data_4787 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignment of 1H, 13C and 15N resonances of domain III of the ectodomain of apical membrane antigen 1 from Plasmodium falciparum ; _BMRB_accession_number 4787 _BMRB_flat_file_name bmr4787.str _Entry_type original _Submission_date 2000-07-19 _Accession_date 2000-07-19 _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 Nair Margie . . 2 Hodder Anthony N. . 3 Hinds Mark G. . 4 Anders Robin F. . 5 Norton Raymond S. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 584 "13C chemical shifts" 358 "15N chemical shifts" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-14 original author . stop_ _Original_release_date 2001-02-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Assignment of 1H, 13C and 15N resonances of domain III of the ectodomain of apical membrane antigen 1 from Plasmodium falciparum ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nair Margie . . 2 Hodder Anthony N. . 3 Hinds Mark G. . 4 Anders Robin F. . 5 Norton Raymond S. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 19 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 85 _Page_last 86 _Year 2001 _Details . loop_ _Keyword 'NMR resonance assignments' antigen malaria stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Hodder AN, Crewther PE, Matthew ML, Reid GE, Moritz RL, Simpson RJ, Anders RF. The disulfide bond structure of Plasmodium apical membrane antigen-1. J Biol Chem. 1996 Nov 15;271(46):29446-52. PMID: 8910611; UI: 97067209 ; _Citation_title 'The disulfide bond structure of Plasmodium apical membrane antigen-1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8910611 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hodder 'A. N.' N. . 2 Crewther 'P. E.' E. . 3 Matthew 'M. L.' L. . 4 Reid 'G. E.' E. . 5 Moritz 'R. L.' L. . 6 Simpson 'R. J.' J. . 7 Anders 'R. F.' F. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 271 _Journal_issue 46 _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 29446 _Page_last 29452 _Year 1996 _Details ; Apical membrane antigen-1 (AMA-1) of Plasmodium falciparum is one of the leading asexual blood stage antigens being considered for inclusion in a malaria vaccine. The ability of this molecule to induce a protective immune response has been shown to be dependent upon a conformation stabilized by disulfide bonds. In this study we have utilized the reversed-phase high performance liquid chromatography of dithiothreitol-reduced and nonreduced tryptic digests of Plasmodium chabaudi AMA-1 secreted from baculovirus-infected insect cells, in conjunction with N-terminal sequencing and electrospray-ionization mass spectrometry, to identify and assign disulfide-linked peptides. All 16 cysteine residues that are conserved in all known sequences of AMA-1 are incorporated into intramolecular disulfide bonds. Six of the eight bonds have been assigned unequivocally, whereas the two unassigned disulfide bonds connect two Cys-Xaa-Cys sequences separated by 14 residues. The eight disulfide bonds fall into three nonoverlapping groups that define three possible subdomains within the AMA-1 ectodomain. Although the pattern of disulfide bonds within subdomain III has not been fully elucidated, one of only two possible linkage patterns closely resembles the cystine knot motif found in growth factors. Sites of amino acid substitutions in AMA-1 that are well separated in the primary sequence are clustered by the disulfide bonds in subdomains II and III. These findings are consistent with the conclusion that these amino acid substitutions are defining conformational disulfide bond-dependent epitopes that are recognized by protective immune responses. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40. PMID: 8589602; UI: 96173087 ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D. S.' S. . 2 Bigam 'C. G.' G. . 3 Yao J. . . 4 Abildgaard F. . . 5 Dyson 'H. J.' J. . 6 Oldfield E. . . 7 Markley 'J. L.' L. . 8 Sykes 'B. D.' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Bartels, C., Xia ,T., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_Pf_AMA_1 _Saveframe_category molecular_system _Mol_system_name 'Apical Membrane Antigen 1' _Abbreviation_common 'Pf AMA 1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Pf AMA 1 domain III' $Pf_AMA_1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state Monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'parasite invasion of erythrocytes' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Pf_AMA_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Apical membrane antigen 1' _Abbreviation_common 'Pf AMA 1' _Molecular_mass 14330 _Mol_thiol_state 'all disulfide bound' _Details ; There are two unassigned disulphide linkages in the molecule. ; ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; MRGSHHHHHHGSEVENNFPC SLYKDEIMKEIERESKRIKL NDNDDEGNKKIIAPRIFISD DKDSLKCPCDPEMVSNSTCR FFVCKCVERRAEVTSNNEVV VKEEYKDEYADIPEHKPTYD KM ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 MET 2 -2 ARG 3 -3 GLY 4 -4 SER 5 -5 HIS 6 -6 HIS 7 -7 HIS 8 -8 HIS 9 -9 HIS 10 -10 HIS 11 -11 GLY 12 -12 SER 13 436 GLU 14 437 VAL 15 438 GLU 16 439 ASN 17 440 ASN 18 441 PHE 19 442 PRO 20 443 CYS 21 444 SER 22 445 LEU 23 446 TYR 24 447 LYS 25 448 ASP 26 449 GLU 27 450 ILE 28 451 MET 29 452 LYS 30 453 GLU 31 454 ILE 32 455 GLU 33 456 ARG 34 457 GLU 35 458 SER 36 459 LYS 37 460 ARG 38 461 ILE 39 462 LYS 40 463 LEU 41 464 ASN 42 465 ASP 43 466 ASN 44 467 ASP 45 468 ASP 46 469 GLU 47 470 GLY 48 471 ASN 49 472 LYS 50 473 LYS 51 474 ILE 52 475 ILE 53 476 ALA 54 477 PRO 55 478 ARG 56 479 ILE 57 480 PHE 58 481 ILE 59 482 SER 60 483 ASP 61 484 ASP 62 485 LYS 63 486 ASP 64 487 SER 65 488 LEU 66 489 LYS 67 490 CYS 68 491 PRO 69 492 CYS 70 493 ASP 71 494 PRO 72 495 GLU 73 496 MET 74 497 VAL 75 498 SER 76 499 ASN 77 500 SER 78 501 THR 79 502 CYS 80 503 ARG 81 504 PHE 82 505 PHE 83 506 VAL 84 507 CYS 85 508 LYS 86 509 CYS 87 510 VAL 88 511 GLU 89 512 ARG 90 513 ARG 91 514 ALA 92 515 GLU 93 516 VAL 94 517 THR 95 518 SER 96 519 ASN 97 520 ASN 98 521 GLU 99 522 VAL 100 523 VAL 101 524 VAL 102 525 LYS 103 526 GLU 104 527 GLU 105 528 TYR 106 529 LYS 107 530 ASP 108 531 GLU 109 532 TYR 110 533 ALA 111 534 ASP 112 535 ILE 113 536 PRO 114 537 GLU 115 538 HIS 116 539 LYS 117 540 PRO 118 541 THR 119 542 TYR 120 543 ASP 121 544 LYS 122 545 MET stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 1HN6 "Solution Structure Of Plasmodium Falciparum Apical Membrane Antigen 1 (Residues 436-545)" 90.16 110 100.00 100.00 1.07e-71 DBJ BAM85373 "apical membrane antigen 1 [Plasmodium falciparum]" 92.62 622 97.35 97.35 3.67e-67 DBJ BAM85381 "apical membrane antigen 1 [Plasmodium falciparum]" 92.62 622 97.35 98.23 1.29e-67 DBJ BAM85383 "apical membrane antigen 1 [Plasmodium falciparum]" 92.62 622 98.23 98.23 3.40e-68 DBJ BAM85388 "apical membrane antigen 1 [Plasmodium falciparum]" 92.62 622 97.35 97.35 3.52e-67 DBJ BAM85400 "apical membrane antigen 1 [Plasmodium falciparum]" 92.62 622 97.35 97.35 3.52e-67 EMBL CAB97182 "apical membrane antigen 1 [Plasmodium falciparum]" 83.61 526 97.06 97.06 6.26e-59 EMBL CAB97190 "apical membrane antigen 1 [Plasmodium falciparum]" 82.79 526 97.03 98.02 2.69e-58 EMBL CAB97197 "apical membrane antigen 1 [Plasmodium falciparum]" 83.61 526 97.06 97.06 3.50e-58 EMBL CAC34760 "Apical Membrane Antigen 1 [Plasmodium falciparum]" 92.62 437 97.35 97.35 8.09e-69 EMBL CAC34761 "Apical Membrane Antigen 1 [Plasmodium falciparum]" 92.62 437 97.35 97.35 8.01e-69 GB AAA29476 "apical membrane antigen 1, partial [Plasmodium falciparum]" 92.62 463 97.35 98.23 1.08e-68 GB AAB36701 "apical membrane antigen 1 [Plasmodium falciparum]" 92.62 622 98.23 98.23 4.37e-68 GB AAC47104 "apical membrane antigen-1, partial [Plasmodium falciparum]" 92.62 596 98.23 98.23 2.64e-68 GB AAC47105 "apical membrane antigen-1, partial [Plasmodium falciparum]" 92.62 592 97.35 97.35 1.32e-67 GB AAG50119 "apical membrane antigen-1 [Plasmodium falciparum]" 92.62 622 98.23 99.12 1.13e-68 REF XP_001348015 "apical membrane antigen 1, AMA1 [Plasmodium falciparum 3D7]" 92.62 622 98.23 98.23 4.37e-68 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $Pf_AMA_1 'malaria parasite' 5833 Eukaryota . Plasmodium falciparum 'Type I membrane Protein' 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 $Pf_AMA_1 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Pf_AMA_1 . mM 0.5 1 '[U-90% 15N]' stop_ save_ save_13C_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Pf_AMA_1 . mM 0.5 1 '[U-95% 13C[' stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR _Version 1.3 loop_ _Task 'Data processing' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'Peak assignment and analysis' stop_ _Details . _Citation_label $ref_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_1H-1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_3D_1H-1H-13C_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-13C NOESY' _Sample_label . save_ save_3D_1H-1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _Sample_label . save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label . save_ save_3D_CCCONH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCCONH' _Sample_label . save_ save_3D_1H-13C-1H_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _Sample_label . save_ save_3D_HNHA_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-13C NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCCONH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.4 0.1 n/a temperature 303 0.2 K stop_ save_ save_sample_conditions_set_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 3.4 0.1 n/a temperature 283 0.2 K stop_ save_ save_sample_conditions_set_3 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 2.8 0.1 n/a temperature 303 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 internal direct . . . . 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_ _Sample_label $15N_sample $13C_sample stop_ _Sample_conditions_label $sample_conditions_set_1 _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'Pf AMA 1 domain III' _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 . 13 GLU N N 122.8 0.1 1 2 . 13 GLU H H 8.64 0.02 1 3 . 13 GLU CA C 56.2 0.1 1 4 . 13 GLU HA H 4.54 0.02 1 5 . 13 GLU CB C 29.6 0.1 1 6 . 13 GLU HB2 H 2.06 0.02 1 7 . 13 GLU HB3 H 2.06 0.02 1 8 . 13 GLU CG C 32.9 0.1 1 9 . 13 GLU HG2 H 2.48 0.02 1 10 . 13 GLU HG3 H 2.48 0.02 1 11 . 13 GLU C C 176.0 0.1 1 12 . 14 VAL N N 121.8 0.1 1 13 . 14 VAL H H 8.20 0.02 1 14 . 14 VAL CA C 62.5 0.1 1 15 . 14 VAL HA H 4.17 0.02 1 16 . 14 VAL CB C 33.1 0.1 1 17 . 14 VAL HB H 2.13 0.02 1 18 . 14 VAL HG1 H 1.02 0.02 2 19 . 14 VAL HG2 H 1.00 0.02 2 20 . 14 VAL CG1 C 20.2 0.1 1 21 . 14 VAL C C 176.1 0.1 1 22 . 15 GLU N N 124.1 0.1 1 23 . 15 GLU H H 8.49 0.02 1 24 . 15 GLU CA C 55.8 0.1 1 25 . 15 GLU HA H 4.43 0.02 1 26 . 15 GLU CB C 29.7 0.1 1 27 . 15 GLU HB2 H 2.08 0.02 1 28 . 15 GLU HB3 H 2.08 0.02 1 29 . 15 GLU CG C 33.2 0.1 1 30 . 15 GLU HG2 H 2.46 0.02 1 31 . 15 GLU HG3 H 2.46 0.02 1 32 . 15 GLU C C 175.7 0.1 1 33 . 16 ASN N N 120.1 0.1 1 34 . 16 ASN H H 8.47 0.02 1 35 . 16 ASN CA C 53.2 0.1 1 36 . 16 ASN HA H 4.77 0.02 1 37 . 16 ASN CB C 39.3 0.1 1 38 . 16 ASN HB2 H 2.81 0.02 1 39 . 16 ASN HB3 H 2.81 0.02 1 40 . 16 ASN HD21 H 6.89 0.02 2 41 . 16 ASN HD22 H 7.62 0.02 2 42 . 16 ASN C C 175.0 0.1 1 43 . 17 ASN N N 118.9 0.1 1 44 . 17 ASN H H 8.49 0.02 1 45 . 17 ASN CA C 53.7 0.1 1 46 . 17 ASN HA H 4.78 0.02 1 47 . 17 ASN CB C 39.1 0.1 1 48 . 17 ASN HB2 H 2.87 0.02 1 49 . 17 ASN HB3 H 2.87 0.02 1 50 . 17 ASN HD21 H 6.97 0.02 2 51 . 17 ASN HD22 H 7.62 0.02 2 52 . 17 ASN C C 175.5 0.1 1 53 . 18 PHE N N 120.7 0.1 1 54 . 18 PHE H H 8.25 0.02 1 55 . 18 PHE CA C 56.6 0.1 1 56 . 18 PHE HA H 4.77 0.02 1 57 . 18 PHE CB C 38.7 0.1 1 58 . 18 PHE HB2 H 3.05 0.02 1 59 . 18 PHE HB3 H 3.05 0.02 1 60 . 18 PHE HE1 H 7.17 0.02 1 61 . 18 PHE HE2 H 7.17 0.02 1 62 . 19 PRO CA C 63.9 0.1 1 63 . 19 PRO HA H 4.59 0.02 1 64 . 19 PRO CB C 31.8 0.1 1 65 . 19 PRO HB2 H 2.42 0.02 1 66 . 19 PRO HB3 H 2.42 0.02 1 67 . 19 PRO HG2 H 2.12 0.02 1 68 . 19 PRO HG3 H 2.12 0.02 1 69 . 19 PRO HD2 H 4.04 0.02 2 70 . 19 PRO HD3 H 3.87 0.02 2 71 . 19 PRO C C 178.4 0.1 1 72 . 20 CYS N N 118.9 0.1 1 73 . 20 CYS H H 8.81 0.02 1 74 . 20 CYS CA C 56.8 0.1 1 75 . 20 CYS HA H 5.00 0.02 1 76 . 20 CYS CB C 38.1 0.1 1 77 . 20 CYS HB2 H 3.43 0.02 2 78 . 20 CYS HB3 H 3.25 0.02 2 79 . 20 CYS C C 176.7 0.1 1 80 . 21 SER N N 116.7 0.1 1 81 . 21 SER H H 8.50 0.02 1 82 . 21 SER CA C 61.7 0.1 1 83 . 21 SER HA H 4.16 0.02 1 84 . 21 SER CB C 61.6 0.1 1 85 . 21 SER HB2 H 4.09 0.02 1 86 . 21 SER HB3 H 4.09 0.02 1 87 . 21 SER C C 176.3 0.1 1 88 . 22 LEU N N 123.1 0.1 1 89 . 22 LEU H H 7.63 0.02 1 90 . 22 LEU CA C 57.7 0.1 1 91 . 22 LEU HA H 4.28 0.02 1 92 . 22 LEU CB C 41.6 0.1 1 93 . 22 LEU HB2 H 1.69 0.02 1 94 . 22 LEU HB3 H 1.69 0.02 1 95 . 22 LEU CG C 26.4 0.1 1 96 . 22 LEU HG H 1.64 0.02 1 97 . 22 LEU HD1 H 0.91 0.02 2 98 . 22 LEU HD2 H 0.89 0.02 2 99 . 22 LEU CD1 C 23.9 0.1 1 100 . 22 LEU CD2 C 23.6 0.1 1 101 . 22 LEU C C 179.4 0.1 1 102 . 23 TYR N N 120.7 0.1 1 103 . 23 TYR H H 7.69 0.02 1 104 . 23 TYR CA C 60.1 0.1 1 105 . 23 TYR HA H 4.55 0.02 1 106 . 23 TYR CB C 38.7 0.1 1 107 . 23 TYR HB2 H 3.31 0.02 1 108 . 23 TYR HB3 H 3.31 0.02 1 109 . 23 TYR HD1 H 7.26 0.02 1 110 . 23 TYR HD2 H 7.26 0.02 1 111 . 23 TYR HE1 H 6.72 0.02 1 112 . 23 TYR HE2 H 6.72 0.02 1 113 . 23 TYR C C 177.3 0.1 1 114 . 24 LYS N N 118.8 0.1 1 115 . 24 LYS H H 8.13 0.02 1 116 . 24 LYS CA C 60.0 0.1 1 117 . 24 LYS HA H 4.17 0.02 1 118 . 24 LYS CB C 32.3 0.1 1 119 . 24 LYS HB2 H 1.65 0.02 1 120 . 24 LYS HB3 H 1.65 0.02 1 121 . 24 LYS HG2 H 0.64 0.02 1 122 . 24 LYS HG3 H 0.64 0.02 1 123 . 24 LYS HE2 H 3.22 0.02 1 124 . 24 LYS HE3 H 3.22 0.02 1 125 . 24 LYS C C 177.9 0.1 1 126 . 25 ASP N N 116.9 0.1 1 127 . 25 ASP H H 7.78 0.02 1 128 . 25 ASP CA C 56.8 0.1 1 129 . 25 ASP HA H 4.34 0.02 1 130 . 25 ASP CB C 39.5 0.1 1 131 . 25 ASP HB2 H 3.00 0.02 2 132 . 25 ASP HB3 H 2.82 0.02 2 133 . 25 ASP C C 177.0 0.1 1 134 . 26 GLU N N 120.2 0.1 1 135 . 26 GLU H H 8.01 0.02 1 136 . 26 GLU CA C 58.9 0.1 1 137 . 26 GLU HA H 4.36 0.02 1 138 . 26 GLU CB C 29.8 0.1 1 139 . 26 GLU HB2 H 1.92 0.02 2 140 . 26 GLU HB3 H 1.75 0.02 2 141 . 26 GLU CG C 33.4 0.1 1 142 . 26 GLU HG2 H 2.27 0.02 2 143 . 26 GLU HG3 H 2.39 0.02 2 144 . 26 GLU C C 176.9 0.1 1 145 . 27 ILE N N 120.5 0.1 1 146 . 27 ILE H H 8.42 0.02 1 147 . 27 ILE CA C 58.8 0.1 1 148 . 27 ILE HB H 1.97 0.02 1 149 . 27 ILE HG2 H 0.78 0.02 1 150 . 27 ILE HG12 H 1.20 0.02 2 151 . 27 ILE HD1 H 0.95 0.02 1 152 . 27 ILE C C 179.4 0.1 1 153 . 28 MET N N 120.1 0.1 1 154 . 28 MET H H 7.90 0.02 1 155 . 28 MET CA C 59.2 0.1 1 156 . 28 MET HA H 4.15 0.02 1 157 . 28 MET CB C 32.4 0.1 1 158 . 28 MET HB2 H 2.29 0.02 1 159 . 28 MET HB3 H 2.29 0.02 1 160 . 28 MET CG C 31.3 0.1 1 161 . 28 MET HG2 H 2.59 0.02 1 162 . 28 MET HG3 H 2.59 0.02 1 163 . 28 MET C C 178.5 0.1 1 164 . 29 LYS N N 118.5 0.1 1 165 . 29 LYS H H 8.04 0.02 1 166 . 29 LYS CA C 59.6 0.1 1 167 . 29 LYS HA H 4.09 0.02 1 168 . 29 LYS CB C 32.4 0.1 1 169 . 29 LYS HB2 H 2.22 0.02 2 170 . 29 LYS HB3 H 1.98 0.02 2 171 . 29 LYS HG2 H 1.51 0.02 1 172 . 29 LYS HG3 H 1.51 0.02 1 173 . 29 LYS CD C 29.4 0.1 1 174 . 29 LYS HD2 H 1.68 0.02 1 175 . 29 LYS HD3 H 1.68 0.02 1 176 . 29 LYS C C 178.5 0.1 1 177 . 30 GLU N N 118.6 0.1 1 178 . 30 GLU H H 8.10 0.02 1 179 . 30 GLU CA C 58.6 0.1 1 180 . 30 GLU CB C 29.3 0.1 1 181 . 30 GLU HB2 H 2.03 0.02 1 182 . 30 GLU HB3 H 2.03 0.02 1 183 . 30 GLU CG C 34.4 0.1 1 184 . 30 GLU HG2 H 2.67 0.02 1 185 . 30 GLU HG3 H 2.67 0.02 1 186 . 30 GLU C C 178.4 0.1 1 187 . 31 ILE N N 119.0 0.1 1 188 . 31 ILE H H 8.29 0.02 1 189 . 31 ILE CA C 58.8 0.1 1 190 . 31 ILE HA H 4.11 0.02 1 191 . 31 ILE CB C 39.4 0.1 1 192 . 31 ILE HB H 1.85 0.02 1 193 . 31 ILE HG2 H 0.61 0.02 1 194 . 31 ILE CG1 C 31.9 0.1 1 195 . 31 ILE HD1 H 0.81 0.02 1 196 . 31 ILE C C 177.0 0.1 1 197 . 32 GLU N N 120.1 0.1 1 198 . 32 GLU H H 8.00 0.02 1 199 . 32 GLU CA C 56.9 0.1 1 200 . 32 GLU HA H 4.36 0.02 1 201 . 32 GLU CB C 28.8 0.1 1 202 . 32 GLU HB2 H 1.91 0.02 2 203 . 32 GLU HB3 H 1.75 0.02 2 204 . 32 GLU CG C 33.7 0.1 1 205 . 32 GLU HG2 H 2.26 0.02 2 206 . 32 GLU HG3 H 2.38 0.02 2 207 . 32 GLU C C 177.0 0.1 1 208 . 33 ARG N N 119.5 0.1 1 209 . 33 ARG H H 8.03 0.02 1 210 . 33 ARG CA C 59.1 0.1 1 211 . 33 ARG HA H 4.17 0.02 1 212 . 33 ARG CB C 30.6 0.1 1 213 . 33 ARG HB2 H 1.74 0.02 2 214 . 33 ARG HB3 H 1.92 0.02 2 215 . 33 ARG CG C 26.9 0.1 1 216 . 33 ARG HG2 H 2.21 0.02 2 217 . 33 ARG HG3 H 2.06 0.02 2 218 . 33 ARG CD C 43.1 0.1 1 219 . 33 ARG HD2 H 3.32 0.02 1 220 . 33 ARG HD3 H 3.32 0.02 1 221 . 33 ARG HE H 7.15 0.02 1 222 . 33 ARG C C 178.7 0.1 1 223 . 34 GLU N N 118.5 0.1 1 224 . 34 GLU H H 8.09 0.02 1 225 . 34 GLU CA C 57.7 0.1 1 226 . 34 GLU HA H 4.22 0.02 1 227 . 34 GLU CB C 29.3 0.1 1 228 . 34 GLU HB2 H 2.20 0.02 2 229 . 34 GLU HB3 H 1.98 0.02 2 230 . 34 GLU CG C 33.6 0.1 1 231 . 34 GLU HG2 H 2.71 0.02 2 232 . 34 GLU HG3 H 2.52 0.02 2 233 . 34 GLU C C 177.8 0.1 1 234 . 35 SER N N 115.0 0.1 1 235 . 35 SER H H 8.08 0.02 1 236 . 35 SER CA C 60.1 0.1 1 237 . 35 SER HA H 4.42 0.02 1 238 . 35 SER CB C 63.0 0.1 1 239 . 35 SER HB2 H 4.01 0.02 1 240 . 35 SER HB3 H 4.01 0.02 1 241 . 35 SER C C 175.0 0.1 1 242 . 36 LYS N N 121.4 0.1 1 243 . 36 LYS H H 7.87 0.02 1 244 . 36 LYS CA C 57.2 0.1 1 245 . 36 LYS HA H 4.39 0.02 1 246 . 36 LYS CB C 33.2 0.1 1 247 . 36 LYS HB2 H 1.95 0.02 1 248 . 36 LYS HB3 H 1.95 0.02 1 249 . 36 LYS CG C 23.9 0.1 1 250 . 36 LYS HG2 H 1.59 0.02 1 251 . 36 LYS HG3 H 1.59 0.02 1 252 . 36 LYS CD C 28.9 0.1 1 253 . 36 LYS HD2 H 1.84 0.02 1 254 . 36 LYS HD3 H 1.84 0.02 1 255 . 38 ILE N N 120.6 0.1 1 256 . 38 ILE H H 7.96 0.02 1 257 . 38 ILE CA C 61.4 0.1 1 258 . 38 ILE HA H 4.20 0.02 1 259 . 38 ILE CB C 39.0 0.1 1 260 . 38 ILE HB H 1.94 0.02 1 261 . 38 ILE HG2 H 0.93 0.02 1 262 . 38 ILE CG2 C 17.0 0.1 1 263 . 38 ILE CG1 C 26.7 0.1 1 264 . 38 ILE HG12 H 1.26 0.02 2 265 . 38 ILE HG13 H 1.57 0.02 2 266 . 38 ILE HD1 H 0.98 0.02 1 267 . 38 ILE C C 176.1 0.1 1 268 . 39 LYS N N 124.5 0.1 1 269 . 39 LYS H H 8.29 0.02 1 270 . 39 LYS CA C 56.4 0.1 1 271 . 39 LYS HA H 4.41 0.02 1 272 . 39 LYS CB C 33.1 0.1 1 273 . 39 LYS HB2 H 1.92 0.02 1 274 . 39 LYS HB3 H 1.92 0.02 1 275 . 39 LYS CG C 24.2 0.1 1 276 . 39 LYS HG2 H 1.51 0.02 1 277 . 39 LYS HG3 H 1.51 0.02 1 278 . 39 LYS CD C 29.0 0.1 1 279 . 39 LYS HD2 H 1.85 0.02 1 280 . 39 LYS HD3 H 1.85 0.02 1 281 . 39 LYS CE C 41.7 0.1 1 282 . 39 LYS HE2 H 2.90 0.02 1 283 . 39 LYS HE3 H 2.90 0.02 1 284 . 39 LYS C C 176.4 0.1 1 285 . 40 LEU N N 123.5 0.1 1 286 . 40 LEU H H 8.35 0.02 1 287 . 40 LEU CA C 55.4 0.1 1 288 . 40 LEU HA H 4.39 0.02 1 289 . 40 LEU CB C 42.6 0.1 1 290 . 40 LEU HB2 H 1.72 0.02 1 291 . 40 LEU HB3 H 1.72 0.02 1 292 . 40 LEU CG C 26.2 0.1 1 293 . 40 LEU HG H 1.63 0.02 1 294 . 40 LEU HD1 H 0.96 0.02 2 295 . 40 LEU HD2 H 0.93 0.02 2 296 . 40 LEU CD1 C 23.9 0.1 1 297 . 40 LEU CD2 C 23.9 0.1 1 298 . 40 LEU C C 177.1 0.1 1 299 . 41 ASN N N 118.4 0.1 1 300 . 41 ASN H H 8.43 0.02 1 301 . 41 ASN CA C 53.2 0.1 1 302 . 41 ASN HA H 4.79 0.02 1 303 . 41 ASN CB C 39.0 0.1 1 304 . 41 ASN HB2 H 2.88 0.02 1 305 . 41 ASN HB3 H 2.88 0.02 1 306 . 41 ASN HD21 H 6.97 0.02 2 307 . 41 ASN HD22 H 7.67 0.02 2 308 . 46 GLU N N 120.1 0.1 1 309 . 46 GLU H H 8.41 0.02 1 310 . 46 GLU CA C 56.5 0.1 1 311 . 46 GLU HA H 4.75 0.02 1 312 . 46 GLU CB C 29.1 0.1 1 313 . 46 GLU HB2 H 2.13 0.02 1 314 . 46 GLU HB3 H 2.13 0.02 1 315 . 46 GLU CG C 33.1 0.1 1 316 . 46 GLU HG2 H 2.50 0.02 2 317 . 46 GLU HG3 H 2.27 0.02 2 318 . 46 GLU C C 177.0 0.1 1 319 . 47 GLY N N 109.1 0.1 1 320 . 47 GLY H H 8.49 0.02 1 321 . 47 GLY CA C 45.8 0.1 1 322 . 47 GLY HA3 H 4.39 0.02 2 323 . 47 GLY HA2 H 4.00 0.02 2 324 . 47 GLY C C 174.3 0.1 1 325 . 48 ASN N N 118.6 0.1 1 326 . 48 ASN H H 8.29 0.02 1 327 . 48 ASN CA C 53.5 0.1 1 328 . 48 ASN HA H 4.79 0.02 1 329 . 48 ASN CB C 39.0 0.1 1 330 . 48 ASN HB2 H 2.91 0.02 1 331 . 48 ASN HB3 H 2.91 0.02 1 332 . 48 ASN HD21 H 6.06 0.02 2 333 . 48 ASN HD22 H 7.67 0.02 2 334 . 48 ASN C C 175.8 0.1 1 335 . 49 LYS N N 120.8 0.1 1 336 . 49 LYS H H 8.22 0.02 1 337 . 49 LYS CA C 56.5 0.1 1 338 . 49 LYS HA H 4.37 0.02 1 339 . 49 LYS CB C 33.2 0.1 1 340 . 49 LYS HB2 H 2.02 0.02 1 341 . 49 LYS HB3 H 2.02 0.02 1 342 . 49 LYS CG C 23.9 0.1 1 343 . 49 LYS HG2 H 1.50 0.02 1 344 . 49 LYS HG3 H 1.50 0.02 1 345 . 49 LYS CD C 29.1 0.1 1 346 . 49 LYS HD2 H 1.87 0.02 1 347 . 49 LYS HD3 H 1.87 0.02 1 348 . 49 LYS C C 176.2 0.1 1 349 . 50 LYS N N 121.4 0.1 1 350 . 50 LYS H H 8.27 0.02 1 351 . 50 LYS CA C 56.2 0.1 1 352 . 50 LYS HA H 4.41 0.02 1 353 . 50 LYS CB C 33.1 0.1 1 354 . 50 LYS HB2 H 1.83 0.02 1 355 . 50 LYS HB3 H 1.83 0.02 1 356 . 50 LYS CG C 24.1 0.1 1 357 . 50 LYS HG2 H 1.48 0.02 1 358 . 50 LYS HG3 H 1.48 0.02 1 359 . 50 LYS CD C 29.1 0.1 1 360 . 50 LYS HD2 H 1.83 0.02 1 361 . 50 LYS HD3 H 1.83 0.02 1 362 . 50 LYS C C 176.1 0.1 1 363 . 51 ILE N N 122.4 0.1 1 364 . 51 ILE H H 8.12 0.02 1 365 . 51 ILE CA C 60.5 0.1 1 366 . 51 ILE HA H 4.38 0.02 1 367 . 51 ILE CB C 38.8 0.1 1 368 . 51 ILE HB H 1.90 0.02 1 369 . 51 ILE HG2 H 0.90 0.02 1 370 . 51 ILE CG2 C 17.2 0.1 1 371 . 51 ILE CG1 C 26.7 0.1 1 372 . 51 ILE HG12 H 1.53 0.02 2 373 . 51 ILE HG13 H 1.26 0.02 2 374 . 51 ILE HD1 H 0.93 0.02 1 375 . 51 ILE C C 175.8 0.1 1 376 . 52 ILE N N 126.0 0.1 1 377 . 52 ILE H H 8.37 0.02 1 378 . 52 ILE CA C 60.5 0.1 1 379 . 52 ILE HA H 4.28 0.02 1 380 . 52 ILE CB C 38.9 0.1 1 381 . 52 ILE HB H 1.90 0.02 1 382 . 52 ILE HG2 H 0.91 0.02 1 383 . 52 ILE CG2 C 17.2 0.1 1 384 . 52 ILE CG1 C 26.5 0.1 1 385 . 52 ILE HG12 H 1.51 0.02 2 386 . 52 ILE HG13 H 1.23 0.02 2 387 . 52 ILE HD1 H 0.93 0.02 1 388 . 52 ILE C C 175.3 0.1 1 389 . 53 ALA N N 129.6 0.1 1 390 . 53 ALA H H 8.37 0.02 1 391 . 53 ALA CA C 50.2 0.1 1 392 . 53 ALA HA H 4.71 0.02 1 393 . 53 ALA HB H 1.41 0.02 1 394 . 53 ALA CB C 18.2 0.1 1 395 . 54 PRO CA C 62.8 0.1 1 396 . 54 PRO CB C 32.5 0.1 1 397 . 54 PRO HB2 H 2.34 0.02 1 398 . 54 PRO HB3 H 2.34 0.02 1 399 . 54 PRO CG C 26.6 0.1 1 400 . 54 PRO HD2 H 3.80 0.02 1 401 . 54 PRO HD3 H 3.80 0.02 1 402 . 54 PRO C C 175.4 0.1 1 403 . 55 ARG N N 121.1 0.1 1 404 . 55 ARG H H 8.37 0.02 1 405 . 55 ARG CA C 56.2 0.1 1 406 . 55 ARG HA H 4.51 0.02 1 407 . 55 ARG CB C 31.4 0.1 1 408 . 55 ARG HB2 H 1.78 0.02 1 409 . 55 ARG HB3 H 1.78 0.02 1 410 . 55 ARG CG C 26.8 0.1 1 411 . 55 ARG HG2 H 1.61 0.02 1 412 . 55 ARG HG3 H 1.61 0.02 1 413 . 55 ARG CD C 43.3 0.1 1 414 . 55 ARG HD2 H 3.26 0.02 1 415 . 55 ARG HD3 H 3.26 0.02 1 416 . 55 ARG C C 175.6 0.1 1 417 . 56 ILE N N 121.1 0.1 1 418 . 56 ILE H H 8.04 0.02 1 419 . 56 ILE CA C 60.4 0.1 1 420 . 56 ILE HA H 4.34 0.02 1 421 . 56 ILE CB C 39.0 0.1 1 422 . 56 ILE HB H 1.83 0.02 1 423 . 56 ILE HG2 H 0.89 0.02 1 424 . 56 ILE CG2 C 12.6 0.1 1 425 . 56 ILE CG1 C 26.9 0.1 1 426 . 56 ILE HG12 H 1.55 0.02 2 427 . 56 ILE HG13 H 1.17 0.02 2 428 . 56 ILE CD1 C 17.0 0.1 1 429 . 56 ILE C C 175.2 0.1 1 430 . 57 PHE N N 122.4 0.1 1 431 . 57 PHE H H 8.37 0.02 1 432 . 57 PHE CA C 57.2 0.1 1 433 . 57 PHE HA H 4.97 0.02 1 434 . 57 PHE CB C 38.4 0.1 1 435 . 57 PHE HB2 H 3.19 0.02 2 436 . 57 PHE HB3 H 2.83 0.02 2 437 . 57 PHE HD1 H 7.01 0.02 1 438 . 57 PHE HD2 H 7.01 0.02 1 439 . 57 PHE HE1 H 7.35 0.02 1 440 . 57 PHE HE2 H 7.35 0.02 1 441 . 59 SER N N 118.0 0.1 1 442 . 59 SER H H 9.07 0.02 1 443 . 59 SER CA C 56.9 0.1 1 444 . 59 SER HA H 4.90 0.02 1 445 . 59 SER CB C 64.4 0.1 1 446 . 59 SER HB2 H 4.03 0.02 2 447 . 59 SER HB3 H 3.63 0.02 2 448 . 59 SER C C 174.0 0.1 1 449 . 60 ASP N N 124.0 0.1 1 450 . 60 ASP H H 9.07 0.02 1 451 . 60 ASP CA C 55.2 0.1 1 452 . 60 ASP HA H 4.91 0.02 1 453 . 60 ASP CB C 39.8 0.1 1 454 . 60 ASP HB2 H 3.01 0.02 1 455 . 60 ASP HB3 H 3.01 0.02 1 456 . 60 ASP C C 174.9 0.1 1 457 . 61 ASP N N 118.8 0.1 1 458 . 61 ASP H H 8.50 0.02 1 459 . 61 ASP CA C 52.3 0.1 1 460 . 61 ASP HA H 4.96 0.02 1 461 . 61 ASP CB C 38.7 0.1 1 462 . 61 ASP HB2 H 2.91 0.02 2 463 . 61 ASP HB3 H 2.77 0.02 2 464 . 61 ASP C C 175.3 0.1 1 465 . 62 LYS N N 125.6 0.1 1 466 . 62 LYS H H 8.37 0.02 1 467 . 62 LYS CA C 59.7 0.1 1 468 . 62 LYS HA H 5.00 0.02 1 469 . 62 LYS CB C 32.3 0.1 1 470 . 62 LYS HB2 H 1.06 0.02 1 471 . 62 LYS HB3 H 1.06 0.02 1 472 . 62 LYS CG C 24.1 0.1 1 473 . 62 LYS HG2 H 0.68 0.02 2 474 . 62 LYS HG3 H 0.75 0.02 2 475 . 62 LYS HE2 H 3.33 0.02 1 476 . 62 LYS HE3 H 3.33 0.02 1 477 . 62 LYS HZ H 7.42 0.02 3 478 . 62 LYS C C 178.1 0.1 1 479 . 63 ASP N N 116.9 0.1 1 480 . 63 ASP H H 8.25 0.02 1 481 . 63 ASP CA C 56.0 0.1 1 482 . 63 ASP HA H 4.48 0.02 1 483 . 63 ASP CB C 39.3 0.1 1 484 . 63 ASP HB2 H 2.83 0.02 1 485 . 63 ASP HB3 H 2.83 0.02 1 486 . 63 ASP C C 177.6 0.1 1 487 . 64 SER N N 114.6 0.1 1 488 . 64 SER H H 7.91 0.02 1 489 . 64 SER CA C 59.8 0.1 1 490 . 64 SER HA H 4.38 0.02 1 491 . 64 SER CB C 62.6 0.1 1 492 . 64 SER HB2 H 3.98 0.02 2 493 . 64 SER HB3 H 4.03 0.02 2 494 . 64 SER C C 174.8 0.1 1 495 . 65 LEU N N 120.5 0.1 1 496 . 65 LEU H H 7.17 0.02 1 497 . 65 LEU CA C 55.4 0.1 1 498 . 65 LEU HA H 4.18 0.02 1 499 . 65 LEU CB C 39.5 0.1 1 500 . 65 LEU HB2 H 1.83 0.02 1 501 . 65 LEU HB3 H 1.83 0.02 1 502 . 65 LEU CG C 27.7 0.1 1 503 . 65 LEU HG H 1.61 0.02 1 504 . 65 LEU HD1 H 0.89 0.02 2 505 . 65 LEU HD2 H 0.85 0.02 2 506 . 65 LEU CD1 C 23.9 0.1 1 507 . 65 LEU C C 178.1 0.1 1 508 . 66 LYS N N 119.2 0.1 1 509 . 66 LYS H H 8.03 0.02 1 510 . 66 LYS CA C 55.8 0.1 1 511 . 66 LYS HA H 4.18 0.02 1 512 . 66 LYS CB C 33.1 0.1 1 513 . 66 LYS HB2 H 1.85 0.02 1 514 . 66 LYS HB3 H 1.85 0.02 1 515 . 66 LYS CG C 24.1 0.1 1 516 . 66 LYS HG2 H 1.44 0.02 1 517 . 66 LYS HG3 H 1.44 0.02 1 518 . 66 LYS CD C 29.6 0.1 1 519 . 66 LYS HD2 H 1.69 0.02 1 520 . 66 LYS HD3 H 1.69 0.02 1 521 . 66 LYS C C 176.1 0.1 1 522 . 67 CYS N N 121.8 0.1 1 523 . 67 CYS H H 8.78 0.02 1 524 . 67 CYS CA C 52.7 0.1 1 525 . 67 CYS HA H 5.08 0.02 1 526 . 67 CYS CB C 39.4 0.1 1 527 . 67 CYS HB2 H 3.43 0.02 2 528 . 67 CYS HB3 H 2.86 0.02 2 529 . 68 PRO CA C 64.2 0.1 1 530 . 68 PRO HA H 4.65 0.02 1 531 . 68 PRO CB C 31.8 0.1 1 532 . 68 PRO HB2 H 2.36 0.02 1 533 . 68 PRO HB3 H 2.36 0.02 1 534 . 68 PRO CG C 26.8 0.1 1 535 . 68 PRO HG2 H 2.07 0.02 1 536 . 68 PRO HG3 H 2.07 0.02 1 537 . 68 PRO HD2 H 3.77 0.02 2 538 . 68 PRO HD3 H 4.10 0.02 2 539 . 68 PRO C C 174.6 0.1 1 540 . 69 CYS N N 116.2 0.1 1 541 . 69 CYS H H 7.69 0.02 1 542 . 69 CYS CA C 55.2 0.1 1 543 . 69 CYS HA H 5.08 0.02 1 544 . 69 CYS CB C 39.0 0.1 1 545 . 69 CYS HB2 H 3.49 0.02 2 546 . 69 CYS HB3 H 3.19 0.02 2 547 . 69 CYS C C 172.3 0.1 1 548 . 70 ASP N N 119.4 0.1 1 549 . 70 ASP H H 8.39 0.02 1 550 . 70 ASP CA C 53.6 0.1 1 551 . 70 ASP HA H 4.79 0.02 1 552 . 70 ASP CB C 39.0 0.1 1 553 . 70 ASP HB2 H 2.82 0.02 1 554 . 70 ASP HB3 H 2.82 0.02 1 555 . 71 PRO CA C 62.8 0.1 1 556 . 71 PRO HA H 4.38 0.02 1 557 . 71 PRO CB C 33.7 0.1 1 558 . 71 PRO HB2 H 2.66 0.02 1 559 . 71 PRO HB3 H 2.66 0.02 1 560 . 71 PRO CG C 27.1 0.1 1 561 . 71 PRO HD2 H 3.85 0.02 1 562 . 71 PRO HD3 H 3.85 0.02 1 563 . 71 PRO C C 175.7 0.1 1 564 . 72 GLU N N 122.0 0.1 1 565 . 72 GLU H H 8.91 0.02 1 566 . 72 GLU CA C 54.8 0.1 1 567 . 72 GLU HA H 4.69 0.02 1 568 . 72 GLU CB C 31.0 0.1 1 569 . 72 GLU HB2 H 2.15 0.02 1 570 . 72 GLU HB3 H 2.15 0.02 1 571 . 72 GLU CG C 32.8 0.1 1 572 . 72 GLU HG2 H 2.47 0.02 1 573 . 72 GLU HG3 H 2.47 0.02 1 574 . 72 GLU C C 175.0 0.1 1 575 . 73 MET N N 125.7 0.1 1 576 . 73 MET H H 8.94 0.02 1 577 . 73 MET CA C 55.2 0.1 1 578 . 73 MET HA H 4.67 0.02 1 579 . 73 MET CB C 34.5 0.1 1 580 . 73 MET HB2 H 2.14 0.02 1 581 . 73 MET HB3 H 2.14 0.02 1 582 . 73 MET CG C 33.8 0.1 1 583 . 73 MET HG2 H 2.64 0.02 2 584 . 73 MET HG3 H 2.44 0.02 2 585 . 73 MET HE H 1.91 0.02 1 586 . 73 MET CE C 16.1 0.1 1 587 . 73 MET C C 175.4 0.1 1 588 . 74 VAL N N 128.3 0.1 1 589 . 74 VAL H H 8.92 0.02 1 590 . 74 VAL CA C 61.2 0.1 1 591 . 74 VAL HA H 4.30 0.02 1 592 . 74 VAL CB C 33.2 0.1 1 593 . 74 VAL HB H 1.49 0.02 1 594 . 74 VAL HG1 H 0.98 0.02 2 595 . 74 VAL HG2 H 0.80 0.02 2 596 . 74 VAL CG1 C 20.2 0.1 1 597 . 74 VAL C C 176.4 0.1 1 598 . 75 SER N N 117.8 0.1 1 599 . 75 SER H H 8.40 0.02 1 600 . 75 SER CA C 62.3 0.1 1 601 . 75 SER HA H 5.30 0.02 1 602 . 75 SER HB2 H 3.87 0.02 2 603 . 75 SER HB3 H 3.76 0.02 2 604 . 75 SER C C 173.8 0.1 1 605 . 76 ASN ND2 N 109.5 0.1 1 606 . 76 ASN HD21 H 5.95 0.02 2 607 . 76 ASN HD22 H 7.06 0.02 2 608 . 77 SER N N 114.3 0.1 1 609 . 77 SER H H 8.54 0.02 1 610 . 77 SER CA C 61.2 0.1 1 611 . 77 SER HA H 4.81 0.02 1 612 . 77 SER CB C 62.0 0.1 1 613 . 77 SER HB2 H 4.10 0.02 1 614 . 77 SER HB3 H 4.10 0.02 1 615 . 77 SER C C 175.4 0.1 1 616 . 78 THR N N 112.3 0.1 1 617 . 78 THR H H 7.95 0.02 1 618 . 78 THR CA C 62.8 0.1 1 619 . 78 THR HA H 4.44 0.02 1 620 . 78 THR CB C 69.2 0.1 1 621 . 78 THR HB H 4.40 0.02 1 622 . 78 THR HG2 H 1.26 0.02 1 623 . 78 THR C C 174.2 0.1 1 624 . 79 CYS N N 120.3 0.1 1 625 . 79 CYS H H 8.34 0.02 1 626 . 79 CYS CA C 54.3 0.1 1 627 . 79 CYS HA H 4.95 0.02 1 628 . 79 CYS CB C 39.0 0.1 1 629 . 79 CYS HB2 H 3.13 0.02 2 630 . 79 CYS HB3 H 2.92 0.02 2 631 . 79 CYS C C 172.4 0.1 1 632 . 80 ARG N N 122.4 0.1 1 633 . 80 ARG H H 8.33 0.02 1 634 . 80 ARG CA C 55.4 0.1 1 635 . 80 ARG HA H 4.97 0.02 1 636 . 80 ARG CB C 29.8 0.1 1 637 . 80 ARG HB2 H 1.71 0.02 1 638 . 80 ARG HB3 H 1.71 0.02 1 639 . 80 ARG CG C 26.8 0.1 1 640 . 80 ARG HG2 H 1.49 0.02 1 641 . 80 ARG HG3 H 1.49 0.02 1 642 . 80 ARG HE H 7.25 0.02 1 643 . 80 ARG C C 174.0 0.1 1 644 . 81 PHE N N 121.1 0.1 1 645 . 81 PHE H H 8.78 0.02 1 646 . 81 PHE CA C 56.6 0.1 1 647 . 81 PHE HA H 4.99 0.02 1 648 . 81 PHE CB C 42.3 0.1 1 649 . 81 PHE HB2 H 3.21 0.02 2 650 . 81 PHE HB3 H 2.69 0.02 2 651 . 81 PHE HD1 H 7.01 0.02 1 652 . 81 PHE HD2 H 7.01 0.02 1 653 . 81 PHE HE1 H 7.41 0.02 1 654 . 81 PHE HE2 H 7.41 0.02 1 655 . 81 PHE C C 171.9 0.1 1 656 . 82 PHE N N 117.6 0.1 1 657 . 82 PHE H H 9.23 0.02 1 658 . 82 PHE CA C 56.8 0.1 1 659 . 82 PHE HA H 5.48 0.02 1 660 . 82 PHE CB C 42.4 0.1 1 661 . 82 PHE HB2 H 3.22 0.02 2 662 . 82 PHE HB3 H 2.77 0.02 2 663 . 82 PHE HD1 H 7.01 0.02 1 664 . 82 PHE HD2 H 7.01 0.02 1 665 . 82 PHE HE1 H 7.40 0.02 1 666 . 82 PHE HE2 H 7.40 0.02 1 667 . 82 PHE HZ H 7.44 0.02 1 668 . 82 PHE C C 174.7 0.1 1 669 . 83 VAL N N 119.7 0.1 1 670 . 83 VAL H H 9.40 0.02 1 671 . 83 VAL CA C 60.1 0.1 1 672 . 83 VAL HA H 5.14 0.02 1 673 . 83 VAL CB C 35.4 0.1 1 674 . 83 VAL HB H 2.11 0.02 1 675 . 83 VAL HG1 H 0.97 0.02 2 676 . 83 VAL HG2 H 0.81 0.02 2 677 . 83 VAL CG1 C 20.8 0.1 1 678 . 83 VAL C C 175.0 0.1 1 679 . 84 CYS N N 125.7 0.1 1 680 . 84 CYS H H 9.35 0.02 1 681 . 84 CYS CA C 54.1 0.1 1 682 . 84 CYS HA H 5.12 0.02 1 683 . 84 CYS CB C 38.6 0.1 1 684 . 84 CYS HB2 H 3.24 0.02 2 685 . 84 CYS HB3 H 2.79 0.02 2 686 . 84 CYS C C 172.6 0.1 1 687 . 85 LYS N N 129.4 0.1 1 688 . 85 LYS H H 8.78 0.02 1 689 . 85 LYS CA C 55.7 0.1 1 690 . 85 LYS HA H 4.71 0.02 1 691 . 85 LYS CB C 31.4 0.1 1 692 . 85 LYS HB2 H 1.90 0.02 1 693 . 85 LYS HB3 H 1.90 0.02 1 694 . 85 LYS CG C 26.5 0.1 1 695 . 85 LYS HD2 H 1.64 0.02 1 696 . 85 LYS HD3 H 1.64 0.02 1 697 . 85 LYS C C 175.0 0.1 1 698 . 86 CYS N N 122.2 0.1 1 699 . 86 CYS H H 8.48 0.02 1 700 . 86 CYS CA C 53.2 0.1 1 701 . 86 CYS HA H 5.13 0.02 1 702 . 86 CYS CB C 38.9 0.1 1 703 . 86 CYS HB2 H 3.30 0.02 2 704 . 86 CYS HB3 H 3.00 0.02 2 705 . 86 CYS C C 172.4 0.1 1 706 . 87 VAL N N 121.6 0.1 1 707 . 87 VAL H H 8.36 0.02 1 708 . 87 VAL CA C 62.2 0.1 1 709 . 87 VAL HA H 4.49 0.02 1 710 . 87 VAL CB C 33.2 0.1 1 711 . 87 VAL HB H 2.17 0.02 1 712 . 87 VAL HG1 H 1.02 0.02 2 713 . 87 VAL HG2 H 0.99 0.02 2 714 . 87 VAL CG1 C 20.2 0.1 1 715 . 87 VAL C C 175.7 0.1 1 716 . 88 GLU N N 124.3 0.1 1 717 . 88 GLU H H 8.58 0.02 1 718 . 88 GLU CA C 55.9 0.1 1 719 . 88 GLU HA H 4.28 0.02 1 720 . 88 GLU CB C 30.1 0.1 1 721 . 88 GLU HB2 H 2.10 0.02 1 722 . 88 GLU HB3 H 2.10 0.02 1 723 . 88 GLU CG C 33.4 0.1 1 724 . 88 GLU HG2 H 2.40 0.02 1 725 . 88 GLU HG3 H 2.40 0.02 1 726 . 88 GLU C C 175.8 0.1 1 727 . 89 ARG N N 123.2 0.1 1 728 . 89 ARG H H 8.53 0.02 1 729 . 89 ARG CA C 56.0 0.1 1 730 . 89 ARG HA H 4.48 0.02 1 731 . 89 ARG CB C 30.1 0.1 1 732 . 89 ARG HB2 H 1.87 0.02 1 733 . 89 ARG HB3 H 1.87 0.02 1 734 . 89 ARG CG C 26.4 0.1 1 735 . 89 ARG HG2 H 1.71 0.02 1 736 . 89 ARG HG3 H 1.71 0.02 1 737 . 89 ARG HD2 H 3.29 0.02 1 738 . 89 ARG HD3 H 3.29 0.02 1 739 . 89 ARG C C 176.0 0.1 1 740 . 90 ARG N N 122.9 0.1 1 741 . 90 ARG H H 8.49 0.02 1 742 . 90 ARG CA C 56.1 0.1 1 743 . 90 ARG HA H 4.43 0.02 1 744 . 90 ARG CB C 29.5 0.1 1 745 . 90 ARG HB2 H 1.89 0.02 1 746 . 90 ARG HB3 H 1.89 0.02 1 747 . 90 ARG CG C 26.4 0.1 1 748 . 90 ARG HG2 H 1.72 0.02 1 749 . 90 ARG HG3 H 1.72 0.02 1 750 . 90 ARG HD2 H 3.28 0.02 1 751 . 90 ARG HD3 H 3.28 0.02 1 752 . 90 ARG C C 175.8 0.1 1 753 . 91 ALA N N 125.9 0.1 1 754 . 91 ALA H H 8.47 0.02 1 755 . 91 ALA CA C 52.3 0.1 1 756 . 91 ALA HA H 4.41 0.02 1 757 . 91 ALA HB H 1.46 0.02 1 758 . 91 ALA CB C 20.3 0.1 1 759 . 91 ALA C C 177.4 0.1 1 760 . 92 GLU N N 120.1 0.1 1 761 . 92 GLU H H 8.42 0.02 1 762 . 92 GLU CA C 56.2 0.1 1 763 . 92 GLU HA H 4.45 0.02 1 764 . 92 GLU CB C 29.8 0.1 1 765 . 92 GLU HB2 H 2.10 0.02 1 766 . 92 GLU HB3 H 2.10 0.02 1 767 . 92 GLU CG C 32.8 0.1 1 768 . 92 GLU HG2 H 2.49 0.02 1 769 . 92 GLU HG3 H 2.49 0.02 1 770 . 92 GLU C C 176.0 0.1 1 771 . 93 VAL N N 121.8 0.1 1 772 . 93 VAL H H 8.20 0.02 1 773 . 93 VAL CA C 62.4 0.1 1 774 . 93 VAL HA H 4.15 0.02 1 775 . 93 VAL CB C 33.2 0.1 1 776 . 93 VAL HB H 2.13 0.02 1 777 . 93 VAL HG1 H 1.00 0.02 1 778 . 93 VAL HG2 H 1.00 0.02 1 779 . 93 VAL CG1 C 20.1 0.1 1 780 . 93 VAL C C 176.4 0.1 1 781 . 94 THR N N 117.8 0.1 1 782 . 94 THR H H 8.39 0.02 1 783 . 94 THR CA C 61.7 0.1 1 784 . 94 THR HA H 4.55 0.02 1 785 . 94 THR CB C 68.9 0.1 1 786 . 94 THR HB H 4.32 0.02 1 787 . 94 THR HG2 H 1.29 0.02 1 788 . 94 THR CG2 C 21.2 0.1 1 789 . 94 THR C C 174.6 0.1 1 790 . 95 SER N N 117.9 0.1 1 791 . 95 SER H H 8.41 0.02 1 792 . 95 SER CA C 58.3 0.1 1 793 . 95 SER HA H 4.56 0.02 1 794 . 95 SER CB C 63.1 0.1 1 795 . 95 SER HB2 H 3.96 0.02 1 796 . 95 SER HB3 H 3.96 0.02 1 797 . 95 SER C C 174.4 0.1 1 798 . 96 ASN N N 120.9 0.1 1 799 . 96 ASN H H 8.58 0.02 1 800 . 96 ASN CA C 53.6 0.1 1 801 . 96 ASN HA H 4.81 0.02 1 802 . 96 ASN CB C 39.0 0.1 1 803 . 96 ASN HB2 H 2.88 0.02 1 804 . 96 ASN HB3 H 2.88 0.02 1 805 . 96 ASN HD22 H 6.91 0.02 2 806 . 96 ASN C C 174.9 0.1 1 807 . 97 ASN N N 119.7 0.1 1 808 . 97 ASN H H 8.40 0.02 1 809 . 97 ASN CA C 53.6 0.1 1 810 . 97 ASN HA H 4.76 0.02 1 811 . 97 ASN CB C 38.7 0.1 1 812 . 97 ASN HB2 H 2.88 0.02 1 813 . 97 ASN HB3 H 2.88 0.02 1 814 . 97 ASN HD21 H 6.99 0.02 2 815 . 97 ASN C C 175.0 0.1 1 816 . 98 GLU N N 120.4 0.1 1 817 . 98 GLU H H 8.29 0.02 1 818 . 98 GLU CA C 56.2 0.1 1 819 . 98 GLU HA H 4.45 0.02 1 820 . 98 GLU CB C 32.9 0.1 1 821 . 98 GLU HB2 H 2.50 0.02 2 822 . 98 GLU HB3 H 2.10 0.02 2 823 . 98 GLU CG C 37.9 0.1 1 824 . 98 GLU C C 176.1 0.1 1 825 . 99 VAL N N 124.7 0.1 1 826 . 99 VAL H H 8.29 0.02 1 827 . 99 VAL CA C 62.8 0.1 1 828 . 99 VAL HA H 4.16 0.02 1 829 . 99 VAL CB C 33.1 0.1 1 830 . 99 VAL HB H 2.10 0.02 1 831 . 99 VAL HG1 H 0.99 0.02 2 832 . 99 VAL HG2 H 0.97 0.02 2 833 . 99 VAL CG1 C 20.7 0.1 1 834 . 99 VAL C C 176.0 0.1 1 835 . 100 VAL N N 124.7 0.1 1 836 . 100 VAL H H 8.32 0.02 1 837 . 100 VAL CA C 62.7 0.1 1 838 . 100 VAL HA H 4.18 0.02 1 839 . 100 VAL CB C 33.1 0.1 1 840 . 100 VAL HB H 2.10 0.02 1 841 . 100 VAL HG1 H 0.96 0.02 2 842 . 100 VAL HG2 H 0.91 0.02 2 843 . 100 VAL CG1 C 20.5 0.1 1 844 . 100 VAL C C 176.0 0.1 1 845 . 101 VAL N N 124.9 0.1 1 846 . 101 VAL H H 8.33 0.02 1 847 . 101 VAL CA C 62.6 0.1 1 848 . 101 VAL HA H 4.18 0.02 1 849 . 101 VAL CB C 33.1 0.1 1 850 . 101 VAL HB H 2.13 0.02 1 851 . 101 VAL HG1 H 0.99 0.02 2 852 . 101 VAL HG2 H 0.97 0.02 2 853 . 101 VAL CG1 C 20.5 0.1 1 854 . 101 VAL C C 176.1 0.1 1 855 . 102 LYS N N 125.2 0.1 1 856 . 102 LYS H H 8.44 0.02 1 857 . 102 LYS CA C 56.5 0.1 1 858 . 102 LYS HA H 4.39 0.02 1 859 . 102 LYS CB C 33.4 0.1 1 860 . 102 LYS HB2 H 1.85 0.02 1 861 . 102 LYS HB3 H 1.85 0.02 1 862 . 102 LYS CG C 24.2 0.1 1 863 . 102 LYS HG2 H 1.50 0.02 1 864 . 102 LYS HG3 H 1.50 0.02 1 865 . 102 LYS HD2 H 1.80 0.02 1 866 . 102 LYS HD3 H 1.80 0.02 1 867 . 102 LYS HE2 H 3.00 0.02 1 868 . 102 LYS HE3 H 3.00 0.02 1 869 . 102 LYS C C 176.5 0.1 1 870 . 103 GLU N N 121.8 0.1 1 871 . 103 GLU H H 8.40 0.02 1 872 . 103 GLU CA C 55.9 0.1 1 873 . 103 GLU HA H 4.40 0.02 1 874 . 103 GLU CB C 30.0 0.1 1 875 . 103 GLU HB2 H 2.03 0.02 1 876 . 103 GLU HB3 H 2.03 0.02 1 877 . 103 GLU CG C 34.4 0.1 1 878 . 103 GLU HG2 H 2.43 0.02 1 879 . 103 GLU HG3 H 2.43 0.02 1 880 . 103 GLU C C 175.4 0.1 1 881 . 104 GLU N N 121.4 0.1 1 882 . 104 GLU H H 8.35 0.02 1 883 . 104 GLU CA C 56.3 0.1 1 884 . 104 GLU HA H 4.69 0.02 1 885 . 104 GLU CB C 29.2 0.1 1 886 . 104 GLU CG C 32.5 0.1 1 887 . 104 GLU C C 175.9 0.1 1 888 . 105 TYR N N 119.7 0.1 1 889 . 105 TYR H H 8.16 0.02 1 890 . 105 TYR CA C 57.6 0.1 1 891 . 105 TYR HA H 4.66 0.02 1 892 . 105 TYR CB C 38.9 0.1 1 893 . 105 TYR HB2 H 3.17 0.02 2 894 . 105 TYR HB3 H 2.94 0.02 2 895 . 105 TYR HD1 H 7.16 0.02 1 896 . 105 TYR HD2 H 7.16 0.02 1 897 . 105 TYR HE1 H 6.84 0.02 1 898 . 105 TYR HE2 H 6.84 0.02 1 899 . 105 TYR C C 175.9 0.1 1 900 . 106 LYS N N 122.5 0.1 1 901 . 106 LYS H H 8.25 0.02 1 902 . 106 LYS CA C 56.5 0.1 1 903 . 106 LYS HA H 4.31 0.02 1 904 . 106 LYS CB C 33.5 0.1 1 905 . 106 LYS HB2 H 1.83 0.02 1 906 . 106 LYS HB3 H 1.83 0.02 1 907 . 106 LYS CG C 24.1 0.1 1 908 . 106 LYS HG2 H 1.43 0.02 1 909 . 106 LYS HG3 H 1.43 0.02 1 910 . 106 LYS HD2 H 1.80 0.02 1 911 . 106 LYS HD3 H 1.80 0.02 1 912 . 106 LYS HE2 H 3.11 0.02 1 913 . 106 LYS HE3 H 3.11 0.02 1 914 . 106 LYS C C 177.4 0.1 1 915 . 107 ASP N N 120.0 0.1 1 916 . 107 ASP H H 8.43 0.02 1 917 . 107 ASP CA C 56.2 0.1 1 918 . 107 ASP HA H 4.71 0.02 1 919 . 107 ASP CB C 38.8 0.1 1 920 . 107 ASP HB2 H 2.89 0.02 1 921 . 107 ASP HB3 H 2.89 0.02 1 922 . 107 ASP C C 176.2 0.1 1 923 . 108 GLU N N 120.9 0.1 1 924 . 108 GLU H H 8.27 0.02 1 925 . 108 GLU CA C 56.5 0.1 1 926 . 108 GLU HA H 4.27 0.02 1 927 . 108 GLU CB C 29.2 0.1 1 928 . 108 GLU HB2 H 2.25 0.02 2 929 . 108 GLU HB3 H 1.94 0.02 2 930 . 108 GLU CG C 32.5 0.1 1 931 . 108 GLU C C 175.8 0.1 1 932 . 109 TYR N N 119.7 0.1 1 933 . 109 TYR H H 8.18 0.02 1 934 . 109 TYR CA C 57.8 0.1 1 935 . 109 TYR HA H 4.69 0.02 1 936 . 109 TYR CB C 38.5 0.1 1 937 . 109 TYR HB2 H 3.19 0.02 2 938 . 109 TYR HB3 H 2.96 0.02 2 939 . 109 TYR HD1 H 7.16 0.02 1 940 . 109 TYR HD2 H 7.16 0.02 1 941 . 109 TYR HE1 H 6.83 0.02 1 942 . 109 TYR HE2 H 6.83 0.02 1 943 . 109 TYR C C 175.6 0.1 1 944 . 110 ALA N N 124.1 0.1 1 945 . 110 ALA H H 8.04 0.02 1 946 . 110 ALA CA C 52.6 0.1 1 947 . 110 ALA HA H 4.33 0.02 1 948 . 110 ALA HB H 1.39 0.02 1 949 . 110 ALA CB C 20.3 0.1 1 950 . 110 ALA C C 177.1 0.1 1 951 . 111 ASP N N 118.0 0.1 1 952 . 111 ASP H H 8.35 0.02 1 953 . 111 ASP CA C 53.0 0.1 1 954 . 111 ASP HA H 4.76 0.02 1 955 . 111 ASP CB C 39.0 0.1 1 956 . 111 ASP HB2 H 2.84 0.02 1 957 . 111 ASP HB3 H 2.84 0.02 1 958 . 111 ASP C C 175.0 0.1 1 959 . 112 ILE N N 122.5 0.1 1 960 . 112 ILE H H 8.04 0.02 1 961 . 112 ILE CA C 58.9 0.1 1 962 . 112 ILE HA H 4.49 0.02 1 963 . 112 ILE CB C 38.2 0.1 1 964 . 112 ILE HB H 1.95 0.02 1 965 . 112 ILE HG2 H 0.94 0.02 1 966 . 112 ILE CG2 C 16.8 0.1 1 967 . 112 ILE CG1 C 26.6 0.1 1 968 . 112 ILE HG12 H 1.56 0.02 2 969 . 112 ILE HG13 H 1.22 0.02 2 970 . 112 ILE HD1 H 0.97 0.02 1 971 . 112 ILE CD1 C 13.2 0.1 1 972 . 113 PRO CB C 34.6 0.1 1 973 . 113 PRO HB2 H 2.06 0.02 1 974 . 113 PRO HB3 H 2.06 0.02 1 975 . 113 PRO HD2 H 3.72 0.02 2 976 . 113 PRO HD3 H 3.93 0.02 2 977 . 113 PRO C C 175.0 0.1 1 978 . 114 GLU N N 120.9 0.1 1 979 . 114 GLU H H 8.65 0.02 1 980 . 114 GLU HA H 4.31 0.02 1 981 . 114 GLU CB C 29.7 0.1 1 982 . 114 GLU HB2 H 2.05 0.02 1 983 . 114 GLU HB3 H 2.05 0.02 1 984 . 114 GLU CG C 32.7 0.1 1 985 . 114 GLU HG2 H 2.48 0.02 1 986 . 114 GLU HG3 H 2.48 0.02 1 987 . 114 GLU C C 176.0 0.1 1 988 . 115 HIS N N 119.5 0.1 1 989 . 115 HIS H H 8.55 0.02 1 990 . 115 HIS CA C 54.9 0.1 1 991 . 115 HIS HA H 4.77 0.02 1 992 . 115 HIS CB C 29.5 0.1 1 993 . 115 HIS HB2 H 3.24 0.02 1 994 . 115 HIS HB3 H 3.24 0.02 1 995 . 115 HIS C C 174.0 0.1 1 996 . 116 LYS N N 124.6 0.1 1 997 . 116 LYS H H 8.46 0.02 1 998 . 116 LYS CA C 54.4 0.1 1 999 . 116 LYS HA H 4.78 0.02 1 1000 . 116 LYS HB2 H 1.88 0.02 1 1001 . 116 LYS HB3 H 1.88 0.02 1 1002 . 116 LYS HG2 H 1.56 0.02 1 1003 . 116 LYS HG3 H 1.56 0.02 1 1004 . 116 LYS HD2 H 1.81 0.02 1 1005 . 116 LYS HD3 H 1.81 0.02 1 1006 . 117 PRO CA C 63.2 0.1 1 1007 . 117 PRO CB C 32.3 0.1 1 1008 . 117 PRO HB2 H 2.28 0.02 1 1009 . 117 PRO HB3 H 2.28 0.02 1 1010 . 117 PRO CG C 26.7 0.1 1 1011 . 117 PRO HG2 H 2.08 0.02 1 1012 . 117 PRO HG3 H 2.08 0.02 1 1013 . 117 PRO HD2 H 3.67 0.02 2 1014 . 117 PRO HD3 H 3.91 0.02 2 1015 . 118 THR N N 114.0 0.1 1 1016 . 118 THR H H 8.22 0.02 1 1017 . 118 THR CA C 61.9 0.1 1 1018 . 118 THR HA H 4.28 0.02 1 1019 . 118 THR CB C 68.9 0.1 1 1020 . 118 THR HB H 4.50 0.02 1 1021 . 118 THR HG2 H 1.23 0.02 1 1022 . 119 TYR N N 121.8 0.1 1 1023 . 119 TYR H H 8.14 0.02 1 1024 . 119 TYR CA C 57.6 0.1 1 1025 . 119 TYR HA H 4.70 0.02 1 1026 . 119 TYR CB C 38.9 0.1 1 1027 . 119 TYR HB2 H 3.04 0.02 1 1028 . 119 TYR HB3 H 3.04 0.02 1 1029 . 119 TYR HD1 H 7.19 0.02 1 1030 . 119 TYR HD2 H 7.19 0.02 1 1031 . 119 TYR HE1 H 6.91 0.02 1 1032 . 119 TYR HE2 H 6.91 0.02 1 1033 . 120 ASP N N 121.4 0.1 1 1034 . 120 ASP H H 8.37 0.02 1 1035 . 120 ASP CA C 53.3 0.1 1 1036 . 120 ASP HA H 4.71 0.02 1 1037 . 120 ASP HB2 H 2.79 0.02 1 1038 . 120 ASP HB3 H 2.79 0.02 1 stop_ save_