data_4413 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; STRUCTURE OF THE C-TERMINAL DOMAIN OF P73 ; _BMRB_accession_number 4413 _BMRB_flat_file_name bmr4413.str _Entry_type original _Submission_date 1999-09-18 _Accession_date 1999-09-21 _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 Chi Seung-Wook . . 2 Ayed Ayeda . . 3 Arrowsmith Cheryl H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 393 "13C chemical shifts" 205 "15N chemical shifts" 74 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-12-06 original author . stop_ _Original_release_date 1999-12-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99380160 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chi Seung-Wook . . 2 Ayed Ayeda . . 3 Arrowsmith Cheryl H. . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 18 _Journal_issue 16 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4438 _Page_last 4445 _Year 1999 _Details . loop_ _Keyword 'NMR spectroscopy' p53 'SAM domain' 'tumor suppressor' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _Citation_full 'Nilges, M. (1995) J.Mol.Biol., 245, 645-660' _Citation_title 'Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7844833 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nilges M. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 245 _Journal_issue 5 _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 645 _Page_last 660 _Year 1995 _Details ; The distances derived from nuclear Overhauser effect (NOE) spectra are usually converted into three-dimensional structures by computer algorithms loosely termed distance geometry. To a varying degree, these methods require that the distance data is unambiguously assigned to pairs of atoms. Typically, however, there are many NOE crosspeaks that cannot be assigned without some knowledge of the structure. These crosspeaks have to be assigned in an iterative manner, using preliminary structures calculated from the unambiguous crosspeaks. In this paper, I present an alternative to this iterative approach. The ambiguity of an NOE crosspeak is correctly described in terms of the distances between all pairs of protons that may be involved. A simple restraining term is defined in terms of "ambiguous" distance restraints that can allow all possible assignments. A new minimization procedure based on simulated annealing is described that is capable of using highly ambiguous data for ab initio structure calculations. In particular, it is feasible to specify the restraint list directly in terms of the proton chemical shift assignment and the NOE peak table, without having assigned NOE crosspeaks to proton pairs. While the primary aim of this paper is determining the global fold of proteins from NMR data, similar strategies can be used for other types of ambiguous distance data. The application to one example, disulphide bridges with unknown connectivity, is described. Model NOE data were generated from the X-ray crystal structure of a small protein with known chemical shift assignments. Varying degrees of ambiguity in the data were assumed. The method obtained the correct polypeptide fold even when all distance restraints were ambiguous. Thus, the new approach may facilitate structure calculations with data derived from very overlapped spectra. It is also a step towards automating the calculation of structures from NMR data. This could prove especially valuable for data derived from three- and four-dimensional experiments. The approach may also prove useful for model building studies and tertiary structure prediction. ; save_ ################################## # Molecular system description # ################################## save_system_p73 _Saveframe_category molecular_system _Mol_system_name p73 _Abbreviation_common p73 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label p73 $p73 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_p73 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common p73 _Name_variant p73alpha _Abbreviation_common p73 _Molecular_mass . _Mol_thiol_state 'not reported' _Details '21 residue HIS tag is attached to the N-terminal of the protein.' ############################## # Polymer residue sequence # ############################## _Residue_count 89 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MYHADPSLVSFLTGLGCPNC IEYFTSQGLQSIYHLQNLTI EDLGALKIPEQYRMTIWRGL QDLKQGHDY ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 SER 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 SER 12 SER 13 GLY 14 LEU 15 VAL 16 PRO 17 ARG 18 GLY 19 SER 20 HIS 21 MET 22 TYR 23 HIS 24 ALA 25 ASP 26 PRO 27 SER 28 LEU 29 VAL 30 SER 31 PHE 32 LEU 33 THR 34 GLY 35 LEU 36 GLY 37 CYS 38 PRO 39 ASN 40 CYS 41 ILE 42 GLU 43 TYR 44 PHE 45 THR 46 SER 47 GLN 48 GLY 49 LEU 50 GLN 51 SER 52 ILE 53 TYR 54 HIS 55 LEU 56 GLN 57 ASN 58 LEU 59 THR 60 ILE 61 GLU 62 ASP 63 LEU 64 GLY 65 ALA 66 LEU 67 LYS 68 ILE 69 PRO 70 GLU 71 GLN 72 TYR 73 ARG 74 MET 75 THR 76 ILE 77 TRP 78 ARG 79 GLY 80 LEU 81 GLN 82 ASP 83 LEU 84 LYS 85 GLN 86 GLY 87 HIS 88 ASP 89 TYR 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 1COK "Structure Of The C-Terminal Domain Of P73" 75.28 68 100.00 100.00 1.34e-41 PDB 1DXS "Crystal Structure Of The C-Terminal Sterile Alpha Motif (Sam) Domain Of Human P73 Alpha Splice Variant" 76.40 80 100.00 100.00 8.02e-43 GB ELK10598 "Tumor protein p73 [Pteropus alecto]" 75.28 698 97.01 100.00 7.95e-38 GB ELV14255 "Tumor protein p73 [Tupaia chinensis]" 76.40 616 97.06 100.00 4.77e-39 REF NP_001191117 "tumor protein p73 isoform l [Homo sapiens]" 66.29 540 100.00 100.00 1.14e-33 REF NP_001191120 "tumor protein p73 isoform g [Homo sapiens]" 66.29 491 100.00 100.00 1.08e-33 REF XP_002750246 "PREDICTED: tumor protein p73 [Callithrix jacchus]" 76.40 635 100.00 100.00 6.16e-40 REF XP_004024582 "PREDICTED: tumor protein p73 isoform 6 [Gorilla gorilla gorilla]" 66.29 540 100.00 100.00 1.18e-33 REF XP_004024584 "PREDICTED: tumor protein p73 isoform 8 [Gorilla gorilla gorilla]" 66.29 491 100.00 100.00 1.11e-33 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Variant $p73 human 9606 Eukaryota Metazoa Homo sapiens p73alpha 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 $p73 'recombinant technology' 'E. coli' . . 'BL21 (DE3)' pET15b 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 $p73 1.2 mM '[U-13C; U-15N]' NaCl 150 mM . 'Sodium Phosphate' 25 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $p73 1.2 mM [U-15N] NaCl 150 mM . 'Sodium Phosphate' 25 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRpipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'raw spectral data processing' stop_ _Details . save_ save_NMRview _Saveframe_category software _Name NMRView _Version . loop_ _Task 'peak picking, analysis of processed data' stop_ _Details . save_ save_InsightII _Saveframe_category software _Name InsightII _Version . loop_ _Task 'graphics generation' stop_ _Details . save_ save_X-Plor _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task 'structure calculation' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version . loop_ _Task 'structure calculation' stop_ _Details . _Citation_label $ref-1 save_ save_procheck-NMR _Saveframe_category software _Name ProcheckNMR _Version . loop_ _Task 'structure validation' stop_ _Details . save_ save_GRASP _Saveframe_category software _Name GRASP _Version . loop_ _Task 'molecular surface generation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 600 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity+ _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_C13,N15_edited_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C13,N15 edited NOESY' _Sample_label . save_ save_2D_1H-15N_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_1H-1H-15N_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_2D_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_HSQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HSQC' _Sample_label . save_ save_3D_1H-13C-1H_HCCH-TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _Sample_label . save_ save_3D_HNHA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_CBCANH_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _Sample_label . save_ save_3D_HBCBCA(CO)NNH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBCBCA(CO)NNH' _Sample_label . save_ save_3D_CCC-TOCSY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCC-TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D C13,N15 edited NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D HSQC' _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_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBCBCA(CO)NNH' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCC-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _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 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chem_shift_ref _Mol_system_component_name p73 _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 . 22 TYR N N 122.351 . 1 2 . 22 TYR H H 8.046 . 1 3 . 22 TYR CA C 57.315 . 1 4 . 22 TYR HA H 4.584 . 1 5 . 22 TYR CB C 38.923 . 1 6 . 22 TYR HB2 H 2.920 . 2 7 . 22 TYR HB3 H 2.834 . 2 8 . 22 TYR HD1 H 7.070 . 1 9 . 22 TYR HE1 H 6.779 . 1 10 . 23 HIS N N 122.438 . 1 11 . 23 HIS H H 8.408 . 1 12 . 23 HIS CA C 55.438 . 1 13 . 23 HIS HA H 4.775 . 1 14 . 23 HIS CB C 30.446 . 1 15 . 23 HIS HB2 H 3.134 . 2 16 . 23 HIS HB3 H 3.050 . 2 17 . 24 ALA N N 126.304 . 1 18 . 24 ALA H H 8.237 . 1 19 . 24 ALA CA C 51.404 . 1 20 . 24 ALA HA H 4.379 . 1 21 . 24 ALA CB C 20.224 . 1 22 . 24 ALA HB H 1.289 . 1 23 . 25 ASP N N 125.668 . 1 24 . 25 ASP H H 8.840 . 1 25 . 25 ASP CA C 52.180 . 1 26 . 25 ASP HA H 4.886 . 1 27 . 25 ASP CB C 41.882 . 1 28 . 25 ASP HB2 H 2.789 . 1 29 . 25 ASP HB3 H 2.789 . 1 30 . 26 PRO CA C 64.533 . 1 31 . 26 PRO HA H 4.301 . 1 32 . 26 PRO CB C 32.017 . 1 33 . 26 PRO HB2 H 2.407 . 1 34 . 26 PRO HB3 H 2.407 . 1 35 . 26 PRO CG C 27.300 . 1 36 . 26 PRO HG2 H 2.157 . 2 37 . 26 PRO HG3 H 2.096 . 2 38 . 26 PRO CD C 50.749 . 1 39 . 26 PRO HD2 H 3.977 . 2 40 . 26 PRO HD3 H 3.825 . 2 41 . 27 SER N N 115.688 . 1 42 . 27 SER H H 8.637 . 1 43 . 27 SER CA C 60.639 . 1 44 . 27 SER HA H 4.234 . 1 45 . 27 SER CB C 62.485 . 1 46 . 27 SER HB2 H 4.075 . 2 47 . 27 SER HB3 H 3.838 . 2 48 . 28 LEU N N 128.006 . 1 49 . 28 LEU H H 7.731 . 1 50 . 28 LEU CA C 57.728 . 1 51 . 28 LEU HA H 4.073 . 1 52 . 28 LEU CB C 42.416 . 1 53 . 28 LEU HB2 H 1.997 . 2 54 . 28 LEU HB3 H 1.142 . 2 55 . 28 LEU CG C 26.240 . 1 56 . 28 LEU HG H 0.752 . 1 57 . 28 LEU CD1 C 24.942 . 1 58 . 28 LEU HD1 H 0.586 . 1 59 . 28 LEU CD2 C 24.942 . 1 60 . 28 LEU HD2 H 0.586 . 1 61 . 29 VAL N N 120.708 . 1 62 . 29 VAL H H 7.627 . 1 63 . 29 VAL CA C 66.509 . 1 64 . 29 VAL HA H 3.447 . 1 65 . 29 VAL CB C 31.873 . 1 66 . 29 VAL HB H 2.110 . 1 67 . 29 VAL CG2 C 20.502 . 1 68 . 29 VAL HG2 H 0.921 . 1 69 . 29 VAL CG1 C 20.502 . 1 70 . 29 VAL HG1 H 0.921 . 1 71 . 30 SER N N 120.076 . 1 72 . 30 SER H H 8.901 . 1 73 . 30 SER CA C 61.896 . 1 74 . 30 SER HA H 3.975 . 1 75 . 30 SER CB C 61.896 . 1 76 . 30 SER HB2 H 4.201 . 1 77 . 30 SER HB3 H 4.201 . 1 78 . 31 PHE N N 124.906 . 1 79 . 31 PHE H H 7.699 . 1 80 . 31 PHE CA C 59.882 . 1 81 . 31 PHE HA H 4.427 . 1 82 . 31 PHE CB C 39.741 . 1 83 . 31 PHE HB2 H 3.365 . 2 84 . 31 PHE HB3 H 2.935 . 2 85 . 31 PHE HD1 H 6.976 . 2 86 . 32 LEU N N 118.542 . 1 87 . 32 LEU H H 8.022 . 1 88 . 32 LEU CA C 57.117 . 1 89 . 32 LEU HA H 3.638 . 1 90 . 32 LEU CB C 40.847 . 1 91 . 32 LEU HB2 H 1.646 . 2 92 . 32 LEU HB3 H 1.379 . 2 93 . 32 LEU CG C 26.986 . 1 94 . 32 LEU HG H 1.857 . 1 95 . 32 LEU CD1 C 22.927 . 1 96 . 32 LEU HD1 H 0.727 . 2 97 . 32 LEU CD2 C 22.927 . 1 98 . 32 LEU HD2 H 0.876 . 2 99 . 33 THR N N 118.654 . 1 100 . 33 THR H H 8.419 . 1 101 . 33 THR CA C 67.878 . 1 102 . 33 THR HA H 4.252 . 1 103 . 33 THR CB C 67.878 . 1 104 . 33 THR HB H 3.658 . 1 105 . 33 THR CG2 C 20.814 . 1 106 . 33 THR HG2 H 1.216 . 1 107 . 34 GLY N N 113.783 . 1 108 . 34 GLY H H 8.294 . 1 109 . 34 GLY CA C 46.760 . 1 110 . 34 GLY HA2 H 3.984 . 2 111 . 34 GLY HA3 H 3.873 . 2 112 . 35 LEU N N 119.149 . 1 113 . 35 LEU H H 6.852 . 1 114 . 35 LEU CA C 54.385 . 1 115 . 35 LEU HA H 4.238 . 1 116 . 35 LEU CB C 43.121 . 1 117 . 35 LEU HB2 H 1.572 . 2 118 . 35 LEU HB3 H 1.370 . 2 119 . 35 LEU CG C 22.313 . 1 120 . 35 LEU HG H 0.643 . 1 121 . 35 LEU CD1 C 26.772 . 1 122 . 35 LEU HD1 H 0.289 . 1 123 . 35 LEU CD2 C 26.772 . 1 124 . 35 LEU HD2 H 0.289 . 1 125 . 36 GLY N N 107.891 . 1 126 . 36 GLY H H 7.792 . 1 127 . 36 GLY CA C 44.898 . 1 128 . 36 GLY HA2 H 4.289 . 2 129 . 36 GLY HA3 H 3.888 . 2 130 . 37 CYS N N 115.659 . 1 131 . 37 CYS H H 8.132 . 1 132 . 37 CYS CA C 54.090 . 1 133 . 37 CYS HA H 5.121 . 1 134 . 37 CYS CB C 28.594 . 1 135 . 37 CYS HB2 H 2.549 . 1 136 . 37 CYS HB3 H 2.549 . 1 137 . 38 PRO CA C 65.172 . 1 138 . 38 PRO HA H 4.106 . 1 139 . 38 PRO CB C 30.473 . 1 140 . 38 PRO HB2 H 2.204 . 2 141 . 38 PRO HB3 H 2.101 . 2 142 . 38 PRO CG C 26.943 . 1 143 . 38 PRO HG2 H 2.151 . 1 144 . 38 PRO HG3 H 2.151 . 1 145 . 38 PRO CD C 50.629 . 1 146 . 38 PRO HD2 H 3.680 . 2 147 . 38 PRO HD3 H 3.483 . 2 148 . 39 ASN N N 118.356 . 1 149 . 39 ASN H H 8.610 . 1 150 . 39 ASN CA C 54.676 . 1 151 . 39 ASN HA H 4.615 . 1 152 . 39 ASN CB C 36.004 . 1 153 . 39 ASN HB2 H 2.957 . 2 154 . 39 ASN HB3 H 2.892 . 2 155 . 39 ASN ND2 N 114.685 . 1 156 . 39 ASN HD21 H 6.278 . 2 157 . 39 ASN HD22 H 7.801 . 2 158 . 40 CYS N N 116.777 . 1 159 . 40 CYS H H 7.739 . 1 160 . 40 CYS CA C 60.151 . 1 161 . 40 CYS HA H 4.780 . 1 162 . 40 CYS CB C 28.165 . 1 163 . 40 CYS HB2 H 3.115 . 2 164 . 40 CYS HB3 H 3.052 . 2 165 . 41 ILE N N 123.184 . 1 166 . 41 ILE H H 7.613 . 1 167 . 41 ILE CA C 66.042 . 1 168 . 41 ILE HA H 3.697 . 1 169 . 41 ILE CB C 38.608 . 1 170 . 41 ILE HB H 1.923 . 1 171 . 41 ILE CG1 C 30.839 . 1 172 . 41 ILE HG12 H 1.759 . 1 173 . 41 ILE HG13 H 1.759 . 1 174 . 41 ILE CD1 C 15.291 . 1 175 . 41 ILE HD1 H 1.015 . 1 176 . 41 ILE CG2 C 17.984 . 1 177 . 41 ILE HG2 H 0.954 . 1 178 . 42 GLU N N 119.701 . 1 179 . 42 GLU H H 8.489 . 1 180 . 42 GLU CA C 58.201 . 1 181 . 42 GLU HA H 4.534 . 1 182 . 42 GLU CB C 29.045 . 1 183 . 42 GLU HB2 H 1.888 . 2 184 . 42 GLU HB3 H 1.839 . 2 185 . 42 GLU CG C 36.331 . 1 186 . 42 GLU HG2 H 2.143 . 2 187 . 42 GLU HG3 H 2.042 . 2 188 . 43 TYR N N 120.121 . 1 189 . 43 TYR H H 7.199 . 1 190 . 43 TYR CA C 60.685 . 1 191 . 43 TYR HA H 4.141 . 1 192 . 43 TYR CB C 37.685 . 1 193 . 43 TYR HB2 H 2.822 . 2 194 . 43 TYR HB3 H 2.491 . 2 195 . 43 TYR HD1 H 7.235 . 2 196 . 43 TYR HE1 H 6.903 . 1 197 . 44 PHE N N 115.336 . 1 198 . 44 PHE H H 7.394 . 1 199 . 44 PHE CA C 60.967 . 1 200 . 44 PHE HA H 4.446 . 1 201 . 44 PHE CB C 62.567 . 1 202 . 44 PHE HB2 H 3.665 . 2 203 . 44 PHE HB3 H 3.195 . 2 204 . 44 PHE HD1 H 7.413 . 2 205 . 44 PHE HE1 H 7.080 . 2 206 . 45 THR N N 115.140 . 1 207 . 45 THR H H 8.648 . 1 208 . 45 THR CA C 65.827 . 1 209 . 45 THR HA H 3.813 . 1 210 . 45 THR CB C 67.964 . 1 211 . 45 THR HB H 4.237 . 1 212 . 45 THR CG2 C 23.112 . 1 213 . 45 THR HG2 H 1.294 . 1 214 . 46 SER N N 119.611 . 1 215 . 46 SER H H 8.242 . 1 216 . 46 SER CA C 60.965 . 1 217 . 46 SER HA H 3.941 . 1 218 . 46 SER CB C 62.919 . 1 219 . 46 SER HB2 H 3.991 . 2 220 . 46 SER HB3 H 3.886 . 2 221 . 47 GLN N N 120.356 . 1 222 . 47 GLN H H 7.088 . 1 223 . 47 GLN CA C 54.032 . 1 224 . 47 GLN HA H 4.576 . 1 225 . 47 GLN CB C 28.716 . 1 226 . 47 GLN HB2 H 1.757 . 1 227 . 47 GLN HB3 H 1.757 . 1 228 . 47 GLN CG C 33.753 . 1 229 . 47 GLN HG2 H 2.491 . 2 230 . 47 GLN HG3 H 2.337 . 2 231 . 47 GLN NE2 N 115.534 . 1 232 . 47 GLN HE21 H 7.009 . 2 233 . 47 GLN HE22 H 7.583 . 2 234 . 48 GLY N N 108.546 . 1 235 . 48 GLY H H 7.683 . 1 236 . 48 GLY CA C 45.466 . 1 237 . 48 GLY HA2 H 3.950 . 2 238 . 48 GLY HA3 H 3.277 . 2 239 . 49 LEU N N 125.051 . 1 240 . 49 LEU H H 7.663 . 1 241 . 49 LEU CA C 54.272 . 1 242 . 49 LEU HA H 4.403 . 1 243 . 49 LEU CB C 40.568 . 1 244 . 49 LEU HB2 H 2.082 . 2 245 . 49 LEU HB3 H 1.290 . 2 246 . 49 LEU CG C 27.379 . 1 247 . 49 LEU HG H 1.107 . 1 248 . 49 LEU CD1 C 24.322 . 1 249 . 49 LEU HD1 H 0.917 . 1 250 . 49 LEU CD2 C 24.322 . 1 251 . 49 LEU HD2 H 0.917 . 1 252 . 50 GLN N N 120.387 . 1 253 . 50 GLN H H 8.327 . 1 254 . 50 GLN CA C 56.173 . 1 255 . 50 GLN HA H 4.386 . 1 256 . 50 GLN CB C 31.560 . 1 257 . 50 GLN HB2 H 1.935 . 1 258 . 50 GLN HB3 H 1.935 . 1 259 . 50 GLN CG C 33.478 . 1 260 . 50 GLN HG2 H 2.262 . 2 261 . 50 GLN HG3 H 2.143 . 2 262 . 50 GLN NE2 N 112.814 . 1 263 . 50 GLN HE21 H 6.888 . 2 264 . 50 GLN HE22 H 7.561 . 2 265 . 51 SER N N 116.339 . 1 266 . 51 SER H H 8.084 . 1 267 . 51 SER CA C 66.911 . 1 268 . 51 SER HA H 4.792 . 1 269 . 51 SER CB C 66.911 . 1 270 . 51 SER HB2 H 3.870 . 2 271 . 51 SER HB3 H 3.530 . 2 272 . 52 ILE N N 123.630 . 1 273 . 52 ILE H H 8.375 . 1 274 . 52 ILE CA C 62.269 . 1 275 . 52 ILE HA H 3.585 . 1 276 . 52 ILE CB C 37.571 . 1 277 . 52 ILE HB H 1.300 . 1 278 . 52 ILE CG1 C 27.770 . 1 279 . 52 ILE HG12 H 0.805 . 1 280 . 52 ILE HG13 H 0.805 . 1 281 . 52 ILE CD1 C 13.004 . 1 282 . 52 ILE HD1 H 0.149 . 1 283 . 52 ILE CG2 C 17.315 . 1 284 . 52 ILE HG2 H 0.357 . 1 285 . 53 TYR N N 122.269 . 1 286 . 53 TYR H H 7.329 . 1 287 . 53 TYR CA C 60.018 . 1 288 . 53 TYR HA H 4.088 . 1 289 . 53 TYR CB C 37.034 . 1 290 . 53 TYR HB2 H 2.892 . 2 291 . 53 TYR HB3 H 2.716 . 2 292 . 53 TYR HD1 H 6.919 . 2 293 . 53 TYR HE1 H 6.750 . 1 294 . 54 HIS N N 118.836 . 1 295 . 54 HIS H H 7.454 . 1 296 . 54 HIS CA C 57.799 . 1 297 . 54 HIS HA H 4.423 . 1 298 . 54 HIS CB C 31.641 . 1 299 . 54 HIS HB2 H 3.289 . 1 300 . 54 HIS HB3 H 3.289 . 1 301 . 55 LEU N N 120.218 . 1 302 . 55 LEU H H 7.387 . 1 303 . 55 LEU CA C 55.891 . 1 304 . 55 LEU HA H 4.243 . 1 305 . 55 LEU CB C 42.394 . 1 306 . 55 LEU HB2 H 1.684 . 2 307 . 55 LEU HB3 H 1.390 . 2 308 . 55 LEU CG C 29.005 . 1 309 . 55 LEU HG H 1.551 . 1 310 . 55 LEU CD1 C 24.619 . 1 311 . 55 LEU HD1 H 0.165 . 2 312 . 55 LEU CD2 C 24.619 . 1 313 . 55 LEU HD2 H 0.433 . 2 314 . 56 GLN N N 117.120 . 1 315 . 56 GLN H H 7.147 . 1 316 . 56 GLN CA C 59.127 . 1 317 . 56 GLN HA H 3.797 . 1 318 . 56 GLN CB C 28.992 . 1 319 . 56 GLN HB2 H 2.019 . 2 320 . 56 GLN HB3 H 1.942 . 2 321 . 56 GLN CG C 33.619 . 1 322 . 56 GLN HG2 H 2.267 . 1 323 . 56 GLN HG3 H 2.267 . 1 324 . 56 GLN NE2 N 112.316 . 1 325 . 56 GLN HE21 H 6.670 . 2 326 . 56 GLN HE22 H 7.067 . 2 327 . 57 ASN N N 117.106 . 1 328 . 57 ASN H H 8.276 . 1 329 . 57 ASN CA C 52.566 . 1 330 . 57 ASN HA H 4.968 . 1 331 . 57 ASN CB C 38.898 . 1 332 . 57 ASN HB2 H 3.022 . 2 333 . 57 ASN HB3 H 2.670 . 2 334 . 57 ASN ND2 N 115.785 . 1 335 . 57 ASN HD21 H 6.891 . 2 336 . 57 ASN HD22 H 7.584 . 2 337 . 58 LEU N N 122.538 . 1 338 . 58 LEU H H 7.511 . 1 339 . 58 LEU CA C 55.424 . 1 340 . 58 LEU HA H 4.712 . 1 341 . 58 LEU CB C 42.184 . 1 342 . 58 LEU HB2 H 1.997 . 2 343 . 58 LEU HB3 H 1.593 . 2 344 . 58 LEU CG C 27.315 . 1 345 . 58 LEU HG H 1.062 . 1 346 . 58 LEU CD1 C 22.360 . 1 347 . 58 LEU HD1 H 0.954 . 1 348 . 58 LEU CD2 C 22.360 . 1 349 . 58 LEU HD2 H 0.954 . 1 350 . 59 THR N N 115.242 . 1 351 . 59 THR H H 9.413 . 1 352 . 59 THR CA C 59.774 . 1 353 . 59 THR HA H 4.859 . 1 354 . 59 THR CB C 72.071 . 1 355 . 59 THR HB H 4.702 . 1 356 . 59 THR CG2 C 21.648 . 1 357 . 59 THR HG2 H 1.414 . 1 358 . 60 ILE N N 122.642 . 1 359 . 60 ILE H H 8.241 . 1 360 . 60 ILE CA C 64.197 . 1 361 . 60 ILE HA H 3.511 . 1 362 . 60 ILE CB C 37.070 . 1 363 . 60 ILE HB H 0.989 . 1 364 . 60 ILE CG1 C 29.089 . 1 365 . 60 ILE HG12 H 0.758 . 2 366 . 60 ILE HG13 H 0.588 . 2 367 . 60 ILE CD1 C 13.004 . 1 368 . 60 ILE HD1 H 0.386 . 1 369 . 60 ILE CG2 C 17.250 . 1 370 . 60 ILE HG2 H 0.611 . 1 371 . 61 GLU N N 124.709 . 1 372 . 61 GLU H H 8.301 . 1 373 . 61 GLU CA C 59.947 . 1 374 . 61 GLU HA H 3.975 . 1 375 . 61 GLU CB C 28.386 . 1 376 . 61 GLU HB2 H 1.996 . 2 377 . 61 GLU HB3 H 1.930 . 2 378 . 61 GLU CG C 36.868 . 1 379 . 61 GLU HG2 H 2.369 . 2 380 . 61 GLU HG3 H 2.194 . 2 381 . 62 ASP N N 124.407 . 1 382 . 62 ASP H H 8.013 . 1 383 . 62 ASP CA C 57.344 . 1 384 . 62 ASP HA H 4.411 . 1 385 . 62 ASP CB C 41.555 . 1 386 . 62 ASP HB2 H 3.224 . 2 387 . 62 ASP HB3 H 2.679 . 2 388 . 63 LEU N N 119.273 . 1 389 . 63 LEU H H 7.856 . 1 390 . 63 LEU CA C 57.808 . 1 391 . 63 LEU HA H 4.043 . 1 392 . 63 LEU CB C 40.671 . 1 393 . 63 LEU HB2 H 2.154 . 1 394 . 63 LEU HB3 H 2.154 . 1 395 . 63 LEU CG C 27.234 . 1 396 . 63 LEU HG H 1.219 . 1 397 . 63 LEU CD1 C 23.747 . 1 398 . 63 LEU HD1 H 1.089 . 1 399 . 63 LEU CD2 C 23.747 . 1 400 . 63 LEU HD2 H 1.089 . 1 401 . 64 GLY N N 107.523 . 1 402 . 64 GLY H H 7.715 . 1 403 . 64 GLY CA C 46.399 . 1 404 . 64 GLY HA2 H 3.946 . 2 405 . 64 GLY HA3 H 3.730 . 2 406 . 65 ALA N N 129.939 . 1 407 . 65 ALA H H 8.000 . 1 408 . 65 ALA CA C 54.472 . 1 409 . 65 ALA HA H 4.209 . 1 410 . 65 ALA CB C 17.826 . 1 411 . 65 ALA HB H 1.577 . 1 412 . 66 LEU N N 119.287 . 1 413 . 66 LEU H H 7.551 . 1 414 . 66 LEU CA C 54.923 . 1 415 . 66 LEU HA H 4.198 . 1 416 . 66 LEU CB C 42.682 . 1 417 . 66 LEU HB2 H 1.772 . 2 418 . 66 LEU HB3 H 1.323 . 2 419 . 66 LEU CG C 22.664 . 1 420 . 66 LEU HG H 0.866 . 1 421 . 66 LEU CD1 C 26.712 . 1 422 . 66 LEU HD1 H 0.756 . 2 423 . 66 LEU CD2 C 26.712 . 1 424 . 66 LEU HD2 H 1.856 . 2 425 . 67 LYS N N 113.074 . 1 426 . 67 LYS H H 7.737 . 1 427 . 67 LYS CA C 56.549 . 1 428 . 67 LYS HA H 3.593 . 1 429 . 67 LYS CB C 28.394 . 1 430 . 67 LYS HB2 H 2.257 . 2 431 . 67 LYS HB3 H 1.897 . 2 432 . 67 LYS CG C 24.672 . 1 433 . 67 LYS HG2 H 1.333 . 2 434 . 67 LYS HG3 H 1.289 . 2 435 . 67 LYS CD C 28.394 . 1 436 . 67 LYS HD2 H 1.743 . 2 437 . 67 LYS HD3 H 1.588 . 2 438 . 67 LYS CE C 42.188 . 1 439 . 67 LYS HE2 H 3.033 . 1 440 . 67 LYS HE3 H 3.033 . 1 441 . 68 ILE N N 120.715 . 1 442 . 68 ILE H H 7.122 . 1 443 . 68 ILE CA C 57.482 . 1 444 . 68 ILE HA H 3.189 . 1 445 . 68 ILE CB C 37.180 . 1 446 . 68 ILE HB H 1.511 . 1 447 . 68 ILE HG12 H 1.123 . 1 448 . 68 ILE HG13 H 1.123 . 1 449 . 68 ILE CD1 C 12.500 . 1 450 . 68 ILE HD1 H 0.332 . 1 451 . 68 ILE HG2 H 0.951 . 1 452 . 69 PRO CA C 63.653 . 1 453 . 69 PRO HA H 4.277 . 1 454 . 69 PRO CB C 32.316 . 1 455 . 69 PRO HB2 H 2.504 . 2 456 . 69 PRO HB3 H 1.818 . 2 457 . 69 PRO CG C 27.809 . 1 458 . 69 PRO HG2 H 2.259 . 2 459 . 69 PRO HG3 H 2.047 . 2 460 . 69 PRO CD C 51.320 . 1 461 . 69 PRO HD2 H 3.639 . 2 462 . 69 PRO HD3 H 3.306 . 2 463 . 70 GLU N N 126.885 . 1 464 . 70 GLU H H 9.041 . 1 465 . 70 GLU CA C 60.645 . 1 466 . 70 GLU HA H 3.535 . 1 467 . 70 GLU CB C 29.671 . 1 468 . 70 GLU HB2 H 2.019 . 2 469 . 70 GLU HB3 H 1.982 . 2 470 . 70 GLU CG C 35.999 . 1 471 . 70 GLU HG2 H 2.263 . 1 472 . 70 GLU HG3 H 2.263 . 1 473 . 71 GLN N N 118.365 . 1 474 . 71 GLN H H 9.180 . 1 475 . 71 GLN CA C 57.840 . 1 476 . 71 GLN HA H 4.110 . 1 477 . 71 GLN CB C 27.347 . 1 478 . 71 GLN HB2 H 1.850 . 2 479 . 71 GLN HB3 H 1.594 . 2 480 . 71 GLN CG C 31.967 . 1 481 . 71 GLN HG2 H 1.576 . 2 482 . 71 GLN HG3 H 1.320 . 2 483 . 71 GLN NE2 N 113.784 . 1 484 . 71 GLN HE21 H 6.854 . 2 485 . 71 GLN HE22 H 7.206 . 2 486 . 72 TYR N N 119.047 . 1 487 . 72 TYR H H 7.685 . 1 488 . 72 TYR CA C 56.953 . 1 489 . 72 TYR HA H 4.978 . 1 490 . 72 TYR CB C 40.393 . 1 491 . 72 TYR HB2 H 3.556 . 2 492 . 72 TYR HB3 H 2.468 . 2 493 . 72 TYR HD1 H 7.010 . 2 494 . 72 TYR HE1 H 6.880 . 1 495 . 73 ARG N N 120.760 . 1 496 . 73 ARG H H 7.604 . 1 497 . 73 ARG CA C 61.918 . 1 498 . 73 ARG HA H 3.750 . 1 499 . 73 ARG CB C 30.429 . 1 500 . 73 ARG HB2 H 1.966 . 2 501 . 73 ARG HB3 H 1.819 . 2 502 . 73 ARG CG C 28.447 . 1 503 . 73 ARG HG2 H 1.282 . 1 504 . 73 ARG HG3 H 1.282 . 1 505 . 73 ARG CD C 43.559 . 1 506 . 73 ARG HD2 H 3.128 . 1 507 . 73 ARG HD3 H 3.128 . 1 508 . 74 MET N N 118.901 . 1 509 . 74 MET H H 8.777 . 1 510 . 74 MET CA C 57.010 . 1 511 . 74 MET HA H 4.734 . 1 512 . 74 MET CB C 29.873 . 1 513 . 74 MET HB2 H 2.168 . 1 514 . 74 MET HB3 H 2.168 . 1 515 . 74 MET CG C 32.468 . 1 516 . 74 MET HG2 H 2.743 . 2 517 . 74 MET HG3 H 2.683 . 2 518 . 75 THR N N 120.328 . 1 519 . 75 THR H H 8.041 . 1 520 . 75 THR CA C 66.468 . 1 521 . 75 THR HA H 3.959 . 1 522 . 75 THR CB C 68.830 . 1 523 . 75 THR HB H 4.326 . 1 524 . 75 THR CG2 C 22.527 . 1 525 . 75 THR HG2 H 1.358 . 1 526 . 76 ILE N N 123.232 . 1 527 . 76 ILE H H 8.115 . 1 528 . 76 ILE CA C 65.520 . 1 529 . 76 ILE HA H 3.690 . 1 530 . 76 ILE CB C 38.301 . 1 531 . 76 ILE HB H 1.990 . 1 532 . 76 ILE CG1 C 30.039 . 1 533 . 76 ILE HG12 H 2.124 . 1 534 . 76 ILE HG13 H 2.124 . 1 535 . 76 ILE CD1 C 14.673 . 1 536 . 76 ILE HD1 H 1.123 . 1 537 . 76 ILE CG2 C 17.176 . 1 538 . 76 ILE HG2 H 1.073 . 1 539 . 77 TRP N N 122.817 . 1 540 . 77 TRP H H 8.867 . 1 541 . 77 TRP CA C 62.421 . 1 542 . 77 TRP HA H 4.239 . 1 543 . 77 TRP CB C 29.492 . 1 544 . 77 TRP HB2 H 3.515 . 2 545 . 77 TRP HB3 H 3.263 . 2 546 . 77 TRP HD1 H 7.512 . 2 547 . 77 TRP NE1 N 132.207 . 1 548 . 77 TRP HE1 H 10.175 . 1 549 . 77 TRP HZ2 H 7.116 . 2 550 . 77 TRP HH2 H 7.116 . 2 551 . 77 TRP HZ3 H 7.116 . 2 552 . 77 TRP HE3 H 7.116 . 2 553 . 78 ARG N N 119.942 . 1 554 . 78 ARG H H 9.119 . 1 555 . 78 ARG CA C 59.319 . 1 556 . 78 ARG HA H 3.684 . 1 557 . 78 ARG CB C 29.638 . 1 558 . 78 ARG HB2 H 2.060 . 1 559 . 78 ARG HB3 H 2.060 . 1 560 . 78 ARG CG C 27.759 . 1 561 . 78 ARG HG2 H 1.997 . 2 562 . 78 ARG HG3 H 1.813 . 2 563 . 78 ARG CD C 43.093 . 1 564 . 78 ARG HD2 H 3.316 . 2 565 . 78 ARG HD3 H 3.263 . 2 566 . 79 GLY N N 109.193 . 1 567 . 79 GLY H H 7.968 . 1 568 . 79 GLY CA C 47.248 . 1 569 . 79 GLY HA2 H 4.093 . 2 570 . 79 GLY HA3 H 3.747 . 2 571 . 80 LEU N N 125.019 . 1 572 . 80 LEU H H 8.549 . 1 573 . 80 LEU CA C 57.385 . 1 574 . 80 LEU HA H 3.948 . 1 575 . 80 LEU CB C 41.240 . 1 576 . 80 LEU HB2 H 1.913 . 2 577 . 80 LEU HB3 H 1.250 . 2 578 . 80 LEU CG C 49.361 . 1 579 . 80 LEU HG H 0.926 . 1 580 . 80 LEU CD1 C 23.577 . 1 581 . 80 LEU HD1 H 0.467 . 1 582 . 80 LEU CD2 C 23.577 . 1 583 . 80 LEU HD2 H 0.467 . 1 584 . 81 GLN N N 120.750 . 1 585 . 81 GLN H H 7.863 . 1 586 . 81 GLN CA C 57.329 . 1 587 . 81 GLN HA H 3.706 . 1 588 . 81 GLN CB C 27.173 . 1 589 . 81 GLN HB2 H 1.891 . 2 590 . 81 GLN HB3 H 1.810 . 2 591 . 81 GLN CG C 32.197 . 1 592 . 81 GLN HG2 H 1.465 . 2 593 . 81 GLN HG3 H 1.376 . 2 594 . 81 GLN NE2 N 116.961 . 1 595 . 81 GLN HE21 H 5.969 . 2 596 . 81 GLN HE22 H 6.778 . 2 597 . 82 ASP N N 121.678 . 1 598 . 82 ASP H H 7.875 . 1 599 . 82 ASP CA C 56.274 . 1 600 . 82 ASP HA H 4.457 . 1 601 . 82 ASP CB C 40.327 . 1 602 . 82 ASP HB2 H 2.744 . 1 603 . 82 ASP HB3 H 2.744 . 1 604 . 83 LEU N N 121.845 . 1 605 . 83 LEU H H 7.432 . 1 606 . 83 LEU CA C 56.499 . 1 607 . 83 LEU HA H 4.142 . 1 608 . 83 LEU CB C 42.023 . 1 609 . 83 LEU HB2 H 1.745 . 2 610 . 83 LEU HB3 H 1.497 . 2 611 . 83 LEU CG C 25.387 . 1 612 . 83 LEU HG H 1.762 . 1 613 . 83 LEU CD1 C 23.157 . 1 614 . 83 LEU HD1 H 0.527 . 2 615 . 83 LEU CD2 C 23.157 . 1 616 . 83 LEU HD2 H 0.634 . 2 617 . 84 LYS N N 120.651 . 1 618 . 84 LYS H H 7.674 . 1 619 . 84 LYS CA C 57.253 . 1 620 . 84 LYS HA H 4.124 . 1 621 . 84 LYS CB C 32.607 . 1 622 . 84 LYS HB2 H 1.851 . 2 623 . 84 LYS HB3 H 1.792 . 2 624 . 84 LYS CG C 24.947 . 1 625 . 84 LYS HG2 H 1.510 . 2 626 . 84 LYS HG3 H 1.385 . 2 627 . 84 LYS CD C 29.202 . 1 628 . 84 LYS HD2 H 1.622 . 1 629 . 84 LYS HD3 H 1.622 . 1 630 . 84 LYS CE C 41.923 . 1 631 . 84 LYS HE2 H 2.923 . 1 632 . 84 LYS HE3 H 2.923 . 1 633 . 85 GLN N N 120.776 . 1 634 . 85 GLN H H 7.844 . 1 635 . 85 GLN CA C 56.058 . 1 636 . 85 GLN HA H 4.219 . 1 637 . 85 GLN CB C 28.885 . 1 638 . 85 GLN HB2 H 2.119 . 2 639 . 85 GLN HB3 H 1.998 . 2 640 . 85 GLN CG C 33.641 . 1 641 . 85 GLN HG2 H 2.383 . 1 642 . 85 GLN HG3 H 2.383 . 1 643 . 85 GLN NE2 N 114.219 . 1 644 . 85 GLN HE21 H 6.805 . 2 645 . 85 GLN HE22 H 7.468 . 2 646 . 86 GLY N N 111.070 . 1 647 . 86 GLY H H 8.162 . 1 648 . 86 GLY CA C 45.224 . 1 649 . 86 GLY HA2 H 3.909 . 1 650 . 86 GLY HA3 H 3.909 . 1 651 . 87 HIS N N 120.199 . 1 652 . 87 HIS H H 8.102 . 1 653 . 87 HIS CA C 55.232 . 1 654 . 87 HIS HA H 4.643 . 1 655 . 87 HIS CB C 29.919 . 1 656 . 87 HIS HB2 H 3.095 . 2 657 . 87 HIS HB3 H 2.998 . 2 658 . 88 ASP N N 123.632 . 1 659 . 88 ASP H H 8.382 . 1 660 . 88 ASP CA C 54.168 . 1 661 . 88 ASP HA H 4.625 . 1 662 . 88 ASP CB C 41.050 . 1 663 . 88 ASP HB2 H 2.652 . 2 664 . 88 ASP HB3 H 2.494 . 2 665 . 89 TYR N N 126.553 . 1 666 . 89 TYR H H 7.618 . 1 667 . 89 TYR CA C 58.846 . 1 668 . 89 TYR HA H 4.363 . 1 669 . 89 TYR CB C 39.186 . 1 670 . 89 TYR HB2 H 3.019 . 2 671 . 89 TYR HB3 H 2.892 . 2 672 . 89 TYR HD1 H 7.030 . 2 stop_ save_