data_50220 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Staphylococcus aureus EF-GC3 methyl chemical shift assignments in complex with FusB ; _BMRB_accession_number 50220 _BMRB_flat_file_name bmr50220.str _Entry_type original _Submission_date 2020-04-01 _Accession_date 2020-04-01 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Chemical shift assignments for methyl containing side chains of EF-GC3 from Staphylococcus aureus when bound to FusB.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tomlinson Jennifer H. . 2 Kalverda Arnout P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 133 "13C chemical shifts" 264 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-10-07 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25504 'Backbone assignments for the same protein system' 50221 'EF-GC3 from Staphylococcus aureus in apo form' stop_ _Original_release_date 2020-04-09 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Fusidic acid resistance through changes in the dynamics of the drug target ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32999060 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tomlinson Jennifer H. . 2 Kalverda Arnout P. . 3 Calabrese Antonio N. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U. S. A.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2020 _Details . loop_ _Keyword 'antibiotic resistance, Elongation Factor G, NMR, FusB, conformational flexibility' stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'Staphylococcus aureus FusB:EF-GC3 complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label EF-GC3 $entity_1 FusB $entity_2 'ZINC ION' $entity_ZN stop_ _System_molecular_weight 60496.31 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'FusB binding to EF-G confers resistance to the antibiotic fusidic acid that otherwise inhibits EF-G.' stop_ _Database_query_date . _Details 'EF-GC3 bound to FusB in a 1:1 complex. Zinc ion coordinated by FusB C-terminal domain.' save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass 32272.721 _Mol_thiol_state 'all free' loop_ _Biological_function 'EF-G translocates the ribosome to allow access for the next tRNA to the next mRNA codon following peptide bond formation.' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 292 _Mol_residue_sequence ; MEFPEPVIHLSVEPKSKADQ DKMTQALVKLQEEDPTFHAH TDEETGQVIIGGMGELHLDI LVDRMKKEFNVECNVGAPMV SYRETFKSSAQVQGKFSRQS GGRGQYGDVHIEFTPNETGA GFEFENAIVGGVVPREYIPS VEAGLKDAMENGVLAGYPLI DVKAKLYDGSYHDVDSSEMA FKIAASLALKEAAKKCDPVI LEPMMKVTIEMPEEYMGDIM GDVTSRRGRVDGMEPRGNAQ VVNAYVPLSEMFGYATSLRS NTQGRGTYTMYFDHYAEVPK SIAEDIIKKNKG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 401 MET 2 402 GLU 3 403 PHE 4 404 PRO 5 405 GLU 6 406 PRO 7 407 VAL 8 408 ILE 9 409 HIS 10 410 LEU 11 411 SER 12 412 VAL 13 413 GLU 14 414 PRO 15 415 LYS 16 416 SER 17 417 LYS 18 418 ALA 19 419 ASP 20 420 GLN 21 421 ASP 22 422 LYS 23 423 MET 24 424 THR 25 425 GLN 26 426 ALA 27 427 LEU 28 428 VAL 29 429 LYS 30 430 LEU 31 431 GLN 32 432 GLU 33 433 GLU 34 434 ASP 35 435 PRO 36 436 THR 37 437 PHE 38 438 HIS 39 439 ALA 40 440 HIS 41 441 THR 42 442 ASP 43 443 GLU 44 444 GLU 45 445 THR 46 446 GLY 47 447 GLN 48 448 VAL 49 449 ILE 50 450 ILE 51 451 GLY 52 452 GLY 53 453 MET 54 454 GLY 55 455 GLU 56 456 LEU 57 457 HIS 58 458 LEU 59 459 ASP 60 460 ILE 61 461 LEU 62 462 VAL 63 463 ASP 64 464 ARG 65 465 MET 66 466 LYS 67 467 LYS 68 468 GLU 69 469 PHE 70 470 ASN 71 471 VAL 72 472 GLU 73 473 CYS 74 474 ASN 75 475 VAL 76 476 GLY 77 477 ALA 78 478 PRO 79 479 MET 80 480 VAL 81 481 SER 82 482 TYR 83 483 ARG 84 484 GLU 85 485 THR 86 486 PHE 87 487 LYS 88 488 SER 89 489 SER 90 490 ALA 91 491 GLN 92 492 VAL 93 493 GLN 94 494 GLY 95 495 LYS 96 496 PHE 97 497 SER 98 498 ARG 99 499 GLN 100 500 SER 101 501 GLY 102 502 GLY 103 503 ARG 104 504 GLY 105 505 GLN 106 506 TYR 107 507 GLY 108 508 ASP 109 509 VAL 110 510 HIS 111 511 ILE 112 512 GLU 113 513 PHE 114 514 THR 115 515 PRO 116 516 ASN 117 517 GLU 118 518 THR 119 519 GLY 120 520 ALA 121 521 GLY 122 522 PHE 123 523 GLU 124 524 PHE 125 525 GLU 126 526 ASN 127 527 ALA 128 528 ILE 129 529 VAL 130 530 GLY 131 531 GLY 132 532 VAL 133 533 VAL 134 534 PRO 135 535 ARG 136 536 GLU 137 537 TYR 138 538 ILE 139 539 PRO 140 540 SER 141 541 VAL 142 542 GLU 143 543 ALA 144 544 GLY 145 545 LEU 146 546 LYS 147 547 ASP 148 548 ALA 149 549 MET 150 550 GLU 151 551 ASN 152 552 GLY 153 553 VAL 154 554 LEU 155 555 ALA 156 556 GLY 157 557 TYR 158 558 PRO 159 559 LEU 160 560 ILE 161 561 ASP 162 562 VAL 163 563 LYS 164 564 ALA 165 565 LYS 166 566 LEU 167 567 TYR 168 568 ASP 169 569 GLY 170 570 SER 171 571 TYR 172 572 HIS 173 573 ASP 174 574 VAL 175 575 ASP 176 576 SER 177 577 SER 178 578 GLU 179 579 MET 180 580 ALA 181 581 PHE 182 582 LYS 183 583 ILE 184 584 ALA 185 585 ALA 186 586 SER 187 587 LEU 188 588 ALA 189 589 LEU 190 590 LYS 191 591 GLU 192 592 ALA 193 593 ALA 194 594 LYS 195 595 LYS 196 596 CYS 197 597 ASP 198 598 PRO 199 599 VAL 200 600 ILE 201 601 LEU 202 602 GLU 203 603 PRO 204 604 MET 205 605 MET 206 606 LYS 207 607 VAL 208 608 THR 209 609 ILE 210 610 GLU 211 611 MET 212 612 PRO 213 613 GLU 214 614 GLU 215 615 TYR 216 616 MET 217 617 GLY 218 618 ASP 219 619 ILE 220 620 MET 221 621 GLY 222 622 ASP 223 623 VAL 224 624 THR 225 625 SER 226 626 ARG 227 627 ARG 228 628 GLY 229 629 ARG 230 630 VAL 231 631 ASP 232 632 GLY 233 633 MET 234 634 GLU 235 635 PRO 236 636 ARG 237 637 GLY 238 638 ASN 239 639 ALA 240 640 GLN 241 641 VAL 242 642 VAL 243 643 ASN 244 644 ALA 245 645 TYR 246 646 VAL 247 647 PRO 248 648 LEU 249 649 SER 250 650 GLU 251 651 MET 252 652 PHE 253 653 GLY 254 654 TYR 255 655 ALA 256 656 THR 257 657 SER 258 658 LEU 259 659 ARG 260 660 SER 261 661 ASN 262 662 THR 263 663 GLN 264 664 GLY 265 665 ARG 266 666 GLY 267 667 THR 268 668 TYR 269 669 THR 270 670 MET 271 671 TYR 272 672 PHE 273 673 ASP 274 674 HIS 275 675 TYR 276 676 ALA 277 677 GLU 278 678 VAL 279 679 PRO 280 680 LYS 281 681 SER 282 682 ILE 283 683 ALA 284 684 GLU 285 685 ASP 286 686 ILE 287 687 ILE 288 688 LYS 289 689 LYS 290 690 ASN 291 691 LYS 292 692 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 NCBI P68790 EF-G . . . . . stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass 25225.330 _Mol_thiol_state 'all other bound' loop_ _Biological_function 'Confers resistance to the antibiotic fusidic acid' stop_ _Details . _Residue_count 233 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPNGSH MKTMIYPHQYNYIRSVILRL KNVYKTVNDKETVKVIQSET YNDINEIFGHIDDDIEESLK VLMNIRLSNKEIEAILNKFL EYVVPFELPSPQKLQKVFKK VKKIKIPQFEEYDLKVSSFV GWNELASNRKYIIYYDEKKQ LKGLYGEISNQVVKGFCTIC NKESNVSLFMKKSKTNSDGQ YVKKGDYICRDSIHCNKQLT DINQFYNFIDKLD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -19 MET 2 -18 GLY 3 -17 SER 4 -16 SER 5 -15 HIS 6 -14 HIS 7 -13 HIS 8 -12 HIS 9 -11 HIS 10 -10 HIS 11 -9 SER 12 -8 SER 13 -7 GLY 14 -6 LEU 15 -5 VAL 16 -4 PRO 17 -3 ASN 18 -2 GLY 19 -1 SER 20 0 HIS 21 1 MET 22 2 LYS 23 3 THR 24 4 MET 25 5 ILE 26 6 TYR 27 7 PRO 28 8 HIS 29 9 GLN 30 10 TYR 31 11 ASN 32 12 TYR 33 13 ILE 34 14 ARG 35 15 SER 36 16 VAL 37 17 ILE 38 18 LEU 39 19 ARG 40 20 LEU 41 21 LYS 42 22 ASN 43 23 VAL 44 24 TYR 45 25 LYS 46 26 THR 47 27 VAL 48 28 ASN 49 29 ASP 50 30 LYS 51 31 GLU 52 32 THR 53 33 VAL 54 34 LYS 55 35 VAL 56 36 ILE 57 37 GLN 58 38 SER 59 39 GLU 60 40 THR 61 41 TYR 62 42 ASN 63 43 ASP 64 44 ILE 65 45 ASN 66 46 GLU 67 47 ILE 68 48 PHE 69 49 GLY 70 50 HIS 71 51 ILE 72 52 ASP 73 53 ASP 74 54 ASP 75 55 ILE 76 56 GLU 77 57 GLU 78 58 SER 79 59 LEU 80 60 LYS 81 61 VAL 82 62 LEU 83 63 MET 84 64 ASN 85 65 ILE 86 66 ARG 87 67 LEU 88 68 SER 89 69 ASN 90 70 LYS 91 71 GLU 92 72 ILE 93 73 GLU 94 74 ALA 95 75 ILE 96 76 LEU 97 77 ASN 98 78 LYS 99 79 PHE 100 80 LEU 101 81 GLU 102 82 TYR 103 83 VAL 104 84 VAL 105 85 PRO 106 86 PHE 107 87 GLU 108 88 LEU 109 89 PRO 110 90 SER 111 91 PRO 112 92 GLN 113 93 LYS 114 94 LEU 115 95 GLN 116 96 LYS 117 97 VAL 118 98 PHE 119 99 LYS 120 100 LYS 121 101 VAL 122 102 LYS 123 103 LYS 124 104 ILE 125 105 LYS 126 106 ILE 127 107 PRO 128 108 GLN 129 109 PHE 130 110 GLU 131 111 GLU 132 112 TYR 133 113 ASP 134 114 LEU 135 115 LYS 136 116 VAL 137 117 SER 138 118 SER 139 119 PHE 140 120 VAL 141 121 GLY 142 122 TRP 143 123 ASN 144 124 GLU 145 125 LEU 146 126 ALA 147 127 SER 148 128 ASN 149 129 ARG 150 130 LYS 151 131 TYR 152 132 ILE 153 133 ILE 154 134 TYR 155 135 TYR 156 136 ASP 157 137 GLU 158 138 LYS 159 139 LYS 160 140 GLN 161 141 LEU 162 142 LYS 163 143 GLY 164 144 LEU 165 145 TYR 166 146 GLY 167 147 GLU 168 148 ILE 169 149 SER 170 150 ASN 171 151 GLN 172 152 VAL 173 153 VAL 174 154 LYS 175 155 GLY 176 156 PHE 177 157 CYS 178 158 THR 179 159 ILE 180 160 CYS 181 161 ASN 182 162 LYS 183 163 GLU 184 164 SER 185 165 ASN 186 166 VAL 187 167 SER 188 168 LEU 189 169 PHE 190 170 MET 191 171 LYS 192 172 LYS 193 173 SER 194 174 LYS 195 175 THR 196 176 ASN 197 177 SER 198 178 ASP 199 179 GLY 200 180 GLN 201 181 TYR 202 182 VAL 203 183 LYS 204 184 LYS 205 185 GLY 206 186 ASP 207 187 TYR 208 188 ILE 209 189 CYS 210 190 ARG 211 191 ASP 212 192 SER 213 193 ILE 214 194 HIS 215 195 CYS 216 196 ASN 217 197 LYS 218 198 GLN 219 199 LEU 220 200 THR 221 201 ASP 222 202 ILE 223 203 ASN 224 204 GLN 225 205 PHE 226 206 TYR 227 207 ASN 228 208 PHE 229 209 ILE 230 210 ASP 231 211 LYS 232 212 LEU 233 213 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 NCBI YP_009078429 FusB . . . . . stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_ZN (ZINC ION)" _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $entity_1 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus fusA 'Truncated form of the full length EF-G protein encoded by fusA.' $entity_2 'Staphylococcus aureus' 1280 Bacteria . Staphylococcus aureus fusB . stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli 'BL21 Gold' plasmid pET-29b $entity_2 'recombinant technology' . Escherichia coli 'BL21 Gold' plasmid pET-28a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '20 mM TrisHCl, 300 mM NaCl, 5 mM DTT, pH 8.0' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.250 mM '[U-100% 13C; U-100% 15N; partial 2H (grown in D2O with 1H glucose)]' $entity_2 0.375 mM 'natural abundance' TRIS 20 mM 'natural abundance' 'sodium chloride' 300 mM 'natural abundance' DTT 5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CcpNmr_Analysis _Version 2.1 loop_ _Task 'chemical shift assignment' processing stop_ _Details 'The CCPN NMR assignment and data analysis application' save_ save_software_3 _Saveframe_category software _Name NMRView _Version 7.9 loop_ _Task 'data analysis' processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 748 _Details 'Bruker Avance console in a Varian magnet.' save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-13C_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CCH-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCH-TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '20 mM TrisHCl, 300 mM NaCl, 5 mM DTT, pH 8.0' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.300 0.002 M pH 8.000 0.01 pH pressure 1.000 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0 internal indirect . . . . DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $software_1 stop_ loop_ _Experiment_label '2D 1H-13C HSQC' '3D CCH-TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name EF-GC3 _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 1 408 8 ILE HG2 H 0.563 0.036 1 2 408 8 ILE HD1 H 0.659 0.027 1 3 408 8 ILE CA C 58.443 . 1 4 408 8 ILE CB C 40.280 . 1 5 408 8 ILE CG1 C 26.316 0.088 1 6 408 8 ILE CG2 C 14.754 0.115 1 7 408 8 ILE CD1 C 13.275 0.121 1 8 410 10 LEU HD1 H 0.592 0.0 1 9 410 10 LEU CB C 45.240 . 1 10 410 10 LEU CD1 C 21.327 0.045 1 11 412 12 VAL HG1 H 0.770 0.034 1 12 412 12 VAL CA C 60.268 . 1 13 412 12 VAL CB C 33.599 . 1 14 412 12 VAL CG1 C 20.572 0.129 1 15 418 18 ALA HB H 1.356 0.0 1 16 418 18 ALA CA C 54.310 . 1 17 418 18 ALA CB C 17.168 0.034 1 18 424 24 THR HG2 H 1.126 0.0 1 19 424 24 THR CA C 66.270 . 1 20 424 24 THR CB C 68.114 . 1 21 424 24 THR CG2 C 20.781 0.033 1 22 426 26 ALA H H 7.923 . 1 23 426 26 ALA HB H 0.750 0.026 1 24 426 26 ALA CA C 53.895 . 1 25 426 26 ALA CB C 17.720 0.024 1 26 427 27 LEU HD1 H 0.656 0.0 1 27 427 27 LEU CA C 57.612 . 1 28 427 27 LEU CB C 40.223 . 1 29 427 27 LEU CG C 25.238 . 1 30 427 27 LEU CD1 C 22.142 0.036 1 31 428 28 VAL HG1 H 0.962 0.0 2 32 428 28 VAL HG2 H 0.839 0.002 2 33 428 28 VAL CA C 65.767 0.033 1 34 428 28 VAL CB C 30.815 0.024 1 35 428 28 VAL CG1 C 21.327 0.035 2 36 428 28 VAL CG2 C 20.101 0.037 2 37 430 30 LEU HD1 H 0.449 0.0 2 38 430 30 LEU HD2 H 0.697 0.0 2 39 430 30 LEU CA C 57.576 0.035 1 40 430 30 LEU CB C 40.352 0.023 1 41 430 30 LEU CG C 25.838 0.103 1 42 430 30 LEU CD1 C 24.345 0.033 2 43 430 30 LEU CD2 C 21.442 0.042 2 44 436 36 THR HG2 H 0.915 0.001 1 45 436 36 THR CA C 61.430 . 1 46 436 36 THR CB C 68.726 . 1 47 439 39 ALA H H 7.845 . 1 48 439 39 ALA HB H 1.040 0.027 1 49 439 39 ALA CA C 50.266 . 1 50 439 39 ALA CB C 22.032 0.018 1 51 441 41 THR HG2 H 0.781 0.0 1 52 441 41 THR CA C 61.285 . 1 53 441 41 THR CB C 68.866 . 1 54 441 41 THR CG2 C 20.168 0.031 1 55 445 45 THR HG2 H 1.086 0.001 1 56 445 45 THR CA C 61.264 . 1 57 445 45 THR CB C 70.567 . 1 58 445 45 THR CG2 C 20.284 0.038 1 59 448 48 VAL HG1 H 0.871 0.001 2 60 448 48 VAL HG2 H 0.852 0.03 2 61 448 48 VAL CA C 60.417 0.005 1 62 448 48 VAL CB C 32.983 0.003 1 63 448 48 VAL CG1 C 19.497 0.1 2 64 448 48 VAL CG2 C 20.322 0.118 2 65 449 49 ILE HG2 H 0.667 0.0 1 66 449 49 ILE HD1 H 0.584 0.001 1 67 449 49 ILE CA C 58.466 0.046 1 68 449 49 ILE CB C 37.271 0.129 1 69 449 49 ILE CG1 C 25.826 . 1 70 449 49 ILE CG2 C 17.186 0.028 1 71 449 49 ILE CD1 C 10.801 0.073 1 72 450 50 ILE HG2 H 0.720 0.032 1 73 450 50 ILE HD1 H 0.572 0.001 1 74 450 50 ILE CA C 58.642 0.02 1 75 450 50 ILE CB C 38.765 0.029 1 76 450 50 ILE CG1 C 25.092 0.026 1 77 450 50 ILE CG2 C 17.223 0.122 1 78 450 50 ILE CD1 C 12.498 0.03 1 79 456 56 LEU HD1 H 0.741 0.001 2 80 456 56 LEU HD2 H 0.692 0.025 2 81 456 56 LEU CA C 54.671 0.012 1 82 456 56 LEU CG C 25.618 0.043 1 83 456 56 LEU CD1 C 23.907 0.059 2 84 456 56 LEU CD2 C 22.408 0.031 2 85 460 60 ILE HG2 H 0.829 0.03 1 86 460 60 ILE HD1 H 0.762 0.028 1 87 460 60 ILE CA C 63.888 0.061 1 88 460 60 ILE CB C 36.716 0.04 1 89 460 60 ILE CG1 C 27.506 . 1 90 460 60 ILE CG2 C 16.152 0.127 1 91 460 60 ILE CD1 C 12.144 0.132 1 92 461 61 LEU HD1 H -0.100 0.0 2 93 461 61 LEU HD2 H 0.325 0.001 2 94 461 61 LEU CB C 40.695 . 1 95 461 61 LEU CG C 25.493 0.011 1 96 461 61 LEU CD1 C 23.875 0.052 2 97 461 61 LEU CD2 C 22.215 0.027 2 98 462 62 VAL HG1 H 0.809 0.001 2 99 462 62 VAL HG2 H 0.774 0.002 2 100 462 62 VAL CA C 66.042 0.052 1 101 462 62 VAL CB C 30.467 0.026 1 102 462 62 VAL CG1 C 22.107 0.023 2 103 462 62 VAL CG2 C 20.909 0.035 2 104 471 71 VAL HG1 H 0.674 0.029 2 105 471 71 VAL HG2 H 0.712 0.0 2 106 471 71 VAL CA C 62.232 0.05 1 107 471 71 VAL CB C 32.218 0.015 1 108 471 71 VAL CG1 C 20.874 0.112 2 109 471 71 VAL CG2 C 20.777 0.021 2 110 475 75 VAL HG1 H 0.816 0.029 2 111 475 75 VAL HG2 H 0.679 0.028 2 112 475 75 VAL CA C 60.654 0.018 1 113 475 75 VAL CB C 33.674 0.065 1 114 475 75 VAL CG1 C 18.474 0.106 2 115 475 75 VAL CG2 C 21.190 0.098 2 116 477 77 ALA H H 7.910 . 1 117 477 77 ALA HB H 1.246 0.035 1 118 477 77 ALA CA C 49.060 . 1 119 477 77 ALA CB C 17.376 0.038 1 120 485 85 THR HG2 H 0.995 0.0 1 121 485 85 THR CA C 61.136 . 1 122 485 85 THR CB C 69.317 . 1 123 485 85 THR CG2 C 21.014 0.021 1 124 490 90 ALA H H 8.490 . 1 125 490 90 ALA HB H 1.254 0.032 1 126 490 90 ALA CA C 52.314 . 1 127 490 90 ALA CB C 23.281 0.024 1 128 492 92 VAL HG1 H 1.134 0.029 2 129 492 92 VAL HG2 H 0.760 0.033 2 130 492 92 VAL CA C 58.796 0.03 1 131 492 92 VAL CB C 35.490 0.017 1 132 492 92 VAL CG1 C 18.641 0.099 2 133 492 92 VAL CG2 C 21.051 0.142 2 134 509 109 VAL HG1 H 1.218 0.03 2 135 509 109 VAL HG2 H 0.790 0.027 2 136 509 109 VAL CA C 57.780 0.026 1 137 509 109 VAL CB C 34.792 0.087 1 138 509 109 VAL CG1 C 23.245 0.098 2 139 509 109 VAL CG2 C 17.634 0.056 2 140 511 111 ILE HG2 H -0.160 0.032 1 141 511 111 ILE HD1 H 0.750 0.026 1 142 511 111 ILE CA C 57.774 0.007 1 143 511 111 ILE CB C 41.364 0.001 1 144 511 111 ILE CG1 C 27.276 0.029 1 145 511 111 ILE CG2 C 16.462 0.114 1 146 511 111 ILE CD1 C 12.795 0.082 1 147 514 114 THR HG2 H 1.166 0.0 1 148 514 114 THR CA C 58.364 . 1 149 514 114 THR CG2 C 20.372 0.036 1 150 518 118 THR HG2 H 1.302 0.0 1 151 518 118 THR CA C 63.748 . 1 152 518 118 THR CB C 68.543 . 1 153 518 118 THR CG2 C 20.897 0.035 1 154 520 120 ALA H H 8.145 . 1 155 520 120 ALA HB H 1.236 0.031 1 156 520 120 ALA CA C 52.524 . 1 157 520 120 ALA CB C 19.386 0.017 1 158 527 127 ALA H H 8.653 . 1 159 527 127 ALA HB H 1.167 0.033 1 160 527 127 ALA CA C 49.804 . 1 161 527 127 ALA CB C 18.536 0.02 1 162 528 128 ILE HG2 H 0.826 0.043 1 163 528 128 ILE HD1 H 0.350 0.029 1 164 528 128 ILE CA C 58.903 . 1 165 528 128 ILE CB C 34.436 . 1 166 528 128 ILE CG1 C 25.641 . 1 167 528 128 ILE CG2 C 16.646 0.101 1 168 528 128 ILE CD1 C 8.572 0.072 1 169 529 129 VAL HG1 H 0.588 0.032 1 170 529 129 VAL CA C 60.149 . 1 171 529 129 VAL CB C 33.455 . 1 172 529 129 VAL CG1 C 20.412 0.108 1 173 532 132 VAL HG1 H 1.079 0.0 2 174 532 132 VAL HG2 H 1.068 0.004 2 175 532 132 VAL CA C 65.054 0.108 1 176 532 132 VAL CB C 30.091 0.053 1 177 532 132 VAL CG1 C 21.027 0.019 2 178 532 132 VAL CG2 C 18.898 0.031 2 179 533 133 VAL HG1 H 0.436 0.036 2 180 533 133 VAL HG2 H 0.955 0.03 2 181 533 133 VAL CA C 59.642 0.014 1 182 533 133 VAL CB C 33.769 0.086 1 183 533 133 VAL CG1 C 19.895 0.121 2 184 533 133 VAL CG2 C 21.042 0.107 2 185 538 138 ILE HG2 H 1.001 0.036 1 186 538 138 ILE HD1 H 0.616 0.027 1 187 538 138 ILE CA C 66.067 0.082 1 188 538 138 ILE CB C 33.485 0.101 1 189 538 138 ILE CG1 C 27.630 0.024 1 190 538 138 ILE CG2 C 16.086 0.117 1 191 538 138 ILE CD1 C 10.253 0.081 1 192 543 143 ALA H H 8.116 . 1 193 543 143 ALA HB H 1.366 0.032 1 194 543 143 ALA CA C 54.378 . 1 195 543 143 ALA CB C 17.773 0.029 1 196 545 145 LEU HD1 H 1.001 0.0 1 197 545 145 LEU CA C 57.149 . 1 198 545 145 LEU CB C 40.955 . 1 199 545 145 LEU CG C 25.525 . 1 200 545 145 LEU CD1 C 23.320 0.037 1 201 548 148 ALA H H 7.593 . 1 202 548 148 ALA HB H 1.365 0.035 1 203 548 148 ALA CA C 54.067 . 1 204 548 148 ALA CB C 17.582 0.027 1 205 555 155 ALA HB H 1.209 0.0 1 206 555 155 ALA CA C 50.003 . 1 207 555 155 ALA CB C 20.487 0.035 1 208 559 159 LEU HD1 H 0.333 0.0 2 209 559 159 LEU HD2 H 0.150 0.001 2 210 559 159 LEU CA C 53.353 0.113 1 211 559 159 LEU CB C 42.952 0.093 1 212 559 159 LEU CG C 25.759 . 1 213 559 159 LEU CD1 C 24.490 0.047 2 214 559 159 LEU CD2 C 25.574 0.016 2 215 560 160 ILE HG2 H 0.678 0.034 1 216 560 160 ILE HD1 H 0.360 0.026 1 217 560 160 ILE CA C 58.335 0.099 1 218 560 160 ILE CB C 41.968 0.109 1 219 560 160 ILE CG1 C 23.683 0.019 1 220 560 160 ILE CG2 C 16.841 0.117 1 221 560 160 ILE CD1 C 13.268 0.099 1 222 562 162 VAL HG1 H 0.988 0.001 2 223 562 162 VAL HG2 H 0.668 0.001 2 224 562 162 VAL CA C 60.629 0.03 1 225 562 162 VAL CB C 35.892 0.001 1 226 562 162 VAL CG1 C 21.704 0.136 2 227 562 162 VAL CG2 C 20.555 0.15 2 228 564 164 ALA H H 8.605 . 1 229 564 164 ALA HB H 1.186 0.032 1 230 564 164 ALA CA C 49.238 . 1 231 564 164 ALA CB C 23.039 0.042 1 232 574 174 VAL HG1 H 0.992 0.031 2 233 574 174 VAL HG2 H 0.969 0.034 2 234 574 174 VAL CA C 63.465 0.014 1 235 574 174 VAL CB C 33.135 0.038 1 236 574 174 VAL CG1 C 20.768 0.137 2 237 574 174 VAL CG2 C 20.525 0.138 2 238 583 183 ILE HG2 H -0.064 0.03 1 239 583 183 ILE HD1 H 0.140 0.026 1 240 583 183 ILE CA C 63.985 0.009 1 241 583 183 ILE CB C 36.191 0.048 1 242 583 183 ILE CG1 C 27.248 0.035 1 243 583 183 ILE CG2 C 15.933 0.11 1 244 583 183 ILE CD1 C 12.057 0.103 1 245 584 184 ALA H H 8.201 . 1 246 584 184 ALA HB H 1.252 0.035 1 247 584 184 ALA CA C 55.517 . 1 248 584 184 ALA CB C 16.261 0.033 1 249 585 185 ALA H H 7.862 . 1 250 585 185 ALA HB H 1.592 0.03 1 251 585 185 ALA CA C 55.032 . 1 252 585 185 ALA CB C 18.613 0.061 1 253 587 187 LEU HD1 H 0.869 0.001 2 254 587 187 LEU HD2 H 0.801 0.0 2 255 587 187 LEU CA C 57.240 0.019 1 256 587 187 LEU CB C 39.833 0.002 1 257 587 187 LEU CG C 25.881 0.038 1 258 587 187 LEU CD1 C 23.199 0.027 2 259 587 187 LEU CD2 C 23.348 0.051 2 260 588 188 ALA H H 8.135 . 1 261 588 188 ALA HB H 1.467 0.032 1 262 588 188 ALA CA C 54.184 . 1 263 588 188 ALA CB C 16.524 0.049 1 264 589 189 LEU HD1 H 0.635 0.003 1 265 589 189 LEU CA C 56.963 . 1 266 589 189 LEU CD1 C 22.714 0.064 1 267 592 192 ALA H H 8.457 . 1 268 592 192 ALA HB H 1.036 0.031 1 269 592 192 ALA CA C 54.102 . 1 270 592 192 ALA CB C 17.842 0.036 1 271 593 193 ALA H H 7.967 . 1 272 593 193 ALA HB H 1.428 0.036 1 273 593 193 ALA CA C 54.249 . 1 274 593 193 ALA CB C 17.597 0.031 1 275 599 199 VAL HG1 H 0.618 0.037 2 276 599 199 VAL HG2 H 0.809 0.009 2 277 599 199 VAL CA C 58.373 . 1 278 599 199 VAL CB C 35.529 0.011 1 279 599 199 VAL CG1 C 17.480 0.116 2 280 599 199 VAL CG2 C 21.111 0.073 2 281 600 200 ILE HG2 H 0.752 0.027 1 282 600 200 ILE HD1 H 0.675 0.028 1 283 600 200 ILE CA C 59.720 0.047 1 284 600 200 ILE CB C 37.602 0.027 1 285 600 200 ILE CG1 C 27.153 0.108 1 286 600 200 ILE CG2 C 17.323 0.024 1 287 600 200 ILE CD1 C 12.825 0.102 1 288 601 201 LEU HD1 H 0.605 0.004 2 289 601 201 LEU HD2 H 0.555 0.038 2 290 601 201 LEU CB C 45.135 0.048 1 291 601 201 LEU CD1 C 23.768 0.025 2 292 601 201 LEU CD2 C 24.342 0.037 2 293 607 207 VAL HG1 H 0.746 0.029 1 294 607 207 VAL CA C 60.209 . 1 295 607 207 VAL CB C 33.459 . 1 296 607 207 VAL CG1 C 20.167 0.15 1 297 609 209 ILE HG2 H 0.972 0.03 1 298 609 209 ILE HD1 H 0.487 0.024 1 299 609 209 ILE CA C 60.107 0.059 1 300 609 209 ILE CB C 40.942 0.042 1 301 609 209 ILE CG1 C 27.403 0.022 1 302 609 209 ILE CG2 C 19.625 0.15 1 303 609 209 ILE CD1 C 14.301 0.132 1 304 619 219 ILE HG2 H 0.765 0.031 1 305 619 219 ILE HD1 H 0.585 0.03 1 306 619 219 ILE CA C 61.510 0.038 1 307 619 219 ILE CB C 34.936 0.013 1 308 619 219 ILE CG1 C 27.380 . 1 309 619 219 ILE CG2 C 17.430 0.118 1 310 619 219 ILE CD1 C 10.299 0.065 1 311 623 223 VAL HG1 H 0.725 0.035 2 312 623 223 VAL HG2 H 0.489 0.003 2 313 623 223 VAL CA C 67.042 0.013 1 314 623 223 VAL CB C 29.966 . 1 315 623 223 VAL CG1 C 21.959 0.096 2 316 623 223 VAL CG2 C 20.811 0.027 2 317 624 224 THR HG2 H 1.235 0.0 1 318 624 224 THR CA C 65.591 . 1 319 624 224 THR CB C 67.871 . 1 320 624 224 THR CG2 C 21.004 0.023 1 321 630 230 VAL HG1 H 0.345 0.032 1 322 630 230 VAL CA C 62.177 . 1 323 630 230 VAL CB C 31.708 . 1 324 630 230 VAL CG1 C 20.406 0.114 1 325 639 239 ALA H H 7.957 . 1 326 639 239 ALA HB H 1.318 0.033 1 327 639 239 ALA CA C 50.282 . 1 328 639 239 ALA CB C 20.828 0.033 1 329 641 241 VAL HG1 H 0.717 0.032 1 330 641 241 VAL CA C 60.001 . 1 331 641 241 VAL CB C 32.461 . 1 332 641 241 VAL CG1 C 20.551 0.111 1 333 644 244 ALA H H 9.303 . 1 334 644 244 ALA HB H 0.978 0.035 1 335 644 244 ALA CA C 49.518 . 1 336 644 244 ALA CB C 22.653 0.015 1 337 646 246 VAL HG1 H 0.529 0.037 1 338 646 246 VAL CA C 58.035 . 1 339 646 246 VAL CB C 36.571 . 1 340 646 246 VAL CG1 C 20.557 0.144 1 341 655 255 ALA H H 8.755 . 1 342 655 255 ALA HB H 1.596 0.035 1 343 655 255 ALA CA C 55.076 . 1 344 655 255 ALA CB C 17.463 0.055 1 345 656 256 THR HG2 H 1.108 0.001 1 346 656 256 THR CA C 65.262 . 1 347 656 256 THR CB C 67.810 . 1 348 656 256 THR CG2 C 20.943 0.025 1 349 658 258 LEU HD1 H 0.505 0.001 1 350 658 258 LEU CA C 56.727 . 1 351 658 258 LEU CB C 39.823 . 1 352 658 258 LEU CG C 25.529 . 1 353 658 258 LEU CD1 C 23.108 0.038 1 354 662 262 THR HG2 H 0.794 0.0 1 355 662 262 THR CA C 69.256 . 1 356 662 262 THR CG2 C 21.133 0.042 1 357 667 267 THR HG2 H 1.062 0.0 1 358 667 267 THR CA C 60.015 . 1 359 667 267 THR CG2 C 20.421 0.016 1 360 669 269 THR HG2 H 1.010 0.001 1 361 669 269 THR CA C 59.788 . 1 362 669 269 THR CG2 C 20.497 0.012 1 363 676 276 ALA H H 8.971 . 1 364 676 276 ALA HB H 1.518 0.03 1 365 676 276 ALA CA C 49.853 . 1 366 676 276 ALA CB C 23.395 0.028 1 367 678 278 VAL HG1 H 0.902 0.033 2 368 678 278 VAL HG2 H 0.941 0.001 2 369 678 278 VAL CA C 59.558 0.06 1 370 678 278 VAL CB C 31.481 0.043 1 371 678 278 VAL CG1 C 21.515 0.129 2 372 678 278 VAL CG2 C 20.937 0.018 2 373 682 282 ILE HG2 H 0.839 0.031 1 374 682 282 ILE HD1 H 0.782 0.034 1 375 682 282 ILE CA C 62.800 0.004 1 376 682 282 ILE CB C 36.914 0.059 1 377 682 282 ILE CG1 C 27.210 0.01 1 378 682 282 ILE CG2 C 16.070 0.112 1 379 682 282 ILE CD1 C 11.119 0.109 1 380 683 283 ALA H H 8.270 . 1 381 683 283 ALA HB H 1.381 0.032 1 382 683 283 ALA CA C 54.819 . 1 383 683 283 ALA CB C 17.536 0.039 1 384 686 286 ILE HG2 H 0.661 0.033 1 385 686 286 ILE HD1 H 0.216 0.026 1 386 686 286 ILE CA C 64.876 0.155 1 387 686 286 ILE CB C 37.575 0.003 1 388 686 286 ILE CG1 C 27.329 . 1 389 686 286 ILE CG2 C 16.855 0.12 1 390 686 286 ILE CD1 C 12.992 0.103 1 391 687 287 ILE HG2 H 0.838 0.034 1 392 687 287 ILE HD1 H 0.739 0.026 1 393 687 287 ILE CA C 65.086 0.001 1 394 687 287 ILE CB C 37.627 0.03 1 395 687 287 ILE CG1 C 28.671 . 1 396 687 287 ILE CG2 C 16.380 0.122 1 397 687 287 ILE CD1 C 13.047 0.121 1 stop_ save_