data_5159 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific resonance assignment of the second Ran-binding domain of human RanBP2 ; _BMRB_accession_number 5159 _BMRB_flat_file_name bmr5159.str _Entry_type original _Submission_date 2001-09-25 _Accession_date 2001-09-25 _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 Doker Rolf . . 2 Geyer Peter . . 3 Zhao Xiaodong . . 4 Kremer Werner . . 5 'Villa Braslavsky' Carolina . . 6 Kuhlmann Jurgen . . 7 Kalbitzer 'Hans Robert' . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 633 "13C chemical shifts" 452 "15N chemical shifts" 133 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-30 original author 'original release.' 2002-12-16 update author 'update chemical shift table.' 2004-10-25 update author 'update chemical shift table.' 2005-04-13 update author 'update publication.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific Resonance Assignment of the Second Ran-binding Domain of Human RanBP2 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21880665 _PubMed_ID 11883781 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Doker Rolf . . 2 Zhao Xiaodong . . 3 Kremer Werner . . 4 'Villa Braslavsky' Carolina . . 5 Kuhlmann Jurgen . . 6 Kalbitzer Hans R. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 185 _Page_last 186 _Year 2002 _Details . loop_ _Keyword Nup358 'Ran-binding domain' RanBP2 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Yokoyama et al. 1995, Nature 376,184-188. ; _Citation_title 'A giant nucleopore protein that binds Ran/TC4.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7603572 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yokoyama N. . . 2 Hayashi N. . . 3 Seki T. . . 4 Pante N. . . 5 Ohba T. . . 6 Nishii K. . . 7 Kuma K. . . 8 Hayashida T. . . 9 Miyata T. . . 10 Aebi U. . . stop_ _Journal_abbreviation Nature _Journal_name_full Nature _Journal_volume 376 _Journal_issue 6536 _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 184 _Page_last 188 _Year 1995 _Details ; Ran/TC4 is a small nuclear G protein that forms a complex with the chromatin-bound guanine nucleotide release factor RCC1 (ref. 2). Loss of RCC1 causes defects in cell cycle progression, RNA export and nuclear protein import. Some of these can be suppressed by overexpression of Ran/TC4 (ref. 1), suggesting that Ran/TC4 functions downstream of RCC1. We have searched for proteins that bind Ran/TC4 by using a two-hybrid screen, and here we report the identification of RanBP2, a novel protein of 3,224 residues. This giant protein comprises an amino-terminal 700-residue leucine-rich region, four RanBP1-homologous (refs 9, 10) domains, eight zinc-finger motifs similar to those of NUP153 (refs 11, 12), and a carboxy terminus with high homology to cyclophilin. The molecule contains the XFXFG pentapeptide motif characteristic of nuclear pore complex (NPC) proteins, and immunolocalization suggests that RanBP2 is a constituent of the NPC. The fact that NLS-mediated nuclear import can be inhibited by an antibody directed against RanBP2 supports a functional role in protein import through the NPC. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Wu et al. 1995, J. Biol. Chem. 270,14209-14213. ; _Citation_title 'Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7775481 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wu J. . . 2 Matunis 'M. J.' J. . 3 Kraemer D. . . 4 Blobel G. . . 5 Coutavas E. . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 270 _Journal_issue 23 _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 14209 _Page_last 14213 _Year 1995 _Details ; The Ras-related nuclear protein, Ran, has been implicated in nuclear transport. By screening a HeLa cell lambda expression library with Ran-GTP and sequencing overlapping cDNA clones, we have obtained the derived primary structure of a protein with a calculated molecular mass of 358 kDa. Using antibodies raised against an expressed segment of this protein, we obtained punctate nuclear surface staining by immunofluorescence microscopy that is characteristic for nucleoporins. Electron microscopy of immunogold-decorated rat liver nuclear envelopes sublocalized the 358-kDa protein at (or near) the tip of the cytoplasmic fibers of the nuclear pore complex (NPC). In agreement with current convention, this protein was therefore termed Nup358 (for nucleoporin of 358 kDa). Nup358 contains a leucine-rich region, four potential Ran binding sites (i.e. Ran binding protein 1 homologous domains) flanked by nucleoporin-characteristic FXFG or FG repeats, eight zinc finger motifs, and a C-terminal cyclophilin A homologous domain. Consistent with the location of Nup358 at the cytoplasmic fibers of the NPC, we found decoration with Ran-gold at only the cytoplasmic side of the NPC. Thus, Nup358 is the first nucleoporin shown to contain binding sites for two of three soluble nuclear transport factors so far isolated, namely karyopherin and Ran-GTP. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Vetter et al. 1999, Nature 398,39-46. ; _Citation_title 'Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10078529 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vetter 'I. R.' R. . 2 Nowak C. . . 3 Nishimoto T. . . 4 Kuhlmann J. . . 5 Wittinghofer A. . . stop_ _Journal_abbreviation Nature _Journal_name_full Nature _Journal_volume 398 _Journal_issue 6722 _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 39 _Page_last 46 _Year 1999 _Details ; The protein Ran is a small GTP-binding protein that binds to two types of effector inside the cell: Ran-binding proteins, which have a role in terminating export processes from the nucleus to the cytoplasm, and importin-beta-like molecules that bind cargo proteins during nuclear transport. The Ran-binding domain is a conserved sequence motif found in several proteins that participate in these transport processes. The Ran-binding protein RanBP2 contains four of these domains and constitutes a large part of the cytoplasmic fibrils that extend from the nuclear-pore complex. The structure of Ran bound to a non-hydrolysable GTP analogue (Ran x GppNHp) in complex with the first Ran-binding domain (RanBD1) of human RanBP2 reveals not only that RanBD1 has a pleckstrin-homology domain fold, but also that the switch-I region of Ran x GppNHp resembles the canonical Ras GppNHp structure and that the carboxy terminus of Ran is wrapped around RanBD1, contacting a basic patch on RanBD1 through its acidic end. This molecular 'embrace' enables RanBDs to sequester the Ran carboxy terminus, triggering the dissociation of Ran x GTP from importin-beta-related transport factors and facilitating GTP hydrolysis by the GTPase-activating protein ranGAP. Such a mechanism represents a new type of switch mechanism and regulatory protein-protein interaction for a Ras-related protein. ; save_ save_ref_4 _Saveframe_category citation _Citation_full ; J.P. Geyer, R. Doeker, W. Kremer, X. Zhao, J. Kuhlmann and H.R. Kalbitzer "Solution Structure of the Ran-binding Domain 2 of RanBP2 and its Interaction with the C Terminus of Ran", J Mol Biol (2005) 348, 711-725. ; _Citation_title 'Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15826666 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Geyer 'J Peter' P. . 2 Doker Rolf . . 3 Kremer Werner . . 4 Zhao Xiaodong . . 5 Kuhlmann Jurgen . . 6 Kalbitzer 'Hans Robert' R. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 348 _Journal_issue 3 _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 711 _Page_last 725 _Year 2005 _Details ; The termination of export processes from the nucleus to the cytoplasm in higher eukaryotes is mediated by binding of the small GTPase Ran as part of the export complexes to the Ran-binding domains (RanBD) of Ran-binding protein 2 (RanBP2) of the nuclear pore complex. So far, the structures of the first RanBD of RanBP2 and of RanBP1 in complexes with Ran have been known from X-ray crystallographic studies. Here we report the NMR solution structure of the uncomplexed second RanBD of RanBP2. The structure shows a pleckstrin homology (PH) fold featuring two almost orthogonal beta-sheets consisting of three and four strands and an alpha-helix sitting on top. This is in contrast to the RanBD in the crystal structure complexes in which one beta-strand is missing. That is probably due to the binding of the C-terminal alpha-helix of Ran to the RanBD in these complexes. To analyze the interaction between RanBD2 and the C terminus of Ran, NMR-titration studies with peptides comprising the six or 28 C-terminal residues of Ran were performed. While the six-residue peptide alone does not bind to RanBD2 in a specific manner, the 28-residue peptide, including the entire C-terminal helix of Ran, binds to RanBD2 in a manner analogous to the crystal structures. By solving the solution structure of the 28mer peptide alone, we confirmed that it adopts a stable alpha-helical structure like in native Ran and therefore serves as a valid model of the Ran C terminus. These results support current models that assume recognition of the transport complexes by the RanBDs through the Ran C terminus that is exposed in these complexes. ; save_ ################################## # Molecular system description # ################################## save_system_RanBP2-RanBD2 _Saveframe_category molecular_system _Mol_system_name 'Ran-binding domain 2 of RanBP2' _Abbreviation_common RanBP2-RanBD2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RanBP2-RanBD2 $RanBP2-RanBD2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RanBP2-RanBD2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ran-binding domain 2 of Ran-binding protein 2' _Abbreviation_common RanBP2-RanBD2 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; GSGEEDEKVLYSQRVKLFRF DAEVSQWKERGLGNLKILKN EVNGKLRMLMRREQVLKVCA NHWITTTMNLKPLSGSDRAW MWLASDFSDGDAKLEQLAAK FKTPELAEEFKQKFEECQRL LLDIPLQTPK ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 GLY 4 GLU 5 GLU 6 ASP 7 GLU 8 LYS 9 VAL 10 LEU 11 TYR 12 SER 13 GLN 14 ARG 15 VAL 16 LYS 17 LEU 18 PHE 19 ARG 20 PHE 21 ASP 22 ALA 23 GLU 24 VAL 25 SER 26 GLN 27 TRP 28 LYS 29 GLU 30 ARG 31 GLY 32 LEU 33 GLY 34 ASN 35 LEU 36 LYS 37 ILE 38 LEU 39 LYS 40 ASN 41 GLU 42 VAL 43 ASN 44 GLY 45 LYS 46 LEU 47 ARG 48 MET 49 LEU 50 MET 51 ARG 52 ARG 53 GLU 54 GLN 55 VAL 56 LEU 57 LYS 58 VAL 59 CYS 60 ALA 61 ASN 62 HIS 63 TRP 64 ILE 65 THR 66 THR 67 THR 68 MET 69 ASN 70 LEU 71 LYS 72 PRO 73 LEU 74 SER 75 GLY 76 SER 77 ASP 78 ARG 79 ALA 80 TRP 81 MET 82 TRP 83 LEU 84 ALA 85 SER 86 ASP 87 PHE 88 SER 89 ASP 90 GLY 91 ASP 92 ALA 93 LYS 94 LEU 95 GLU 96 GLN 97 LEU 98 ALA 99 ALA 100 LYS 101 PHE 102 LYS 103 THR 104 PRO 105 GLU 106 LEU 107 ALA 108 GLU 109 GLU 110 PHE 111 LYS 112 GLN 113 LYS 114 PHE 115 GLU 116 GLU 117 CYS 118 GLN 119 ARG 120 LEU 121 LEU 122 LEU 123 ASP 124 ILE 125 PRO 126 LEU 127 GLN 128 THR 129 PRO 130 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 16459 RanBD2(delta)N 100.00 130 100.00 100.00 7.42e-89 PDB 1XKE "Solution Structure Of The Second Ran-Binding Domain From Human Ranbp2" 100.00 130 100.00 100.00 7.42e-89 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $RanBP2-RanBD2 Human 9606 Eukaryota Metazoa Homo sapiens 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 $RanBP2-RanBD2 'recombinant technology' . . . . . 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 $RanBP2-RanBD2 0.8 mM '[U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RanBP2-RanBD2 0.7 mM '[U-13C; U-15N]' D2O 100 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RanBP2-RanBD2 1.1 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_AUREMOL _Saveframe_category software _Name AUREMOL _Version . _Details . save_ save_AURELIA _Saveframe_category software _Name AURELIA _Version . _Details . save_ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version . _Details . 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 DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HCCH-TOCSY_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 internal indirect cylindrical internal . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.00 internal indirect cylindrical internal . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name RanBP2-RanBD2 _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 . 2 SER CA C 58.6 0.4 1 2 . 2 SER HA H 4.62 0.11 1 3 . 2 SER CB C 63.7 0.6 1 4 . 2 SER HB3 H 4.03 0.11 1 5 . 2 SER HB2 H 4.03 0.11 1 6 . 2 SER C C 175.1 0.17 1 7 . 3 GLY N N 110.8 0.17 1 8 . 3 GLY H H 8.81 0.02 1 9 . 3 GLY CA C 45.6 0.4 1 10 . 3 GLY HA2 H 4.16 0.11 2 11 . 3 GLY HA3 H 4.10 0.11 2 12 . 3 GLY C C 174.6 0.17 1 13 . 4 GLU N N 119.6 0.17 1 14 . 4 GLU H H 8.44 0.02 1 15 . 4 GLU CA C 57.0 0.4 1 16 . 4 GLU HA H 4.45 0.11 1 17 . 4 GLU CB C 30.1 0.6 1 18 . 4 GLU HB3 H 2.06 0.11 2 19 . 4 GLU HB2 H 2.20 0.11 2 20 . 4 GLU CG C 36.3 0.6 1 21 . 4 GLU HG3 H 2.33 0.11 1 22 . 4 GLU HG2 H 2.33 0.11 1 23 . 4 GLU C C 177.1 0.17 1 24 . 5 GLU N N 119.6 0.17 1 25 . 5 GLU H H 8.73 0.02 1 26 . 5 GLU CA C 57.3 0.4 1 27 . 5 GLU HA H 4.38 0.11 1 28 . 5 GLU CB C 30.0 0.6 1 29 . 5 GLU HB3 H 2.10 0.11 2 30 . 5 GLU HB2 H 2.20 0.11 2 31 . 5 GLU CG C 36.2 0.6 1 32 . 5 GLU HG3 H 2.42 0.11 1 33 . 5 GLU HG2 H 2.42 0.11 1 34 . 5 GLU C C 176.4 0.17 1 35 . 6 ASP N N 118.7 0.17 1 36 . 6 ASP H H 8.30 0.02 1 37 . 6 ASP CA C 54.8 0.4 1 38 . 6 ASP HA H 4.77 0.11 1 39 . 6 ASP CB C 41.3 0.6 1 40 . 6 ASP HB3 H 2.78 0.11 2 41 . 6 ASP HB2 H 2.93 0.11 2 42 . 6 ASP C C 175.7 0.17 1 43 . 7 GLU N N 118.4 0.17 1 44 . 7 GLU H H 7.86 0.02 1 45 . 7 GLU CA C 55.5 0.4 1 46 . 7 GLU HA H 5.06 0.11 1 47 . 7 GLU CB C 32.9 0.6 1 48 . 7 GLU HB3 H 2.07 0.11 2 49 . 7 GLU HB2 H 1.95 0.11 2 50 . 7 GLU CG C 37.3 0.6 1 51 . 7 GLU HG3 H 2.12 0.11 2 52 . 7 GLU HG2 H 2.45 0.11 2 53 . 7 GLU C C 175.7 0.17 1 54 . 8 LYS N N 122.1 0.17 1 55 . 8 LYS H H 8.89 0.02 1 56 . 8 LYS CA C 54.4 0.4 1 57 . 8 LYS HA H 4.69 0.11 1 58 . 8 LYS CB C 34.9 0.6 1 59 . 8 LYS HB3 H 1.92 0.11 1 60 . 8 LYS HB2 H 1.92 0.11 1 61 . 8 LYS C C 176.0 0.17 1 62 . 9 VAL N N 123.9 0.17 1 63 . 9 VAL H H 8.91 0.02 1 64 . 9 VAL CA C 63.3 0.4 1 65 . 9 VAL HA H 4.25 0.11 1 66 . 9 VAL CB C 31.8 0.6 1 67 . 9 VAL HB H 2.21 0.11 1 68 . 9 VAL CG1 C 21.7 0.6 2 69 . 9 VAL HG1 H 1.01 0.11 2 70 . 9 VAL CG2 C 21.4 0.6 2 71 . 9 VAL HG2 H 1.13 0.11 2 72 . 9 VAL C C 176.6 0.17 1 73 . 10 LEU N N 127.7 0.17 1 74 . 10 LEU H H 9.53 0.02 1 75 . 10 LEU CA C 55.3 0.4 1 76 . 10 LEU HA H 4.59 0.11 1 77 . 10 LEU CB C 42.7 0.6 1 78 . 10 LEU HB3 H 1.64 0.11 1 79 . 10 LEU HB2 H 1.64 0.11 1 80 . 10 LEU HD1 H 0.96 0.11 4 81 . 10 LEU C C 177.1 0.17 1 82 . 11 TYR N N 118.3 0.17 1 83 . 11 TYR H H 7.69 0.02 1 84 . 11 TYR CA C 58.1 0.4 1 85 . 11 TYR HA H 4.68 0.11 1 86 . 11 TYR CB C 42.1 0.6 1 87 . 11 TYR HB3 H 2.49 0.11 2 88 . 11 TYR HB2 H 3.29 0.11 2 89 . 11 TYR C C 172.9 0.17 1 90 . 12 SER N N 119.3 0.17 1 91 . 12 SER H H 7.32 0.02 1 92 . 12 SER CA C 56.8 0.4 1 93 . 12 SER HA H 5.41 0.11 1 94 . 12 SER CB C 64.5 0.6 1 95 . 12 SER HB3 H 3.58 0.11 1 96 . 12 SER HB2 H 3.58 0.11 1 97 . 12 SER C C 172.9 0.17 1 98 . 13 GLN N N 125.0 0.17 1 99 . 13 GLN H H 8.60 0.02 1 100 . 13 GLN CA C 55.0 0.4 1 101 . 13 GLN HA H 4.53 0.11 1 102 . 13 GLN CB C 35.1 0.6 1 103 . 13 GLN HB3 H 2.20 0.11 1 104 . 13 GLN HB2 H 2.20 0.11 1 105 . 13 GLN CG C 34.6 0.6 1 106 . 13 GLN HG3 H 2.82 0.11 2 107 . 13 GLN HG2 H 3.00 0.11 2 108 . 13 GLN NE2 N 112.8 0.17 1 109 . 13 GLN HE21 H 7.94 0.11 2 110 . 13 GLN HE22 H 7.32 0.11 2 111 . 13 GLN C C 173.4 0.17 1 112 . 14 ARG N N 127.4 0.17 1 113 . 14 ARG H H 8.54 0.02 1 114 . 14 ARG CA C 56.9 0.4 1 115 . 14 ARG HA H 4.81 0.11 1 116 . 14 ARG CB C 30.5 0.6 1 117 . 14 ARG HB3 H 1.84 0.11 2 118 . 14 ARG HB2 H 1.89 0.11 2 119 . 14 ARG CG C 27.5 0.6 1 120 . 14 ARG HG3 H 1.53 0.11 1 121 . 14 ARG HG2 H 1.53 0.11 1 122 . 14 ARG C C 175.7 0.17 1 123 . 15 VAL N N 119.1 0.17 1 124 . 15 VAL H H 9.03 0.02 1 125 . 15 VAL CA C 58.7 0.4 1 126 . 15 VAL HA H 4.73 0.11 1 127 . 15 VAL CB C 36.7 0.6 1 128 . 15 VAL HB H 1.69 0.11 1 129 . 15 VAL CG1 C 20.0 0.6 2 130 . 15 VAL HG1 H 0.65 0.11 2 131 . 15 VAL CG2 C 22.0 0.6 2 132 . 15 VAL HG2 H 0.28 0.11 2 133 . 15 VAL C C 173.9 0.17 1 134 . 16 LYS N N 117.1 0.17 1 135 . 16 LYS H H 7.59 0.02 1 136 . 16 LYS CA C 55.7 0.4 1 137 . 16 LYS HA H 4.88 0.11 1 138 . 16 LYS CB C 35.1 0.6 1 139 . 16 LYS HB3 H 1.70 0.11 1 140 . 16 LYS HB2 H 1.70 0.11 1 141 . 16 LYS C C 174.2 0.17 1 142 . 17 LEU N N 127.1 0.17 1 143 . 17 LEU H H 8.96 0.02 1 144 . 17 LEU CA C 53.1 0.4 1 145 . 17 LEU HA H 5.46 0.11 1 146 . 17 LEU CB C 45.9 0.6 1 147 . 17 LEU HB3 H 1.26 0.11 2 148 . 17 LEU HB2 H 1.67 0.11 2 149 . 17 LEU C C 175.6 0.17 1 150 . 18 PHE N N 124.6 0.17 1 151 . 18 PHE H H 9.94 0.02 1 152 . 18 PHE CA C 56.4 0.4 1 153 . 18 PHE HA H 5.45 0.11 1 154 . 18 PHE CB C 44.7 0.6 1 155 . 18 PHE HB3 H 2.93 0.11 2 156 . 18 PHE HB2 H 3.30 0.11 2 157 . 18 PHE C C 173.7 0.17 1 158 . 19 ARG N N 117.9 0.17 1 159 . 19 ARG H H 9.44 0.02 1 160 . 19 ARG CA C 54.4 0.4 1 161 . 19 ARG HA H 5.74 0.11 1 162 . 19 ARG CB C 34.8 0.6 1 163 . 19 ARG HB3 H 1.78 0.11 2 164 . 19 ARG HB2 H 1.91 0.11 2 165 . 19 ARG C C 175.2 0.17 1 166 . 20 PHE N N 129.8 0.17 1 167 . 20 PHE H H 8.76 0.02 1 168 . 20 PHE CA C 58.9 0.4 1 169 . 20 PHE HA H 3.90 0.11 1 170 . 20 PHE CB C 39.2 0.6 1 171 . 20 PHE HB3 H 0.99 0.11 2 172 . 20 PHE HB2 H 2.36 0.11 2 173 . 20 PHE C C 173.8 0.17 1 174 . 21 ASP N N 128.0 0.17 1 175 . 21 ASP H H 8.16 0.02 1 176 . 21 ASP CA C 52.3 0.4 1 177 . 21 ASP HA H 4.71 0.11 1 178 . 21 ASP CB C 41.8 0.6 1 179 . 21 ASP HB3 H 2.35 0.11 2 180 . 21 ASP HB2 H 2.88 0.11 2 181 . 21 ASP C C 175.7 0.17 1 182 . 22 ALA N N 126.3 0.17 1 183 . 22 ALA H H 8.79 0.02 1 184 . 22 ALA CA C 53.7 0.4 1 185 . 22 ALA HA H 3.89 0.11 1 186 . 22 ALA CB C 18.7 0.6 1 187 . 22 ALA HB H 1.61 0.11 1 188 . 22 ALA C C 178.9 0.17 1 189 . 23 GLU N N 117.3 0.17 1 190 . 23 GLU H H 8.39 0.02 1 191 . 23 GLU CA C 59.2 0.4 1 192 . 23 GLU HA H 4.18 0.11 1 193 . 23 GLU CB C 29.6 0.6 1 194 . 23 GLU HB3 H 2.20 0.11 2 195 . 23 GLU HB2 H 2.31 0.11 2 196 . 23 GLU CG C 36.5 0.6 1 197 . 23 GLU HG3 H 2.42 0.11 2 198 . 23 GLU HG2 H 2.30 0.11 2 199 . 23 GLU C C 178.4 0.17 1 200 . 24 VAL N N 106.0 0.17 1 201 . 24 VAL H H 6.73 0.02 1 202 . 24 VAL CA C 60.1 0.4 1 203 . 24 VAL HA H 4.54 0.11 1 204 . 24 VAL CB C 32.1 0.6 1 205 . 24 VAL HB H 2.41 0.11 1 206 . 24 VAL CG1 C 21.2 0.6 2 207 . 24 VAL HG1 H 0.92 0.11 2 208 . 24 VAL CG2 C 18.4 0.6 2 209 . 24 VAL HG2 H 0.78 0.11 2 210 . 24 VAL C C 175.1 0.17 1 211 . 25 SER N N 116.3 0.17 1 212 . 25 SER H H 7.68 0.02 1 213 . 25 SER CA C 58.8 0.4 1 214 . 25 SER HA H 3.59 0.11 1 215 . 25 SER CB C 60.9 0.6 1 216 . 25 SER HB3 H 4.05 0.11 2 217 . 25 SER HB2 H 4.23 0.11 2 218 . 25 SER C C 173.5 0.17 1 219 . 26 GLN N N 113.9 0.17 1 220 . 26 GLN H H 6.79 0.02 1 221 . 26 GLN CA C 53.5 0.4 1 222 . 26 GLN HA H 4.76 0.11 1 223 . 26 GLN CB C 33.9 0.6 1 224 . 26 GLN HB3 H 1.60 0.11 2 225 . 26 GLN HB2 H 2.06 0.11 2 226 . 26 GLN CG C 32.9 0.6 1 227 . 26 GLN HG3 H 2.45 0.11 1 228 . 26 GLN HG2 H 2.45 0.11 1 229 . 26 GLN NE2 N 110.3 0.17 1 230 . 26 GLN HE21 H 7.40 0.11 2 231 . 26 GLN HE22 H 6.87 0.11 2 232 . 26 GLN C C 174.7 0.17 1 233 . 27 TRP N N 122.9 0.17 1 234 . 27 TRP H H 9.04 0.02 1 235 . 27 TRP CA C 57.9 0.4 1 236 . 27 TRP HA H 4.76 0.11 1 237 . 27 TRP CB C 29.7 0.6 1 238 . 27 TRP HB3 H 2.97 0.11 2 239 . 27 TRP HB2 H 3.21 0.11 2 240 . 27 TRP C C 173.8 0.17 1 241 . 28 LYS N N 123.1 0.17 1 242 . 28 LYS H H 9.09 0.02 1 243 . 28 LYS CA C 54.3 0.4 1 244 . 28 LYS HA H 5.01 0.11 1 245 . 28 LYS CB C 34.7 0.6 1 246 . 28 LYS HB3 H 2.03 0.11 1 247 . 28 LYS HB2 H 2.03 0.11 1 248 . 28 LYS C C 176.2 0.17 1 249 . 29 GLU N N 124.6 0.17 1 250 . 29 GLU H H 9.25 0.02 1 251 . 29 GLU CA C 58.2 0.4 1 252 . 29 GLU HA H 3.67 0.11 1 253 . 29 GLU CB C 30.3 0.6 1 254 . 29 GLU HB3 H 1.94 0.11 1 255 . 29 GLU HB2 H 1.94 0.11 1 256 . 29 GLU CG C 36.5 0.6 1 257 . 29 GLU HG3 H 1.90 0.11 1 258 . 29 GLU HG2 H 1.90 0.11 1 259 . 29 GLU C C 176.3 0.17 1 260 . 30 ARG N N 125.7 0.17 1 261 . 30 ARG H H 9.59 0.02 1 262 . 30 ARG CA C 54.9 0.4 1 263 . 30 ARG HA H 4.70 0.11 1 264 . 30 ARG CB C 31.8 0.6 1 265 . 30 ARG HB3 H 1.60 0.11 2 266 . 30 ARG HB2 H 1.80 0.11 2 267 . 30 ARG HG3 H 1.72 0.11 1 268 . 30 ARG HG2 H 1.72 0.11 1 269 . 30 ARG C C 175.4 0.17 1 270 . 31 GLY N N 103.2 0.17 1 271 . 31 GLY H H 7.34 0.02 1 272 . 31 GLY CA C 45.6 0.4 1 273 . 31 GLY HA2 H 4.30 0.11 2 274 . 31 GLY HA3 H 4.09 0.11 2 275 . 31 GLY C C 169.7 0.17 1 276 . 32 LEU N N 121.6 0.17 1 277 . 32 LEU H H 8.30 0.02 1 278 . 32 LEU CA C 53.9 0.4 1 279 . 32 LEU HA H 5.31 0.11 1 280 . 32 LEU CB C 45.2 0.6 1 281 . 32 LEU HB3 H 1.64 0.11 1 282 . 32 LEU HB2 H 1.64 0.11 1 283 . 32 LEU CG C 28.0 0.6 1 284 . 32 LEU HG H 1.58 0.11 1 285 . 32 LEU CD1 C 25.0 0.6 1 286 . 32 LEU HD1 H 0.96 0.11 1 287 . 32 LEU C C 176.2 0.17 1 288 . 33 GLY N N 108.0 0.17 1 289 . 33 GLY H H 8.29 0.02 1 290 . 33 GLY CA C 45.2 0.4 1 291 . 33 GLY HA2 H 4.65 0.11 2 292 . 33 GLY HA3 H 4.09 0.11 2 293 . 33 GLY C C 170.9 0.17 1 294 . 34 ASN N N 117.5 0.17 1 295 . 34 ASN H H 8.91 0.02 1 296 . 34 ASN CA C 52.9 0.4 1 297 . 34 ASN HA H 5.18 0.11 1 298 . 34 ASN CB C 38.5 0.6 1 299 . 34 ASN HB3 H 2.44 0.11 2 300 . 34 ASN HB2 H 2.83 0.11 2 301 . 34 ASN ND2 N 113.7 0.17 1 302 . 34 ASN HD21 H 7.88 0.11 2 303 . 34 ASN HD22 H 6.85 0.11 2 304 . 34 ASN C C 173.6 0.17 1 305 . 35 LEU N N 130.3 0.17 1 306 . 35 LEU H H 9.25 0.02 1 307 . 35 LEU CA C 54.8 0.4 1 308 . 35 LEU HA H 4.72 0.11 1 309 . 35 LEU CB C 44.7 0.6 1 310 . 35 LEU HB3 H 1.54 0.11 2 311 . 35 LEU HB2 H 2.12 0.11 2 312 . 35 LEU C C 174.4 0.17 1 313 . 36 LYS N N 123.1 0.17 1 314 . 36 LYS H H 9.12 0.02 1 315 . 36 LYS CA C 54.4 0.4 1 316 . 36 LYS HA H 5.76 0.11 1 317 . 36 LYS CB C 36.9 0.6 1 318 . 36 LYS HB3 H 1.92 0.11 1 319 . 36 LYS HB2 H 1.92 0.11 1 320 . 36 LYS C C 175.5 0.17 1 321 . 37 ILE N N 117.5 0.17 1 322 . 37 ILE H H 8.27 0.02 1 323 . 37 ILE CA C 61.1 0.4 1 324 . 37 ILE HA H 5.09 0.11 1 325 . 37 ILE CB C 39.5 0.6 1 326 . 37 ILE HB H 1.77 0.11 1 327 . 37 ILE HG13 H 1.24 0.11 2 328 . 37 ILE HG12 H 1.95 0.11 2 329 . 37 ILE CG2 C 17.9 0.6 1 330 . 37 ILE HG2 H 0.98 0.11 1 331 . 37 ILE CD1 C 12.7 0.6 1 332 . 37 ILE HD1 H 0.71 0.11 1 333 . 37 ILE C C 175.4 0.17 1 334 . 38 LEU N N 127.5 0.17 1 335 . 38 LEU H H 9.65 0.02 1 336 . 38 LEU CA C 53.5 0.4 1 337 . 38 LEU HA H 5.53 0.11 1 338 . 38 LEU CB C 45.7 0.6 1 339 . 38 LEU HB3 H 1.64 0.11 2 340 . 38 LEU HB2 H 1.82 0.11 2 341 . 38 LEU HD1 H 0.96 0.11 4 342 . 38 LEU C C 175.5 0.17 1 343 . 39 LYS N N 120.0 0.17 1 344 . 39 LYS H H 9.23 0.02 1 345 . 39 LYS CA C 54.2 0.4 1 346 . 39 LYS HA H 5.29 0.11 1 347 . 39 LYS CB C 36.9 0.6 1 348 . 39 LYS HB3 H 1.64 0.11 2 349 . 39 LYS HB2 H 1.89 0.11 2 350 . 39 LYS C C 175.1 0.17 1 351 . 40 ASN N N 127.1 0.17 1 352 . 40 ASN H H 9.13 0.02 1 353 . 40 ASN CA C 53.5 0.4 1 354 . 40 ASN HA H 4.97 0.11 1 355 . 40 ASN CB C 39.2 0.6 1 356 . 40 ASN HB3 H 2.99 0.11 2 357 . 40 ASN HB2 H 3.61 0.11 2 358 . 40 ASN ND2 N 115.0 0.17 1 359 . 40 ASN HD21 H 8.26 0.11 2 360 . 40 ASN HD22 H 7.34 0.11 2 361 . 40 ASN C C 176.3 0.17 1 362 . 41 GLU N N 125.6 0.17 1 363 . 41 GLU H H 9.14 0.02 1 364 . 41 GLU CA C 58.3 0.4 1 365 . 41 GLU HA H 4.32 0.11 1 366 . 41 GLU CB C 30.4 0.6 1 367 . 41 GLU HB3 H 2.11 0.11 2 368 . 41 GLU HB2 H 2.28 0.11 2 369 . 41 GLU CG C 36.8 0.6 1 370 . 41 GLU HG3 H 2.29 0.11 2 371 . 41 GLU HG2 H 2.47 0.11 2 372 . 41 GLU C C 177.0 0.17 1 373 . 42 VAL N N 118.4 0.17 1 374 . 42 VAL H H 8.62 0.02 1 375 . 42 VAL CA C 64.8 0.4 1 376 . 42 VAL HA H 4.06 0.11 1 377 . 42 VAL CB C 32.1 0.6 1 378 . 42 VAL HB H 2.36 0.11 1 379 . 42 VAL CG1 C 21.7 0.6 2 380 . 42 VAL HG1 H 1.12 0.11 2 381 . 42 VAL CG2 C 20.7 0.6 2 382 . 42 VAL HG2 H 1.04 0.11 2 383 . 42 VAL C C 177.4 0.17 1 384 . 43 ASN N N 113.2 0.17 1 385 . 43 ASN H H 7.88 0.02 1 386 . 43 ASN CA C 51.8 0.4 1 387 . 43 ASN HA H 4.92 0.11 1 388 . 43 ASN CB C 39.3 0.6 1 389 . 43 ASN HB3 H 2.69 0.11 2 390 . 43 ASN HB2 H 3.19 0.11 2 391 . 43 ASN ND2 N 108.4 0.17 1 392 . 43 ASN HD21 H 7.39 0.11 2 393 . 43 ASN HD22 H 6.55 0.11 2 394 . 43 ASN C C 177.0 0.17 1 395 . 44 GLY N N 108.4 0.17 1 396 . 44 GLY H H 8.00 0.02 1 397 . 44 GLY CA C 46.4 0.4 1 398 . 44 GLY HA2 H 4.17 0.11 2 399 . 44 GLY HA3 H 3.86 0.11 2 400 . 44 GLY C C 174.1 0.17 1 401 . 45 LYS N N 118.2 0.17 1 402 . 45 LYS H H 8.10 0.02 1 403 . 45 LYS CA C 57.9 0.4 1 404 . 45 LYS HA H 4.14 0.11 1 405 . 45 LYS CB C 34.1 0.6 1 406 . 45 LYS HB3 H 1.71 0.11 1 407 . 45 LYS HB2 H 1.71 0.11 1 408 . 45 LYS C C 176.2 0.17 1 409 . 46 LEU N N 120.6 0.17 1 410 . 46 LEU H H 8.48 0.02 1 411 . 46 LEU CA C 53.3 0.4 1 412 . 46 LEU HA H 5.82 0.11 1 413 . 46 LEU CB C 46.9 0.6 1 414 . 46 LEU HB3 H 1.48 0.11 2 415 . 46 LEU HB2 H 1.91 0.11 2 416 . 46 LEU HD1 H 0.90 0.11 4 417 . 46 LEU C C 176.1 0.17 1 418 . 47 ARG N N 123.9 0.17 1 419 . 47 ARG H H 9.54 0.02 1 420 . 47 ARG CA C 54.7 0.4 1 421 . 47 ARG HA H 5.29 0.11 1 422 . 47 ARG CB C 36.4 0.6 1 423 . 47 ARG HB3 H 1.88 0.11 1 424 . 47 ARG HB2 H 1.88 0.11 1 425 . 48 MET N N 123.2 0.17 1 426 . 48 MET H H 9.07 0.02 1 427 . 48 MET CA C 54.2 0.4 1 428 . 48 MET HA H 5.43 0.11 1 429 . 48 MET CB C 35.3 0.6 1 430 . 48 MET HB3 H 1.43 0.11 1 431 . 48 MET HB2 H 1.43 0.11 1 432 . 48 MET CG C 32.5 0.6 1 433 . 48 MET HG3 H 2.43 0.11 2 434 . 48 MET HG2 H 2.59 0.11 2 435 . 48 MET C C 173.9 0.17 1 436 . 49 LEU N N 123.3 0.17 1 437 . 49 LEU H H 8.65 0.02 1 438 . 49 LEU CA C 53.0 0.4 1 439 . 49 LEU HA H 5.12 0.11 1 440 . 49 LEU CB C 47.7 0.6 1 441 . 49 LEU HB3 H 1.21 0.11 2 442 . 49 LEU HB2 H 1.58 0.11 2 443 . 49 LEU HD1 H 0.92 0.11 4 444 . 49 LEU C C 175.1 0.17 1 445 . 50 MET N N 124.9 0.17 1 446 . 50 MET H H 8.97 0.02 1 447 . 50 MET CA C 55.5 0.4 1 448 . 50 MET HA H 5.21 0.11 1 449 . 50 MET CB C 37.6 0.6 1 450 . 50 MET HB3 H 1.95 0.11 1 451 . 50 MET HB2 H 1.95 0.11 1 452 . 50 MET CG C 33.2 0.6 1 453 . 50 MET HG3 H 1.97 0.11 2 454 . 50 MET HG2 H 2.42 0.11 2 455 . 50 MET C C 174.3 0.17 1 456 . 51 ARG N N 125.7 0.17 1 457 . 51 ARG H H 8.81 0.02 1 458 . 51 ARG CA C 54.3 0.4 1 459 . 51 ARG HA H 5.11 0.11 1 460 . 51 ARG CB C 32.6 0.6 1 461 . 51 ARG HB3 H 1.53 0.11 2 462 . 51 ARG HB2 H 1.76 0.11 2 463 . 51 ARG CG C 27.8 0.6 1 464 . 51 ARG HG3 H 1.58 0.11 1 465 . 51 ARG HG2 H 1.58 0.11 1 466 . 51 ARG C C 175.5 0.17 1 467 . 52 ARG N N 123.1 0.17 1 468 . 52 ARG H H 8.80 0.02 1 469 . 52 ARG CA C 56.6 0.4 1 470 . 52 ARG HA H 4.31 0.11 1 471 . 52 ARG CB C 32.2 0.6 1 472 . 52 ARG HB3 H 1.76 0.11 2 473 . 52 ARG HB2 H 2.09 0.11 2 474 . 52 ARG C C 176.6 0.17 1 475 . 53 GLU N N 122.0 0.17 1 476 . 53 GLU H H 9.13 0.02 1 477 . 53 GLU CA C 57.2 0.4 1 478 . 53 GLU HA H 4.32 0.11 1 479 . 53 GLU CB C 30.0 0.6 1 480 . 53 GLU HB3 H 2.20 0.11 1 481 . 53 GLU HB2 H 2.20 0.11 1 482 . 53 GLU CG C 34.9 0.6 1 483 . 53 GLU HG3 H 2.32 0.11 2 484 . 53 GLU HG2 H 2.54 0.11 2 485 . 53 GLU C C 178.1 0.17 1 486 . 54 GLN N N 116.9 0.17 1 487 . 54 GLN H H 9.25 0.02 1 488 . 54 GLN CA C 61.0 0.4 1 489 . 54 GLN HA H 3.94 0.11 1 490 . 54 GLN CB C 28.0 0.6 1 491 . 54 GLN HB3 H 2.47 0.11 2 492 . 54 GLN HB2 H 2.55 0.11 2 493 . 54 GLN CG C 34.2 0.6 1 494 . 54 GLN HG3 H 2.47 0.11 1 495 . 54 GLN HG2 H 2.47 0.11 1 496 . 54 GLN C C 177.2 0.17 1 497 . 55 VAL N N 115.7 0.17 1 498 . 55 VAL H H 8.78 0.02 1 499 . 55 VAL CA C 62.3 0.4 1 500 . 55 VAL HA H 4.31 0.11 1 501 . 55 VAL CB C 32.8 0.6 1 502 . 55 VAL HB H 2.35 0.11 1 503 . 55 VAL CG1 C 21.6 0.6 2 504 . 55 VAL HG1 H 1.16 0.11 2 505 . 55 VAL CG2 C 20.2 0.6 2 506 . 55 VAL HG2 H 1.10 0.11 2 507 . 55 VAL C C 176.3 0.17 1 508 . 56 LEU N N 115.4 0.17 1 509 . 56 LEU H H 7.93 0.02 1 510 . 56 LEU CA C 56.4 0.4 1 511 . 56 LEU HA H 4.23 0.11 1 512 . 56 LEU CB C 38.5 0.6 1 513 . 56 LEU HB3 H 1.65 0.11 2 514 . 56 LEU HB2 H 2.13 0.11 2 515 . 56 LEU HG H 1.56 0.11 4 516 . 56 LEU C C 175.7 0.17 1 517 . 57 LYS N N 117.9 0.17 1 518 . 57 LYS H H 6.51 0.02 1 519 . 57 LYS CA C 55.5 0.4 1 520 . 57 LYS HA H 4.54 0.11 1 521 . 57 LYS CB C 34.6 0.6 1 522 . 57 LYS HB3 H 1.77 0.11 1 523 . 57 LYS HB2 H 1.77 0.11 1 524 . 57 LYS C C 176.4 0.17 1 525 . 58 VAL N N 127.3 0.17 1 526 . 58 VAL H H 9.11 0.02 1 527 . 58 VAL CA C 64.3 0.4 1 528 . 58 VAL HA H 4.30 0.11 1 529 . 58 VAL CB C 32.0 0.6 1 530 . 58 VAL HB H 2.28 0.11 1 531 . 58 VAL CG1 C 22.1 0.6 1 532 . 58 VAL HG1 H 1.21 0.11 2 533 . 58 VAL CG2 C 22.1 0.6 1 534 . 58 VAL HG2 H 1.14 0.11 2 535 . 58 VAL C C 176.2 0.17 1 536 . 59 CYS N N 121.9 0.17 1 537 . 59 CYS H H 9.11 0.02 1 538 . 59 CYS CA C 57.4 0.4 1 539 . 59 CYS HA H 4.93 0.11 1 540 . 59 CYS CB C 30.4 0.6 1 541 . 59 CYS HB3 H 2.53 0.11 2 542 . 59 CYS HB2 H 3.07 0.11 2 543 . 59 CYS C C 172.6 0.17 1 544 . 60 ALA N N 121.2 0.17 1 545 . 60 ALA H H 7.66 0.02 1 546 . 60 ALA CA C 52.9 0.4 1 547 . 60 ALA HA H 4.81 0.11 1 548 . 60 ALA CB C 21.2 0.6 1 549 . 60 ALA HB H 1.38 0.11 1 550 . 60 ALA C C 175.5 0.17 1 551 . 61 ASN N N 121.1 0.17 1 552 . 61 ASN H H 9.77 0.02 1 553 . 61 ASN CA C 52.4 0.4 1 554 . 61 ASN HA H 5.28 0.11 1 555 . 61 ASN CB C 37.6 0.6 1 556 . 61 ASN HB3 H 2.29 0.11 2 557 . 61 ASN HB2 H 2.65 0.11 2 558 . 61 ASN ND2 N 104.7 0.17 1 559 . 61 ASN HD21 H 7.02 0.11 2 560 . 61 ASN HD22 H 6.48 0.11 2 561 . 61 ASN C C 172.3 0.17 1 562 . 62 HIS N N 117.1 0.17 1 563 . 62 HIS H H 8.34 0.02 1 564 . 62 HIS CA C 54.3 0.4 1 565 . 62 HIS HA H 4.62 0.11 1 566 . 62 HIS CB C 31.6 0.6 1 567 . 62 HIS HB3 H 3.56 0.11 2 568 . 62 HIS HB2 H 3.22 0.11 2 569 . 62 HIS C C 173.4 0.17 1 570 . 63 TRP N N 118.6 0.17 1 571 . 63 TRP H H 8.64 0.02 1 572 . 63 TRP CA C 56.1 0.4 1 573 . 63 TRP HA H 5.73 0.11 1 574 . 63 TRP CB C 30.3 0.6 1 575 . 63 TRP HB3 H 3.32 0.11 2 576 . 63 TRP HB2 H 3.72 0.11 2 577 . 63 TRP C C 178.0 0.17 1 578 . 64 ILE N N 122.7 0.17 1 579 . 64 ILE H H 8.75 0.02 1 580 . 64 ILE CA C 62.6 0.4 1 581 . 64 ILE HA H 4.64 0.11 1 582 . 64 ILE CB C 38.3 0.6 1 583 . 64 ILE HB H 1.80 0.11 1 584 . 64 ILE HG13 H 1.22 0.11 2 585 . 64 ILE HG12 H 1.89 0.11 2 586 . 64 ILE CG2 C 16.9 0.6 1 587 . 64 ILE HG2 H 0.90 0.11 1 588 . 64 ILE CD1 C 14.0 0.6 1 589 . 64 ILE HD1 H 0.91 0.11 1 590 . 64 ILE C C 175.2 0.17 1 591 . 65 THR N N 114.6 0.17 1 592 . 65 THR H H 7.40 0.02 1 593 . 65 THR CA C 59.2 0.4 1 594 . 65 THR HA H 5.23 0.11 1 595 . 65 THR CB C 71.7 0.6 1 596 . 65 THR HB H 4.84 0.11 1 597 . 65 THR CG2 C 21.3 0.6 1 598 . 65 THR HG2 H 1.53 0.11 1 599 . 65 THR C C 176.4 0.17 1 600 . 66 THR N N 109.5 0.17 1 601 . 66 THR H H 8.99 0.02 1 602 . 66 THR CA C 64.4 0.4 1 603 . 66 THR HA H 4.18 0.11 1 604 . 66 THR CB C 68.7 0.6 1 605 . 66 THR HB H 4.52 0.11 1 606 . 66 THR CG2 C 23.0 0.6 1 607 . 66 THR HG2 H 1.44 0.11 1 608 . 66 THR C C 175.3 0.17 1 609 . 67 THR N N 107.6 0.17 1 610 . 67 THR H H 7.55 0.02 1 611 . 67 THR CA C 61.5 0.4 1 612 . 67 THR HA H 4.54 0.11 1 613 . 67 THR CB C 68.9 0.6 1 614 . 67 THR HB H 4.59 0.11 1 615 . 67 THR CG2 C 21.7 0.6 1 616 . 67 THR HG2 H 1.35 0.11 1 617 . 67 THR C C 175.0 0.17 1 618 . 68 MET N N 122.3 0.17 1 619 . 68 MET H H 7.03 0.02 1 620 . 68 MET CA C 57.0 0.4 1 621 . 68 MET HA H 4.59 0.11 1 622 . 68 MET CB C 35.3 0.6 1 623 . 68 MET HB3 H 2.40 0.11 2 624 . 68 MET HB2 H 2.45 0.11 2 625 . 68 MET CG C 31.8 0.6 1 626 . 68 MET HG3 H 2.88 0.11 2 627 . 68 MET HG2 H 3.10 0.11 2 628 . 68 MET C C 174.5 0.17 1 629 . 69 ASN N N 119.6 0.17 1 630 . 69 ASN H H 8.51 0.02 1 631 . 69 ASN CA C 52.4 0.4 1 632 . 69 ASN HA H 5.15 0.11 1 633 . 69 ASN CB C 41.7 0.6 1 634 . 69 ASN HB3 H 2.81 0.11 2 635 . 69 ASN HB2 H 2.95 0.11 2 636 . 69 ASN ND2 N 112.5 0.17 1 637 . 69 ASN HD21 H 7.54 0.11 2 638 . 69 ASN HD22 H 6.96 0.11 2 639 . 69 ASN C C 173.1 0.17 1 640 . 70 LEU N N 120.7 0.17 1 641 . 70 LEU H H 8.53 0.02 1 642 . 70 LEU CA C 54.3 0.4 1 643 . 70 LEU HA H 5.02 0.11 1 644 . 70 LEU CB C 42.1 0.6 1 645 . 70 LEU HB3 H 1.04 0.11 2 646 . 70 LEU HB2 H 1.18 0.11 2 647 . 70 LEU CG C 25.9 0.6 1 648 . 70 LEU HG H 0.96 0.11 1 649 . 70 LEU CD1 C 25.6 0.6 2 650 . 70 LEU HD1 H -0.16 0.11 2 651 . 70 LEU CD2 C 22.0 0.6 2 652 . 70 LEU HD2 H 0.00 0.11 2 653 . 70 LEU C C 176.8 0.17 1 654 . 71 LYS N N 122.5 0.17 1 655 . 71 LYS H H 9.32 0.02 1 656 . 71 LYS CA C 53.2 0.4 1 657 . 71 LYS HA H 5.31 0.11 1 658 . 71 LYS CB C 34.8 0.6 1 659 . 71 LYS HB3 H 1.90 0.11 2 660 . 71 LYS HB2 H 2.17 0.11 2 661 . 72 PRO CA C 63.2 0.4 1 662 . 72 PRO HA H 4.62 0.11 1 663 . 72 PRO CB C 31.7 0.6 1 664 . 72 PRO HB3 H 1.94 0.11 2 665 . 72 PRO HB2 H 2.35 0.11 2 666 . 72 PRO CG C 27.4 0.6 1 667 . 72 PRO HG3 H 2.30 0.11 1 668 . 72 PRO HG2 H 2.30 0.11 1 669 . 72 PRO CD C 50.4 0.6 1 670 . 72 PRO HD3 H 3.96 0.11 2 671 . 72 PRO HD2 H 4.26 0.11 2 672 . 72 PRO C C 176.4 0.17 1 673 . 73 LEU N N 123.2 0.17 1 674 . 73 LEU H H 7.64 0.02 1 675 . 73 LEU CA C 53.9 0.4 1 676 . 73 LEU HA H 4.33 0.11 1 677 . 73 LEU CB C 43.4 0.6 1 678 . 73 LEU HB3 H 0.70 0.11 2 679 . 73 LEU HB2 H 1.52 0.11 2 680 . 73 LEU CG C 26.5 0.6 1 681 . 73 LEU HG H 1.20 0.11 1 682 . 73 LEU CD1 C 24.4 0.6 2 683 . 73 LEU HD1 H 0.09 0.11 2 684 . 73 LEU CD2 C 22.9 0.6 2 685 . 73 LEU HD2 H -0.01 0.11 2 686 . 74 SER N N 121.1 0.17 1 687 . 74 SER H H 8.49 0.02 1 688 . 74 SER CA C 59.7 0.4 1 689 . 74 SER HA H 4.17 0.11 1 690 . 74 SER CB C 62.5 0.6 1 691 . 74 SER HB3 H 3.87 0.11 2 692 . 74 SER HB2 H 3.94 0.11 2 693 . 74 SER C C 175.5 0.17 1 694 . 75 GLY N N 111.0 0.17 1 695 . 75 GLY H H 8.66 0.02 1 696 . 75 GLY CA C 45.3 0.4 1 697 . 75 GLY HA2 H 4.17 0.11 2 698 . 75 GLY HA3 H 3.80 0.11 2 699 . 75 GLY C C 173.7 0.17 1 700 . 76 SER N N 111.9 0.17 1 701 . 76 SER H H 7.78 0.02 1 702 . 76 SER CA C 57.1 0.4 1 703 . 76 SER HA H 4.73 0.11 1 704 . 76 SER CB C 64.9 0.6 1 705 . 76 SER HB3 H 3.48 0.11 2 706 . 76 SER HB2 H 3.69 0.11 2 707 . 76 SER C C 174.1 0.17 1 708 . 77 ASP N N 124.8 0.17 1 709 . 77 ASP H H 8.28 0.02 1 710 . 77 ASP CA C 52.8 0.4 1 711 . 77 ASP HA H 4.72 0.11 1 712 . 77 ASP CB C 40.6 0.6 1 713 . 77 ASP HB3 H 2.72 0.11 2 714 . 77 ASP HB2 H 3.10 0.11 2 715 . 77 ASP C C 176.2 0.17 1 716 . 78 ARG N N 114.7 0.17 1 717 . 78 ARG H H 8.38 0.02 1 718 . 78 ARG CA C 53.9 0.4 1 719 . 78 ARG HA H 4.53 0.11 1 720 . 78 ARG CB C 28.7 0.6 1 721 . 78 ARG HB3 H 1.21 0.11 2 722 . 78 ARG HB2 H 1.74 0.11 2 723 . 78 ARG C C 172.5 0.17 1 724 . 79 ALA N N 118.7 0.17 1 725 . 79 ALA H H 7.08 0.02 1 726 . 79 ALA CA C 51.3 0.4 1 727 . 79 ALA HA H 5.79 0.11 1 728 . 79 ALA CB C 24.4 0.6 1 729 . 79 ALA HB H 1.19 0.11 1 730 . 79 ALA C C 176.4 0.17 1 731 . 80 TRP N N 117.7 0.17 1 732 . 80 TRP H H 8.27 0.02 1 733 . 80 TRP CA C 54.5 0.4 1 734 . 80 TRP HA H 5.68 0.11 1 735 . 80 TRP CB C 36.5 0.6 1 736 . 80 TRP HB3 H 3.17 0.11 2 737 . 80 TRP HB2 H 3.69 0.11 2 738 . 80 TRP C C 174.0 0.17 1 739 . 81 MET N N 117.8 0.17 1 740 . 81 MET H H 10.21 0.02 1 741 . 81 MET CA C 53.9 0.4 1 742 . 81 MET HA H 6.17 0.11 1 743 . 81 MET CB C 37.3 0.6 1 744 . 81 MET HB3 H 1.86 0.11 2 745 . 81 MET HB2 H 2.44 0.11 2 746 . 81 MET CG C 31.4 0.6 1 747 . 81 MET HG3 H 2.70 0.11 2 748 . 81 MET HG2 H 2.78 0.11 2 749 . 81 MET C C 174.8 0.17 1 750 . 82 TRP N N 119.4 0.17 1 751 . 82 TRP H H 9.36 0.02 1 752 . 82 TRP CA C 57.8 0.4 1 753 . 82 TRP HA H 5.27 0.11 1 754 . 82 TRP CB C 32.2 0.6 1 755 . 82 TRP HB3 H 3.18 0.11 2 756 . 82 TRP HB2 H 3.82 0.11 2 757 . 82 TRP C C 177.5 0.17 1 758 . 83 LEU N N 119.9 0.17 1 759 . 83 LEU H H 8.37 0.02 1 760 . 83 LEU CA C 53.7 0.4 1 761 . 83 LEU HA H 5.34 0.11 1 762 . 83 LEU CB C 44.5 0.6 1 763 . 83 LEU HB3 H 1.72 0.11 2 764 . 83 LEU HB2 H 1.76 0.11 2 765 . 83 LEU CG C 27.7 0.6 1 766 . 83 LEU HG H 1.71 0.11 1 767 . 83 LEU CD1 C 24.5 0.6 1 768 . 83 LEU HD1 H 1.02 0.11 1 769 . 83 LEU C C 176.7 0.17 1 770 . 84 ALA N N 124.2 0.17 1 771 . 84 ALA H H 9.00 0.02 1 772 . 84 ALA CA C 50.8 0.4 1 773 . 84 ALA HA H 4.71 0.11 1 774 . 84 ALA CB C 22.6 0.6 1 775 . 84 ALA HB H 0.77 0.11 1 776 . 84 ALA C C 175.6 0.17 1 777 . 85 SER N N 115.2 0.17 1 778 . 85 SER H H 8.08 0.02 1 779 . 85 SER CA C 56.9 0.4 1 780 . 85 SER HA H 4.83 0.11 1 781 . 85 SER CB C 61.3 0.6 1 782 . 85 SER HB3 H 3.88 0.11 2 783 . 85 SER HB2 H 4.02 0.11 2 784 . 85 SER C C 172.7 0.17 1 785 . 86 ASP N N 126.8 0.17 1 786 . 86 ASP H H 8.89 0.02 1 787 . 86 ASP CA C 55.1 0.4 1 788 . 86 ASP HA H 5.06 0.11 1 789 . 86 ASP CB C 46.0 0.6 1 790 . 86 ASP HB3 H 2.36 0.11 2 791 . 86 ASP HB2 H 2.98 0.11 2 792 . 86 ASP C C 176.2 0.17 1 793 . 87 PHE N N 121.5 0.17 1 794 . 87 PHE H H 8.88 0.02 1 795 . 87 PHE CA C 56.4 0.4 1 796 . 87 PHE HA H 5.29 0.11 1 797 . 87 PHE CB C 38.4 0.6 1 798 . 87 PHE HB3 H 2.94 0.11 2 799 . 87 PHE HB2 H 3.50 0.11 2 800 . 87 PHE C C 177.3 0.17 1 801 . 88 SER N N 118.2 0.17 1 802 . 88 SER H H 8.69 0.02 1 803 . 88 SER CA C 63.4 0.4 1 804 . 88 SER HA H 4.09 0.11 1 805 . 88 SER CB C 62.9 0.6 1 806 . 88 SER HB3 H 3.70 0.11 1 807 . 88 SER HB2 H 3.70 0.11 1 808 . 88 SER C C 175 0.17 1 809 . 89 ASP N N 118.1 0.17 1 810 . 89 ASP H H 8.53 0.02 1 811 . 89 ASP CA C 53.8 0.4 1 812 . 89 ASP HA H 5.06 0.11 1 813 . 89 ASP CB C 41.6 0.6 1 814 . 89 ASP HB3 H 2.75 0.11 2 815 . 89 ASP HB2 H 2.99 0.11 2 816 . 89 ASP C C 176.0 0.17 1 817 . 90 GLY N N 108.4 0.17 1 818 . 90 GLY H H 7.76 0.02 1 819 . 90 GLY CA C 45.8 0.4 1 820 . 90 GLY HA2 H 4.54 0.11 2 821 . 90 GLY HA3 H 3.73 0.11 2 822 . 90 GLY C C 173.0 0.17 1 823 . 91 ASP N N 121.0 0.17 1 824 . 91 ASP H H 8.07 0.02 1 825 . 91 ASP CA C 53.8 0.4 1 826 . 91 ASP HA H 4.77 0.11 1 827 . 91 ASP CB C 41.9 0.6 1 828 . 91 ASP HB3 H 2.64 0.11 2 829 . 91 ASP HB2 H 2.79 0.11 2 830 . 91 ASP C C 175.3 0.17 1 831 . 92 ALA N N 122.7 0.17 1 832 . 92 ALA H H 8.39 0.02 1 833 . 92 ALA CA C 52.7 0.4 1 834 . 92 ALA HA H 4.38 0.11 1 835 . 92 ALA CB C 18.8 0.6 1 836 . 92 ALA HB H 1.38 0.11 1 837 . 92 ALA C C 177.6 0.17 1 838 . 93 LYS N N 122.1 0.17 1 839 . 93 LYS H H 8.55 0.02 1 840 . 93 LYS CA C 55.0 0.4 1 841 . 93 LYS HA H 4.70 0.11 1 842 . 93 LYS CB C 35.6 0.6 1 843 . 93 LYS HB3 H 1.92 0.11 1 844 . 93 LYS HB2 H 1.92 0.11 1 845 . 93 LYS C C 174.9 0.17 1 846 . 94 LEU N N 124.3 0.17 1 847 . 94 LEU H H 8.54 0.02 1 848 . 94 LEU CA C 55.6 0.4 1 849 . 94 LEU HA H 4.87 0.11 1 850 . 94 LEU CB C 41.7 0.6 1 851 . 94 LEU HB3 H 1.70 0.11 2 852 . 94 LEU HB2 H 1.78 0.11 2 853 . 94 LEU C C 176.7 0.17 1 854 . 95 GLU N N 125.8 0.17 1 855 . 95 GLU H H 9.28 0.02 1 856 . 95 GLU CA C 54.4 0.4 1 857 . 95 GLU HA H 4.97 0.11 1 858 . 95 GLU CB C 33.7 0.6 1 859 . 95 GLU HB3 H 1.74 0.11 2 860 . 95 GLU HB2 H 2.07 0.11 2 861 . 95 GLU CG C 34.9 0.6 1 862 . 95 GLU HG3 H 2.42 0.11 1 863 . 95 GLU HG2 H 2.42 0.11 1 864 . 95 GLU C C 174.3 0.17 1 865 . 96 GLN N N 121.1 0.17 1 866 . 96 GLN H H 9.05 0.02 1 867 . 96 GLN CA C 55.1 0.4 1 868 . 96 GLN HA H 5.06 0.11 1 869 . 96 GLN CB C 30.4 0.6 1 870 . 96 GLN HB3 H 1.91 0.11 2 871 . 96 GLN HB2 H 2.11 0.11 2 872 . 96 GLN CG C 34.4 0.6 1 873 . 96 GLN HG3 H 2.21 0.11 2 874 . 96 GLN HG2 H 2.36 0.11 2 875 . 96 GLN NE2 N 119.4 0.17 1 876 . 96 GLN HE21 H 6.81 0.11 2 877 . 96 GLN HE22 H 6.48 0.11 2 878 . 96 GLN C C 173.8 0.17 1 879 . 97 LEU N N 125.4 0.17 1 880 . 97 LEU H H 8.63 0.02 1 881 . 97 LEU CA C 52.9 0.4 1 882 . 97 LEU HA H 5.46 0.11 1 883 . 97 LEU CB C 45.5 0.6 1 884 . 97 LEU HB3 H 0.40 0.11 2 885 . 97 LEU HB2 H 0.83 0.11 2 886 . 97 LEU C C 174.9 0.17 1 887 . 98 ALA N N 115.3 0.17 1 888 . 98 ALA H H 8.35 0.02 1 889 . 98 ALA CA C 51.0 0.4 1 890 . 98 ALA HA H 5.41 0.11 1 891 . 98 ALA CB C 24.0 0.6 1 892 . 98 ALA HB H 0.69 0.11 1 893 . 98 ALA C C 175.4 0.17 1 894 . 99 ALA N N 120.9 0.17 1 895 . 99 ALA H H 8.95 0.02 1 896 . 99 ALA CA C 49.9 0.4 1 897 . 99 ALA HA H 5.48 0.11 1 898 . 99 ALA CB C 22.1 0.6 1 899 . 99 ALA HB H 1.28 0.11 1 900 . 99 ALA C C 174.4 0.17 1 901 . 100 LYS N N 120.4 0.17 1 902 . 100 LYS H H 9.12 0.02 1 903 . 100 LYS CA C 55.1 0.4 1 904 . 100 LYS HA H 5.05 0.11 1 905 . 100 LYS CB C 36.6 0.6 1 906 . 100 LYS HB3 H 1.66 0.11 2 907 . 100 LYS HB2 H 2.05 0.11 2 908 . 100 LYS C C 175.5 0.17 1 909 . 101 PHE N N 124.9 0.17 1 910 . 101 PHE H H 9.05 0.02 1 911 . 101 PHE CA C 57.2 0.4 1 912 . 101 PHE HA H 4.70 0.11 1 913 . 101 PHE CB C 42.7 0.6 1 914 . 101 PHE HB3 H 3.01 0.11 2 915 . 101 PHE HB2 H 3.32 0.11 2 916 . 101 PHE C C 176.8 0.17 1 917 . 102 LYS N N 117.9 0.17 1 918 . 102 LYS H H 9.25 0.02 1 919 . 102 LYS CA C 59.5 0.4 1 920 . 102 LYS HA H 4.18 0.11 1 921 . 102 LYS CB C 33.7 0.6 1 922 . 102 LYS HB3 H 2.07 0.11 2 923 . 102 LYS HB2 H 2.19 0.11 2 924 . 102 LYS CG C 25.0 0.6 1 925 . 102 LYS HG3 H 1.72 0.11 2 926 . 102 LYS HG2 H 1.81 0.11 2 927 . 102 LYS CD C 28.8 0.6 1 928 . 102 LYS HD3 H 1.93 0.11 1 929 . 102 LYS HD2 H 1.93 0.11 1 930 . 102 LYS CE C 41.7 0.6 1 931 . 102 LYS HE3 H 3.17 0.11 1 932 . 102 LYS HE2 H 3.17 0.11 1 933 . 102 LYS C C 177.2 0.17 1 934 . 103 THR N N 100.8 0.17 1 935 . 103 THR H H 7.21 0.02 1 936 . 103 THR CA C 57.4 0.4 1 937 . 103 THR HA H 5.16 0.11 1 938 . 103 THR CB C 70.3 0.6 1 939 . 103 THR HB H 4.92 0.11 1 940 . 103 THR CG2 C 21.9 0.6 1 941 . 103 THR HG2 H 1.41 0.11 1 942 . 104 PRO CA C 65.1 0.4 1 943 . 104 PRO HA H 4.42 0.11 1 944 . 104 PRO CB C 32.3 0.6 1 945 . 104 PRO HB3 H 2.10 0.11 2 946 . 104 PRO HB2 H 2.66 0.11 2 947 . 104 PRO HG3 H 1.78 0.11 1 948 . 104 PRO HG2 H 1.78 0.11 1 949 . 104 PRO C C 178.8 0.17 1 950 . 105 GLU N N 117.2 0.17 1 951 . 105 GLU H H 9.02 0.02 1 952 . 105 GLU CA C 61.0 0.4 1 953 . 105 GLU HA H 4.18 0.11 1 954 . 105 GLU CB C 28.7 0.6 1 955 . 105 GLU HB3 H 2.08 0.11 2 956 . 105 GLU HB2 H 2.28 0.11 2 957 . 105 GLU CG C 37.3 0.6 1 958 . 105 GLU HG3 H 2.43 0.11 2 959 . 105 GLU HG2 H 2.64 0.11 2 960 . 105 GLU C C 180.2 0.17 1 961 . 106 LEU N N 120.5 0.17 1 962 . 106 LEU H H 8.03 0.02 1 963 . 106 LEU CA C 57.6 0.4 1 964 . 106 LEU HA H 4.37 0.11 1 965 . 106 LEU CB C 41.9 0.6 1 966 . 106 LEU HB3 H 1.92 0.11 1 967 . 106 LEU HB2 H 1.92 0.11 1 968 . 106 LEU C C 179.9 0.17 1 969 . 107 ALA N N 122.7 0.17 1 970 . 107 ALA H H 7.68 0.02 1 971 . 107 ALA CA C 54.9 0.4 1 972 . 107 ALA HA H 2.95 0.11 1 973 . 107 ALA CB C 17.1 0.6 1 974 . 107 ALA HB H 1.39 0.11 1 975 . 107 ALA C C 181.1 0.17 1 976 . 108 GLU N N 122.1 0.17 1 977 . 108 GLU H H 8.77 0.02 1 978 . 108 GLU CA C 59.4 0.4 1 979 . 108 GLU HA H 4.40 0.11 1 980 . 108 GLU CB C 29.1 0.6 1 981 . 108 GLU HB3 H 2.27 0.11 2 982 . 108 GLU HB2 H 2.35 0.11 2 983 . 108 GLU CG C 35.7 0.6 1 984 . 108 GLU HG3 H 2.54 0.11 1 985 . 108 GLU HG2 H 2.54 0.11 1 986 . 108 GLU C C 178.3 0.17 1 987 . 109 GLU N N 120.0 0.17 1 988 . 109 GLU H H 8.06 0.02 1 989 . 109 GLU CA C 59.5 0.4 1 990 . 109 GLU HA H 4.14 0.11 1 991 . 109 GLU CB C 29.6 0.6 1 992 . 109 GLU HB3 H 2.33 0.11 1 993 . 109 GLU HB2 H 2.33 0.11 1 994 . 109 GLU CG C 36.8 0.6 1 995 . 109 GLU HG3 H 2.35 0.11 2 996 . 109 GLU HG2 H 2.57 0.11 2 997 . 109 GLU C C 178.5 0.17 1 998 . 110 PHE N N 118.3 0.17 1 999 . 110 PHE H H 7.69 0.02 1 1000 . 110 PHE CA C 61.3 0.4 1 1001 . 110 PHE HA H 3.86 0.11 1 1002 . 110 PHE CB C 39.6 0.6 1 1003 . 110 PHE HB3 H 2.64 0.11 2 1004 . 110 PHE HB2 H 3.39 0.11 2 1005 . 110 PHE C C 175.6 0.17 1 1006 . 111 LYS N N 118.6 0.17 1 1007 . 111 LYS H H 7.47 0.02 1 1008 . 111 LYS CA C 59.2 0.4 1 1009 . 111 LYS HA H 3.16 0.11 1 1010 . 111 LYS CB C 32.2 0.6 1 1011 . 111 LYS HB3 H 0.94 0.11 2 1012 . 111 LYS HB2 H 1.85 0.11 2 1013 . 111 LYS C C 177.5 0.17 1 1014 . 112 GLN N N 115.3 0.17 1 1015 . 112 GLN H H 8.00 0.02 1 1016 . 112 GLN CA C 58.8 0.4 1 1017 . 112 GLN HA H 4.03 0.11 1 1018 . 112 GLN CB C 28.1 0.6 1 1019 . 112 GLN HB3 H 2.19 0.11 1 1020 . 112 GLN HB2 H 2.19 0.11 1 1021 . 112 GLN CG C 33.5 0.6 1 1022 . 112 GLN HG3 H 2.47 0.11 2 1023 . 112 GLN HG2 H 2.63 0.11 2 1024 . 112 GLN C C 179.2 0.17 1 1025 . 113 LYS N N 119.8 0.17 1 1026 . 113 LYS H H 8.13 0.02 1 1027 . 113 LYS CA C 57.1 0.4 1 1028 . 113 LYS HA H 4.08 0.11 1 1029 . 113 LYS CB C 30.4 0.6 1 1030 . 113 LYS HB3 H 1.36 0.11 2 1031 . 113 LYS HB2 H 1.69 0.11 2 1032 . 113 LYS C C 178.5 0.17 1 1033 . 114 PHE N N 121.6 0.17 1 1034 . 114 PHE H H 8.95 0.02 1 1035 . 114 PHE CA C 62.3 0.4 1 1036 . 114 PHE HA H 3.46 0.11 1 1037 . 114 PHE CB C 39.1 0.6 1 1038 . 114 PHE HB3 H 1.96 0.11 2 1039 . 114 PHE HB2 H 2.67 0.11 2 1040 . 114 PHE C C 177.0 0.17 1 1041 . 115 GLU N N 116.7 0.17 1 1042 . 115 GLU H H 8.19 0.02 1 1043 . 115 GLU CA C 59.5 0.4 1 1044 . 115 GLU HA H 3.94 0.11 1 1045 . 115 GLU CB C 28.9 0.6 1 1046 . 115 GLU HB3 H 2.15 0.11 2 1047 . 115 GLU HB2 H 2.03 0.11 2 1048 . 115 GLU CG C 37.3 0.6 1 1049 . 115 GLU HG3 H 2.36 0.11 2 1050 . 115 GLU HG2 H 2.76 0.11 2 1051 . 115 GLU C C 179.6 0.17 1 1052 . 116 GLU N N 120.0 0.17 1 1053 . 116 GLU H H 8.06 0.02 1 1054 . 116 GLU CA C 59.6 0.4 1 1055 . 116 GLU HA H 4.01 0.11 1 1056 . 116 GLU CB C 29.9 0.6 1 1057 . 116 GLU HB3 H 2.29 0.11 1 1058 . 116 GLU HB2 H 2.29 0.11 1 1059 . 116 GLU CG C 36.1 0.6 1 1060 . 116 GLU HG3 H 2.44 0.11 2 1061 . 116 GLU HG2 H 2.21 0.11 2 1062 . 116 GLU C C 179.4 0.17 1 1063 . 117 CYS N N 116.7 0.17 1 1064 . 117 CYS H H 8.23 0.02 1 1065 . 117 CYS CA C 63.6 0.4 1 1066 . 117 CYS HA H 4.08 0.11 1 1067 . 117 CYS CB C 25.8 0.6 1 1068 . 117 CYS HB3 H 2.50 0.11 2 1069 . 117 CYS HB2 H 2.98 0.11 2 1070 . 117 CYS C C 176.3 0.17 1 1071 . 118 GLN N N 117.5 0.17 1 1072 . 118 GLN H H 8.09 0.02 1 1073 . 118 GLN CA C 59.3 0.4 1 1074 . 118 GLN HA H 3.59 0.11 1 1075 . 118 GLN CB C 29.4 0.6 1 1076 . 118 GLN HB3 H 1.82 0.11 2 1077 . 118 GLN HB2 H 1.96 0.11 2 1078 . 118 GLN CG C 34.9 0.6 1 1079 . 118 GLN HG3 H 1.81 0.11 2 1080 . 118 GLN HG2 H 1.97 0.11 2 1081 . 118 GLN C C 177.9 0.17 1 1082 . 119 ARG N N 116.4 0.17 1 1083 . 119 ARG H H 7.57 0.02 1 1084 . 119 ARG CA C 59.1 0.4 1 1085 . 119 ARG HA H 4.11 0.11 1 1086 . 119 ARG CB C 29.7 0.6 1 1087 . 119 ARG HB3 H 2.02 0.11 1 1088 . 119 ARG HB2 H 2.02 0.11 1 1089 . 119 ARG CG C 28.0 0.6 1 1090 . 119 ARG HG3 H 1.74 0.11 2 1091 . 119 ARG HG2 H 2.00 0.11 2 1092 . 119 ARG CD C 43.3 0.6 1 1093 . 119 ARG HD3 H 3.29 0.11 2 1094 . 119 ARG HD2 H 3.35 0.11 2 1095 . 119 ARG NE N 123.4 0.17 1 1096 . 119 ARG HE H 7.40 0.11 1 1097 . 119 ARG C C 178.6 0.17 1 1098 . 120 LEU N N 117.7 0.17 1 1099 . 120 LEU H H 7.68 0.02 1 1100 . 120 LEU CA C 56.7 0.4 1 1101 . 120 LEU HA H 4.29 0.11 1 1102 . 120 LEU CB C 41.6 0.6 1 1103 . 120 LEU HB3 H 1.71 0.11 2 1104 . 120 LEU HB2 H 2.11 0.11 2 1105 . 120 LEU CD1 C 25.1 0.6 4 1106 . 120 LEU HD1 H 1.01 0.11 4 1107 . 120 LEU C C 179.2 0.17 1 1108 . 121 LEU N N 116.5 0.17 1 1109 . 121 LEU H H 7.49 0.02 1 1110 . 121 LEU CA C 55.9 0.4 1 1111 . 121 LEU HA H 4.30 0.11 1 1112 . 121 LEU CB C 42.2 0.6 1 1113 . 121 LEU HB3 H 1.65 0.11 2 1114 . 121 LEU HB2 H 2.00 0.11 2 1115 . 121 LEU HD1 H 0.97 0.11 4 1116 . 121 LEU C C 178.0 0.17 1 1117 . 122 LEU N N 117.9 0.17 1 1118 . 122 LEU H H 7.53 0.02 1 1119 . 122 LEU CA C 55.5 0.4 1 1120 . 122 LEU HA H 4.39 0.11 1 1121 . 122 LEU CB C 42.4 0.6 1 1122 . 122 LEU HB3 H 1.67 0.11 2 1123 . 122 LEU HB2 H 1.86 0.11 2 1124 . 122 LEU C C 177.0 0.17 1 1125 . 123 ASP N N 118.9 0.17 1 1126 . 123 ASP H H 7.94 0.02 1 1127 . 123 ASP CA C 54.3 0.4 1 1128 . 123 ASP HA H 4.74 0.11 1 1129 . 123 ASP CB C 41.0 0.6 1 1130 . 123 ASP HB3 H 2.68 0.11 2 1131 . 123 ASP HB2 H 2.87 0.11 2 1132 . 123 ASP C C 173.0 0.17 1 1133 . 124 ILE N N 121.1 0.17 1 1134 . 124 ILE H H 7.79 0.02 1 1135 . 124 ILE CA C 59.3 0.4 1 1136 . 124 ILE HA H 4.51 0.11 1 1137 . 124 ILE CB C 38.6 0.6 1 1138 . 124 ILE HB H 1.99 0.11 1 1139 . 124 ILE CG1 C 27.0 0.6 1 1140 . 124 ILE HG13 H 1.27 0.11 2 1141 . 124 ILE HG12 H 1.67 0.11 2 1142 . 124 ILE CG2 C 17.0 0.6 1 1143 . 124 ILE HG2 H 1.06 0.11 1 1144 . 124 ILE CD1 C 12.7 0.6 1 1145 . 124 ILE HD1 H 0.99 0.11 1 1146 . 125 PRO CA C 63.2 0.4 1 1147 . 125 PRO HA H 4.54 0.11 1 1148 . 125 PRO CB C 32.1 0.6 1 1149 . 125 PRO HB3 H 1.96 0.11 2 1150 . 125 PRO HB2 H 2.39 0.11 2 1151 . 125 PRO CG C 27.2 0.6 1 1152 . 125 PRO HG3 H 2.12 0.11 1 1153 . 125 PRO HG2 H 2.12 0.11 1 1154 . 125 PRO CD C 50.8 0.6 1 1155 . 125 PRO HD3 H 3.78 0.11 2 1156 . 125 PRO HD2 H 3.99 0.11 2 1157 . 125 PRO C C 176.8 0.17 1 1158 . 126 LEU N N 121.3 0.17 1 1159 . 126 LEU H H 8.30 0.02 1 1160 . 126 LEU CA C 55.3 0.4 1 1161 . 126 LEU HA H 4.41 0.11 1 1162 . 126 LEU CB C 42.4 0.6 1 1163 . 126 LEU HB3 H 1.71 0.11 2 1164 . 126 LEU HB2 H 1.76 0.11 2 1165 . 126 LEU CG C 27.1 0.6 1 1166 . 126 LEU HG H 1.79 0.11 1 1167 . 126 LEU CD1 C 24.6 0.6 2 1168 . 126 LEU HD1 H 1.05 0.11 2 1169 . 126 LEU CD2 C 23.1 0.6 2 1170 . 126 LEU HD2 H 1.00 0.11 2 1171 . 126 LEU C C 172.2 0.17 1 1172 . 127 GLN N N 120.3 0.17 1 1173 . 127 GLN H H 8.39 0.02 1 1174 . 127 GLN CA C 55.5 0.4 1 1175 . 127 GLN HA H 4.54 0.11 1 1176 . 127 GLN CB C 29.7 0.6 1 1177 . 127 GLN HB3 H 2.09 0.11 2 1178 . 127 GLN HB2 H 2.21 0.11 2 1179 . 127 GLN CG C 33.6 0.6 1 1180 . 127 GLN HG3 H 2.47 0.11 1 1181 . 127 GLN HG2 H 2.47 0.11 1 1182 . 127 GLN C C 175.7 0.17 1 1183 . 128 THR N N 117.1 0.17 1 1184 . 128 THR H H 8.27 0.02 1 1185 . 128 THR CA C 59.8 0.4 1 1186 . 128 THR HA H 4.68 0.11 1 1187 . 128 THR CB C 69.6 0.6 1 1188 . 128 THR HB H 4.26 0.11 1 1189 . 128 THR CG2 C 21.2 0.6 1 1190 . 128 THR HG2 H 1.37 0.11 1 1191 . 129 PRO CA C 63.4 0.4 1 1192 . 129 PRO HA H 4.54 0.11 1 1193 . 129 PRO CB C 32.0 0.6 1 1194 . 129 PRO HB3 H 2.03 0.11 2 1195 . 129 PRO HB2 H 2.41 0.11 2 1196 . 129 PRO CG C 27.2 0.6 1 1197 . 129 PRO HG3 H 2.10 0.11 2 1198 . 129 PRO HG2 H 2.17 0.11 2 1199 . 129 PRO CD C 51.0 0.6 1 1200 . 129 PRO HD3 H 3.83 0.11 2 1201 . 129 PRO HD2 H 3.97 0.11 2 1202 . 129 PRO C C 176.0 0.17 1 1203 . 130 LYS N N 126.2 0.17 1 1204 . 130 LYS H H 8.06 0.02 1 1205 . 130 LYS CA C 57.7 0.4 1 1206 . 130 LYS HA H 4.26 0.11 1 1207 . 130 LYS CB C 33.1 0.6 1 1208 . 130 LYS HB3 H 1.82 0.11 2 1209 . 130 LYS HB2 H 1.94 0.11 2 1210 . 130 LYS CG C 24.6 0.6 1 1211 . 130 LYS HG3 H 1.55 0.11 1 1212 . 130 LYS HG2 H 1.55 0.11 1 1213 . 130 LYS CD C 28.8 0.6 1 1214 . 130 LYS HD3 H 1.81 0.11 1 1215 . 130 LYS HD2 H 1.81 0.11 1 1216 . 130 LYS CE C 41.8 0.6 1 1217 . 130 LYS HE3 H 3.15 0.11 1 1218 . 130 LYS HE2 H 3.15 0.11 1 stop_ save_