data_18435 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the C-terminal domain of Tetrahymena telomerase protein p65 ; _BMRB_accession_number 18435 _BMRB_flat_file_name bmr18435.str _Entry_type original _Submission_date 2012-05-01 _Accession_date 2012-05-01 _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 Singh Mahavir . . 2 Wang Zhonghua . . 3 Koo Bon-Kyung . . 4 Patel Anooj . . 5 Cascio Duilio . . 6 Collins Kathleen . . 7 Feigon Juli . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 666 "13C chemical shifts" 532 "15N chemical shifts" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-15 update BMRB 'update entry citation' 2012-06-18 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22705372 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Singh Mahavir . . 2 Wang Zhonghua . . 3 Koo Bon-Kyung . . 4 Patel Anooj . . 5 Cascio Duilio . . 6 Collins Kathleen . . 7 Feigon Juli . . stop_ _Journal_abbreviation 'Mol. Cell' _Journal_name_full 'Molecular cell' _Journal_volume 47 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16 _Page_last 26 _Year 2012 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C-terminal domain of Tetrahymena telomerase protein p65' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C-terminal domain of Tetrahymena telomerase protein p65' $p65 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_p65 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 15231.342 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 137 _Mol_residue_sequence ; MHHHHHHSVSIDVEIKQNCL IKIINIPQGTLKAEVVLAVR HLGYEFYCDYIDENSNQINS NLIQQDQHPQLNDLLKEGQA MIRFQNSDEQRLAIQKLLNH NNNKLQIEIRGQICDVISTI PEDEEKNYWNYIKFKKN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 461 MET 2 462 HIS 3 463 HIS 4 464 HIS 5 465 HIS 6 466 HIS 7 467 HIS 8 468 SER 9 469 VAL 10 470 SER 11 471 ILE 12 472 ASP 13 473 VAL 14 474 GLU 15 475 ILE 16 476 LYS 17 477 GLN 18 478 ASN 19 479 CYS 20 480 LEU 21 481 ILE 22 482 LYS 23 483 ILE 24 484 ILE 25 485 ASN 26 486 ILE 27 487 PRO 28 488 GLN 29 489 GLY 30 490 THR 31 491 LEU 32 492 LYS 33 493 ALA 34 494 GLU 35 495 VAL 36 496 VAL 37 497 LEU 38 498 ALA 39 499 VAL 40 500 ARG 41 501 HIS 42 502 LEU 43 503 GLY 44 504 TYR 45 505 GLU 46 506 PHE 47 507 TYR 48 508 CYS 49 509 ASP 50 510 TYR 51 511 ILE 52 512 ASP 53 513 GLU 54 514 ASN 55 515 SER 56 516 ASN 57 517 GLN 58 518 ILE 59 519 ASN 60 520 SER 61 521 ASN 62 522 LEU 63 523 ILE 64 524 GLN 65 525 GLN 66 526 ASP 67 527 GLN 68 528 HIS 69 529 PRO 70 530 GLN 71 531 LEU 72 532 ASN 73 533 ASP 74 534 LEU 75 535 LEU 76 536 LYS 77 537 GLU 78 538 GLY 79 539 GLN 80 540 ALA 81 541 MET 82 542 ILE 83 543 ARG 84 544 PHE 85 545 GLN 86 546 ASN 87 547 SER 88 548 ASP 89 549 GLU 90 550 GLN 91 551 ARG 92 552 LEU 93 553 ALA 94 554 ILE 95 555 GLN 96 556 LYS 97 557 LEU 98 558 LEU 99 559 ASN 100 560 HIS 101 561 ASN 102 562 ASN 103 563 ASN 104 564 LYS 105 565 LEU 106 566 GLN 107 567 ILE 108 568 GLU 109 569 ILE 110 570 ARG 111 571 GLY 112 572 GLN 113 573 ILE 114 574 CYS 115 575 ASP 116 576 VAL 117 577 ILE 118 578 SER 119 579 THR 120 580 ILE 121 581 PRO 122 582 GLU 123 583 ASP 124 584 GLU 125 585 GLU 126 586 LYS 127 587 ASN 128 588 TYR 129 589 TRP 130 590 ASN 131 591 TYR 132 592 ILE 133 593 LYS 134 594 PHE 135 595 LYS 136 596 LYS 137 597 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 PDB 2LSL "Solution Structure Of The C-Terminal Domain Of Tetrahymena Telomerase Protein P65" 100.00 137 100.00 100.00 1.23e-93 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $p65 'Tetrahymena thermophila' 5911 Bacteria . Tetrahymena thermophila TAP65 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 $p65 'recombinant technology' . Escherichia coli . 'pET30 LIC' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p65 1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % '[U-100% 2H]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.01 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p65 1 mM 'natural abundance' D2O 100 % '[U-100% 2H]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.01 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_2 save_ save_3D_HCCH-COSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-COSY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_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 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HNCACO' '3D HCCH-TOCSY' '3D HCCH-COSY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'C-terminal domain of Tetrahymena telomerase protein p65' _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 1 368 8 SER HA H 4.38 0.02 1 2 368 8 SER HB2 H 3.75 0.02 2 3 368 8 SER HB3 H 3.75 0.02 2 4 368 8 SER C C 174.25 0.3 1 5 368 8 SER CA C 58.24 0.3 1 6 368 8 SER CB C 63.75 0.3 1 7 369 9 VAL H H 8.09 0.02 1 8 369 9 VAL HA H 4.1 0.02 1 9 369 9 VAL HB H 2.02 0.02 1 10 369 9 VAL HG1 H 0.83 0.02 2 11 369 9 VAL HG2 H 0.83 0.02 2 12 369 9 VAL C C 175.94 0.3 1 13 369 9 VAL CA C 62.05 0.3 1 14 369 9 VAL CB C 32.77 0.3 1 15 369 9 VAL CG1 C 17.71 0.3 1 16 369 9 VAL CG2 C 18.6 0.3 1 17 369 9 VAL N N 121.23 0.3 1 18 370 10 SER H H 8.28 0.02 1 19 370 10 SER HA H 4.41 0.02 1 20 370 10 SER HB2 H 3.74 0.02 2 21 370 10 SER HB3 H 3.75 0.02 2 22 370 10 SER C C 174.32 0.3 1 23 370 10 SER CA C 58.12 0.3 1 24 370 10 SER CB C 63.67 0.3 1 25 370 10 SER N N 119.42 0.3 1 26 371 11 ILE H H 8.08 0.02 1 27 371 11 ILE HA H 4.11 0.02 1 28 371 11 ILE HB H 1.78 0.02 1 29 371 11 ILE HG12 H 1.07 0.02 1 30 371 11 ILE HG13 H 1.07 0.02 1 31 371 11 ILE HG2 H 0.8 0.02 1 32 371 11 ILE HD1 H 0.53 0.02 1 33 371 11 ILE C C 175.56 0.3 1 34 371 11 ILE CA C 61.09 0.3 1 35 371 11 ILE CB C 38.99 0.3 1 36 371 11 ILE CG1 C 24.49 0.3 1 37 371 11 ILE CG2 C 14.97 0.3 1 38 371 11 ILE CD1 C 10.65 0.3 1 39 371 11 ILE N N 122.2 0.3 1 40 372 12 ASP H H 8.25 0.02 1 41 372 12 ASP HA H 4.55 0.02 1 42 372 12 ASP HB2 H 2.5 0.02 2 43 372 12 ASP HB3 H 2.61 0.02 2 44 372 12 ASP C C 175.96 0.3 1 45 372 12 ASP CA C 54.39 0.3 1 46 372 12 ASP CB C 41.19 0.3 1 47 372 12 ASP N N 124.04 0.3 1 48 373 13 VAL H H 7.93 0.02 1 49 373 13 VAL HA H 4.03 0.02 1 50 373 13 VAL HB H 2.01 0.02 1 51 373 13 VAL HG1 H 0.83 0.02 2 52 373 13 VAL HG2 H 0.85 0.02 2 53 373 13 VAL C C 175.23 0.3 1 54 373 13 VAL CA C 61.95 0.3 1 55 373 13 VAL CB C 32.87 0.3 1 56 373 13 VAL CG1 C 18.5 0.3 1 57 373 13 VAL CG2 C 18.5 0.3 1 58 373 13 VAL N N 119.83 0.3 1 59 374 14 GLU H H 8.19 0.02 1 60 374 14 GLU HA H 4.12 0.02 1 61 374 14 GLU HB2 H 1.76 0.02 2 62 374 14 GLU HB3 H 1.82 0.02 2 63 374 14 GLU HG2 H 2.17 0.02 2 64 374 14 GLU HG3 H 2.17 0.02 2 65 374 14 GLU C C 175.51 0.3 1 66 374 14 GLU CA C 55.92 0.3 1 67 374 14 GLU CB C 30.38 0.3 1 68 374 14 GLU CG C 33.57 0.3 1 69 374 14 GLU N N 124.72 0.3 1 70 375 15 ILE H H 7.85 0.02 1 71 375 15 ILE HA H 2.69 0.02 1 72 375 15 ILE HB H 1.22 0.02 1 73 375 15 ILE HG12 H 0.57 0.02 1 74 375 15 ILE HG13 H 1.03 0.02 1 75 375 15 ILE HG2 H 0.61 0.02 1 76 375 15 ILE HD1 H 0.17 0.02 1 77 375 15 ILE C C 175.38 0.3 1 78 375 15 ILE CA C 61.38 0.3 1 79 375 15 ILE CB C 38.32 0.3 1 80 375 15 ILE CG1 C 25.56 0.3 1 81 375 15 ILE CG2 C 24.72 0.3 1 82 375 15 ILE CD1 C 13.62 0.3 1 83 375 15 ILE N N 122.28 0.3 1 84 376 16 LYS H H 6.03 0.02 1 85 376 16 LYS HA H 4.25 0.02 1 86 376 16 LYS HB2 H 1.66 0.02 2 87 376 16 LYS HB3 H 1.62 0.02 2 88 376 16 LYS C C 175.52 0.3 1 89 376 16 LYS CA C 54.58 0.3 1 90 376 16 LYS CB C 33.64 0.3 1 91 376 16 LYS CG C 21.91 0.3 1 92 376 16 LYS N N 125.62 0.3 1 93 377 17 GLN H H 8.37 0.02 1 94 377 17 GLN HA H 4.22 0.02 1 95 377 17 GLN HB2 H 1.91 0.02 2 96 377 17 GLN HB3 H 2.03 0.02 2 97 377 17 GLN HG2 H 2.29 0.02 2 98 377 17 GLN HG3 H 2.29 0.02 2 99 377 17 GLN C C 176.29 0.3 1 100 377 17 GLN CA C 56.5 0.3 1 101 377 17 GLN CB C 30.1 0.3 1 102 377 17 GLN CG C 31.63 0.3 1 103 377 17 GLN N N 122.16 0.3 1 104 378 18 ASN H H 9.42 0.02 1 105 378 18 ASN HA H 4.69 0.02 1 106 378 18 ASN HB2 H 2.85 0.02 2 107 378 18 ASN HB3 H 3.05 0.02 2 108 378 18 ASN HD21 H 7.63 0.02 2 109 378 18 ASN HD22 H 6.85 0.02 2 110 378 18 ASN C C 173.39 0.3 1 111 378 18 ASN CA C 54.87 0.3 1 112 378 18 ASN CB C 37.65 0.3 1 113 378 18 ASN N N 117.5 0.3 1 114 379 19 CYS H H 8.36 0.02 1 115 379 19 CYS HA H 4.62 0.02 1 116 379 19 CYS HB2 H 3.02 0.02 2 117 379 19 CYS HB3 H 3.22 0.02 2 118 379 19 CYS C C 174.19 0.3 1 119 379 19 CYS CA C 59.94 0.3 1 120 379 19 CYS CB C 29.52 0.3 1 121 379 19 CYS N N 109.37 0.3 1 122 380 20 LEU H H 8.3 0.02 1 123 380 20 LEU HA H 5.8 0.02 1 124 380 20 LEU HB2 H 1.34 0.02 2 125 380 20 LEU HB3 H 1.81 0.02 2 126 380 20 LEU HG H 1.85 0.02 1 127 380 20 LEU HD1 H 0.73 0.02 2 128 380 20 LEU HD2 H 0.54 0.02 2 129 380 20 LEU C C 179.19 0.3 1 130 380 20 LEU CA C 54.2 0.3 1 131 380 20 LEU CB C 44.35 0.3 1 132 380 20 LEU CG C 24.01 0.3 1 133 380 20 LEU CD1 C 23.28 0.3 1 134 380 20 LEU CD2 C 20.6 0.3 1 135 380 20 LEU N N 119.79 0.3 1 136 381 21 ILE H H 8.67 0.02 1 137 381 21 ILE HA H 4.61 0.02 1 138 381 21 ILE HB H 1.68 0.02 1 139 381 21 ILE HG12 H 1.17 0.02 1 140 381 21 ILE HG13 H 1.17 0.02 1 141 381 21 ILE HG2 H 0.87 0.02 1 142 381 21 ILE HD1 H 0.57 0.02 1 143 381 21 ILE C C 172.22 0.3 1 144 381 21 ILE CA C 61.38 0.3 1 145 381 21 ILE CB C 41.67 0.3 1 146 381 21 ILE CG1 C 23.77 0.3 1 147 381 21 ILE CG2 C 15.9 0.3 1 148 381 21 ILE CD1 C 9.66 0.3 1 149 381 21 ILE N N 111.7 0.3 1 150 382 22 LYS H H 8.57 0.02 1 151 382 22 LYS HA H 5.41 0.02 1 152 382 22 LYS HB2 H 1.54 0.02 2 153 382 22 LYS HB3 H 1.54 0.02 2 154 382 22 LYS HG2 H 1.33 0.02 2 155 382 22 LYS HG3 H 1.33 0.02 2 156 382 22 LYS C C 174.55 0.3 1 157 382 22 LYS CA C 54.2 0.3 1 158 382 22 LYS CB C 37.46 0.3 1 159 382 22 LYS CG C 22.11 0.3 1 160 382 22 LYS CD C 27.73 0.3 1 161 382 22 LYS N N 122.5 0.3 1 162 383 23 ILE H H 9.15 0.02 1 163 383 23 ILE HA H 4.74 0.02 1 164 383 23 ILE HB H 1.42 0.02 1 165 383 23 ILE HG12 H 1.43 0.02 1 166 383 23 ILE HG13 H 1.43 0.02 1 167 383 23 ILE HG2 H 0.75 0.02 1 168 383 23 ILE HD1 H 0.66 0.02 1 169 383 23 ILE C C 175.43 0.3 1 170 383 23 ILE CA C 60.13 0.3 1 171 383 23 ILE CB C 40.33 0.3 1 172 383 23 ILE CG1 C 24.76 0.3 1 173 383 23 ILE CG2 C 15.39 0.3 1 174 383 23 ILE CD1 C 11.66 0.3 1 175 383 23 ILE N N 126.61 0.3 1 176 384 24 ILE H H 8.68 0.02 1 177 384 24 ILE HA H 5.25 0.02 1 178 384 24 ILE HB H 1.99 0.02 1 179 384 24 ILE HG12 H 1.33 0.02 1 180 384 24 ILE HG13 H 1.33 0.02 1 181 384 24 ILE HG2 H 0.77 0.02 1 182 384 24 ILE HD1 H 0.74 0.02 1 183 384 24 ILE C C 174.19 0.3 1 184 384 24 ILE CA C 59.94 0.3 1 185 384 24 ILE CB C 41.38 0.3 1 186 384 24 ILE CG1 C 24.16 0.3 1 187 384 24 ILE CG2 C 15.89 0.3 1 188 384 24 ILE CD1 C 10.96 0.3 1 189 384 24 ILE N N 118.16 0.3 1 190 385 25 ASN H H 8.21 0.02 1 191 385 25 ASN HA H 4.3 0.02 1 192 385 25 ASN HB2 H 3.04 0.02 2 193 385 25 ASN HB3 H 3.22 0.02 2 194 385 25 ASN HD21 H 8.02 0.02 2 195 385 25 ASN HD22 H 6.88 0.02 2 196 385 25 ASN C C 175.05 0.3 1 197 385 25 ASN CA C 54.2 0.3 1 198 385 25 ASN CB C 36.7 0.3 1 199 385 25 ASN N N 113.02 0.3 1 200 386 26 ILE H H 9.08 0.02 1 201 386 26 ILE HA H 4.19 0.02 1 202 386 26 ILE HB H 1.48 0.02 1 203 386 26 ILE C C 176.09 0.3 1 204 386 26 ILE CA C 60.61 0.3 1 205 386 26 ILE CB C 38.71 0.3 1 206 386 26 ILE N N 122.07 0.3 1 207 387 27 PRO HA H 4.24 0.02 1 208 387 27 PRO HB2 H 1.65 0.02 2 209 387 27 PRO HB3 H 2.26 0.02 2 210 387 27 PRO HG2 H 1.84 0.02 2 211 387 27 PRO HG3 H 1.84 0.02 2 212 387 27 PRO HD2 H 3.81 0.02 2 213 387 27 PRO HD3 H 3.81 0.02 2 214 387 27 PRO C C 177.89 0.3 1 215 387 27 PRO CA C 63.04 0.3 1 216 387 27 PRO CB C 31.8 0.3 1 217 387 27 PRO CG C 25.18 0.3 1 218 387 27 PRO CD C 48.45 0.3 1 219 388 28 GLN H H 8.82 0.02 1 220 388 28 GLN HA H 4.17 0.02 1 221 388 28 GLN HB2 H 1.97 0.02 2 222 388 28 GLN HB3 H 1.98 0.02 2 223 388 28 GLN HG2 H 2.33 0.02 2 224 388 28 GLN HG3 H 2.33 0.02 2 225 388 28 GLN C C 176.82 0.3 1 226 388 28 GLN CA C 57.64 0.3 1 227 388 28 GLN CB C 28.37 0.3 1 228 388 28 GLN CG C 31.09 0.3 1 229 388 28 GLN N N 125.84 0.3 1 230 389 29 GLY H H 9.26 0.02 1 231 389 29 GLY HA2 H 3.63 0.02 2 232 389 29 GLY HA3 H 4.21 0.02 2 233 389 29 GLY C C 174.67 0.3 1 234 389 29 GLY CA C 44.73 0.3 1 235 389 29 GLY N N 114.5 0.3 1 236 390 30 THR H H 7.47 0.02 1 237 390 30 THR HA H 3.92 0.02 1 238 390 30 THR HB H 3.83 0.02 1 239 390 30 THR HG2 H 0.94 0.02 1 240 390 30 THR C C 175.38 0.3 1 241 390 30 THR CA C 64.34 0.3 1 242 390 30 THR CB C 68.17 0.3 1 243 390 30 THR CG2 C 19.9 0.3 1 244 390 30 THR N N 117.92 0.3 1 245 391 31 LEU H H 9.4 0.02 1 246 391 31 LEU HA H 4.74 0.02 1 247 391 31 LEU HB2 H 1.69 0.02 2 248 391 31 LEU HB3 H 1.8 0.02 2 249 391 31 LEU HG H 1.81 0.02 1 250 391 31 LEU HD1 H 0.91 0.02 2 251 391 31 LEU HD2 H 0.91 0.02 2 252 391 31 LEU C C 179.07 0.3 1 253 391 31 LEU CA C 54.39 0.3 1 254 391 31 LEU CB C 42.44 0.3 1 255 391 31 LEU CG C 24.8 0.3 1 256 391 31 LEU CD1 C 22.82 0.3 1 257 391 31 LEU CD2 C 20.02 0.3 1 258 391 31 LEU N N 131.72 0.3 1 259 392 32 LYS H H 9.92 0.02 1 260 392 32 LYS HA H 3.48 0.02 1 261 392 32 LYS HB2 H 1.94 0.02 2 262 392 32 LYS HB3 H 2.03 0.02 2 263 392 32 LYS HG2 H 1.41 0.02 2 264 392 32 LYS HG3 H 1.41 0.02 2 265 392 32 LYS HD2 H 1.86 0.02 2 266 392 32 LYS HD3 H 1.86 0.02 2 267 392 32 LYS HE2 H 1.83 0.02 2 268 392 32 LYS HE3 H 1.83 0.02 2 269 392 32 LYS C C 178.26 0.3 1 270 392 32 LYS CA C 61.18 0.3 1 271 392 32 LYS CB C 31.82 0.3 1 272 392 32 LYS CG C 23.36 0.3 1 273 392 32 LYS CD C 27.12 0.3 1 274 392 32 LYS CE C 39.98 0.3 1 275 392 32 LYS N N 125.44 0.3 1 276 393 33 ALA H H 8.71 0.02 1 277 393 33 ALA HA H 3.95 0.02 1 278 393 33 ALA HB H 1.35 0.02 1 279 393 33 ALA C C 180.33 0.3 1 280 393 33 ALA CA C 55.16 0.3 1 281 393 33 ALA CB C 18.62 0.3 1 282 393 33 ALA N N 117 0.3 1 283 394 34 GLU H H 7.4 0.02 1 284 394 34 GLU HA H 3.95 0.02 1 285 394 34 GLU HB2 H 1.81 0.02 2 286 394 34 GLU HB3 H 2.39 0.02 2 287 394 34 GLU HG2 H 2.21 0.02 2 288 394 34 GLU HG3 H 2.21 0.02 2 289 394 34 GLU C C 179.17 0.3 1 290 394 34 GLU CA C 58.79 0.3 1 291 394 34 GLU CB C 29.9 0.3 1 292 394 34 GLU CG C 35.21 0.3 1 293 394 34 GLU N N 115.33 0.3 1 294 395 35 VAL H H 7.16 0.02 1 295 395 35 VAL HA H 3.26 0.02 1 296 395 35 VAL HB H 1.94 0.02 1 297 395 35 VAL HG1 H 0.41 0.02 2 298 395 35 VAL HG2 H 0.35 0.02 2 299 395 35 VAL C C 177 0.3 1 300 395 35 VAL CA C 66.45 0.3 1 301 395 35 VAL CB C 31.24 0.3 1 302 395 35 VAL CG1 C 19.22 0.3 1 303 395 35 VAL CG2 C 18.63 0.3 1 304 395 35 VAL N N 121.91 0.3 1 305 396 36 VAL H H 8.13 0.02 1 306 396 36 VAL HA H 3.45 0.02 1 307 396 36 VAL HB H 2 0.02 1 308 396 36 VAL HG1 H 0.9 0.02 2 309 396 36 VAL HG2 H 0.97 0.02 2 310 396 36 VAL C C 177 0.3 1 311 396 36 VAL CA C 66.83 0.3 1 312 396 36 VAL CB C 31.91 0.3 1 313 396 36 VAL CG1 C 18.35 0.3 1 314 396 36 VAL CG2 C 20.86 0.3 1 315 396 36 VAL N N 117.39 0.3 1 316 397 37 LEU H H 7.84 0.02 1 317 397 37 LEU HA H 3.85 0.02 1 318 397 37 LEU HB2 H 1.64 0.02 2 319 397 37 LEU HB3 H 1.69 0.02 2 320 397 37 LEU HG H 1.61 0.02 1 321 397 37 LEU HD1 H 0.88 0.02 2 322 397 37 LEU HD2 H 0.88 0.02 2 323 397 37 LEU C C 178.23 0.3 1 324 397 37 LEU CA C 58.41 0.3 1 325 397 37 LEU CB C 42.05 0.3 1 326 397 37 LEU CG C 24.19 0.3 1 327 397 37 LEU CD1 C 21.97 0.3 1 328 397 37 LEU CD2 C 21.97 0.3 1 329 397 37 LEU N N 118.76 0.3 1 330 398 38 ALA H H 7.06 0.02 1 331 398 38 ALA HA H 4.11 0.02 1 332 398 38 ALA HB H 1.45 0.02 1 333 398 38 ALA C C 179.97 0.3 1 334 398 38 ALA CA C 54.78 0.3 1 335 398 38 ALA CB C 18.81 0.3 1 336 398 38 ALA N N 118.67 0.3 1 337 399 39 VAL H H 7.62 0.02 1 338 399 39 VAL HA H 3.38 0.02 1 339 399 39 VAL HB H 1.39 0.02 1 340 399 39 VAL HG1 H 0.18 0.02 2 341 399 39 VAL HG2 H 0.51 0.02 2 342 399 39 VAL C C 179.02 0.3 1 343 399 39 VAL CA C 64.91 0.3 1 344 399 39 VAL CB C 31.44 0.3 1 345 399 39 VAL CG1 C 18.17 0.3 1 346 399 39 VAL CG2 C 20.33 0.3 1 347 399 39 VAL N N 117.17 0.3 1 348 400 40 ARG H H 8.9 0.02 1 349 400 40 ARG HA H 4.22 0.02 1 350 400 40 ARG HB2 H 2 0.02 2 351 400 40 ARG HB3 H 2.07 0.02 2 352 400 40 ARG HG2 H 1.83 0.02 2 353 400 40 ARG HG3 H 1.83 0.02 2 354 400 40 ARG HD2 H 3.11 0.02 2 355 400 40 ARG HD3 H 3.11 0.02 2 356 400 40 ARG C C 178.56 0.3 1 357 400 40 ARG CA C 59.37 0.3 1 358 400 40 ARG CB C 29.81 0.3 1 359 400 40 ARG CG C 24.82 0.3 1 360 400 40 ARG CD C 40.9 0.3 1 361 400 40 ARG N N 124.05 0.3 1 362 401 41 HIS H H 7.31 0.02 1 363 401 41 HIS HA H 4.39 0.02 1 364 401 41 HIS HB2 H 3.01 0.02 2 365 401 41 HIS HB3 H 3.12 0.02 2 366 401 41 HIS HD2 H 7.06 0.02 1 367 401 41 HIS C C 176.57 0.3 1 368 401 41 HIS CA C 58.44 0.3 1 369 401 41 HIS CB C 30.38 0.3 1 370 401 41 HIS CD2 C 117.8 0.3 1 371 401 41 HIS N N 116.67 0.3 1 372 402 42 LEU H H 7.82 0.02 1 373 402 42 LEU HA H 4.02 0.02 1 374 402 42 LEU HB2 H 1.53 0.02 2 375 402 42 LEU HB3 H 2.31 0.02 2 376 402 42 LEU HG H 1.41 0.02 1 377 402 42 LEU HD1 H 1.15 0.02 2 378 402 42 LEU HD2 H 0.82 0.02 2 379 402 42 LEU C C 177.55 0.3 1 380 402 42 LEU CA C 56.5 0.3 1 381 402 42 LEU CB C 40.24 0.3 1 382 402 42 LEU CG C 24.26 0.3 1 383 402 42 LEU CD1 C 22.63 0.3 1 384 402 42 LEU CD2 C 18.93 0.3 1 385 402 42 LEU N N 115.95 0.3 1 386 403 43 GLY H H 7.34 0.02 1 387 403 43 GLY HA2 H 3.51 0.02 2 388 403 43 GLY HA3 H 3.75 0.02 2 389 403 43 GLY C C 173.61 0.3 1 390 403 43 GLY CA C 45.59 0.3 1 391 403 43 GLY N N 101.04 0.3 1 392 404 44 TYR H H 8.09 0.02 1 393 404 44 TYR HA H 4.89 0.02 1 394 404 44 TYR HB2 H 2.65 0.02 2 395 404 44 TYR HB3 H 3.53 0.02 2 396 404 44 TYR C C 176.57 0.3 1 397 404 44 TYR CA C 57.07 0.3 1 398 404 44 TYR CB C 41.19 0.3 1 399 404 44 TYR N N 119 0.3 1 400 405 45 GLU H H 9.62 0.02 1 401 405 45 GLU HA H 4.19 0.02 1 402 405 45 GLU HB2 H 1.93 0.02 2 403 405 45 GLU C C 175.61 0.3 1 404 405 45 GLU CA C 57.17 0.3 1 405 405 45 GLU CB C 30.1 0.3 1 406 405 45 GLU CG C 33.48 0.3 1 407 405 45 GLU N N 124.77 0.3 1 408 406 46 PHE H H 7.45 0.02 1 409 406 46 PHE HA H 5.06 0.02 1 410 406 46 PHE HB2 H 2.13 0.02 2 411 406 46 PHE HB3 H 2.6 0.02 2 412 406 46 PHE C C 172.75 0.3 1 413 406 46 PHE CA C 55.92 0.3 1 414 406 46 PHE CB C 40.62 0.3 1 415 406 46 PHE N N 115.61 0.3 1 416 407 47 TYR H H 8.73 0.02 1 417 407 47 TYR HA H 4.38 0.02 1 418 407 47 TYR HB2 H 2.68 0.02 2 419 407 47 TYR HB3 H 3.07 0.02 2 420 407 47 TYR C C 174.7 0.3 1 421 407 47 TYR CA C 56.5 0.3 1 422 407 47 TYR CB C 40.81 0.3 1 423 407 47 TYR N N 118.9 0.3 1 424 408 48 CYS HA H 5.35 0.02 1 425 408 48 CYS HB2 H 2.63 0.02 2 426 408 48 CYS HB3 H 2.63 0.02 2 427 408 48 CYS C C 172.63 0.3 1 428 408 48 CYS CA C 56.43 0.3 1 429 408 48 CYS CB C 30 0.3 1 430 409 49 ASP H H 9.02 0.02 1 431 409 49 ASP HA H 5.24 0.02 1 432 409 49 ASP HB2 H 2.5 0.02 2 433 409 49 ASP HB3 H 2.59 0.02 2 434 409 49 ASP C C 173.84 0.3 1 435 409 49 ASP CA C 53.91 0.3 1 436 409 49 ASP CB C 44.92 0.3 1 437 409 49 ASP N N 129.29 0.3 1 438 410 50 TYR H H 8.5 0.02 1 439 410 50 TYR HA H 4.8 0.02 1 440 410 50 TYR HB2 H 2.26 0.02 2 441 410 50 TYR HB3 H 3.08 0.02 2 442 410 50 TYR C C 172.8 0.3 1 443 410 50 TYR CA C 57.17 0.3 1 444 410 50 TYR CB C 42.63 0.3 1 445 410 50 TYR N N 122.83 0.3 1 446 411 51 ILE H H 7.88 0.02 1 447 411 51 ILE HA H 3.86 0.02 1 448 411 51 ILE HB H 1.59 0.02 1 449 411 51 ILE HG12 H 0.88 0.02 1 450 411 51 ILE HG13 H 1.23 0.02 1 451 411 51 ILE HG2 H 0.68 0.02 1 452 411 51 ILE HD1 H 0.58 0.02 1 453 411 51 ILE C C 173.28 0.3 1 454 411 51 ILE CA C 60.51 0.3 1 455 411 51 ILE CB C 37.27 0.3 1 456 411 51 ILE CG1 C 24.66 0.3 1 457 411 51 ILE CG2 C 14.75 0.3 1 458 411 51 ILE CD1 C 9.69 0.3 1 459 411 51 ILE N N 128.91 0.3 1 460 412 52 ASP H H 7.77 0.02 1 461 412 52 ASP HA H 4.49 0.02 1 462 412 52 ASP HB2 H 2.6 0.02 2 463 412 52 ASP HB3 H 2.93 0.02 2 464 412 52 ASP C C 176.67 0.3 1 465 412 52 ASP CA C 52.67 0.3 1 466 412 52 ASP CB C 42.24 0.3 1 467 412 52 ASP N N 125.34 0.3 1 468 413 53 GLU H H 8.43 0.02 1 469 413 53 GLU HA H 4.18 0.02 1 470 413 53 GLU HB2 H 1.96 0.02 2 471 413 53 GLU HB3 H 1.96 0.02 2 472 413 53 GLU C C 176.59 0.3 1 473 413 53 GLU CA C 57.36 0.3 1 474 413 53 GLU CB C 30 0.3 1 475 413 53 GLU CG C 33.06 0.3 1 476 413 53 GLU N N 119.05 0.3 1 477 414 54 ASN H H 8.54 0.02 1 478 414 54 ASN HA H 4.71 0.02 1 479 414 54 ASN HB2 H 2.8 0.02 2 480 414 54 ASN HB3 H 2.8 0.02 2 481 414 54 ASN C C 176.01 0.3 1 482 414 54 ASN CA C 53.82 0.3 1 483 414 54 ASN CB C 39.09 0.3 1 484 414 54 ASN N N 118.87 0.3 1 485 415 55 SER H H 8.1 0.02 1 486 415 55 SER HA H 4.38 0.02 1 487 415 55 SER HB2 H 3.9 0.02 2 488 415 55 SER HB3 H 3.9 0.02 2 489 415 55 SER C C 174.54 0.3 1 490 415 55 SER CA C 59.37 0.3 1 491 415 55 SER CB C 63.58 0.3 1 492 415 55 SER N N 116.16 0.3 1 493 416 56 ASN H H 8.29 0.02 1 494 416 56 ASN HA H 4.46 0.02 1 495 416 56 ASN HB2 H 2.56 0.02 2 496 416 56 ASN HB3 H 2.56 0.02 2 497 416 56 ASN C C 179.19 0.3 1 498 416 56 ASN CA C 53.53 0.3 1 499 416 56 ASN CB C 38.51 0.3 1 500 416 56 ASN N N 120.25 0.3 1 501 417 57 GLN H H 8.12 0.02 1 502 417 57 GLN C C 176.11 0.3 1 503 417 57 GLN CA C 55.92 0.3 1 504 417 57 GLN CB C 29.24 0.3 1 505 417 57 GLN N N 119.88 0.3 1 506 418 58 ILE H H 7.99 0.02 1 507 418 58 ILE C C 176.09 0.3 1 508 418 58 ILE CA C 61.66 0.3 1 509 418 58 ILE CB C 38.51 0.3 1 510 418 58 ILE N N 120.87 0.3 1 511 419 59 ASN H H 8.42 0.02 1 512 419 59 ASN HA H 4.7 0.02 1 513 419 59 ASN HB2 H 2.77 0.02 2 514 419 59 ASN C C 175.48 0.3 1 515 419 59 ASN CA C 53.15 0.3 1 516 419 59 ASN CB C 38.71 0.3 1 517 419 59 ASN N N 122.31 0.3 1 518 420 60 SER H H 8.27 0.02 1 519 420 60 SER HA H 4.31 0.02 1 520 420 60 SER HB2 H 3.83 0.02 2 521 420 60 SER HB3 H 3.83 0.02 2 522 420 60 SER C C 174.48 0.3 1 523 420 60 SER CA C 58.89 0.3 1 524 420 60 SER CB C 63.67 0.3 1 525 420 60 SER N N 116.81 0.3 1 526 443 61 ASN H H 8.38 0.02 1 527 443 61 ASN HA H 4.63 0.02 1 528 443 61 ASN HB2 H 2.76 0.02 2 529 443 61 ASN HB3 H 2.76 0.02 2 530 443 61 ASN C C 175.1 0.3 1 531 443 61 ASN CA C 53.53 0.3 1 532 443 61 ASN CB C 38.51 0.3 1 533 443 61 ASN N N 119.98 0.3 1 534 444 62 LEU H H 7.91 0.02 1 535 444 62 LEU HA H 4.26 0.02 1 536 444 62 LEU HB2 H 1.54 0.02 2 537 444 62 LEU HB3 H 1.54 0.02 2 538 444 62 LEU HG H 1.57 0.02 1 539 444 62 LEU HD1 H 0.77 0.02 2 540 444 62 LEU HD2 H 0.66 0.02 2 541 444 62 LEU C C 177.22 0.3 1 542 444 62 LEU CA C 55.54 0.3 1 543 444 62 LEU CB C 42.15 0.3 1 544 444 62 LEU CG C 24.23 0.3 1 545 444 62 LEU CD1 C 22.3 0.3 1 546 444 62 LEU CD2 C 20.8 0.3 1 547 444 62 LEU N N 121.14 0.3 1 548 445 63 ILE H H 7.91 0.02 1 549 445 63 ILE HA H 4.11 0.02 1 550 445 63 ILE HB H 1.81 0.02 1 551 445 63 ILE HG12 H 1.09 0.02 1 552 445 63 ILE HG13 H 1.32 0.02 1 553 445 63 ILE HG2 H 0.81 0.02 1 554 445 63 ILE HD1 H 0.75 0.02 1 555 445 63 ILE C C 176.16 0.3 1 556 445 63 ILE CA C 61.18 0.3 1 557 445 63 ILE CB C 38.42 0.3 1 558 445 63 ILE CG1 C 24.68 0.3 1 559 445 63 ILE CG2 C 14.98 0.3 1 560 445 63 ILE CD1 C 10.35 0.3 1 561 445 63 ILE N N 120.76 0.3 1 562 446 64 GLN H H 8.31 0.02 1 563 446 64 GLN HA H 4.27 0.02 1 564 446 64 GLN HB2 H 1.97 0.02 2 565 446 64 GLN HB3 H 1.97 0.02 2 566 446 64 GLN C C 175.83 0.3 1 567 446 64 GLN CA C 55.83 0.3 1 568 446 64 GLN CB C 29.33 0.3 1 569 446 64 GLN CG C 31.12 0.3 1 570 446 64 GLN N N 123.86 0.3 1 571 447 65 GLN H H 8.37 0.02 1 572 447 65 GLN HA H 4.22 0.02 1 573 447 65 GLN HB2 H 1.9 0.02 2 574 447 65 GLN HB3 H 2.01 0.02 2 575 447 65 GLN C C 175.62 0.3 1 576 447 65 GLN CA C 56.11 0.3 1 577 447 65 GLN CB C 29.62 0.3 1 578 447 65 GLN CG C 31.04 0.3 1 579 447 65 GLN N N 121.39 0.3 1 580 448 66 ASP H H 8.25 0.02 1 581 448 66 ASP HA H 4.49 0.02 1 582 448 66 ASP HB2 H 2.58 0.02 2 583 448 66 ASP HB3 H 2.58 0.02 2 584 448 66 ASP C C 175.91 0.3 1 585 448 66 ASP CA C 54.39 0.3 1 586 448 66 ASP CB C 41.1 0.3 1 587 448 66 ASP N N 120.41 0.3 1 588 449 67 GLN H H 8.18 0.02 1 589 449 67 GLN HA H 4.14 0.02 1 590 449 67 GLN HB2 H 1.8 0.02 2 591 449 67 GLN C C 175.3 0.3 1 592 449 67 GLN CA C 55.91 0.3 1 593 449 67 GLN CB C 29 0.3 1 594 449 67 GLN CG C 31.12 0.30 1 595 449 67 GLN N N 118.73 0.3 1 596 450 68 HIS H H 7.99 0.02 1 597 450 68 HIS HA H 4.06 0.02 1 598 450 68 HIS C C 172.94 0.3 1 599 450 68 HIS CA C 54.03 0.3 1 600 450 68 HIS CB C 29.59 0.3 1 601 450 68 HIS N N 120.25 0.3 1 602 451 69 PRO HA H 4.38 0.02 1 603 451 69 PRO HB2 H 1.79 0.02 2 604 451 69 PRO HB3 H 2.29 0.02 2 605 451 69 PRO HG2 H 2.09 0.02 2 606 451 69 PRO HG3 H 1.97 0.02 2 607 451 69 PRO HD2 H 3.74 0.02 2 608 451 69 PRO HD3 H 3.74 0.02 2 609 451 69 PRO C C 176.34 0.3 1 610 451 69 PRO CA C 63.25 0.3 1 611 451 69 PRO CB C 32.19 0.3 1 612 451 69 PRO CG C 25.15 0.3 1 613 451 69 PRO CD C 48.32 0.3 1 614 452 70 GLN H H 8.83 0.02 1 615 452 70 GLN HA H 4.56 0.02 1 616 452 70 GLN HB2 H 1.86 0.02 2 617 452 70 GLN HB3 H 2.2 0.02 2 618 452 70 GLN HG2 H 2.47 0.02 2 619 452 70 GLN HG3 H 2.36 0.02 2 620 452 70 GLN HE21 H 6.7 0.02 2 621 452 70 GLN HE22 H 6.29 0.02 2 622 452 70 GLN C C 177.27 0.3 1 623 452 70 GLN CA C 54.33 0.3 1 624 452 70 GLN CB C 30.58 0.3 1 625 452 70 GLN CG C 31.09 0.3 1 626 452 70 GLN N N 120.05 0.3 1 627 453 71 LEU H H 8.57 0.02 1 628 453 71 LEU HA H 3.46 0.02 1 629 453 71 LEU HB2 H 1.33 0.02 2 630 453 71 LEU HB3 H 1.53 0.02 2 631 453 71 LEU HG H 1.37 0.02 1 632 453 71 LEU HD1 H 0.72 0.02 2 633 453 71 LEU HD2 H 0.61 0.02 2 634 453 71 LEU C C 178.17 0.3 1 635 453 71 LEU CA C 57.4 0.3 1 636 453 71 LEU CB C 40.78 0.3 1 637 453 71 LEU CG C 23.64 0.3 1 638 453 71 LEU CD1 C 22.65 0.3 1 639 453 71 LEU CD2 C 20.02 0.3 1 640 453 71 LEU N N 123.88 0.3 1 641 454 72 ASN H H 8.25 0.02 1 642 454 72 ASN HA H 4.49 0.02 1 643 454 72 ASN HB2 H 2.71 0.02 2 644 454 72 ASN HB3 H 2.71 0.02 2 645 454 72 ASN C C 175.18 0.3 1 646 454 72 ASN CA C 54.53 0.3 1 647 454 72 ASN CB C 37.31 0.3 1 648 454 72 ASN N N 113.34 0.3 1 649 455 73 ASP H H 7.54 0.02 1 650 455 73 ASP HA H 4.5 0.02 1 651 455 73 ASP HB2 H 2.67 0.02 2 652 455 73 ASP HB3 H 2.93 0.02 2 653 455 73 ASP C C 176.37 0.3 1 654 455 73 ASP CA C 55.82 0.3 1 655 455 73 ASP CB C 41.07 0.3 1 656 455 73 ASP N N 116.7 0.3 1 657 456 74 LEU H H 7.54 0.02 1 658 456 74 LEU HA H 4.29 0.02 1 659 456 74 LEU HB2 H 1.45 0.02 2 660 456 74 LEU HB3 H 1.63 0.02 2 661 456 74 LEU HG H 1.65 0.02 1 662 456 74 LEU HD1 H 0.7 0.02 2 663 456 74 LEU HD2 H 0.67 0.02 2 664 456 74 LEU C C 176.11 0.3 1 665 456 74 LEU CA C 55.72 0.3 1 666 456 74 LEU CB C 43.55 0.3 1 667 456 74 LEU CG C 23.98 0.3 1 668 456 74 LEU CD1 C 23.51 0.3 1 669 456 74 LEU CD2 C 21.64 0.3 1 670 456 74 LEU N N 118.87 0.3 1 671 457 75 LEU H H 7.77 0.02 1 672 457 75 LEU HA H 4.47 0.02 1 673 457 75 LEU HB2 H 1.35 0.02 2 674 457 75 LEU HB3 H 1.45 0.02 2 675 457 75 LEU HD1 H 0.76 0.02 2 676 457 75 LEU HD2 H 0.72 0.02 2 677 457 75 LEU C C 175.03 0.3 1 678 457 75 LEU CA C 53.14 0.3 1 679 457 75 LEU CB C 44.54 0.3 1 680 457 75 LEU CG C 23.53 0.3 1 681 457 75 LEU CD1 C 20.81 0.3 1 682 457 75 LEU N N 119.55 0.3 1 683 458 76 LYS H H 7.33 0.02 1 684 458 76 LYS HA H 4.35 0.02 1 685 458 76 LYS HB2 H 1.3 0.02 2 686 458 76 LYS HB3 H 1.9 0.02 2 687 458 76 LYS C C 175.56 0.3 1 688 458 76 LYS CA C 53.24 0.3 1 689 458 76 LYS CB C 33.85 0.3 1 690 458 76 LYS CG C 22 0.3 1 691 458 76 LYS CD C 25.89 0.3 1 692 458 76 LYS CE C 39.48 0.3 1 693 458 76 LYS N N 119.38 0.3 1 694 459 77 GLU H H 8.24 0.02 1 695 459 77 GLU HA H 3.93 0.02 1 696 459 77 GLU HB2 H 1.88 0.02 2 697 459 77 GLU HB3 H 1.88 0.02 2 698 459 77 GLU HG2 H 2.2 0.02 2 699 459 77 GLU HG3 H 2.2 0.02 2 700 459 77 GLU C C 178.26 0.3 1 701 459 77 GLU CA C 57.79 0.3 1 702 459 77 GLU CB C 29.4 0.3 1 703 459 77 GLU CG C 33.8 0.3 1 704 459 77 GLU N N 118.41 0.3 1 705 460 78 GLY H H 9.01 0.02 1 706 460 78 GLY HA2 H 4.17 0.02 2 707 460 78 GLY HA3 H 4.17 0.02 2 708 460 78 GLY C C 173.17 0.3 1 709 460 78 GLY CA C 46.32 0.3 1 710 460 78 GLY N N 112.36 0.3 1 711 461 79 GLN H H 7.48 0.02 1 712 461 79 GLN HA H 5.72 0.02 1 713 461 79 GLN HB2 H 1.63 0.02 2 714 461 79 GLN HB3 H 2.3 0.02 2 715 461 79 GLN HG2 H 2.16 0.02 2 716 461 79 GLN HG3 H 2.16 0.02 2 717 461 79 GLN C C 174.61 0.3 1 718 461 79 GLN CA C 53.14 0.3 1 719 461 79 GLN CB C 31.57 0.3 1 720 461 79 GLN CG C 31.03 0.3 1 721 461 79 GLN N N 114.22 0.3 1 722 462 80 ALA H H 9.29 0.02 1 723 462 80 ALA HA H 5.5 0.02 1 724 462 80 ALA HB H 1.1 0.02 1 725 462 80 ALA C C 175.35 0.3 1 726 462 80 ALA CA C 50.18 0.3 1 727 462 80 ALA CB C 23.76 0.3 1 728 462 80 ALA N N 121.53 0.3 1 729 463 81 MET H H 8.93 0.02 1 730 463 81 MET HA H 5.03 0.02 1 731 463 81 MET HB2 H 1.48 0.02 2 732 463 81 MET HB3 H 1.93 0.02 2 733 463 81 MET HG2 H 1.39 0.02 2 734 463 81 MET HG3 H 1.26 0.02 2 735 463 81 MET C C 174.1 0.3 1 736 463 81 MET CA C 53.64 0.3 1 737 463 81 MET CB C 35.53 0.3 1 738 463 81 MET CG C 30.04 0.3 1 739 463 81 MET N N 121.62 0.3 1 740 464 82 ILE H H 8.95 0.02 1 741 464 82 ILE HA H 4.73 0.02 1 742 464 82 ILE HB H 1.89 0.02 1 743 464 82 ILE HG2 H 0.04 0.02 1 744 464 82 ILE HD1 H 0.78 0.02 1 745 464 82 ILE C C 173.16 0.3 1 746 464 82 ILE CA C 57.3 0.3 1 747 464 82 ILE CB C 36.52 0.3 1 748 464 82 ILE CG1 C 24.38 0.3 1 749 464 82 ILE CG2 C 15.85 0.3 1 750 464 82 ILE N N 128.44 0.3 1 751 465 83 ARG H H 8.65 0.02 1 752 465 83 ARG HA H 5.04 0.02 1 753 465 83 ARG HB2 H 1.39 0.02 2 754 465 83 ARG HB3 H 1.92 0.02 2 755 465 83 ARG HG2 H 1.46 0.02 2 756 465 83 ARG HG3 H 1.46 0.02 2 757 465 83 ARG HD2 H 3.22 0.02 2 758 465 83 ARG HD3 H 3.19 0.02 2 759 465 83 ARG C C 175.82 0.3 1 760 465 83 ARG CA C 54.03 0.3 1 761 465 83 ARG CB C 34.34 0.3 1 762 465 83 ARG CG C 25.24 0.3 1 763 465 83 ARG CD C 41.75 0.3 1 764 465 83 ARG N N 125.87 0.3 1 765 466 84 PHE H H 9.03 0.02 1 766 466 84 PHE HA H 4.81 0.02 1 767 466 84 PHE HB2 H 2.68 0.02 2 768 466 84 PHE HB3 H 3.77 0.02 2 769 466 84 PHE HD1 H 7.4 0.02 3 770 466 84 PHE HD2 H 7.4 0.02 3 771 466 84 PHE HE1 H 6.98 0.02 3 772 466 84 PHE HE2 H 6.98 0.02 3 773 466 84 PHE C C 175.73 0.3 1 774 466 84 PHE CA C 58.78 0.3 1 775 466 84 PHE CB C 39.88 0.3 1 776 466 84 PHE CD1 C 129.2 0.3 3 777 466 84 PHE CD2 C 129.2 0.3 3 778 466 84 PHE CE1 C 127.6 0.3 3 779 466 84 PHE CE2 C 127.6 0.3 3 780 466 84 PHE N N 125.75 0.3 1 781 467 85 GLN H H 10.38 0.02 1 782 467 85 GLN HA H 4.16 0.02 1 783 467 85 GLN HB2 H 2.1 0.02 2 784 467 85 GLN HB3 H 2.1 0.02 2 785 467 85 GLN HG2 H 2.55 0.02 2 786 467 85 GLN HG3 H 2.55 0.02 2 787 467 85 GLN C C 176.42 0.3 1 788 467 85 GLN CA C 58.56 0.3 1 789 467 85 GLN CB C 29.85 0.3 1 790 467 85 GLN CG C 31.81 0.3 1 791 467 85 GLN N N 117.83 0.3 1 792 468 86 ASN H H 7.64 0.02 1 793 468 86 ASN HA H 4.72 0.02 1 794 468 86 ASN HB2 H 2.98 0.02 2 795 468 86 ASN HB3 H 3.16 0.02 2 796 468 86 ASN C C 175.23 0.3 1 797 468 86 ASN CA C 52.65 0.3 1 798 468 86 ASN CB C 39.88 0.3 1 799 468 86 ASN N N 107.54 0.3 1 800 469 87 SER H H 8.95 0.02 1 801 469 87 SER HA H 4.42 0.02 1 802 469 87 SER HB2 H 3.98 0.02 2 803 469 87 SER HB3 H 3.98 0.02 2 804 469 87 SER C C 176.8 0.3 1 805 469 87 SER CA C 60.07 0.3 1 806 469 87 SER CB C 63.24 0.3 1 807 469 87 SER N N 115.18 0.3 1 808 470 88 ASP H H 8.1 0.02 1 809 470 88 ASP HA H 4.36 0.02 1 810 470 88 ASP HB2 H 2.52 0.02 2 811 470 88 ASP HB3 H 2.66 0.02 2 812 470 88 ASP C C 178.58 0.3 1 813 470 88 ASP CA C 57.4 0.3 1 814 470 88 ASP CB C 40.18 0.3 1 815 470 88 ASP N N 123.98 0.3 1 816 471 89 GLU H H 8.06 0.02 1 817 471 89 GLU HA H 3.35 0.02 1 818 471 89 GLU HB2 H 1.88 0.02 2 819 471 89 GLU HB3 H 1.68 0.02 2 820 471 89 GLU HG2 H 2.59 0.02 2 821 471 89 GLU HG3 H 2.59 0.02 2 822 471 89 GLU C C 176.7 0.3 1 823 471 89 GLU CA C 59.54 0.3 1 824 471 89 GLU CB C 28.19 0.3 1 825 471 89 GLU CG C 35.91 0.3 1 826 471 89 GLU N N 118.67 0.3 1 827 472 90 GLN H H 7.29 0.02 1 828 472 90 GLN HA H 4.47 0.02 1 829 472 90 GLN HB2 H 1.71 0.02 2 830 472 90 GLN HB3 H 2.59 0.02 2 831 472 90 GLN C C 177.22 0.3 1 832 472 90 GLN CA C 60.47 0.3 1 833 472 90 GLN CB C 27.22 0.3 1 834 472 90 GLN CG C 29.85 0.3 1 835 472 90 GLN N N 119.7 0.3 1 836 473 91 ARG H H 7.53 0.02 1 837 473 91 ARG HA H 3.68 0.02 1 838 473 91 ARG HB2 H 1.82 0.02 2 839 473 91 ARG HB3 H 1.93 0.02 2 840 473 91 ARG HG2 H 1.53 0.02 2 841 473 91 ARG HG3 H 1.53 0.02 2 842 473 91 ARG HD2 H 3.17 0.02 2 843 473 91 ARG HD3 H 3.17 0.02 2 844 473 91 ARG C C 180 0.3 1 845 473 91 ARG CA C 59.48 0.3 1 846 473 91 ARG CB C 29.79 0.3 1 847 473 91 ARG CG C 25.38 0.3 1 848 473 91 ARG CD C 40.85 0.3 1 849 473 91 ARG N N 117.14 0.3 1 850 474 92 LEU H H 7.61 0.02 1 851 474 92 LEU HA H 3.85 0.02 1 852 474 92 LEU HB2 H 1.36 0.02 2 853 474 92 LEU HB3 H 1.46 0.02 2 854 474 92 LEU HD1 H 0.79 0.02 2 855 474 92 LEU HD2 H 0.73 0.02 2 856 474 92 LEU C C 179.9 0.3 1 857 474 92 LEU CA C 57.5 0.3 1 858 474 92 LEU CB C 40.78 0.3 1 859 474 92 LEU CG C 23.91 0.3 1 860 474 92 LEU CD1 C 19.84 0.3 1 861 474 92 LEU CD2 C 22.54 0.3 1 862 474 92 LEU N N 120.88 0.3 1 863 475 93 ALA H H 8.1 0.02 1 864 475 93 ALA HA H 3.83 0.02 1 865 475 93 ALA HB H 0.89 0.02 1 866 475 93 ALA C C 179.61 0.3 1 867 475 93 ALA CA C 55.82 0.3 1 868 475 93 ALA CB C 18.61 0.3 1 869 475 93 ALA N N 123.82 0.3 1 870 476 94 ILE H H 7.8 0.02 1 871 476 94 ILE HA H 3.51 0.02 1 872 476 94 ILE HB H 1.87 0.02 1 873 476 94 ILE HG12 H 1.02 0.02 1 874 476 94 ILE HG13 H 1.47 0.02 1 875 476 94 ILE HG2 H 0.8 0.02 1 876 476 94 ILE HD1 H 0.65 0.02 1 877 476 94 ILE C C 177.94 0.3 1 878 476 94 ILE CA C 64.42 0.3 1 879 476 94 ILE CB C 37.01 0.3 1 880 476 94 ILE CG1 C 26.3 0.3 1 881 476 94 ILE CG2 C 14.95 0.3 1 882 476 94 ILE N N 115.85 0.3 1 883 477 95 GLN H H 7.74 0.02 1 884 477 95 GLN HA H 3.88 0.02 1 885 477 95 GLN HB2 H 2.12 0.02 2 886 477 95 GLN HB3 H 2.12 0.02 2 887 477 95 GLN HG2 H 2.36 0.02 2 888 477 95 GLN HG3 H 2.44 0.02 2 889 477 95 GLN C C 178.71 0.3 1 890 477 95 GLN CA C 58.88 0.3 1 891 477 95 GLN CB C 28.31 0.3 1 892 477 95 GLN CG C 31.53 0.3 1 893 477 95 GLN N N 118.01 0.3 1 894 478 96 LYS H H 7.77 0.02 1 895 478 96 LYS HA H 3.85 0.02 1 896 478 96 LYS HB2 H 1.63 0.02 2 897 478 96 LYS HB3 H 1.63 0.02 2 898 478 96 LYS HG2 H 1.27 0.02 2 899 478 96 LYS HG3 H 1.27 0.02 2 900 478 96 LYS HD2 H 1.22 0.02 2 901 478 96 LYS HD3 H 1.22 0.02 2 902 478 96 LYS HE2 H 2.43 0.02 2 903 478 96 LYS HE3 H 2.43 0.02 2 904 478 96 LYS C C 177.45 0.3 1 905 478 96 LYS CA C 58.39 0.3 1 906 478 96 LYS CB C 32.27 0.3 1 907 478 96 LYS CG C 22.32 0.3 1 908 478 96 LYS CD C 26.74 0.3 1 909 478 96 LYS CE C 39.62 0.3 1 910 478 96 LYS N N 118.84 0.3 1 911 479 97 LEU H H 7.44 0.02 1 912 479 97 LEU HA H 4.46 0.02 1 913 479 97 LEU HB2 H 2.77 0.02 2 914 479 97 LEU HB3 H 2.77 0.02 2 915 479 97 LEU C C 175.93 0.3 1 916 479 97 LEU CA C 58.59 0.3 1 917 479 97 LEU CB C 39.39 0.3 1 918 479 97 LEU N N 116.7 0.3 1 919 480 98 LEU C C 173.84 0.3 1 920 480 98 LEU CA C 61.39 0.3 1 921 480 98 LEU CB C 38.44 0.3 1 922 481 99 ASN H H 8.47 0.02 1 923 481 99 ASN C C 177.05 0.3 1 924 481 99 ASN CA C 53.19 0.3 1 925 481 99 ASN CB C 38.7 0.3 1 926 481 99 ASN N N 122.37 0.3 1 927 485 103 ASN HA H 4.67 0.02 1 928 485 103 ASN HB2 H 2.79 0.02 2 929 485 103 ASN HB3 H 2.79 0.02 2 930 485 103 ASN CA C 53.44 0.3 1 931 485 103 ASN CB C 38.64 0.3 1 932 486 104 LYS H H 8.17 0.02 1 933 486 104 LYS HA H 4.26 0.02 1 934 486 104 LYS HB2 H 1.92 0.02 2 935 486 104 LYS HB3 H 2.05 0.02 2 936 486 104 LYS HD2 H 1.62 0.02 2 937 486 104 LYS HD3 H 1.62 0.02 2 938 486 104 LYS C C 176.13 0.3 1 939 486 104 LYS CA C 56.12 0.3 1 940 486 104 LYS CB C 29.27 0.3 1 941 486 104 LYS CG C 27.26 0.3 1 942 486 104 LYS CD C 31.24 0.3 1 943 486 104 LYS CE C 35.07 0.3 1 944 486 104 LYS N N 120.24 0.3 1 945 487 105 LEU H H 8.04 0.02 1 946 487 105 LEU HA H 4.05 0.02 1 947 487 105 LEU HB2 H 1.73 0.02 2 948 487 105 LEU HB3 H 1.73 0.02 2 949 487 105 LEU HG H 1.12 0.02 1 950 487 105 LEU C C 176.06 0.3 1 951 487 105 LEU CA C 61.46 0.3 1 952 487 105 LEU CB C 38.5 0.3 1 953 487 105 LEU CG C 27.26 0.3 1 954 487 105 LEU CD1 C 24.86 0.3 1 955 487 105 LEU CD2 C 14.86 0.3 1 956 487 105 LEU N N 121.28 0.3 1 957 488 106 GLN H H 8.11 0.02 1 958 488 106 GLN HA H 5.17 0.02 1 959 488 106 GLN HB2 H 1.93 0.02 2 960 488 106 GLN HB3 H 1.95 0.02 2 961 488 106 GLN HG2 H 2.24 0.02 2 962 488 106 GLN HG3 H 2.24 0.02 2 963 488 106 GLN C C 172.17 0.3 1 964 488 106 GLN CA C 54.07 0.3 1 965 488 106 GLN CB C 33.27 0.3 1 966 488 106 GLN N N 123.19 0.3 1 967 489 107 ILE H H 8.62 0.02 1 968 489 107 ILE HA H 4.47 0.02 1 969 489 107 ILE HB H 1.48 0.02 1 970 489 107 ILE HG2 H 0.91 0.02 1 971 489 107 ILE HD1 H 0.59 0.02 1 972 489 107 ILE C C 171.91 0.3 1 973 489 107 ILE CA C 59.58 0.3 1 974 489 107 ILE CB C 42.66 0.3 1 975 489 107 ILE CG1 C 25.87 0.3 1 976 489 107 ILE CG2 C 13.03 0.3 1 977 489 107 ILE CD1 C 12.22 0.3 1 978 489 107 ILE N N 116.5 0.3 1 979 490 108 GLU H H 8.47 0.02 1 980 490 108 GLU HA H 4.9 0.02 1 981 490 108 GLU HB2 H 1.71 0.02 2 982 490 108 GLU HB3 H 1.71 0.02 2 983 490 108 GLU HG2 H 1.74 0.02 2 984 490 108 GLU HG3 H 1.74 0.02 2 985 490 108 GLU C C 175.76 0.3 1 986 490 108 GLU CA C 55.22 0.3 1 987 490 108 GLU CB C 30.78 0.3 1 988 490 108 GLU CG C 34.38 0.3 1 989 490 108 GLU N N 128.9 0.3 1 990 491 109 ILE H H 8.8 0.02 1 991 491 109 ILE HA H 4.01 0.02 1 992 491 109 ILE HB H 1.62 0.02 1 993 491 109 ILE HG12 H 1.4 0.02 1 994 491 109 ILE HG13 H 1.4 0.02 1 995 491 109 ILE HG2 H 0.61 0.02 1 996 491 109 ILE HD1 H 0.63 0.02 1 997 491 109 ILE C C 174.9 0.3 1 998 491 109 ILE CA C 60.96 0.3 1 999 491 109 ILE CB C 40.68 0.3 1 1000 491 109 ILE CG1 C 24.39 0.3 1 1001 491 109 ILE CG2 C 15.39 0.3 1 1002 491 109 ILE CD1 C 11.54 0.3 1 1003 491 109 ILE N N 126.06 0.3 1 1004 492 110 ARG H H 9.06 0.02 1 1005 492 110 ARG HA H 3.74 0.02 1 1006 492 110 ARG HB2 H 1.46 0.02 2 1007 492 110 ARG HB3 H 2.13 0.02 2 1008 492 110 ARG HG2 H 1.53 0.02 2 1009 492 110 ARG HG3 H 1.53 0.02 2 1010 492 110 ARG HD2 H 3.25 0.02 2 1011 492 110 ARG HD3 H 3.07 0.02 2 1012 492 110 ARG C C 176.47 0.3 1 1013 492 110 ARG CA C 57.1 0.3 1 1014 492 110 ARG CB C 29.1 0.3 1 1015 492 110 ARG CG C 25.22 0.3 1 1016 492 110 ARG CD C 41.57 0.3 1 1017 492 110 ARG N N 126.62 0.3 1 1018 493 111 GLY H H 8.62 0.02 1 1019 493 111 GLY HA2 H 3.59 0.02 2 1020 493 111 GLY HA3 H 3.94 0.02 2 1021 493 111 GLY C C 173.46 0.3 1 1022 493 111 GLY CA C 45.62 0.3 1 1023 493 111 GLY N N 103.39 0.3 1 1024 494 112 GLN H H 7.89 0.02 1 1025 494 112 GLN HA H 4.58 0.02 1 1026 494 112 GLN HB2 H 1.81 0.02 2 1027 494 112 GLN HB3 H 2.03 0.02 2 1028 494 112 GLN HG2 H 2.23 0.02 2 1029 494 112 GLN HG3 H 2.23 0.02 2 1030 494 112 GLN C C 174.24 0.3 1 1031 494 112 GLN CA C 53.39 0.3 1 1032 494 112 GLN CB C 31.02 0.3 1 1033 494 112 GLN CG C 31.08 0.3 1 1034 494 112 GLN N N 120.43 0.3 1 1035 495 113 ILE H H 8.62 0.02 1 1036 495 113 ILE HA H 3.94 0.02 1 1037 495 113 ILE HB H 1.79 0.02 1 1038 495 113 ILE HG12 H 1.43 0.02 1 1039 495 113 ILE HG13 H 1.43 0.02 1 1040 495 113 ILE HG2 H 0.66 0.02 1 1041 495 113 ILE C C 176.39 0.3 1 1042 495 113 ILE CA C 61.26 0.3 1 1043 495 113 ILE CB C 36.42 0.3 1 1044 495 113 ILE CG1 C 24.81 0.3 1 1045 495 113 ILE CG2 C 15.95 0.3 1 1046 495 113 ILE N N 124.09 0.3 1 1047 496 114 CYS H H 9.15 0.02 1 1048 496 114 CYS HA H 4.58 0.02 1 1049 496 114 CYS HB2 H 2.66 0.02 2 1050 496 114 CYS HB3 H 3.21 0.02 2 1051 496 114 CYS C C 173.63 0.3 1 1052 496 114 CYS CA C 58.17 0.3 1 1053 496 114 CYS CB C 28.58 0.3 1 1054 496 114 CYS N N 129.84 0.3 1 1055 497 115 ASP H H 7.52 0.02 1 1056 497 115 ASP HA H 4.77 0.02 1 1057 497 115 ASP HB2 H 2.33 0.02 2 1058 497 115 ASP HB3 H 2.58 0.02 2 1059 497 115 ASP C C 173.69 0.3 1 1060 497 115 ASP CA C 55.62 0.3 1 1061 497 115 ASP CB C 42.46 0.3 1 1062 497 115 ASP N N 122.83 0.3 1 1063 498 116 VAL H H 7.55 0.02 1 1064 498 116 VAL HA H 4.68 0.02 1 1065 498 116 VAL HB H 1.5 0.02 1 1066 498 116 VAL HG1 H 0.6 0.02 2 1067 498 116 VAL HG2 H 0.6 0.02 2 1068 498 116 VAL C C 174.02 0.3 1 1069 498 116 VAL CA C 60.52 0.3 1 1070 498 116 VAL CB C 33.66 0.3 1 1071 498 116 VAL CG1 C 19.18 0.3 1 1072 498 116 VAL CG2 C 19.18 0.3 1 1073 498 116 VAL N N 118.89 0.3 1 1074 499 117 ILE H H 9.46 0.02 1 1075 499 117 ILE HA H 4.3 0.02 1 1076 499 117 ILE HB H 1.85 0.02 1 1077 499 117 ILE HG12 H 1.15 0.02 1 1078 499 117 ILE HG13 H 1.35 0.02 1 1079 499 117 ILE HG2 H 0.77 0.02 1 1080 499 117 ILE HD1 H 0.86 0.02 1 1081 499 117 ILE C C 175.52 0.3 1 1082 499 117 ILE CA C 59.64 0.3 1 1083 499 117 ILE CB C 39.23 0.3 1 1084 499 117 ILE CG1 C 23.73 0.3 1 1085 499 117 ILE CG2 C 15.51 0.3 1 1086 499 117 ILE CD1 C 15.51 0.3 1 1087 499 117 ILE N N 127.76 0.3 1 1088 500 118 SER H H 8.7 0.02 1 1089 500 118 SER HA H 4.57 0.02 1 1090 500 118 SER HB2 H 3.38 0.02 2 1091 500 118 SER HB3 H 4.09 0.02 2 1092 500 118 SER C C 173.56 0.3 1 1093 500 118 SER CA C 58.39 0.3 1 1094 500 118 SER CB C 64.52 0.3 1 1095 500 118 SER N N 119.21 0.3 1 1096 501 119 THR H H 7.33 0.02 1 1097 501 119 THR HA H 4.47 0.02 1 1098 501 119 THR HB H 4.02 0.02 1 1099 501 119 THR HG2 H 1.02 0.02 1 1100 501 119 THR C C 173.06 0.3 1 1101 501 119 THR CA C 60.27 0.3 1 1102 501 119 THR CB C 69.37 0.3 1 1103 501 119 THR CG2 C 18.57 0.3 1 1104 501 119 THR N N 117.71 0.3 1 1105 502 120 ILE H H 8.46 0.02 1 1106 502 120 ILE HA H 4.3 0.02 1 1107 502 120 ILE HB H 1.95 0.02 1 1108 502 120 ILE HG12 H 1.12 0.02 1 1109 502 120 ILE HG13 H 1.23 0.02 1 1110 502 120 ILE HG2 H 0.84 0.02 1 1111 502 120 ILE HD1 H 0.51 0.02 1 1112 502 120 ILE C C 173.92 0.3 1 1113 502 120 ILE CA C 56.71 0.3 1 1114 502 120 ILE CB C 37.41 0.3 1 1115 502 120 ILE N N 127.79 0.3 1 1116 503 121 PRO HA H 4.54 0.02 1 1117 503 121 PRO HB2 H 1.99 0.02 2 1118 503 121 PRO HB3 H 2.45 0.02 2 1119 503 121 PRO HG2 H 1.77 0.02 2 1120 503 121 PRO HG3 H 1.92 0.02 2 1121 503 121 PRO HD2 H 3.85 0.02 2 1122 503 121 PRO HD3 H 3.85 0.02 2 1123 503 121 PRO C C 177.11 0.3 1 1124 503 121 PRO CA C 63.14 0.3 1 1125 503 121 PRO CB C 33.06 0.3 1 1126 503 121 PRO CG C 25.31 0.3 1 1127 503 121 PRO CD C 48.53 0.3 1 1128 504 122 GLU H H 8.82 0.02 1 1129 504 122 GLU HA H 4.09 0.02 1 1130 504 122 GLU HB2 H 2.04 0.02 2 1131 504 122 GLU HB3 H 2.1 0.02 2 1132 504 122 GLU HG2 H 2.38 0.02 2 1133 504 122 GLU HG3 H 2.38 0.02 2 1134 504 122 GLU C C 178.54 0.3 1 1135 504 122 GLU CA C 60.27 0.3 1 1136 504 122 GLU CB C 29.99 0.3 1 1137 504 122 GLU CG C 34.1 0.3 1 1138 504 122 GLU N N 123.01 0.3 1 1139 505 123 ASP H H 8.92 0.02 1 1140 505 123 ASP HA H 4.31 0.02 1 1141 505 123 ASP HB2 H 2.55 0.02 2 1142 505 123 ASP HB3 H 2.58 0.02 2 1143 505 123 ASP C C 177.89 0.3 1 1144 505 123 ASP CA C 57.1 0.3 1 1145 505 123 ASP CB C 39.39 0.3 1 1146 505 123 ASP N N 117.45 0.3 1 1147 506 124 GLU H H 7.14 0.02 1 1148 506 124 GLU HA H 4.04 0.02 1 1149 506 124 GLU HB2 H 1.95 0.02 2 1150 506 124 GLU HB3 H 1.97 0.02 2 1151 506 124 GLU HG2 H 2.27 0.02 2 1152 506 124 GLU HG3 H 2.27 0.02 2 1153 506 124 GLU C C 178.59 0.3 1 1154 506 124 GLU CA C 59.08 0.3 1 1155 506 124 GLU CB C 29.69 0.3 1 1156 506 124 GLU CG C 33.57 0.3 1 1157 506 124 GLU N N 121.96 0.3 1 1158 507 125 GLU H H 8.48 0.02 1 1159 507 125 GLU HA H 3.77 0.02 1 1160 507 125 GLU HB2 H 1.98 0.02 2 1161 507 125 GLU HB3 H 2.31 0.02 2 1162 507 125 GLU HG2 H 2.39 0.02 2 1163 507 125 GLU HG3 H 2.39 0.02 2 1164 507 125 GLU C C 177.9 0.3 1 1165 507 125 GLU CA C 60.37 0.3 1 1166 507 125 GLU CB C 29.99 0.3 1 1167 507 125 GLU CG C 35 0.3 1 1168 507 125 GLU N N 120.96 0.3 1 1169 508 126 LYS H H 8.3 0.02 1 1170 508 126 LYS HA H 4.08 0.02 1 1171 508 126 LYS HB2 H 1.9 0.02 2 1172 508 126 LYS HB3 H 1.93 0.02 2 1173 508 126 LYS HG2 H 1.65 0.02 2 1174 508 126 LYS HG3 H 1.65 0.02 2 1175 508 126 LYS HD2 H 1.63 0.02 2 1176 508 126 LYS HD3 H 1.63 0.02 2 1177 508 126 LYS HE2 H 2.92 0.02 2 1178 508 126 LYS HE3 H 2.92 0.02 2 1179 508 126 LYS C C 179.3 0.3 1 1180 508 126 LYS CA C 60.17 0.3 1 1181 508 126 LYS CB C 32.17 0.3 1 1182 508 126 LYS CG C 22.86 0.3 1 1183 508 126 LYS CD C 26.83 0.3 1 1184 508 126 LYS CE C 39.4 0.3 1 1185 508 126 LYS N N 118.64 0.3 1 1186 509 127 ASN H H 8.1 0.02 1 1187 509 127 ASN HA H 4.53 0.02 1 1188 509 127 ASN HB2 H 2.91 0.02 2 1189 509 127 ASN HB3 H 2.68 0.02 2 1190 509 127 ASN HD21 H 6.94 0.02 2 1191 509 127 ASN HD22 H 7.82 0.02 2 1192 509 127 ASN C C 177.83 0.3 1 1193 509 127 ASN CA C 55.82 0.3 1 1194 509 127 ASN CB C 37.81 0.3 1 1195 509 127 ASN N N 117.4 0.3 1 1196 510 128 TYR H H 8.53 0.02 1 1197 510 128 TYR HA H 4.08 0.02 1 1198 510 128 TYR HB2 H 2.93 0.02 2 1199 510 128 TYR HB3 H 2.96 0.02 2 1200 510 128 TYR HD1 H 6.36 0.02 3 1201 510 128 TYR HD2 H 6.36 0.02 3 1202 510 128 TYR HE1 H 6.74 0.02 3 1203 510 128 TYR HE2 H 6.74 0.02 3 1204 510 128 TYR C C 177.06 0.3 1 1205 510 128 TYR CA C 62.25 0.3 1 1206 510 128 TYR CB C 37.61 0.3 1 1207 510 128 TYR CD1 C 129.7 0.3 3 1208 510 128 TYR CD2 C 129.7 0.3 3 1209 510 128 TYR CE1 C 130.7 0.3 3 1210 510 128 TYR CE2 C 130.7 0.3 3 1211 510 128 TYR N N 122.87 0.3 1 1212 511 129 TRP H H 8.4 0.02 1 1213 511 129 TRP HA H 4.13 0.02 1 1214 511 129 TRP HB2 H 3.11 0.02 2 1215 511 129 TRP HB3 H 3.18 0.02 2 1216 511 129 TRP HD1 H 7.52 0.02 1 1217 511 129 TRP HE1 H 10.67 0.02 1 1218 511 129 TRP C C 178.81 0.3 1 1219 511 129 TRP CA C 60.96 0.3 1 1220 511 129 TRP CB C 28.76 0.3 1 1221 511 129 TRP CD1 C 118.1 0.3 1 1222 511 129 TRP N N 118.79 0.3 1 1223 511 129 TRP NE1 N 128.46 0.3 1 1224 512 130 ASN H H 8.2 0.02 1 1225 512 130 ASN HA H 4.51 0.02 1 1226 512 130 ASN HB2 H 2.85 0.02 2 1227 512 130 ASN HB3 H 2.93 0.02 2 1228 512 130 ASN C C 176.82 0.3 1 1229 512 130 ASN CA C 56.04 0.3 1 1230 512 130 ASN CB C 38.3 0.3 1 1231 512 130 ASN N N 118.22 0.3 1 1232 513 131 TYR H H 7.74 0.02 1 1233 513 131 TYR HA H 4.12 0.02 1 1234 513 131 TYR HB2 H 2.93 0.02 2 1235 513 131 TYR HB3 H 3.13 0.02 2 1236 513 131 TYR HD1 H 6.7 0.02 3 1237 513 131 TYR HD2 H 6.7 0.02 3 1238 513 131 TYR HE1 H 6.96 0.02 3 1239 513 131 TYR HE2 H 6.96 0.02 3 1240 513 131 TYR C C 177.06 0.3 1 1241 513 131 TYR CA C 60.8 0.3 1 1242 513 131 TYR CB C 37.61 0.3 1 1243 513 131 TYR CD2 C 115.2 0.3 3 1244 513 131 TYR N N 121.38 0.3 1 1245 514 132 ILE H H 7.75 0.02 1 1246 514 132 ILE HA H 3.14 0.02 1 1247 514 132 ILE HB H 1.74 0.02 1 1248 514 132 ILE HG12 H 0.76 0.02 1 1249 514 132 ILE HG13 H 0.76 0.02 1 1250 514 132 ILE HG2 H 0.51 0.02 1 1251 514 132 ILE HD1 H 0.09 0.02 1 1252 514 132 ILE C C 178.21 0.3 1 1253 514 132 ILE CA C 62.74 0.3 1 1254 514 132 ILE CB C 36.58 0.3 1 1255 514 132 ILE CG1 C 24.15 0.3 1 1256 514 132 ILE CG2 C 15.38 0.3 1 1257 514 132 ILE CD1 C 9.06 0.3 1 1258 514 132 ILE N N 116.89 0.3 1 1259 515 133 LYS H H 7.72 0.02 1 1260 515 133 LYS HA H 3.83 0.02 1 1261 515 133 LYS HB2 H 1.6 0.02 2 1262 515 133 LYS HB3 H 1.68 0.02 2 1263 515 133 LYS HD2 H 2.09 0.02 2 1264 515 133 LYS HD3 H 2.09 0.02 2 1265 515 133 LYS HE2 H 2.34 0.02 2 1266 515 133 LYS HE3 H 2.34 0.02 2 1267 515 133 LYS C C 177.48 0.3 1 1268 515 133 LYS CA C 58.38 0.3 1 1269 515 133 LYS CB C 32.27 0.3 1 1270 515 133 LYS CG C 22.15 0.3 1 1271 515 133 LYS CD C 26.79 0.3 1 1272 515 133 LYS CE C 39.78 0.3 1 1273 515 133 LYS N N 118.99 0.3 1 1274 516 134 PHE H H 7.37 0.02 1 1275 516 134 PHE HA H 4.41 0.02 1 1276 516 134 PHE HB2 H 2.76 0.02 2 1277 516 134 PHE HB3 H 3.03 0.02 2 1278 516 134 PHE C C 175.71 0.3 1 1279 516 134 PHE CA C 58.45 0.3 1 1280 516 134 PHE CB C 39.29 0.3 1 1281 516 134 PHE N N 116.32 0.3 1 1282 517 135 LYS H H 7.47 0.02 1 1283 517 135 LYS HA H 3.99 0.02 1 1284 517 135 LYS HB2 H 1.45 0.02 2 1285 517 135 LYS HB3 H 1.45 0.02 2 1286 517 135 LYS HG2 H 1.13 0.02 2 1287 517 135 LYS HG3 H 1.13 0.02 2 1288 517 135 LYS HD2 H 1.5 0.02 2 1289 517 135 LYS HD3 H 1.5 0.02 2 1290 517 135 LYS C C 176.03 0.3 1 1291 517 135 LYS CA C 56.41 0.3 1 1292 517 135 LYS CB C 32.12 0.3 1 1293 517 135 LYS CG C 21.44 0.3 1 1294 517 135 LYS CD C 26.44 0.3 1 1295 517 135 LYS CE C 39.45 0.3 1 1296 517 135 LYS N N 121.59 0.3 1 1297 518 136 LYS H H 8.16 0.02 1 1298 518 136 LYS HA H 4.16 0.02 1 1299 518 136 LYS HB2 H 1.61 0.02 2 1300 518 136 LYS HB3 H 1.74 0.02 2 1301 518 136 LYS HG2 H 1.36 0.02 2 1302 518 136 LYS HG3 H 1.36 0.02 2 1303 518 136 LYS HE2 H 1.99 0.02 2 1304 518 136 LYS HE3 H 1.99 0.02 2 1305 518 136 LYS C C 175.51 0.3 1 1306 518 136 LYS CA C 56.21 0.3 1 1307 518 136 LYS CB C 32.76 0.3 1 1308 518 136 LYS CG C 21.93 0.3 1 1309 518 136 LYS CD C 26.31 0.3 1 1310 518 136 LYS CE C 39.16 0.3 1 1311 518 136 LYS N N 122.98 0.3 1 1312 519 137 ASN H H 7.91 0.02 1 1313 519 137 ASN HA H 4.36 0.02 1 1314 519 137 ASN HB2 H 2.59 0.02 2 1315 519 137 ASN HB3 H 2.59 0.02 2 1316 519 137 ASN C C 179.39 0.3 1 1317 519 137 ASN CA C 54.53 0.3 1 1318 519 137 ASN CB C 40.38 0.3 1 1319 519 137 ASN N N 125.16 0.3 1 stop_ save_