40 40 PRO CG C 24.911 0.200 1 338 40 40 PRO CD C 49.000 0.200 1 339 41 41 ASP H H 8.262 0.020 1 340 41 41 ASP HA H 4.473 0.020 1 341 41 41 ASP HB2 H 2.518 0.020 1 342 41 41 ASP CA C 54.890 0.200 1 343 41 41 ASP CB C 41.037 0.200 1 344 41 41 ASP N N 121.249 0.200 1 345 42 42 LYS H H 8.807 0.020 1 346 42 42 LYS HA H 4.194 0.020 1 347 42 42 LYS HB3 H 1.789 0.020 1 348 42 42 LYS HG3 H 1.328 0.020 1 349 42 42 LYS HD3 H 1.654 0.020 1 350 42 42 LYS HE2 H 2.965 0.020 1 351 42 42 LYS CA C 56.539 0.200 1 352 42 42 LYS CB C 29.526 0.200 1 353 42 42 LYS CG C 24.514 0.200 1 354 42 42 LYS CD C 28.673 0.200 1 355 42 42 LYS CE C 42.029 0.200 1 356 42 42 LYS N N 119.186 0.200 1 357 43 43 LEU H H 7.463 0.020 1 358 43 43 LEU HA H 3.505 0.020 1 359 43 43 LEU HB3 H 1.748 0.020 1 360 43 43 LEU HG H 1.938 0.020 1 361 43 43 LEU HD1 H 1.135 0.020 1 362 43 43 LEU CA C 59.669 0.200 1 363 43 43 LEU CB C 40.973 0.200 1 364 43 43 LEU CG C 26.288 0.200 1 365 43 43 LEU CD1 C 26.338 0.200 1 366 43 43 LEU N N 119.987 0.200 1 367 44 44 GLU H H 10.509 0.020 1 368 44 44 GLU HA H 3.897 0.020 1 369 44 44 GLU HB2 H 0.835 0.020 1 370 44 44 GLU HG2 H 1.843 0.020 1 371 44 44 GLU CA C 57.199 0.200 1 372 44 44 GLU CB C 24.767 0.200 1 373 44 44 GLU CG C 35.661 0.200 1 374 44 44 GLU N N 123.756 0.200 1 375 45 45 GLU H H 7.383 0.020 1 376 45 45 GLU HA H 4.503 0.020 1 377 45 45 GLU HB2 H 1.905 0.020 1 378 45 45 GLU HG2 H 2.094 0.020 1 379 45 45 GLU CA C 56.582 0.200 1 380 45 45 GLU CB C 30.109 0.200 1 381 45 45 GLU CG C 35.893 0.200 1 382 45 45 GLU N N 120.446 0.200 1 383 46 46 LYS H H 8.283 0.020 1 384 46 46 LYS HA H 4.221 0.020 1 385 46 46 LYS HB3 H 1.922 0.020 1 386 46 46 LYS HG3 H 1.561 0.020 1 387 46 46 LYS HD3 H 1.479 0.020 1 388 46 46 LYS HE2 H 2.939 0.020 1 389 46 46 LYS CA C 58.580 0.200 1 390 46 46 LYS CB C 33.479 0.200 1 391 46 46 LYS CG C 25.098 0.200 1 392 46 46 LYS CD C 28.469 0.200 1 393 46 46 LYS CE C 41.996 0.200 1 394 46 46 LYS N N 120.307 0.200 1 395 47 47 PHE H H 8.695 0.020 1 396 47 47 PHE HA H 4.302 0.020 1 397 47 47 PHE HE1 H 6.489 0.020 1 398 47 47 PHE HE2 H 6.489 0.020 1 399 47 47 PHE CA C 63.688 0.200 1 400 47 47 PHE CE1 C 130.148 0.200 1 401 47 47 PHE N N 116.985 0.200 1 402 48 48 PRO HA H 3.743 0.020 1 403 48 48 PRO HB2 H 1.873 0.020 1 404 48 48 PRO HG2 H 2.205 0.020 1 405 48 48 PRO HD3 H 3.322 0.020 1 406 48 48 PRO CA C 65.538 0.200 1 407 48 48 PRO CB C 30.007 0.200 1 408 48 48 PRO CG C 28.033 0.200 1 409 48 48 PRO CD C 49.347 0.200 1 410 49 49 GLN H H 6.895 0.020 1 411 49 49 GLN HA H 4.143 0.020 1 412 49 49 GLN HB2 H 2.272 0.020 1 413 49 49 GLN HG2 H 2.347 0.020 1 414 49 49 GLN HE21 H 7.345 0.020 2 415 49 49 GLN HE22 H 6.783 0.020 2 416 49 49 GLN CA C 58.156 0.200 1 417 49 49 GLN CB C 28.605 0.200 1 418 49 49 GLN CG C 33.498 0.200 1 419 49 49 GLN N N 114.877 0.200 1 420 49 49 GLN NE2 N 111.127 0.200 1 421 50 50 VAL H H 7.712 0.020 1 422 50 50 VAL HA H 4.372 0.020 1 423 50 50 VAL HB H 2.014 0.020 1 424 50 50 VAL HG2 H 0.916 0.020 1 425 50 50 VAL CA C 62.300 0.200 1 426 50 50 VAL CB C 32.136 0.200 1 427 50 50 VAL CG2 C 19.593 0.200 1 428 50 50 VAL N N 110.874 0.200 1 429 51 51 ALA H H 8.326 0.020 1 430 51 51 ALA HA H 3.979 0.020 1 431 51 51 ALA HB H 0.579 0.020 1 432 51 51 ALA CA C 54.830 0.200 1 433 51 51 ALA CB C 17.545 0.200 1 434 51 51 ALA N N 125.556 0.200 1 435 52 52 ALA H H 7.490 0.020 1 436 52 52 ALA HA H 4.156 0.020 1 437 52 52 ALA HB H 1.407 0.020 1 438 52 52 ALA CA C 53.358 0.200 1 439 52 52 ALA CB C 18.071 0.200 1 440 52 52 ALA N N 117.927 0.200 1 441 53 53 THR H H 7.293 0.020 1 442 53 53 THR HA H 4.519 0.020 1 443 53 53 THR HB H 4.537 0.020 1 444 53 53 THR HG2 H 1.207 0.020 1 445 53 53 THR CA C 61.176 0.200 1 446 53 53 THR CB C 70.016 0.200 1 447 53 53 THR CG2 C 21.240 0.200 1 448 53 53 THR N N 106.235 0.200 1 449 54 54 GLY H H 7.854 0.020 1 450 54 54 GLY HA3 H 4.177 0.020 1 451 54 54 GLY CA C 45.501 0.200 1 452 54 54 GLY N N 108.765 0.200 1 453 55 55 ASP H H 7.500 0.020 1 454 55 55 ASP HA H 4.888 0.020 1 455 55 55 ASP HB2 H 2.327 0.020 1 456 55 55 ASP CA C 52.584 0.200 1 457 55 55 ASP CB C 43.196 0.200 1 458 55 55 ASP N N 119.342 0.200 1 459 56 56 GLY H H 8.352 0.020 1 460 56 56 GLY HA3 H 3.495 0.020 1 461 56 56 GLY CA C 43.654 0.200 1 462 56 56 GLY N N 105.696 0.200 1 463 57 57 PRO HA H 4.003 0.020 1 464 57 57 PRO HB2 H 1.749 0.020 1 465 57 57 PRO HG2 H 1.209 0.020 1 466 57 57 PRO CA C 61.604 0.200 1 467 57 57 PRO CB C 30.679 0.200 1 468 57 57 PRO CG C 26.095 0.200 1 469 58 58 ASP H H 8.779 0.020 1 470 58 58 ASP HA H 4.507 0.020 1 471 58 58 ASP HB2 H 2.613 0.020 1 472 58 58 ASP CA C 58.424 0.200 1 473 58 58 ASP CB C 43.969 0.200 1 474 58 58 ASP N N 117.810 0.200 1 475 59 59 ILE H H 7.690 0.020 1 476 59 59 ILE HA H 5.310 0.020 1 477 59 59 ILE HB H 1.651 0.020 1 478 59 59 ILE HG2 H 0.879 0.020 1 479 59 59 ILE HD1 H 0.767 0.020 1 480 59 59 ILE CA C 58.949 0.200 1 481 59 59 ILE CB C 42.839 0.200 1 482 59 59 ILE CG2 C 18.604 0.200 1 483 59 59 ILE CD1 C 13.565 0.200 1 484 59 59 ILE N N 114.149 0.200 1 485 60 60 ILE H H 8.949 0.020 1 486 60 60 ILE HA H 5.412 0.020 1 487 60 60 ILE HB H 1.108 0.020 1 488 60 60 ILE HG12 H 0.861 0.020 1 489 60 60 ILE HG2 H 0.077 0.020 1 490 60 60 ILE HD1 H 0.480 0.020 1 491 60 60 ILE CA C 57.867 0.200 1 492 60 60 ILE CB C 41.613 0.200 1 493 60 60 ILE CG1 C 28.775 0.200 1 494 60 60 ILE CG2 C 13.551 0.200 1 495 60 60 ILE CD1 C 14.391 0.200 1 496 60 60 ILE N N 124.372 0.200 1 497 61 61 PHE H H 8.690 0.020 1 498 61 61 PHE HA H 6.384 0.020 1 499 61 61 PHE HB3 H 2.794 0.020 1 500 61 61 PHE HE1 H 7.148 0.020 1 501 61 61 PHE HE2 H 7.148 0.020 1 502 61 61 PHE CA C 55.700 0.200 1 503 61 61 PHE CB C 41.925 0.200 1 504 61 61 PHE CE1 C 130.711 0.200 1 505 61 61 PHE N N 126.160 0.200 1 506 62 62 TRP H H 9.212 0.020 1 507 62 62 TRP HA H 4.353 0.020 1 508 62 62 TRP HB3 H 2.942 0.020 1 509 62 62 TRP HD1 H 7.651 0.020 1 510 62 62 TRP HE1 H 10.370 0.020 1 511 62 62 TRP HE3 H 7.647 0.020 1 512 62 62 TRP HH2 H 7.279 0.020 1 513 62 62 TRP CA C 57.381 0.200 1 514 62 62 TRP CB C 31.732 0.200 1 515 62 62 TRP CD1 C 128.228 0.200 1 516 62 62 TRP CE3 C 120.295 0.200 1 517 62 62 TRP CH2 C 125.880 0.200 1 518 62 62 TRP N N 121.274 0.200 1 519 62 62 TRP NE1 N 129.076 0.200 1 520 63 63 ALA H H 6.405 0.020 1 521 63 63 ALA HA H 4.119 0.020 1 522 63 63 ALA HB H 1.120 0.020 1 523 63 63 ALA CA C 53.864 0.200 1 524 63 63 ALA CB C 18.700 0.200 1 525 63 63 ALA N N 126.176 0.200 1 526 64 64 HIS H H 8.142 0.020 1 527 64 64 HIS HA H 3.785 0.020 1 528 64 64 HIS HB3 H 3.484 0.020 1 529 64 64 HIS HD2 H 7.266 0.020 1 530 64 64 HIS CA C 60.273 0.200 1 531 64 64 HIS CB C 30.164 0.200 1 532 64 64 HIS CD2 C 119.785 0.200 1 533 64 64 HIS N N 116.177 0.200 1 534 65 65 ASP H H 7.741 0.020 1 535 65 65 ASP HA H 3.760 0.020 1 536 65 65 ASP HB2 H 2.719 0.020 1 537 65 65 ASP CA C 56.458 0.200 1 538 65 65 ASP CB C 39.109 0.200 1 539 65 65 ASP N N 119.134 0.200 1 540 66 66 ARG H H 7.039 0.020 1 541 66 66 ARG HA H 4.191 0.020 1 542 66 66 ARG HB3 H 1.598 0.020 1 543 66 66 ARG HD2 H 2.988 0.020 1 544 66 66 ARG CA C 54.867 0.200 1 545 66 66 ARG CB C 29.939 0.200 1 546 66 66 ARG CD C 40.844 0.200 1 547 66 66 ARG N N 116.783 0.200 1 548 67 67 PHE H H 7.698 0.020 1 549 67 67 PHE HA H 4.145 0.020 1 550 67 67 PHE HB3 H 3.066 0.020 1 551 67 67 PHE HE1 H 7.137 0.020 1 552 67 67 PHE HE2 H 7.137 0.020 1 553 67 67 PHE CA C 58.444 0.200 1 554 67 67 PHE CB C 36.489 0.200 1 555 67 67 PHE CE1 C 131.112 0.200 1 556 67 67 PHE N N 116.588 0.200 1 557 68 68 GLY H H 7.368 0.020 1 558 68 68 GLY HA3 H 4.431 0.020 1 559 68 68 GLY CA C 47.430 0.200 1 560 68 68 GLY N N 107.195 0.200 1 561 69 69 GLY H H 7.790 0.020 1 562 69 69 GLY HA3 H 3.909 0.020 1 563 69 69 GLY CA C 46.778 0.200 1 564 69 69 GLY N N 107.416 0.200 1 565 70 70 TYR H H 6.951 0.020 1 566 70 70 TYR HA H 4.705 0.020 1 567 70 70 TYR HB3 H 3.080 0.020 1 568 70 70 TYR HE1 H 6.579 0.020 1 569 70 70 TYR HE2 H 6.579 0.020 1 570 70 70 TYR CA C 57.098 0.200 1 571 70 70 TYR CB C 35.791 0.200 1 572 70 70 TYR CE1 C 118.476 0.200 1 573 70 70 TYR N N 119.016 0.200 1 574 71 71 ALA H H 8.639 0.020 1 575 71 71 ALA HA H 4.477 0.020 1 576 71 71 ALA HB H 1.332 0.020 1 577 71 71 ALA CA C 54.428 0.200 1 578 71 71 ALA CB C 17.904 0.200 1 579 71 71 ALA N N 122.656 0.200 1 580 72 72 GLN H H 8.697 0.020 1 581 72 72 GLN HA H 4.183 0.020 1 582 72 72 GLN HB2 H 2.428 0.020 1 583 72 72 GLN HG2 H 2.594 0.020 1 584 72 72 GLN HE21 H 7.694 0.020 2 585 72 72 GLN HE22 H 7.045 0.020 2 586 72 72 GLN CA C 58.619 0.200 1 587 72 72 GLN CB C 27.647 0.200 1 588 72 72 GLN CG C 33.138 0.200 1 589 72 72 GLN N N 122.561 0.200 1 590 72 72 GLN NE2 N 113.079 0.200 1 591 73 73 SER H H 7.369 0.020 1 592 73 73 SER HA H 4.616 0.020 1 593 73 73 SER HB2 H 3.957 0.020 1 594 73 73 SER CA C 59.136 0.200 1 595 73 73 SER CB C 64.054 0.200 1 596 73 73 SER N N 112.035 0.200 1 597 74 74 GLY H H 8.096 0.020 1 598 74 74 GLY HA3 H 4.063 0.020 1 599 74 74 GLY CA C 46.261 0.200 1 600 74 74 GLY N N 109.189 0.200 1 601 75 75 LEU H H 7.861 0.020 1 602 75 75 LEU HA H 4.242 0.020 1 603 75 75 LEU HB3 H 1.454 0.020 1 604 75 75 LEU HG H 1.893 0.020 1 605 75 75 LEU HD1 H 0.688 0.020 1 606 75 75 LEU CA C 55.550 0.200 1 607 75 75 LEU CB C 42.571 0.200 1 608 75 75 LEU CG C 27.315 0.200 1 609 75 75 LEU CD1 C 25.434 0.200 1 610 75 75 LEU N N 113.801 0.200 1 611 76 76 LEU H H 7.424 0.020 1 612 76 76 LEU HA H 5.264 0.020 1 613 76 76 LEU HB3 H 1.948 0.020 1 614 76 76 LEU HG H 1.314 0.020 1 615 76 76 LEU HD1 H 0.878 0.020 1 616 76 76 LEU CA C 52.442 0.200 1 617 76 76 LEU CB C 43.753 0.200 1 618 76 76 LEU CG C 26.990 0.200 1 619 76 76 LEU CD1 C 26.845 0.200 1 620 76 76 LEU N N 115.778 0.200 1 621 77 77 ALA H H 9.048 0.020 1 622 77 77 ALA HA H 4.316 0.020 1 623 77 77 ALA HB H 1.211 0.020 1 624 77 77 ALA CA C 50.964 0.200 1 625 77 77 ALA CB C 19.017 0.200 1 626 77 77 ALA N N 125.879 0.200 1 627 78 78 GLU H H 8.249 0.020 1 628 78 78 GLU HA H 4.435 0.020 1 629 78 78 GLU HB2 H 1.975 0.020 1 630 78 78 GLU CA C 56.027 0.200 1 631 78 78 GLU CB C 29.543 0.200 1 632 78 78 GLU N N 120.903 0.200 1 633 79 79 ILE H H 8.211 0.020 1 634 79 79 ILE HA H 4.581 0.020 1 635 79 79 ILE HB H 1.652 0.020 1 636 79 79 ILE HG12 H 0.687 0.020 1 637 79 79 ILE HG2 H 0.730 0.020 1 638 79 79 ILE HD1 H 0.170 0.020 1 639 79 79 ILE CA C 59.742 0.200 1 640 79 79 ILE CB C 39.428 0.200 1 641 79 79 ILE CG1 C 26.020 0.200 1 642 79 79 ILE CG2 C 18.032 0.200 1 643 79 79 ILE CD1 C 12.198 0.200 1 644 79 79 ILE N N 122.343 0.200 1 645 80 80 THR H H 8.799 0.020 1 646 80 80 THR HA H 4.698 0.020 1 647 80 80 THR HB H 4.390 0.020 1 648 80 80 THR HG2 H 1.012 0.020 1 649 80 80 THR CA C 57.917 0.200 1 650 80 80 THR CB C 69.317 0.200 1 651 80 80 THR CG2 C 20.539 0.200 1 652 80 80 THR N N 112.312 0.200 1 653 81 81 PRO HA H 4.482 0.020 1 654 81 81 PRO HB2 H 1.911 0.020 1 655 81 81 PRO HG2 H 2.028 0.020 1 656 81 81 PRO HD3 H 3.409 0.020 1 657 81 81 PRO CA C 64.706 0.200 1 658 81 81 PRO CB C 31.788 0.200 1 659 81 81 PRO CG C 26.841 0.200 1 660 81 81 PRO CD C 49.343 0.200 1 661 82 82 ASP H H 7.540 0.020 1 662 82 82 ASP HA H 5.165 0.020 1 663 82 82 ASP HB2 H 2.544 0.020 1 664 82 82 ASP CA C 49.594 0.200 1 665 82 82 ASP CB C 39.915 0.200 1 666 82 82 ASP N N 112.781 0.200 1 667 83 83 LYS H H 8.098 0.020 1 668 83 83 LYS HA H 3.760 0.020 1 669 83 83 LYS HB3 H 1.808 0.020 1 670 83 83 LYS HG3 H 1.447 0.020 1 671 83 83 LYS HD3 H 1.579 0.020 1 672 83 83 LYS HE2 H 3.011 0.020 1 673 83 83 LYS CA C 59.849 0.200 1 674 83 83 LYS CB C 31.836 0.200 1 675 83 83 LYS CG C 24.261 0.200 1 676 83 83 LYS CD C 28.155 0.200 1 677 83 83 LYS CE C 41.968 0.200 1 678 83 83 LYS N N 120.766 0.200 1 679 84 84 ALA H H 8.235 0.020 1 680 84 84 ALA HA H 4.157 0.020 1 681 84 84 ALA HB H 1.475 0.020 1 682 84 84 ALA CA C 54.855 0.200 1 683 84 84 ALA CB C 17.451 0.200 1 684 84 84 ALA N N 119.378 0.200 1 685 85 85 PHE H H 7.980 0.020 1 686 85 85 PHE HA H 4.119 0.020 1 687 85 85 PHE HB3 H 3.187 0.020 1 688 85 85 PHE HE1 H 7.807 0.020 1 689 85 85 PHE HE2 H 7.807 0.020 1 690 85 85 PHE CA C 62.308 0.200 1 691 85 85 PHE CB C 39.282 0.200 1 692 85 85 PHE CE1 C 130.698 0.200 1 693 85 85 PHE N N 118.448 0.200 1 694 86 86 GLN H H 8.537 0.020 1 695 86 86 GLN HA H 4.245 0.020 1 696 86 86 GLN HB2 H 1.914 0.020 1 697 86 86 GLN HG2 H 0.994 0.020 1 698 86 86 GLN HE21 H 6.591 0.020 2 699 86 86 GLN HE22 H 6.401 0.020 2 700 86 86 GLN CA C 59.784 0.200 1 701 86 86 GLN CB C 28.322 0.200 1 702 86 86 GLN CG C 33.713 0.200 1 703 86 86 GLN N N 117.129 0.200 1 704 86 86 GLN NE2 N 110.302 0.200 1 705 87 87 ASP H H 8.107 0.020 1 706 87 87 ASP HA H 4.664 0.020 1 707 87 87 ASP HB2 H 2.711 0.020 1 708 87 87 ASP CA C 56.125 0.200 1 709 87 87 ASP CB C 40.890 0.200 1 710 87 87 ASP N N 116.901 0.200 1 711 88 88 LYS H H 7.847 0.020 1 712 88 88 LYS HA H 4.129 0.020 1 713 88 88 LYS HB3 H 1.679 0.020 1 714 88 88 LYS HG3 H 1.762 0.020 1 715 88 88 LYS HD3 H 1.629 0.020 1 716 88 88 LYS HE2 H 2.921 0.020 1 717 88 88 LYS CA C 58.166 0.200 1 718 88 88 LYS CB C 32.044 0.200 1 719 88 88 LYS CG C 25.354 0.200 1 720 88 88 LYS CD C 29.367 0.200 1 721 88 88 LYS CE C 41.959 0.200 1 722 88 88 LYS N N 117.112 0.200 1 723 89 89 LEU H H 7.703 0.020 1 724 89 89 LEU HA H 5.315 0.020 1 725 89 89 LEU HB3 H 1.189 0.020 1 726 89 89 LEU HG H 1.357 0.020 1 727 89 89 LEU HD1 H 0.575 0.020 1 728 89 89 LEU CA C 53.438 0.200 1 729 89 89 LEU CB C 42.716 0.200 1 730 89 89 LEU CG C 28.469 0.200 1 731 89 89 LEU CD1 C 25.764 0.200 1 732 89 89 LEU N N 120.000 0.200 1 733 90 90 TYR H H 7.766 0.020 1 734 90 90 TYR HA H 4.304 0.020 1 735 90 90 TYR HB3 H 3.041 0.020 1 736 90 90 TYR CA C 59.126 0.200 1 737 90 90 TYR CB C 39.045 0.200 1 738 90 90 TYR N N 117.027 0.200 1 739 91 91 PRO HA H 4.636 0.020 1 740 91 91 PRO HB2 H 2.369 0.020 1 741 91 91 PRO HG2 H 2.432 0.020 1 742 91 91 PRO HD3 H 4.237 0.020 1 743 91 91 PRO CA C 66.827 0.200 1 744 91 91 PRO CB C 31.570 0.200 1 745 91 91 PRO CG C 27.062 0.200 1 746 91 91 PRO CD C 51.248 0.200 1 747 92 92 PHE H H 8.069 0.020 1 748 92 92 PHE HA H 4.748 0.020 1 749 92 92 PHE HB3 H 3.283 0.020 1 750 92 92 PHE HE1 H 6.899 0.020 1 751 92 92 PHE HE2 H 6.899 0.020 1 752 92 92 PHE CA C 59.294 0.200 1 753 92 92 PHE CB C 36.699 0.200 1 754 92 92 PHE CE1 C 130.393 0.200 1 755 92 92 PHE N N 112.682 0.200 1 756 93 93 THR H H 7.146 0.020 1 757 93 93 THR HA H 3.496 0.020 1 758 93 93 THR HG2 H 0.252 0.020 1 759 93 93 THR CA C 64.761 0.200 1 760 93 93 THR CG2 C 22.615 0.200 1 761 93 93 THR N N 110.914 0.200 1 762 94 94 TRP H H 6.710 0.020 1 763 94 94 TRP HA H 4.656 0.020 1 764 94 94 TRP HB3 H 3.278 0.020 1 765 94 94 TRP HD1 H 7.221 0.020 1 766 94 94 TRP HE1 H 10.526 0.020 1 767 94 94 TRP HE3 H 7.762 0.020 1 768 94 94 TRP CA C 58.524 0.200 1 769 94 94 TRP CB C 29.577 0.200 1 770 94 94 TRP CD1 C 127.993 0.200 1 771 94 94 TRP CE3 C 123.099 0.200 1 772 94 94 TRP N N 119.778 0.200 1 773 94 94 TRP NE1 N 128.542 0.200 1 774 95 95 ASP H H 7.295 0.020 1 775 95 95 ASP HA H 4.485 0.020 1 776 95 95 ASP HB2 H 2.926 0.020 1 777 95 95 ASP CA C 57.232 0.200 1 778 95 95 ASP CB C 39.872 0.200 1 779 95 95 ASP N N 115.541 0.200 1 780 96 96 ALA H H 7.043 0.020 1 781 96 96 ALA HA H 3.980 0.020 1 782 96 96 ALA HB H 0.785 0.020 1 783 96 96 ALA CA C 53.671 0.200 1 784 96 96 ALA CB C 17.737 0.200 1 785 96 96 ALA N N 118.538 0.200 1 786 97 97 VAL H H 7.018 0.020 1 787 97 97 VAL HA H 4.533 0.020 1 788 97 97 VAL HB H 2.724 0.020 1 789 97 97 VAL HG2 H 1.375 0.020 1 790 97 97 VAL CA C 59.692 0.200 1 791 97 97 VAL CB C 30.598 0.200 1 792 97 97 VAL CG2 C 19.189 0.200 1 793 97 97 VAL N N 105.952 0.200 1 794 98 98 ARG H H 7.082 0.020 1 795 98 98 ARG HA H 5.360 0.020 1 796 98 98 ARG HB3 H 1.856 0.020 1 797 98 98 ARG HG3 H 1.663 0.020 1 798 98 98 ARG HD2 H 3.272 0.020 1 799 98 98 ARG CA C 54.808 0.200 1 800 98 98 ARG CB C 31.895 0.200 1 801 98 98 ARG CG C 28.085 0.200 1 802 98 98 ARG CD C 43.129 0.200 1 803 98 98 ARG N N 121.107 0.200 1 804 99 99 TYR H H 9.725 0.020 1 805 99 99 TYR HA H 4.971 0.020 1 806 99 99 TYR HB3 H 2.879 0.020 1 807 99 99 TYR HE1 H 6.852 0.020 1 808 99 99 TYR HE2 H 6.852 0.020 1 809 99 99 TYR CA C 58.404 0.200 1 810 99 99 TYR CB C 42.092 0.200 1 811 99 99 TYR CE1 C 118.275 0.200 1 812 99 99 TYR N N 126.662 0.200 1 813 100 100 ASN H H 7.980 0.020 1 814 100 100 ASN HA H 4.274 0.020 1 815 100 100 ASN HB2 H 2.334 0.020 1 816 100 100 ASN HD21 H 7.366 0.020 2 817 100 100 ASN HD22 H 6.773 0.020 2 818 100 100 ASN CA C 53.791 0.200 1 819 100 100 ASN CB C 37.106 0.200 1 820 100 100 ASN N N 124.739 0.200 1 821 100 100 ASN ND2 N 111.104 0.200 1 822 101 101 GLY H H 8.645 0.020 1 823 101 101 GLY HA3 H 4.265 0.020 1 824 101 101 GLY CA C 45.428 0.200 1 825 101 101 GLY N N 102.085 0.200 1 826 102 102 LYS H H 7.809 0.020 1 827 102 102 LYS HA H 4.702 0.020 1 828 102 102 LYS HB3 H 1.716 0.020 1 829 102 102 LYS HG3 H 1.462 0.020 1 830 102 102 LYS HD3 H 1.637 0.020 1 831 102 102 LYS HE2 H 3.062 0.020 1 832 102 102 LYS CA C 54.563 0.200 1 833 102 102 LYS CB C 34.875 0.200 1 834 102 102 LYS CG C 24.264 0.200 1 835 102 102 LYS CD C 28.613 0.200 1 836 102 102 LYS CE C 42.112 0.200 1 837 102 102 LYS N N 121.140 0.200 1 838 103 103 LEU H H 9.003 0.020 1 839 103 103 LEU HA H 5.087 0.020 1 840 103 103 LEU HB3 H 1.275 0.020 1 841 103 103 LEU HG H 1.735 0.020 1 842 103 103 LEU HD1 H 0.544 0.020 1 843 103 103 LEU CA C 55.144 0.200 1 844 103 103 LEU CB C 42.434 0.200 1 845 103 103 LEU CG C 26.291 0.200 1 846 103 103 LEU CD1 C 24.492 0.200 1 847 103 103 LEU N N 123.389 0.200 1 848 104 104 ILE H H 8.842 0.020 1 849 104 104 ILE HA H 4.941 0.020 1 850 104 104 ILE HB H 2.590 0.020 1 851 104 104 ILE HG12 H 1.234 0.020 1 852 104 104 ILE HG2 H 0.928 0.020 1 853 104 104 ILE HD1 H 0.885 0.020 1 854 104 104 ILE CA C 59.673 0.200 1 855 104 104 ILE CB C 39.313 0.200 1 856 104 104 ILE CG1 C 27.238 0.200 1 857 104 104 ILE CG2 C 20.021 0.200 1 858 104 104 ILE CD1 C 14.459 0.200 1 859 104 104 ILE N N 112.530 0.200 1 860 105 105 ALA H H 7.713 0.020 1 861 105 105 ALA HA H 4.645 0.020 1 862 105 105 ALA HB H 1.446 0.020 1 863 105 105 ALA CA C 52.071 0.200 1 864 105 105 ALA CB C 21.986 0.200 1 865 105 105 ALA N N 117.098 0.200 1 866 106 106 TYR H H 9.013 0.020 1 867 106 106 TYR HA H 4.857 0.020 1 868 106 106 TYR HB3 H 2.717 0.020 1 869 106 106 TYR HE1 H 6.656 0.020 1 870 106 106 TYR HE2 H 6.656 0.020 1 871 106 106 TYR CA C 56.017 0.200 1 872 106 106 TYR CB C 40.203 0.200 1 873 106 106 TYR CE1 C 118.641 0.200 1 874 106 106 TYR N N 113.778 0.200 1 875 107 107 PRO HA H 4.115 0.020 1 876 107 107 PRO HB2 H 1.169 0.020 1 877 107 107 PRO HG2 H 0.831 0.020 1 878 107 107 PRO HD3 H 3.550 0.020 1 879 107 107 PRO CA C 62.308 0.200 1 880 107 107 PRO CB C 32.897 0.200 1 881 107 107 PRO CG C 25.833 0.200 1 882 107 107 PRO CD C 50.616 0.200 1 883 108 108 ILE H H 8.569 0.020 1 884 108 108 ILE HA H 4.406 0.020 1 885 108 108 ILE HB H 2.017 0.020 1 886 108 108 ILE HG12 H 1.838 0.020 1 887 108 108 ILE HG2 H 0.896 0.020 1 888 108 108 ILE HD1 H 0.676 0.020 1 889 108 108 ILE CA C 60.953 0.200 1 890 108 108 ILE CB C 37.953 0.200 1 891 108 108 ILE CG1 C 25.679 0.200 1 892 108 108 ILE CG2 C 16.282 0.200 1 893 108 108 ILE CD1 C 9.758 0.200 1 894 108 108 ILE N N 115.349 0.200 1 895 109 109 ALA H H 7.912 0.020 1 896 109 109 ALA HA H 5.226 0.020 1 897 109 109 ALA HB H 1.556 0.020 1 898 109 109 ALA CA C 50.621 0.200 1 899 109 109 ALA CB C 23.182 0.200 1 900 109 109 ALA N N 118.217 0.200 1 901 110 110 VAL H H 8.794 0.020 1 902 110 110 VAL HA H 4.525 0.020 1 903 110 110 VAL HB H 1.635 0.020 1 904 110 110 VAL HG2 H 0.523 0.020 1 905 110 110 VAL CA C 61.911 0.200 1 906 110 110 VAL CB C 34.276 0.200 1 907 110 110 VAL CG2 C 20.432 0.200 1 908 110 110 VAL N N 120.816 0.200 1 909 111 111 GLU H H 9.589 0.020 1 910 111 111 GLU HA H 4.502 0.020 1 911 111 111 GLU HB2 H 2.164 0.020 1 912 111 111 GLU HG2 H 2.363 0.020 1 913 111 111 GLU CA C 54.930 0.200 1 914 111 111 GLU CB C 33.297 0.200 1 915 111 111 GLU CG C 35.089 0.200 1 916 111 111 GLU N N 123.373 0.200 1 917 112 112 ALA H H 6.450 0.020 1 918 112 112 ALA HA H 5.102 0.020 1 919 112 112 ALA HB H 1.383 0.020 1 920 112 112 ALA CA C 50.831 0.200 1 921 112 112 ALA CB C 22.054 0.200 1 922 112 112 ALA N N 117.468 0.200 1 923 113 113 LEU H H 8.490 0.020 1 924 113 113 LEU HA H 3.933 0.020 1 925 113 113 LEU HB3 H 1.300 0.020 1 926 113 113 LEU HG H 1.896 0.020 1 927 113 113 LEU HD1 H 0.747 0.020 1 928 113 113 LEU CA C 55.242 0.200 1 929 113 113 LEU CB C 43.536 0.200 1 930 113 113 LEU CG C 25.445 0.200 1 931 113 113 LEU CD1 C 26.478 0.200 1 932 113 113 LEU N N 123.008 0.200 1 933 114 114 SER H H 7.513 0.020 1 934 114 114 SER HA H 4.836 0.020 1 935 114 114 SER HB2 H 3.752 0.020 1 936 114 114 SER CA C 57.156 0.200 1 937 114 114 SER CB C 67.283 0.200 1 938 114 114 SER N N 107.994 0.200 1 939 115 115 LEU H H 7.315 0.020 1 940 115 115 LEU HA H 4.538 0.020 1 941 115 115 LEU HB3 H 1.834 0.020 1 942 115 115 LEU HG H 1.314 0.020 1 943 115 115 LEU HD1 H 0.696 0.020 1 944 115 115 LEU CA C 54.419 0.200 1 945 115 115 LEU CB C 43.793 0.200 1 946 115 115 LEU CG C 26.990 0.200 1 947 115 115 LEU CD1 C 22.497 0.200 1 948 115 115 LEU N N 122.044 0.200 1 949 116 116 ILE H H 8.684 0.020 1 950 116 116 ILE HB H 1.105 0.020 1 951 116 116 ILE HG2 H 0.523 0.020 1 952 116 116 ILE HD1 H 0.487 0.020 1 953 116 116 ILE CB C 38.424 0.200 1 954 116 116 ILE CG2 C 17.593 0.200 1 955 116 116 ILE CD1 C 13.443 0.200 1 956 116 116 ILE N N 129.545 0.200 1 957 117 117 TYR H H 9.109 0.020 1 958 117 117 TYR HA H 6.160 0.020 1 959 117 117 TYR HB3 H 2.664 0.020 1 960 117 117 TYR CA C 54.502 0.200 1 961 117 117 TYR CB C 42.269 0.200 1 962 117 117 TYR N N 121.762 0.200 1 963 118 118 ASN H H 9.338 0.020 1 964 118 118 ASN HA H 4.618 0.020 1 965 118 118 ASN HB2 H 2.732 0.020 1 966 118 118 ASN CA C 52.098 0.200 1 967 118 118 ASN CB C 37.723 0.200 1 968 118 118 ASN N N 121.130 0.200 1 969 119 119 LYS H H 8.839 0.020 1 970 119 119 LYS HA H 4.136 0.020 1 971 119 119 LYS HB3 H 1.821 0.020 1 972 119 119 LYS HG3 H 0.971 0.020 1 973 119 119 LYS HD3 H 1.385 0.020 1 974 119 119 LYS HE2 H 2.664 0.020 1 975 119 119 LYS CA C 58.863 0.200 1 976 119 119 LYS CB C 32.576 0.200 1 977 119 119 LYS CG C 25.725 0.200 1 978 119 119 LYS CD C 29.251 0.200 1 979 119 119 LYS CE C 41.409 0.200 1 980 119 119 LYS N N 125.468 0.200 1 981 120 120 ASP H H 8.201 0.020 1 982 120 120 ASP HA H 4.592 0.020 1 983 120 120 ASP HB2 H 2.784 0.020 1 984 120 120 ASP CA C 56.332 0.200 1 985 120 120 ASP CB C 40.387 0.200 1 986 120 120 ASP N N 115.554 0.200 1 987 121 121 LEU H H 7.153 0.020 1 988 121 121 LEU HA H 4.420 0.020 1 989 121 121 LEU HB3 H 1.372 0.020 1 990 121 121 LEU HG H 1.540 0.020 1 991 121 121 LEU HD1 H 0.683 0.020 1 992 121 121 LEU CA C 55.254 0.200 1 993 121 121 LEU CB C 44.213 0.200 1 994 121 121 LEU CG C 26.402 0.200 1 995 121 121 LEU CD1 C 24.396 0.200 1 996 121 121 LEU N N 117.701 0.200 1 997 122 122 LEU H H 8.358 0.020 1 998 122 122 LEU HA H 4.779 0.020 1 999 122 122 LEU HB3 H 1.929 0.020 1 1000 122 122 LEU HG H 1.364 0.020 1 1001 122 122 LEU HD1 H 0.952 0.020 1 1002 122 122 LEU CA C 51.687 0.200 1 1003 122 122 LEU CB C 44.154 0.200 1 1004 122 122 LEU CG C 26.402 0.200 1 1005 122 122 LEU CD1 C 25.247 0.200 1 1006 122 122 LEU N N 119.732 0.200 1 1007 123 123 PRO HA H 4.747 0.020 1 1008 123 123 PRO HB2 H 2.008 0.020 1 1009 123 123 PRO HG2 H 1.572 0.020 1 1010 123 123 PRO HD3 H 3.224 0.020 1 1011 123 123 PRO CA C 62.392 0.200 1 1012 123 123 PRO CB C 31.842 0.200 1 1013 123 123 PRO CG C 26.739 0.200 1 1014 123 123 PRO CD C 49.575 0.200 1 1015 124 124 ASN H H 9.134 0.020 1 1016 124 124 ASN HA H 4.563 0.020 1 1017 124 124 ASN HB2 H 3.061 0.020 1 1018 124 124 ASN CA C 53.501 0.200 1 1019 124 124 ASN CB C 41.486 0.200 1 1020 124 124 ASN N N 123.723 0.200 1 1021 126 126 PRO HA H 4.357 0.020 1 1022 126 126 PRO HB2 H 1.929 0.020 1 1023 126 126 PRO HG2 H 1.647 0.020 1 1024 126 126 PRO CA C 62.311 0.200 1 1025 126 126 PRO CB C 31.311 0.200 1 1026 126 126 PRO CG C 26.984 0.200 1 1027 127 127 LYS H H 8.167 0.020 1 1028 127 127 LYS HA H 4.194 0.020 1 1029 127 127 LYS HB3 H 1.922 0.020 1 1030 127 127 LYS HG3 H 1.514 0.020 1 1031 127 127 LYS HD3 H 1.621 0.020 1 1032 127 127 LYS HE2 H 2.974 0.020 1 1033 127 127 LYS CA C 56.539 0.200 1 1034 127 127 LYS CB C 33.479 0.200 1 1035 127 127 LYS CG C 24.761 0.200 1 1036 127 127 LYS CD C 28.060 0.200 1 1037 127 127 LYS CE C 41.939 0.200 1 1038 127 127 LYS N N 118.380 0.200 1 1039 128 128 THR H H 7.898 0.020 1 1040 128 128 THR HA H 5.163 0.020 1 1041 128 128 THR HB H 4.851 0.020 1 1042 128 128 THR HG2 H 1.068 0.020 1 1043 128 128 THR CA C 60.028 0.200 1 1044 128 128 THR CB C 71.837 0.200 1 1045 128 128 THR CG2 C 21.091 0.200 1 1046 128 128 THR N N 108.566 0.200 1 1047 129 129 TRP H H 10.201 0.020 1 1048 129 129 TRP HA H 4.123 0.020 1 1049 129 129 TRP HB3 H 3.113 0.020 1 1050 129 129 TRP HD1 H 6.773 0.020 1 1051 129 129 TRP HE1 H 9.249 0.020 1 1052 129 129 TRP HE3 H 7.587 0.020 1 1053 129 129 TRP HH2 H 6.677 0.020 1 1054 129 129 TRP CA C 60.993 0.200 1 1055 129 129 TRP CB C 28.618 0.200 1 1056 129 129 TRP CD1 C 127.576 0.200 1 1057 129 129 TRP CE3 C 122.174 0.200 1 1058 129 129 TRP CH2 C 123.890 0.200 1 1059 129 129 TRP N N 123.870 0.200 1 1060 129 129 TRP NE1 N 126.055 0.200 1 1061 130 130 GLU H H 10.621 0.020 1 1062 130 130 GLU HA H 4.186 0.020 1 1063 130 130 GLU HB2 H 2.117 0.020 1 1064 130 130 GLU HG2 H 2.764 0.020 1 1065 130 130 GLU CA C 61.845 0.200 1 1066 130 130 GLU CB C 28.135 0.200 1 1067 130 130 GLU CG C 38.213 0.200 1 1068 130 130 GLU N N 118.001 0.200 1 1069 131 131 GLU H H 7.640 0.020 1 1070 131 131 GLU HA H 4.437 0.020 1 1071 131 131 GLU HB2 H 2.410 0.020 1 1072 131 131 GLU HG2 H 2.642 0.020 1 1073 131 131 GLU CA C 57.173 0.200 1 1074 131 131 GLU CB C 31.319 0.200 1 1075 131 131 GLU CG C 36.751 0.200 1 1076 131 131 GLU N N 116.543 0.200 1 1077 132 132 ILE H H 8.238 0.020 1 1078 132 132 ILE HA H 3.797 0.020 1 1079 132 132 ILE HB H 2.623 0.020 1 1080 132 132 ILE HG12 H 1.042 0.020 1 1081 132 132 ILE HG2 H 0.845 0.020 1 1082 132 132 ILE HD1 H 0.593 0.020 1 1083 132 132 ILE CA C 67.181 0.200 1 1084 132 132 ILE CB C 34.297 0.200 1 1085 132 132 ILE CG1 C 30.282 0.200 1 1086 132 132 ILE CG2 C 16.496 0.200 1 1087 132 132 ILE CD1 C 12.202 0.200 1 1088 132 132 ILE N N 121.442 0.200 1 1089 133 133 PRO HA H 2.977 0.020 1 1090 133 133 PRO HB2 H 1.836 0.020 1 1091 133 133 PRO HD3 H 3.752 0.020 1 1092 133 133 PRO CA C 67.118 0.200 1 1093 133 133 PRO CB C 30.606 0.200 1 1094 133 133 PRO CD C 50.349 0.200 1 1095 134 134 ALA H H 7.854 0.020 1 1096 134 134 ALA HA H 4.102 0.020 1 1097 134 134 ALA HB H 1.495 0.020 1 1098 134 134 ALA CA C 55.219 0.200 1 1099 134 134 ALA CB C 17.857 0.200 1 1100 134 134 ALA N N 118.047 0.200 1 1101 135 135 LEU H H 7.651 0.020 1 1102 135 135 LEU HA H 4.267 0.020 1 1103 135 135 LEU HB3 H 1.610 0.020 1 1104 135 135 LEU HG H 1.742 0.020 1 1105 135 135 LEU HD1 H 0.908 0.020 1 1106 135 135 LEU CA C 57.403 0.200 1 1107 135 135 LEU CB C 42.110 0.200 1 1108 135 135 LEU CG C 26.561 0.200 1 1109 135 135 LEU CD1 C 23.645 0.200 1 1110 135 135 LEU N N 119.945 0.200 1 1111 136 136 ASP H H 8.868 0.020 1 1112 136 136 ASP HA H 4.413 0.020 1 1113 136 136 ASP HB2 H 2.636 0.020 1 1114 136 136 ASP CA C 58.835 0.200 1 1115 136 136 ASP CB C 41.854 0.200 1 1116 136 136 ASP N N 118.457 0.200 1 1117 137 137 LYS H H 8.068 0.020 1 1118 137 137 LYS HA H 4.120 0.020 1 1119 137 137 LYS HB3 H 2.042 0.020 1 1120 137 137 LYS HG3 H 1.819 0.020 1 1121 137 137 LYS HD3 H 1.832 0.020 1 1122 137 137 LYS HE2 H 3.108 0.020 1 1123 137 137 LYS CA C 60.407 0.200 1 1124 137 137 LYS CB C 32.145 0.200 1 1125 137 137 LYS CG C 25.066 0.200 1 1126 137 137 LYS CD C 29.111 0.200 1 1127 137 137 LYS CE C 42.126 0.200 1 1128 137 137 LYS N N 117.222 0.200 1 1129 138 138 GLU H H 7.515 0.020 1 1130 138 138 GLU HA H 4.184 0.020 1 1131 138 138 GLU HB2 H 2.274 0.020 1 1132 138 138 GLU HG2 H 2.281 0.020 1 1133 138 138 GLU CA C 59.237 0.200 1 1134 138 138 GLU CB C 29.482 0.200 1 1135 138 138 GLU CG C 35.861 0.200 1 1136 138 138 GLU N N 118.518 0.200 1 1137 139 139 LEU H H 8.443 0.020 1 1138 139 139 LEU HA H 4.050 0.020 1 1139 139 139 LEU HB3 H 1.151 0.020 1 1140 139 139 LEU HG H 1.794 0.020 1 1141 139 139 LEU HD1 H 0.811 0.020 1 1142 139 139 LEU CA C 57.983 0.200 1 1143 139 139 LEU CB C 40.453 0.200 1 1144 139 139 LEU CG C 27.649 0.200 1 1145 139 139 LEU CD1 C 25.540 0.200 1 1146 139 139 LEU N N 121.194 0.200 1 1147 140 140 LYS H H 9.296 0.020 1 1148 140 140 LYS HA H 4.568 0.020 1 1149 140 140 LYS HB3 H 1.747 0.020 1 1150 140 140 LYS HG3 H 1.668 0.020 1 1151 140 140 LYS HD3 H 1.843 0.020 1 1152 140 140 LYS HE2 H 3.215 0.020 1 1153 140 140 LYS CA C 58.871 0.200 1 1154 140 140 LYS CB C 32.026 0.200 1 1155 140 140 LYS CG C 25.427 0.200 1 1156 140 140 LYS CD C 28.169 0.200 1 1157 140 140 LYS CE C 42.528 0.200 1 1158 140 140 LYS N N 124.073 0.200 1 1159 141 141 ALA H H 7.305 0.020 1 1160 141 141 ALA HA H 4.360 0.020 1 1161 141 141 ALA HB H 1.617 0.020 1 1162 141 141 ALA CA C 54.370 0.200 1 1163 141 141 ALA CB C 17.713 0.200 1 1164 141 141 ALA N N 121.993 0.200 1 1165 142 142 LYS H H 7.680 0.020 1 1166 142 142 LYS HA H 4.654 0.020 1 1167 142 142 LYS HB3 H 2.149 0.020 1 1168 142 142 LYS HG3 H 1.525 0.020 1 1169 142 142 LYS HD3 H 1.738 0.020 1 1170 142 142 LYS HE2 H 3.017 0.020 1 1171 142 142 LYS CA C 54.962 0.200 1 1172 142 142 LYS CB C 32.480 0.200 1 1173 142 142 LYS CG C 24.356 0.200 1 1174 142 142 LYS CD C 28.864 0.200 1 1175 142 142 LYS CE C 41.973 0.200 1 1176 142 142 LYS N N 115.700 0.200 1 1177 143 143 GLY H H 7.914 0.020 1 1178 143 143 GLY HA3 H 4.205 0.020 1 1179 143 143 GLY CA C 45.980 0.200 1 1180 143 143 GLY N N 107.577 0.200 1 1181 144 144 LYS H H 7.891 0.020 1 1182 144 144 LYS HA H 5.023 0.020 1 1183 144 144 LYS HB3 H 1.751 0.020 1 1184 144 144 LYS HG3 H 1.338 0.020 1 1185 144 144 LYS HE2 H 2.978 0.020 1 1186 144 144 LYS CA C 53.294 0.200 1 1187 144 144 LYS CB C 35.132 0.200 1 1188 144 144 LYS CG C 24.203 0.200 1 1189 144 144 LYS CE C 42.584 0.200 1 1190 144 144 LYS N N 119.749 0.200 1 1191 145 145 SER H H 7.609 0.020 1 1192 145 145 SER HA H 5.028 0.020 1 1193 145 145 SER HB2 H 4.162 0.020 1 1194 145 145 SER CA C 56.604 0.200 1 1195 145 145 SER CB C 66.397 0.200 1 1196 145 145 SER N N 109.382 0.200 1 1197 146 146 ALA H H 9.610 0.020 1 1198 146 146 ALA HA H 4.285 0.020 1 1199 146 146 ALA HB H 1.331 0.020 1 1200 146 146 ALA CA C 55.711 0.200 1 1201 146 146 ALA CB C 17.857 0.200 1 1202 146 146 ALA N N 122.815 0.200 1 1203 147 147 LEU H H 8.713 0.020 1 1204 147 147 LEU HA H 5.116 0.020 1 1205 147 147 LEU HB3 H 1.669 0.020 1 1206 147 147 LEU HG H 1.590 0.020 1 1207 147 147 LEU HD1 H 0.703 0.020 1 1208 147 147 LEU CA C 54.347 0.200 1 1209 147 147 LEU CB C 45.634 0.200 1 1210 147 147 LEU CG C 27.843 0.200 1 1211 147 147 LEU CD1 C 22.189 0.200 1 1212 147 147 LEU N N 116.728 0.200 1 1213 148 148 MET H H 8.211 0.020 1 1214 148 148 MET HA H 5.007 0.020 1 1215 148 148 MET HB2 H 2.144 0.020 1 1216 148 148 MET HG2 H 2.723 0.020 1 1217 148 148 MET HE H 2.036 0.020 1 1218 148 148 MET CA C 55.799 0.200 1 1219 148 148 MET CB C 37.978 0.200 1 1220 148 148 MET CG C 32.036 0.200 1 1221 148 148 MET CE C 17.133 0.200 1 1222 148 148 MET N N 121.582 0.200 1 1223 149 149 PHE H H 8.614 0.020 1 1224 149 149 PHE HA H 4.887 0.020 1 1225 149 149 PHE HB3 H 3.179 0.020 1 1226 149 149 PHE HE1 H 7.333 0.020 1 1227 149 149 PHE HE2 H 7.333 0.020 1 1228 149 149 PHE CA C 55.657 0.200 1 1229 149 149 PHE CB C 41.467 0.200 1 1230 149 149 PHE CE1 C 131.346 0.200 1 1231 149 149 PHE N N 120.053 0.200 1 1232 150 150 ASN H H 8.709 0.020 1 1233 150 150 ASN HA H 3.811 0.020 1 1234 150 150 ASN HB2 H 1.866 0.020 1 1235 150 150 ASN CA C 53.452 0.200 1 1236 150 150 ASN CB C 37.267 0.200 1 1237 150 150 ASN N N 115.896 0.200 1 1238 151 151 LEU H H 7.354 0.020 1 1239 151 151 LEU HA H 4.089 0.020 1 1240 151 151 LEU HB3 H 1.324 0.020 1 1241 151 151 LEU HG H 1.480 0.020 1 1242 151 151 LEU HD1 H 0.767 0.020 1 1243 151 151 LEU CA C 54.446 0.200 1 1244 151 151 LEU CB C 42.011 0.200 1 1245 151 151 LEU CG C 26.089 0.200 1 1246 151 151 LEU CD1 C 25.852 0.200 1 1247 151 151 LEU N N 122.998 0.200 1 1248 152 152 GLN H H 7.976 0.020 1 1249 152 152 GLN HA H 4.122 0.020 1 1250 152 152 GLN HB2 H 2.155 0.020 1 1251 152 152 GLN HG2 H 2.525 0.020 1 1252 152 152 GLN HE21 H 6.994 0.020 2 1253 152 152 GLN HE22 H 6.907 0.020 2 1254 152 152 GLN CA C 55.625 0.200 1 1255 152 152 GLN CB C 28.499 0.200 1 1256 152 152 GLN CG C 32.978 0.200 1 1257 152 152 GLN N N 112.914 0.200 1 1258 152 152 GLN NE2 N 113.935 0.200 1 1259 153 153 GLU H H 6.505 0.020 1 1260 153 153 GLU HA H 5.251 0.020 1 1261 153 153 GLU HB2 H 2.059 0.020 1 1262 153 153 GLU HG2 H 2.352 0.020 1 1263 153 153 GLU CA C 51.375 0.200 1 1264 153 153 GLU CB C 33.234 0.200 1 1265 153 153 GLU CG C 35.895 0.200 1 1266 153 153 GLU N N 113.705 0.200 1 1267 154 154 PRO HA H 4.981 0.020 1 1268 154 154 PRO HB2 H 2.346 0.020 1 1269 154 154 PRO HG2 H 2.622 0.020 1 1270 154 154 PRO HD3 H 3.728 0.020 1 1271 154 154 PRO CA C 63.549 0.200 1 1272 154 154 PRO CB C 32.111 0.200 1 1273 154 154 PRO CG C 27.681 0.200 1 1274 154 154 PRO CD C 51.090 0.200 1 1275 155 155 TYR H H 7.999 0.020 1 1276 155 155 TYR HA H 4.528 0.020 1 1277 155 155 TYR HB3 H 2.639 0.020 1 1278 155 155 TYR CA C 62.477 0.200 1 1279 155 155 TYR CB C 40.196 0.200 1 1280 155 155 TYR N N 117.674 0.200 1 1281 156 156 PHE H H 8.086 0.020 1 1282 156 156 PHE HA H 4.518 0.020 1 1283 156 156 PHE HB3 H 3.610 0.020 1 1284 156 156 PHE CA C 60.636 0.200 1 1285 156 156 PHE CB C 41.595 0.200 1 1286 156 156 PHE N N 111.953 0.200 1 1287 157 157 THR H H 7.629 0.020 1 1288 157 157 THR HA H 4.485 0.020 1 1289 157 157 THR HB H 4.311 0.020 1 1290 157 157 THR HG2 H 1.446 0.020 1 1291 157 157 THR CA C 62.926 0.200 1 1292 157 157 THR CB C 69.372 0.200 1 1293 157 157 THR CG2 C 23.914 0.200 1 1294 157 157 THR N N 105.724 0.200 1 1295 158 158 TRP H H 8.400 0.020 1 1296 158 158 TRP HA H 4.501 0.020 1 1297 158 158 TRP HH2 H 6.827 0.020 1 1298 158 158 TRP CA C 60.778 0.200 1 1299 158 158 TRP CH2 C 122.030 0.200 1 1300 158 158 TRP N N 124.175 0.200 1 1301 159 159 PRO HA H 3.922 0.020 1 1302 159 159 PRO HB2 H 1.713 0.020 1 1303 159 159 PRO HG2 H 1.981 0.020 1 1304 159 159 PRO HD3 H 3.707 0.020 1 1305 159 159 PRO CA C 65.849 0.200 1 1306 159 159 PRO CB C 30.181 0.200 1 1307 159 159 PRO CG C 27.620 0.200 1 1308 159 159 PRO CD C 49.323 0.200 1 1309 160 160 LEU H H 6.445 0.020 1 1310 160 160 LEU HA H 3.758 0.020 1 1311 160 160 LEU HB3 H 1.093 0.020 1 1312 160 160 LEU HG H 1.712 0.020 1 1313 160 160 LEU HD1 H -0.998 0.020 1 1314 160 160 LEU CA C 55.957 0.200 1 1315 160 160 LEU CB C 42.369 0.200 1 1316 160 160 LEU CG C 26.541 0.200 1 1317 160 160 LEU CD1 C 19.246 0.200 1 1318 160 160 LEU N N 111.322 0.200 1 1319 161 161 ILE H H 7.009 0.020 1 1320 161 161 ILE HA H 3.002 0.020 1 1321 161 161 ILE HB H 1.209 0.020 1 1322 161 161 ILE HG12 H 0.620 0.020 1 1323 161 161 ILE HG2 H 0.540 0.020 1 1324 161 161 ILE HD1 H 0.790 0.020 1 1325 161 161 ILE CA C 65.808 0.200 1 1326 161 161 ILE CB C 37.692 0.200 1 1327 161 161 ILE CG1 C 28.565 0.200 1 1328 161 161 ILE CG2 C 16.339 0.200 1 1329 161 161 ILE CD1 C 12.941 0.200 1 1330 161 161 ILE N N 119.299 0.200 1 1331 162 162 ALA H H 8.028 0.020 1 1332 162 162 ALA HA H 3.535 0.020 1 1333 162 162 ALA HB H 0.386 0.020 1 1334 162 162 ALA CA C 52.244 0.200 1 1335 162 162 ALA CB C 18.296 0.200 1 1336 162 162 ALA N N 115.050 0.200 1 1337 163 163 ALA H H 6.684 0.020 1 1338 163 163 ALA HA H 4.065 0.020 1 1339 163 163 ALA HB H 1.604 0.020 1 1340 163 163 ALA CA C 56.324 0.200 1 1341 163 163 ALA CB C 19.674 0.200 1 1342 163 163 ALA N N 120.619 0.200 1 1343 164 164 ASP H H 9.615 0.020 1 1344 164 164 ASP HA H 5.023 0.020 1 1345 164 164 ASP HB2 H 2.176 0.020 1 1346 164 164 ASP CA C 53.294 0.200 1 1347 164 164 ASP CB C 42.337 0.200 1 1348 164 164 ASP N N 114.837 0.200 1 1349 165 165 GLY H H 7.521 0.020 1 1350 165 165 GLY HA3 H 4.567 0.020 1 1351 165 165 GLY CA C 45.592 0.200 1 1352 165 165 GLY N N 103.469 0.200 1 1353 166 166 GLY H H 7.437 0.020 1 1354 166 166 GLY HA3 H 3.159 0.020 1 1355 166 166 GLY CA C 45.282 0.200 1 1356 166 166 GLY N N 107.843 0.200 1 1357 167 167 TYR H H 8.279 0.020 1 1358 167 167 TYR HA H 5.470 0.020 1 1359 167 167 TYR HB3 H 3.370 0.020 1 1360 167 167 TYR HE1 H 6.752 0.020 1 1361 167 167 TYR HE2 H 6.752 0.020 1 1362 167 167 TYR CA C 57.542 0.200 1 1363 167 167 TYR CB C 39.078 0.200 1 1364 167 167 TYR CE1 C 118.004 0.200 1 1365 167 167 TYR N N 115.233 0.200 1 1366 168 168 ALA H H 10.587 0.020 1 1367 168 168 ALA HA H 4.249 0.020 1 1368 168 168 ALA HB H 0.490 0.020 1 1369 168 168 ALA CA C 53.170 0.200 1 1370 168 168 ALA CB C 16.457 0.200 1 1371 168 168 ALA N N 124.284 0.200 1 1372 169 169 PHE H H 6.342 0.020 1 1373 169 169 PHE HA H 5.568 0.020 1 1374 169 169 PHE HB3 H 3.215 0.020 1 1375 169 169 PHE HE1 H 7.049 0.020 1 1376 169 169 PHE HE2 H 7.049 0.020 1 1377 169 169 PHE CA C 55.616 0.200 1 1378 169 169 PHE CB C 42.528 0.200 1 1379 169 169 PHE CE1 C 130.570 0.200 1 1380 169 169 PHE N N 107.884 0.200 1 1381 170 170 LYS H H 8.912 0.020 1 1382 170 170 LYS HA H 4.035 0.020 1 1383 170 170 LYS HB3 H 2.107 0.020 1 1384 170 170 LYS HG3 H 1.205 0.020 1 1385 170 170 LYS HD3 H 1.456 0.020 1 1386 170 170 LYS HE2 H 2.740 0.020 1 1387 170 170 LYS CA C 57.084 0.200 1 1388 170 170 LYS CB C 32.599 0.200 1 1389 170 170 LYS CG C 23.585 0.200 1 1390 170 170 LYS CD C 27.321 0.200 1 1391 170 170 LYS CE C 41.361 0.200 1 1392 170 170 LYS N N 125.554 0.200 1 1393 171 171 TYR H H 8.642 0.020 1 1394 171 171 TYR HA H 4.858 0.020 1 1395 171 171 TYR HB3 H 2.946 0.020 1 1396 171 171 TYR HE1 H 6.465 0.020 1 1397 171 171 TYR HE2 H 6.465 0.020 1 1398 171 171 TYR CA C 56.286 0.200 1 1399 171 171 TYR CB C 39.847 0.200 1 1400 171 171 TYR CE1 C 117.426 0.200 1 1401 171 171 TYR N N 129.785 0.200 1 1402 172 172 GLU H H 8.276 0.020 1 1403 172 172 GLU N N 126.723 0.200 1 1404 173 173 ASN HA H 4.243 0.020 1 1405 173 173 ASN HB2 H 2.651 0.020 1 1406 173 173 ASN HD21 H 7.602 0.020 2 1407 173 173 ASN HD22 H 6.865 0.020 2 1408 173 173 ASN CA C 54.063 0.200 1 1409 173 173 ASN CB C 37.238 0.200 1 1410 173 173 ASN ND2 N 113.331 0.200 1 1411 174 174 GLY H H 7.501 0.020 1 1412 174 174 GLY HA3 H 3.906 0.020 1 1413 174 174 GLY CA C 45.520 0.200 1 1414 174 174 GLY N N 101.844 0.200 1 1415 175 175 LYS H H 7.119 0.020 1 1416 175 175 LYS HA H 4.665 0.020 1 1417 175 175 LYS HB3 H 1.767 0.020 1 1418 175 175 LYS HG3 H 1.254 0.020 1 1419 175 175 LYS HD3 H 1.640 0.020 1 1420 175 175 LYS HE2 H 2.960 0.020 1 1421 175 175 LYS CA C 54.505 0.200 1 1422 175 175 LYS CB C 35.477 0.200 1 1423 175 175 LYS CG C 23.294 0.200 1 1424 175 175 LYS CD C 28.759 0.200 1 1425 175 175 LYS CE C 41.986 0.200 1 1426 175 175 LYS N N 118.340 0.200 1 1427 176 176 TYR H H 8.758 0.020 1 1428 176 176 TYR HA H 5.339 0.020 1 1429 176 176 TYR HB3 H 2.623 0.020 1 1430 176 176 TYR HE1 H 7.134 0.020 1 1431 176 176 TYR HE2 H 7.134 0.020 1 1432 176 176 TYR CA C 58.842 0.200 1 1433 176 176 TYR CB C 39.859 0.200 1 1434 176 176 TYR CE1 C 118.254 0.200 1 1435 176 176 TYR N N 119.767 0.200 1 1436 177 177 ASP H H 9.036 0.020 1 1437 177 177 ASP HA H 4.900 0.020 1 1438 177 177 ASP HB2 H 2.716 0.020 1 1439 177 177 ASP CA C 52.826 0.200 1 1440 177 177 ASP CB C 41.345 0.200 1 1441 177 177 ASP N N 123.754 0.200 1 1442 178 178 ILE H H 7.754 0.020 1 1443 178 178 ILE HA H 4.263 0.020 1 1444 178 178 ILE HB H 2.045 0.020 1 1445 178 178 ILE HG12 H 1.341 0.020 1 1446 178 178 ILE HG2 H 0.691 0.020 1 1447 178 178 ILE HD1 H 0.888 0.020 1 1448 178 178 ILE CA C 63.629 0.200 1 1449 178 178 ILE CB C 37.063 0.200 1 1450 178 178 ILE CG1 C 25.485 0.200 1 1451 178 178 ILE CG2 C 17.847 0.200 1 1452 178 178 ILE CD1 C 13.695 0.200 1 1453 178 178 ILE N N 116.924 0.200 1 1454 179 179 LYS H H 8.327 0.020 1 1455 179 179 LYS HA H 4.636 0.020 1 1456 179 179 LYS HB3 H 2.084 0.020 1 1457 179 179 LYS HG3 H 1.588 0.020 1 1458 179 179 LYS HD3 H 1.783 0.020 1 1459 179 179 LYS HE2 H 3.041 0.020 1 1460 179 179 LYS CA C 54.597 0.200 1 1461 179 179 LYS CB C 32.155 0.200 1 1462 179 179 LYS CG C 24.262 0.200 1 1463 179 179 LYS CD C 28.095 0.200 1 1464 179 179 LYS CE C 42.065 0.200 1 1465 179 179 LYS N N 115.948 0.200 1 1466 180 180 ASP H H 7.801 0.020 1 1467 180 180 ASP HA H 4.932 0.020 1 1468 180 180 ASP HB2 H 2.389 0.020 1 1469 180 180 ASP CA C 53.293 0.200 1 1470 180 180 ASP CB C 40.971 0.200 1 1471 180 180 ASP N N 123.078 0.200 1 1472 181 181 VAL H H 7.513 0.020 1 1473 181 181 VAL HA H 5.040 0.020 1 1474 181 181 VAL HB H 1.743 0.020 1 1475 181 181 VAL HG2 H 0.729 0.020 1 1476 181 181 VAL CA C 59.232 0.200 1 1477 181 181 VAL CB C 34.872 0.200 1 1478 181 181 VAL CG2 C 22.265 0.200 1 1479 181 181 VAL N N 122.798 0.200 1 1480 182 182 GLY H H 7.101 0.020 1 1481 182 182 GLY HA3 H 1.546 0.020 1 1482 182 182 GLY CA C 46.298 0.200 1 1483 182 182 GLY N N 120.520 0.200 1 1484 183 183 VAL H H 6.739 0.020 1 1485 183 183 VAL HA H 4.110 0.020 1 1486 183 183 VAL HB H 2.083 0.020 1 1487 183 183 VAL HG2 H 0.861 0.020 1 1488 183 183 VAL CA C 63.340 0.200 1 1489 183 183 VAL CB C 32.661 0.200 1 1490 183 183 VAL CG2 C 22.113 0.200 1 1491 183 183 VAL N N 113.914 0.200 1 1492 184 184 ASP H H 7.874 0.020 1 1493 184 184 ASP HA H 4.825 0.020 1 1494 184 184 ASP HB2 H 2.436 0.020 1 1495 184 184 ASP CA C 51.559 0.200 1 1496 184 184 ASP CB C 39.855 0.200 1 1497 184 184 ASP N N 114.640 0.200 1 1498 185 185 ASN H H 6.920 0.020 1 1499 185 185 ASN HA H 4.646 0.020 1 1500 185 185 ASN HB2 H 3.133 0.020 1 1501 185 185 ASN HD21 H 7.392 0.020 2 1502 185 185 ASN HD22 H 6.475 0.020 2 1503 185 185 ASN CA C 51.589 0.200 1 1504 185 185 ASN CB C 39.281 0.200 1 1505 185 185 ASN N N 116.139 0.200 1 1506 185 185 ASN ND2 N 109.924 0.200 1 1507 186 186 ALA HA H 3.989 0.020 1 1508 186 186 ALA HB H 1.455 0.020 1 1509 186 186 ALA CA C 55.489 0.200 1 1510 186 186 ALA CB C 18.184 0.200 1 1511 187 187 GLY H H 8.406 0.020 1 1512 187 187 GLY HA3 H 3.476 0.020 1 1513 187 187 GLY CA C 47.147 0.200 1 1514 187 187 GLY N N 109.160 0.200 1 1515 188 188 ALA H H 8.097 0.020 1 1516 188 188 ALA HA H 4.749 0.020 1 1517 188 188 ALA HB H 1.267 0.020 1 1518 188 188 ALA CA C 53.862 0.200 1 1519 188 188 ALA CB C 18.251 0.200 1 1520 188 188 ALA N N 127.606 0.200 1 1521 189 189 LYS H H 8.024 0.020 1 1522 189 189 LYS HA H 3.731 0.020 1 1523 189 189 LYS HB3 H 1.883 0.020 1 1524 189 189 LYS HG3 H 1.483 0.020 1 1525 189 189 LYS HD3 H 1.717 0.020 1 1526 189 189 LYS HE2 H 2.859 0.020 1 1527 189 189 LYS CA C 59.686 0.200 1 1528 189 189 LYS CB C 31.973 0.200 1 1529 189 189 LYS CG C 26.355 0.200 1 1530 189 189 LYS CD C 29.287 0.200 1 1531 189 189 LYS CE C 42.145 0.200 1 1532 189 189 LYS N N 115.096 0.200 1 1533 190 190 ALA H H 8.256 0.020 1 1534 190 190 ALA HA H 4.268 0.020 1 1535 190 190 ALA HB H 1.797 0.020 1 1536 190 190 ALA CA C 55.713 0.200 1 1537 190 190 ALA CB C 17.797 0.200 1 1538 190 190 ALA N N 124.586 0.200 1 1539 191 191 GLY H H 8.260 0.020 1 1540 191 191 GLY HA3 H 3.580 0.020 1 1541 191 191 GLY CA C 47.714 0.200 1 1542 191 191 GLY N N 107.353 0.200 1 1543 192 192 LEU H H 8.703 0.020 1 1544 192 192 LEU HA H 4.198 0.020 1 1545 192 192 LEU HB3 H 2.003 0.020 1 1546 192 192 LEU HD1 H 1.098 0.020 1 1547 192 192 LEU CA C 57.252 0.200 1 1548 192 192 LEU CB C 40.257 0.200 1 1549 192 192 LEU CD1 C 23.893 0.200 1 1550 192 192 LEU N N 121.126 0.200 1 1551 193 193 THR H H 8.574 0.020 1 1552 193 193 THR HA H 3.838 0.020 1 1553 193 193 THR HG2 H 1.318 0.020 1 1554 193 193 THR CA C 68.163 0.200 1 1555 193 193 THR CG2 C 20.705 0.200 1 1556 193 193 THR N N 116.338 0.200 1 1557 194 194 PHE H H 7.697 0.020 1 1558 194 194 PHE HA H 4.257 0.020 1 1559 194 194 PHE HB3 H 2.768 0.020 1 1560 194 194 PHE HE1 H 7.548 0.020 1 1561 194 194 PHE HE2 H 7.548 0.020 1 1562 194 194 PHE CA C 62.332 0.200 1 1563 194 194 PHE CB C 39.155 0.200 1 1564 194 194 PHE CE1 C 131.001 0.200 1 1565 194 194 PHE N N 121.984 0.200 1 1566 195 195 LEU H H 7.765 0.020 1 1567 195 195 LEU HA H 3.817 0.020 1 1568 195 195 LEU HB3 H 2.088 0.020 1 1569 195 195 LEU HD1 H 0.918 0.020 1 1570 195 195 LEU CA C 58.725 0.200 1 1571 195 195 LEU CB C 41.391 0.200 1 1572 195 195 LEU CD1 C 23.378 0.200 1 1573 195 195 LEU N N 119.496 0.200 1 1574 196 196 VAL H H 8.636 0.020 1 1575 196 196 VAL HA H 3.523 0.020 1 1576 196 196 VAL HB H 2.229 0.020 1 1577 196 196 VAL HG2 H 0.874 0.020 1 1578 196 196 VAL CA C 67.316 0.200 1 1579 196 196 VAL CB C 30.830 0.200 1 1580 196 196 VAL CG2 C 23.073 0.200 1 1581 196 196 VAL N N 117.487 0.200 1 1582 197 197 ASP H H 8.623 0.020 1 1583 197 197 ASP HA H 4.540 0.020 1 1584 197 197 ASP HB2 H 2.777 0.020 1 1585 197 197 ASP CA C 58.016 0.200 1 1586 197 197 ASP CB C 39.859 0.200 1 1587 197 197 ASP N N 122.894 0.200 1 1588 198 198 LEU H H 7.929 0.020 1 1589 198 198 LEU HA H 4.207 0.020 1 1590 198 198 LEU HB3 H 1.252 0.020 1 1591 198 198 LEU HG H 1.686 0.020 1 1592 198 198 LEU HD1 H 1.029 0.020 1 1593 198 198 LEU CA C 58.583 0.200 1 1594 198 198 LEU CB C 42.248 0.200 1 1595 198 198 LEU CG C 25.666 0.200 1 1596 198 198 LEU CD1 C 25.189 0.200 1 1597 198 198 LEU N N 120.142 0.200 1 1598 199 199 ILE H H 7.477 0.020 1 1599 199 199 ILE HA H 4.336 0.020 1 1600 199 199 ILE HB H 2.176 0.020 1 1601 199 199 ILE HG12 H 0.744 0.020 1 1602 199 199 ILE HG2 H 1.048 0.020 1 1603 199 199 ILE HD1 H 0.782 0.020 1 1604 199 199 ILE CA C 63.377 0.200 1 1605 199 199 ILE CB C 38.562 0.200 1 1606 199 199 ILE CG1 C 28.596 0.200 1 1607 199 199 ILE CG2 C 17.399 0.200 1 1608 199 199 ILE CD1 C 14.056 0.200 1 1609 199 199 ILE N N 119.897 0.200 1 1610 200 200 LYS H H 9.436 0.020 1 1611 200 200 LYS HA H 4.077 0.020 1 1612 200 200 LYS HB3 H 1.917 0.020 1 1613 200 200 LYS HG3 H 1.682 0.020 1 1614 200 200 LYS HD3 H 1.712 0.020 1 1615 200 200 LYS HE2 H 3.002 0.020 1 1616 200 200 LYS CA C 59.911 0.200 1 1617 200 200 LYS CB C 32.322 0.200 1 1618 200 200 LYS CG C 24.841 0.200 1 1619 200 200 LYS CD C 28.963 0.200 1 1620 200 200 LYS CE C 41.810 0.200 1 1621 200 200 LYS N N 124.445 0.200 1 1622 201 201 ASN H H 8.035 0.020 1 1623 201 201 ASN HA H 4.718 0.020 1 1624 201 201 ASN HB2 H 2.783 0.020 1 1625 201 201 ASN HD21 H 7.868 0.020 2 1626 201 201 ASN HD22 H 7.031 0.020 2 1627 201 201 ASN CA C 53.442 0.200 1 1628 201 201 ASN CB C 38.713 0.200 1 1629 201 201 ASN N N 113.824 0.200 1 1630 201 201 ASN ND2 N 115.297 0.200 1 1631 202 202 LYS H H 7.972 0.020 1 1632 202 202 LYS HA H 3.960 0.020 1 1633 202 202 LYS HB3 H 1.973 0.020 1 1634 202 202 LYS HG3 H 1.344 0.020 1 1635 202 202 LYS HD3 H 1.721 0.020 1 1636 202 202 LYS HE2 H 3.039 0.020 1 1637 202 202 LYS CA C 57.519 0.200 1 1638 202 202 LYS CB C 27.327 0.200 1 1639 202 202 LYS CG C 24.512 0.200 1 1640 202 202 LYS CD C 28.420 0.200 1 1641 202 202 LYS CE C 42.076 0.200 1 1642 202 202 LYS N N 111.252 0.200 1 1643 203 203 HIS H H 8.400 0.020 1 1644 203 203 HIS HA H 4.836 0.020 1 1645 203 203 HIS HB3 H 3.074 0.020 1 1646 203 203 HIS HD2 H 7.061 0.020 1 1647 203 203 HIS HE1 H 7.775 0.020 1 1648 203 203 HIS CA C 57.156 0.200 1 1649 203 203 HIS CB C 28.459 0.200 1 1650 203 203 HIS CD2 C 120.242 0.200 1 1651 203 203 HIS CE1 C 139.568 0.200 1 1652 203 203 HIS N N 116.037 0.200 1 1653 204 204 MET H H 7.520 0.020 1 1654 204 204 MET HA H 4.692 0.020 1 1655 204 204 MET HB2 H 1.673 0.020 1 1656 204 204 MET HG2 H 2.812 0.020 1 1657 204 204 MET HE H 2.059 0.020 1 1658 204 204 MET CA C 54.569 0.200 1 1659 204 204 MET CB C 37.489 0.200 1 1660 204 204 MET CG C 31.775 0.200 1 1661 204 204 MET CE C 16.649 0.200 1 1662 204 204 MET N N 113.977 0.200 1 1663 205 205 ASN H H 8.741 0.020 1 1664 205 205 ASN N N 118.478 0.200 1 1665 206 206 ALA HA H 3.867 0.020 1 1666 206 206 ALA HB H 1.369 0.020 1 1667 206 206 ALA CA C 54.640 0.200 1 1668 206 206 ALA CB C 18.199 0.200 1 1669 207 207 ASP H H 8.199 0.020 1 1670 207 207 ASP HA H 4.486 0.020 1 1671 207 207 ASP HB2 H 2.740 0.020 1 1672 207 207 ASP CA C 53.638 0.200 1 1673 207 207 ASP CB C 39.847 0.200 1 1674 207 207 ASP N N 112.704 0.200 1 1675 208 208 THR H H 7.372 0.020 1 1676 208 208 THR HA H 3.585 0.020 1 1677 208 208 THR HB H 4.093 0.020 1 1678 208 208 THR HG2 H 1.216 0.020 1 1679 208 208 THR CA C 66.757 0.200 1 1680 208 208 THR CB C 69.145 0.200 1 1681 208 208 THR CG2 C 23.281 0.200 1 1682 208 208 THR N N 116.414 0.200 1 1683 209 209 ASP H H 7.016 0.020 1 1684 209 209 ASP HA H 5.314 0.020 1 1685 209 209 ASP HB2 H 3.260 0.020 1 1686 209 209 ASP CA C 51.748 0.200 1 1687 209 209 ASP CB C 42.053 0.200 1 1688 209 209 ASP N N 130.744 0.200 1 1689 210 210 TYR H H 7.899 0.020 1 1690 210 210 TYR HA H 3.550 0.020 1 1691 210 210 TYR HB3 H 3.057 0.020 1 1692 210 210 TYR CA C 63.440 0.200 1 1693 210 210 TYR CB C 39.054 0.200 1 1694 210 210 TYR N N 117.263 0.200 1 1695 211 211 SER H H 8.243 0.020 1 1696 211 211 SER HA H 4.400 0.020 1 1697 211 211 SER HB2 H 4.085 0.020 1 1698 211 211 SER CA C 61.828 0.200 1 1699 211 211 SER CB C 62.777 0.200 1 1700 211 211 SER N N 114.636 0.200 1 1701 212 212 ILE H H 9.032 0.020 1 1702 212 212 ILE HA H 3.823 0.020 1 1703 212 212 ILE HB H 1.667 0.020 1 1704 212 212 ILE HG12 H 1.146 0.020 1 1705 212 212 ILE HG2 H 1.002 0.020 1 1706 212 212 ILE HD1 H 0.895 0.020 1 1707 212 212 ILE CA C 65.030 0.200 1 1708 212 212 ILE CB C 38.753 0.200 1 1709 212 212 ILE CG1 C 29.259 0.200 1 1710 212 212 ILE CG2 C 17.184 0.200 1 1711 212 212 ILE CD1 C 12.809 0.200 1 1712 212 212 ILE N N 124.410 0.200 1 1713 213 213 ALA H H 7.662 0.020 1 1714 213 213 ALA HA H 4.006 0.020 1 1715 213 213 ALA HB H 1.143 0.020 1 1716 213 213 ALA CA C 55.256 0.200 1 1717 213 213 ALA CB C 17.029 0.200 1 1718 213 213 ALA N N 120.602 0.200 1 1719 214 214 GLU H H 7.911 0.020 1 1720 214 214 GLU N N 117.279 0.200 1 1721 215 215 ALA H H 8.025 0.020 1 1722 215 215 ALA HA H 4.155 0.020 1 1723 215 215 ALA HB H 1.465 0.020 1 1724 215 215 ALA CA C 54.564 0.200 1 1725 215 215 ALA CB C 17.760 0.200 1 1726 215 215 ALA N N 119.617 0.200 1 1727 216 216 ALA H H 7.853 0.020 1 1728 216 216 ALA HA H 4.113 0.020 1 1729 216 216 ALA HB H 1.543 0.020 1 1730 216 216 ALA CA C 54.875 0.200 1 1731 216 216 ALA CB C 19.712 0.200 1 1732 216 216 ALA N N 117.522 0.200 1 1733 217 217 PHE H H 8.378 0.020 1 1734 217 217 PHE HA H 4.061 0.020 1 1735 217 217 PHE HB3 H 3.055 0.020 1 1736 217 217 PHE CA C 62.994 0.200 1 1737 217 217 PHE CB C 38.082 0.200 1 1738 217 217 PHE N N 119.285 0.200 1 1739 218 218 ASN HA H 4.491 0.020 1 1740 218 218 ASN CA C 55.486 0.200 1 1741 219 219 LYS H H 7.745 0.020 1 1742 219 219 LYS HA H 4.375 0.020 1 1743 219 219 LYS HB3 H 2.004 0.020 1 1744 219 219 LYS HG3 H 1.668 0.020 1 1745 219 219 LYS HD3 H 1.654 0.020 1 1746 219 219 LYS HE2 H 2.946 0.020 1 1747 219 219 LYS CA C 56.032 0.200 1 1748 219 219 LYS CB C 32.990 0.200 1 1749 219 219 LYS CG C 25.432 0.200 1 1750 219 219 LYS CD C 28.798 0.200 1 1751 219 219 LYS CE C 41.748 0.200 1 1752 219 219 LYS N N 116.621 0.200 1 1753 220 220 GLY H H 7.758 0.020 1 1754 220 220 GLY HA3 H 3.921 0.020 1 1755 220 220 GLY CA C 45.993 0.200 1 1756 220 220 GLY N N 108.538 0.200 1 1757 221 221 GLU H H 8.399 0.020 1 1758 221 221 GLU HA H 4.267 0.020 1 1759 221 221 GLU HB2 H 1.968 0.020 1 1760 221 221 GLU HG2 H 2.223 0.020 1 1761 221 221 GLU CA C 57.403 0.200 1 1762 221 221 GLU CB C 30.422 0.200 1 1763 221 221 GLU CG C 36.164 0.200 1 1764 221 221 GLU N N 116.265 0.200 1 1765 222 222 THR H H 6.900 0.020 1 1766 222 222 THR HA H 5.313 0.020 1 1767 222 222 THR HB H 3.764 0.020 1 1768 222 222 THR HG2 H 1.179 0.020 1 1769 222 222 THR CA C 58.003 0.200 1 1770 222 222 THR CB C 70.621 0.200 1 1771 222 222 THR CG2 C 19.219 0.200 1 1772 222 222 THR N N 110.397 0.200 1 1773 223 223 ALA H H 8.710 0.020 1 1774 223 223 ALA HA H 4.304 0.020 1 1775 223 223 ALA HB H 1.741 0.020 1 1776 223 223 ALA CA C 54.627 0.200 1 1777 223 223 ALA CB C 20.369 0.200 1 1778 223 223 ALA N N 127.335 0.200 1 1779 224 224 MET H H 8.111 0.020 1 1780 224 224 MET HA H 5.858 0.020 1 1781 224 224 MET HG2 H 2.581 0.020 1 1782 224 224 MET HE H 1.853 0.020 1 1783 224 224 MET CA C 54.568 0.200 1 1784 224 224 MET CG C 32.759 0.200 1 1785 224 224 MET CE C 16.702 0.200 1 1786 224 224 MET N N 114.125 0.200 1 1787 225 225 THR H H 9.189 0.020 1 1788 225 225 THR HA H 4.926 0.020 1 1789 225 225 THR HG2 H 0.212 0.020 1 1790 225 225 THR CA C 59.648 0.200 1 1791 225 225 THR CG2 C 17.172 0.200 1 1792 225 225 THR N N 113.217 0.200 1 1793 226 226 ILE H H 7.205 0.020 1 1794 226 226 ILE HA H 4.998 0.020 1 1795 226 226 ILE HB H 1.459 0.020 1 1796 226 226 ILE HG12 H 0.628 0.020 1 1797 226 226 ILE HG2 H 0.911 0.020 1 1798 226 226 ILE HD1 H 0.095 0.020 1 1799 226 226 ILE CA C 60.312 0.200 1 1800 226 226 ILE CB C 40.720 0.200 1 1801 226 226 ILE CG1 C 27.477 0.200 1 1802 226 226 ILE CG2 C 17.983 0.200 1 1803 226 226 ILE CD1 C 11.560 0.200 1 1804 226 226 ILE N N 122.476 0.200 1 1805 227 227 ASN H H 8.471 0.020 1 1806 227 227 ASN HA H 5.218 0.020 1 1807 227 227 ASN HB2 H 2.534 0.020 1 1808 227 227 ASN CA C 52.369 0.200 1 1809 227 227 ASN CB C 42.753 0.200 1 1810 227 227 ASN N N 121.809 0.200 1 1811 228 228 GLY H H 8.296 0.020 1 1812 228 228 GLY HA3 H 1.539 0.020 1 1813 228 228 GLY CA C 42.265 0.200 1 1814 228 228 GLY N N 110.557 0.200 1 1815 229 229 PRO HA H 1.254 0.020 1 1816 229 229 PRO HB2 H 1.219 0.020 1 1817 229 229 PRO CA C 62.647 0.200 1 1818 229 229 PRO CB C 29.857 0.200 1 1819 230 230 TRP H H 6.023 0.020 1 1820 230 230 TRP HA H 4.394 0.020 1 1821 230 230 TRP HB3 H 3.328 0.020 1 1822 230 230 TRP CA C 59.068 0.200 1 1823 230 230 TRP N N 111.846 0.200 1 1824 231 231 ALA H H 7.021 0.020 1 1825 231 231 ALA N N 125.177 0.200 1 1826 235 235 ILE H H 7.873 0.020 1 1827 235 235 ILE N N 120.166 0.200 1 1828 236 236 ASP H H 8.368 0.020 1 1829 236 236 ASP N N 126.074 0.200 1 1830 238 238 SER H H 7.708 0.020 1 1831 238 238 SER N N 118.208 0.200 1 1832 240 240 VAL H H 7.385 0.020 1 1833 240 240 VAL N N 120.257 0.200 1 1834 242 242 TYR H H 7.907 0.020 1 1835 242 242 TYR HA H 5.871 0.020 1 1836 242 242 TYR HB3 H 2.664 0.020 1 1837 242 242 TYR CA C 54.580 0.200 1 1838 242 242 TYR CB C 41.409 0.200 1 1839 242 242 TYR N N 121.641 0.200 1 1840 243 243 GLY H H 8.542 0.020 1 1841 243 243 GLY HA3 H 2.868 0.020 1 1842 243 243 GLY CA C 42.903 0.200 1 1843 243 243 GLY N N 107.321 0.200 1 1844 244 244 VAL H H 8.219 0.020 1 1845 244 244 VAL HA H 5.013 0.020 1 1846 244 244 VAL HB H 1.609 0.020 1 1847 244 244 VAL HG2 H 0.649 0.020 1 1848 244 244 VAL CA C 61.411 0.200 1 1849 244 244 VAL CB C 34.400 0.200 1 1850 244 244 VAL CG2 C 21.235 0.200 1 1851 244 244 VAL N N 120.543 0.200 1 1852 245 245 THR H H 9.517 0.020 1 1853 245 245 THR HA H 4.949 0.020 1 1854 245 245 THR HB H 4.112 0.020 1 1855 245 245 THR HG2 H 1.146 0.020 1 1856 245 245 THR CA C 58.948 0.200 1 1857 245 245 THR CB C 71.572 0.200 1 1858 245 245 THR CG2 C 18.518 0.200 1 1859 245 245 THR N N 119.475 0.200 1 1860 246 246 VAL H H 8.171 0.020 1 1861 246 246 VAL HA H 4.076 0.020 1 1862 246 246 VAL HB H 1.974 0.020 1 1863 246 246 VAL HG2 H 0.999 0.020 1 1864 246 246 VAL CA C 62.320 0.200 1 1865 246 246 VAL CB C 32.239 0.200 1 1866 246 246 VAL CG2 C 21.331 0.200 1 1867 246 246 VAL N N 123.454 0.200 1 1868 247 247 LEU H H 8.621 0.020 1 1869 247 247 LEU N N 125.568 0.200 1 1870 248 248 PRO HA H 4.317 0.020 1 1871 248 248 PRO HB2 H 1.158 0.020 1 1872 248 248 PRO HG2 H 0.250 0.020 1 1873 248 248 PRO HD3 H 3.278 0.020 1 1874 248 248 PRO CA C 61.885 0.200 1 1875 248 248 PRO CB C 30.398 0.200 1 1876 248 248 PRO CG C 25.394 0.200 1 1877 248 248 PRO CD C 48.899 0.200 1 1878 249 249 THR H H 8.824 0.020 1 1879 249 249 THR HA H 4.849 0.020 1 1880 249 249 THR HB H 3.934 0.020 1 1881 249 249 THR HG2 H 1.079 0.020 1 1882 249 249 THR CA C 60.939 0.200 1 1883 249 249 THR CB C 71.397 0.200 1 1884 249 249 THR CG2 C 20.697 0.200 1 1885 249 249 THR N N 111.503 0.200 1 1886 250 250 PHE H H 9.599 0.020 1 1887 250 250 PHE HA H 5.303 0.020 1 1888 250 250 PHE HB3 H 2.452 0.020 1 1889 250 250 PHE HE1 H 6.797 0.020 1 1890 250 250 PHE HE2 H 6.797 0.020 1 1891 250 250 PHE CA C 56.755 0.200 1 1892 250 250 PHE CB C 41.807 0.200 1 1893 250 250 PHE CE1 C 130.701 0.200 1 1894 250 250 PHE N N 121.817 0.200 1 1895 251 251 LYS H H 10.608 0.020 1 1896 251 251 LYS HA H 3.311 0.020 1 1897 251 251 LYS HG3 H -0.232 0.020 1 1898 251 251 LYS HD3 H 0.972 0.020 1 1899 251 251 LYS HE2 H 2.816 0.020 1 1900 251 251 LYS CA C 57.333 0.200 1 1901 251 251 LYS CG C 23.580 0.200 1 1902 251 251 LYS CD C 29.048 0.200 1 1903 251 251 LYS CE C 41.561 0.200 1 1904 251 251 LYS N N 129.537 0.200 1 1905 252 252 GLY H H 9.055 0.020 1 1906 252 252 GLY HA3 H 4.098 0.020 1 1907 252 252 GLY CA C 44.908 0.200 1 1908 252 252 GLY N N 103.324 0.200 1 1909 253 253 GLN H H 8.286 0.020 1 1910 253 253 GLN HA H 4.835 0.020 1 1911 253 253 GLN HB2 H 1.936 0.020 1 1912 253 253 GLN HG2 H 2.246 0.020 1 1913 253 253 GLN HE21 H 7.298 0.020 1 1914 253 253 GLN HE22 H 7.298 0.020 1 1915 253 253 GLN CA C 52.300 0.200 1 1916 253 253 GLN CB C 30.097 0.200 1 1917 253 253 GLN CG C 32.978 0.200 1 1918 253 253 GLN N N 122.254 0.200 1 1919 253 253 GLN NE2 N 112.325 0.200 1 1920 254 254 PRO HA H 4.454 0.020 1 1921 254 254 PRO HB2 H 1.929 0.020 1 1922 254 254 PRO HG2 H 2.164 0.020 1 1923 254 254 PRO HD3 H 3.885 0.020 1 1924 254 254 PRO CA C 63.279 0.200 1 1925 254 254 PRO CB C 31.311 0.200 1 1926 254 254 PRO CG C 27.390 0.200 1 1927 254 254 PRO CD C 49.884 0.200 1 1928 255 255 SER H H 8.031 0.020 1 1929 255 255 SER HA H 4.404 0.020 1 1930 255 255 SER HB2 H 3.730 0.020 1 1931 255 255 SER CA C 62.220 0.200 1 1932 255 255 SER CB C 64.916 0.200 1 1933 255 255 SER N N 117.917 0.200 1 1934 256 256 LYS H H 7.700 0.020 1 1935 256 256 LYS HA H 4.989 0.020 1 1936 256 256 LYS HB3 H 1.563 0.020 1 1937 256 256 LYS HE2 H 3.003 0.020 1 1938 256 256 LYS CA C 53.020 0.200 1 1939 256 256 LYS CB C 33.454 0.200 1 1940 256 256 LYS CE C 41.946 0.200 1 1941 256 256 LYS N N 123.215 0.200 1 1942 257 257 PRO HA H 4.308 0.020 1 1943 257 257 PRO HB2 H 2.124 0.020 1 1944 257 257 PRO CA C 62.228 0.200 1 1945 257 257 PRO CB C 31.588 0.200 1 1946 258 258 PHE H H 9.392 0.020 1 1947 258 258 PHE HA H 5.711 0.020 1 1948 258 258 PHE HB3 H 3.094 0.020 1 1949 258 258 PHE HE1 H 6.677 0.020 1 1950 258 258 PHE HE2 H 6.677 0.020 1 1951 258 258 PHE CA C 58.390 0.200 1 1952 258 258 PHE CB C 40.081 0.200 1 1953 258 258 PHE CE1 C 130.796 0.200 1 1954 258 258 PHE N N 118.339 0.200 1 1955 259 259 VAL H H 8.776 0.020 1 1956 259 259 VAL HA H 4.808 0.020 1 1957 259 259 VAL HB H 1.885 0.020 1 1958 259 259 VAL HG2 H 1.030 0.020 1 1959 259 259 VAL CA C 61.873 0.200 1 1960 259 259 VAL CB C 33.878 0.200 1 1961 259 259 VAL CG2 C 22.448 0.200 1 1962 259 259 VAL N N 121.740 0.200 1 1963 260 260 GLY H H 8.886 0.020 1 1964 260 260 GLY HA3 H 4.273 0.020 1 1965 260 260 GLY CA C 44.726 0.200 1 1966 260 260 GLY N N 115.811 0.200 1 1967 261 261 VAL H H 11.049 0.020 1 1968 261 261 VAL HA H 5.278 0.020 1 1969 261 261 VAL HB H 1.858 0.020 1 1970 261 261 VAL HG2 H 0.572 0.020 1 1971 261 261 VAL CA C 60.148 0.200 1 1972 261 261 VAL CB C 32.525 0.200 1 1973 261 261 VAL CG2 C 20.756 0.200 1 1974 261 261 VAL N N 128.942 0.200 1 1975 262 262 LEU H H 8.832 0.020 1 1976 262 262 LEU HA H 4.090 0.020 1 1977 262 262 LEU HB3 H 1.793 0.020 1 1978 262 262 LEU HD1 H 0.826 0.020 1 1979 262 262 LEU CA C 56.584 0.200 1 1980 262 262 LEU CB C 41.122 0.200 1 1981 262 262 LEU CD1 C 22.355 0.200 1 1982 262 262 LEU N N 134.277 0.200 1 1983 263 263 SER H H 8.802 0.020 1 1984 263 263 SER HA H 5.353 0.020 1 1985 263 263 SER HB2 H 3.156 0.020 1 1986 263 263 SER CA C 58.789 0.200 1 1987 263 263 SER CB C 66.192 0.200 1 1988 263 263 SER N N 126.567 0.200 1 1989 264 264 ALA H H 9.161 0.020 1 1990 264 264 ALA HA H 5.128 0.020 1 1991 264 264 ALA HB H 0.574 0.020 1 1992 264 264 ALA CA C 49.728 0.200 1 1993 264 264 ALA CB C 20.759 0.200 1 1994 264 264 ALA N N 123.610 0.200 1 1995 265 265 GLY H H 9.453 0.020 1 1996 265 265 GLY HA3 H 3.214 0.020 1 1997 265 265 GLY CA C 42.710 0.200 1 1998 265 265 GLY N N 110.658 0.200 1 1999 266 266 ILE H H 10.349 0.020 1 2000 266 266 ILE HB H 1.607 0.020 1 2001 266 266 ILE HG12 H 0.735 0.020 1 2002 266 266 ILE HG2 H 0.854 0.020 1 2003 266 266 ILE HD1 H 0.950 0.020 1 2004 266 266 ILE CB C 39.863 0.200 1 2005 266 266 ILE CG1 C 27.766 0.200 1 2006 266 266 ILE CG2 C 16.186 0.200 1 2007 266 266 ILE CD1 C 13.653 0.200 1 2008 266 266 ILE N N 123.493 0.200 1 2009 267 267 ASN H H 8.268 0.020 1 2010 267 267 ASN HA H 4.537 0.020 1 2011 267 267 ASN HB2 H 2.941 0.020 1 2012 267 267 ASN CA C 53.506 0.200 1 2013 267 267 ASN CB C 38.825 0.200 1 2014 267 267 ASN N N 125.821 0.200 1 2015 268 268 ALA H H 8.878 0.020 1 2016 268 268 ALA HA H 3.831 0.020 1 2017 268 268 ALA HB H 1.235 0.020 1 2018 268 268 ALA CA C 55.308 0.200 1 2019 268 268 ALA CB C 17.823 0.200 1 2020 268 268 ALA N N 131.045 0.200 1 2021 269 269 ALA H H 8.182 0.020 1 2022 269 269 ALA HA H 4.379 0.020 1 2023 269 269 ALA HB H 1.294 0.020 1 2024 269 269 ALA CA C 51.368 0.200 1 2025 269 269 ALA CB C 18.523 0.200 1 2026 269 269 ALA N N 117.838 0.200 1 2027 270 270 SER H H 7.621 0.020 1 2028 270 270 SER HA H 4.498 0.020 1 2029 270 270 SER HB2 H 4.157 0.020 1 2030 270 270 SER CA C 56.244 0.200 1 2031 270 270 SER CB C 64.380 0.200 1 2032 270 270 SER N N 112.759 0.200 1 2033 271 271 PRO HA H 4.981 0.020 1 2034 271 271 PRO HB2 H 2.178 0.020 1 2035 271 271 PRO HG2 H 1.819 0.020 1 2036 271 271 PRO HD3 H 3.921 0.020 1 2037 271 271 PRO CA C 63.549 0.200 1 2038 271 271 PRO CB C 31.160 0.200 1 2039 271 271 PRO CG C 25.569 0.200 1 2040 271 271 PRO CD C 50.267 0.200 1 2041 272 272 ASN H H 8.884 0.020 1 2042 272 272 ASN HA H 5.421 0.020 1 2043 272 272 ASN HB2 H 2.423 0.020 1 2044 272 272 ASN CA C 52.634 0.200 1 2045 272 272 ASN CB C 40.339 0.200 1 2046 272 272 ASN N N 119.642 0.200 1 2047 273 273 LYS H H 7.819 0.020 1 2048 273 273 LYS HA H 3.760 0.020 1 2049 273 273 LYS HB3 H 1.808 0.020 1 2050 273 273 LYS HG3 H 1.941 0.020 1 2051 273 273 LYS HE2 H 3.259 0.020 1 2052 273 273 LYS CA C 61.718 0.200 1 2053 273 273 LYS CB C 31.836 0.200 1 2054 273 273 LYS CG C 25.484 0.200 1 2055 273 273 LYS CE C 42.536 0.200 1 2056 273 273 LYS N N 119.131 0.200 1 2057 274 274 GLU H H 8.880 0.020 1 2058 274 274 GLU HA H 4.165 0.020 1 2059 274 274 GLU HB2 H 2.110 0.020 1 2060 274 274 GLU HG2 H 2.443 0.020 1 2061 274 274 GLU CA C 59.845 0.200 1 2062 274 274 GLU CB C 28.140 0.200 1 2063 274 274 GLU CG C 36.440 0.200 1 2064 274 274 GLU N N 118.257 0.200 1 2065 275 275 LEU H H 7.438 0.020 1 2066 275 275 LEU HA H 4.327 0.020 1 2067 275 275 LEU HB3 H 1.426 0.020 1 2068 275 275 LEU HG H 1.897 0.020 1 2069 275 275 LEU HD1 H 0.962 0.020 1 2070 275 275 LEU CA C 57.368 0.200 1 2071 275 275 LEU CB C 42.217 0.200 1 2072 275 275 LEU CG C 26.518 0.200 1 2073 275 275 LEU CD1 C 24.943 0.200 1 2074 275 275 LEU N N 120.547 0.200 1 2075 276 276 ALA H H 8.403 0.020 1 2076 276 276 ALA HA H 3.849 0.020 1 2077 276 276 ALA HB H 1.336 0.020 1 2078 276 276 ALA CA C 55.326 0.200 1 2079 276 276 ALA CB C 17.857 0.200 1 2080 276 276 ALA N N 120.235 0.200 1 2081 277 277 LYS H H 7.912 0.020 1 2082 277 277 LYS HA H 3.774 0.020 1 2083 277 277 LYS HB3 H 1.954 0.020 1 2084 277 277 LYS HG3 H 1.588 0.020 1 2085 277 277 LYS HD3 H 1.727 0.020 1 2086 277 277 LYS CA C 60.267 0.200 1 2087 277 277 LYS CB C 32.630 0.200 1 2088 277 277 LYS CG C 23.958 0.200 1 2089 277 277 LYS CD C 29.624 0.200 1 2090 277 277 LYS N N 118.217 0.200 1 2091 278 278 GLU H H 7.633 0.020 1 2092 278 278 GLU HA H 4.057 0.020 1 2093 278 278 GLU HB2 H 2.363 0.020 1 2094 278 278 GLU HG2 H 2.563 0.020 1 2095 278 278 GLU CA C 59.690 0.200 1 2096 278 278 GLU CB C 29.275 0.200 1 2097 278 278 GLU CG C 35.564 0.200 1 2098 278 278 GLU N N 118.642 0.200 1 2099 279 279 PHE H H 8.429 0.020 1 2100 279 279 PHE HA H 3.666 0.020 1 2101 279 279 PHE HB3 H 2.576 0.020 1 2102 279 279 PHE HE1 H 6.889 0.020 1 2103 279 279 PHE HE2 H 6.889 0.020 1 2104 279 279 PHE CA C 61.677 0.200 1 2105 279 279 PHE CB C 38.537 0.200 1 2106 279 279 PHE CE1 C 130.049 0.200 1 2107 279 279 PHE N N 118.304 0.200 1 2108 280 280 LEU H H 8.470 0.020 1 2109 280 280 LEU HA H 3.608 0.020 1 2110 280 280 LEU HB3 H 0.402 0.020 1 2111 280 280 LEU HG H 1.551 0.020 1 2112 280 280 LEU HD1 H 0.688 0.020 1 2113 280 280 LEU CA C 58.320 0.200 1 2114 280 280 LEU CB C 40.846 0.200 1 2115 280 280 LEU CG C 25.864 0.200 1 2116 280 280 LEU CD1 C 25.434 0.200 1 2117 280 280 LEU N N 119.959 0.200 1 2118 281 281 GLU H H 8.457 0.020 1 2119 281 281 GLU HA H 3.756 0.020 1 2120 281 281 GLU HB2 H 1.810 0.020 1 2121 281 281 GLU HG2 H 3.259 0.020 1 2122 281 281 GLU CA C 59.614 0.200 1 2123 281 281 GLU CB C 28.895 0.200 1 2124 281 281 GLU CG C 42.536 0.200 1 2125 281 281 GLU N N 112.784 0.200 1 2126 282 282 ASN H H 7.745 0.020 1 2127 282 282 ASN HA H 4.886 0.020 1 2128 282 282 ASN HB2 H 3.110 0.020 1 2129 282 282 ASN HD21 H 7.795 0.020 2 2130 282 282 ASN HD22 H 6.951 0.020 2 2131 282 282 ASN CA C 52.988 0.200 1 2132 282 282 ASN CB C 39.054 0.200 1 2133 282 282 ASN N N 108.770 0.200 1 2134 282 282 ASN ND2 N 113.375 0.200 1 2135 283 283 TYR H H 7.206 0.020 1 2136 283 283 TYR HA H 4.353 0.020 1 2137 283 283 TYR HB3 H 2.294 0.020 1 2138 283 283 TYR HE1 H 6.998 0.020 1 2139 283 283 TYR HE2 H 6.998 0.020 1 2140 283 283 TYR CA C 59.795 0.200 1 2141 283 283 TYR CB C 38.026 0.200 1 2142 283 283 TYR CE1 C 118.036 0.200 1 2143 283 283 TYR N N 116.204 0.200 1 2144 284 284 LEU H H 8.142 0.020 1 2145 284 284 LEU HA H 4.074 0.020 1 2146 284 284 LEU HB3 H 1.977 0.020 1 2147 284 284 LEU HD1 H 0.863 0.020 1 2148 284 284 LEU CA C 58.183 0.200 1 2149 284 284 LEU CB C 41.147 0.200 1 2150 284 284 LEU CD1 C 23.548 0.200 1 2151 284 284 LEU N N 121.308 0.200 1 2152 285 285 LEU H H 7.867 0.020 1 2153 285 285 LEU HA H 4.445 0.020 1 2154 285 285 LEU HB3 H 1.850 0.020 1 2155 285 285 LEU HG H 1.545 0.020 1 2156 285 285 LEU HD1 H 1.082 0.020 1 2157 285 285 LEU CA C 54.491 0.200 1 2158 285 285 LEU CB C 38.617 0.200 1 2159 285 285 LEU CG C 27.831 0.200 1 2160 285 285 LEU CD1 C 25.342 0.200 1 2161 285 285 LEU N N 119.195 0.200 1 2162 286 286 THR H H 8.575 0.020 1 2163 286 286 THR HA H 4.495 0.020 1 2164 286 286 THR HB H 4.353 0.020 1 2165 286 286 THR HG2 H 0.849 0.020 1 2166 286 286 THR CA C 58.849 0.200 1 2167 286 286 THR CB C 73.592 0.200 1 2168 286 286 THR CG2 C 20.647 0.200 1 2169 286 286 THR N N 108.553 0.200 1 2170 287 287 ASP H H 8.568 0.020 1 2171 287 287 ASP HA H 3.782 0.020 1 2172 287 287 ASP HB2 H 2.484 0.020 1 2173 287 287 ASP CA C 58.370 0.200 1 2174 287 287 ASP CB C 39.543 0.200 1 2175 287 287 ASP N N 122.095 0.200 1 2176 288 288 GLU H H 8.458 0.020 1 2177 288 288 GLU HA H 3.925 0.020 1 2178 288 288 GLU HB2 H 1.962 0.020 1 2179 288 288 GLU HG2 H 2.338 0.020 1 2180 288 288 GLU CA C 59.349 0.200 1 2181 288 288 GLU CB C 29.256 0.200 1 2182 288 288 GLU CG C 36.459 0.200 1 2183 288 288 GLU N N 115.546 0.200 1 2184 289 289 GLY H H 8.358 0.020 1 2185 289 289 GLY HA3 H 4.418 0.020 1 2186 289 289 GLY CA C 46.743 0.200 1 2187 289 289 GLY N N 112.692 0.200 1 2188 290 290 LEU H H 8.237 0.020 1 2189 290 290 LEU HA H 4.075 0.020 1 2190 290 290 LEU HB3 H 1.186 0.020 1 2191 290 290 LEU HG H 2.497 0.020 1 2192 290 290 LEU HD1 H 1.102 0.020 1 2193 290 290 LEU CA C 57.298 0.200 1 2194 290 290 LEU CB C 41.813 0.200 1 2195 290 290 LEU CG C 25.624 0.200 1 2196 290 290 LEU CD1 C 27.532 0.200 1 2197 290 290 LEU N N 119.461 0.200 1 2198 291 291 GLU H H 7.784 0.020 1 2199 291 291 GLU HA H 4.250 0.020 1 2200 291 291 GLU HB2 H 2.016 0.020 1 2201 291 291 GLU HG2 H 2.129 0.020 1 2202 291 291 GLU CA C 59.410 0.200 1 2203 291 291 GLU CB C 29.203 0.200 1 2204 291 291 GLU CG C 36.032 0.200 1 2205 291 291 GLU N N 120.894 0.200 1 2206 292 292 ALA H H 7.221 0.020 1 2207 292 292 ALA HA H 4.021 0.020 1 2208 292 292 ALA HB H 1.493 0.020 1 2209 292 292 ALA CA C 55.267 0.200 1 2210 292 292 ALA CB C 17.598 0.200 1 2211 292 292 ALA N N 119.803 0.200 1 2212 293 293 VAL H H 7.295 0.020 1 2213 293 293 VAL HA H 3.588 0.020 1 2214 293 293 VAL HB H 2.120 0.020 1 2215 293 293 VAL HG2 H 0.913 0.020 1 2216 293 293 VAL CA C 67.357 0.200 1 2217 293 293 VAL CB C 31.911 0.200 1 2218 293 293 VAL CG2 C 21.921 0.200 1 2219 293 293 VAL N N 115.778 0.200 1 2220 294 294 ASN H H 8.742 0.020 1 2221 294 294 ASN HA H 4.693 0.020 1 2222 294 294 ASN HB2 H 2.836 0.020 1 2223 294 294 ASN CA C 56.378 0.200 1 2224 294 294 ASN CB C 40.929 0.200 1 2225 294 294 ASN N N 117.311 0.200 1 2226 295 295 LYS H H 8.306 0.020 1 2227 295 295 LYS HA H 4.028 0.020 1 2228 295 295 LYS HB3 H 1.837 0.020 1 2229 295 295 LYS HG3 H 1.654 0.020 1 2230 295 295 LYS HD3 H 1.701 0.020 1 2231 295 295 LYS HE2 H 3.002 0.020 1 2232 295 295 LYS CA C 58.374 0.200 1 2233 295 295 LYS CB C 32.243 0.200 1 2234 295 295 LYS CG C 25.023 0.200 1 2235 295 295 LYS CD C 28.970 0.200 1 2236 295 295 LYS CE C 41.810 0.200 1 2237 295 295 LYS N N 115.886 0.200 1 2238 296 296 ASP H H 7.322 0.020 1 2239 296 296 ASP HA H 4.595 0.020 1 2240 296 296 ASP HB2 H 2.571 0.020 1 2241 296 296 ASP CA C 56.135 0.200 1 2242 296 296 ASP CB C 42.077 0.200 1 2243 296 296 ASP N N 118.729 0.200 1 2244 297 297 LYS H H 7.672 0.020 1 2245 297 297 LYS HA H 4.773 0.020 1 2246 297 297 LYS HB3 H 1.623 0.020 1 2247 297 297 LYS CA C 52.557 0.200 1 2248 297 297 LYS CB C 34.898 0.200 1 2249 297 297 LYS N N 115.749 0.200 1 2250 298 298 PRO HA H 4.591 0.020 1 2251 298 298 PRO HB2 H 1.966 0.020 1 2252 298 298 PRO HG2 H 2.308 0.020 1 2253 298 298 PRO HD3 H 3.882 0.020 1 2254 298 298 PRO CA C 63.163 0.200 1 2255 298 298 PRO CB C 31.407 0.200 1 2256 298 298 PRO CG C 27.320 0.200 1 2257 298 298 PRO CD C 50.418 0.200 1 2258 299 299 LEU H H 8.651 0.020 1 2259 299 299 LEU HA H 4.131 0.020 1 2260 299 299 LEU HB3 H 1.400 0.020 1 2261 299 299 LEU HG H 1.734 0.020 1 2262 299 299 LEU HD1 H 0.926 0.020 1 2263 299 299 LEU CA C 55.630 0.200 1 2264 299 299 LEU CB C 43.904 0.200 1 2265 299 299 LEU CG C 26.806 0.200 1 2266 299 299 LEU CD1 C 26.280 0.200 1 2267 299 299 LEU N N 122.502 0.200 1 2268 300 300 GLY H H 8.174 0.020 1 2269 300 300 GLY HA3 H 4.503 0.020 1 2270 300 300 GLY CA C 44.223 0.200 1 2271 300 300 GLY N N 103.940 0.200 1 2272 301 301 ALA H H 7.562 0.020 1 2273 301 301 ALA HA H 4.932 0.020 1 2274 301 301 ALA HB H 1.398 0.020 1 2275 301 301 ALA CA C 51.412 0.200 1 2276 301 301 ALA CB C 19.384 0.200 1 2277 301 301 ALA N N 123.807 0.200 1 2278 302 302 VAL H H 8.199 0.020 1 2279 302 302 VAL HA H 5.187 0.020 1 2280 302 302 VAL HB H 2.544 0.020 1 2281 302 302 VAL HG2 H 1.278 0.020 1 2282 302 302 VAL CA C 59.606 0.200 1 2283 302 302 VAL CB C 35.370 0.200 1 2284 302 302 VAL CG2 C 18.667 0.200 1 2285 302 302 VAL N N 110.224 0.200 1 2286 303 303 ALA H H 7.681 0.020 1 2287 303 303 ALA HA H 4.034 0.020 1 2288 303 303 ALA HB H 1.026 0.020 1 2289 303 303 ALA CA C 53.080 0.200 1 2290 303 303 ALA CB C 19.424 0.200 1 2291 303 303 ALA N N 117.082 0.200 1 2292 304 304 LEU H H 6.419 0.020 1 2293 304 304 LEU HA H 4.266 0.020 1 2294 304 304 LEU HB3 H 1.929 0.020 1 2295 304 304 LEU HD1 H 0.872 0.020 1 2296 304 304 LEU CA C 54.309 0.200 1 2297 304 304 LEU CB C 44.154 0.200 1 2298 304 304 LEU CD1 C 23.959 0.200 1 2299 304 304 LEU N N 114.860 0.200 1 2300 305 305 LYS H H 8.093 0.020 1 2301 305 305 LYS HA H 3.766 0.020 1 2302 305 305 LYS HB3 H 1.593 0.020 1 2303 305 305 LYS HG3 H 0.653 0.020 1 2304 305 305 LYS HD3 H 1.337 0.020 1 2305 305 305 LYS HE2 H 2.664 0.020 1 2306 305 305 LYS CA C 60.541 0.200 1 2307 305 305 LYS CB C 31.848 0.200 1 2308 305 305 LYS CG C 23.683 0.200 1 2309 305 305 LYS CD C 29.496 0.200 1 2310 305 305 LYS CE C 41.409 0.200 1 2311 305 305 LYS N N 129.429 0.200 1 2312 306 306 SER H H 8.772 0.020 1 2313 306 306 SER HA H 4.049 0.020 1 2314 306 306 SER HB2 H 4.189 0.020 1 2315 306 306 SER CA C 61.418 0.200 1 2316 306 306 SER CB C 63.152 0.200 1 2317 306 306 SER N N 112.267 0.200 1 2318 307 307 TYR H H 6.675 0.020 1 2319 307 307 TYR HA H 4.884 0.020 1 2320 307 307 TYR HB3 H 2.648 0.020 1 2321 307 307 TYR HE1 H 6.699 0.020 1 2322 307 307 TYR HE2 H 6.699 0.020 1 2323 307 307 TYR CA C 59.101 0.200 1 2324 307 307 TYR CB C 38.609 0.200 1 2325 307 307 TYR CE1 C 117.728 0.200 1 2326 307 307 TYR N N 122.110 0.200 1 2327 308 308 GLU H H 8.538 0.020 1 2328 308 308 GLU HA H 4.194 0.020 1 2329 308 308 GLU HB2 H 2.558 0.020 1 2330 308 308 GLU HG2 H 2.923 0.020 1 2331 308 308 GLU CA C 57.980 0.200 1 2332 308 308 GLU CB C 25.899 0.200 1 2333 308 308 GLU CG C 33.089 0.200 1 2334 308 308 GLU N N 121.290 0.200 1 2335 309 309 GLU H H 7.766 0.020 1 2336 309 309 GLU HA H 4.000 0.020 1 2337 309 309 GLU HB2 H 2.070 0.020 1 2338 309 309 GLU HG2 H 2.349 0.020 1 2339 309 309 GLU CA C 59.270 0.200 1 2340 309 309 GLU CB C 29.029 0.200 1 2341 309 309 GLU CG C 36.233 0.200 1 2342 309 309 GLU N N 115.446 0.200 1 2343 310 310 GLU H H 6.919 0.020 1 2344 310 310 GLU HA H 4.252 0.020 1 2345 310 310 GLU HB2 H 2.065 0.020 1 2346 310 310 GLU HG2 H 2.439 0.020 1 2347 310 310 GLU CA C 57.858 0.200 1 2348 310 310 GLU CB C 29.280 0.200 1 2349 310 310 GLU CG C 34.685 0.200 1 2350 310 310 GLU N N 117.463 0.200 1 2351 311 311 LEU H H 8.257 0.020 1 2352 311 311 LEU HA H 4.008 0.020 1 2353 311 311 LEU HB3 H 1.523 0.020 1 2354 311 311 LEU HD1 H 0.908 0.020 1 2355 311 311 LEU CA C 57.126 0.200 1 2356 311 311 LEU CB C 41.956 0.200 1 2357 311 311 LEU CD1 C 25.849 0.200 1 2358 311 311 LEU N N 120.903 0.200 1 2359 312 312 ALA H H 8.602 0.020 1 2360 312 312 ALA HA H 3.973 0.020 1 2361 312 312 ALA HB H 1.447 0.020 1 2362 312 312 ALA CA C 53.993 0.200 1 2363 312 312 ALA CB C 16.993 0.200 1 2364 312 312 ALA N N 117.908 0.200 1 2365 313 313 LYS H H 7.143 0.020 1 2366 313 313 LYS HA H 4.050 0.020 1 2367 313 313 LYS HB3 H 1.952 0.020 1 2368 313 313 LYS HG3 H 1.619 0.020 1 2369 313 313 LYS CA C 58.835 0.200 1 2370 313 313 LYS CB C 31.940 0.200 1 2371 313 313 LYS CG C 25.445 0.200 1 2372 313 313 LYS N N 117.302 0.200 1 2373 314 314 ASP H H 8.337 0.020 1 2374 314 314 ASP HA H 4.991 0.020 1 2375 314 314 ASP HB2 H 2.741 0.020 1 2376 314 314 ASP CA C 50.524 0.200 1 2377 314 314 ASP CB C 41.642 0.200 1 2378 314 314 ASP N N 121.133 0.200 1 2379 315 315 PRO HA H 4.421 0.020 1 2380 315 315 PRO HB2 H 2.104 0.020 1 2381 315 315 PRO HG2 H 2.028 0.020 1 2382 315 315 PRO HD3 H 4.163 0.020 1 2383 315 315 PRO CA C 64.431 0.200 1 2384 315 315 PRO CB C 32.217 0.200 1 2385 315 315 PRO CG C 26.841 0.200 1 2386 315 315 PRO CD C 51.207 0.200 1 2387 316 316 ARG H H 8.482 0.020 1 2388 316 316 ARG HA H 3.806 0.020 1 2389 316 316 ARG HB3 H 2.059 0.020 1 2390 316 316 ARG HD2 H 2.493 0.020 1 2391 316 316 ARG CA C 58.391 0.200 1 2392 316 316 ARG CB C 29.486 0.200 1 2393 316 316 ARG CD C 39.863 0.200 1 2394 316 316 ARG N N 116.850 0.200 1 2395 317 317 ILE H H 7.571 0.020 1 2396 317 317 ILE HA H 3.772 0.020 1 2397 317 317 ILE HB H 2.338 0.020 1 2398 317 317 ILE HG12 H 1.352 0.020 1 2399 317 317 ILE HG2 H 0.999 0.020 1 2400 317 317 ILE HD1 H 1.133 0.020 1 2401 317 317 ILE CA C 64.627 0.200 1 2402 317 317 ILE CB C 36.747 0.200 1 2403 317 317 ILE CG1 C 29.506 0.200 1 2404 317 317 ILE CG2 C 17.599 0.200 1 2405 317 317 ILE CD1 C 12.387 0.200 1 2406 317 317 ILE N N 122.935 0.200 1 2407 318 318 ALA H H 7.902 0.020 1 2408 318 318 ALA HA H 4.074 0.020 1 2409 318 318 ALA HB H 1.667 0.020 1 2410 318 318 ALA CA C 55.836 0.200 1 2411 318 318 ALA CB C 17.257 0.200 1 2412 318 318 ALA N N 122.597 0.200 1 2413 319 319 ALA H H 8.174 0.020 1 2414 319 319 ALA HA H 4.154 0.020 1 2415 319 319 ALA HB H 1.348 0.020 1 2416 319 319 ALA CA C 55.138 0.200 1 2417 319 319 ALA CB C 17.878 0.200 1 2418 319 319 ALA N N 118.616 0.200 1 2419 320 320 THR H H 7.383 0.020 1 2420 320 320 THR HA H 3.759 0.020 1 2421 320 320 THR HG2 H 1.400 0.020 1 2422 320 320 THR CA C 68.178 0.200 1 2423 320 320 THR CG2 C 20.269 0.200 1 2424 320 320 THR N N 114.667 0.200 1 2425 321 321 MET H H 8.205 0.020 1 2426 321 321 MET HA H 4.267 0.020 1 2427 321 321 MET HB2 H 1.896 0.020 1 2428 321 321 MET HG2 H 2.475 0.020 1 2429 321 321 MET HE H 1.579 0.020 1 2430 321 321 MET CA C 57.086 0.200 1 2431 321 321 MET CB C 31.579 0.200 1 2432 321 321 MET CG C 32.752 0.200 1 2433 321 321 MET CE C 17.627 0.200 1 2434 321 321 MET N N 119.298 0.200 1 2435 322 322 GLU H H 8.273 0.020 1 2436 322 322 GLU HA H 3.982 0.020 1 2437 322 322 GLU HB2 H 2.085 0.020 1 2438 322 322 GLU HG2 H 2.094 0.020 1 2439 322 322 GLU CA C 59.923 0.200 1 2440 322 322 GLU CB C 28.976 0.200 1 2441 322 322 GLU CG C 35.893 0.200 1 2442 322 322 GLU N N 121.354 0.200 1 2443 323 323 ASN H H 8.328 0.020 1 2444 323 323 ASN HA H 4.435 0.020 1 2445 323 323 ASN HB2 H 2.739 0.020 1 2446 323 323 ASN CA C 56.904 0.200 1 2447 323 323 ASN CB C 39.132 0.200 1 2448 323 323 ASN N N 115.178 0.200 1 2449 324 324 ALA H H 8.135 0.020 1 2450 324 324 ALA HA H 3.798 0.020 1 2451 324 324 ALA HB H 1.321 0.020 1 2452 324 324 ALA CA C 54.398 0.200 1 2453 324 324 ALA CB C 17.623 0.200 1 2454 324 324 ALA N N 119.622 0.200 1 2455 325 325 GLN H H 8.294 0.020 1 2456 325 325 GLN HA H 3.524 0.020 1 2457 325 325 GLN HB2 H 2.073 0.020 1 2458 325 325 GLN HG2 H 1.967 0.020 1 2459 325 325 GLN HE21 H 6.751 0.020 2 2460 325 325 GLN HE22 H 6.604 0.020 2 2461 325 325 GLN CA C 58.391 0.200 1 2462 325 325 GLN CB C 28.057 0.200 1 2463 325 325 GLN CG C 34.947 0.200 1 2464 325 325 GLN N N 116.236 0.200 1 2465 325 325 GLN NE2 N 109.482 0.200 1 2466 326 326 LYS H H 7.091 0.020 1 2467 326 326 LYS HA H 4.386 0.020 1 2468 326 326 LYS HB3 H 2.182 0.020 1 2469 326 326 LYS HG3 H 1.550 0.020 1 2470 326 326 LYS HD3 H 1.665 0.020 1 2471 326 326 LYS HE2 H 2.956 0.020 1 2472 326 326 LYS CA C 56.032 0.200 1 2473 326 326 LYS CB C 32.809 0.200 1 2474 326 326 LYS CG C 25.577 0.200 1 2475 326 326 LYS CD C 28.837 0.200 1 2476 326 326 LYS CE C 42.428 0.200 1 2477 326 326 LYS N N 117.725 0.200 1 2478 327 327 GLY H H 7.297 0.020 1 2479 327 327 GLY HA3 H 3.890 0.020 1 2480 327 327 GLY CA C 44.512 0.200 1 2481 327 327 GLY N N 106.260 0.200 1 2482 328 328 GLU H H 8.577 0.020 1 2483 328 328 GLU HA H 4.820 0.020 1 2484 328 328 GLU HB2 H 1.764 0.020 1 2485 328 328 GLU HG2 H 2.314 0.020 1 2486 328 328 GLU CA C 53.870 0.200 1 2487 328 328 GLU CB C 32.935 0.200 1 2488 328 328 GLU CG C 35.073 0.200 1 2489 328 328 GLU N N 121.738 0.200 1 2490 329 329 ILE H H 9.222 0.020 1 2491 329 329 ILE HA H 4.187 0.020 1 2492 329 329 ILE HB H 1.878 0.020 1 2493 329 329 ILE HG12 H 1.215 0.020 1 2494 329 329 ILE HG2 H 0.869 0.020 1 2495 329 329 ILE HD1 H 0.852 0.020 1 2496 329 329 ILE CA C 61.169 0.200 1 2497 329 329 ILE CB C 38.039 0.200 1 2498 329 329 ILE CG1 C 27.519 0.200 1 2499 329 329 ILE CG2 C 17.083 0.200 1 2500 329 329 ILE CD1 C 12.204 0.200 1 2501 329 329 ILE N N 128.136 0.200 1 2502 330 330 MET H H 8.537 0.020 1 2503 330 330 MET HA H 4.306 0.020 1 2504 330 330 MET HB2 H 2.175 0.020 1 2505 330 330 MET HE H 2.113 0.020 1 2506 330 330 MET CA C 56.574 0.200 1 2507 330 330 MET CB C 34.511 0.200 1 2508 330 330 MET CE C 17.061 0.200 1 2509 330 330 MET N N 125.147 0.200 1 2510 331 331 PRO HA H 4.406 0.020 1 2511 331 331 PRO HB2 H 1.611 0.020 1 2512 331 331 PRO HD3 H 4.322 0.020 1 2513 331 331 PRO CA C 63.514 0.200 1 2514 331 331 PRO CB C 31.315 0.200 1 2515 331 331 PRO CD C 49.930 0.200 1 2516 332 332 ASN H H 7.636 0.020 1 2517 332 332 ASN HA H 4.946 0.020 1 2518 332 332 ASN HB2 H 3.304 0.020 1 2519 332 332 ASN CA C 51.427 0.200 1 2520 332 332 ASN CB C 38.389 0.200 1 2521 332 332 ASN N N 118.064 0.200 1 2522 333 333 ILE H H 6.432 0.020 1 2523 333 333 ILE HA H 4.682 0.020 1 2524 333 333 ILE HB H 2.352 0.020 1 2525 333 333 ILE HG2 H 1.216 0.020 1 2526 333 333 ILE HD1 H -0.123 0.020 1 2527 333 333 ILE CA C 59.559 0.200 1 2528 333 333 ILE CB C 36.799 0.200 1 2529 333 333 ILE CG2 C 19.396 0.200 1 2530 333 333 ILE CD1 C 12.098 0.200 1 2531 333 333 ILE N N 108.425 0.200 1 2532 334 334 PRO HA H 4.362 0.020 1 2533 334 334 PRO HB2 H 1.966 0.020 1 2534 334 334 PRO HG2 H 2.162 0.020 1 2535 334 334 PRO HD3 H 3.874 0.020 1 2536 334 334 PRO CA C 65.389 0.200 1 2537 334 334 PRO CB C 31.407 0.200 1 2538 334 334 PRO CG C 27.071 0.200 1 2539 334 334 PRO CD C 50.832 0.200 1 2540 335 335 GLN H H 8.394 0.020 1 2541 335 335 GLN HA H 4.310 0.020 1 2542 335 335 GLN HB2 H 1.586 0.020 1 2543 335 335 GLN HG2 H 2.821 0.020 1 2544 335 335 GLN HE21 H 7.793 0.020 2 2545 335 335 GLN HE22 H 6.894 0.020 2 2546 335 335 GLN CA C 59.448 0.200 1 2547 335 335 GLN CB C 26.285 0.200 1 2548 335 335 GLN CG C 34.900 0.200 1 2549 335 335 GLN N N 116.430 0.200 1 2550 335 335 GLN NE2 N 111.328 0.200 1 2551 336 336 MET H H 7.878 0.020 1 2552 336 336 MET HA H 4.511 0.020 1 2553 336 336 MET HB2 H 1.925 0.020 1 2554 336 336 MET HG2 H 2.077 0.020 1 2555 336 336 MET HE H 0.317 0.020 1 2556 336 336 MET CA C 56.016 0.200 1 2557 336 336 MET CB C 30.357 0.200 1 2558 336 336 MET CG C 32.436 0.200 1 2559 336 336 MET CE C 16.957 0.200 1 2560 336 336 MET N N 118.315 0.200 1 2561 337 337 SER H H 7.998 0.020 1 2562 337 337 SER HA H 4.103 0.020 1 2563 337 337 SER CA C 62.154 0.200 1 2564 337 337 SER N N 113.614 0.200 1 2565 338 338 ALA H H 7.390 0.020 1 2566 338 338 ALA HA H 4.446 0.020 1 2567 338 338 ALA HB H 1.716 0.020 1 2568 338 338 ALA CA C 54.618 0.200 1 2569 338 338 ALA CB C 18.554 0.200 1 2570 338 338 ALA N N 122.865 0.200 1 2571 339 339 PHE H H 7.555 0.020 1 2572 339 339 PHE HA H 3.949 0.020 1 2573 339 339 PHE HB3 H 3.502 0.020 1 2574 339 339 PHE HE1 H 6.425 0.020 1 2575 339 339 PHE HE2 H 6.425 0.020 1 2576 339 339 PHE CA C 61.808 0.200 1 2577 339 339 PHE CB C 38.988 0.200 1 2578 339 339 PHE CE1 C 130.053 0.200 1 2579 339 339 PHE N N 118.818 0.200 1 2580 340 340 TRP H H 8.808 0.020 1 2581 340 340 TRP HA H 4.596 0.020 1 2582 340 340 TRP HB3 H 3.353 0.020 1 2583 340 340 TRP HD1 H 7.337 0.020 1 2584 340 340 TRP HE1 H 10.673 0.020 1 2585 340 340 TRP HE3 H 7.609 0.020 1 2586 340 340 TRP HH2 H 6.412 0.020 1 2587 340 340 TRP CA C 60.022 0.200 1 2588 340 340 TRP CB C 30.444 0.200 1 2589 340 340 TRP CD1 C 130.844 0.200 1 2590 340 340 TRP CE3 C 120.726 0.200 1 2591 340 340 TRP CH2 C 124.723 0.200 1 2592 340 340 TRP N N 117.997 0.200 1 2593 340 340 TRP NE1 N 130.504 0.200 1 2594 341 341 TYR H H 7.460 0.020 1 2595 341 341 TYR HA H 4.302 0.020 1 2596 341 341 TYR HB3 H 3.138 0.020 1 2597 341 341 TYR CA C 61.412 0.200 1 2598 341 341 TYR CB C 38.437 0.200 1 2599 341 341 TYR N N 114.579 0.200 1 2600 342 342 ALA H H 8.475 0.020 1 2601 342 342 ALA HA H 4.034 0.020 1 2602 342 342 ALA HB H 1.514 0.020 1 2603 342 342 ALA CA C 54.857 0.200 1 2604 342 342 ALA CB C 19.079 0.200 1 2605 342 342 ALA N N 121.809 0.200 1 2606 343 343 VAL H H 8.709 0.020 1 2607 343 343 VAL HA H 3.446 0.020 1 2608 343 343 VAL HB H 1.535 0.020 1 2609 343 343 VAL HG2 H 0.158 0.020 1 2610 343 343 VAL CA C 67.015 0.200 1 2611 343 343 VAL CB C 30.801 0.200 1 2612 343 343 VAL CG2 C 22.925 0.200 1 2613 343 343 VAL N N 118.352 0.200 1 2614 344 344 ARG H H 8.147 0.020 1 2615 344 344 ARG HA H 3.945 0.020 1 2616 344 344 ARG CA C 60.354 0.200 1 2617 344 344 ARG N N 120.762 0.200 1 2618 345 345 THR H H 7.572 0.020 1 2619 345 345 THR HA H 3.793 0.020 1 2620 345 345 THR HB H 4.139 0.020 1 2621 345 345 THR HG2 H 1.170 0.020 1 2622 345 345 THR CA C 66.530 0.200 1 2623 345 345 THR CB C 69.288 0.200 1 2624 345 345 THR CG2 C 21.183 0.200 1 2625 345 345 THR N N 113.564 0.200 1 2626 346 346 ALA H H 7.821 0.020 1 2627 346 346 ALA HA H 4.225 0.020 1 2628 346 346 ALA HB H 1.311 0.020 1 2629 346 346 ALA CA C 55.491 0.200 1 2630 346 346 ALA CB C 18.589 0.200 1 2631 346 346 ALA N N 122.753 0.200 1 2632 347 347 VAL H H 8.192 0.020 1 2633 347 347 VAL HA H 3.526 0.020 1 2634 347 347 VAL HB H 2.192 0.020 1 2635 347 347 VAL HG2 H 1.057 0.020 1 2636 347 347 VAL CA C 67.563 0.200 1 2637 347 347 VAL CB C 31.161 0.200 1 2638 347 347 VAL CG2 C 22.025 0.200 1 2639 347 347 VAL N N 115.878 0.200 1 2640 348 348 ILE H H 7.808 0.020 1 2641 348 348 ILE HA H 3.834 0.020 1 2642 348 348 ILE HB H 1.927 0.020 1 2643 348 348 ILE HG12 H 1.305 0.020 1 2644 348 348 ILE HG2 H 0.962 0.020 1 2645 348 348 ILE HD1 H 0.895 0.020 1 2646 348 348 ILE CA C 65.038 0.200 1 2647 348 348 ILE CB C 37.697 0.200 1 2648 348 348 ILE CG1 C 28.747 0.200 1 2649 348 348 ILE CG2 C 16.574 0.200 1 2650 348 348 ILE CD1 C 12.809 0.200 1 2651 348 348 ILE N N 118.355 0.200 1 2652 349 349 ASN H H 8.856 0.020 1 2653 349 349 ASN HA H 4.405 0.020 1 2654 349 349 ASN HB2 H 3.160 0.020 1 2655 349 349 ASN HD21 H 7.436 0.020 2 2656 349 349 ASN HD22 H 6.784 0.020 2 2657 349 349 ASN CA C 55.873 0.200 1 2658 349 349 ASN CB C 37.106 0.200 1 2659 349 349 ASN N N 121.058 0.200 1 2660 349 349 ASN ND2 N 109.714 0.200 1 2661 350 350 ALA H H 8.554 0.020 1 2662 350 350 ALA HA H 4.734 0.020 1 2663 350 350 ALA HB H 1.335 0.020 1 2664 350 350 ALA CA C 53.925 0.200 1 2665 350 350 ALA CB C 17.856 0.200 1 2666 350 350 ALA N N 122.684 0.200 1 2667 351 351 ALA H H 9.182 0.020 1 2668 351 351 ALA HA H 4.025 0.020 1 2669 351 351 ALA HB H 1.476 0.020 1 2670 351 351 ALA CA C 55.518 0.200 1 2671 351 351 ALA CB C 17.910 0.200 1 2672 351 351 ALA N N 120.917 0.200 1 2673 352 352 SER H H 7.923 0.020 1 2674 352 352 SER HA H 4.413 0.020 1 2675 352 352 SER HB2 H 4.088 0.020 1 2676 352 352 SER CA C 58.835 0.200 1 2677 352 352 SER CB C 64.295 0.200 1 2678 352 352 SER N N 107.833 0.200 1 2679 353 353 GLY H H 7.657 0.020 1 2680 353 353 GLY HA3 H 4.242 0.020 1 2681 353 353 GLY CA C 45.578 0.200 1 2682 353 353 GLY N N 109.659 0.200 1 2683 354 354 ARG H H 8.262 0.020 1 2684 354 354 ARG HA H 4.145 0.020 1 2685 354 354 ARG HB3 H 1.803 0.020 1 2686 354 354 ARG HD2 H 3.161 0.020 1 2687 354 354 ARG CA C 58.444 0.200 1 2688 354 354 ARG CB C 30.877 0.200 1 2689 354 354 ARG CD C 43.012 0.200 1 2690 354 354 ARG N N 120.903 0.200 1 2691 355 355 GLN H H 7.371 0.020 1 2692 355 355 GLN HA H 4.744 0.020 1 2693 355 355 GLN HB2 H 1.519 0.020 1 2694 355 355 GLN HG2 H 2.449 0.020 1 2695 355 355 GLN HE21 H 7.521 0.020 2 2696 355 355 GLN HE22 H 6.891 0.020 2 2697 355 355 GLN CA C 54.190 0.200 1 2698 355 355 GLN CB C 36.472 0.200 1 2699 355 355 GLN CG C 35.753 0.200 1 2700 355 355 GLN N N 113.533 0.200 1 2701 355 355 GLN NE2 N 112.090 0.200 1 2702 356 356 THR H H 8.586 0.020 1 2703 356 356 THR HA H 4.362 0.020 1 2704 356 356 THR HB H 4.763 0.020 1 2705 356 356 THR HG2 H 1.362 0.020 1 2706 356 356 THR CA C 61.341 0.200 1 2707 356 356 THR CB C 70.561 0.200 1 2708 356 356 THR CG2 C 21.692 0.200 1 2709 356 356 THR N N 111.666 0.200 1 2710 357 357 VAL H H 8.763 0.020 1 2711 357 357 VAL HA H 3.380 0.020 1 2712 357 357 VAL HB H 2.063 0.020 1 2713 357 357 VAL HG2 H 1.070 0.020 1 2714 357 357 VAL CA C 67.942 0.200 1 2715 357 357 VAL CB C 31.385 0.200 1 2716 357 357 VAL CG2 C 23.080 0.200 1 2717 357 357 VAL N N 121.350 0.200 1 2718 358 358 ASP H H 8.156 0.020 1 2719 358 358 ASP HA H 4.121 0.020 1 2720 358 358 ASP HB2 H 2.551 0.020 1 2721 358 358 ASP CA C 57.663 0.200 1 2722 358 358 ASP CB C 40.880 0.200 1 2723 358 358 ASP N N 115.098 0.200 1 2724 359 359 GLU H H 7.627 0.020 1 2725 359 359 GLU HA H 3.893 0.020 1 2726 359 359 GLU HB2 H 2.111 0.020 1 2727 359 359 GLU HG2 H 2.247 0.020 1 2728 359 359 GLU CA C 58.834 0.200 1 2729 359 359 GLU CB C 30.212 0.200 1 2730 359 359 GLU CG C 36.511 0.200 1 2731 359 359 GLU N N 118.595 0.200 1 2732 360 360 ALA H H 8.724 0.020 1 2733 360 360 ALA HA H 4.050 0.020 1 2734 360 360 ALA HB H 1.437 0.020 1 2735 360 360 ALA CA C 54.849 0.200 1 2736 360 360 ALA CB C 18.306 0.200 1 2737 360 360 ALA N N 121.421 0.200 1 2738 361 361 LEU H H 8.111 0.020 1 2739 361 361 LEU HA H 4.055 0.020 1 2740 361 361 LEU HB3 H 1.648 0.020 1 2741 361 361 LEU HG H 1.572 0.020 1 2742 361 361 LEU HD1 H 0.919 0.020 1 2743 361 361 LEU CA C 57.411 0.200 1 2744 361 361 LEU CB C 39.921 0.200 1 2745 361 361 LEU CG C 26.739 0.200 1 2746 361 361 LEU CD1 C 24.300 0.200 1 2747 361 361 LEU N N 116.136 0.200 1 2748 362 362 LYS H H 7.739 0.020 1 2749 362 362 LYS HA H 4.125 0.020 1 2750 362 362 LYS HB3 H 1.865 0.020 1 2751 362 362 LYS HG3 H 1.504 0.020 1 2752 362 362 LYS HD3 H 1.670 0.020 1 2753 362 362 LYS CA C 59.791 0.200 1 2754 362 362 LYS CB C 31.695 0.200 1 2755 362 362 LYS CG C 24.343 0.200 1 2756 362 362 LYS CD C 28.502 0.200 1 2757 362 362 LYS N N 121.437 0.200 1 2758 363 363 ASP H H 8.184 0.020 1 2759 363 363 ASP HA H 4.406 0.020 1 2760 363 363 ASP HB2 H 2.889 0.020 1 2761 363 363 ASP CA C 57.213 0.200 1 2762 363 363 ASP CB C 40.401 0.200 1 2763 363 363 ASP N N 120.039 0.200 1 2764 364 364 ALA H H 7.771 0.020 1 2765 364 364 ALA HA H 4.128 0.020 1 2766 364 364 ALA HB H 1.282 0.020 1 2767 364 364 ALA CA C 55.215 0.200 1 2768 364 364 ALA CB C 17.673 0.200 1 2769 364 364 ALA N N 121.260 0.200 1 2770 365 365 GLN H H 8.288 0.020 1 2771 365 365 GLN HA H 3.598 0.020 1 2772 365 365 GLN HB2 H 2.208 0.020 1 2773 365 365 GLN HG2 H 2.602 0.020 1 2774 365 365 GLN HE21 H 7.368 0.020 2 2775 365 365 GLN HE22 H 7.001 0.020 2 2776 365 365 GLN CA C 60.400 0.200 1 2777 365 365 GLN CB C 27.403 0.200 1 2778 365 365 GLN CG C 31.719 0.200 1 2779 365 365 GLN N N 118.108 0.200 1 2780 365 365 GLN NE2 N 110.523 0.200 1 2781 366 366 THR H H 8.198 0.020 1 2782 366 366 THR HA H 3.915 0.020 1 2783 366 366 THR HB H 4.403 0.020 1 2784 366 366 THR HG2 H 1.285 0.020 1 2785 366 366 THR CA C 66.170 0.200 1 2786 366 366 THR CB C 69.017 0.200 1 2787 366 366 THR CG2 C 21.319 0.200 1 2788 366 366 THR N N 115.167 0.200 1 2789 367 367 ARG H H 7.998 0.020 1 2790 367 367 ARG HA H 4.136 0.020 1 2791 367 367 ARG HB3 H 2.015 0.020 1 2792 367 367 ARG HG3 H 1.879 0.020 1 2793 367 367 ARG HD2 H 3.236 0.020 1 2794 367 367 ARG CA C 58.863 0.200 1 2795 367 367 ARG CB C 29.947 0.200 1 2796 367 367 ARG CG C 27.685 0.200 1 2797 367 367 ARG CD C 43.163 0.200 1 2798 367 367 ARG N N 119.967 0.200 1 2799 368 368 ILE H H 8.044 0.020 1 2800 368 368 ILE HA H 3.773 0.020 1 2801 368 368 ILE HB H 1.765 0.020 1 2802 368 368 ILE HG12 H 0.613 0.020 1 2803 368 368 ILE HG2 H 1.076 0.020 1 2804 368 368 ILE HD1 H 0.707 0.020 1 2805 368 368 ILE CA C 64.885 0.200 1 2806 368 368 ILE CB C 38.897 0.200 1 2807 368 368 ILE CG1 C 28.999 0.200 1 2808 368 368 ILE CG2 C 19.697 0.200 1 2809 368 368 ILE CD1 C 14.999 0.200 1 2810 368 368 ILE N N 117.263 0.200 1 2811 369 369 THR H H 7.668 0.020 1 2812 369 369 THR HA H 4.528 0.020 1 2813 369 369 THR HB H 4.636 0.020 1 2814 369 369 THR HG2 H 1.397 0.020 1 2815 369 369 THR CA C 62.477 0.200 1 2816 369 369 THR CB C 70.386 0.200 1 2817 369 369 THR CG2 C 21.724 0.200 1 2818 369 369 THR N N 106.881 0.200 1 2819 370 370 LYS H H 7.430 0.020 1 2820 370 370 LYS HA H 4.180 0.020 1 2821 370 370 LYS HB3 H 1.891 0.020 1 2822 370 370 LYS HG3 H 1.510 0.020 1 2823 370 370 LYS HD3 H 1.726 0.020 1 2824 370 370 LYS CA C 58.917 0.200 1 2825 370 370 LYS CB C 32.647 0.200 1 2826 370 370 LYS CG C 23.539 0.200 1 2827 370 370 LYS CD C 28.936 0.200 1 2828 370 370 LYS N N 128.109 0.200 1 stop_ save_