data_4354 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR Studies of a 42kDa Escherichia coli Maltose Binding Protein/ Beta-Cyclodextrin Complex: Chemical Shift Assignments and Analysis ; _BMRB_accession_number 4354 _BMRB_flat_file_name bmr4354.str _Entry_type original _Submission_date 1999-06-10 _Accession_date 1999-06-10 _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 Gardner Kevin H. . 2 Zhang Xiaochen . . 3 Gehring Kalle . . 4 Kay Lewis E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 472 "13C chemical shifts" 1198 "15N chemical shifts" 330 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-24 update author 'chemical shift update for residues 81 and 82' 1999-06-10 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Gardner, K. H., Zhang, X., Gehring, K., and Kay, L. E., "Solution NMR Studies of a 42kDa Escherichia coli Maltose Binding Protein/Beta-Cyclodextrin Complex: Chemical Shift Assignments and Analysis," J. Am. Chem. Soc. 120, 11738-11748 (1998). ; _Citation_title ; Solution NMR Studies of a 42kDa Escherichia coli Maltose Binding Protein/ Beta-Cyclodextrin Complex: Chemical Shift Assignments and Analysis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gardner Kevin H. . 2 Zhang Xiaochen . . 3 Gehring Kalle . . 4 Kay Lewis E. . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 120 _Journal_issue 45 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11738 _Page_last 11748 _Year 1998 _Details . loop_ _Keyword deuteration MBP stop_ save_ ####################################### # Cited references within the entry # ####################################### save_reference_1 _Saveframe_category citation _Citation_full ; Gardner, K.H., Zhang, X., Gehring, K. and Kay, L.E. "Solution NMR Studies of a 42KDa Escherichia coli Maltose Binding Protein/Beta-Cyclodextrin Complex: Chemical Shift Assignments and Analysis." J. Am. Chem. Soc. 120(1998): 11738-11748. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_MBP _Saveframe_category molecular_system _Mol_system_name 'E. coli maltose binding protein' _Abbreviation_common MBP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label MBP $MBP beta-cyclodextrin $BCD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'binds maltose and related sugars' stop_ _Database_query_date . _Details ; As of late 1998, this was one of the largest monomeric proteins with >95% complete backbone assignments and a significant number of sidechain assignments. This protein was also used to demonstrate the utility of 2H (1H-methyl) labeling protocols. ; save_ ######################## # Monomeric polymers # ######################## save_MBP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'E. coli maltose binding protein' _Abbreviation_common MBP _Molecular_mass 40695.2 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 370 _Mol_residue_sequence ; KTEEGKLVIWINGDKGYNGL AEVGKKFEKDTGIKVTVEHP DKLEEKFPQVAATGDGPDII FWAHDRFGGYAQSGLLAEIT PDKAFQDKLYPFTWDAVRYN GKLIAYPIAVEALSLIYNKD LLPNPPKTWEEIPALDKELK AKGKSALMFNLQEPYFTWPL IAADGGYAFKYENGKYDIKD VGVDNAGAKAGLTFLVDLIK NKHMNADTDYSIAEAAFNKG ETAMTINGPWAWSNIDTSKV NYGVTVLPTFKGQPSKPFVG VLSAGINAASPNKELAKEFL ENYLLTDEGLEAVNKDKPLG AVALKSYEEELAKDPRIAAT MENAQKGEIMPNIPQMSAFW YAVRTAVINAASGRQTVDEA LKDAQTRITK ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 THR 3 GLU 4 GLU 5 GLY 6 LYS 7 LEU 8 VAL 9 ILE 10 TRP 11 ILE 12 ASN 13 GLY 14 ASP 15 LYS 16 GLY 17 TYR 18 ASN 19 GLY 20 LEU 21 ALA 22 GLU 23 VAL 24 GLY 25 LYS 26 LYS 27 PHE 28 GLU 29 LYS 30 ASP 31 THR 32 GLY 33 ILE 34 LYS 35 VAL 36 THR 37 VAL 38 GLU 39 HIS 40 PRO 41 ASP 42 LYS 43 LEU 44 GLU 45 GLU 46 LYS 47 PHE 48 PRO 49 GLN 50 VAL 51 ALA 52 ALA 53 THR 54 GLY 55 ASP 56 GLY 57 PRO 58 ASP 59 ILE 60 ILE 61 PHE 62 TRP 63 ALA 64 HIS 65 ASP 66 ARG 67 PHE 68 GLY 69 GLY 70 TYR 71 ALA 72 GLN 73 SER 74 GLY 75 LEU 76 LEU 77 ALA 78 GLU 79 ILE 80 THR 81 PRO 82 ASP 83 LYS 84 ALA 85 PHE 86 GLN 87 ASP 88 LYS 89 LEU 90 TYR 91 PRO 92 PHE 93 THR 94 TRP 95 ASP 96 ALA 97 VAL 98 ARG 99 TYR 100 ASN 101 GLY 102 LYS 103 LEU 104 ILE 105 ALA 106 TYR 107 PRO 108 ILE 109 ALA 110 VAL 111 GLU 112 ALA 113 LEU 114 SER 115 LEU 116 ILE 117 TYR 118 ASN 119 LYS 120 ASP 121 LEU 122 LEU 123 PRO 124 ASN 125 PRO 126 PRO 127 LYS 128 THR 129 TRP 130 GLU 131 GLU 132 ILE 133 PRO 134 ALA 135 LEU 136 ASP 137 LYS 138 GLU 139 LEU 140 LYS 141 ALA 142 LYS 143 GLY 144 LYS 145 SER 146 ALA 147 LEU 148 MET 149 PHE 150 ASN 151 LEU 152 GLN 153 GLU 154 PRO 155 TYR 156 PHE 157 THR 158 TRP 159 PRO 160 LEU 161 ILE 162 ALA 163 ALA 164 ASP 165 GLY 166 GLY 167 TYR 168 ALA 169 PHE 170 LYS 171 TYR 172 GLU 173 ASN 174 GLY 175 LYS 176 TYR 177 ASP 178 ILE 179 LYS 180 ASP 181 VAL 182 GLY 183 VAL 184 ASP 185 ASN 186 ALA 187 GLY 188 ALA 189 LYS 190 ALA 191 GLY 192 LEU 193 THR 194 PHE 195 LEU 196 VAL 197 ASP 198 LEU 199 ILE 200 LYS 201 ASN 202 LYS 203 HIS 204 MET 205 ASN 206 ALA 207 ASP 208 THR 209 ASP 210 TYR 211 SER 212 ILE 213 ALA 214 GLU 215 ALA 216 ALA 217 PHE 218 ASN 219 LYS 220 GLY 221 GLU 222 THR 223 ALA 224 MET 225 THR 226 ILE 227 ASN 228 GLY 229 PRO 230 TRP 231 ALA 232 TRP 233 SER 234 ASN 235 ILE 236 ASP 237 THR 238 SER 239 LYS 240 VAL 241 ASN 242 TYR 243 GLY 244 VAL 245 THR 246 VAL 247 LEU 248 PRO 249 THR 250 PHE 251 LYS 252 GLY 253 GLN 254 PRO 255 SER 256 LYS 257 PRO 258 PHE 259 VAL 260 GLY 261 VAL 262 LEU 263 SER 264 ALA 265 GLY 266 ILE 267 ASN 268 ALA 269 ALA 270 SER 271 PRO 272 ASN 273 LYS 274 GLU 275 LEU 276 ALA 277 LYS 278 GLU 279 PHE 280 LEU 281 GLU 282 ASN 283 TYR 284 LEU 285 LEU 286 THR 287 ASP 288 GLU 289 GLY 290 LEU 291 GLU 292 ALA 293 VAL 294 ASN 295 LYS 296 ASP 297 LYS 298 PRO 299 LEU 300 GLY 301 ALA 302 VAL 303 ALA 304 LEU 305 LYS 306 SER 307 TYR 308 GLU 309 GLU 310 GLU 311 LEU 312 ALA 313 LYS 314 ASP 315 PRO 316 ARG 317 ILE 318 ALA 319 ALA 320 THR 321 MET 322 GLU 323 ASN 324 ALA 325 GLN 326 LYS 327 GLY 328 GLU 329 ILE 330 MET 331 PRO 332 ASN 333 ILE 334 PRO 335 GLN 336 MET 337 SER 338 ALA 339 PHE 340 TRP 341 TYR 342 ALA 343 VAL 344 ARG 345 THR 346 ALA 347 VAL 348 ILE 349 ASN 350 ALA 351 ALA 352 SER 353 GLY 354 ARG 355 GLN 356 THR 357 VAL 358 ASP 359 GLU 360 ALA 361 LEU 362 LYS 363 ASP 364 ALA 365 GLN 366 THR 367 ARG 368 ILE 369 THR 370 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-24 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 25237 ER690 100.00 370 99.46 99.46 0.00e+00 PDB 1A7L "Dominant B-Cell Epitope From The Pres2 Region Of Hepatitis B Virus In The Form Of An Inserted Peptide Segment In Maltodextrin-B" 98.65 389 99.18 99.18 0.00e+00 PDB 1ANF "Maltodextrin Binding Protein With Bound Maltose" 100.00 370 99.73 99.73 0.00e+00 PDB 1DMB "Refined 1.8 Angstroms Structure Reveals The Mechanism Of Binding Of A Cyclic Sugar, Beta-Cyclodextrin, To The Maltodextrin Bind" 100.00 370 99.73 99.73 0.00e+00 PDB 1EZ9 "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P1 Crystal Form" 100.00 370 99.73 99.73 0.00e+00 PDB 1EZO "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 100.00 100.00 0.00e+00 PDB 1EZP "Global Fold Of Maltodextrin Binding Protein Complexed With Beta-Cyclodextrin Using Peptide Orientations From Dipolar Couplings" 100.00 370 100.00 100.00 0.00e+00 PDB 1FQA "Structure Of Maltotetraitol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQB "Structure Of Maltotriotol Bound To Open-Form Maltodextrin Binding Protein In P2(1)crystal Form" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQC "Crystal Structure Of Maltotriotol Bound To Closed-Form Maltodextrin Binding Protein" 99.46 370 100.00 100.00 0.00e+00 PDB 1FQD "Crystal Structure Of Maltotetraitol Bound To Closed-Form Maltodextrin Binding Protein" 99.46 370 100.00 100.00 0.00e+00 PDB 1HSJ "Sarr Mbp Fusion Structure" 98.92 487 99.18 99.18 0.00e+00 PDB 1JVX "Maltodextrin-Binding Protein Variant D207cA301GSP316C Cross-Linked In Crystal" 100.27 372 98.65 98.92 0.00e+00 PDB 1JVY "Maltodextrin-Binding Protein Variant D207cA301GSP316C With Beta-Mercaptoethanol Mixed Disulfides" 100.27 372 98.65 98.92 0.00e+00 PDB 1JW4 "Structure Of Ligand-Free Maltodextrin-Binding Protein" 100.00 370 99.73 99.73 0.00e+00 PDB 1JW5 "Structure Of Maltose Bound To Open-Form Maltodextrin- Binding Protein In P1 Crystal" 100.00 370 99.73 99.73 0.00e+00 PDB 1LAX "Crystal Structure Of Male31, A Defective Folding Mutant Of Maltose-Binding Protein" 100.00 370 99.19 99.19 0.00e+00 PDB 1LLS "Crystal Structure Of Unliganded Maltose Binding Protein With Xenon" 100.00 370 99.73 99.73 0.00e+00 PDB 1MDP "Refined Structures Of Two Insertion(Slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.00 363 97.30 97.30 0.00e+00 PDB 1MDQ "Refined Structures Of Two Insertion(slash)deletion Mutants Probe Function Of The Maltodextrin Binding Protein" 100.27 371 99.19 99.46 0.00e+00 PDB 1MG1 "Htlv-1 Gp21 EctodomainMALTOSE-Binding Protein Chimera" 97.84 450 99.17 99.17 0.00e+00 PDB 1MH3 "Maltose Binding-A1 Homeodomain Protein Chimera, Crystal Form I" 98.92 421 98.91 98.91 0.00e+00 PDB 1MH4 "Maltose Binding-A1 Homeodomain Protein Chimera, Crystal Form Ii" 98.92 421 98.91 98.91 0.00e+00 PDB 1MPB "Maltodextrin-Binding Protein (Maltose-Binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (Trp-230-Arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1MPC "Maltodextrin-binding Protein (maltose-binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (trp-230-arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1MPD "Maltodextrin-Binding Protein (Maltose-Binding Protein) Mutant, With Arginine Replacing Tryptophan At Position 230 (Trp-230-Arg)" 100.00 370 99.46 99.46 0.00e+00 PDB 1N3W "Engineered High-affinity Maltose-binding Protein" 100.00 366 98.38 98.38 0.00e+00 PDB 1N3X "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 98.38 98.38 0.00e+00 PDB 1NL5 "Engineered High-affinity Maltose-binding Protein" 100.00 366 97.84 97.84 0.00e+00 PDB 1NMU Mbp-L30 98.92 382 99.73 99.73 0.00e+00 PDB 1OMP "Crystallographic Evidence Of A Large Ligand-Induced Hinge- Twist Motion Between The Two Domains Of The Maltodextrin- Binding Pr" 100.00 370 99.73 99.73 0.00e+00 PDB 1PEB "Ligand-Free High-Affinity Maltose-Binding Protein" 100.00 366 97.84 97.84 0.00e+00 PDB 1R6Z "The Crystal Structure Of The Argonaute2 Paz Domain (as A Mbp Fusion)" 98.92 509 99.73 99.73 0.00e+00 PDB 1SVX "Crystal Structure Of A Designed Selected Ankyrin Repeat Protein In Complex With The Maltose Binding Protein" 98.92 395 100.00 100.00 0.00e+00 PDB 1T0K "Joint X-ray And Nmr Refinement Of Yeast L30e-mrna Complex" 98.92 381 99.73 99.73 0.00e+00 PDB 1Y4C "Designed Helical Protein Fusion Mbp" 98.92 494 99.73 99.73 0.00e+00 PDB 1YTV "Maltose-binding Protein Fusion To A C-terminal Fragment Of The V1a Vasopressin Receptor" 98.92 366 99.73 99.73 0.00e+00 PDB 1ZIU "Crystal Structure Of Nickel-bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZJL "Crystal Structure Of Zinc-Bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZKB "Zinc-Free Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 1ZMG "Crystal Structure Of Copper-Bound Engineered Maltose Binding Protein" 100.00 370 98.38 98.38 0.00e+00 PDB 2D21 "Nmr Structure Of Stereo-Array Isotope Labelled (Sail) Maltodextrin-Binding Protein (Mbp)" 100.00 370 99.73 99.73 0.00e+00 PDB 2H25 "Solution Structure Of Maltose Binding Protein Complexed With Beta-Cyclodextrin" 100.00 370 100.00 100.00 0.00e+00 PDB 2KLF "Pere Nmr Structure Of Maltodextrin-Binding Protein" 100.00 370 100.00 100.00 0.00e+00 PDB 2MV0 "Solution Nmr Structure Of Maltose-binding Protein From Escherichia Coli, Northeast Structural Genomics Consortium (nesg) Target" 100.00 370 99.73 99.73 0.00e+00 PDB 2N44 "Ec-nmr Structure Of Escherichia Coli Maltose-binding Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr" 100.00 370 99.73 99.73 0.00e+00 PDB 2N45 "Ec-nmr Structure Of Escherichia Coli Maltose-binding Protein Determined By Combining Evolutionary Couplings (ec) And Sparse Nmr" 100.00 370 99.73 99.73 0.00e+00 PDB 2NVU "Structure Of Appbp1-Uba3~nedd8-Nedd8-Mgatp-Ubc12(C111a), A Trapped Ubiquitin-Like Protein Activation Complex" 98.92 805 98.91 98.91 0.00e+00 PDB 2OBG "Crystal Structure Of Monobody Mbp-74MALTOSE BINDING PROTEIN FUSION Complex" 98.92 461 100.00 100.00 0.00e+00 PDB 2OK2 "Muts C-Terminal Domain Fused To Maltose Binding Protein" 98.92 402 99.45 99.73 0.00e+00 PDB 2R6G "The Crystal Structure Of The E. Coli Maltose Transporter" 100.00 370 99.73 99.73 0.00e+00 PDB 2V93 "Equillibrium Mixture Of Open And Partially-Closed Species In The Apo State Of Maltodextrin-Binding Protein By Paramagnetic Rela" 100.00 370 99.19 99.19 0.00e+00 PDB 2VGQ "Crystal Structure Of Human Ips-1 Card" 98.92 477 99.73 99.73 0.00e+00 PDB 2XZ3 "Blv Tm Hairpin" 98.92 463 98.91 98.91 0.00e+00 PDB 2ZXT "Crystal Structure Of Tim40/mia40, A Disulfide Relay System In Mitochondria, Solved As Mbp Fusion Protein" 98.92 465 99.73 99.73 0.00e+00 PDB 3A3C "Crystal Structure Of Tim40/mia40 Fusing Mbp, C296s And C298s Mutant" 98.38 451 100.00 100.00 0.00e+00 PDB 3C4M "Structure Of Human Parathyroid Hormone In Complex With The Extracellular Domain Of Its G-Protein-Coupled Receptor (Pth1r)" 98.92 539 99.73 99.73 0.00e+00 PDB 3CSB "Crystal Structure Of Monobody Ysx1MALTOSE BINDING PROTEIN Fusion Complex" 98.92 465 100.00 100.00 0.00e+00 PDB 3CSG "Crystal Structure Of Monobody Ys1(Mbp-74)MALTOSE BINDING Protein Fusion Complex" 98.92 461 100.00 100.00 0.00e+00 PDB 3D4C "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form I)" 98.92 481 99.18 99.18 0.00e+00 PDB 3D4G "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Ii)" 98.92 481 99.18 99.18 0.00e+00 PDB 3DM0 "Maltose Binding Protein Fusion With Rack1 From A. Thaliana" 98.92 694 98.09 98.09 0.00e+00 PDB 3EF7 "Zp-N Domain Of Mammalian Sperm Receptor Zp3 (Crystal Form Iii)" 98.92 481 99.18 99.18 0.00e+00 PDB 3EHS "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (Crfr1)" 98.92 476 99.73 99.73 0.00e+00 PDB 3EHT "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (crfr1) In Complex With C" 98.92 476 99.45 99.45 0.00e+00 PDB 3EHU "Crystal Structure Of The Extracellular Domain Of Human Corticotropin Releasing Factor Receptor Type 1 (crfr1) In Complex With C" 98.92 476 99.45 99.45 0.00e+00 PDB 3F5F "Crystal Structure Of Heparan Sulfate 2-O-Sulfotransferase From Gallus Gallus As A Maltose Binding Protein Fusion" 98.92 658 98.91 98.91 0.00e+00 PDB 3G7V "Islet Amyloid Polypeptide (iapp Or Amylin) Fused To Maltose Binding Protein" 99.19 408 98.64 98.64 0.00e+00 PDB 3G7W "Islet Amyloid Polypeptide (Iapp Or Amylin) Residues 1 To 22 Fused To Maltose Binding Protein" 98.92 393 98.91 98.91 0.00e+00 PDB 3H3G "Crystal Structure Of The Extracellular Domain Of The Human Parathyroid Hormone Receptor (Pth1r) In Complex With Parathyroid Hor" 98.92 539 99.73 99.73 0.00e+00 PDB 3H4Z "Crystal Structure Of An Mbp-Der P 7 Fusion Protein" 98.92 568 97.54 97.54 0.00e+00 PDB 3HPI "Crystal Structure Of Maltose-Binding Protein Mutant With Bound Sucrose" 100.00 372 98.65 98.92 0.00e+00 PDB 3HST "N-Terminal Rnase H Domain Of Rv2228c From Mycobacterium Tuberculosis As A Fusion Protein With Maltose Binding Protein" 99.19 387 99.46 99.46 0.00e+00 PDB 3IO4 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C90" 98.92 449 98.91 98.91 0.00e+00 PDB 3IO6 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-A" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOR "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C95" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOT "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C92-b" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOU "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C94" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOV "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C99" 98.92 449 98.91 98.91 0.00e+00 PDB 3IOW "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C99-hg" 98.92 449 98.91 98.91 0.00e+00 PDB 3J9P "Structure Of The Trpa1 Ion Channel Determined By Electron Cryo- Microscopy" 98.92 1528 99.73 99.73 0.00e+00 PDB 3KJT "Stimulation Of The Maltose Transporter By A Mutant Sucrose B Protein Gives Insights Into Abc Transporter Coupling" 100.00 372 98.65 98.92 0.00e+00 PDB 3L2J "Dimeric Structure Of The Ligand-Free Extracellular Domain Of Parathyroid Hormone Receptor (Pth1r)" 98.38 535 100.00 100.00 0.00e+00 PDB 3LBS "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Bound Form)" 98.38 384 99.45 100.00 0.00e+00 PDB 3LC8 "Crystal Structure Of The Cytoplasmic Tail Of (Pro)renin Receptor As A Mbp Fusion (Maltose-Free Form)" 98.38 384 99.45 100.00 0.00e+00 PDB 3MBP "Maltodextrin-Binding Protein With Bound Maltotriose" 100.00 370 99.73 99.73 0.00e+00 PDB 3MP1 "Complex Structure Of Sgf29 And Trimethylated H3k4" 98.92 522 99.18 99.18 0.00e+00 PDB 3MP6 "Complex Structure Of Sgf29 And Dimethylated H3k4" 98.92 522 99.18 99.18 0.00e+00 PDB 3MP8 "Crystal Structure Of Sgf29 Tudor Domain" 98.92 522 99.18 99.18 0.00e+00 PDB 3MQ9 "Crystal Structure Of Ectodomain Mutant Of Bst-2TETHERINCD317 FUSED To Mbp" 99.73 471 99.73 99.73 0.00e+00 PDB 3N93 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 3" 98.92 482 99.73 99.73 0.00e+00 PDB 3N94 "Crystal Structure Of Human Pituitary Adenylate Cyclase 1 Receptor- Short N-Terminal Extracellular Domain" 98.92 475 99.73 99.73 0.00e+00 PDB 3N95 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 2" 98.92 482 99.73 99.73 0.00e+00 PDB 3N96 "Crystal Structure Of Human Crfr2 Alpha Extracellular Domain In Complex With Urocortin 1" 98.92 482 99.73 99.73 0.00e+00 PDB 3O3U "Crystal Structure Of Human Receptor For Advanced Glycation Endproducts (Rage)" 98.38 581 99.18 99.18 0.00e+00 PDB 3OAI "Crystal Structure Of The Extra-Cellular Domain Of Human Myelin Protein Zero" 99.19 507 99.46 99.46 0.00e+00 PDB 3OB4 "Mbp-Fusion Protein Of The Major Peanut Allergen Ara H 2" 98.92 500 97.54 97.54 0.00e+00 PDB 3PGF "Crystal Structure Of Maltose Bound Mbp With A Conformationally Specific Synthetic Antigen Binder (Sab)" 99.19 398 99.46 99.46 0.00e+00 PDB 3PUV "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Vo4" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUW "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Alf4" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUX "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Adp-Bef3" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUY "Crystal Structure Of An Outward-Facing Mbp-Maltose Transporter Complex Bound To Amp-Pnp After Crystal Soaking Of The Pretranslo" 100.00 378 99.73 99.73 0.00e+00 PDB 3PUZ "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Bound To Amp-Pnp" 100.00 370 99.19 99.19 0.00e+00 PDB 3PV0 "Crystal Structure Of A Pre-Translocation State Mbp-Maltose Transporter Complex Without Nucleotide" 100.00 370 99.19 99.19 0.00e+00 PDB 3PY7 "Crystal Structure Of Full-length Bovine Papillomavirus Oncoprotein E6 In Complex With Ld1 Motif Of Paxillin At 2.3a Resolution" 98.92 523 98.09 98.09 0.00e+00 PDB 3Q25 "Crystal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 99.73 99.73 0.00e+00 PDB 3Q26 "Cyrstal Structure Of Human Alpha-Synuclein (10-42) Fused To Maltose Binding Protein (Mbp)" 98.92 404 99.73 99.73 0.00e+00 PDB 3Q27 "Cyrstal Structure Of Human Alpha-Synuclein (32-57) Fused To Maltose Binding Protein (Mbp)" 98.92 397 99.73 99.73 0.00e+00 PDB 3Q28 "Cyrstal Structure Of Human Alpha-Synuclein (58-79) Fused To Maltose Binding Protein (Mbp)" 99.19 393 99.46 99.46 0.00e+00 PDB 3Q29 "Cyrstal Structure Of Human Alpha-Synuclein (1-19) Fused To Maltose Binding Protein (Mbp)" 98.92 390 99.73 99.73 0.00e+00 PDB 3RLF "Crystal Structure Of The Maltose-Binding ProteinMALTOSE TRANSPORTER Complex In An Outward-Facing Conformation Bound To Mgamppnp" 100.00 380 99.73 99.73 0.00e+00 PDB 3RUM "New Strategy To Analyze Structures Of Glycopeptide Antibiotic-Target Complexes" 98.92 378 99.73 99.73 0.00e+00 PDB 3SER "Zn-Mediated Polymer Of Maltose-Binding Protein K26hK30H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SES "Cu-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SET "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form I)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEU "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Iii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEV "Zn-Mediated Trimer Of Maltose-Binding Protein E310hK314H BY SYNTHETIC Symmetrization" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEW "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form I)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEX "Ni-Mediated Dimer Of Maltose-Binding Protein A216hK220H BY SYNTHETIC Symmetrization (Form Ii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3SEY "Zn-Mediated Polymer Of Maltose-Binding Protein A216hK220H BY Synthetic Symmetrization (Form Ii)" 99.19 372 98.09 98.09 0.00e+00 PDB 3VD8 "Crystal Structure Of Human Aim2 Pyd Domain With Mbp Fusion" 98.92 489 97.54 97.54 0.00e+00 PDB 3VFJ "The Structure Of Monodechloro-teicoplanin In Complex With Its Ligand, Using Mbp As A Ligand Carrier" 98.92 378 99.73 99.73 0.00e+00 PDB 3W15 "Structure Of Peroxisomal Targeting Signal 2 (pts2) Of Saccharomyces Cerevisiae 3-ketoacyl-coa Thiolase In Complex With Pex7p An" 100.00 389 99.73 99.73 0.00e+00 PDB 3WAI "Crystal Structure Of The C-terminal Globular Domain Of Oligosaccharyltransferase (afaglb-l, O29867_arcfu) From Archaeoglobus Fu" 98.92 739 99.73 99.73 0.00e+00 PDB 3WOA "Crystal Structure Of Lambda Repressor (1-45) Fused With Maltose- Binding Protein" 98.92 417 99.73 99.73 0.00e+00 PDB 4B3N "Crystal Structure Of Rhesus Trim5alpha PrySPRY DOMAIN" 100.00 602 99.19 99.73 0.00e+00 PDB 4BL8 "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu)" 98.92 831 99.18 99.18 0.00e+00 PDB 4BL9 "Crystal Structure Of Full-length Human Suppressor Of Fused ( Sufu) Mutant Lacking A Regulatory Subdomain (crystal Form I)" 98.92 756 99.18 99.18 0.00e+00 PDB 4BLA "Crystal Structure Of Full-length Human Suppressor Of Fused (sufu) Mutant Lacking A Regulatory Subdomain (crystal Form Ii)" 98.92 756 99.18 99.18 0.00e+00 PDB 4BLB "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli1p Complex" 98.92 753 98.63 98.63 0.00e+00 PDB 4BLD "Crystal Structure Of A Human Suppressor Of Fused (sufu)- Gli3p Complex" 98.92 753 98.63 98.63 0.00e+00 PDB 4EDQ "Mbp-fusion Protein Of Myosin-binding Protein C Residues 149-269" 98.92 492 98.91 98.91 0.00e+00 PDB 4EGC "Crystal Structure Of Mbp-fused Human Six1 Bound To Human Eya2 Eya Domain" 98.92 559 98.36 98.36 0.00e+00 PDB 4EXK "A Chimera Protein Containing Mbp Fused To The C-Terminal Domain Of The Uncharacterized Protein Stm14_2015 From Salmonella Enter" 98.92 487 97.54 97.54 0.00e+00 PDB 4FE8 "Crystal Structure Of Htt36q3h-ex1-x1-c1(alpha)" 98.92 452 98.91 98.91 0.00e+00 PDB 4FEB "Crystal Structure Of Htt36q3h-ex1-x1-c2(beta)" 98.92 452 98.91 98.91 0.00e+00 PDB 4FEC "Crystal Structure Of Htt36q3h" 98.92 452 98.91 98.91 0.00e+00 PDB 4FED "Crystal Structure Of Htt36q3h" 98.92 452 98.91 98.91 0.00e+00 PDB 4GIZ "Crystal Structure Of Full-length Human Papillomavirus Oncoprotein E6 In Complex With Lxxll Peptide Of Ubiquitin Ligase E6ap At " 98.92 382 98.09 98.09 0.00e+00 PDB 4GLI "Crystal Structure Of Human Smn Yg-Dimer" 99.73 401 99.73 99.73 0.00e+00 PDB 4H1G "Structure Of Candida Albicans Kar3 Motor Domain Fused To Maltose- Binding Protein" 98.92 715 98.91 98.91 0.00e+00 PDB 4IFP "X-ray Crystal Structure Of Human Nlrp1 Card Domain" 98.92 466 97.54 97.54 0.00e+00 PDB 4JBZ "Structure Of Mcm10 Coiled-coil Region" 98.92 403 97.54 97.54 0.00e+00 PDB 4JKM "Crystal Structure Of Clostridium Perfringens Beta-glucuronidase" 99.19 400 99.18 99.18 0.00e+00 PDB 4KEG "Crystal Structure Of Mbp Fused Human Splunc1" 98.92 584 99.18 99.18 0.00e+00 PDB 4KHZ "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Pre-translocation Conformation Bound To Malt" 100.00 380 99.73 99.73 0.00e+00 PDB 4KI0 "Crystal Structure Of The Maltose-binding Protein/maltose Transporter Complex In An Outward-facing Conformation Bound To Maltohe" 100.00 380 99.73 99.73 0.00e+00 PDB 4KV3 "Ubiquitin-like Domain Of The Mycobacterium Tuberculosis Type Vii Secretion System Protein Eccd1 As Maltose-binding Protein Fusi" 98.92 461 98.91 98.91 0.00e+00 PDB 4KYC "Structure Of The C-terminal Domain Of The Menangle Virus Phosphoprotein, Fused To Mbp" 98.92 420 98.36 98.36 0.00e+00 PDB 4KYD "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp." 98.92 420 98.36 98.36 0.00e+00 PDB 4KYE "Partial Structure Of The C-terminal Domain Of The Hpiv4b Phosphoprotein, Fused To Mbp" 98.92 420 98.36 98.36 0.00e+00 PDB 4LOG "The Crystal Structure Of The Orphan Nuclear Receptor Pnr Ligand Binding Domain Fused With Mbp" 98.92 574 99.73 99.73 0.00e+00 PDB 4MBP "Maltodextrin Binding Protein With Bound Maltetrose" 100.00 370 99.73 99.73 0.00e+00 PDB 4MY2 "Crystal Structure Of Norrin In Fusion With Maltose Binding Protein" 98.92 477 99.73 99.73 0.00e+00 PDB 4N4X "Crystal Structure Of The Mbp Fused Human Splunc1 (native Form)" 98.92 584 99.18 99.18 0.00e+00 PDB 4NDZ "Structure Of Maltose Binding Protein Fusion To 2-o-sulfotransferase With Bound Heptasaccharide And Pap" 98.92 658 98.91 98.91 0.00e+00 PDB 4NUF "Crystal Structure Of Shp/eid1" 98.92 580 99.73 99.73 0.00e+00 PDB 4O4B "Crystal Structure Of An Inositol Hexakisphosphate Kinase Ehip6ka As A Fusion Protein With Maltose Binding Protein" 98.92 396 99.73 99.73 0.00e+00 PDB 4OGM "Mbp-fusion Protein Of Pila1 Residues 26-159" 99.19 520 97.28 97.28 0.00e+00 PDB 4OZQ "Crystal Structure Of The Mouse Kif14 Motor Domain" 98.92 720 98.91 98.91 0.00e+00 PDB 4PE2 "Mbp Pila1 Cd160" 99.19 516 99.46 99.46 0.00e+00 PDB 4PQK "C-terminal Domain Of Dna Binding Protein" 99.19 487 99.46 99.46 0.00e+00 PDB 4QSZ "Crystal Structure Of Mouse Jmjd7 Fused With Maltose-binding Protein" 98.92 687 99.18 99.18 0.00e+00 PDB 4QVH "Crystal Structure Of The Essential Mycobacterium Tuberculosis Phosphopantetheinyl Transferase Pptt, Solved As A Fusion Protein " 98.92 598 98.36 98.36 0.00e+00 PDB 4R0Y "Structure Of Maltose-binding Protein Fusion With The C-terminal Gh1 Domain Of Guanylate Kinase-associated Protein From Rattus N" 97.57 501 99.72 99.72 0.00e+00 PDB 4RG5 "Crystal Structure Of S. Pombe Smn Yg-dimer" 99.73 401 99.73 99.73 0.00e+00 PDB 4RWF "Crystal Structure Of The Clr:ramp2 Extracellular Domain Heterodimer With Bound Adrenomedullin" 98.92 591 99.73 99.73 0.00e+00 PDB 4RWG "Crystal Structure Of The Clr:ramp1 Extracellular Domain Heterodimer With Bound High Affinity Cgrp Analog" 98.92 593 99.73 99.73 0.00e+00 PDB 4TSM "Mbp-fusion Protein Of Pila1 From C. Difficile R20291 Residues 26-166" 99.19 520 97.28 97.28 0.00e+00 PDB 4WGI "A Single Diastereomer Of A Macrolactam Core Binds Specifically To Myeloid Cell Leukemia 1 (mcl1)" 98.92 518 99.73 99.73 0.00e+00 PDB 4WJV "Crystal Structure Of Rsa4 In Complex With The Nsa2 Binding Peptide" 99.19 381 97.82 97.82 0.00e+00 PDB 4WMS "Structure Of Apo Mbp-mcl1 At 1.9a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMT "Structure Of Mbp-mcl1 Bound To Ligand 1 At 2.35a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMU "Structure Of Mbp-mcl1 Bound To Ligand 2 At 1.55a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMV "Structure Of Mbp-mcl1 Bound To Ligand 4 At 2.4a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMW "The Structure Of Mbp-mcl1 Bound To Ligand 5 At 1.9a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WMX "The Structure Of Mbp-mcl1 Bound To Ligand 6 At 2.0a" 98.92 518 99.73 99.73 0.00e+00 PDB 4WVG "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb)" 97.30 542 99.72 100.00 0.00e+00 PDB 4WVH "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb) In Complex With A Substrate Peptide (pep1)." 97.30 533 98.89 99.17 0.00e+00 PDB 4WVI "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb) In Complex With A Substrate Peptide (pep2)." 97.30 533 98.89 99.17 0.00e+00 PDB 4WVJ "Crystal Structure Of The Type-i Signal Peptidase From Staphylococcus Aureus (spsb) In Complex With An Inhibitor Peptide (pep3)" 97.30 533 98.89 99.17 0.00e+00 PDB 4XAI "Crystal Structure Of Red Flour Beetle Nr2e1/tlx" 98.92 573 99.73 99.73 0.00e+00 PDB 4XAJ "Crystal Structure Of Human Nr2e1/tlx" 98.92 576 99.73 99.73 0.00e+00 PDB 5C7R "Revealing Surface Waters On An Antifreeze Protein By Fusion Protein Crystallography" 98.92 444 98.91 98.91 0.00e+00 PDB 5CL1 "Complex Structure Of Norrin With Human Frizzled 4" 98.92 483 99.73 99.73 0.00e+00 PDB 5DFM "Structure Of Tetrahymena Telomerase P19 Fused To Mbp" 98.92 534 98.91 98.91 0.00e+00 PDB 5DIS "Crystal Structure Of A Crm1-rangtp-spn1 Export Complex Bound To A 113 Amino Acid Fg-repeat Containing Fragment Of Nup214" 97.84 479 99.17 99.17 0.00e+00 DBJ BAB38440 "periplasmic maltose-binding protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAE78036 "maltose transporter subunit [Escherichia coli str. K12 substr. W3110]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAG79849 "maltose ABC transporter substrate binding component [Escherichia coli SE11]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAI28296 "periplasmic maltose-binding protein MalE [Escherichia coli O26:H11 str. 11368]" 100.00 396 99.73 99.73 0.00e+00 DBJ BAI33473 "periplasmic maltose-binding protein MalE [Escherichia coli O103:H2 str. 12009]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAP78494 "Maltose-binding periplasmic protein [Escherichia coli LF82]" 100.00 396 98.65 99.46 0.00e+00 EMBL CAQ34383 "malE, subunit of maltose ABC transporter [Escherichia coli BL21(DE3)]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAR01012 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli IAI1]" 100.00 396 99.73 99.73 0.00e+00 EMBL CAR05669 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli S88]" 100.00 396 98.65 99.46 0.00e+00 EMBL CAR10711 "maltose transporter subunit ; periplasmic-binding component of ABC superfamily [Escherichia coli ED1a]" 100.00 396 98.65 99.46 0.00e+00 GB AAB59056 "periplasmic maltose-binding protein [Escherichia coli]" 100.00 396 99.73 99.73 0.00e+00 GB AAB86559 "maltose binding protein-lacZ alpha peptide fusion protein precursor [Shuttle vector pMAL-pIII]" 98.92 482 99.73 99.73 0.00e+00 GB AAB87675 "maltose binding protein-lacZ-alpha fusion protein [Expression vector pMal-X]" 98.38 496 100.00 100.00 0.00e+00 GB AAC43128 "periplasmic maltose-binding protein [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 GB AAC77004 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 REF NP_313044 "maltose ABC transporter periplasmic protein [Escherichia coli O157:H7 str. Sakai]" 100.00 396 99.73 99.73 0.00e+00 REF NP_418458 "maltose transporter subunit [Escherichia coli str. K-12 substr. MG1655]" 100.00 396 99.73 99.73 0.00e+00 REF NP_709885 "maltose ABC transporter substrate-binding protein [Shigella flexneri 2a str. 301]" 100.00 396 99.46 99.46 0.00e+00 REF WP_000367925 "hypothetical protein [Escherichia coli]" 50.81 188 99.47 100.00 1.50e-127 REF WP_000695369 "MULTISPECIES: sugar ABC transporter substrate-binding protein [Enterobacteriaceae]" 100.00 396 99.73 99.73 0.00e+00 SP P0AEX9 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 99.73 99.73 0.00e+00 SP P0AEY0 "RecName: Full=Maltose-binding periplasmic protein; AltName: Full=MBP; AltName: Full=MMBP; AltName: Full=Maltodextrin-binding pr" 100.00 396 99.73 99.73 0.00e+00 stop_ save_ ############# # 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 Thu Jul 14 17:08:06 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 Eubacteria . 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_type _Vector_name $MBP 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pmal-c0 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Exchangeable proton sites in MBP were fully protonated by partially unfolding this protein in 2.5M GuHCl at room temperature for 3hr and subsequently refolding in GuHCl-free phosphate buffer containing 2mM beta-cyclodextrin. The protein under study has high level (>95%) deuterium labeling at all aliphatic and aromatic sites except at the following methyl groups which are highly protonated: Ile d1, Val g1/g2 and Leu d1/d2. No attempt has been made here to correct the 2H isotope effects on the 15N and 13C chemical shifts that are reported. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MBP . mM 0.7 0.9 '[U-15N;U-13C; U-2H;1H-95% Ile HD1, 1H-50% LeuHD1/HD2, 1H-85% Val HG1/HG2]' $BCD 2.0 mM . . . 'sodium phosphate buffer' 20 mM . . . EDTA 100 uM . . . Pefabloc 0.1 mg/mL . . . pepstatin 1.0 ug/uL . . . D2O 10 % . . . H2O 90 % . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 3 loop_ _Task 'peak picking, partially automated backbone and sidechain assignments' ; Used in conjunction with some in-house Tcl scripts for sidechain assignments ; stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label $sample_1 save_ save_CT-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name CT-HNCA _Sample_label $sample_1 save_ save_CT-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name CT-HN(CO)CA _Sample_label $sample_1 save_ save_CT-HN(CA)CB_4 _Saveframe_category NMR_applied_experiment _Experiment_name CT-HN(CA)CB _Sample_label $sample_1 save_ save_CT-HN(COCA)CB_5 _Saveframe_category NMR_applied_experiment _Experiment_name CT-HN(COCA)CB _Sample_label $sample_1 save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_CT-1H-13C_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name 'CT-1H-13C HSQC' _Sample_label $sample_1 save_ save_(H)C(CO)NH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH-TOCSY _Sample_label $sample_1 save_ save_H(CCO)NH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH-TOCSY _Sample_label $sample_1 save_ save_(H)C(CA)NH-TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CA)NH-TOCSY _Sample_label $sample_1 save_ save_(HM)CMC(CM)HM_11 _Saveframe_category NMR_applied_experiment _Experiment_name (HM)CMC(CM)HM _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.2 0.05 n/a temperature 310 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio 'sodium acetate' C 13 'methyl carbon' ppm 25.85 external direct cylindrical external_to_the_sample parallel_to_Bo 1.000 H2O H 1 proton ppm 4.658 internal direct cylindrical internal parallel_to_Bo 1.000 urea N 15 guanidinyl ppm 78.98 external direct cylindrical external_to_the_sample parallel_to_Bo 1.000 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name MBP _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 LYS CA C 55.781 . 1 2 . 1 LYS CB C 32.207 . 1 3 . 1 LYS C C 176.349 . 1 4 . 2 THR N N 116.283 . 1 5 . 2 THR H H 8.201 . 1 6 . 2 THR CA C 61.547 . 1 7 . 2 THR CB C 69.111 . 1 8 . 2 THR C C 174.253 . 1 9 . 3 GLU N N 122.654 . 1 10 . 3 GLU H H 8.519 . 1 11 . 3 GLU CA C 55.644 . 1 12 . 3 GLU CB C 30.300 . 1 13 . 3 GLU C C 175.942 . 1 14 . 4 GLU N N 122.312 . 1 15 . 4 GLU H H 8.476 . 1 16 . 4 GLU CA C 56.196 . 1 17 . 4 GLU CB C 29.513 . 1 18 . 4 GLU C C 176.820 . 1 19 . 5 GLY N N 110.384 . 1 20 . 5 GLY H H 8.574 . 1 21 . 5 GLY CA C 45.216 . 1 22 . 5 GLY C C 172.158 . 1 23 . 6 LYS N N 119.307 . 1 24 . 6 LYS H H 7.707 . 1 25 . 6 LYS CA C 54.459 . 1 26 . 6 LYS CB C 34.440 . 1 27 . 6 LYS C C 173.423 . 1 28 . 7 LEU N N 118.692 . 1 29 . 7 LEU H H 8.385 . 1 30 . 7 LEU CA C 52.843 . 1 31 . 7 LEU CB C 45.566 . 1 32 . 7 LEU CG C 25.849 . 1 33 . 7 LEU CD1 C 25.068 . 1 34 . 7 LEU HD1 H 0.351 . 1 35 . 7 LEU CD2 C 24.299 . 1 36 . 7 LEU HD2 H 0.527 . 1 37 . 7 LEU C C 175.168 . 1 38 . 8 VAL N N 125.539 . 1 39 . 8 VAL H H 10.009 . 1 40 . 8 VAL CA C 61.285 . 1 41 . 8 VAL CB C 33.278 . 1 42 . 8 VAL CG2 C 21.211 . 1 43 . 8 VAL HG2 H 0.923 . 1 44 . 8 VAL CG1 C 20.894 . 1 45 . 8 VAL HG1 H 0.878 . 1 46 . 8 VAL C C 175.761 . 1 47 . 9 ILE N N 128.453 . 1 48 . 9 ILE H H 9.117 . 1 49 . 9 ILE CA C 59.433 . 1 50 . 9 ILE CB C 40.346 . 1 51 . 9 ILE CG1 C 26.592 . 1 52 . 9 ILE CD1 C 14.504 . 1 53 . 9 ILE HD1 H 0.325 . 1 54 . 9 ILE CG2 C 18.126 . 1 55 . 9 ILE HG2 H 0.985 . 1 56 . 9 ILE C C 174.570 . 1 57 . 10 TRP N N 126.764 . 1 58 . 10 TRP H H 9.036 . 1 59 . 10 TRP CA C 53.678 . 1 60 . 10 TRP CB C 32.163 . 1 61 . 10 TRP HE1 H 10.627 . 1 62 . 10 TRP C C 173.976 . 1 63 . 11 ILE N N 121.988 . 1 64 . 11 ILE H H 8.701 . 1 65 . 11 ILE CA C 59.348 . 1 66 . 11 ILE CB C 40.705 . 1 67 . 11 ILE CG1 C 27.744 . 1 68 . 11 ILE CD1 C 13.151 . 1 69 . 11 ILE HD1 H 0.108 . 1 70 . 11 ILE CG2 C 14.232 . 1 71 . 11 ILE HG2 H 0.634 . 1 72 . 11 ILE C C 171.008 . 1 73 . 12 ASN N N 122.594 . 1 74 . 12 ASN H H 8.854 . 1 75 . 12 ASN CA C 53.871 . 1 76 . 12 ASN CB C 39.211 . 1 77 . 12 ASN C C 177.256 . 1 78 . 13 GLY N N 106.526 . 1 79 . 13 GLY H H 8.224 . 1 80 . 13 GLY CA C 45.882 . 1 81 . 13 GLY C C 173.099 . 1 82 . 14 ASP N N 116.761 . 1 83 . 14 ASP H H 7.923 . 1 84 . 14 ASP CA C 52.575 . 1 85 . 14 ASP CB C 39.142 . 1 86 . 14 ASP C C 176.028 . 1 87 . 15 LYS N N 118.647 . 1 88 . 15 LYS H H 7.558 . 1 89 . 15 LYS CA C 52.499 . 1 90 . 15 LYS CB C 32.319 . 1 91 . 15 LYS C C 177.355 . 1 92 . 16 GLY N N 107.960 . 1 93 . 16 GLY H H 8.732 . 1 94 . 16 GLY CA C 47.565 . 1 95 . 16 GLY C C 175.557 . 1 96 . 17 TYR N N 120.510 . 1 97 . 17 TYR H H 8.203 . 1 98 . 17 TYR CA C 59.207 . 1 99 . 17 TYR CB C 37.030 . 1 100 . 17 TYR C C 177.021 . 1 101 . 18 ASN N N 123.445 . 1 102 . 18 ASN H H 8.095 . 1 103 . 18 ASN CA C 55.679 . 1 104 . 18 ASN CB C 36.875 . 1 105 . 18 ASN C C 178.888 . 1 106 . 19 GLY N N 111.600 . 1 107 . 19 GLY H H 8.929 . 1 108 . 19 GLY CA C 46.935 . 1 109 . 19 GLY C C 175.825 . 1 110 . 20 LEU N N 121.780 . 1 111 . 20 LEU H H 8.302 . 1 112 . 20 LEU CA C 57.088 . 1 113 . 20 LEU CB C 40.697 . 1 114 . 20 LEU CG C 26.321 . 1 115 . 20 LEU CD1 C 24.784 . 1 116 . 20 LEU HD1 H 0.867 . 1 117 . 20 LEU CD2 C 26.813 . 1 118 . 20 LEU HD2 H 0.638 . 1 119 . 20 LEU C C 178.611 . 1 120 . 21 ALA N N 121.081 . 1 121 . 21 ALA H H 8.074 . 1 122 . 21 ALA CA C 54.592 . 1 123 . 21 ALA CB C 16.804 . 1 124 . 21 ALA C C 180.494 . 1 125 . 22 GLU N N 120.436 . 1 126 . 22 GLU H H 7.792 . 1 127 . 22 GLU CA C 59.192 . 1 128 . 22 GLU CB C 27.950 . 1 129 . 22 GLU C C 180.027 . 1 130 . 23 VAL N N 123.021 . 1 131 . 23 VAL H H 7.811 . 1 132 . 23 VAL CA C 66.262 . 1 133 . 23 VAL CB C 30.960 . 1 134 . 23 VAL CG2 C 23.491 . 1 135 . 23 VAL HG2 H 1.257 . 1 136 . 23 VAL CG1 C 22.314 . 1 137 . 23 VAL HG1 H 0.823 . 1 138 . 23 VAL C C 179.336 . 1 139 . 24 GLY N N 106.724 . 1 140 . 24 GLY H H 8.696 . 1 141 . 24 GLY CA C 47.106 . 1 142 . 24 GLY C C 175.022 . 1 143 . 25 LYS N N 122.711 . 1 144 . 25 LYS H H 8.278 . 1 145 . 25 LYS CA C 58.751 . 1 146 . 25 LYS CB C 31.126 . 1 147 . 25 LYS C C 179.381 . 1 148 . 26 LYS N N 122.725 . 1 149 . 26 LYS H H 7.638 . 1 150 . 26 LYS CA C 59.158 . 1 151 . 26 LYS CB C 31.306 . 1 152 . 26 LYS C C 178.018 . 1 153 . 27 PHE N N 120.100 . 1 154 . 27 PHE H H 8.061 . 1 155 . 27 PHE CA C 60.874 . 1 156 . 27 PHE CB C 38.593 . 1 157 . 27 PHE C C 178.856 . 1 158 . 28 GLU N N 124.145 . 1 159 . 28 GLU H H 8.892 . 1 160 . 28 GLU CA C 58.562 . 1 161 . 28 GLU CB C 29.134 . 1 162 . 28 GLU C C 179.749 . 1 163 . 29 LYS N N 121.899 . 1 164 . 29 LYS H H 8.081 . 1 165 . 29 LYS CA C 58.758 . 1 166 . 29 LYS CB C 30.678 . 1 167 . 29 LYS C C 178.224 . 1 168 . 30 ASP N N 116.368 . 1 169 . 30 ASP H H 7.559 . 1 170 . 30 ASP CA C 55.965 . 1 171 . 30 ASP CB C 40.362 . 1 172 . 30 ASP C C 178.159 . 1 173 . 31 THR N N 107.204 . 1 174 . 31 THR H H 7.908 . 1 175 . 31 THR CA C 62.217 . 1 176 . 31 THR CB C 71.633 . 1 177 . 31 THR C C 176.098 . 1 178 . 32 GLY N N 112.688 . 1 179 . 32 GLY H H 8.587 . 1 180 . 32 GLY CA C 44.874 . 1 181 . 32 GLY C C 173.355 . 1 182 . 33 ILE N N 124.219 . 1 183 . 33 ILE H H 7.739 . 1 184 . 33 ILE CA C 58.247 . 1 185 . 33 ILE CB C 35.129 . 1 186 . 33 ILE CG1 C 25.054 . 1 187 . 33 ILE CD1 C 10.246 . 1 188 . 33 ILE HD1 H 0.576 . 1 189 . 33 ILE CG2 C 16.031 . 1 190 . 33 ILE HG2 H 0.626 . 1 191 . 33 ILE C C 173.616 . 1 192 . 34 LYS N N 124.598 . 1 193 . 34 LYS H H 7.701 . 1 194 . 34 LYS CA C 55.997 . 1 195 . 34 LYS CB C 32.144 . 1 196 . 34 LYS C C 175.524 . 1 197 . 35 VAL N N 124.774 . 1 198 . 35 VAL H H 8.461 . 1 199 . 35 VAL CA C 60.571 . 1 200 . 35 VAL CB C 32.665 . 1 201 . 35 VAL CG2 C 22.478 . 1 202 . 35 VAL HG2 H 0.776 . 1 203 . 35 VAL CG1 C 20.783 . 1 204 . 35 VAL HG1 H 0.364 . 1 205 . 35 VAL C C 175.614 . 1 206 . 36 THR N N 125.131 . 1 207 . 36 THR H H 9.115 . 1 208 . 36 THR CA C 60.887 . 1 209 . 36 THR CB C 70.364 . 1 210 . 36 THR C C 172.497 . 1 211 . 37 VAL N N 127.364 . 1 212 . 37 VAL H H 8.859 . 1 213 . 37 VAL CA C 60.977 . 1 214 . 37 VAL CB C 31.983 . 1 215 . 37 VAL CG2 C 20.673 . 1 216 . 37 VAL HG2 H 0.766 . 1 217 . 37 VAL CG1 C 22.850 . 1 218 . 37 VAL HG1 H 0.955 . 1 219 . 37 VAL C C 175.166 . 1 220 . 38 GLU N N 126.959 . 1 221 . 38 GLU H H 9.613 . 1 222 . 38 GLU CA C 53.736 . 1 223 . 38 GLU CB C 32.497 . 1 224 . 38 GLU C C 173.335 . 1 225 . 39 HIS N N 115.269 . 1 226 . 39 HIS H H 8.300 . 1 227 . 39 HIS CA C 50.797 . 1 228 . 39 HIS CB C 27.988 . 1 229 . 40 PRO CA C 61.733 . 1 230 . 40 PRO CB C 30.094 . 1 231 . 40 PRO C C 176.579 . 1 232 . 41 ASP N N 121.155 . 1 233 . 41 ASP H H 8.203 . 1 234 . 41 ASP CA C 54.296 . 1 235 . 41 ASP CB C 40.447 . 1 236 . 41 ASP C C 176.300 . 1 237 . 42 LYS N N 119.315 . 1 238 . 42 LYS H H 8.752 . 1 239 . 42 LYS CA C 55.951 . 1 240 . 42 LYS CB C 28.784 . 1 241 . 42 LYS C C 178.275 . 1 242 . 43 LEU N N 120.008 . 1 243 . 43 LEU H H 7.413 . 1 244 . 43 LEU CA C 58.961 . 1 245 . 43 LEU CB C 40.176 . 1 246 . 43 LEU CG C 25.804 . 1 247 . 43 LEU CD1 C 26.612 . 1 248 . 43 LEU HD1 H 1.103 . 1 249 . 43 LEU CD2 C 26.519 . 1 250 . 43 LEU HD2 H 1.121 . 1 251 . 43 LEU C C 175.788 . 1 252 . 44 GLU N N 123.796 . 1 253 . 44 GLU H H 10.393 . 1 254 . 44 GLU CA C 56.540 . 1 255 . 44 GLU CB C 24.113 . 1 256 . 44 GLU C C 178.380 . 1 257 . 45 GLU N N 120.662 . 1 258 . 45 GLU H H 7.330 . 1 259 . 45 GLU CA C 56.025 . 1 260 . 45 GLU CB C 29.386 . 1 261 . 45 GLU C C 178.098 . 1 262 . 46 LYS N N 120.213 . 1 263 . 46 LYS H H 8.205 . 1 264 . 46 LYS CA C 57.911 . 1 265 . 46 LYS CB C 32.707 . 1 266 . 46 LYS C C 178.939 . 1 267 . 47 PHE N N 117.144 . 1 268 . 47 PHE H H 8.569 . 1 269 . 47 PHE CA C 62.863 . 1 270 . 47 PHE CB C 35.526 . 1 271 . 48 PRO CA C 64.946 . 1 272 . 48 PRO CB C 29.502 . 1 273 . 48 PRO C C 177.674 . 1 274 . 49 GLN N N 114.643 . 1 275 . 49 GLN H H 6.940 . 1 276 . 49 GLN CA C 57.367 . 1 277 . 49 GLN CB C 27.972 . 1 278 . 49 GLN C C 178.192 . 1 279 . 50 VAL N N 110.178 . 1 280 . 50 VAL H H 7.569 . 1 281 . 50 VAL CA C 61.300 . 1 282 . 50 VAL CB C 31.993 . 1 283 . 50 VAL CG2 C 19.728 . 1 284 . 50 VAL HG2 H 0.864 . 1 285 . 50 VAL CG1 C 21.123 . 1 286 . 50 VAL HG1 H 0.965 . 1 287 . 50 VAL C C 177.960 . 1 288 . 51 ALA N N 124.923 . 1 289 . 51 ALA H H 8.075 . 1 290 . 51 ALA CA C 54.455 . 1 291 . 51 ALA CB C 17.164 . 1 292 . 51 ALA C C 179.715 . 1 293 . 52 ALA N N 117.577 . 1 294 . 52 ALA H H 7.706 . 1 295 . 52 ALA CA C 52.606 . 1 296 . 52 ALA CB C 17.579 . 1 297 . 52 ALA C C 178.322 . 1 298 . 53 THR N N 106.339 . 1 299 . 53 THR H H 7.251 . 1 300 . 53 THR CA C 61.034 . 1 301 . 53 THR CB C 69.445 . 1 302 . 53 THR C C 175.144 . 1 303 . 54 GLY N N 109.026 . 1 304 . 54 GLY H H 7.843 . 1 305 . 54 GLY CA C 45.018 . 1 306 . 54 GLY C C 173.399 . 1 307 . 55 ASP N N 119.254 . 1 308 . 55 ASP H H 7.555 . 1 309 . 55 ASP CA C 52.935 . 1 310 . 55 ASP CB C 41.653 . 1 311 . 55 ASP C C 175.079 . 1 312 . 56 GLY N N 106.420 . 1 313 . 56 GLY H H 8.149 . 1 314 . 56 GLY CA C 43.513 . 1 315 . 57 PRO CA C 61.262 . 1 316 . 57 PRO CB C 30.034 . 1 317 . 57 PRO C C 174.831 . 1 318 . 58 ASP N N 117.912 . 1 319 . 58 ASP H H 8.711 . 1 320 . 58 ASP CA C 57.692 . 1 321 . 58 ASP CB C 43.120 . 1 322 . 58 ASP C C 175.436 . 1 323 . 59 ILE N N 114.482 . 1 324 . 59 ILE H H 7.621 . 1 325 . 59 ILE CA C 58.400 . 1 326 . 59 ILE CB C 42.004 . 1 327 . 59 ILE CG1 C 26.606 . 1 328 . 59 ILE CD1 C 13.813 . 1 329 . 59 ILE HD1 H 0.739 . 1 330 . 59 ILE CG2 C 18.249 . 1 331 . 59 ILE HG2 H 0.814 . 1 332 . 59 ILE C C 173.541 . 1 333 . 60 ILE N N 124.328 . 1 334 . 60 ILE H H 8.880 . 1 335 . 60 ILE CA C 57.440 . 1 336 . 60 ILE CB C 40.758 . 1 337 . 60 ILE CG1 C 28.121 . 1 338 . 60 ILE CD1 C 14.627 . 1 339 . 60 ILE HD1 H 0.408 . 1 340 . 60 ILE CG2 C 13.331 . 1 341 . 60 ILE HG2 H 0.039 . 1 342 . 60 ILE C C 172.723 . 1 343 . 61 PHE N N 126.039 . 1 344 . 61 PHE H H 8.630 . 1 345 . 61 PHE CA C 55.204 . 1 346 . 61 PHE CB C 41.457 . 1 347 . 61 PHE C C 176.471 . 1 348 . 62 TRP N N 121.296 . 1 349 . 62 TRP H H 9.168 . 1 350 . 62 TRP CA C 56.787 . 1 351 . 62 TRP CB C 31.095 . 1 352 . 62 TRP C C 173.445 . 1 353 . 63 ALA N N 126.171 . 1 354 . 63 ALA H H 6.387 . 1 355 . 63 ALA CA C 53.303 . 1 356 . 63 ALA CB C 18.125 . 1 357 . 63 ALA C C 179.532 . 1 358 . 64 HIS N N 116.192 . 1 359 . 64 HIS H H 8.096 . 1 360 . 64 HIS CA C 59.703 . 1 361 . 64 HIS CB C 29.572 . 1 362 . 64 HIS C C 178.183 . 1 363 . 65 ASP N N 119.241 . 1 364 . 65 ASP H H 7.714 . 1 365 . 65 ASP CA C 56.083 . 1 366 . 65 ASP CB C 38.476 . 1 367 . 65 ASP C C 177.565 . 1 368 . 66 ARG N N 117.088 . 1 369 . 66 ARG H H 7.008 . 1 370 . 66 ARG CA C 54.304 . 1 371 . 66 ARG CB C 29.246 . 1 372 . 66 ARG C C 177.276 . 1 373 . 67 PHE N N 116.544 . 1 374 . 67 PHE H H 7.641 . 1 375 . 67 PHE CA C 57.587 . 1 376 . 67 PHE CB C 35.922 . 1 377 . 67 PHE C C 177.753 . 1 378 . 68 GLY N N 107.416 . 1 379 . 68 GLY H H 7.341 . 1 380 . 68 GLY CA C 47.030 . 1 381 . 68 GLY C C 175.629 . 1 382 . 69 GLY N N 107.604 . 1 383 . 69 GLY H H 7.737 . 1 384 . 69 GLY CA C 46.357 . 1 385 . 69 GLY C C 177.088 . 1 386 . 70 TYR N N 119.064 . 1 387 . 70 TYR H H 6.885 . 1 388 . 70 TYR CA C 56.502 . 1 389 . 70 TYR CB C 35.179 . 1 390 . 70 TYR C C 178.026 . 1 391 . 71 ALA N N 122.768 . 1 392 . 71 ALA H H 8.586 . 1 393 . 71 ALA CA C 53.750 . 1 394 . 71 ALA CB C 17.309 . 1 395 . 71 ALA C C 181.898 . 1 396 . 72 GLN N N 122.515 . 1 397 . 72 GLN H H 8.623 . 1 398 . 72 GLN CA C 57.994 . 1 399 . 72 GLN CB C 27.015 . 1 400 . 72 GLN C C 177.560 . 1 401 . 73 SER N N 112.020 . 1 402 . 73 SER H H 7.318 . 1 403 . 73 SER CA C 58.529 . 1 404 . 73 SER CB C 63.458 . 1 405 . 73 SER C C 173.533 . 1 406 . 74 GLY N N 109.327 . 1 407 . 74 GLY H H 8.036 . 1 408 . 74 GLY CA C 45.807 . 1 409 . 74 GLY C C 175.952 . 1 410 . 75 LEU N N 113.771 . 1 411 . 75 LEU H H 7.829 . 1 412 . 75 LEU CA C 55.052 . 1 413 . 75 LEU CB C 41.971 . 1 414 . 75 LEU CG C 25.584 . 1 415 . 75 LEU CD1 C 25.725 . 1 416 . 75 LEU HD1 H 0.638 . 1 417 . 75 LEU CD2 C 20.693 . 1 418 . 75 LEU HD2 H 0.516 . 1 419 . 75 LEU C C 177.483 . 1 420 . 76 LEU N N 116.035 . 1 421 . 76 LEU H H 7.426 . 1 422 . 76 LEU CA C 52.035 . 1 423 . 76 LEU CB C 42.899 . 1 424 . 76 LEU CG C 26.525 . 1 425 . 76 LEU CD1 C 27.203 . 1 426 . 76 LEU HD1 H 0.862 . 1 427 . 76 LEU CD2 C 21.772 . 1 428 . 76 LEU HD2 H 0.516 . 1 429 . 76 LEU C C 176.491 . 1 430 . 77 ALA N N 125.983 . 1 431 . 77 ALA H H 9.024 . 1 432 . 77 ALA CA C 50.450 . 1 433 . 77 ALA CB C 18.310 . 1 434 . 77 ALA C C 176.223 . 1 435 . 78 GLU N N 120.908 . 1 436 . 78 GLU H H 8.186 . 1 437 . 78 GLU CA C 55.759 . 1 438 . 78 GLU CB C 28.773 . 1 439 . 78 GLU C C 176.549 . 1 440 . 79 ILE N N 122.771 . 1 441 . 79 ILE H H 8.174 . 1 442 . 79 ILE CA C 59.095 . 1 443 . 79 ILE CB C 38.448 . 1 444 . 79 ILE CG1 C 25.497 . 1 445 . 79 ILE CD1 C 12.326 . 1 446 . 79 ILE HD1 H 0.171 . 1 447 . 79 ILE CG2 C 17.578 . 1 448 . 79 ILE HG2 H 0.647 . 1 449 . 79 ILE C C 175.459 . 1 450 . 80 THR N N 112.714 . 1 451 . 80 THR H H 8.734 . 1 452 . 80 THR CA C 57.256 . 1 453 . 80 THR CB C 68.682 . 1 454 . 81 PRO CA C 61.791 . 1 455 . 81 PRO CB C 31.035 . 1 456 . 81 PRO C C 177.322 . 1 457 . 82 ASP N N 123.615 . 1 458 . 82 ASP H H 9.062 . 1 459 . 82 ASP CA C 52.964 . 1 460 . 82 ASP CB C 40.944 . 1 461 . 83 LYS CA C 59.220 . 1 462 . 83 LYS CB C 31.081 . 1 463 . 83 LYS C C 177.472 . 1 464 . 84 ALA N N 119.410 . 1 465 . 84 ALA H H 8.193 . 1 466 . 84 ALA CA C 54.221 . 1 467 . 84 ALA CB C 16.902 . 1 468 . 84 ALA C C 180.128 . 1 469 . 85 PHE N N 118.531 . 1 470 . 85 PHE H H 7.917 . 1 471 . 85 PHE CA C 61.722 . 1 472 . 85 PHE CB C 38.483 . 1 473 . 85 PHE C C 178.096 . 1 474 . 86 GLN N N 117.150 . 1 475 . 86 GLN H H 8.491 . 1 476 . 86 GLN CA C 59.123 . 1 477 . 86 GLN CB C 27.655 . 1 478 . 86 GLN C C 179.849 . 1 479 . 87 ASP N N 116.882 . 1 480 . 87 ASP H H 8.064 . 1 481 . 87 ASP CA C 55.523 . 1 482 . 87 ASP CB C 40.292 . 1 483 . 87 ASP C C 176.306 . 1 484 . 88 LYS N N 117.171 . 1 485 . 88 LYS H H 7.791 . 1 486 . 88 LYS CA C 57.580 . 1 487 . 88 LYS CB C 31.333 . 1 488 . 88 LYS C C 176.580 . 1 489 . 89 LEU N N 120.029 . 1 490 . 89 LEU H H 7.650 . 1 491 . 89 LEU CA C 52.912 . 1 492 . 89 LEU CB C 41.978 . 1 493 . 89 LEU CG C 28.095 . 1 494 . 89 LEU CD1 C 26.107 . 1 495 . 89 LEU C C 176.257 . 1 496 . 89 LEU HD1 H 0.546 . 1 497 . 89 LEU CD2 C 25.230 . 1 498 . 89 LEU HD2 H 0.501 . 1 499 . 90 TYR N N 117.006 . 1 500 . 90 TYR H H 7.717 . 1 501 . 90 TYR CA C 58.474 . 1 502 . 90 TYR CB C 38.388 . 1 503 . 91 PRO CA C 66.217 . 1 504 . 91 PRO CB C 30.833 . 1 505 . 91 PRO C C 179.350 . 1 506 . 92 PHE N N 112.695 . 1 507 . 92 PHE H H 8.008 . 1 508 . 92 PHE CA C 58.702 . 1 509 . 92 PHE CB C 36.115 . 1 510 . 92 PHE C C 176.165 . 1 511 . 93 THR N N 111.043 . 1 512 . 93 THR H H 7.103 . 1 513 . 93 THR CA C 64.143 . 1 514 . 93 THR CB C 66.513 . 1 515 . 93 THR C C 176.221 . 1 516 . 94 TRP N N 119.822 . 1 517 . 94 TRP H H 6.663 . 1 518 . 94 TRP CA C 57.955 . 1 519 . 94 TRP CB C 28.794 . 1 520 . 94 TRP C C 178.105 . 1 521 . 95 ASP N N 115.514 . 1 522 . 95 ASP H H 7.254 . 1 523 . 95 ASP CA C 56.665 . 1 524 . 95 ASP CB C 39.326 . 1 525 . 95 ASP C C 178.216 . 1 526 . 96 ALA N N 118.598 . 1 527 . 96 ALA H H 6.996 . 1 528 . 96 ALA CA C 53.097 . 1 529 . 96 ALA CB C 17.171 . 1 530 . 96 ALA C C 176.659 . 1 531 . 97 VAL N N 106.048 . 1 532 . 97 VAL H H 6.974 . 1 533 . 97 VAL CA C 59.141 . 1 534 . 97 VAL CB C 30.273 . 1 535 . 97 VAL CG2 C 19.482 . 1 536 . 97 VAL HG2 H 1.354 . 1 537 . 97 VAL CG1 C 22.207 . 1 538 . 97 VAL HG1 H 0.585 . 1 539 . 97 VAL C C 172.465 . 1 540 . 98 ARG N N 121.274 . 1 541 . 98 ARG H H 7.037 . 1 542 . 98 ARG CA C 54.285 . 1 543 . 98 ARG CB C 30.954 . 1 544 . 98 ARG C C 176.403 . 1 545 . 99 TYR N N 126.760 . 1 546 . 99 TYR H H 9.686 . 1 547 . 99 TYR CA C 57.755 . 1 548 . 99 TYR CB C 41.234 . 1 549 . 100 ASN CA C 53.259 . 1 550 . 100 ASN CB C 36.538 . 1 551 . 100 ASN C C 175.131 . 1 552 . 101 GLY N N 102.20 . 1 553 . 101 GLY H H 8.591 . 1 554 . 101 GLY CA C 44.972 . 1 555 . 101 GLY C C 173.747 . 1 556 . 102 LYS N N 121.183 . 1 557 . 102 LYS H H 7.759 . 1 558 . 102 LYS CA C 54.019 . 1 559 . 102 LYS CB C 34.068 . 1 560 . 102 LYS C C 175.040 . 1 561 . 103 LEU N N 123.364 . 1 562 . 103 LEU H H 8.948 . 1 563 . 103 LEU CA C 54.594 . 1 564 . 103 LEU CB C 41.609 . 1 565 . 103 LEU CG C 25.965 . 1 566 . 103 LEU CD1 C 24.815 . 1 567 . 103 LEU HD1 H 0.523 . 1 568 . 103 LEU CD2 C 24.237 . 1 569 . 103 LEU HD2 H 0.986 . 1 570 . 103 LEU C C 178.266 . 1 571 . 104 ILE N N 112.703 . 1 572 . 104 ILE H H 8.806 . 1 573 . 104 ILE CA C 59.107 . 1 574 . 104 ILE CB C 38.509 . 1 575 . 104 ILE CG1 C 26.677 . 1 576 . 104 ILE CD1 C 14.654 . 1 577 . 104 ILE HD1 H 0.856 . 1 578 . 104 ILE CG2 C 19.636 . 1 579 . 104 ILE HG2 H 0.874 . 1 580 . 104 ILE C C 175.297 . 1 581 . 105 ALA N N 117.214 . 1 582 . 105 ALA H H 7.669 . 1 583 . 105 ALA CA C 51.479 . 1 584 . 105 ALA CB C 21.391 . 1 585 . 105 ALA C C 173.514 . 1 586 . 106 TYR N N 113.725 . 1 587 . 106 TYR H H 8.958 . 1 588 . 106 TYR CA C 55.395 . 1 589 . 106 TYR CB C 39.348 . 1 590 . 107 PRO CA C 61.764 . 1 591 . 107 PRO CB C 32.194 . 1 592 . 107 PRO C C 174.363 . 1 593 . 108 ILE N N 115.410 . 1 594 . 108 ILE H H 8.500 . 1 595 . 108 ILE CA C 60.331 . 1 596 . 108 ILE CB C 37.082 . 1 597 . 108 ILE CG1 C 25.268 . 1 598 . 108 ILE CD1 C 10.048 . 1 599 . 108 ILE HD1 H 0.650 . 1 600 . 108 ILE CG2 C 15.894 . 1 601 . 108 ILE HG2 H 0.839 . 1 602 . 108 ILE C C 176.343 . 1 603 . 109 ALA N N 118.306 . 1 604 . 109 ALA H H 7.872 . 1 605 . 109 ALA CA C 50.078 . 1 606 . 109 ALA CB C 22.605 . 1 607 . 109 ALA C C 174.483 . 1 608 . 110 VAL N N 120.942 . 1 609 . 110 VAL H H 8.759 . 1 610 . 110 VAL CA C 61.361 . 1 611 . 110 VAL CB C 33.859 . 1 612 . 110 VAL CG2 C 20.747 . 1 613 . 110 VAL HG2 H 0.505 . 1 614 . 110 VAL CG1 C 21.169 . 1 615 . 110 VAL HG1 H 0.753 . 1 616 . 110 VAL C C 173.524 . 1 617 . 111 GLU N N 123.492 . 1 618 . 111 GLU H H 9.559 . 1 619 . 111 GLU CA C 54.374 . 1 620 . 111 GLU CB C 32.509 . 1 621 . 111 GLU C C 173.654 . 1 622 . 112 ALA N N 117.454 . 1 623 . 112 ALA H H 6.379 . 1 624 . 112 ALA CA C 50.282 . 1 625 . 112 ALA CB C 21.474 . 1 626 . 112 ALA C C 176.296 . 1 627 . 113 LEU N N 122.970 . 1 628 . 113 LEU H H 8.420 . 1 629 . 113 LEU CA C 54.543 . 1 630 . 113 LEU CB C 42.782 . 1 631 . 113 LEU CG C 25.064 . 1 632 . 113 LEU CD1 C 26.851 . 1 633 . 113 LEU HD1 H 0.715 . 1 634 . 113 LEU CD2 C 23.625 . 1 635 . 113 LEU HD2 H 0.854 . 1 636 . 113 LEU C C 173.342 . 1 637 . 114 SER N N 107.984 . 1 638 . 114 SER H H 7.464 . 1 639 . 114 SER CA C 56.553 . 1 640 . 114 SER CB C 66.689 . 1 641 . 114 SER C C 171.741 . 1 642 . 115 LEU N N 122.091 . 1 643 . 115 LEU H H 7.280 . 1 644 . 115 LEU CA C 53.808 . 1 645 . 115 LEU CB C 43.068 . 1 646 . 115 LEU CG C 26.632 . 1 647 . 115 LEU CD1 C 22.828 . 1 648 . 115 LEU HD1 H 0.684 . 1 649 . 115 LEU CD2 C 24.605 . 1 650 . 115 LEU HD2 H 0.588 . 1 651 . 115 LEU C C 173.979 . 1 652 . 116 ILE N N 129.558 . 1 653 . 116 ILE H H 8.642 . 1 654 . 116 ILE CA C 59.470 . 1 655 . 116 ILE CB C 37.551 . 1 656 . 116 ILE CG1 C 26.378 . 1 657 . 116 ILE CD1 C 13.724 . 1 658 . 116 ILE HD1 H 0.462 . 1 659 . 116 ILE CG2 C 17.310 . 1 660 . 116 ILE HG2 H 0.453 . 1 661 . 116 ILE C C 174.372 . 1 662 . 117 TYR N N 121.731 . 1 663 . 117 TYR H H 9.057 . 1 664 . 117 TYR CA C 54.000 . 1 665 . 117 TYR CB C 41.625 . 1 666 . 117 TYR C C 172.684 . 1 667 . 118 ASN N N 121.140 . 1 668 . 118 ASN H H 9.302 . 1 669 . 118 ASN CA C 51.565 . 1 670 . 118 ASN CB C 37.122 . 1 671 . 118 ASN C C 175.506 . 1 672 . 119 LYS N N 125.460 . 1 673 . 119 LYS H H 8.786 . 1 674 . 119 LYS CA C 58.109 . 1 675 . 119 LYS CB C 31.955 . 1 676 . 119 LYS C C 177.418 . 1 677 . 120 ASP N N 115.604 . 1 678 . 120 ASP H H 8.146 . 1 679 . 120 ASP CA C 55.771 . 1 680 . 120 ASP CB C 39.805 . 1 681 . 120 ASP C C 177.378 . 1 682 . 121 LEU N N 117.771 . 1 683 . 121 LEU H H 7.112 . 1 684 . 121 LEU CA C 54.837 . 1 685 . 121 LEU CB C 43.418 . 1 686 . 121 LEU CG C 26.068 . 1 687 . 121 LEU CD1 C 24.726 . 1 688 . 121 LEU HD1 H 0.667 . 1 689 . 121 LEU CD2 C 22.791 . 1 690 . 121 LEU HD2 H 0.779 . 1 691 . 121 LEU C C 176.467 . 1 692 . 122 LEU N N 119.843 . 1 693 . 122 LEU H H 8.319 . 1 694 . 122 LEU CA C 51.127 . 1 695 . 122 LEU CB C 43.407 . 1 696 . 122 LEU CG C 26.052 . 1 697 . 122 LEU CD1 C 25.616 . 1 698 . 122 LEU HD1 H 0.937 . 1 699 . 122 LEU CD2 C 26.775 . 1 700 . 122 LEU HD2 H 0.945 . 1 701 . 123 PRO CA C 61.791 . 1 702 . 123 PRO CB C 31.035 . 1 703 . 123 PRO C C 177.322 . 1 704 . 124 ASN N N 123.615 . 1 705 . 124 ASN H H 9.062 . 1 706 . 124 ASN CA C 52.964 . 1 707 . 124 ASN CB C 40.944 . 1 708 . 126 PRO CA C 61.774 . 1 709 . 126 PRO CB C 30.573 . 1 710 . 126 PRO C C 175.835 . 1 711 . 127 LYS N N 118.469 . 1 712 . 127 LYS H H 8.117 . 1 713 . 127 LYS CA C 55.965 . 1 714 . 127 LYS CB C 32.562 . 1 715 . 127 LYS C C 177.152 . 1 716 . 128 THR N N 108.676 . 1 717 . 128 THR H H 7.863 . 1 718 . 128 THR CA C 59.464 . 1 719 . 128 THR CB C 71.230 . 1 720 . 128 THR C C 174.337 . 1 721 . 129 TRP N N 123.811 . 1 722 . 129 TRP H H 10.152 . 1 723 . 129 TRP CA C 60.393 . 1 724 . 129 TRP CB C 27.940 . 1 725 . 129 TRP C C 179.650 . 1 726 . 130 GLU N N 117.989 . 1 727 . 130 GLU H H 10.571 . 1 728 . 130 GLU CA C 61.152 . 1 729 . 130 GLU CB C 27.554 . 1 730 . 130 GLU C C 178.368 . 1 731 . 131 GLU N N 116.640 . 1 732 . 131 GLU H H 7.595 . 1 733 . 131 GLU CA C 56.554 . 1 734 . 131 GLU CB C 30.630 . 1 735 . 131 GLU C C 176.729 . 1 736 . 132 ILE N N 121.552 . 1 737 . 132 ILE H H 8.186 . 1 738 . 132 ILE CA C 66.318 . 1 739 . 132 ILE CB C 33.444 . 1 740 . 132 ILE CG1 C 29.579 . 1 741 . 132 ILE CD1 C 12.401 . 1 742 . 132 ILE HD1 H 0.564 . 1 743 . 132 ILE CG2 C 16.112 . 1 744 . 132 ILE HG2 H 0.788 . 1 745 . 133 PRO CA C 66.476 . 1 746 . 133 PRO CB C 29.857 . 1 747 . 133 PRO C C 177.450 . 1 748 . 134 ALA N N 118.070 . 1 749 . 134 ALA H H 7.803 . 1 750 . 134 ALA CA C 54.614 . 1 751 . 134 ALA CB C 17.294 . 1 752 . 134 ALA C C 180.986 . 1 753 . 135 LEU N N 120.009 . 1 754 . 135 LEU H H 7.602 . 1 755 . 135 LEU CA C 56.809 . 1 756 . 135 LEU CB C 41.352 . 1 757 . 135 LEU CG C 26.229 . 1 758 . 135 LEU CD1 C 24.030 . 1 759 . 135 LEU HD1 H 0.890 . 1 760 . 135 LEU CD2 C 24.239 . 1 761 . 135 LEU HD2 H 0.888 . 1 762 . 135 LEU C C 178.996 . 1 763 . 136 ASP N N 118.531 . 1 764 . 136 ASP H H 8.817 . 1 765 . 136 ASP CA C 58.408 . 1 766 . 136 ASP CB C 41.259 . 1 767 . 136 ASP C C 177.122 . 1 768 . 137 LYS N N 117.267 . 1 769 . 137 LYS H H 8.029 . 1 770 . 137 LYS CA C 59.759 . 1 771 . 137 LYS CB C 31.388 . 1 772 . 137 LYS C C 179.577 . 1 773 . 138 GLU N N 118.554 . 1 774 . 138 GLU H H 7.467 . 1 775 . 138 GLU CA C 58.618 . 1 776 . 138 GLU CB C 28.786 . 1 777 . 138 GLU C C 179.496 . 1 778 . 139 LEU N N 121.200 . 1 779 . 139 LEU H H 8.396 . 1 780 . 139 LEU CA C 57.376 . 1 781 . 139 LEU CB C 39.742 . 1 782 . 139 LEU CG C 27.235 . 1 783 . 139 LEU CD1 C 25.914 . 1 784 . 139 LEU HD1 H 0.787 . 1 785 . 139 LEU CD2 C 23.005 . 1 786 . 139 LEU HD2 H 0.854 . 1 787 . 139 LEU C C 180.400 . 1 788 . 140 LYS N N 124.092 . 1 789 . 140 LYS H H 9.247 . 1 790 . 140 LYS CA C 58.284 . 1 791 . 140 LYS CB C 31.263 . 1 792 . 140 LYS C C 181.328 . 1 793 . 141 ALA N N 121.994 . 1 794 . 141 ALA H H 7.255 . 1 795 . 141 ALA CA C 53.808 . 1 796 . 141 ALA CB C 17.169 . 1 797 . 141 ALA C C 178.373 . 1 798 . 142 LYS N N 115.771 . 1 799 . 142 LYS H H 7.636 . 1 800 . 142 LYS CA C 54.423 . 1 801 . 142 LYS CB C 31.734 . 1 802 . 142 LYS C C 176.494 . 1 803 . 143 GLY N N 107.737 . 1 804 . 143 GLY H H 7.870 . 1 805 . 143 GLY CA C 45.520 . 1 806 . 143 GLY C C 174.066 . 1 807 . 144 LYS N N 119.876 . 1 808 . 144 LYS H H 7.849 . 1 809 . 144 LYS CA C 52.740 . 1 810 . 144 LYS CB C 34.517 . 1 811 . 144 LYS C C 173.568 . 1 812 . 145 SER N N 109.461 . 1 813 . 145 SER H H 7.567 . 1 814 . 145 SER CA C 56.047 . 1 815 . 145 SER CB C 65.829 . 1 816 . 145 SER C C 174.422 . 1 817 . 146 ALA N N 122.808 . 1 818 . 146 ALA H H 9.573 . 1 819 . 146 ALA CA C 55.073 . 1 820 . 146 ALA CB C 17.335 . 1 821 . 146 ALA C C 175.662 . 1 822 . 147 LEU N N 116.815 . 1 823 . 147 LEU H H 8.663 . 1 824 . 147 LEU CA C 53.816 . 1 825 . 147 LEU CB C 44.878 . 1 826 . 147 LEU CG C 27.423 . 1 827 . 147 LEU CD1 C 22.490 . 1 828 . 147 LEU HD1 H 0.689 . 1 829 . 147 LEU CD2 C 27.604 . 1 830 . 147 LEU HD2 H 0.943 . 1 831 . 147 LEU C C 174.822 . 1 832 . 148 MET N N 121.573 . 1 833 . 148 MET H H 8.177 . 1 834 . 148 MET CA C 55.222 . 1 835 . 148 MET CB C 37.204 . 1 836 . 148 MET C C 174.047 . 1 837 . 149 PHE N N 120.074 . 1 838 . 149 PHE H H 8.566 . 1 839 . 149 PHE CA C 55.154 . 1 840 . 149 PHE CB C 40.830 . 1 841 . 149 PHE C C 171.328 . 1 842 . 150 ASN N N 115.856 . 1 843 . 150 ASN H H 8.651 . 1 844 . 150 ASN CA C 52.761 . 1 845 . 150 ASN CB C 36.636 . 1 846 . 150 ASN C C 172.351 . 1 847 . 151 LEU N N 123.033 . 1 848 . 151 LEU H H 7.303 . 1 849 . 151 LEU CA C 53.863 . 1 850 . 151 LEU CB C 41.260 . 1 851 . 151 LEU CG C 25.776 . 1 852 . 151 LEU CD1 C 26.242 . 1 853 . 151 LEU HD1 H 0.751 . 1 854 . 151 LEU CD2 C 23.619 . 1 855 . 151 LEU HD2 H 0.148 . 1 856 . 151 LEU C C 177.743 . 1 857 . 152 GLN N N 113.019 . 1 858 . 152 GLN H H 7.930 . 1 859 . 152 GLN CA C 54.999 . 1 860 . 152 GLN CB C 27.792 . 1 861 . 152 GLN C C 175.840 . 1 862 . 153 GLU N N 113.712 . 1 863 . 153 GLU H H 6.448 . 1 864 . 153 GLU CA C 50.806 . 1 865 . 153 GLU CB C 32.456 . 1 866 . 154 PRO CA C 63.042 . 1 867 . 154 PRO CB C 31.457 . 1 868 . 154 PRO C C 176.660 . 1 869 . 155 TYR N N 117.704 . 1 870 . 155 TYR H H 7.929 . 1 871 . 155 TYR CA C 61.912 . 1 872 . 155 TYR CB C 39.543 . 1 873 . 155 TYR C C 175.603 . 1 874 . 156 PHE N N 112.053 . 1 875 . 156 PHE H H 8.048 . 1 876 . 156 PHE CA C 60.029 . 1 877 . 156 PHE CB C 40.947 . 1 878 . 156 PHE C C 175.848 . 1 879 . 157 THR N N 105.904 . 1 880 . 157 THR H H 7.577 . 1 881 . 157 THR CA C 62.351 . 1 882 . 157 THR CB C 68.672 . 1 883 . 157 THR C C 175.754 . 1 884 . 158 TRP N N 124.112 . 1 885 . 158 TRP H H 8.353 . 1 886 . 158 TRP CA C 60.123 . 1 887 . 158 TRP CB C 28.016 . 1 888 . 159 PRO CA C 65.262 . 1 889 . 159 PRO CB C 29.432 . 1 890 . 159 PRO C C 177.847 . 1 891 . 160 LEU N N 111.471 . 1 892 . 160 LEU H H 6.410 . 1 893 . 160 LEU CA C 55.369 . 1 894 . 160 LEU CB C 41.550 . 1 895 . 160 LEU CG C 25.601 . 1 896 . 160 LEU CD1 C 19.560 . 1 897 . 160 LEU HD1 H -1.012 . 1 898 . 160 LEU CD2 C 25.122 . 1 899 . 160 LEU HD2 H -0.286 . 1 900 . 160 LEU C C 176.519 . 1 901 . 161 ILE N N 119.393 . 1 902 . 161 ILE H H 6.953 . 1 903 . 161 ILE CA C 65.031 . 1 904 . 161 ILE CB C 36.779 . 1 905 . 161 ILE CG1 C 27.906 . 1 906 . 161 ILE CD1 C 13.139 . 1 907 . 161 ILE HD1 H 0.761 . 1 908 . 161 ILE CG2 C 16.035 . 1 909 . 161 ILE HG2 H 0.483 . 1 910 . 161 ILE C C 175.369 . 1 911 . 162 ALA N N 115.117 . 1 912 . 162 ALA H H 7.977 . 1 913 . 162 ALA CA C 51.655 . 1 914 . 162 ALA CB C 17.763 . 1 915 . 162 ALA C C 179.353 . 1 916 . 163 ALA N N 120.709 . 1 917 . 163 ALA H H 6.644 . 1 918 . 163 ALA CA C 55.725 . 1 919 . 163 ALA CB C 19.062 . 1 920 . 163 ALA C C 178.006 . 1 921 . 164 ASP N N 114.910 . 1 922 . 164 ASP H H 9.555 . 1 923 . 164 ASP CA C 52.782 . 1 924 . 164 ASP CB C 41.761 . 1 925 . 164 ASP C C 176.376 . 1 926 . 165 GLY N N 103.615 . 1 927 . 165 GLY H H 7.471 . 1 928 . 165 GLY CA C 45.144 . 1 929 . 165 GLY C C 175.438 . 1 930 . 166 GLY N N 108.038 . 1 931 . 166 GLY H H 7.388 . 1 932 . 166 GLY CA C 44.790 . 1 933 . 166 GLY C C 171.916 . 1 934 . 167 TYR N N 115.473 . 1 935 . 167 TYR H H 8.255 . 1 936 . 167 TYR CA C 56.995 . 1 937 . 167 TYR CB C 38.504 . 1 938 . 167 TYR C C 173.146 . 1 939 . 168 ALA N N 124.250 . 1 940 . 168 ALA H H 10.481 . 1 941 . 168 ALA CA C 52.580 . 1 942 . 168 ALA CB C 15.894 . 1 943 . 168 ALA C C 172.878 . 1 944 . 169 PHE N N 107.990 . 1 945 . 169 PHE H H 6.304 . 1 946 . 169 PHE CA C 55.034 . 1 947 . 169 PHE CB C 42.023 . 1 948 . 169 PHE C C 176.457 . 1 949 . 170 LYS N N 125.548 . 1 950 . 170 LYS H H 8.856 . 1 951 . 170 LYS CA C 56.452 . 1 952 . 170 LYS CB C 31.814 . 1 953 . 170 LYS C C 174.459 . 1 954 . 171 TYR N N 129.745 . 1 955 . 171 TYR H H 8.582 . 1 956 . 171 TYR CA C 55.707 . 1 957 . 171 TYR CB C 39.206 . 1 958 . 171 TYR C C 174.640 . 1 959 . 172 GLU N N 126.717 . 1 960 . 172 GLU H H 8.223 . 1 961 . 172 GLU CA C 55.126 . 1 962 . 172 GLU CB C 31.885 . 1 963 . 173 ASN CA C 53.533 . 1 964 . 173 ASN CB C 36.679 . 1 965 . 173 ASN C C 175.178 . 1 966 . 174 GLY N N 101.99 . 1 967 . 174 GLY H H 7.452 . 1 968 . 174 GLY CA C 45.074 . 1 969 . 174 GLY C C 172.980 . 1 970 . 175 LYS N N 118.520 . 1 971 . 175 LYS H H 7.072 . 1 972 . 175 LYS CA C 53.955 . 1 973 . 175 LYS CB C 34.710 . 1 974 . 175 LYS C C 174.471 . 1 975 . 176 TYR N N 119.870 . 1 976 . 176 TYR H H 8.709 . 1 977 . 176 TYR CA C 58.284 . 1 978 . 176 TYR CB C 39.218 . 1 979 . 176 TYR C C 176.014 . 1 980 . 177 ASP N N 123.833 . 1 981 . 177 ASP H H 9.002 . 1 982 . 177 ASP CA C 52.268 . 1 983 . 177 ASP CB C 40.680 . 1 984 . 177 ASP C C 177.224 . 1 985 . 178 ILE N N 116.929 . 1 986 . 178 ILE H H 7.707 . 1 987 . 178 ILE CA C 62.970 . 1 988 . 178 ILE CB C 36.218 . 1 989 . 178 ILE CG1 C 24.927 . 1 990 . 178 ILE CD1 C 13.918 . 1 991 . 178 ILE HD1 H 0.857 . 1 992 . 178 ILE CG2 C 17.533 . 1 993 . 178 ILE HG2 H 0.623 . 1 994 . 178 ILE C C 175.577 . 1 995 . 179 LYS N N 116.056 . 1 996 . 179 LYS H H 8.284 . 1 997 . 179 LYS CA C 54.115 . 1 998 . 179 LYS CB C 31.346 . 1 999 . 179 LYS C C 176.249 . 1 1000 . 180 ASP N N 123.217 . 1 1001 . 180 ASP H H 7.752 . 1 1002 . 180 ASP CA C 52.734 . 1 1003 . 180 ASP CB C 40.333 . 1 1004 . 180 ASP C C 172.793 . 1 1005 . 181 VAL N N 122.789 . 1 1006 . 181 VAL H H 7.463 . 1 1007 . 181 VAL CA C 58.711 . 1 1008 . 181 VAL CB C 34.493 . 1 1009 . 181 VAL CG2 C 22.585 . 1 1010 . 181 VAL HG2 H 0.705 . 1 1011 . 181 VAL CG1 C 21.588 . 1 1012 . 181 VAL HG1 H 0.823 . 1 1013 . 181 VAL C C 176.640 . 1 1014 . 182 GLY N N 120.680 . 1 1015 . 182 GLY H H 7.059 . 1 1016 . 182 GLY CA C 45.818 . 1 1017 . 182 GLY C C 173.951 . 1 1018 . 183 VAL N N 113.962 . 1 1019 . 183 VAL H H 6.697 . 1 1020 . 183 VAL CA C 62.761 . 1 1021 . 183 VAL CB C 32.320 . 1 1022 . 183 VAL CG2 C 22.406 . 1 1023 . 183 VAL HG2 H 0.841 . 1 1024 . 183 VAL CG1 C 22.415 . 1 1025 . 183 VAL HG1 H 0.882 . 1 1026 . 183 VAL C C 173.018 . 1 1027 . 184 ASP N N 114.790 . 1 1028 . 184 ASP H H 7.831 . 1 1029 . 184 ASP CA C 51.011 . 1 1030 . 184 ASP CB C 39.199 . 1 1031 . 184 ASP C C 175.987 . 1 1032 . 185 ASN N N 116.227 . 1 1033 . 185 ASN H H 6.887 . 1 1034 . 185 ASN CA C 51.028 . 1 1035 . 185 ASN CB C 38.770 . 1 1036 . 186 ALA CA C 54.879 . 1 1037 . 186 ALA CB C 17.595 . 1 1038 . 186 ALA C C 180.229 . 1 1039 . 187 GLY N N 109.345 . 1 1040 . 187 GLY H H 8.360 . 1 1041 . 187 GLY CA C 46.708 . 1 1042 . 187 GLY C C 175.758 . 1 1043 . 188 ALA N N 127.624 . 1 1044 . 188 ALA H H 8.053 . 1 1045 . 188 ALA CA C 53.314 . 1 1046 . 188 ALA CB C 17.701 . 1 1047 . 188 ALA C C 180.549 . 1 1048 . 189 LYS N N 115.165 . 1 1049 . 189 LYS H H 7.975 . 1 1050 . 189 LYS CA C 59.048 . 1 1051 . 189 LYS CB C 31.235 . 1 1052 . 189 LYS C C 180.067 . 1 1053 . 190 ALA N N 124.632 . 1 1054 . 190 ALA H H 8.206 . 1 1055 . 190 ALA CA C 55.113 . 1 1056 . 190 ALA CB C 17.233 . 1 1057 . 190 ALA C C 181.048 . 1 1058 . 191 GLY N N 107.507 . 1 1059 . 191 GLY H H 8.210 . 1 1060 . 191 GLY CA C 47.264 . 1 1061 . 191 GLY C C 174.759 . 1 1062 . 192 LEU N N 121.157 . 1 1063 . 192 LEU H H 8.652 . 1 1064 . 192 LEU CA C 56.627 . 1 1065 . 192 LEU CB C 39.531 . 1 1066 . 192 LEU CG C 26.302 . 1 1067 . 192 LEU CD1 C 24.249 . 1 1068 . 192 LEU HD1 H 1.085 . 1 1069 . 192 LEU CD2 C 25.291 . 1 1070 . 192 LEU HD2 H 0.852 . 1 1071 . 192 LEU C C 178.141 . 1 1072 . 193 THR N N 116.385 . 1 1073 . 193 THR H H 8.527 . 1 1074 . 193 THR CA C 67.442 . 1 1075 . 193 THR CB C 68.008 . 1 1076 . 193 THR C C 174.971 . 1 1077 . 194 PHE N N 122.015 . 1 1078 . 194 PHE H H 7.645 . 1 1079 . 194 PHE CA C 61.725 . 1 1080 . 194 PHE CB C 38.544 . 1 1081 . 194 PHE C C 177.200 . 1 1082 . 195 LEU N N 119.501 . 1 1083 . 195 LEU H H 7.714 . 1 1084 . 195 LEU CA C 58.054 . 1 1085 . 195 LEU CB C 40.646 . 1 1086 . 195 LEU CG C 26.490 . 1 1087 . 195 LEU CD1 C 23.701 . 1 1088 . 195 LEU HD1 H 0.900 . 1 1089 . 195 LEU CD2 C 25.220 . 1 1090 . 195 LEU HD2 H 0.852 . 1 1091 . 195 LEU C C 177.877 . 1 1092 . 196 VAL N N 117.482 . 1 1093 . 196 VAL H H 8.583 . 1 1094 . 196 VAL CA C 66.659 . 1 1095 . 196 VAL CB C 30.538 . 1 1096 . 196 VAL CG2 C 23.397 . 1 1097 . 196 VAL HG2 H 0.864 . 1 1098 . 196 VAL CG1 C 21.649 . 1 1099 . 196 VAL C C 178.196 . 1 1100 . 196 VAL HG1 H 0.969 . 1 1101 . 197 ASP N N 122.885 . 1 1102 . 197 ASP H H 8.573 . 1 1103 . 197 ASP CA C 57.404 . 1 1104 . 197 ASP CB C 39.275 . 1 1105 . 197 ASP C C 179.107 . 1 1106 . 198 LEU N N 120.155 . 1 1107 . 198 LEU H H 7.876 . 1 1108 . 198 LEU CA C 57.901 . 1 1109 . 198 LEU CB C 41.444 . 1 1110 . 198 LEU CG C 25.393 . 1 1111 . 198 LEU CD1 C 25.598 . 1 1112 . 198 LEU HD1 H 1.018 . 1 1113 . 198 LEU CD2 C 23.397 . 1 1114 . 198 LEU HD2 H 0.808 . 1 1115 . 198 LEU C C 178.861 . 1 1116 . 199 ILE N N 119.950 . 1 1117 . 199 ILE H H 7.435 . 1 1118 . 199 ILE CA C 62.685 . 1 1119 . 199 ILE CB C 37.657 . 1 1120 . 199 ILE CG1 C 27.965 . 1 1121 . 199 ILE CD1 C 14.231 . 1 1122 . 199 ILE HD1 H 0.749 . 1 1123 . 199 ILE CG2 C 17.037 . 1 1124 . 199 ILE HG2 H 0.990 . 1 1125 . 199 ILE C C 180.835 . 1 1126 . 200 LYS N N 124.444 . 1 1127 . 200 LYS H H 9.382 . 1 1128 . 200 LYS CA C 59.282 . 1 1129 . 200 LYS CB C 31.491 . 1 1130 . 200 LYS C C 178.553 . 1 1131 . 201 ASN N N 113.883 . 1 1132 . 201 ASN H H 7.988 . 1 1133 . 201 ASN CA C 52.987 . 1 1134 . 201 ASN CB C 38.058 . 1 1135 . 201 ASN C C 172.984 . 1 1136 . 202 LYS N N 111.412 . 1 1137 . 202 LYS H H 7.923 . 1 1138 . 202 LYS CA C 56.915 . 1 1139 . 202 LYS CB C 26.699 . 1 1140 . 202 LYS C C 175.542 . 1 1141 . 203 HIS N N 116.197 . 1 1142 . 203 HIS H H 8.346 . 1 1143 . 203 HIS CA C 56.618 . 1 1144 . 203 HIS CB C 27.905 . 1 1145 . 203 HIS C C 175.360 . 1 1146 . 204 MET N N 114.057 . 1 1147 . 204 MET H H 7.463 . 1 1148 . 204 MET CA C 54.026 . 1 1149 . 204 MET CB C 36.766 . 1 1150 . 204 MET C C 172.956 . 1 1151 . 205 ASN N N 118.546 . 1 1152 . 205 ASN H H 8.692 . 1 1153 . 205 ASN CA C 51.541 . 1 1154 . 205 ASN CB C 39.627 . 1 1155 . 205 ASN C C 175.913 . 1 1156 . 206 ALA N N 124.944 . 1 1157 . 206 ALA H H 9.059 . 1 1158 . 206 ALA CA C 54.047 . 1 1159 . 206 ALA CB C 17.643 . 1 1160 . 206 ALA C C 176.127 . 1 1161 . 207 ASP N N 112.763 . 1 1162 . 207 ASP H H 8.160 . 1 1163 . 207 ASP CA C 53.113 . 1 1164 . 207 ASP CB C 39.282 . 1 1165 . 207 ASP C C 176.257 . 1 1166 . 208 THR N N 116.465 . 1 1167 . 208 THR H H 7.320 . 1 1168 . 208 THR CA C 66.101 . 1 1169 . 208 THR CB C 68.438 . 1 1170 . 208 THR C C 173.033 . 1 1171 . 209 ASP N N 130.733 . 1 1172 . 209 ASP H H 6.978 . 1 1173 . 209 ASP CA C 51.244 . 1 1174 . 209 ASP CB C 41.486 . 1 1175 . 209 ASP C C 175.589 . 1 1176 . 210 TYR N N 117.355 . 1 1177 . 210 TYR H H 7.843 . 1 1178 . 210 TYR CA C 62.747 . 1 1179 . 210 TYR CB C 38.456 . 1 1180 . 210 TYR C C 178.154 . 1 1181 . 211 SER N N 114.625 . 1 1182 . 211 SER H H 8.191 . 1 1183 . 211 SER CA C 61.243 . 1 1184 . 211 SER CB C 62.203 . 1 1185 . 211 SER C C 177.301 . 1 1186 . 212 ILE N N 124.420 . 1 1187 . 212 ILE H H 8.967 . 1 1188 . 212 ILE CA C 64.324 . 1 1189 . 212 ILE CB C 37.982 . 1 1190 . 212 ILE CG1 C 28.097 . 1 1191 . 212 ILE CD1 C 13.100 . 1 1192 . 212 ILE HD1 H 0.872 . 1 1193 . 212 ILE CG2 C 16.848 . 1 1194 . 212 ILE HG2 H 0.946 . 1 1195 . 212 ILE C C 178.686 . 1 1196 . 213 ALA N N 120.631 . 1 1197 . 213 ALA H H 7.607 . 1 1198 . 213 ALA CA C 54.792 . 1 1199 . 213 ALA CB C 16.432 . 1 1200 . 213 ALA C C 177.626 . 1 1201 . 214 GLU N N 117.327 . 1 1202 . 214 GLU H H 7.860 . 1 1203 . 214 GLU CA C 58.351 . 1 1204 . 214 GLU CB C 29.259 . 1 1205 . 215 ALA N N 119.669 . 1 1206 . 215 ALA H H 7.782 . 1 1207 . 215 ALA CA C 54.125 . 1 1208 . 215 ALA CB C 17.201 . 1 1209 . 216 ALA N N 117.587 . 1 1210 . 216 ALA H H 7.806 . 1 1211 . 216 ALA CA C 54.388 . 1 1212 . 216 ALA CB C 19.131 . 1 1213 . 216 ALA C C 180.429 . 1 1214 . 217 PHE N N 119.381 . 1 1215 . 217 PHE H H 8.321 . 1 1216 . 217 PHE CA C 62.241 . 1 1217 . 217 PHE CB C 37.490 . 1 1218 . 218 ASN CA C 54.914 . 1 1219 . 218 ASN C C 176.515 . 1 1220 . 219 LYS N N 116.691 . 1 1221 . 219 LYS H H 7.706 . 1 1222 . 219 LYS CA C 55.486 . 1 1223 . 219 LYS CB C 32.218 . 1 1224 . 219 LYS C C 177.490 . 1 1225 . 220 GLY N N 108.654 . 1 1226 . 220 GLY H H 7.709 . 1 1227 . 220 GLY CA C 45.514 . 1 1228 . 220 GLY C C 174.916 . 1 1229 . 221 GLU N N 116.370 . 1 1230 . 221 GLU H H 8.353 . 1 1231 . 221 GLU CA C 56.794 . 1 1232 . 221 GLU CB C 29.818 . 1 1233 . 221 GLU C C 175.557 . 1 1234 . 222 THR N N 110.491 . 1 1235 . 222 THR H H 6.845 . 1 1236 . 222 THR CA C 57.437 . 1 1237 . 222 THR CB C 69.896 . 1 1238 . 222 THR C C 172.510 . 1 1239 . 223 ALA N N 127.267 . 1 1240 . 223 ALA H H 8.667 . 1 1241 . 223 ALA CA C 54.024 . 1 1242 . 223 ALA CB C 19.777 . 1 1243 . 223 ALA C C 176.214 . 1 1244 . 224 MET N N 114.242 . 1 1245 . 224 MET H H 8.065 . 1 1246 . 224 MET CA C 53.996 . 1 1247 . 224 MET CB C 39.522 . 1 1248 . 224 MET C C 173.714 . 1 1249 . 225 THR N N 113.254 . 1 1250 . 225 THR H H 9.137 . 1 1251 . 225 THR CA C 58.969 . 1 1252 . 225 THR CB C 70.323 . 1 1253 . 225 THR C C 171.154 . 1 1254 . 226 ILE N N 122.548 . 1 1255 . 226 ILE H H 7.143 . 1 1256 . 226 ILE CA C 59.713 . 1 1257 . 226 ILE CB C 39.812 . 1 1258 . 226 ILE CG1 C 26.879 . 1 1259 . 226 ILE CD1 C 11.812 . 1 1260 . 226 ILE HD1 H 0.072 . 1 1261 . 226 ILE CG2 C 17.574 . 1 1262 . 226 ILE HG2 H 0.845 . 1 1263 . 226 ILE C C 174.500 . 1 1264 . 227 ASN N N 121.729 . 1 1265 . 227 ASN H H 8.417 . 1 1266 . 227 ASN CA C 51.829 . 1 1267 . 227 ASN CB C 42.187 . 1 1268 . 227 ASN C C 175.287 . 1 1269 . 228 GLY N N 110.654 . 1 1270 . 228 GLY H H 8.241 . 1 1271 . 228 GLY CA C 41.777 . 1 1272 . 232 TRP HE1 H 10.489 . 1 1273 . 242 TYR N N 121.680 . 1 1274 . 242 TYR H H 7.861 . 1 1275 . 242 TYR CA C 54.155 . 1 1276 . 242 TYR CB C 40.932 . 1 1277 . 242 TYR C C 174.190 . 1 1278 . 243 GLY N N 107.404 . 1 1279 . 243 GLY H H 8.498 . 1 1280 . 243 GLY CA C 42.390 . 1 1281 . 243 GLY C C 170.921 . 1 1282 . 244 VAL N N 120.686 . 1 1283 . 244 VAL H H 8.213 . 1 1284 . 244 VAL CA C 60.891 . 1 1285 . 244 VAL CB C 34.006 . 1 1286 . 244 VAL CG2 C 21.547 . 1 1287 . 244 VAL HG2 H 0.623 . 1 1288 . 244 VAL CG1 C 22.005 . 1 1289 . 244 VAL HG1 H 1.072 . 1 1290 . 244 VAL C C 174.607 . 1 1291 . 245 THR N N 119.531 . 1 1292 . 245 THR H H 9.475 . 1 1293 . 245 THR CA C 58.384 . 1 1294 . 245 THR CB C 70.888 . 1 1295 . 245 THR C C 173.968 . 1 1296 . 246 VAL N N 123.396 . 1 1297 . 246 VAL H H 8.128 . 1 1298 . 246 VAL CA C 61.762 . 1 1299 . 246 VAL CB C 31.902 . 1 1300 . 246 VAL CG2 C 21.596 . 1 1301 . 246 VAL HG2 H 0.983 . 1 1302 . 246 VAL CG1 C 20.500 . 1 1303 . 246 VAL HG1 H 0.979 . 1 1304 . 246 VAL C C 174.863 . 1 1305 . 247 LEU N N 125.413 . 1 1306 . 247 LEU H H 8.573 . 1 1307 . 247 LEU CA C 53.809 . 1 1308 . 247 LEU CB C 39.736 . 1 1309 . 247 LEU CG C 27.703 . 1 1310 . 247 LEU CD1 C 25.833 . 1 1311 . 247 LEU HD1 H 0.663 . 1 1312 . 247 LEU CD2 C 23.892 . 1 1313 . 247 LEU HD2 H 0.651 . 1 1314 . 248 PRO CA C 61.349 . 1 1315 . 248 PRO CB C 29.690 . 1 1316 . 248 PRO C C 175.317 . 1 1317 . 249 THR N N 111.586 . 1 1318 . 249 THR H H 8.785 . 1 1319 . 249 THR CA C 60.374 . 1 1320 . 249 THR CB C 70.732 . 1 1321 . 249 THR C C 174.342 . 1 1322 . 250 PHE N N 121.837 . 1 1323 . 250 PHE H H 9.556 . 1 1324 . 250 PHE CA C 56.198 . 1 1325 . 250 PHE CB C 41.159 . 1 1326 . 250 PHE C C 174.418 . 1 1327 . 251 LYS N N 129.596 . 1 1328 . 251 LYS H H 10.552 . 1 1329 . 251 LYS CA C 56.733 . 1 1330 . 251 LYS CB C 27.627 . 1 1331 . 251 LYS C C 177.436 . 1 1332 . 252 GLY N N 103.500 . 1 1333 . 252 GLY H H 9.010 . 1 1334 . 252 GLY CA C 44.461 . 1 1335 . 252 GLY C C 173.646 . 1 1336 . 253 GLN N N 122.291 . 1 1337 . 253 GLN H H 8.227 . 1 1338 . 253 GLN CA C 51.730 . 1 1339 . 253 GLN CB C 28.740 . 1 1340 . 254 PRO CA C 62.660 . 1 1341 . 254 PRO CB C 30.600 . 1 1342 . 254 PRO C C 178.347 . 1 1343 . 255 SER N N 117.900 . 1 1344 . 255 SER H H 7.971 . 1 1345 . 255 SER CA C 61.510 . 1 1346 . 255 SER CB C 64.260 . 1 1347 . 255 SER C C 173.318 . 1 1348 . 256 LYS N N 123.300 . 1 1349 . 256 LYS H H 7.646 . 1 1350 . 256 LYS CA C 52.450 . 1 1351 . 256 LYS CB C 32.690 . 1 1352 . 257 PRO CA C 61.655 . 1 1353 . 257 PRO CB C 30.833 . 1 1354 . 257 PRO C C 176.914 . 1 1355 . 258 PHE N N 118.379 . 1 1356 . 258 PHE H H 9.326 . 1 1357 . 258 PHE CA C 57.839 . 1 1358 . 258 PHE CB C 39.472 . 1 1359 . 258 PHE C C 177.387 . 1 1360 . 259 VAL N N 121.827 . 1 1361 . 259 VAL H H 8.747 . 1 1362 . 259 VAL CA C 61.340 . 1 1363 . 259 VAL CB C 33.556 . 1 1364 . 259 VAL CG2 C 22.726 . 1 1365 . 259 VAL HG2 H 1.013 . 1 1366 . 259 VAL CG1 C 21.685 . 1 1367 . 259 VAL HG1 H 0.933 . 1 1368 . 259 VAL C C 176.248 . 1 1369 . 260 GLY N N 115.956 . 1 1370 . 260 GLY H H 8.845 . 1 1371 . 260 GLY CA C 44.249 . 1 1372 . 260 GLY C C 171.353 . 1 1373 . 261 VAL N N 129.077 . 1 1374 . 261 VAL H H 11.034 . 1 1375 . 261 VAL CA C 59.609 . 1 1376 . 261 VAL CB C 32.506 . 1 1377 . 261 VAL CG2 C 21.102 . 1 1378 . 261 VAL HG2 H 0.563 . 1 1379 . 261 VAL CG1 C 20.328 . 1 1380 . 261 VAL HG1 H 0.695 . 1 1381 . 261 VAL C C 179.117 . 1 1382 . 262 LEU N N 134.21 . 1 1383 . 262 LEU H H 8.807 . 1 1384 . 262 LEU CA C 55.980 . 1 1385 . 262 LEU CB C 40.387 . 1 1386 . 262 LEU CG C 26.966 . 1 1387 . 262 LEU CD1 C 22.681 . 1 1388 . 262 LEU HD1 H 0.806 . 1 1389 . 262 LEU CD2 C 25.246 . 1 1390 . 262 LEU HD2 H 0.887 . 1 1391 . 262 LEU C C 174.968 . 1 1392 . 263 SER N N 126.557 . 1 1393 . 263 SER H H 8.765 . 1 1394 . 263 SER CA C 58.166 . 1 1395 . 263 SER CB C 65.537 . 1 1396 . 263 SER C C 170.462 . 1 1397 . 264 ALA N N 123.637 . 1 1398 . 264 ALA H H 9.127 . 1 1399 . 264 ALA CA C 49.243 . 1 1400 . 264 ALA CB C 20.238 . 1 1401 . 264 ALA C C 175.938 . 1 1402 . 265 GLY N N 110.678 . 1 1403 . 265 GLY H H 9.411 . 1 1404 . 265 GLY CA C 42.324 . 1 1405 . 265 GLY C C 170.871 . 1 1406 . 266 ILE N N 123.631 . 1 1407 . 266 ILE H H 10.279 . 1 1408 . 266 ILE CA C 59.199 . 1 1409 . 266 ILE CB C 38.984 . 1 1410 . 266 ILE CG1 C 27.140 . 1 1411 . 266 ILE CD1 C 13.820 . 1 1412 . 266 ILE HD1 H 0.925 . 1 1413 . 266 ILE CG2 C 15.815 . 1 1414 . 266 ILE HG2 H 0.805 . 1 1415 . 266 ILE C C 174.997 . 1 1416 . 267 ASN N N 125.609 . 1 1417 . 267 ASN H H 8.178 . 1 1418 . 267 ASN CA C 52.884 . 1 1419 . 267 ASN CB C 38.180 . 1 1420 . 267 ASN C C 177.019 . 1 1421 . 268 ALA N N 130.971 . 1 1422 . 268 ALA H H 8.832 . 1 1423 . 268 ALA CA C 54.667 . 1 1424 . 268 ALA CB C 17.265 . 1 1425 . 268 ALA C C 178.176 . 1 1426 . 269 ALA N N 118.137 . 1 1427 . 269 ALA H H 8.165 . 1 1428 . 269 ALA CA C 50.743 . 1 1429 . 269 ALA CB C 17.931 . 1 1430 . 269 ALA C C 177.853 . 1 1431 . 270 SER N N 113.584 . 1 1432 . 270 SER H H 7.530 . 1 1433 . 270 SER CA C 55.531 . 1 1434 . 270 SER CB C 63.833 . 1 1435 . 271 PRO CA C 62.991 . 1 1436 . 271 PRO CB C 30.570 . 1 1437 . 271 PRO C C 175.759 . 1 1438 . 272 ASN N N 119.511 . 1 1439 . 272 ASN H H 8.772 . 1 1440 . 272 ASN CA C 52.040 . 1 1441 . 272 ASN CB C 39.875 . 1 1442 . 272 ASN C C 176.026 . 1 1443 . 273 LYS N N 119.215 . 1 1444 . 273 LYS H H 7.816 . 1 1445 . 273 LYS CA C 61.061 . 1 1446 . 273 LYS CB C 31.136 . 1 1447 . 273 LYS C C 178.610 . 1 1448 . 274 GLU N N 118.213 . 1 1449 . 274 GLU H H 8.805 . 1 1450 . 274 GLU CA C 59.324 . 1 1451 . 274 GLU CB C 27.425 . 1 1452 . 274 GLU C C 179.494 . 1 1453 . 275 LEU N N 120.704 . 1 1454 . 275 LEU H H 7.445 . 1 1455 . 275 LEU CA C 56.738 . 1 1456 . 275 LEU CB C 41.540 . 1 1457 . 275 LEU CG C 26.244 . 1 1458 . 275 LEU CD1 C 25.419 . 1 1459 . 275 LEU HD1 H 0.953 . 1 1460 . 275 LEU CD2 C 22.700 . 1 1461 . 275 LEU HD2 H 0.962 . 1 1462 . 275 LEU C C 178.176 . 1 1463 . 276 ALA N N 120.313 . 1 1464 . 276 ALA H H 8.309 . 1 1465 . 276 ALA CA C 54.791 . 1 1466 . 276 ALA CB C 17.208 . 1 1467 . 276 ALA C C 178.331 . 1 1468 . 277 LYS N N 118.217 . 1 1469 . 277 LYS H H 7.812 . 1 1470 . 277 LYS CA C 59.603 . 1 1471 . 277 LYS CB C 31.774 . 1 1472 . 277 LYS C C 177.006 . 1 1473 . 278 GLU N N 118.789 . 1 1474 . 278 GLU H H 7.597 . 1 1475 . 278 GLU CA C 59.045 . 1 1476 . 278 GLU CB C 28.612 . 1 1477 . 278 GLU C C 179.014 . 1 1478 . 279 PHE N N 118.370 . 1 1479 . 279 PHE H H 8.396 . 1 1480 . 279 PHE CA C 61.034 . 1 1481 . 279 PHE CB C 37.809 . 1 1482 . 279 PHE C C 177.325 . 1 1483 . 280 LEU N N 119.928 . 1 1484 . 280 LEU H H 8.343 . 1 1485 . 280 LEU CA C 57.670 . 1 1486 . 280 LEU CB C 40.127 . 1 1487 . 280 LEU CG C 26.930 . 1 1488 . 280 LEU CD1 C 25.779 . 1 1489 . 280 LEU HD1 H 0.672 . 1 1490 . 280 LEU CD2 C 23.425 . 1 1491 . 280 LEU HD2 H 0.717 . 1 1492 . 280 LEU C C 176.882 . 1 1493 . 281 GLU N N 112.877 . 1 1494 . 281 GLU H H 8.405 . 1 1495 . 281 GLU CA C 58.919 . 1 1496 . 281 GLU CB C 28.863 . 1 1497 . 281 GLU C C 176.822 . 1 1498 . 282 ASN N N 108.873 . 1 1499 . 282 ASN H H 7.730 . 1 1500 . 282 ASN CA C 52.467 . 1 1501 . 282 ASN CB C 38.449 . 1 1502 . 282 ASN C C 174.985 . 1 1503 . 283 TYR N N 116.280 . 1 1504 . 283 TYR H H 7.162 . 1 1505 . 283 TYR CA C 59.176 . 1 1506 . 283 TYR CB C 37.351 . 1 1507 . 283 TYR C C 176.025 . 1 1508 . 284 LEU N N 121.293 . 1 1509 . 284 LEU H H 8.070 . 1 1510 . 284 LEU CA C 57.548 . 1 1511 . 284 LEU CB C 40.447 . 1 1512 . 284 LEU CG C 26.900 . 1 1513 . 284 LEU CD1 C 23.916 . 1 1514 . 284 LEU HD1 H 0.848 . 1 1515 . 284 LEU CD2 C 27.320 . 1 1516 . 284 LEU HD2 H 1.045 . 1 1517 . 284 LEU C C 176.696 . 1 1518 . 285 LEU N N 119.221 . 1 1519 . 285 LEU H H 7.817 . 1 1520 . 285 LEU CA C 53.834 . 1 1521 . 285 LEU CB C 37.817 . 1 1522 . 285 LEU CG C 27.470 . 1 1523 . 285 LEU CD1 C 25.696 . 1 1524 . 285 LEU HD1 H 1.061 . 1 1525 . 285 LEU CD2 C 24.053 . 1 1526 . 285 LEU HD2 H 1.122 . 1 1527 . 285 LEU C C 174.717 . 1 1528 . 286 THR N N 108.711 . 1 1529 . 286 THR H H 8.533 . 1 1530 . 286 THR CA C 58.306 . 1 1531 . 286 THR CB C 72.916 . 1 1532 . 286 THR C C 174.055 . 1 1533 . 287 ASP N N 122.011 . 1 1534 . 287 ASP H H 8.505 . 1 1535 . 287 ASP CA C 57.788 . 1 1536 . 287 ASP CB C 38.986 . 1 1537 . 287 ASP C C 177.530 . 1 1538 . 288 GLU N N 115.590 . 1 1539 . 288 GLU H H 8.404 . 1 1540 . 288 GLU CA C 58.668 . 1 1541 . 288 GLU CB C 28.589 . 1 1542 . 288 GLU C C 179.860 . 1 1543 . 289 GLY N N 112.872 . 1 1544 . 289 GLY H H 8.314 . 1 1545 . 289 GLY CA C 46.308 . 1 1546 . 289 GLY C C 175.007 . 1 1547 . 290 LEU N N 119.452 . 1 1548 . 290 LEU H H 8.190 . 1 1549 . 290 LEU CA C 56.683 . 1 1550 . 290 LEU CB C 41.001 . 1 1551 . 290 LEU CG C 25.326 . 1 1552 . 290 LEU CD1 C 27.903 . 1 1553 . 290 LEU HD1 H 1.081 . 1 1554 . 290 LEU CD2 C 21.851 . 1 1555 . 290 LEU HD2 H 0.800 . 1 1556 . 290 LEU C C 178.641 . 1 1557 . 291 GLU N N 120.911 . 1 1558 . 291 GLU H H 7.725 . 1 1559 . 291 GLU CA C 58.822 . 1 1560 . 291 GLU CB C 28.456 . 1 1561 . 291 GLU C C 177.928 . 1 1562 . 292 ALA N N 119.805 . 1 1563 . 292 ALA H H 7.176 . 1 1564 . 292 ALA CA C 54.649 . 1 1565 . 292 ALA CB C 17.004 . 1 1566 . 292 ALA C C 180.528 . 1 1567 . 293 VAL N N 115.817 . 1 1568 . 293 VAL H H 7.249 . 1 1569 . 293 VAL CA C 66.704 . 1 1570 . 293 VAL CB C 31.507 . 1 1571 . 293 VAL CG2 C 22.246 . 1 1572 . 293 VAL HG2 H 0.901 . 1 1573 . 293 VAL CG1 C 21.422 . 1 1574 . 293 VAL HG1 H 1.004 . 1 1575 . 293 VAL C C 176.790 . 1 1576 . 294 ASN N N 117.365 . 1 1577 . 294 ASN H H 8.689 . 1 1578 . 294 ASN CA C 55.618 . 1 1579 . 294 ASN CB C 40.348 . 1 1580 . 294 ASN C C 176.122 . 1 1581 . 295 LYS N N 115.969 . 1 1582 . 295 LYS H H 8.246 . 1 1583 . 295 LYS CA C 57.790 . 1 1584 . 295 LYS CB C 31.477 . 1 1585 . 295 LYS C C 177.164 . 1 1586 . 296 ASP N N 118.788 . 1 1587 . 296 ASP H H 7.272 . 1 1588 . 296 ASP CA C 55.530 . 1 1589 . 296 ASP CB C 41.470 . 1 1590 . 296 ASP C C 175.889 . 1 1591 . 297 LYS N N 115.853 . 1 1592 . 297 LYS H H 7.625 . 1 1593 . 297 LYS CA C 52.010 . 1 1594 . 297 LYS CB C 34.110 . 1 1595 . 298 PRO CA C 62.580 . 1 1596 . 298 PRO CB C 31.041 . 1 1597 . 298 PRO C C 178.563 . 1 1598 . 299 LEU N N 122.429 . 1 1599 . 299 LEU H H 8.598 . 1 1600 . 299 LEU CA C 55.063 . 1 1601 . 299 LEU CB C 43.177 . 1 1602 . 299 LEU CG C 26.483 . 1 1603 . 299 LEU CD1 C 26.679 . 1 1604 . 299 LEU HD1 H 0.912 . 1 1605 . 299 LEU CD2 C 22.958 . 1 1606 . 299 LEU HD2 H 0.813 . 1 1607 . 299 LEU C C 177.235 . 1 1608 . 300 GLY N N 104.046 . 1 1609 . 300 GLY H H 8.122 . 1 1610 . 300 GLY CA C 43.755 . 1 1611 . 300 GLY C C 173.603 . 1 1612 . 301 ALA N N 123.826 . 1 1613 . 301 ALA H H 7.507 . 1 1614 . 301 ALA CA C 50.852 . 1 1615 . 301 ALA CB C 18.783 . 1 1616 . 301 ALA C C 177.424 . 1 1617 . 302 VAL N N 110.311 . 1 1618 . 302 VAL H H 8.155 . 1 1619 . 302 VAL CA C 59.056 . 1 1620 . 302 VAL CB C 35.021 . 1 1621 . 302 VAL CG2 C 18.998 . 1 1622 . 302 VAL HG2 H 1.255 . 1 1623 . 302 VAL CG1 C 22.334 . 1 1624 . 302 VAL HG1 H 1.069 . 1 1625 . 302 VAL C C 173.421 . 1 1626 . 303 ALA N N 117.091 . 1 1627 . 303 ALA H H 7.632 . 1 1628 . 303 ALA CA C 52.476 . 1 1629 . 303 ALA CB C 18.835 . 1 1630 . 303 ALA C C 175.512 . 1 1631 . 304 LEU N N 114.985 . 1 1632 . 304 LEU H H 6.376 . 1 1633 . 304 LEU CA C 53.707 . 1 1634 . 304 LEU CB C 43.410 . 1 1635 . 304 LEU CG C 26.350 . 1 1636 . 304 LEU CD1 C 24.317 . 1 1637 . 304 LEU HD1 H 0.851 . 1 1638 . 304 LEU CD2 C 26.518 . 1 1639 . 304 LEU HD2 H 0.709 . 1 1640 . 304 LEU C C 175.243 . 1 1641 . 305 LYS N N 129.375 . 1 1642 . 305 LYS H H 8.039 . 1 1643 . 305 LYS CA C 59.903 . 1 1644 . 305 LYS CB C 31.117 . 1 1645 . 305 LYS C C 178.380 . 1 1646 . 306 SER N N 112.263 . 1 1647 . 306 SER H H 8.724 . 1 1648 . 306 SER CA C 60.769 . 1 1649 . 306 SER CB C 59.898 . 1 1650 . 306 SER C C 176.844 . 1 1651 . 307 TYR N N 122.210 . 1 1652 . 307 TYR H H 6.631 . 1 1653 . 307 TYR CA C 58.500 . 1 1654 . 307 TYR CB C 37.974 . 1 1655 . 307 TYR C C 177.158 . 1 1656 . 308 GLU N N 121.342 . 1 1657 . 308 GLU H H 8.489 . 1 1658 . 308 GLU CA C 57.378 . 1 1659 . 308 GLU CB C 25.262 . 1 1660 . 308 GLU C C 177.516 . 1 1661 . 309 GLU N N 115.493 . 1 1662 . 309 GLU H H 7.731 . 1 1663 . 309 GLU CA C 58.621 . 1 1664 . 309 GLU CB C 28.376 . 1 1665 . 309 GLU C C 178.557 . 1 1666 . 310 GLU N N 117.486 . 1 1667 . 310 GLU H H 6.873 . 1 1668 . 310 GLU CA C 57.250 . 1 1669 . 310 GLU CB C 28.590 . 1 1670 . 310 GLU C C 178.986 . 1 1671 . 311 LEU N N 120.952 . 1 1672 . 311 LEU H H 8.220 . 1 1673 . 311 LEU CA C 56.538 . 1 1674 . 311 LEU CB C 41.201 . 1 1675 . 311 LEU CG C 25.116 . 1 1676 . 311 LEU CD1 C 26.260 . 1 1677 . 311 LEU HD1 H 0.885 . 1 1678 . 311 LEU CD2 C 22.652 . 1 1679 . 311 LEU HD2 H 0.797 . 1 1680 . 311 LEU C C 179.366 . 1 1681 . 312 ALA N N 117.952 . 1 1682 . 312 ALA H H 8.553 . 1 1683 . 312 ALA CA C 53.394 . 1 1684 . 312 ALA CB C 16.431 . 1 1685 . 312 ALA C C 176.426 . 1 1686 . 313 LYS N N 117.329 . 1 1687 . 313 LYS H H 7.093 . 1 1688 . 313 LYS CA C 58.223 . 1 1689 . 313 LYS CB C 31.219 . 1 1690 . 313 LYS C C 177.861 . 1 1691 . 314 ASP N N 121.198 . 1 1692 . 314 ASP H H 8.286 . 1 1693 . 314 ASP CA C 49.986 . 1 1694 . 314 ASP CB C 40.789 . 1 1695 . 315 PRO CA C 63.857 . 1 1696 . 315 PRO CB C 31.505 . 1 1697 . 315 PRO C C 178.908 . 1 1698 . 316 ARG N N 116.863 . 1 1699 . 316 ARG H H 8.437 . 1 1700 . 316 ARG CA C 57.839 . 1 1701 . 316 ARG CB C 28.780 . 1 1702 . 316 ARG C C 179.565 . 1 1703 . 317 ILE N N 122.900 . 1 1704 . 317 ILE H H 7.525 . 1 1705 . 317 ILE CA C 63.909 . 1 1706 . 317 ILE CB C 35.813 . 1 1707 . 317 ILE CG1 C 28.858 . 1 1708 . 317 ILE CD1 C 12.540 . 1 1709 . 317 ILE HD1 H 1.105 . 1 1710 . 317 ILE CG2 C 17.182 . 1 1711 . 317 ILE HG2 H 0.934 . 1 1712 . 317 ILE C C 177.724 . 1 1713 . 318 ALA N N 122.557 . 1 1714 . 318 ALA H H 7.852 . 1 1715 . 318 ALA CA C 55.214 . 1 1716 . 318 ALA CB C 16.685 . 1 1717 . 318 ALA C C 181.043 . 1 1718 . 319 ALA N N 118.673 . 1 1719 . 319 ALA H H 8.128 . 1 1720 . 319 ALA CA C 54.581 . 1 1721 . 319 ALA CB C 17.315 . 1 1722 . 319 ALA C C 178.611 . 1 1723 . 320 THR N N 114.749 . 1 1724 . 320 THR H H 7.335 . 1 1725 . 320 THR CA C 67.440 . 1 1726 . 320 THR CB C 68.246 . 1 1727 . 320 THR C C 175.140 . 1 1728 . 321 MET N N 119.303 . 1 1729 . 321 MET H H 8.149 . 1 1730 . 321 MET CA C 56.472 . 1 1731 . 321 MET CB C 30.778 . 1 1732 . 321 MET C C 177.117 . 1 1733 . 322 GLU N N 121.370 . 1 1734 . 322 GLU H H 8.227 . 1 1735 . 322 GLU CA C 59.277 . 1 1736 . 322 GLU CB C 28.255 . 1 1737 . 322 GLU C C 179.193 . 1 1738 . 323 ASN N N 115.223 . 1 1739 . 323 ASN H H 8.282 . 1 1740 . 323 ASN CA C 56.298 . 1 1741 . 323 ASN CB C 38.599 . 1 1742 . 323 ASN C C 176.781 . 1 1743 . 324 ALA N N 119.661 . 1 1744 . 324 ALA H H 8.085 . 1 1745 . 324 ALA CA C 53.809 . 1 1746 . 324 ALA CB C 17.060 . 1 1747 . 324 ALA C C 179.956 . 1 1748 . 325 GLN N N 116.198 . 1 1749 . 325 GLN H H 8.239 . 1 1750 . 325 GLN CA C 57.729 . 1 1751 . 325 GLN CB C 27.390 . 1 1752 . 325 GLN C C 177.506 . 1 1753 . 326 LYS N N 117.718 . 1 1754 . 326 LYS H H 7.049 . 1 1755 . 326 LYS CA C 55.518 . 1 1756 . 326 LYS CB C 32.080 . 1 1757 . 326 LYS C C 175.911 . 1 1758 . 327 GLY N N 106.356 . 1 1759 . 327 GLY H H 7.243 . 1 1760 . 327 GLY CA C 44.032 . 1 1761 . 327 GLY C C 172.326 . 1 1762 . 328 GLU N N 121.715 . 1 1763 . 328 GLU H H 8.516 . 1 1764 . 328 GLU CA C 53.337 . 1 1765 . 328 GLU CB C 32.240 . 1 1766 . 328 GLU C C 176.471 . 1 1767 . 329 ILE N N 127.878 . 1 1768 . 329 ILE H H 9.159 . 1 1769 . 329 ILE CA C 61.680 . 1 1770 . 329 ILE CB C 37.141 . 1 1771 . 329 ILE CG1 C 26.858 . 1 1772 . 329 ILE CD1 C 12.343 . 1 1773 . 329 ILE HD1 H 0.821 . 1 1774 . 329 ILE CG2 C 16.745 . 1 1775 . 329 ILE HG2 H 0.808 . 1 1776 . 329 ILE C C 177.934 . 1 1777 . 330 MET N N 124.939 . 1 1778 . 330 MET H H 8.478 . 1 1779 . 330 MET CA C 55.904 . 1 1780 . 330 MET CB C 33.770 . 1 1781 . 331 PRO CA C 62.962 . 1 1782 . 331 PRO CB C 30.584 . 1 1783 . 331 PRO C C 175.164 . 1 1784 . 332 ASN N N 118.144 . 1 1785 . 332 ASN H H 7.588 . 1 1786 . 332 ASN CA C 50.931 . 1 1787 . 332 ASN CB C 37.799 . 1 1788 . 332 ASN C C 175.369 . 1 1789 . 333 ILE N N 108.496 . 1 1790 . 333 ILE H H 6.371 . 1 1791 . 333 ILE CA C 58.955 . 1 1792 . 333 ILE CB C 36.027 . 1 1793 . 333 ILE CG1 C 24.616 . 1 1794 . 333 ILE CD1 C 12.276 . 1 1795 . 333 ILE HD1 H -0.149 . 1 1796 . 333 ILE CG2 C 19.035 . 1 1797 . 333 ILE HG2 H 1.147 . 1 1798 . 334 PRO CA C 64.813 . 1 1799 . 334 PRO CB C 30.706 . 1 1800 . 334 PRO C C 178.493 . 1 1801 . 335 GLN N N 116.455 . 1 1802 . 335 GLN H H 8.346 . 1 1803 . 335 GLN CA C 58.793 . 1 1804 . 335 GLN CB C 25.838 . 1 1805 . 335 GLN C C 176.798 . 1 1806 . 336 MET N N 118.366 . 1 1807 . 336 MET H H 7.832 . 1 1808 . 336 MET CA C 55.427 . 1 1809 . 336 MET CB C 29.682 . 1 1810 . 337 SER C C 176.973 . 1 1811 . 338 ALA N N 122.929 . 1 1812 . 338 ALA H H 7.345 . 1 1813 . 338 ALA CA C 54.016 . 1 1814 . 338 ALA CB C 17.967 . 1 1815 . 338 ALA C C 179.737 . 1 1816 . 339 PHE N N 118.840 . 1 1817 . 339 PHE H H 7.514 . 1 1818 . 339 PHE CA C 61.159 . 1 1819 . 339 PHE CB C 38.326 . 1 1820 . 339 PHE C C 176.317 . 1 1821 . 340 TRP N N 118.018 . 1 1822 . 340 TRP H H 8.769 . 1 1823 . 340 TRP CA C 59.384 . 1 1824 . 340 TRP CB C 29.719 . 1 1825 . 340 TRP C C 178.773 . 1 1826 . 341 TYR N N 114.622 . 1 1827 . 341 TYR H H 7.426 . 1 1828 . 341 TYR CA C 60.795 . 1 1829 . 341 TYR CB C 37.800 . 1 1830 . 341 TYR C C 178.355 . 1 1831 . 342 ALA N N 121.845 . 1 1832 . 342 ALA H H 8.420 . 1 1833 . 342 ALA CA C 54.277 . 1 1834 . 342 ALA CB C 18.480 . 1 1835 . 342 ALA C C 180.594 . 1 1836 . 343 VAL N N 118.415 . 1 1837 . 343 VAL H H 8.658 . 1 1838 . 343 VAL CA C 66.381 . 1 1839 . 343 VAL CB C 30.458 . 1 1840 . 343 VAL CG2 C 23.254 . 1 1841 . 343 VAL HG2 H 0.144 . 1 1842 . 343 VAL CG1 C 21.260 . 1 1843 . 343 VAL HG1 H 0.856 . 1 1844 . 343 VAL C C 176.827 . 1 1845 . 344 ARG N N 120.776 . 1 1846 . 344 ARG H H 8.105 . 1 1847 . 344 ARG CA C 59.662 . 1 1848 . 344 ARG CB C 29.312 . 1 1849 . 344 ARG C C 178.217 . 1 1850 . 345 THR N N 113.591 . 1 1851 . 345 THR H H 7.524 . 1 1852 . 345 THR CA C 65.852 . 1 1853 . 345 THR CB C 68.619 . 1 1854 . 345 THR C C 174.836 . 1 1855 . 346 ALA N N 122.839 . 1 1856 . 346 ALA H H 7.785 . 1 1857 . 346 ALA CA C 54.851 . 1 1858 . 346 ALA CB C 18.046 . 1 1859 . 346 ALA C C 178.931 . 1 1860 . 347 VAL N N 115.898 . 1 1861 . 347 VAL H H 8.139 . 1 1862 . 347 VAL CA C 66.910 . 1 1863 . 347 VAL CB C 30.836 . 1 1864 . 347 VAL CG2 C 22.336 . 1 1865 . 347 VAL HG2 H 1.048 . 1 1866 . 347 VAL CG1 C 20.517 . 1 1867 . 347 VAL HG1 H 0.925 . 1 1868 . 347 VAL C C 177.752 . 1 1869 . 348 ILE N N 118.315 . 1 1870 . 348 ILE H H 7.759 . 1 1871 . 348 ILE CA C 64.275 . 1 1872 . 348 ILE CB C 36.802 . 1 1873 . 348 ILE CG1 C 28.625 . 1 1874 . 348 ILE CD1 C 13.073 . 1 1875 . 348 ILE HD1 H 0.872 . 1 1876 . 348 ILE CG2 C 16.235 . 1 1877 . 348 ILE HG2 H 0.908 . 1 1878 . 348 ILE C C 180.023 . 1 1879 . 349 ASN N N 121.044 . 1 1880 . 349 ASN H H 8.807 . 1 1881 . 349 ASN CA C 55.254 . 1 1882 . 349 ASN CB C 36.542 . 1 1883 . 349 ASN C C 177.771 . 1 1884 . 350 ALA N N 122.692 . 1 1885 . 350 ALA H H 8.500 . 1 1886 . 350 ALA CA C 53.372 . 1 1887 . 350 ALA CB C 17.287 . 1 1888 . 350 ALA C C 180.861 . 1 1889 . 351 ALA N N 120.994 . 1 1890 . 351 ALA H H 9.141 . 1 1891 . 351 ALA CA C 54.926 . 1 1892 . 351 ALA CB C 17.333 . 1 1893 . 351 ALA C C 178.034 . 1 1894 . 352 SER N N 107.885 . 1 1895 . 352 SER H H 7.875 . 1 1896 . 352 SER CA C 58.284 . 1 1897 . 352 SER CB C 63.746 . 1 1898 . 352 SER C C 175.453 . 1 1899 . 353 GLY N N 109.757 . 1 1900 . 353 GLY H H 7.606 . 1 1901 . 353 GLY CA C 45.132 . 1 1902 . 353 GLY C C 174.286 . 1 1903 . 354 ARG N N 121.015 . 1 1904 . 354 ARG H H 8.212 . 1 1905 . 354 ARG CA C 57.844 . 1 1906 . 354 ARG CB C 30.120 . 1 1907 . 354 ARG C C 176.562 . 1 1908 . 355 GLN N N 113.570 . 1 1909 . 355 GLN H H 7.322 . 1 1910 . 355 GLN CA C 53.621 . 1 1911 . 355 GLN CB C 35.713 . 1 1912 . 355 GLN C C 175.820 . 1 1913 . 356 THR N N 111.703 . 1 1914 . 356 THR H H 8.550 . 1 1915 . 356 THR CA C 60.768 . 1 1916 . 356 THR CB C 69.900 . 1 1917 . 356 THR C C 174.686 . 1 1918 . 357 VAL N N 121.298 . 1 1919 . 357 VAL H H 8.710 . 1 1920 . 357 VAL CA C 67.294 . 1 1921 . 357 VAL CB C 31.000 . 1 1922 . 357 VAL CG2 C 23.411 . 1 1923 . 357 VAL HG2 H 1.052 . 1 1924 . 357 VAL CG1 C 21.315 . 1 1925 . 357 VAL HG1 H 0.991 . 1 1926 . 357 VAL C C 176.887 . 1 1927 . 358 ASP N N 115.119 . 1 1928 . 358 ASP H H 8.101 . 1 1929 . 358 ASP CA C 57.032 . 1 1930 . 358 ASP CB C 40.286 . 1 1931 . 358 ASP C C 178.645 . 1 1932 . 359 GLU N N 118.602 . 1 1933 . 359 GLU H H 7.587 . 1 1934 . 359 GLU CA C 58.188 . 1 1935 . 359 GLU CB C 29.515 . 1 1936 . 359 GLU C C 178.344 . 1 1937 . 360 ALA N N 121.458 . 1 1938 . 360 ALA H H 8.681 . 1 1939 . 360 ALA CA C 54.209 . 1 1940 . 360 ALA CB C 17.674 . 1 1941 . 360 ALA C C 181.257 . 1 1942 . 361 LEU N N 116.148 . 1 1943 . 361 LEU H H 8.059 . 1 1944 . 361 LEU CA C 56.834 . 1 1945 . 361 LEU CB C 39.193 . 1 1946 . 361 LEU CG C 26.006 . 1 1947 . 361 LEU CD1 C 25.226 . 1 1948 . 361 LEU HD1 H 0.895 . 1 1949 . 361 LEU CD2 C 19.591 . 1 1950 . 361 LEU HD2 H 0.722 . 1 1951 . 361 LEU C C 178.651 . 1 1952 . 362 LYS N N 121.483 . 1 1953 . 362 LYS H H 7.680 . 1 1954 . 362 LYS CA C 59.136 . 1 1955 . 362 LYS CB C 30.889 . 1 1956 . 362 LYS C C 179.626 . 1 1957 . 363 ASP N N 120.033 . 1 1958 . 363 ASP H H 8.132 . 1 1959 . 363 ASP CA C 56.640 . 1 1960 . 363 ASP CB C 39.818 . 1 1961 . 363 ASP C C 178.639 . 1 1962 . 364 ALA N N 121.232 . 1 1963 . 364 ALA H H 7.727 . 1 1964 . 364 ALA CA C 54.656 . 1 1965 . 364 ALA CB C 17.130 . 1 1966 . 364 ALA C C 178.152 . 1 1967 . 365 GLN N N 118.119 . 1 1968 . 365 GLN H H 8.230 . 1 1969 . 365 GLN CA C 59.731 . 1 1970 . 365 GLN CB C 26.723 . 1 1971 . 365 GLN C C 179.014 . 1 1972 . 366 THR N N 115.203 . 1 1973 . 366 THR H H 8.143 . 1 1974 . 366 THR CA C 65.512 . 1 1975 . 366 THR CB C 68.352 . 1 1976 . 366 THR C C 175.698 . 1 1977 . 367 ARG N N 120.044 . 1 1978 . 367 ARG H H 7.951 . 1 1979 . 367 ARG CA C 58.231 . 1 1980 . 367 ARG CB C 29.202 . 1 1981 . 367 ARG C C 178.453 . 1 1982 . 368 ILE N N 117.302 . 1 1983 . 368 ILE H H 7.986 . 1 1984 . 368 ILE CA C 64.271 . 1 1985 . 368 ILE CB C 38.073 . 1 1986 . 368 ILE CG1 C 28.350 . 1 1987 . 368 ILE CD1 C 15.275 . 1 1988 . 368 ILE HD1 H 0.684 . 1 1989 . 368 ILE CG2 C 19.304 . 1 1990 . 368 ILE HG2 H 1.023 . 1 1991 . 368 ILE C C 176.912 . 1 1992 . 369 THR N N 107.071 . 1 1993 . 369 THR H H 7.629 . 1 1994 . 369 THR CA C 61.884 . 1 1995 . 369 THR CB C 69.751 . 1 1996 . 369 THR C C 174.046 . 1 1997 . 370 LYS N N 128.198 . 1 1998 . 370 LYS H H 7.390 . 1 1999 . 370 LYS CA C 58.269 . 1 2000 . 370 LYS CB C 31.892 . 1 stop_ save_