data_6229 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift assignments for the Nucleotide-binding domain of Thermus Thermophilus DnaK ; _BMRB_accession_number 6229 _BMRB_flat_file_name bmr6229.str _Entry_type original _Submission_date 2004-06-10 _Accession_date 2004-06-11 _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 Revington Matthew J. . 2 Zuiderweg Erik R.P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 330 "13C chemical shifts" 1009 "15N chemical shifts" 330 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-14 original author . stop_ _Original_release_date 2005-11-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15452445 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Revington Matthew J. . 2 Zuiderweg Erik R.P. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 30 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 113 _Page_last 114 _Year 2004 _Details . loop_ _Keyword DnaK TROSY chaperone Hsp70 atpase stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Letter to the Editor: TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone. Revington, M., and Zuiderweg, E.R.P. J. Biol. NMR in press ; _Citation_title 'TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15452445 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Revington Matthew . . 2 Zuiderweg 'Erik R. P.' R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 30 _Journal_issue 1 _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 113 _Page_last 114 _Year 2004 _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus Thermophilus Hsp70 chaperone DnaK: Implications for the allosteric mechanism. Revington M, Holder TM, Zuiderweg ER. J Biol Chem. 2004 Jun 2 [Epub ahead of print] ; _Citation_title 'NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15175340 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Revington Matthew . . 2 Holder 'Tina M.' M. . 3 Zuiderweg 'Erik R. P.' R. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 279 _Journal_issue 32 _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 33958 _Page_last 33967 _Year 2004 _Details ; We present an NMR investigation of the nucleotide-dependent conformational properties of a 44-kDa nucleotide binding domain (NBD) of an Hsp70 protein. Conformational changes driven by ATP binding and hydrolysis in the N-terminal NBD are believed to allosterically regulate substrate affinity in the C-terminal substrate binding domain. Several crystal structures of Hsc70 NBDs in different nucleotide states have, however, not shown significant structural differences. We have previously reported the NMR assignments of the backbone resonances of the NBD of the bacterial Hsp70 homologue Thermus thermophilus DnaK in the ADP-bound state. In this study we show, by assigning the NBD with the ATP/transition state analogue, ADP.AlFx, bound, that it closely mimics the ATP-bound state. Chemical shift difference mapping of the two nucleotide states identified differences in a cluster of residues at the interface between subdomains 1A and 1B. Further analysis of the spectra revealed that the ATP state exhibited a single conformation, whereas the ADP state was in slow conformational exchange between a form similar to the ATP state and another state unique to the ADP-bound form. A model is proposed of the allosteric mechanism based on the nucleotide state altering the balance of a dynamic equilibrium between the open and closed states. The observed chemical shift perturbations were concentrated in an area close to a previously described J-domain binding channel, confirming the importance of that region in the allosteric mechanism. ; save_ ################################## # Molecular system description # ################################## save_DnaK_NBD _Saveframe_category molecular_system _Mol_system_name 'Thermus Thermophilus Dnak Nucleotide binding domain' _Abbreviation_common 'DnaK NBD' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'DnaK nucleotide binding domain, Dnak NBD' $DnaK stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'Protein chaperone' ATPase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DnaK _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'DnaK NBD' _Abbreviation_common DnaK _Molecular_mass . _Mol_thiol_state 'not present' _Details ; ASP44 converted to Isoasp when sample pH was decreased from pH 7.4 to pH 6.0 ; ############################## # Polymer residue sequence # ############################## _Residue_count 401 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MAKAVGIDLGTTNSVIAVLE GGKPVVLENAEGERVTPSVV AFRDGETLVGRMAKRQAVLN PEGTIFEIKRFIGRRFEEVQ EEAKRVPYKVVPGPDGGVRV EVKGKLYTPEEISAMILRKL VEDASKKLGEKITKAVITVP AYFNNAQREATANAGRIAGL EVLRIINEPTAAALAYGLDK KGNETVLVFDLGGGTFDVTI LEIGEGVFEVKATSGDTHLG GSDMDHAIVNWLAEEFKKEH GVDLKADRQALQRLIEAAEK AKIELSSTLETTISLPFIAL DPASKTPLHLEKKLTRAKFE ELIQPLLKRLRGPVEQALKD AGLTPAQIDEVILVGGATRV PAVQQVVRELLGKEPNRSVN PDEVVAMGAAIQAGVLMGEV R ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -20 MET 2 -19 GLY 3 -18 SER 4 -17 SER 5 -16 HIS 6 -15 HIS 7 -14 HIS 8 -13 HIS 9 -12 HIS 10 -11 HIS 11 -10 SER 12 -9 SER 13 -8 GLY 14 -7 LEU 15 -6 VAL 16 -5 PRO 17 -4 ARG 18 -3 GLY 19 -2 SER 20 -1 HIS 21 1 MET 22 2 ALA 23 3 LYS 24 4 ALA 25 5 VAL 26 6 GLY 27 7 ILE 28 8 ASP 29 9 LEU 30 10 GLY 31 11 THR 32 12 THR 33 13 ASN 34 14 SER 35 15 VAL 36 16 ILE 37 17 ALA 38 18 VAL 39 19 LEU 40 20 GLU 41 21 GLY 42 22 GLY 43 23 LYS 44 24 PRO 45 25 VAL 46 26 VAL 47 27 LEU 48 28 GLU 49 29 ASN 50 30 ALA 51 31 GLU 52 32 GLY 53 33 GLU 54 34 ARG 55 35 VAL 56 36 THR 57 37 PRO 58 38 SER 59 39 VAL 60 40 VAL 61 41 ALA 62 42 PHE 63 43 ARG 64 44 ASP 65 45 GLY 66 46 GLU 67 47 THR 68 48 LEU 69 49 VAL 70 50 GLY 71 51 ARG 72 52 MET 73 53 ALA 74 54 LYS 75 55 ARG 76 56 GLN 77 57 ALA 78 58 VAL 79 59 LEU 80 60 ASN 81 61 PRO 82 62 GLU 83 63 GLY 84 64 THR 85 65 ILE 86 66 PHE 87 67 GLU 88 68 ILE 89 69 LYS 90 70 ARG 91 71 PHE 92 72 ILE 93 73 GLY 94 74 ARG 95 75 ARG 96 76 PHE 97 77 GLU 98 78 GLU 99 79 VAL 100 80 GLN 101 81 GLU 102 82 GLU 103 83 ALA 104 84 LYS 105 85 ARG 106 86 VAL 107 87 PRO 108 88 TYR 109 89 LYS 110 90 VAL 111 91 VAL 112 92 PRO 113 93 GLY 114 94 PRO 115 95 ASP 116 96 GLY 117 97 GLY 118 98 VAL 119 99 ARG 120 100 VAL 121 101 GLU 122 102 VAL 123 103 LYS 124 104 GLY 125 105 LYS 126 106 LEU 127 107 TYR 128 108 THR 129 109 PRO 130 110 GLU 131 111 GLU 132 112 ILE 133 113 SER 134 114 ALA 135 115 MET 136 116 ILE 137 117 LEU 138 118 ARG 139 119 LYS 140 120 LEU 141 121 VAL 142 122 GLU 143 123 ASP 144 124 ALA 145 125 SER 146 126 LYS 147 127 LYS 148 128 LEU 149 129 GLY 150 130 GLU 151 131 LYS 152 132 ILE 153 133 THR 154 134 LYS 155 135 ALA 156 136 VAL 157 137 ILE 158 138 THR 159 139 VAL 160 140 PRO 161 141 ALA 162 142 TYR 163 143 PHE 164 144 ASN 165 145 ASN 166 146 ALA 167 147 GLN 168 148 ARG 169 149 GLU 170 150 ALA 171 151 THR 172 152 ALA 173 153 ASN 174 154 ALA 175 155 GLY 176 156 ARG 177 157 ILE 178 158 ALA 179 159 GLY 180 160 LEU 181 161 GLU 182 162 VAL 183 163 LEU 184 164 ARG 185 165 ILE 186 166 ILE 187 167 ASN 188 168 GLU 189 169 PRO 190 170 THR 191 171 ALA 192 172 ALA 193 173 ALA 194 174 LEU 195 175 ALA 196 176 TYR 197 177 GLY 198 178 LEU 199 179 ASP 200 180 LYS 201 181 LYS 202 182 GLY 203 183 ASN 204 184 GLU 205 185 THR 206 186 VAL 207 187 LEU 208 188 VAL 209 189 PHE 210 190 ASP 211 191 LEU 212 192 GLY 213 193 GLY 214 194 GLY 215 195 THR 216 196 PHE 217 197 ASP 218 198 VAL 219 199 THR 220 200 ILE 221 201 LEU 222 202 GLU 223 203 ILE 224 204 GLY 225 205 GLU 226 206 GLY 227 207 VAL 228 208 PHE 229 209 GLU 230 210 VAL 231 211 LYS 232 212 ALA 233 213 THR 234 214 SER 235 215 GLY 236 216 ASP 237 217 THR 238 218 HIS 239 219 LEU 240 220 GLY 241 221 GLY 242 222 SER 243 223 ASP 244 224 MET 245 225 ASP 246 226 HIS 247 227 ALA 248 228 ILE 249 229 VAL 250 230 ASN 251 231 TRP 252 232 LEU 253 233 ALA 254 234 GLU 255 235 GLU 256 236 PHE 257 237 LYS 258 238 LYS 259 239 GLU 260 240 HIS 261 241 GLY 262 242 VAL 263 243 ASP 264 244 LEU 265 245 LYS 266 246 ALA 267 247 ASP 268 248 ARG 269 249 GLN 270 250 ALA 271 251 LEU 272 252 GLN 273 253 ARG 274 254 LEU 275 255 ILE 276 256 GLU 277 257 ALA 278 258 ALA 279 259 GLU 280 260 LYS 281 261 ALA 282 262 LYS 283 263 ILE 284 264 GLU 285 265 LEU 286 266 SER 287 267 SER 288 268 THR 289 269 LEU 290 270 GLU 291 271 THR 292 272 THR 293 273 ILE 294 274 SER 295 275 LEU 296 276 PRO 297 277 PHE 298 278 ILE 299 279 ALA 300 280 LEU 301 281 ASP 302 282 PRO 303 283 ALA 304 284 SER 305 285 LYS 306 286 THR 307 287 PRO 308 288 LEU 309 289 HIS 310 290 LEU 311 291 GLU 312 292 LYS 313 293 LYS 314 294 LEU 315 295 THR 316 296 ARG 317 297 ALA 318 298 LYS 319 299 PHE 320 300 GLU 321 301 GLU 322 302 LEU 323 303 ILE 324 304 GLN 325 305 PRO 326 306 LEU 327 307 LEU 328 308 LYS 329 309 ARG 330 310 LEU 331 311 ARG 332 312 GLY 333 313 PRO 334 314 VAL 335 315 GLU 336 316 GLN 337 317 ALA 338 318 LEU 339 319 LYS 340 320 ASP 341 321 ALA 342 322 GLY 343 323 LEU 344 324 THR 345 325 PRO 346 326 ALA 347 327 GLN 348 328 ILE 349 329 ASP 350 330 GLU 351 331 VAL 352 332 ILE 353 333 LEU 354 334 VAL 355 335 GLY 356 336 GLY 357 337 ALA 358 338 THR 359 339 ARG 360 340 VAL 361 341 PRO 362 342 ALA 363 343 VAL 364 344 GLN 365 345 GLN 366 346 VAL 367 347 VAL 368 348 ARG 369 349 GLU 370 350 LEU 371 351 LEU 372 352 GLY 373 353 LYS 374 354 GLU 375 355 PRO 376 356 ASN 377 357 ARG 378 358 SER 379 359 VAL 380 360 ASN 381 361 PRO 382 362 ASP 383 363 GLU 384 364 VAL 385 365 VAL 386 366 ALA 387 367 MET 388 368 GLY 389 369 ALA 390 370 ALA 391 371 ILE 392 372 GLN 393 373 ALA 394 374 GLY 395 375 VAL 396 376 LEU 397 377 MET 398 378 GLY 399 379 GLU 400 380 VAL 401 381 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value DBJ BAA12280 "DnaK homologue [Thermus thermophilus HB8]" 95.01 615 100.00 100.00 0.00e+00 DBJ BAA81741 "DnaK [Thermus thermophilus HB8]" 95.01 615 100.00 100.00 0.00e+00 DBJ BAA96089 "DnaK [Thermus thermophilus HB8]" 95.01 615 100.00 100.00 0.00e+00 DBJ BAD71314 "chaperone protein DnaK (heat shock protein 70) [Thermus thermophilus HB8]" 95.01 615 100.00 100.00 0.00e+00 EMBL CAA69159 "DnaK-homologue [Thermus thermophilus HB8]" 95.01 615 100.00 100.00 0.00e+00 GB AAB04676 "dnaK [Thermus thermophilus HB8]" 95.26 616 98.95 99.21 0.00e+00 GB AAS81469 "chaperone protein dnaK [Thermus thermophilus HB27]" 95.01 615 99.74 100.00 0.00e+00 GB AEG33909 "Chaperone protein dnaK [Thermus thermophilus SG0.5JP17-16]" 95.01 615 98.43 99.74 0.00e+00 GB AFH38459 "chaperone protein DnaK [Thermus thermophilus JL-18]" 95.01 615 98.43 99.74 0.00e+00 REF WP_011173541 "chaperone protein DnaK [Thermus thermophilus]" 95.01 615 99.74 100.00 0.00e+00 REF WP_011228715 "chaperone protein DnaK [Thermus thermophilus]" 95.01 615 100.00 100.00 0.00e+00 REF WP_014510666 "chaperone protein DnaK [Thermus thermophilus]" 95.01 615 98.43 99.74 0.00e+00 REF WP_014629205 "chaperone protein DnaK [Thermus thermophilus]" 95.01 615 98.43 99.74 0.00e+00 REF WP_024119965 "chaperone protein DnaK [Thermus thermophilus]" 95.01 615 100.00 100.00 0.00e+00 SP Q56235 "RecName: Full=Chaperone protein DnaK; AltName: Full=HSP70; AltName: Full=Heat shock 70 kDa protein; AltName: Full=Heat shock pr" 95.01 615 100.00 100.00 0.00e+00 SP Q72IK5 "RecName: Full=Chaperone protein DnaK; AltName: Full=HSP70; AltName: Full=Heat shock 70 kDa protein; AltName: Full=Heat shock pr" 95.01 615 99.74 100.00 0.00e+00 stop_ save_ ############# # Ligands # ############# save_ADP _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common ADENOSINE-5'-DIPHOSPHATE _Abbreviation_common ADP _BMRB_code ADP _PDB_code ADP _Molecular_mass 427.201 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1' C1' C . 0 . ? C2 C2 C . 0 . ? C2' C2' C . 0 . ? C3' C3' C . 0 . ? C4 C4 C . 0 . ? C4' C4' C . 0 . ? C5 C5 C . 0 . ? C5' C5' C . 0 . ? C6 C6 C . 0 . ? C8 C8 C . 0 . ? H1' H1' H . 0 . ? H2 H2 H . 0 . ? H2' H2' H . 0 . ? H3' H3' H . 0 . ? H4' H4' H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H8 H8 H . 0 . ? HN61 HN61 H . 0 . ? HN62 HN62 H . 0 . ? HO2' HO2' H . 0 . ? HO3' HO3' H . 0 . ? HOA2 HOA2 H . 0 . ? HOB2 HOB2 H . 0 . ? HOB3 HOB3 H . 0 . ? N1 N1 N . 0 . ? N3 N3 N . 0 . ? N6 N6 N . 0 . ? N7 N7 N . 0 . ? N9 N9 N . 0 . ? O1A O1A O . 0 . ? O1B O1B O . 0 . ? O2' O2' O . 0 . ? O2A O2A O . 0 . ? O2B O2B O . 0 . ? O3' O3' O . 0 . ? O3A O3A O . 0 . ? O3B O3B O . 0 . ? O4' O4' O . 0 . ? O5' O5' O . 0 . ? PA PA P . 0 . ? PB PB P . 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 DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? SING O3B HOB3 ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O3A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'1 ? ? SING C5' H5'2 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? SING C6 N6 ? ? DOUB C6 N1 ? ? SING N6 HN61 ? ? SING N6 HN62 ? ? SING N1 C2 ? ? DOUB C2 N3 ? ? SING C2 H2 ? ? SING N3 C4 ? ? 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 _Strain _ATCC_number _Gene_mnemonic $DnaK 'Thermus thermophilus' 274 Eubacteria . Thermus thermophilus HB8 'ATCC 27634' 'DNAK THETH' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DnaK 'recombinant technology' E.coli Escherichia coli 'BL21 De3' . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $DnaK . mM 0.4 0.6 '[U-97% 2H; U-95% 13C; U-95% 15N]' HEPES . mM 50 50 . 'Potassium Chloride' . mM 10 10 . 'magnesium chloride' . mM 5 5 . ADP . mM 5 5 . 'Sodium phosphate' . mM 5 5 . stop_ save_ ############################ # Computer software used # ############################ save_NMRPIPE _Saveframe_category software _Name NMRPIPE _Version . loop_ _Task 'Data processing' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task Assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_TROSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _Sample_label $Sample_1 save_ save_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _Sample_label $Sample_1 save_ save_TROSY-HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _Sample_label $Sample_1 save_ save_TROSY-HN(CA)CO_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _Sample_label $Sample_1 save_ save_TROSY-HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _Sample_label $Sample_1 save_ save_TROSY-HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _Sample_label $Sample_1 save_ save_TROSY-HN(CO)CACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _Sample_label $Sample_1 save_ save_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label $Sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TROSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name TROSY-HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Cond-1 _Saveframe_category sample_conditions _Details 'Samples were equilibrated at 55C for 20 minutes before data collection.' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 na temperature 328 0.5 K 'ionic strength' 0.1 0.02 M 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 DSS H 1 'methyl protons' ppm 0.0 . indirect . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_ _Experiment_label '1H-15N TROSY' TROSY-HNCA TROSY-HNCO TROSY-HN(CA)CO TROSY-HN(CO)CA TROSY-HNCACB TROSY-HN(CO)CACB '1H-15N NOESY' stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $Cond-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'DnaK nucleotide binding domain, Dnak NBD' _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 . 21 MET H H 8.206 0.01 1 2 . 21 MET CA C 54.584 0.2 1 3 . 21 MET C C 174.68 0.2 1 4 . 21 MET N N 119.96 0.2 1 5 . 22 ALA H H 7.977 0.01 1 6 . 22 ALA CA C 51.484 0.2 1 7 . 22 ALA C C 179.38 0.2 1 8 . 22 ALA CB C 19.284 0.2 1 9 . 22 ALA N N 126.332 0.2 1 10 . 23 LYS H H 8.117 0.01 1 11 . 23 LYS CA C 54.984 0.2 1 12 . 23 LYS C C 173.58 0.2 1 13 . 23 LYS CB C 32.184 0.2 1 14 . 23 LYS N N 120.055 0.2 1 15 . 24 ALA H H 8.305 0.01 1 16 . 24 ALA CA C 50.284 0.2 1 17 . 24 ALA C C 175.18 0.2 1 18 . 24 ALA CB C 19.584 0.2 1 19 . 24 ALA N N 125.065 0.2 1 20 . 25 VAL H H 7.887 0.01 1 21 . 25 VAL CA C 59.384 0.2 1 22 . 25 VAL C C 173.88 0.2 1 23 . 25 VAL CB C 33.784 0.2 1 24 . 25 VAL N N 116.426 0.2 1 25 . 26 GLY H H 9 0.01 1 26 . 26 GLY CA C 43.784 0.2 1 27 . 26 GLY C C 170.98 0.2 1 28 . 26 GLY N N 109.793 0.2 1 29 . 27 ILE H H 8.48 0.01 1 30 . 27 ILE CA C 59.984 0.2 1 31 . 27 ILE C C 174.78 0.2 1 32 . 27 ILE CB C 41.684 0.2 1 33 . 27 ILE N N 123.656 0.2 1 34 . 28 ASP H H 8.295 0.01 1 35 . 28 ASP CA C 50.284 0.2 1 36 . 28 ASP C C 177.48 0.2 1 37 . 28 ASP CB C 41.984 0.2 1 38 . 28 ASP N N 125.725 0.2 1 39 . 29 LEU H H 6.93 0.01 1 40 . 29 LEU CA C 52.684 0.2 1 41 . 29 LEU CB C 40.984 0.2 1 42 . 29 LEU N N 130.145 0.2 1 43 . 34 SER CA C 57.984 0.2 1 44 . 34 SER C C 175.08 0.2 1 45 . 35 VAL H H 8.549 0.01 1 46 . 35 VAL CA C 60.984 0.2 1 47 . 35 VAL C C 171.88 0.2 1 48 . 35 VAL CB C 36.384 0.2 1 49 . 35 VAL N N 124.454 0.2 1 50 . 36 ILE H H 9.108 0.01 1 51 . 36 ILE CA C 57.884 0.2 1 52 . 36 ILE C C 170.88 0.2 1 53 . 36 ILE CB C 41.384 0.2 1 54 . 36 ILE N N 127.262 0.2 1 55 . 37 ALA H H 8.956 0.01 1 56 . 37 ALA CA C 49.484 0.2 1 57 . 37 ALA C C 174.08 0.2 1 58 . 37 ALA CB C 22.184 0.2 1 59 . 37 ALA N N 128.654 0.2 1 60 . 38 VAL H H 8.888 0.01 1 61 . 38 VAL CA C 58.484 0.2 1 62 . 38 VAL C C 172.78 0.2 1 63 . 38 VAL CB C 35.384 0.2 1 64 . 38 VAL N N 118.168 0.2 1 65 . 39 LEU H H 8.151 0.01 1 66 . 39 LEU CA C 54.084 0.2 1 67 . 39 LEU C C 175.88 0.2 1 68 . 39 LEU CB C 40.984 0.2 1 69 . 39 LEU N N 125.149 0.2 1 70 . 40 GLU H H 8.87 0.01 1 71 . 40 GLU CA C 55.284 0.2 1 72 . 40 GLU C C 176.18 0.2 1 73 . 40 GLU CB C 30.884 0.2 1 74 . 40 GLU N N 127.653 0.2 1 75 . 44 PRO CA C 62.084 0.2 1 76 . 44 PRO C C 175.08 0.2 1 77 . 44 PRO CB C 31.184 0.2 1 78 . 45 VAL H H 9.205 0.01 1 79 . 45 VAL CA C 60.484 0.2 1 80 . 45 VAL C C 174.48 0.2 1 81 . 45 VAL CB C 34.184 0.2 1 82 . 45 VAL N N 124.235 0.2 1 83 . 46 VAL H H 8.199 0.01 1 84 . 46 VAL CA C 62.384 0.2 1 85 . 46 VAL C C 175.08 0.2 1 86 . 46 VAL CB C 31.184 0.2 1 87 . 46 VAL N N 127.581 0.2 1 88 . 47 LEU H H 8.072 0.01 1 89 . 47 LEU CA C 53.184 0.2 1 90 . 47 LEU C C 174.98 0.2 1 91 . 47 LEU CB C 41.784 0.2 1 92 . 47 LEU N N 128.229 0.2 1 93 . 48 GLU H H 8.202 0.01 1 94 . 48 GLU CA C 55.184 0.2 1 95 . 48 GLU C C 175.58 0.2 1 96 . 48 GLU CB C 29.884 0.2 1 97 . 48 GLU N N 121.455 0.2 1 98 . 49 ASN H H 8.048 0.01 1 99 . 49 ASN CA C 50.984 0.2 1 100 . 49 ASN C C 177.28 0.2 1 101 . 49 ASN CB C 37.984 0.2 1 102 . 49 ASN N N 118.563 0.2 1 103 . 50 ALA H H 8.85 0.01 1 104 . 50 ALA CA C 53.884 0.2 1 105 . 50 ALA C C 178.08 0.2 1 106 . 50 ALA CB C 18.584 0.2 1 107 . 50 ALA N N 122.681 0.2 1 108 . 51 GLU H H 7.875 0.01 1 109 . 51 GLU CA C 57.584 0.2 1 110 . 51 GLU C C 175.68 0.2 1 111 . 51 GLU CB C 27.684 0.2 1 112 . 51 GLU N N 118.175 0.2 1 113 . 52 GLY H H 8.184 0.01 1 114 . 52 GLY CA C 45.084 0.2 1 115 . 52 GLY C C 173.38 0.2 1 116 . 52 GLY N N 109.26 0.2 1 117 . 53 GLU H H 7.873 0.01 1 118 . 53 GLU CA C 55.284 0.2 1 119 . 53 GLU C C 174.68 0.2 1 120 . 53 GLU CB C 31.484 0.2 1 121 . 53 GLU N N 121.336 0.2 1 122 . 54 ARG H H 8.337 0.01 1 123 . 54 ARG CA C 61.184 0.2 1 124 . 54 ARG C C 175.58 0.2 1 125 . 54 ARG CB C 31.484 0.2 1 126 . 54 ARG N N 120.414 0.2 1 127 . 57 PRO CA C 63.084 0.2 1 128 . 57 PRO C C 176.98 0.2 1 129 . 58 SER H H 9.426 0.01 1 130 . 58 SER CA C 61.384 0.2 1 131 . 58 SER C C 175.18 0.2 1 132 . 58 SER N N 125.419 0.2 1 133 . 59 VAL H H 8.574 0.01 1 134 . 59 VAL CA C 60.384 0.2 1 135 . 59 VAL C C 172.28 0.2 1 136 . 59 VAL CB C 35.184 0.2 1 137 . 59 VAL N N 127.195 0.2 1 138 . 60 VAL H H 7.962 0.01 1 139 . 60 VAL CA C 59.584 0.2 1 140 . 60 VAL C C 172.48 0.2 1 141 . 60 VAL CB C 35.284 0.2 1 142 . 60 VAL N N 126.937 0.2 1 143 . 61 ALA H H 9.265 0.01 1 144 . 61 ALA CA C 49.084 0.2 1 145 . 61 ALA C C 173.58 0.2 1 146 . 61 ALA CB C 24.184 0.2 1 147 . 61 ALA N N 127.737 0.2 1 148 . 62 PHE H H 8.577 0.01 1 149 . 62 PHE CA C 56.384 0.2 1 150 . 62 PHE C C 175.48 0.2 1 151 . 62 PHE CB C 39.384 0.2 1 152 . 62 PHE N N 121.703 0.2 1 153 . 63 ARG H H 8.462 0.01 1 154 . 63 ARG CA C 54.484 0.2 1 155 . 63 ARG C C 174.48 0.2 1 156 . 63 ARG CB C 31.184 0.2 1 157 . 63 ARG N N 125.401 0.2 1 158 . 64 ASP H H 8.811 0.01 1 159 . 64 ASP CA C 50.984 0.2 1 160 . 64 ASP CB C 36.684 0.2 1 161 . 64 ASP N N 124.216 0.2 1 162 . 65 GLY H H 7.558 0.01 1 163 . 65 GLY CA C 45.584 0.2 1 164 . 65 GLY C C 174.18 0.2 1 165 . 65 GLY N N 116.034 0.2 1 166 . 66 GLU H H 8.401 0.01 1 167 . 66 GLU CA C 55.484 0.2 1 168 . 66 GLU C C 175.48 0.2 1 169 . 66 GLU CB C 35.684 0.2 1 170 . 66 GLU N N 123.222 0.2 1 171 . 67 THR H H 8.308 0.01 1 172 . 67 THR CA C 61.084 0.2 1 173 . 67 THR C C 173.08 0.2 1 174 . 67 THR CB C 69.684 0.2 1 175 . 67 THR N N 120.485 0.2 1 176 . 68 LEU H H 9.121 0.01 1 177 . 68 LEU CA C 52.584 0.2 1 178 . 68 LEU C C 174.68 0.2 1 179 . 68 LEU CB C 43.284 0.2 1 180 . 68 LEU N N 128.175 0.2 1 181 . 69 VAL H H 8.52 0.01 1 182 . 69 VAL CA C 60.584 0.2 1 183 . 69 VAL C C 175.48 0.2 1 184 . 69 VAL CB C 33.984 0.2 1 185 . 69 VAL N N 122.07 0.2 1 186 . 70 GLY H H 8.748 0.01 1 187 . 70 GLY CA C 44.484 0.2 1 188 . 70 GLY C C 175.28 0.2 1 189 . 70 GLY N N 114.584 0.2 1 190 . 71 ARG H H 10.577 0.01 1 191 . 71 ARG CA C 59.884 0.2 1 192 . 71 ARG C C 177.08 0.2 1 193 . 71 ARG CB C 28.884 0.2 1 194 . 71 ARG N N 132.72 0.2 1 195 . 72 MET H H 9.365 0.01 1 196 . 72 MET CA C 57.184 0.2 1 197 . 72 MET C C 177.68 0.2 1 198 . 72 MET CB C 31.284 0.2 1 199 . 72 MET N N 115.781 0.2 1 200 . 73 ALA H H 6.67 0.01 1 201 . 73 ALA CA C 52.784 0.2 1 202 . 73 ALA C C 179.28 0.2 1 203 . 73 ALA CB C 18.284 0.2 1 204 . 73 ALA N N 118.635 0.2 1 205 . 74 LYS H H 8.193 0.01 1 206 . 74 LYS CA C 59.684 0.2 1 207 . 74 LYS C C 177.48 0.2 1 208 . 74 LYS CB C 32.084 0.2 1 209 . 74 LYS N N 123.265 0.2 1 210 . 75 ARG H H 7.871 0.01 1 211 . 75 ARG CA C 57.884 0.2 1 212 . 75 ARG C C 174.28 0.2 1 213 . 75 ARG CB C 29.584 0.2 1 214 . 75 ARG N N 115.429 0.2 1 215 . 76 GLN H H 7.086 0.01 1 216 . 76 GLN CA C 52.984 0.2 1 217 . 76 GLN C C 174.98 0.2 1 218 . 76 GLN CB C 28.784 0.2 1 219 . 76 GLN N N 111.806 0.2 1 220 . 77 ALA H H 7.226 0.01 1 221 . 77 ALA CA C 54.984 0.2 1 222 . 77 ALA C C 179.38 0.2 1 223 . 77 ALA CB C 18.884 0.2 1 224 . 77 ALA N N 124.616 0.2 1 225 . 78 VAL H H 8.811 0.01 1 226 . 78 VAL CA C 63.584 0.2 1 227 . 78 VAL C C 176.38 0.2 1 228 . 78 VAL CB C 31.084 0.2 1 229 . 78 VAL N N 117.142 0.2 1 230 . 79 LEU H H 6.852 0.01 1 231 . 79 LEU CA C 55.484 0.2 1 232 . 79 LEU C C 176.38 0.2 1 233 . 79 LEU CB C 40.784 0.2 1 234 . 79 LEU N N 117.386 0.2 1 235 . 80 ASN H H 7.24 0.01 1 236 . 80 ASN CA C 49.484 0.2 1 237 . 80 ASN C C 174.48 0.2 1 238 . 80 ASN CB C 37.884 0.2 1 239 . 80 ASN N N 115.571 0.2 1 240 . 81 PRO CA C 64.184 0.2 1 241 . 81 PRO C C 178.48 0.2 1 242 . 81 PRO CB C 30.884 0.2 1 243 . 82 GLU H H 8.714 0.01 1 244 . 82 GLU CA C 57.984 0.2 1 245 . 82 GLU C C 176.78 0.2 1 246 . 82 GLU CB C 28.584 0.2 1 247 . 82 GLU N N 115.825 0.2 1 248 . 83 GLY H H 6.966 0.01 1 249 . 83 GLY CA C 44.184 0.2 1 250 . 83 GLY C C 176.88 0.2 1 251 . 83 GLY N N 102.799 0.2 1 252 . 89 LYS CA C 57.784 0.2 1 253 . 89 LYS C C 176.18 0.2 1 254 . 89 LYS CB C 34.384 0.2 1 255 . 90 ARG H H 7.669 0.01 1 256 . 90 ARG CA C 57.784 0.2 1 257 . 90 ARG C C 175.08 0.2 1 258 . 90 ARG CB C 28.784 0.2 1 259 . 90 ARG N N 115.039 0.2 1 260 . 91 PHE H H 8.061 0.01 1 261 . 91 PHE CA C 57.784 0.2 1 262 . 91 PHE C C 175.48 0.2 1 263 . 91 PHE CB C 40.684 0.2 1 264 . 91 PHE N N 113.147 0.2 1 265 . 92 ILE H H 6.865 0.01 1 266 . 92 ILE CA C 61.884 0.2 1 267 . 92 ILE C C 174.78 0.2 1 268 . 92 ILE CB C 38.484 0.2 1 269 . 92 ILE N N 119.716 0.2 1 270 . 93 GLY H H 9.901 0.01 1 271 . 93 GLY CA C 46.184 0.2 1 272 . 93 GLY C C 172.58 0.2 1 273 . 93 GLY N N 115.793 0.2 1 274 . 94 ARG H H 7.295 0.01 1 275 . 94 ARG CA C 53.884 0.2 1 276 . 94 ARG C C 176.08 0.2 1 277 . 94 ARG CB C 31.284 0.2 1 278 . 94 ARG N N 117.537 0.2 1 279 . 95 ARG H H 8.867 0.01 1 280 . 95 ARG CA C 54.984 0.2 1 281 . 95 ARG C C 177.88 0.2 1 282 . 95 ARG CB C 29.784 0.2 1 283 . 95 ARG N N 121.273 0.2 1 284 . 96 PHE H H 8.867 0.01 1 285 . 96 PHE CA C 62.184 0.2 1 286 . 96 PHE C C 176.78 0.2 1 287 . 96 PHE CB C 37.784 0.2 1 288 . 96 PHE N N 125.141 0.2 1 289 . 97 GLU H H 9.062 0.01 1 290 . 97 GLU CA C 58.584 0.2 1 291 . 97 GLU C C 177.18 0.2 1 292 . 97 GLU CB C 28.284 0.2 1 293 . 97 GLU N N 115.538 0.2 1 294 . 98 GLU H H 7.428 0.01 1 295 . 98 GLU CA C 56.884 0.2 1 296 . 98 GLU C C 177.48 0.2 1 297 . 98 GLU CB C 30.484 0.2 1 298 . 98 GLU N N 116.525 0.2 1 299 . 99 VAL H H 7.323 0.01 1 300 . 99 VAL CA C 59.884 0.2 1 301 . 99 VAL C C 175.48 0.2 1 302 . 99 VAL CB C 31.184 0.2 1 303 . 99 VAL N N 110.501 0.2 1 304 . 100 GLN H H 7.231 0.01 1 305 . 100 GLN CA C 59.484 0.2 1 306 . 100 GLN C C 177.38 0.2 1 307 . 100 GLN CB C 27.884 0.2 1 308 . 100 GLN N N 122.924 0.2 1 309 . 101 GLU H H 7.902 0.01 1 310 . 101 GLU CA C 59.484 0.2 1 311 . 101 GLU C C 178.78 0.2 1 312 . 101 GLU CB C 27.884 0.2 1 313 . 101 GLU N N 118.513 0.2 1 314 . 102 GLU H H 7.39 0.01 1 315 . 102 GLU CA C 57.784 0.2 1 316 . 102 GLU C C 178.98 0.2 1 317 . 102 GLU CB C 28.384 0.2 1 318 . 102 GLU N N 121.662 0.2 1 319 . 103 ALA H H 8.456 0.01 1 320 . 103 ALA CA C 54.084 0.2 1 321 . 103 ALA C C 177.58 0.2 1 322 . 103 ALA CB C 16.984 0.2 1 323 . 103 ALA N N 121.018 0.2 1 324 . 104 LYS H H 7.118 0.01 1 325 . 104 LYS CA C 56.784 0.2 1 326 . 104 LYS C C 176.08 0.2 1 327 . 104 LYS CB C 31.684 0.2 1 328 . 104 LYS N N 114.669 0.2 1 329 . 105 ARG H H 7.394 0.01 1 330 . 105 ARG CA C 56.284 0.2 1 331 . 105 ARG C C 176.08 0.2 1 332 . 105 ARG CB C 30.784 0.2 1 333 . 105 ARG N N 117.554 0.2 1 334 . 106 VAL H H 6.986 0.01 1 335 . 106 VAL CA C 57.684 0.2 1 336 . 106 VAL C C 175.28 0.2 1 337 . 106 VAL CB C 31.984 0.2 1 338 . 106 VAL N N 111.889 0.2 1 339 . 108 TYR CA C 53.884 0.2 1 340 . 108 TYR C C 178.18 0.2 1 341 . 108 TYR CB C 37.184 0.2 1 342 . 109 LYS H H 7.84 0.01 1 343 . 109 LYS CA C 57.084 0.2 1 344 . 109 LYS C C 177.08 0.2 1 345 . 109 LYS CB C 31.984 0.2 1 346 . 109 LYS N N 118.156 0.2 1 347 . 110 VAL H H 7.349 0.01 1 348 . 110 VAL CA C 60.884 0.2 1 349 . 110 VAL C C 177.18 0.2 1 350 . 110 VAL CB C 31.984 0.2 1 351 . 110 VAL N N 121.251 0.2 1 352 . 111 VAL H H 7.287 0.01 1 353 . 111 VAL CA C 57.284 0.2 1 354 . 111 VAL C C 176.98 0.2 1 355 . 111 VAL CB C 33.284 0.2 1 356 . 111 VAL N N 119.175 0.2 1 357 . 112 PRO CA C 61.384 0.2 1 358 . 112 PRO C C 177.78 0.2 1 359 . 112 PRO CB C 29.984 0.2 1 360 . 113 GLY H H 8.347 0.01 1 361 . 113 GLY CA C 42.784 0.2 1 362 . 113 GLY C C 173.88 0.2 1 363 . 113 GLY N N 108.345 0.2 1 364 . 115 ASP CA C 52.384 0.2 1 365 . 115 ASP C C 176.38 0.2 1 366 . 115 ASP CB C 40.184 0.2 1 367 . 116 GLY H H 7.946 0.01 1 368 . 116 GLY CA C 45.084 0.2 1 369 . 116 GLY C C 174.68 0.2 1 370 . 116 GLY N N 109.572 0.2 1 371 . 117 GLY H H 8.218 0.01 1 372 . 117 GLY CA C 44.284 0.2 1 373 . 117 GLY C C 172.08 0.2 1 374 . 117 GLY N N 110.125 0.2 1 375 . 118 VAL H H 8.338 0.01 1 376 . 118 VAL CA C 62.484 0.2 1 377 . 118 VAL C C 175.38 0.2 1 378 . 118 VAL CB C 32.884 0.2 1 379 . 118 VAL N N 120.822 0.2 1 380 . 119 ARG H H 9.03 0.01 1 381 . 119 ARG CA C 52.584 0.2 1 382 . 119 ARG C C 173.58 0.2 1 383 . 119 ARG CB C 32.784 0.2 1 384 . 119 ARG N N 125.12 0.2 1 385 . 120 VAL H H 9.063 0.01 1 386 . 120 VAL CA C 59.784 0.2 1 387 . 120 VAL C C 174.08 0.2 1 388 . 120 VAL CB C 32.784 0.2 1 389 . 120 VAL N N 119.899 0.2 1 390 . 121 GLU H H 8.534 0.01 1 391 . 121 GLU CA C 54.084 0.2 1 392 . 121 GLU C C 174.78 0.2 1 393 . 121 GLU CB C 31.184 0.2 1 394 . 121 GLU N N 129.379 0.2 1 395 . 122 VAL H H 8.933 0.01 1 396 . 122 VAL CA C 61.184 0.2 1 397 . 122 VAL C C 174.98 0.2 1 398 . 122 VAL CB C 33.084 0.2 1 399 . 122 VAL N N 127.421 0.2 1 400 . 123 LYS H H 9.316 0.01 1 401 . 123 LYS CA C 56.384 0.2 1 402 . 123 LYS C C 175.78 0.2 1 403 . 123 LYS CB C 29.284 0.2 1 404 . 123 LYS N N 130.127 0.2 1 405 . 124 GLY H H 8.477 0.01 1 406 . 124 GLY CA C 45.084 0.2 1 407 . 124 GLY C C 172.78 0.2 1 408 . 124 GLY N N 105.758 0.2 1 409 . 125 LYS H H 7.696 0.01 1 410 . 125 LYS CA C 54.584 0.2 1 411 . 125 LYS C C 173.48 0.2 1 412 . 125 LYS CB C 33.084 0.2 1 413 . 125 LYS N N 123.569 0.2 1 414 . 126 LEU H H 7.755 0.01 1 415 . 126 LEU CA C 52.984 0.2 1 416 . 126 LEU C C 176.28 0.2 1 417 . 126 LEU CB C 42.984 0.2 1 418 . 126 LEU N N 122.726 0.2 1 419 . 127 TYR H H 9.087 0.01 1 420 . 127 TYR CA C 56.284 0.2 1 421 . 127 TYR C C 175.98 0.2 1 422 . 127 TYR CB C 41.684 0.2 1 423 . 127 TYR N N 121.643 0.2 1 424 . 128 THR H H 9.369 0.01 1 425 . 128 THR CA C 59.384 0.2 1 426 . 128 THR C C 174.48 0.2 1 427 . 128 THR CB C 68.384 0.2 1 428 . 128 THR N N 114.677 0.2 1 429 . 129 PRO CA C 65.284 0.2 1 430 . 129 PRO C C 178.98 0.2 1 431 . 129 PRO CB C 31.184 0.2 1 432 . 130 GLU H H 11.127 0.01 1 433 . 130 GLU CA C 61.184 0.2 1 434 . 130 GLU C C 178.38 0.2 1 435 . 130 GLU CB C 28.084 0.2 1 436 . 130 GLU N N 122.561 0.2 1 437 . 131 GLU H H 8.113 0.01 1 438 . 131 GLU CA C 59.184 0.2 1 439 . 131 GLU C C 178.78 0.2 1 440 . 131 GLU CB C 29.284 0.2 1 441 . 131 GLU N N 122.304 0.2 1 442 . 132 ILE H H 7.806 0.01 1 443 . 132 ILE CA C 62.384 0.2 1 444 . 132 ILE C C 177.98 0.2 1 445 . 132 ILE CB C 35.584 0.2 1 446 . 132 ILE N N 120.121 0.2 1 447 . 133 SER H H 8.427 0.01 1 448 . 133 SER CA C 62.484 0.2 1 449 . 133 SER C C 175.08 0.2 1 450 . 133 SER CB C 62.784 0.2 1 451 . 133 SER N N 116.239 0.2 1 452 . 134 ALA H H 8.529 0.01 1 453 . 134 ALA CA C 54.384 0.2 1 454 . 134 ALA C C 178.48 0.2 1 455 . 134 ALA CB C 18.884 0.2 1 456 . 134 ALA N N 124.288 0.2 1 457 . 135 MET H H 7.598 0.01 1 458 . 135 MET CA C 59.484 0.2 1 459 . 135 MET C C 178.28 0.2 1 460 . 135 MET CB C 31.184 0.2 1 461 . 135 MET N N 118.87 0.2 1 462 . 136 ILE H H 6.989 0.01 1 463 . 136 ILE CA C 64.884 0.2 1 464 . 136 ILE C C 176.58 0.2 1 465 . 136 ILE CB C 37.684 0.2 1 466 . 136 ILE N N 120.737 0.2 1 467 . 137 LEU H H 7.845 0.01 1 468 . 137 LEU CA C 57.784 0.2 1 469 . 137 LEU C C 177.38 0.2 1 470 . 137 LEU CB C 41.684 0.2 1 471 . 137 LEU N N 117.928 0.2 1 472 . 138 ARG H H 8.768 0.01 1 473 . 138 ARG CA C 59.384 0.2 1 474 . 138 ARG C C 177.28 0.2 1 475 . 138 ARG CB C 29.284 0.2 1 476 . 138 ARG N N 118.178 0.2 1 477 . 139 LYS H H 7.079 0.01 1 478 . 139 LYS CA C 59.084 0.2 1 479 . 139 LYS C C 176.98 0.2 1 480 . 139 LYS CB C 30.984 0.2 1 481 . 139 LYS N N 120.827 0.2 1 482 . 140 LEU H H 7.637 0.01 1 483 . 140 LEU CA C 57.784 0.2 1 484 . 140 LEU C C 178.88 0.2 1 485 . 140 LEU CB C 41.384 0.2 1 486 . 140 LEU N N 118.031 0.2 1 487 . 141 VAL H H 8.3 0.01 1 488 . 141 VAL CA C 60.984 0.2 1 489 . 141 VAL C C 178.78 0.2 1 490 . 141 VAL CB C 30.784 0.2 1 491 . 141 VAL N N 116.564 0.2 1 492 . 142 GLU H H 8.996 0.01 1 493 . 142 GLU CA C 58.884 0.2 1 494 . 142 GLU C C 179.28 0.2 1 495 . 142 GLU CB C 28.184 0.2 1 496 . 142 GLU N N 126.65 0.2 1 497 . 143 ASP H H 8.734 0.01 1 498 . 143 ASP CA C 57.384 0.2 1 499 . 143 ASP C C 179.68 0.2 1 500 . 143 ASP CB C 39.084 0.2 1 501 . 143 ASP N N 122.853 0.2 1 502 . 144 ALA H H 8.409 0.01 1 503 . 144 ALA CA C 54.884 0.2 1 504 . 144 ALA C C 178.88 0.2 1 505 . 144 ALA CB C 18.384 0.2 1 506 . 144 ALA N N 124.301 0.2 1 507 . 145 SER H H 8.437 0.01 1 508 . 145 SER CA C 62.184 0.2 1 509 . 145 SER C C 176.58 0.2 1 510 . 145 SER CB C 62.884 0.2 1 511 . 145 SER N N 116.457 0.2 1 512 . 146 LYS H H 7.661 0.01 1 513 . 146 LYS CA C 58.484 0.2 1 514 . 146 LYS C C 178.18 0.2 1 515 . 146 LYS CB C 31.184 0.2 1 516 . 146 LYS N N 123.143 0.2 1 517 . 147 LYS H H 7.366 0.01 1 518 . 147 LYS CA C 57.384 0.2 1 519 . 147 LYS C C 177.88 0.2 1 520 . 147 LYS CB C 31.284 0.2 1 521 . 147 LYS N N 119.476 0.2 1 522 . 148 LEU H H 8.178 0.01 1 523 . 148 LEU CA C 55.184 0.2 1 524 . 148 LEU C C 177.58 0.2 1 525 . 148 LEU CB C 42.084 0.2 1 526 . 148 LEU N N 117.564 0.2 1 527 . 149 GLY H H 7.976 0.01 1 528 . 149 GLY CA C 45.484 0.2 1 529 . 149 GLY C C 172.58 0.2 1 530 . 149 GLY N N 107.916 0.2 1 531 . 150 GLU H H 7.341 0.01 1 532 . 150 GLU CA C 53.884 0.2 1 533 . 150 GLU C C 173.08 0.2 1 534 . 150 GLU CB C 32.384 0.2 1 535 . 150 GLU N N 117.882 0.2 1 536 . 151 LYS H H 8.193 0.01 1 537 . 151 LYS CA C 56.184 0.2 1 538 . 151 LYS C C 175.58 0.2 1 539 . 151 LYS CB C 31.484 0.2 1 540 . 151 LYS N N 121.908 0.2 1 541 . 152 ILE H H 7.956 0.01 1 542 . 152 ILE CA C 60.484 0.2 1 543 . 152 ILE C C 174.98 0.2 1 544 . 152 ILE CB C 37.484 0.2 1 545 . 152 ILE N N 128.895 0.2 1 546 . 153 THR H H 8.459 0.01 1 547 . 153 THR CA C 61.884 0.2 1 548 . 153 THR C C 173.48 0.2 1 549 . 153 THR CB C 70.084 0.2 1 550 . 153 THR N N 115.199 0.2 1 551 . 154 LYS H H 7.68 0.01 1 552 . 154 LYS CA C 55.084 0.2 1 553 . 154 LYS C C 174.68 0.2 1 554 . 154 LYS CB C 35.684 0.2 1 555 . 154 LYS N N 122.979 0.2 1 556 . 155 ALA H H 8.345 0.01 1 557 . 155 ALA CA C 50.884 0.2 1 558 . 155 ALA C C 175.98 0.2 1 559 . 155 ALA CB C 23.684 0.2 1 560 . 155 ALA N N 120.5 0.2 1 561 . 156 VAL H H 8.439 0.01 1 562 . 156 VAL CA C 61.584 0.2 1 563 . 156 VAL C C 173.78 0.2 1 564 . 156 VAL CB C 32.784 0.2 1 565 . 156 VAL N N 122.426 0.2 1 566 . 157 ILE H H 7.333 0.01 1 567 . 157 ILE CA C 58.984 0.2 1 568 . 157 ILE C C 173.78 0.2 1 569 . 157 ILE CB C 40.484 0.2 1 570 . 157 ILE N N 126.354 0.2 1 571 . 158 THR H H 7.921 0.01 1 572 . 158 THR CA C 59.584 0.2 1 573 . 158 THR C C 173.58 0.2 1 574 . 158 THR CB C 69.184 0.2 1 575 . 158 THR N N 116.829 0.2 1 576 . 159 VAL H H 7.944 0.01 1 577 . 159 VAL CA C 57.484 0.2 1 578 . 159 VAL C C 172.98 0.2 1 579 . 159 VAL CB C 32.784 0.2 1 580 . 159 VAL N N 109.359 0.2 1 581 . 160 PRO CA C 62.384 0.2 1 582 . 161 ALA H H 10.295 0.01 1 583 . 161 ALA CA C 54.184 0.2 1 584 . 161 ALA C C 178.78 0.2 1 585 . 161 ALA CB C 17.984 0.2 1 586 . 161 ALA N N 124.767 0.2 1 587 . 162 TYR H H 10.071 0.01 1 588 . 162 TYR CA C 57.784 0.2 1 589 . 162 TYR C C 175.18 0.2 1 590 . 162 TYR N N 118.757 0.2 1 591 . 163 PHE H H 8.023 0.01 1 592 . 163 PHE CA C 59.084 0.2 1 593 . 163 PHE C C 172.48 0.2 1 594 . 163 PHE CB C 37.684 0.2 1 595 . 163 PHE N N 120.02 0.2 1 596 . 164 ASN H H 6.963 0.01 1 597 . 164 ASN CA C 57.884 0.2 1 598 . 164 ASN C C 175.38 0.2 1 599 . 164 ASN CB C 36.284 0.2 1 600 . 164 ASN N N 109.423 0.2 1 601 . 165 ASN CA C 57.284 0.2 1 602 . 165 ASN C C 176.38 0.2 1 603 . 165 ASN CB C 37.184 0.2 1 604 . 166 ALA H H 8.029 0.01 1 605 . 166 ALA CA C 54.884 0.2 1 606 . 166 ALA C C 180.98 0.2 1 607 . 166 ALA CB C 16.884 0.2 1 608 . 166 ALA N N 124.636 0.2 1 609 . 167 GLN H H 8.447 0.01 1 610 . 167 GLN CA C 59.084 0.2 1 611 . 167 GLN C C 178.9 0.2 1 612 . 167 GLN CB C 28.584 0.2 1 613 . 167 GLN N N 120.009 0.2 1 614 . 168 ARG H H 8.424 0.01 1 615 . 168 ARG CA C 60.584 0.2 1 616 . 168 ARG C C 177.28 0.2 1 617 . 168 ARG CB C 28.784 0.2 1 618 . 168 ARG N N 123.269 0.2 1 619 . 169 GLU H H 8.669 0.01 1 620 . 169 GLU CA C 58.584 0.2 1 621 . 169 GLU C C 178.38 0.2 1 622 . 169 GLU CB C 28.184 0.2 1 623 . 169 GLU N N 121.841 0.2 1 624 . 170 ALA H H 8.143 0.01 1 625 . 170 ALA CA C 54.684 0.2 1 626 . 170 ALA C C 178.38 0.2 1 627 . 170 ALA CB C 18.984 0.2 1 628 . 170 ALA N N 122.023 0.2 1 629 . 171 THR H H 7.518 0.01 1 630 . 171 THR CA C 64.684 0.2 1 631 . 171 THR C C 180.18 0.2 1 632 . 171 THR CB C 67.884 0.2 1 633 . 171 THR N N 116.747 0.2 1 634 . 172 ALA H H 8.182 0.01 1 635 . 172 ALA CA C 55.284 0.2 1 636 . 172 ALA C C 179.58 0.2 1 637 . 172 ALA CB C 16.184 0.2 1 638 . 172 ALA N N 125.056 0.2 1 639 . 173 ASN H H 8.749 0.01 1 640 . 173 ASN CA C 55.684 0.2 1 641 . 173 ASN C C 176.98 0.2 1 642 . 173 ASN CB C 36.884 0.2 1 643 . 173 ASN N N 119.192 0.2 1 644 . 174 ALA H H 8.166 0.01 1 645 . 174 ALA CA C 54.884 0.2 1 646 . 174 ALA C C 178.48 0.2 1 647 . 174 ALA CB C 17.784 0.2 1 648 . 174 ALA N N 124.239 0.2 1 649 . 175 GLY H H 7.611 0.01 1 650 . 175 GLY CA C 47.084 0.2 1 651 . 175 GLY C C 173.58 0.2 1 652 . 175 GLY N N 104.055 0.2 1 653 . 176 ARG H H 8.141 0.01 1 654 . 176 ARG CA C 59.284 0.2 1 655 . 176 ARG C C 181.18 0.2 1 656 . 176 ARG CB C 28.984 0.2 1 657 . 176 ARG N N 124.311 0.2 1 658 . 177 ILE H H 8.809 0.01 1 659 . 177 ILE CA C 64.984 0.2 1 660 . 177 ILE C C 177.28 0.2 1 661 . 177 ILE CB C 37.284 0.2 1 662 . 177 ILE N N 124.736 0.2 1 663 . 178 ALA H H 7.546 0.01 1 664 . 178 ALA CA C 52.284 0.2 1 665 . 178 ALA C C 174.08 0.2 1 666 . 178 ALA CB C 18.484 0.2 1 667 . 178 ALA N N 121.781 0.2 1 668 . 179 GLY H H 7.762 0.01 1 669 . 179 GLY CA C 44.784 0.2 1 670 . 179 GLY C C 173.98 0.2 1 671 . 179 GLY N N 106.097 0.2 1 672 . 180 LEU H H 8.053 0.01 1 673 . 180 LEU CA C 52.884 0.2 1 674 . 180 LEU C C 175.88 0.2 1 675 . 180 LEU CB C 42.284 0.2 1 676 . 180 LEU N N 120.794 0.2 1 677 . 181 GLU H H 8.57 0.01 1 678 . 181 GLU CA C 55.284 0.2 1 679 . 181 GLU C C 174.68 0.2 1 680 . 181 GLU CB C 28.884 0.2 1 681 . 181 GLU N N 123.295 0.2 1 682 . 182 VAL H H 8.245 0.01 1 683 . 182 VAL CA C 61.384 0.2 1 684 . 182 VAL C C 175.68 0.2 1 685 . 182 VAL CB C 29.684 0.2 1 686 . 182 VAL N N 128.996 0.2 1 687 . 183 LEU H H 8.897 0.01 1 688 . 183 LEU CA C 56.384 0.2 1 689 . 183 LEU C C 176.78 0.2 1 690 . 183 LEU CB C 42.284 0.2 1 691 . 183 LEU N N 130.485 0.2 1 692 . 184 ARG H H 7.017 0.01 1 693 . 184 ARG CA C 54.584 0.2 1 694 . 184 ARG C C 172.48 0.2 1 695 . 184 ARG CB C 33.284 0.2 1 696 . 184 ARG N N 113.853 0.2 1 697 . 185 ILE H H 8.117 0.01 1 698 . 185 ILE C C 176.48 0.2 1 699 . 185 ILE CB C 36.284 0.2 1 700 . 185 ILE N N 125.663 0.2 1 701 . 186 ILE H H 7.693 0.01 1 702 . 186 ILE CA C 57.584 0.2 1 703 . 186 ILE C C 173.48 0.2 1 704 . 186 ILE CB C 40.384 0.2 1 705 . 186 ILE N N 120.06 0.2 1 706 . 187 ASN H H 8.369 0.01 1 707 . 187 ASN CA C 51.384 0.2 1 708 . 187 ASN C C 176.58 0.2 1 709 . 187 ASN CB C 38.084 0.2 1 710 . 187 ASN N N 118.531 0.2 1 711 . 188 GLU H H 8.965 0.01 1 712 . 188 GLU CA C 60.884 0.2 1 713 . 188 GLU C C 174.98 0.2 1 714 . 188 GLU CB C 27.884 0.2 1 715 . 188 GLU N N 123.523 0.2 1 716 . 189 PRO C C 173.18 0.2 1 717 . 190 THR H H 6.611 0.01 1 718 . 190 THR CA C 60.984 0.2 1 719 . 190 THR C C 174.48 0.2 1 720 . 190 THR CB C 66.884 0.2 1 721 . 190 THR N N 115.355 0.2 1 722 . 191 ALA H H 7.867 0.01 1 723 . 191 ALA CA C 54.884 0.2 1 724 . 191 ALA C C 178.68 0.2 1 725 . 191 ALA CB C 17.884 0.2 1 726 . 191 ALA N N 124.586 0.2 1 727 . 192 ALA H H 8.148 0.01 1 728 . 192 ALA CA C 54.384 0.2 1 729 . 192 ALA C C 177.68 0.2 1 730 . 192 ALA CB C 17.184 0.2 1 731 . 192 ALA N N 119.298 0.2 1 732 . 193 ALA H H 7.688 0.01 1 733 . 193 ALA CA C 54.884 0.2 1 734 . 193 ALA C C 178.78 0.2 1 735 . 193 ALA CB C 17.284 0.2 1 736 . 193 ALA N N 119.482 0.2 1 737 . 194 LEU H H 8.13 0.01 1 738 . 194 LEU CA C 57.584 0.2 1 739 . 194 LEU C C 176.38 0.2 1 740 . 194 LEU CB C 40.784 0.2 1 741 . 194 LEU N N 119.752 0.2 1 742 . 195 ALA H H 7.884 0.01 1 743 . 195 ALA CA C 54.684 0.2 1 744 . 195 ALA C C 178.38 0.2 1 745 . 195 ALA CB C 18.684 0.2 1 746 . 195 ALA N N 123.697 0.2 1 747 . 196 TYR H H 7.47 0.01 1 748 . 196 TYR CA C 59.984 0.2 1 749 . 196 TYR C C 175.28 0.2 1 750 . 196 TYR CB C 38.584 0.2 1 751 . 196 TYR N N 115.511 0.2 1 752 . 197 GLY H H 7.987 0.01 1 753 . 197 GLY CA C 45.784 0.2 1 754 . 197 GLY C C 176.78 0.2 1 755 . 197 GLY N N 109.927 0.2 1 756 . 198 LEU H H 8.036 0.01 1 757 . 198 LEU CA C 56.484 0.2 1 758 . 198 LEU C C 176.58 0.2 1 759 . 198 LEU CB C 39.584 0.2 1 760 . 198 LEU N N 118.005 0.2 1 761 . 199 ASP H H 9.757 0.01 1 762 . 199 ASP CA C 54.784 0.2 1 763 . 199 ASP C C 175.88 0.2 1 764 . 199 ASP CB C 38.184 0.2 1 765 . 199 ASP N N 115.449 0.2 1 766 . 200 LYS H H 7.165 0.01 1 767 . 200 LYS CA C 55.184 0.2 1 768 . 200 LYS C C 176.28 0.2 1 769 . 200 LYS CB C 31.284 0.2 1 770 . 200 LYS N N 118.454 0.2 1 771 . 201 LYS H H 7.2 0.01 1 772 . 201 LYS CA C 55.884 0.2 1 773 . 201 LYS C C 175.48 0.2 1 774 . 201 LYS CB C 31.884 0.2 1 775 . 201 LYS N N 120.314 0.2 1 776 . 202 GLY H H 7.709 0.01 1 777 . 202 GLY CA C 44.584 0.2 1 778 . 202 GLY C C 172.28 0.2 1 779 . 202 GLY N N 107.912 0.2 1 780 . 203 ASN H H 7.96 0.01 1 781 . 203 ASN CA C 53.084 0.2 1 782 . 203 ASN C C 174.58 0.2 1 783 . 203 ASN CB C 38.184 0.2 1 784 . 203 ASN N N 119.743 0.2 1 785 . 204 GLU H H 8.222 0.01 1 786 . 204 GLU CA C 55.084 0.2 1 787 . 204 GLU C C 173.68 0.2 1 788 . 204 GLU CB C 32.084 0.2 1 789 . 204 GLU N N 120.513 0.2 1 790 . 205 THR H H 9.672 0.01 1 791 . 205 THR CA C 61.884 0.2 1 792 . 205 THR C C 173.78 0.2 1 793 . 205 THR CB C 68.684 0.2 1 794 . 205 THR N N 120.196 0.2 1 795 . 206 VAL H H 9.211 0.01 1 796 . 206 VAL CA C 58.784 0.2 1 797 . 206 VAL C C 172.88 0.2 1 798 . 206 VAL CB C 34.984 0.2 1 799 . 206 VAL N N 125.674 0.2 1 800 . 207 LEU H H 8.397 0.01 1 801 . 207 LEU CA C 54.084 0.2 1 802 . 207 LEU C C 173.38 0.2 1 803 . 207 LEU CB C 44.284 0.2 1 804 . 207 LEU N N 128.231 0.2 1 805 . 208 VAL H H 9.61 0.01 1 806 . 208 VAL CA C 61.684 0.2 1 807 . 208 VAL C C 172.68 0.2 1 808 . 208 VAL CB C 30.484 0.2 1 809 . 208 VAL N N 129.758 0.2 1 810 . 209 PHE H H 8.741 0.01 1 811 . 209 PHE CA C 57.084 0.2 1 812 . 209 PHE C C 171.58 0.2 1 813 . 209 PHE CB C 39.984 0.2 1 814 . 209 PHE N N 134.32 0.2 1 815 . 210 ASP H H 8.372 0.01 1 816 . 210 ASP CA C 51.284 0.2 1 817 . 210 ASP C C 175.18 0.2 1 818 . 210 ASP CB C 42.584 0.2 1 819 . 210 ASP N N 129.609 0.2 1 820 . 211 LEU H H 8.299 0.01 1 821 . 211 LEU CA C 53.584 0.2 1 822 . 211 LEU C C 177.38 0.2 1 823 . 211 LEU N N 127.894 0.2 1 824 . 212 GLY H H 8.283 0.01 1 825 . 212 GLY CA C 46.584 0.2 1 826 . 212 GLY C C 175.78 0.2 1 827 . 212 GLY N N 107.529 0.2 1 828 . 213 GLY CA C 44.984 0.2 1 829 . 213 GLY C C 175.48 0.2 1 830 . 214 GLY H H 8.684 0.01 1 831 . 214 GLY CA C 44.584 0.2 1 832 . 214 GLY C C 172.38 0.2 1 833 . 214 GLY N N 114.43 0.2 1 834 . 215 THR H H 6.903 0.01 1 835 . 215 THR CA C 62.484 0.2 1 836 . 215 THR C C 171.78 0.2 1 837 . 215 THR CB C 67.884 0.2 1 838 . 215 THR N N 116.443 0.2 1 839 . 216 PHE H H 9.586 0.01 1 840 . 216 PHE CA C 59.184 0.2 1 841 . 216 PHE C C 173.18 0.2 1 842 . 216 PHE CB C 34.884 0.2 1 843 . 216 PHE N N 128.728 0.2 1 844 . 217 ASP H H 6.498 0.01 1 845 . 217 ASP CA C 53.584 0.2 1 846 . 217 ASP C C 172.48 0.2 1 847 . 217 ASP CB C 41.284 0.2 1 848 . 217 ASP N N 124.089 0.2 1 849 . 218 VAL H H 8.374 0.01 1 850 . 218 VAL CA C 59.884 0.2 1 851 . 218 VAL C C 174.08 0.2 1 852 . 218 VAL CB C 31.984 0.2 1 853 . 218 VAL N N 124.373 0.2 1 854 . 219 THR H H 8.199 0.01 1 855 . 219 THR CA C 61.484 0.2 1 856 . 219 THR C C 172.98 0.2 1 857 . 219 THR CB C 70.584 0.2 1 858 . 219 THR N N 122.174 0.2 1 859 . 220 ILE H H 8.692 0.01 1 860 . 220 ILE CA C 59.484 0.2 1 861 . 220 ILE C C 173.88 0.2 1 862 . 220 ILE CB C 36.884 0.2 1 863 . 220 ILE N N 127.454 0.2 1 864 . 221 LEU H H 9.338 0.01 1 865 . 221 LEU CA C 52.584 0.2 1 866 . 221 LEU C C 174.38 0.2 1 867 . 221 LEU CB C 45.284 0.2 1 868 . 221 LEU N N 130.22 0.2 1 869 . 222 GLU H H 9.144 0.01 1 870 . 222 GLU CA C 55.284 0.2 1 871 . 222 GLU C C 174.68 0.2 1 872 . 222 GLU CB C 31.184 0.2 1 873 . 222 GLU N N 125.237 0.2 1 874 . 223 ILE H H 8.902 0.01 1 875 . 223 ILE CA C 59.584 0.2 1 876 . 223 ILE C C 175.08 0.2 1 877 . 223 ILE CB C 37.784 0.2 1 878 . 223 ILE N N 128.154 0.2 1 879 . 224 GLY H H 8.141 0.01 1 880 . 224 GLY CA C 44.584 0.2 1 881 . 224 GLY C C 174.08 0.2 1 882 . 224 GLY N N 115.367 0.2 1 883 . 225 GLU H H 8.72 0.01 1 884 . 225 GLU CA C 56.484 0.2 1 885 . 225 GLU C C 175.88 0.2 1 886 . 225 GLU CB C 26.984 0.2 1 887 . 225 GLU N N 124.424 0.2 1 888 . 226 GLY H H 8.313 0.01 1 889 . 226 GLY CA C 45.084 0.2 1 890 . 226 GLY C C 172.68 0.2 1 891 . 226 GLY N N 109.632 0.2 1 892 . 227 VAL H H 7.339 0.01 1 893 . 227 VAL CA C 60.484 0.2 1 894 . 227 VAL C C 174.78 0.2 1 895 . 227 VAL CB C 33.484 0.2 1 896 . 227 VAL N N 119.428 0.2 1 897 . 228 PHE H H 8.291 0.01 1 898 . 228 PHE CA C 55.584 0.2 1 899 . 228 PHE C C 174.48 0.2 1 900 . 228 PHE CB C 39.584 0.2 1 901 . 228 PHE N N 124.628 0.2 1 902 . 229 GLU H H 8.788 0.01 1 903 . 229 GLU CA C 54.784 0.2 1 904 . 229 GLU C C 175.18 0.2 1 905 . 229 GLU CB C 31.684 0.2 1 906 . 229 GLU N N 125.086 0.2 1 907 . 230 VAL H H 8.752 0.01 1 908 . 230 VAL CA C 62.984 0.2 1 909 . 230 VAL C C 175.38 0.2 1 910 . 230 VAL CB C 30.684 0.2 1 911 . 230 VAL N N 127.955 0.2 1 912 . 231 LYS H H 9.042 0.01 1 913 . 231 LYS CA C 55.084 0.2 1 914 . 231 LYS C C 176.08 0.2 1 915 . 231 LYS CB C 31.784 0.2 1 916 . 231 LYS N N 129.147 0.2 1 917 . 232 ALA H H 7.412 0.01 1 918 . 232 ALA CA C 52.284 0.2 1 919 . 232 ALA C C 175.18 0.2 1 920 . 232 ALA CB C 23.084 0.2 1 921 . 232 ALA N N 117.462 0.2 1 922 . 233 THR H H 8.296 0.01 1 923 . 233 THR CA C 59.184 0.2 1 924 . 233 THR C C 172.68 0.2 1 925 . 233 THR CB C 71.284 0.2 1 926 . 233 THR N N 112.29 0.2 1 927 . 234 SER H H 8.926 0.01 1 928 . 234 SER CA C 56.884 0.2 1 929 . 234 SER C C 173.88 0.2 1 930 . 234 SER CB C 64.684 0.2 1 931 . 234 SER N N 117.469 0.2 1 932 . 235 GLY H H 8.244 0.01 1 933 . 235 GLY CA C 45.984 0.2 1 934 . 235 GLY C C 170.08 0.2 1 935 . 235 GLY N N 110.113 0.2 1 936 . 236 ASP H H 8.967 0.01 1 937 . 236 ASP CA C 53.384 0.2 1 938 . 236 ASP C C 175.78 0.2 1 939 . 236 ASP CB C 43.984 0.2 1 940 . 236 ASP N N 120.342 0.2 1 941 . 237 THR H H 8.172 0.01 1 942 . 237 THR CA C 62.384 0.2 1 943 . 237 THR C C 173.18 0.2 1 944 . 237 THR CB C 69.284 0.2 1 945 . 237 THR N N 121.605 0.2 1 946 . 238 HIS H H 8.965 0.01 1 947 . 238 HIS CA C 54.084 0.2 1 948 . 238 HIS C C 171.68 0.2 1 949 . 238 HIS CB C 27.884 0.2 1 950 . 238 HIS N N 123.327 0.2 1 951 . 239 LEU H H 6.697 0.01 1 952 . 239 LEU CA C 54.584 0.2 1 953 . 239 LEU C C 171.78 0.2 1 954 . 239 LEU CB C 42.784 0.2 1 955 . 239 LEU N N 126.105 0.2 1 956 . 240 GLY H H 8.436 0.01 1 957 . 240 GLY CA C 44.284 0.2 1 958 . 240 GLY C C 174.58 0.2 1 959 . 240 GLY N N 107.799 0.2 1 960 . 241 GLY H H 10.173 0.01 1 961 . 241 GLY CA C 47.884 0.2 1 962 . 241 GLY N N 107.893 0.2 1 963 . 242 SER C C 176.18 0.2 1 964 . 243 ASP H H 7.709 0.01 1 965 . 243 ASP CA C 57.584 0.2 1 966 . 243 ASP C C 179.08 0.2 1 967 . 243 ASP CB C 41.284 0.2 1 968 . 243 ASP N N 121.82 0.2 1 969 . 244 MET H H 7.399 0.01 1 970 . 244 MET CA C 58.584 0.2 1 971 . 244 MET C C 176.18 0.2 1 972 . 244 MET CB C 31.084 0.2 1 973 . 244 MET N N 119.302 0.2 1 974 . 245 ASP H H 7.416 0.01 1 975 . 245 ASP CA C 57.384 0.2 1 976 . 245 ASP C C 178.68 0.2 1 977 . 245 ASP CB C 38.784 0.2 1 978 . 245 ASP N N 121.734 0.2 1 979 . 246 HIS H H 7.925 0.01 1 980 . 246 HIS CA C 59.384 0.2 1 981 . 246 HIS C C 176.58 0.2 1 982 . 246 HIS CB C 29.984 0.2 1 983 . 246 HIS N N 118.518 0.2 1 984 . 247 ALA H H 7.668 0.01 1 985 . 247 ALA CA C 54.784 0.2 1 986 . 247 ALA C C 180.28 0.2 1 987 . 247 ALA CB C 16.884 0.2 1 988 . 247 ALA N N 123.485 0.2 1 989 . 248 ILE H H 7.468 0.01 1 990 . 248 ILE CA C 65.384 0.2 1 991 . 248 ILE C C 177.28 0.2 1 992 . 248 ILE CB C 37.384 0.2 1 993 . 248 ILE N N 119.065 0.2 1 994 . 249 VAL H H 8.488 0.01 1 995 . 249 VAL CA C 67.584 0.2 1 996 . 249 VAL C C 176.48 0.2 1 997 . 249 VAL CB C 30.984 0.2 1 998 . 249 VAL N N 121.651 0.2 1 999 . 250 ASN H H 8.699 0.01 1 1000 . 250 ASN CA C 55.984 0.2 1 1001 . 250 ASN C C 177.08 0.2 1 1002 . 250 ASN CB C 37.184 0.2 1 1003 . 250 ASN N N 117.823 0.2 1 1004 . 251 TRP H H 7.664 0.01 1 1005 . 251 TRP CA C 60.984 0.2 1 1006 . 251 TRP C C 176.68 0.2 1 1007 . 251 TRP CB C 27.984 0.2 1 1008 . 251 TRP N N 124.075 0.2 1 1009 . 252 LEU H H 8.654 0.01 1 1010 . 252 LEU CA C 57.184 0.2 1 1011 . 252 LEU C C 179.08 0.2 1 1012 . 252 LEU CB C 41.984 0.2 1 1013 . 252 LEU N N 119.72 0.2 1 1014 . 253 ALA H H 8.85 0.01 1 1015 . 253 ALA CA C 54.284 0.2 1 1016 . 253 ALA C C 180.38 0.2 1 1017 . 253 ALA CB C 16.984 0.2 1 1018 . 253 ALA N N 119.769 0.2 1 1019 . 254 GLU H H 8.446 0.01 1 1020 . 254 GLU CA C 58.984 0.2 1 1021 . 254 GLU C C 178.98 0.2 1 1022 . 254 GLU CB C 28.184 0.2 1 1023 . 254 GLU N N 123.414 0.2 1 1024 . 255 GLU H H 8.196 0.01 1 1025 . 255 GLU CA C 59.184 0.2 1 1026 . 255 GLU C C 178.18 0.2 1 1027 . 255 GLU CB C 28.184 0.2 1 1028 . 255 GLU N N 120.479 0.2 1 1029 . 256 PHE H H 8.325 0.01 1 1030 . 256 PHE CA C 61.084 0.2 1 1031 . 256 PHE C C 177.48 0.2 1 1032 . 256 PHE CB C 38.684 0.2 1 1033 . 256 PHE N N 122.28 0.2 1 1034 . 257 LYS H H 8.068 0.01 1 1035 . 257 LYS CA C 59.284 0.2 1 1036 . 257 LYS C C 173.08 0.2 1 1037 . 257 LYS CB C 31.784 0.2 1 1038 . 257 LYS N N 121.159 0.2 1 1039 . 258 LYS H H 7.867 0.01 1 1040 . 258 LYS CA C 59.284 0.2 1 1041 . 258 LYS C C 177.38 0.2 1 1042 . 258 LYS CB C 31.584 0.2 1 1043 . 258 LYS N N 121.625 0.2 1 1044 . 259 GLU H H 7.444 0.01 1 1045 . 259 GLU CA C 57.984 0.2 1 1046 . 259 GLU C C 177.18 0.2 1 1047 . 259 GLU CB C 29.784 0.2 1 1048 . 259 GLU N N 116.54 0.2 1 1049 . 260 HIS H H 7.894 0.01 1 1050 . 260 HIS CA C 55.184 0.2 1 1051 . 260 HIS C C 175.78 0.2 1 1052 . 260 HIS CB C 31.584 0.2 1 1053 . 260 HIS N N 113.358 0.2 1 1054 . 261 GLY H H 8.406 0.01 1 1055 . 261 GLY CA C 45.984 0.2 1 1056 . 261 GLY C C 172.78 0.2 1 1057 . 261 GLY N N 109.605 0.2 1 1058 . 262 VAL H H 6.369 0.01 1 1059 . 262 VAL CA C 60.284 0.2 1 1060 . 262 VAL C C 174.28 0.2 1 1061 . 262 VAL CB C 34.384 0.2 1 1062 . 262 VAL N N 117.768 0.2 1 1063 . 263 ASP H H 8.756 0.01 1 1064 . 263 ASP CA C 51.584 0.2 1 1065 . 263 ASP C C 173.88 0.2 1 1066 . 263 ASP CB C 40.184 0.2 1 1067 . 263 ASP N N 127.67 0.2 1 1068 . 264 LEU H H 9.34 0.01 1 1069 . 264 LEU CA C 57.284 0.2 1 1070 . 264 LEU C C 173.88 0.2 1 1071 . 264 LEU CB C 42.784 0.2 1 1072 . 264 LEU N N 127.797 0.2 1 1073 . 265 LYS H H 7.77 0.01 1 1074 . 265 LYS CA C 57.884 0.2 1 1075 . 265 LYS C C 175.88 0.2 1 1076 . 265 LYS CB C 29.484 0.2 1 1077 . 265 LYS N N 112.117 0.2 1 1078 . 266 ALA H H 6.898 0.01 1 1079 . 266 ALA CA C 51.084 0.2 1 1080 . 266 ALA C C 177.18 0.2 1 1081 . 266 ALA CB C 18.084 0.2 1 1082 . 266 ALA N N 119.413 0.2 1 1083 . 267 ASP H H 7.079 0.01 1 1084 . 267 ASP CA C 51.984 0.2 1 1085 . 267 ASP C C 174.88 0.2 1 1086 . 267 ASP CB C 41.984 0.2 1 1087 . 267 ASP N N 121.048 0.2 1 1088 . 268 ARG H H 8.592 0.01 1 1089 . 268 ARG CA C 59.484 0.2 1 1090 . 268 ARG C C 176.98 0.2 1 1091 . 268 ARG CB C 29.484 0.2 1 1092 . 268 ARG N N 125.252 0.2 1 1093 . 269 GLN H H 7.893 0.01 1 1094 . 269 GLN CA C 58.584 0.2 1 1095 . 269 GLN C C 178.08 0.2 1 1096 . 269 GLN CB C 27.084 0.2 1 1097 . 269 GLN N N 117.221 0.2 1 1098 . 270 ALA H H 7.579 0.01 1 1099 . 270 ALA CA C 54.484 0.2 1 1100 . 270 ALA C C 179.28 0.2 1 1101 . 270 ALA N N 124.143 0.2 1 1102 . 271 LEU H H 8.777 0.01 1 1103 . 271 LEU CA C 57.584 0.2 1 1104 . 271 LEU C C 177.48 0.2 1 1105 . 271 LEU CB C 40.084 0.2 1 1106 . 271 LEU N N 120.528 0.2 1 1107 . 272 GLN H H 8.1 0.01 1 1108 . 272 GLN CA C 58.284 0.2 1 1109 . 272 GLN C C 177.78 0.2 1 1110 . 272 GLN CB C 28.284 0.2 1 1111 . 272 GLN N N 119.328 0.2 1 1112 . 273 ARG H H 7.284 0.01 1 1113 . 273 ARG CA C 58.884 0.2 1 1114 . 273 ARG C C 179.28 0.2 1 1115 . 273 ARG CB C 30.184 0.2 1 1116 . 273 ARG N N 117.791 0.2 1 1117 . 274 LEU H H 8.787 0.01 1 1118 . 274 LEU CA C 57.684 0.2 1 1119 . 274 LEU C C 180.98 0.2 1 1120 . 274 LEU CB C 40.884 0.2 1 1121 . 274 LEU N N 122.69 0.2 1 1122 . 275 ILE H H 8.454 0.01 1 1123 . 275 ILE CA C 64.184 0.2 1 1124 . 275 ILE C C 177.58 0.2 1 1125 . 275 ILE CB C 37.384 0.2 1 1126 . 275 ILE N N 120.744 0.2 1 1127 . 276 GLU H H 7.208 0.01 1 1128 . 276 GLU CA C 58.884 0.2 1 1129 . 276 GLU C C 178.28 0.2 1 1130 . 276 GLU CB C 29.484 0.2 1 1131 . 276 GLU N N 122.17 0.2 1 1132 . 277 ALA H H 8.069 0.01 1 1133 . 277 ALA CA C 53.984 0.2 1 1134 . 277 ALA C C 179.88 0.2 1 1135 . 277 ALA CB C 18.184 0.2 1 1136 . 277 ALA N N 121.983 0.2 1 1137 . 278 ALA H H 8.858 0.01 1 1138 . 278 ALA CA C 55.084 0.2 1 1139 . 278 ALA C C 177.28 0.2 1 1140 . 278 ALA CB C 19.184 0.2 1 1141 . 278 ALA N N 123.046 0.2 1 1142 . 279 GLU H H 7.373 0.01 1 1143 . 279 GLU CA C 58.884 0.2 1 1144 . 279 GLU C C 172.58 0.2 1 1145 . 279 GLU CB C 27.884 0.2 1 1146 . 279 GLU N N 118.392 0.2 1 1147 . 280 LYS H H 7.301 0.01 1 1148 . 280 LYS CA C 59.084 0.2 1 1149 . 280 LYS C C 177.78 0.2 1 1150 . 280 LYS CB C 31.584 0.2 1 1151 . 280 LYS N N 118.148 0.2 1 1152 . 281 ALA H H 7.986 0.01 1 1153 . 281 ALA CA C 53.884 0.2 1 1154 . 281 ALA C C 178.18 0.2 1 1155 . 281 ALA CB C 17.384 0.2 1 1156 . 281 ALA N N 122.56 0.2 1 1157 . 282 LYS H H 7.898 0.01 1 1158 . 282 LYS CA C 59.084 0.2 1 1159 . 282 LYS C C 177.68 0.2 1 1160 . 282 LYS CB C 33.784 0.2 1 1161 . 282 LYS N N 118.337 0.2 1 1162 . 283 ILE H H 7.682 0.01 1 1163 . 283 ILE CA C 64.984 0.2 1 1164 . 283 ILE C C 180.18 0.2 1 1165 . 283 ILE CB C 36.284 0.2 1 1166 . 283 ILE N N 119.739 0.2 1 1167 . 284 GLU H H 8.175 0.01 1 1168 . 284 GLU CA C 59.984 0.2 1 1169 . 284 GLU C C 179.28 0.2 1 1170 . 284 GLU CB C 27.984 0.2 1 1171 . 284 GLU N N 124.704 0.2 1 1172 . 285 LEU H H 7.8 0.01 1 1173 . 285 LEU CA C 55.484 0.2 1 1174 . 285 LEU C C 178.58 0.2 1 1175 . 285 LEU CB C 40.484 0.2 1 1176 . 285 LEU N N 119.009 0.2 1 1177 . 286 SER H H 7.954 0.01 1 1178 . 286 SER CA C 60.584 0.2 1 1179 . 286 SER C C 173.18 0.2 1 1180 . 286 SER CB C 61.484 0.2 1 1181 . 286 SER N N 120.324 0.2 1 1182 . 287 SER H H 8.107 0.01 1 1183 . 287 SER CA C 58.784 0.2 1 1184 . 287 SER C C 172.78 0.2 1 1185 . 287 SER CB C 64.484 0.2 1 1186 . 287 SER N N 114.114 0.2 1 1187 . 288 THR H H 8.008 0.01 1 1188 . 288 THR CA C 60.084 0.2 1 1189 . 288 THR C C 172.88 0.2 1 1190 . 288 THR CB C 70.584 0.2 1 1191 . 288 THR N N 116.408 0.2 1 1192 . 289 LEU H H 8.08 0.01 1 1193 . 289 LEU CA C 55.284 0.2 1 1194 . 289 LEU C C 176.78 0.2 1 1195 . 289 LEU CB C 41.784 0.2 1 1196 . 289 LEU N N 118.973 0.2 1 1197 . 290 GLU H H 7.561 0.01 1 1198 . 290 GLU CA C 55.084 0.2 1 1199 . 290 GLU C C 172.28 0.2 1 1200 . 290 GLU CB C 32.084 0.2 1 1201 . 290 GLU N N 117.907 0.2 1 1202 . 291 THR H H 8.401 0.01 1 1203 . 291 THR CA C 59.884 0.2 1 1204 . 291 THR C C 170.78 0.2 1 1205 . 291 THR CB C 69.384 0.2 1 1206 . 291 THR N N 118.486 0.2 1 1207 . 292 THR H H 8.091 0.01 1 1208 . 292 THR CA C 61.884 0.2 1 1209 . 292 THR C C 173.08 0.2 1 1210 . 292 THR CB C 69.884 0.2 1 1211 . 292 THR N N 121.994 0.2 1 1212 . 293 ILE H H 9.167 0.01 1 1213 . 293 ILE CA C 60.684 0.2 1 1214 . 293 ILE C C 173.08 0.2 1 1215 . 293 ILE CB C 37.884 0.2 1 1216 . 293 ILE N N 131.383 0.2 1 1217 . 294 SER H H 8.457 0.01 1 1218 . 294 SER CA C 55.984 0.2 1 1219 . 294 SER C C 172.98 0.2 1 1220 . 294 SER CB C 62.884 0.2 1 1221 . 294 SER N N 123.646 0.2 1 1222 . 295 LEU H H 9.177 0.01 1 1223 . 295 LEU CA C 50.884 0.2 1 1224 . 295 LEU C C 172.08 0.2 1 1225 . 295 LEU CB C 43.184 0.2 1 1226 . 295 LEU N N 128.096 0.2 1 1227 . 298 ILE CA C 58.584 0.2 1 1228 . 298 ILE C C 175.48 0.2 1 1229 . 298 ILE CB C 38.384 0.2 1 1230 . 299 ALA H H 7.566 0.01 1 1231 . 299 ALA CA C 50.384 0.2 1 1232 . 299 ALA C C 174.08 0.2 1 1233 . 299 ALA CB C 22.384 0.2 1 1234 . 299 ALA N N 121.364 0.2 1 1235 . 300 LEU H H 8.138 0.01 1 1236 . 300 LEU CA C 52.884 0.2 1 1237 . 300 LEU C C 175.68 0.2 1 1238 . 300 LEU CB C 43.284 0.2 1 1239 . 300 LEU N N 120.983 0.2 1 1240 . 301 ASP H H 8.66 0.01 1 1241 . 301 ASP CA C 51.884 0.2 1 1242 . 301 ASP C C 175.68 0.2 1 1243 . 301 ASP CB C 42.184 0.2 1 1244 . 301 ASP N N 125.465 0.2 1 1245 . 302 PRO CA C 64.484 0.2 1 1246 . 302 PRO C C 176.78 0.2 1 1247 . 302 PRO CB C 31.384 0.2 1 1248 . 303 ALA H H 8.064 0.01 1 1249 . 303 ALA CA C 53.384 0.2 1 1250 . 303 ALA C C 178.18 0.2 1 1251 . 303 ALA CB C 18.484 0.2 1 1252 . 303 ALA N N 120.185 0.2 1 1253 . 304 SER H H 8.057 0.01 1 1254 . 304 SER CA C 58.584 0.2 1 1255 . 304 SER C C 174.48 0.2 1 1256 . 304 SER CB C 65.084 0.2 1 1257 . 304 SER N N 112.415 0.2 1 1258 . 305 LYS H H 8.4 0.01 1 1259 . 305 LYS CA C 56.984 0.2 1 1260 . 305 LYS C C 174.18 0.2 1 1261 . 305 LYS CB C 27.884 0.2 1 1262 . 305 LYS N N 118.942 0.2 1 1263 . 306 THR H H 7.294 0.01 1 1264 . 306 THR CA C 59.484 0.2 1 1265 . 306 THR C C 172.58 0.2 1 1266 . 306 THR CB C 69.084 0.2 1 1267 . 306 THR N N 112.946 0.2 1 1268 . 307 PRO CA C 63.184 0.2 1 1269 . 307 PRO C C 174.38 0.2 1 1270 . 307 PRO CB C 32.084 0.2 1 1271 . 308 LEU H H 8.26 0.01 1 1272 . 308 LEU CA C 52.184 0.2 1 1273 . 308 LEU C C 173.98 0.2 1 1274 . 308 LEU CB C 44.284 0.2 1 1275 . 308 LEU N N 122.374 0.2 1 1276 . 309 HIS H H 8.05 0.01 1 1277 . 309 HIS CA C 53.184 0.2 1 1278 . 309 HIS C C 174.08 0.2 1 1279 . 309 HIS CB C 32.384 0.2 1 1280 . 309 HIS N N 120.534 0.2 1 1281 . 310 LEU H H 7.841 0.01 1 1282 . 310 LEU CA C 54.384 0.2 1 1283 . 310 LEU C C 174.48 0.2 1 1284 . 310 LEU CB C 43.484 0.2 1 1285 . 310 LEU N N 125.962 0.2 1 1286 . 311 GLU H H 8.705 0.01 1 1287 . 311 GLU CA C 55.584 0.2 1 1288 . 311 GLU C C 174.28 0.2 1 1289 . 311 GLU CB C 30.884 0.2 1 1290 . 311 GLU N N 131.477 0.2 1 1291 . 312 LYS H H 8.875 0.01 1 1292 . 312 LYS CA C 53.684 0.2 1 1293 . 312 LYS C C 173.88 0.2 1 1294 . 312 LYS CB C 36.584 0.2 1 1295 . 312 LYS N N 127.299 0.2 1 1296 . 313 LYS H H 8.529 0.01 1 1297 . 313 LYS CA C 55.584 0.2 1 1298 . 313 LYS C C 174.68 0.2 1 1299 . 313 LYS CB C 31.884 0.2 1 1300 . 313 LYS N N 125.853 0.2 1 1301 . 314 LEU H H 8.882 0.01 1 1302 . 314 LEU CA C 52.984 0.2 1 1303 . 314 LEU C C 174.58 0.2 1 1304 . 314 LEU CB C 43.284 0.2 1 1305 . 314 LEU N N 128.739 0.2 1 1306 . 315 THR H H 7.838 0.01 1 1307 . 315 THR CA C 59.284 0.2 1 1308 . 315 THR C C 174.68 0.2 1 1309 . 315 THR CB C 70.184 0.2 1 1310 . 315 THR N N 116.722 0.2 1 1311 . 316 ARG H H 8.853 0.01 1 1312 . 316 ARG CA C 59.784 0.2 1 1313 . 316 ARG C C 175.88 0.2 1 1314 . 316 ARG CB C 29.184 0.2 1 1315 . 316 ARG N N 124.15 0.2 1 1316 . 317 ALA H H 8.287 0.01 1 1317 . 317 ALA CA C 54.984 0.2 1 1318 . 317 ALA C C 179.68 0.2 1 1319 . 317 ALA CB C 16.984 0.2 1 1320 . 317 ALA N N 120.837 0.2 1 1321 . 318 LYS H H 7.896 0.01 1 1322 . 318 LYS CA C 56.784 0.2 1 1323 . 318 LYS C C 177.28 0.2 1 1324 . 318 LYS CB C 29.684 0.2 1 1325 . 318 LYS N N 121.613 0.2 1 1326 . 319 PHE H H 8.335 0.01 1 1327 . 319 PHE CA C 59.784 0.2 1 1328 . 319 PHE C C 175.48 0.2 1 1329 . 319 PHE CB C 38.584 0.2 1 1330 . 319 PHE N N 121.511 0.2 1 1331 . 320 GLU H H 8.59 0.01 1 1332 . 320 GLU CA C 59.084 0.2 1 1333 . 320 GLU C C 178.48 0.2 1 1334 . 320 GLU CB C 27.684 0.2 1 1335 . 320 GLU N N 117.928 0.2 1 1336 . 321 GLU H H 7.497 0.01 1 1337 . 321 GLU CA C 59.084 0.2 1 1338 . 321 GLU C C 179.38 0.2 1 1339 . 321 GLU CB C 27.284 0.2 1 1340 . 321 GLU N N 121.424 0.2 1 1341 . 322 LEU H H 8.066 0.01 1 1342 . 322 LEU CA C 56.784 0.2 1 1343 . 322 LEU C C 178.58 0.2 1 1344 . 322 LEU CB C 41.284 0.2 1 1345 . 322 LEU N N 119.986 0.2 1 1346 . 323 ILE H H 7.289 0.01 1 1347 . 323 ILE CA C 60.184 0.2 1 1348 . 323 ILE C C 175.98 0.2 1 1349 . 323 ILE CB C 37.884 0.2 1 1350 . 323 ILE N N 106.194 0.2 1 1351 . 324 GLN H H 7.389 0.01 1 1352 . 324 GLN CA C 61.084 0.2 1 1353 . 324 GLN C C 174.38 0.2 1 1354 . 324 GLN CB C 25.684 0.2 1 1355 . 324 GLN N N 126.832 0.2 1 1356 . 325 PRO CA C 65.784 0.2 1 1357 . 325 PRO C C 178.48 0.2 1 1358 . 325 PRO CB C 30.484 0.2 1 1359 . 326 LEU H H 7.093 0.01 1 1360 . 326 LEU CA C 51.484 0.2 1 1361 . 326 LEU C C 177.88 0.2 1 1362 . 326 LEU CB C 40.184 0.2 1 1363 . 326 LEU N N 116.205 0.2 1 1364 . 327 LEU H H 7.702 0.01 1 1365 . 327 LEU CA C 56.784 0.2 1 1366 . 327 LEU C C 180.18 0.2 1 1367 . 327 LEU CB C 39.784 0.2 1 1368 . 327 LEU N N 118.167 0.2 1 1369 . 328 LYS H H 7.802 0.01 1 1370 . 328 LYS CA C 58.384 0.2 1 1371 . 328 LYS C C 178.78 0.2 1 1372 . 328 LYS CB C 31.484 0.2 1 1373 . 328 LYS N N 118.17 0.2 1 1374 . 329 ARG H H 7.16 0.01 1 1375 . 329 ARG CA C 57.284 0.2 1 1376 . 329 ARG C C 175.88 0.2 1 1377 . 329 ARG CB C 30.484 0.2 1 1378 . 329 ARG N N 119.056 0.2 1 1379 . 330 LEU H H 7.185 0.01 1 1380 . 330 LEU CA C 55.584 0.2 1 1381 . 330 LEU C C 176.58 0.2 1 1382 . 330 LEU CB C 40.784 0.2 1 1383 . 330 LEU N N 117.789 0.2 1 1384 . 331 ARG H H 6.899 0.01 1 1385 . 331 ARG CA C 59.184 0.2 1 1386 . 331 ARG C C 177.78 0.2 1 1387 . 331 ARG CB C 29.784 0.2 1 1388 . 331 ARG N N 114.194 0.2 1 1389 . 332 GLY H H 8.085 0.01 1 1390 . 332 GLY CA C 47.984 0.2 1 1391 . 332 GLY C C 175.58 0.2 1 1392 . 332 GLY N N 106.385 0.2 1 1393 . 333 PRO CA C 64.684 0.2 1 1394 . 333 PRO C C 178.48 0.2 1 1395 . 333 PRO CB C 31.184 0.2 1 1396 . 334 VAL H H 6.928 0.01 1 1397 . 334 VAL CA C 66.784 0.2 1 1398 . 334 VAL C C 175.88 0.2 1 1399 . 334 VAL CB C 30.984 0.2 1 1400 . 334 VAL N N 117.018 0.2 1 1401 . 335 GLU H H 8.027 0.01 1 1402 . 335 GLU CA C 59.384 0.2 1 1403 . 335 GLU C C 179.08 0.2 1 1404 . 335 GLU CB C 28.384 0.2 1 1405 . 335 GLU N N 118.532 0.2 1 1406 . 336 GLN H H 8.695 0.01 1 1407 . 336 GLN CA C 58.084 0.2 1 1408 . 336 GLN C C 176.58 0.2 1 1409 . 336 GLN CB C 27.884 0.2 1 1410 . 336 GLN N N 120.358 0.2 1 1411 . 337 ALA H H 7.798 0.01 1 1412 . 337 ALA CA C 54.784 0.2 1 1413 . 337 ALA C C 178.48 0.2 1 1414 . 337 ALA CB C 16.084 0.2 1 1415 . 337 ALA N N 121.945 0.2 1 1416 . 338 LEU H H 7.522 0.01 1 1417 . 338 LEU CA C 58.384 0.2 1 1418 . 338 LEU C C 177.68 0.2 1 1419 . 338 LEU CB C 39.784 0.2 1 1420 . 338 LEU N N 116.582 0.2 1 1421 . 339 LYS H H 7.82 0.01 1 1422 . 339 LYS CA C 58.884 0.2 1 1423 . 339 LYS C C 180.18 0.2 1 1424 . 339 LYS CB C 30.684 0.2 1 1425 . 339 LYS N N 120.26 0.2 1 1426 . 340 ASP H H 8.752 0.01 1 1427 . 340 ASP CA C 56.984 0.2 1 1428 . 340 ASP C C 179.28 0.2 1 1429 . 340 ASP CB C 39.184 0.2 1 1430 . 340 ASP N N 123.202 0.2 1 1431 . 341 ALA H H 7.786 0.01 1 1432 . 341 ALA CA C 51.484 0.2 1 1433 . 341 ALA C C 176.18 0.2 1 1434 . 341 ALA CB C 18.684 0.2 1 1435 . 341 ALA N N 120.258 0.2 1 1436 . 342 GLY H H 7.897 0.01 1 1437 . 342 GLY CA C 45.884 0.2 1 1438 . 342 GLY C C 173.98 0.2 1 1439 . 342 GLY N N 110.105 0.2 1 1440 . 343 LEU H H 8.023 0.01 1 1441 . 343 LEU CA C 52.684 0.2 1 1442 . 343 LEU C C 175.08 0.2 1 1443 . 343 LEU CB C 45.484 0.2 1 1444 . 343 LEU N N 119.51 0.2 1 1445 . 344 THR H H 7.823 0.01 1 1446 . 344 THR CA C 58.584 0.2 1 1447 . 344 THR C C 173.58 0.2 1 1448 . 344 THR CB C 68.784 0.2 1 1449 . 344 THR N N 111.356 0.2 1 1450 . 345 PRO C C 177.38 0.2 1 1451 . 346 ALA H H 7.486 0.01 1 1452 . 346 ALA CA C 53.284 0.2 1 1453 . 346 ALA C C 178.08 0.2 1 1454 . 346 ALA CB C 17.784 0.2 1 1455 . 346 ALA N N 117.044 0.2 1 1456 . 347 GLN H H 7.669 0.01 1 1457 . 347 GLN CA C 55.584 0.2 1 1458 . 347 GLN C C 173.98 0.2 1 1459 . 347 GLN CB C 29.984 0.2 1 1460 . 347 GLN N N 116.078 0.2 1 1461 . 348 ILE H H 7.147 0.01 1 1462 . 348 ILE CA C 57.484 0.2 1 1463 . 348 ILE C C 174.48 0.2 1 1464 . 348 ILE CB C 34.884 0.2 1 1465 . 348 ILE N N 120.183 0.2 1 1466 . 349 ASP H H 8.612 0.01 1 1467 . 349 ASP CA C 57.384 0.2 1 1468 . 349 ASP C C 175.98 0.2 1 1469 . 349 ASP CB C 42.184 0.2 1 1470 . 349 ASP N N 127.674 0.2 1 1471 . 350 GLU H H 7.24 0.01 1 1472 . 350 GLU CA C 54.484 0.2 1 1473 . 350 GLU C C 172.28 0.2 1 1474 . 350 GLU CB C 33.284 0.2 1 1475 . 350 GLU N N 115.267 0.2 1 1476 . 351 VAL H H 8.787 0.01 1 1477 . 351 VAL CA C 59.284 0.2 1 1478 . 351 VAL C C 174.78 0.2 1 1479 . 351 VAL CB C 33.684 0.2 1 1480 . 351 VAL N N 124.738 0.2 1 1481 . 352 ILE H H 8.519 0.01 1 1482 . 352 ILE CA C 58.584 0.2 1 1483 . 352 ILE C C 173.68 0.2 1 1484 . 352 ILE N N 122.302 0.2 1 1485 . 353 LEU H H 7.634 0.01 1 1486 . 353 LEU CA C 53.684 0.2 1 1487 . 353 LEU C C 174.78 0.2 1 1488 . 353 LEU CB C 40.484 0.2 1 1489 . 353 LEU N N 123.1 0.2 1 1490 . 354 VAL H H 9.139 0.01 1 1491 . 354 VAL CA C 61.484 0.2 1 1492 . 354 VAL C C 171.88 0.2 1 1493 . 354 VAL CB C 34.784 0.2 1 1494 . 354 VAL N N 125.942 0.2 1 1495 . 355 GLY H H 7.136 0.01 1 1496 . 355 GLY CA C 42.784 0.2 1 1497 . 355 GLY C C 175.98 0.2 1 1498 . 355 GLY N N 112.047 0.2 1 1499 . 356 GLY H H 10.226 0.01 1 1500 . 356 GLY CA C 47.784 0.2 1 1501 . 356 GLY N N 116.257 0.2 1 1502 . 357 ALA H H 7.101 0.01 1 1503 . 357 ALA CA C 52.284 0.2 1 1504 . 357 ALA C C 175.68 0.2 1 1505 . 357 ALA N N 118.081 0.2 1 1506 . 358 THR CA C 63.584 0.2 1 1507 . 358 THR C C 176.38 0.2 1 1508 . 359 ARG H H 6.848 0.01 1 1509 . 359 ARG CA C 56.884 0.2 1 1510 . 359 ARG C C 175.68 0.2 1 1511 . 359 ARG CB C 29.784 0.2 1 1512 . 359 ARG N N 118.15 0.2 1 1513 . 360 VAL H H 6.736 0.01 1 1514 . 360 VAL CA C 60.684 0.2 1 1515 . 360 VAL C C 175.58 0.2 1 1516 . 360 VAL CB C 32.084 0.2 1 1517 . 360 VAL N N 120.317 0.2 1 1518 . 361 PRO CA C 66.084 0.2 1 1519 . 361 PRO C C 178.98 0.2 1 1520 . 361 PRO CB C 30.384 0.2 1 1521 . 362 ALA H H 9.519 0.01 1 1522 . 362 ALA CA C 54.384 0.2 1 1523 . 362 ALA C C 180.18 0.2 1 1524 . 362 ALA CB C 17.884 0.2 1 1525 . 362 ALA N N 120.679 0.2 1 1526 . 363 VAL H H 7.401 0.01 1 1527 . 363 VAL CA C 65.784 0.2 1 1528 . 363 VAL C C 176.38 0.2 1 1529 . 363 VAL CB C 29.984 0.2 1 1530 . 363 VAL N N 117.935 0.2 1 1531 . 364 GLN H H 7.08 0.01 1 1532 . 364 GLN CA C 60.084 0.2 1 1533 . 364 GLN C C 177.38 0.2 1 1534 . 364 GLN N N 118.915 0.2 1 1535 . 365 GLN H H 7.876 0.01 1 1536 . 365 GLN CA C 59.584 0.2 1 1537 . 365 GLN C C 174.38 0.2 1 1538 . 365 GLN CB C 30.484 0.2 1 1539 . 365 GLN N N 117.95 0.2 1 1540 . 367 VAL CA C 61.784 0.2 1 1541 . 367 VAL C C 176.98 0.2 1 1542 . 367 VAL CB C 31.784 0.2 1 1543 . 368 ARG H H 11.835 0.01 1 1544 . 368 ARG CA C 58.284 0.2 1 1545 . 368 ARG C C 175.38 0.2 1 1546 . 368 ARG CB C 35.284 0.2 1 1547 . 368 ARG N N 126.388 0.2 1 1548 . 369 GLU H H 8.069 0.01 1 1549 . 369 GLU CA C 58.784 0.2 1 1550 . 369 GLU C C 178.28 0.2 1 1551 . 369 GLU CB C 28.884 0.2 1 1552 . 369 GLU N N 120.844 0.2 1 1553 . 370 LEU H H 8.297 0.01 1 1554 . 370 LEU CA C 56.784 0.2 1 1555 . 370 LEU C C 178.08 0.2 1 1556 . 370 LEU CB C 42.584 0.2 1 1557 . 370 LEU N N 118.61 0.2 1 1558 . 371 LEU H H 7.892 0.01 1 1559 . 371 LEU CA C 53.484 0.2 1 1560 . 371 LEU C C 176.38 0.2 1 1561 . 371 LEU CB C 41.284 0.2 1 1562 . 371 LEU N N 115.454 0.2 1 1563 . 372 GLY H H 7.955 0.01 1 1564 . 372 GLY CA C 46.184 0.2 1 1565 . 372 GLY C C 172.98 0.2 1 1566 . 372 GLY N N 109.905 0.2 1 1567 . 373 LYS H H 6.82 0.01 1 1568 . 373 LYS CA C 53.184 0.2 1 1569 . 373 LYS C C 173.68 0.2 1 1570 . 373 LYS CB C 34.484 0.2 1 1571 . 373 LYS N N 116.24 0.2 1 1572 . 374 GLU H H 8.256 0.01 1 1573 . 374 GLU CA C 52.284 0.2 1 1574 . 374 GLU C C 174.58 0.2 1 1575 . 374 GLU CB C 28.784 0.2 1 1576 . 374 GLU N N 122.185 0.2 1 1577 . 381 PRO CA C 63.084 0.2 1 1578 . 381 PRO C C 176.78 0.2 1 1579 . 381 PRO CB C 31.284 0.2 1 1580 . 382 ASP H H 6.218 0.01 1 1581 . 382 ASP CA C 54.084 0.2 1 1582 . 382 ASP C C 172.98 0.2 1 1583 . 382 ASP CB C 37.084 0.2 1 1584 . 382 ASP N N 115.492 0.2 1 1585 . 383 GLU H H 8.957 0.01 1 1586 . 383 GLU CA C 57.184 0.2 1 1587 . 383 GLU C C 173.88 0.2 1 1588 . 383 GLU CB C 32.084 0.2 1 1589 . 383 GLU N N 122.895 0.2 1 1590 . 384 VAL H H 7.632 0.01 1 1591 . 384 VAL CA C 60.904 0.2 1 1592 . 384 VAL C C 174.98 0.2 1 1593 . 384 VAL CB C 32.184 0.2 1 1594 . 384 VAL N N 127.917 0.2 1 1595 . 385 VAL H H 8.953 0.01 1 1596 . 385 VAL CA C 57.384 0.2 1 1597 . 385 VAL C C 172.68 0.2 1 1598 . 385 VAL CB C 32.684 0.2 1 1599 . 385 VAL N N 121.179 0.2 1 1600 . 387 MET CA C 57.084 0.2 1 1601 . 387 MET C C 177.28 0.2 1 1602 . 387 MET CB C 35.884 0.2 1 1603 . 388 GLY H H 8.087 0.01 1 1604 . 388 GLY CA C 46.584 0.2 1 1605 . 388 GLY C C 175.08 0.2 1 1606 . 388 GLY N N 107.229 0.2 1 1607 . 389 ALA H H 7.988 0.01 1 1608 . 389 ALA CA C 54.884 0.2 1 1609 . 389 ALA C C 177.88 0.2 1 1610 . 389 ALA CB C 16.784 0.2 1 1611 . 389 ALA N N 124.837 0.2 1 1612 . 390 ALA H H 7.999 0.01 1 1613 . 390 ALA CA C 54.084 0.2 1 1614 . 390 ALA C C 175.38 0.2 1 1615 . 390 ALA CB C 17.084 0.2 1 1616 . 390 ALA N N 123.322 0.2 1 1617 . 391 ILE H H 7.626 0.01 1 1618 . 391 ILE CA C 65.284 0.2 1 1619 . 391 ILE C C 177.28 0.2 1 1620 . 391 ILE CB C 36.984 0.2 1 1621 . 391 ILE N N 120.912 0.2 1 1622 . 392 GLN H H 7.98 0.01 1 1623 . 392 GLN CA C 57.784 0.2 1 1624 . 392 GLN C C 177.78 0.2 1 1625 . 392 GLN CB C 27.184 0.2 1 1626 . 392 GLN N N 119.562 0.2 1 1627 . 393 ALA H H 8.332 0.01 1 1628 . 393 ALA CA C 55.084 0.2 1 1629 . 393 ALA C C 177.68 0.2 1 1630 . 393 ALA CB C 16.884 0.2 1 1631 . 393 ALA N N 123.233 0.2 1 1632 . 394 GLY H H 7.976 0.01 1 1633 . 394 GLY CA C 46.984 0.2 1 1634 . 394 GLY C C 175.88 0.2 1 1635 . 394 GLY N N 105.408 0.2 1 1636 . 395 VAL H H 8.071 0.01 1 1637 . 395 VAL CA C 65.284 0.2 1 1638 . 395 VAL C C 179.18 0.2 1 1639 . 395 VAL CB C 31.284 0.2 1 1640 . 395 VAL N N 123.953 0.2 1 1641 . 396 LEU H H 7.702 0.01 1 1642 . 396 LEU CA C 56.584 0.2 1 1643 . 396 LEU C C 178.08 0.2 1 1644 . 396 LEU CB C 40.384 0.2 1 1645 . 396 LEU N N 120.785 0.2 1 1646 . 397 MET H H 7.666 0.01 1 1647 . 397 MET CA C 54.884 0.2 1 1648 . 397 MET C C 176.28 0.2 1 1649 . 397 MET CB C 31.884 0.2 1 1650 . 397 MET N N 117.083 0.2 1 1651 . 398 GLY H H 7.669 0.01 1 1652 . 398 GLY CA C 45.284 0.2 1 1653 . 398 GLY C C 173.68 0.2 1 1654 . 398 GLY N N 108.361 0.2 1 1655 . 399 GLU H H 7.973 0.01 1 1656 . 399 GLU CA C 56.284 0.2 1 1657 . 399 GLU C C 175.38 0.2 1 1658 . 399 GLU CB C 29.584 0.2 1 1659 . 399 GLU N N 121.102 0.2 1 1660 . 400 VAL H H 7.536 0.01 1 1661 . 400 VAL CA C 61.484 0.2 1 1662 . 400 VAL C C 173.98 0.2 1 1663 . 400 VAL CB C 32.584 0.2 1 1664 . 400 VAL N N 120.82 0.2 1 1665 . 401 ARG H H 7.736 0.01 1 1666 . 401 ARG CA C 56.784 0.2 1 1667 . 401 ARG C C 178.18 0.2 1 1668 . 401 ARG CB C 30.884 0.2 1 1669 . 401 ARG N N 130.828 0.2 1 stop_ save_