data_4788 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H,15N, and 13C NMR resonance assignments for the Eps15 Homology domain Resp1 ; _BMRB_accession_number 4788 _BMRB_flat_file_name bmr4788.str _Entry_type original _Submission_date 2000-07-19 _Accession_date 2000-07-19 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim Soyoun . . 2 Feig Larry A . 3 Baleja James D . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 585 "13C chemical shifts" 286 "15N chemical shifts" 93 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-18 original author . stop_ _Original_release_date 2000-12-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N, and 13C NMR resonance assignments for the Eps15 homology domain of Reps1 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim Soyoun . . 2 Dubelman Ari M. . 3 Goonesekera Sunali . . 4 Feig Larry A. . 5 Baleja James D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 18 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 367 _Page_last 368 _Year 2000 _Details . loop_ _Keyword 'calcium binding protein' 'EH domain' 'EF hand' Ral stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Yamaguchi A, Urano T, Goi T, Feig LA. An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1. J Biol Chem. 1997 Dec 12;272(50):31230-4. ; _Citation_title 'An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9395447 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Yamaguchi A . . 2 Urano T . . 3 Goi T . . 4 Feig 'L A' A. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'The Journal of biological chemistry' _Journal_volume 272 _Journal_issue 50 _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 31230 _Page_last 31234 _Year 1997 _Details ; Ral proteins constitute a family of small GTPases that can be activated by Ras in cells. In the GTP-bound state, Ral proteins bind to RalBP1, a GTPase-activating protein for CDC42 and Rac GTPases. We have used the two-hybrid system in yeast to clone a cDNA for a novel approximately 85-kDa protein that can bind to an additional site on RalBP1. This newly identified protein contains an Eps homology (EH) domain, which was first detected in the epidermal growth factor (EGF) receptor substrate Eps15. Recently, the EH domain of Eps15 has been shown to bind to proteins containing an asparagine-proline-phenylalanine motif. Moreover, EH domains have been found in proteins involved in endocytosis and/or actin cytoskeleton regulation. The RalBP1 associated Eps-homology domain protein, Reps1, is tyrosine-phosphorylated in response to EGF stimulation of cells. In addition, Reps1 has the capacity to form a complex with the SH3 domains of the adapter proteins Crk and Grb2, which may link Reps1 to an EGF-responsive tyrosine kinase. Thus, Reps1 may coordinate the cellular actions of activated EGF receptors and Ral-GTPases. ; save_ ################################## # Molecular system description # ################################## save_system_EH_domain _Saveframe_category molecular_system _Mol_system_name 'Reps1 EH domain' _Abbreviation_common 'EH domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Reps1 EH domain' $EH_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'protein binding domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EH_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Eps15 homology domain' _Abbreviation_common 'EH domain' _Molecular_mass 11093 _Mol_thiol_state 'not reported' _Details ; The authentic numbers for the EH domain are W227 to K318. Here, it is renumbered from W6 to K97. The N-terminal 5 residues originate from the cloning vector. ; ############################## # Polymer residue sequence # ############################## _Residue_count 97 _Mol_residue_sequence ; ASVGSWKITDEQRQYYVNQF KTIQPDLNGFIPGSAAKEFF TKSKLPILELSHIWELSDFD KDGALTLDEFCAAFHLVVAR KNGYDLPEKLPESLMPK ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 VAL 4 GLY 5 SER 6 TRP 7 LYS 8 ILE 9 THR 10 ASP 11 GLU 12 GLN 13 ARG 14 GLN 15 TYR 16 TYR 17 VAL 18 ASN 19 GLN 20 PHE 21 LYS 22 THR 23 ILE 24 GLN 25 PRO 26 ASP 27 LEU 28 ASN 29 GLY 30 PHE 31 ILE 32 PRO 33 GLY 34 SER 35 ALA 36 ALA 37 LYS 38 GLU 39 PHE 40 PHE 41 THR 42 LYS 43 SER 44 LYS 45 LEU 46 PRO 47 ILE 48 LEU 49 GLU 50 LEU 51 SER 52 HIS 53 ILE 54 TRP 55 GLU 56 LEU 57 SER 58 ASP 59 PHE 60 ASP 61 LYS 62 ASP 63 GLY 64 ALA 65 LEU 66 THR 67 LEU 68 ASP 69 GLU 70 PHE 71 CYS 72 ALA 73 ALA 74 PHE 75 HIS 76 LEU 77 VAL 78 VAL 79 ALA 80 ARG 81 LYS 82 ASN 83 GLY 84 TYR 85 ASP 86 LEU 87 PRO 88 GLU 89 LYS 90 LEU 91 PRO 92 GLU 93 SER 94 LEU 95 MET 96 PRO 97 LYS 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 1FI6 "Solution Structure Of The Reps1 Eh Domain" 94.85 92 100.00 100.00 6.92e-61 DBJ BAC31117 "unnamed protein product [Mus musculus]" 94.85 210 100.00 100.00 5.16e-61 DBJ BAE29439 "unnamed protein product [Mus musculus]" 94.85 743 100.00 100.00 4.98e-58 DBJ BAE30291 "unnamed protein product [Mus musculus]" 94.85 743 100.00 100.00 4.98e-58 DBJ BAG35780 "unnamed protein product [Homo sapiens]" 94.85 744 100.00 100.00 6.43e-58 EMBL CAG03521 "unnamed protein product, partial [Tetraodon nigroviridis]" 94.85 559 98.91 100.00 2.84e-58 EMBL CAG31901 "hypothetical protein RCJMB04_13f17 [Gallus gallus]" 94.85 773 100.00 100.00 1.66e-57 EMBL CDQ63378 "unnamed protein product [Oncorhynchus mykiss]" 94.85 771 98.91 100.00 3.49e-57 EMBL CDQ64642 "unnamed protein product [Oncorhynchus mykiss]" 94.85 699 97.83 98.91 1.23e-56 GB AAB94736 "RalBP1-associated EH domain protein Reps1 [Mus musculus]" 94.85 743 100.00 100.00 4.84e-58 GB AAH12764 "RALBP1 associated Eps domain containing 1 [Homo sapiens]" 94.85 743 100.00 100.00 6.86e-58 GB AAH21211 "REPS1 protein [Homo sapiens]" 94.85 653 100.00 100.00 4.79e-58 GB AAH87547 "Reps1 protein [Mus musculus]" 94.85 716 100.00 100.00 4.17e-58 GB AAI33364 "REPS1 protein [Bos taurus]" 94.85 758 100.00 100.00 9.25e-58 REF NP_001012895 "ralBP1-associated Eps domain-containing protein 1 [Gallus gallus]" 94.85 773 100.00 100.00 1.66e-57 REF NP_001099734 "ralBP1-associated Eps domain-containing protein 1 [Rattus norvegicus]" 94.85 615 100.00 100.00 1.05e-57 REF NP_001104535 "ralBP1-associated Eps domain-containing protein 1 isoform 2 [Mus musculus]" 94.85 768 100.00 100.00 8.20e-58 REF NP_001122089 "ralBP1-associated Eps domain-containing protein 1 isoform b [Homo sapiens]" 94.85 769 100.00 100.00 1.01e-57 REF NP_001179940 "ralBP1-associated Eps domain-containing protein 1 [Bos taurus]" 94.85 794 100.00 100.00 9.95e-58 SP O54916 "RecName: Full=RalBP1-associated Eps domain-containing protein 1; AltName: Full=RalBP1-interacting protein 1 [Mus musculus]" 94.85 795 100.00 100.00 1.05e-57 SP Q96D71 "RecName: Full=RalBP1-associated Eps domain-containing protein 1; AltName: Full=RalBP1-interacting protein 1 [Homo sapiens]" 94.85 796 100.00 100.00 1.12e-57 TPG DAA26089 "TPA: RALBP1 associated Eps domain containing 1 [Bos taurus]" 94.85 786 100.00 100.00 1.10e-57 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EH_domain Mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $EH_domain 'recombinant technology' 'E. coli' Escherichia coli BL21 pLysS plasmid pGEX-2T 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $EH_domain 1.3 mM 0.5 1.5 '[U-99% 13C; U-99% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EH_domain 1.0 mM '[U-10% 13C; U-99% 15N]' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EH_domain 0.5 mM [U-15N]-Leu stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EH_domain 0.5 mM [U-15N]-Phe stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 4.2 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCBCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCBCA _Sample_label . save_ save_HNCB(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCB(CO)CA _Sample_label . save_ save_HNHB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label . save_ save_CT_1H-13C_HSQC_experiments_were_used_for_stereospecific_assignment_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'CT 1H-13C HSQC experiments were used for stereospecific assignment' _Sample_label . save_ save_of_methyl_protons_of_Val_and_Leu_with_10%_13C_and_99%_15N_labeled_sample._11 _Saveframe_category NMR_applied_experiment _Experiment_name 'of methyl protons of Val and Leu with 10% 13C and 99% 15N labeled sample.' _Sample_label . save_ save_(sample_2)_12 _Saveframe_category NMR_applied_experiment _Experiment_name (sample_2) _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCBCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCB(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name 'CT 1H-13C HSQC experiments were used for stereospecific assignment' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name 'of methyl protons of Val and Leu with 10% 13C and 99% 15N labeled sample.' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name (sample_2) _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 6.8 0.1 n/a temperature 303 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 $sample_4 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Reps1 EH domain' _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 . 3 VAL CA C 63.27 0.05 1 2 . 3 VAL CB C 32.69 0.05 1 3 . 3 VAL CG1 C 20.73 0.05 1 4 . 3 VAL CG2 C 20.73 0.05 1 5 . 6 TRP HA H 4.73 0.02 1 6 . 6 TRP HB2 H 3.47 0.02 2 7 . 6 TRP HB3 H 3.03 0.02 2 8 . 6 TRP HD1 H 7.22 0.02 1 9 . 6 TRP HE1 H 10.25 0.02 1 10 . 6 TRP HE3 H 7.58 0.02 1 11 . 6 TRP HZ2 H 7.65 0.02 1 12 . 6 TRP HZ3 H 6.86 0.02 1 13 . 6 TRP HH2 H 7.15 0.02 1 14 . 6 TRP CA C 58.35 0.05 1 15 . 6 TRP CB C 30.58 0.05 1 16 . 6 TRP NE1 N 128.8 0.05 1 17 . 7 LYS H H 7.74 0.02 1 18 . 7 LYS HA H 4.23 0.02 1 19 . 7 LYS HB2 H 1.78 0.02 1 20 . 7 LYS HB3 H 1.78 0.02 1 21 . 7 LYS HG2 H 1.68 0.02 2 22 . 7 LYS HG3 H 1.8 0.02 2 23 . 7 LYS HD2 H 1.38 0.02 2 24 . 7 LYS HD3 H 1.43 0.02 2 25 . 7 LYS HE2 H 3.05 0.02 1 26 . 7 LYS HE3 H 3.05 0.02 1 27 . 7 LYS CA C 57.30 0.05 1 28 . 7 LYS CB C 34.09 0.05 1 29 . 7 LYS CG C 29.87 0.05 1 30 . 7 LYS CD C 25.66 0.05 1 31 . 7 LYS CE C 42.53 0.05 1 32 . 7 LYS N N 119.2 0.05 1 33 . 8 ILE H H 8.54 0.02 1 34 . 8 ILE HA H 4.23 0.02 1 35 . 8 ILE HB H 1.66 0.02 1 36 . 8 ILE HG12 H 1.39 0.02 2 37 . 8 ILE HG13 H -0.15 0.02 2 38 . 8 ILE HG2 H 1.05 0.02 1 39 . 8 ILE HD1 H 0.83 0.02 1 40 . 8 ILE CA C 62.57 0.05 1 41 . 8 ILE CB C 39.02 0.05 1 42 . 8 ILE CG1 C 24.95 0.05 1 43 . 8 ILE CG2 C 17.92 0.05 1 44 . 8 ILE CD1 C 13.70 0.05 1 45 . 8 ILE N N 126.5 0.05 1 46 . 9 THR H H 8.97 0.02 1 47 . 9 THR HA H 4.52 0.02 1 48 . 9 THR HB H 4.78 0.02 1 49 . 9 THR HG2 H 1.34 0.02 1 50 . 9 THR CA C 61.87 0.05 1 51 . 9 THR CB C 71.20 0.05 1 52 . 9 THR CG2 C 22.14 0.05 1 53 . 9 THR N N 121.1 0.05 1 54 . 10 ASP H H 9.00 0.02 1 55 . 10 ASP HA H 4.42 0.02 1 56 . 10 ASP HB2 H 2.70 0.02 2 57 . 10 ASP HB3 H 2.73 0.02 2 58 . 10 ASP CA C 58.35 0.05 1 59 . 10 ASP CB C 40.40 0.05 1 60 . 10 ASP N N 121.1 0.05 1 61 . 11 GLU H H 8.75 0.02 1 62 . 11 GLU HA H 4.05 0.02 1 63 . 11 GLU HB2 H 1.98 0.02 1 64 . 11 GLU HB3 H 1.73 0.02 1 65 . 11 GLU HG2 H 2.08 0.02 2 66 . 11 GLU HG3 H 2.35 0.02 2 67 . 11 GLU CA C 61.16 0.05 1 68 . 11 GLU CB C 30.58 0.05 1 69 . 11 GLU CG C 37.61 0.05 1 70 . 11 GLU N N 118.9 0.05 1 71 . 12 GLN H H 7.61 0.02 1 72 . 12 GLN HA H 3.83 0.02 1 73 . 12 GLN HB2 H 2.21 0.02 1 74 . 12 GLN HB3 H 1.63 0.02 1 75 . 12 GLN HG2 H 2.42 0.02 1 76 . 12 GLN HG3 H 2.42 0.02 1 77 . 12 GLN HE21 H 6.94 0.02 2 78 . 12 GLN HE22 H 7.40 0.02 2 79 . 12 GLN CA C 59.05 0.05 1 80 . 12 GLN CB C 28.47 0.05 1 81 . 12 GLN CG C 34.80 0.05 1 82 . 12 GLN N N 120.8 0.05 1 83 . 12 GLN NE2 N 118.4 0.05 1 84 . 13 ARG H H 8.65 0.02 1 85 . 13 ARG HA H 3.73 0.02 1 86 . 13 ARG HB2 H 2.05 0.02 1 87 . 13 ARG HB3 H 1.95 0.02 1 88 . 13 ARG HG2 H 1.73 0.02 2 89 . 13 ARG HG3 H 1.79 0.02 2 90 . 13 ARG HD2 H 3.32 0.02 2 91 . 13 ARG HD3 H 3.37 0.02 2 92 . 13 ARG CA C 61.16 0.05 1 93 . 13 ARG CB C 30.58 0.05 1 94 . 13 ARG CD C 43.94 0.05 1 95 . 13 ARG N N 118.2 0.05 1 96 . 14 GLN H H 7.91 0.02 1 97 . 14 GLN HA H 3.98 0.02 1 98 . 14 GLN HB2 H 2.09 0.02 1 99 . 14 GLN HB3 H 2.09 0.02 1 100 . 14 GLN HG2 H 2.43 0.02 1 101 . 14 GLN HG3 H 2.43 0.02 1 102 . 14 GLN HE21 H 7.06 0.02 2 103 . 14 GLN HE22 H 7.60 0.02 2 104 . 14 GLN CA C 59.76 0.05 1 105 . 14 GLN CB C 29.17 0.05 1 106 . 14 GLN CG C 34.80 0.05 1 107 . 14 GLN N N 114.9 0.05 1 108 . 14 GLN NE2 N 112.8 0.05 1 109 . 15 TYR H H 7.36 0.02 1 110 . 15 TYR HA H 4.45 0.02 1 111 . 15 TYR HB2 H 3.12 0.02 1 112 . 15 TYR HB3 H 3.18 0.02 1 113 . 15 TYR HD1 H 7.18 0.02 1 114 . 15 TYR HD2 H 7.18 0.02 1 115 . 15 TYR HE1 H 6.95 0.02 1 116 . 15 TYR HE2 H 6.95 0.02 1 117 . 15 TYR CA C 61.87 0.05 1 118 . 15 TYR CB C 38.31 0.05 1 119 . 15 TYR N N 122.2 0.05 1 120 . 16 TYR H H 8.43 0.02 1 121 . 16 TYR HA H 4.22 0.02 1 122 . 16 TYR HB2 H 3.54 0.02 2 123 . 16 TYR HB3 H 3.58 0.02 2 124 . 16 TYR HD1 H 6.58 0.02 1 125 . 16 TYR HD2 H 6.58 0.02 1 126 . 16 TYR HE1 H 6.80 0.02 1 127 . 16 TYR HE2 H 6.80 0.02 1 128 . 16 TYR CA C 59.05 0.05 1 129 . 16 TYR CB C 39.02 0.05 1 130 . 16 TYR N N 120.02 0.05 1 131 . 17 VAL H H 9.2 0.02 1 132 . 17 VAL HA H 3.6 0.02 1 133 . 17 VAL HB H 2.17 0.02 1 134 . 17 VAL HG1 H 1.03 0.02 1 135 . 17 VAL HG2 H 1.17 0.02 1 136 . 17 VAL CA C 67.49 0.05 1 137 . 17 VAL CB C 32.69 0.05 1 138 . 17 VAL CG1 C 21.35 0.05 1 139 . 17 VAL CG2 C 23.16 0.05 1 140 . 17 VAL N N 120.4 0.05 1 141 . 18 ASN H H 8.11 0.02 1 142 . 18 ASN HA H 4.49 0.02 1 143 . 18 ASN HB2 H 2.77 0.02 1 144 . 18 ASN HB3 H 3.12 0.02 1 145 . 18 ASN HD21 H 7.03 0.02 2 146 . 18 ASN HD22 H 7.63 0.02 2 147 . 18 ASN CA C 56.94 0.05 1 148 . 18 ASN CB C 38.31 0.05 1 149 . 18 ASN N N 117.7 0.05 1 150 . 18 ASN ND2 N 111.7 0.05 1 151 . 19 GLN H H 8.17 0.02 1 152 . 19 GLN HA H 4.17 0.02 1 153 . 19 GLN HB2 H 2.50 0.02 1 154 . 19 GLN HB3 H 2.53 0.02 1 155 . 19 GLN HG2 H 2.18 0.02 2 156 . 19 GLN HG3 H 2.28 0.02 2 157 . 19 GLN HE21 H 6.99 0.02 2 158 . 19 GLN HE22 H 7.06 0.02 2 159 . 19 GLN CA C 58.70 0.05 1 160 . 19 GLN CB C 29.17 0.05 1 161 . 19 GLN CG C 34.09 0.05 1 162 . 19 GLN N N 118.2 0.05 1 163 . 19 GLN NE2 N 114.1 0.05 1 164 . 20 PHE H H 8.86 0.02 1 165 . 20 PHE HA H 2.90 0.02 1 166 . 20 PHE HB2 H 3.32 0.02 1 167 . 20 PHE HB3 H 2.69 0.02 1 168 . 20 PHE HD1 H 7.34 0.02 1 169 . 20 PHE HD2 H 7.34 0.02 1 170 . 20 PHE HE1 H 7.26 0.02 1 171 . 20 PHE HE2 H 7.26 0.02 1 172 . 20 PHE HZ H 6.68 0.02 1 173 . 20 PHE CA C 62.57 0.05 1 174 . 20 PHE CB C 39.02 0.05 1 175 . 20 PHE N N 124.5 0.05 1 176 . 21 LYS H H 7.36 0.02 1 177 . 21 LYS HA H 4.19 0.02 1 178 . 21 LYS HB2 H 1.85 0.02 1 179 . 21 LYS HB3 H 1.85 0.02 1 180 . 21 LYS HG2 H 1.68 0.02 1 181 . 21 LYS HG3 H 1.68 0.02 1 182 . 21 LYS HD2 H 1.52 0.02 1 183 . 21 LYS HD3 H 1.52 0.02 1 184 . 21 LYS HE2 H 2.93 0.02 1 185 . 21 LYS HE3 H 2.93 0.02 1 186 . 21 LYS CA C 58.35 0.05 1 187 . 21 LYS CB C 34.09 0.05 1 188 . 21 LYS CG C 31.28 0.05 1 189 . 21 LYS CD C 26.36 0.05 1 190 . 21 LYS CE C 43.23 0.05 1 191 . 21 LYS N N 115.6 0.05 1 192 . 22 THR H H 7.32 0.02 1 193 . 22 THR HA H 4.07 0.02 1 194 . 22 THR HB H 4.28 0.02 1 195 . 22 THR HG2 H 1.46 0.02 1 196 . 22 THR CA C 64.68 0.05 1 197 . 22 THR CB C 69.60 0.05 1 198 . 22 THR CG2 C 22.14 0.05 1 199 . 22 THR N N 109.3 0.05 1 200 . 23 ILE H H 7.11 0.02 1 201 . 23 ILE HA H 3.93 0.02 1 202 . 23 ILE HB H 1.20 0.02 1 203 . 23 ILE HG12 H 0.68 0.02 2 204 . 23 ILE HG13 H 1.31 0.02 2 205 . 23 ILE HG2 H 0.73 0.02 1 206 . 23 ILE HD1 H 0.19 0.02 1 207 . 23 ILE CA C 63.27 0.05 1 208 . 23 ILE CB C 40.42 0.05 1 209 . 23 ILE CG1 C 27.06 0.05 1 210 . 23 ILE CG2 C 18.61 0.05 1 211 . 23 ILE CD1 C 13.00 0.05 1 212 . 23 ILE N N 120.6 0.05 1 213 . 24 GLN H H 8.19 0.02 1 214 . 24 GLN HA H 4.53 0.02 1 215 . 24 GLN HB2 H 0.75 0.02 1 216 . 24 GLN HB3 H 1.08 0.02 1 217 . 24 GLN HG2 H 1.69 0.02 2 218 . 24 GLN HG3 H 2.51 0.02 2 219 . 24 GLN HE21 H 6.77 0.02 2 220 . 24 GLN HE22 H 7.57 0.02 2 221 . 24 GLN CA C 51.32 0.05 1 222 . 24 GLN CB C 31.98 0.05 1 223 . 24 GLN CG C 35.50 0.05 1 224 . 24 GLN N N 122.2 0.05 1 225 . 24 GLN NE2 N 111.0 0.05 1 226 . 25 PRO HA H 4.40 0.02 1 227 . 25 PRO HB2 H 2.33 0.02 1 228 . 25 PRO HB3 H 2.33 0.02 1 229 . 25 PRO HG2 H 1.97 0.02 1 230 . 25 PRO HG3 H 1.97 0.02 1 231 . 25 PRO HD2 H 3.31 0.02 2 232 . 25 PRO HD3 H 3.68 0.02 2 233 . 25 PRO CA C 64.68 0.05 1 234 . 25 PRO CB C 33.39 0.05 1 235 . 25 PRO CG C 32.69 0.05 1 236 . 25 PRO CD C 50.62 0.05 1 237 . 26 ASP H H 8.34 0.02 1 238 . 26 ASP HA H 4.75 0.02 1 239 . 26 ASP HB2 H 2.82 0.02 1 240 . 26 ASP HB3 H 2.5 0.02 1 241 . 26 ASP CA C 52.73 0.05 1 242 . 26 ASP CB C 42.12 0.05 1 243 . 26 ASP N N 116.6 0.05 1 244 . 27 LEU H H 8.54 0.02 1 245 . 27 LEU HA H 4.25 0.02 1 246 . 27 LEU HB2 H 1.6 0.02 1 247 . 27 LEU HB3 H 1.8 0.02 1 248 . 27 LEU HG H 1.92 0.02 1 249 . 27 LEU HD1 H 0.99 0.02 1 250 . 27 LEU HD2 H 0.99 0.02 1 251 . 27 LEU CA C 57.65 0.05 1 252 . 27 LEU CB C 41.83 0.05 1 253 . 27 LEU CG C 27.77 0.05 1 254 . 27 LEU CD1 C 24.00 0.05 1 255 . 27 LEU CD2 C 24.00 0.05 1 256 . 27 LEU N N 125.2 0.05 1 257 . 28 ASN H H 8.56 0.02 1 258 . 28 ASN HA H 4.88 0.02 1 259 . 28 ASN HB2 H 3.02 0.02 1 260 . 28 ASN HB3 H 2.82 0.02 1 261 . 28 ASN HD21 H 7.85 0.02 2 262 . 28 ASN HD22 H 6.95 0.02 2 263 . 28 ASN CA C 53.43 0.05 1 264 . 28 ASN CB C 39.72 0.05 1 265 . 28 ASN N N 116.1 0.05 1 266 . 28 ASN ND2 N 113.7 0.05 1 267 . 29 GLY H H 8.13 0.02 1 268 . 29 GLY HA2 H 4.25 0.02 2 269 . 29 GLY HA3 H 3.59 0.02 2 270 . 29 GLY CA C 44.64 0.05 1 271 . 29 GLY N N 108.9 0.05 1 272 . 30 PHE H H 8.19 0.02 1 273 . 30 PHE HA H 5.65 0.02 1 274 . 30 PHE HB2 H 2.83 0.02 1 275 . 30 PHE HB3 H 2.92 0.02 1 276 . 30 PHE HD1 H 7.10 0.02 1 277 . 30 PHE HD2 H 7.10 0.02 1 278 . 30 PHE HE1 H 7.45 0.02 1 279 . 30 PHE HE2 H 7.45 0.02 1 280 . 30 PHE HZ H 7.40 0.02 1 281 . 30 PHE CA C 55.54 0.05 1 282 . 30 PHE CB C 43.23 0.05 1 283 . 30 PHE N N 113.8 0.05 1 284 . 31 ILE H H 9.73 0.02 1 285 . 31 ILE HA H 4.65 0.02 1 286 . 31 ILE HB H 1.84 0.02 1 287 . 31 ILE HG12 H 1.26 0.02 2 288 . 31 ILE HG13 H 0.41 0.02 2 289 . 31 ILE HG2 H 1.02 0.02 1 290 . 31 ILE HD1 H 0.13 0.02 1 291 . 31 ILE CA C 59.05 0.05 1 292 . 31 ILE CB C 41.12 0.05 1 293 . 31 ILE CG1 C 28.47 0.05 1 294 . 31 ILE CG2 C 18.62 0.05 1 295 . 31 ILE CD1 C 15.81 0.05 1 296 . 31 ILE N N 122.3 0.05 1 297 . 32 PRO HA H 4.78 0.02 1 298 . 32 PRO HB2 H 2.68 0.02 2 299 . 32 PRO HB3 H 2.09 0.02 2 300 . 32 PRO HG2 H 2.20 0.02 2 301 . 32 PRO HG3 H 2.19 0.02 2 302 . 32 PRO HD2 H 3.80 0.02 2 303 . 32 PRO HD3 H 4.14 0.02 2 304 . 32 PRO CA C 63.98 0.05 1 305 . 32 PRO CB C 33.39 0.05 1 306 . 32 PRO CG C 28.47 0.05 1 307 . 32 PRO CD C 52.73 0.05 1 308 . 33 GLY H H 8.87 0.02 1 309 . 33 GLY HA2 H 4.18 0.02 2 310 . 33 GLY HA3 H 3.97 0.02 2 311 . 33 GLY CA C 49.91 0.05 1 312 . 33 GLY N N 111.1 0.05 1 313 . 34 SER H H 8.93 0.02 1 314 . 34 SER HA H 4.85 0.02 1 315 . 34 SER HB2 H 4.08 0.02 2 316 . 34 SER HB3 H 3.96 0.02 2 317 . 34 SER CA C 61.75 0.05 5 318 . 34 SER N N 114.7 0.05 1 319 . 35 ALA H H 7.03 0.02 1 320 . 35 ALA HA H 4.41 0.02 1 321 . 35 ALA HB H 1.52 0.02 1 322 . 35 ALA CA C 54.84 0.05 1 323 . 35 ALA CB C 19.33 0.05 1 324 . 35 ALA N N 124.2 0.05 1 325 . 36 ALA H H 8.64 0.02 1 326 . 36 ALA HA H 4.06 0.02 1 327 . 36 ALA HB H 1.89 0.02 1 328 . 36 ALA CA C 56.24 0.05 1 329 . 36 ALA CB C 19.33 0.05 1 330 . 36 ALA N N 122.1 0.05 1 331 . 37 LYS H H 8.93 0.02 1 332 . 37 LYS HA H 4.08 0.02 1 333 . 37 LYS HB2 H 1.81 0.02 1 334 . 37 LYS HB3 H 1.72 0.02 1 335 . 37 LYS HG2 H 1.15 0.02 2 336 . 37 LYS HG3 H 1.28 0.02 2 337 . 37 LYS HD2 H 1.00 0.02 2 338 . 37 LYS HD3 H 1.15 0.02 2 339 . 37 LYS HE2 H 3.13 0.02 1 340 . 37 LYS HE3 H 3.13 0.02 1 341 . 37 LYS CA C 61.87 0.05 1 342 . 37 LYS CB C 32.69 0.05 1 343 . 37 LYS CG C 29.89 0.05 1 344 . 37 LYS CD C 27.00 0.05 1 345 . 37 LYS CE C 42.53 0.05 1 346 . 37 LYS N N 117.1 0.05 1 347 . 38 GLU H H 7.73 0.02 1 348 . 38 GLU HA H 4.11 0.02 1 349 . 38 GLU HB2 H 2.19 0.02 1 350 . 38 GLU HB3 H 2.25 0.02 1 351 . 38 GLU HG2 H 2.42 0.02 2 352 . 38 GLU HG3 H 2.32 0.02 2 353 . 38 GLU CA C 60.46 0.05 1 354 . 38 GLU CB C 30.58 0.05 1 355 . 38 GLU CG C 36.91 0.05 1 356 . 38 GLU N N 120.0 0.05 1 357 . 39 PHE H H 7.93 0.02 1 358 . 39 PHE HA H 4.26 0.02 1 359 . 39 PHE HB2 H 3.06 0.02 1 360 . 39 PHE HB3 H 3.18 0.02 1 361 . 39 PHE HD1 H 6.48 0.02 1 362 . 39 PHE HD2 H 6.48 0.02 1 363 . 39 PHE HE1 H 7.02 0.02 1 364 . 39 PHE HE2 H 7.02 0.02 1 365 . 39 PHE HZ H 7.54 0.02 1 366 . 39 PHE CA C 62.00 0.05 1 367 . 39 PHE CB C 39.72 0.05 1 368 . 39 PHE N N 120.0 0.05 1 369 . 40 PHE H H 8.53 0.02 1 370 . 40 PHE HA H 4.43 0.02 1 371 . 40 PHE HB2 H 3.33 0.02 1 372 . 40 PHE HB3 H 3.05 0.02 1 373 . 40 PHE HD1 H 7.29 0.02 1 374 . 40 PHE HD2 H 7.29 0.02 1 375 . 40 PHE HE1 H 6.78 0.02 1 376 . 40 PHE HE2 H 6.78 0.02 1 377 . 40 PHE HZ H 6.53 0.02 1 378 . 40 PHE CA C 61.87 0.05 1 379 . 40 PHE CB C 39.02 0.05 1 380 . 40 PHE N N 115.5 0.05 1 381 . 41 THR H H 8.48 0.02 1 382 . 41 THR HA H 4.19 0.02 1 383 . 41 THR HB H 4.43 0.02 1 384 . 41 THR HG1 H 5.63 0.02 1 385 . 41 THR HG2 H 1.43 0.02 1 386 . 41 THR CA C 66.79 0.05 1 387 . 41 THR CB C 68.90 0.05 1 388 . 41 THR CG2 C 22.14 0.05 1 389 . 41 THR N N 118.5 0.05 1 390 . 42 LYS H H 7.35 0.02 1 391 . 42 LYS HA H 4.81 0.02 1 392 . 42 LYS HB2 H 1.85 0.02 1 393 . 42 LYS HB3 H 1.95 0.02 1 394 . 42 LYS HG2 H 1.68 0.02 2 395 . 42 LYS HG3 H 1.71 0.02 2 396 . 42 LYS HD2 H 1.51 0.02 1 397 . 42 LYS HD3 H 1.51 0.02 1 398 . 42 LYS HE2 H 3.10 0.02 1 399 . 42 LYS HE3 H 3.10 0.02 1 400 . 42 LYS CA C 58.40 0.05 1 401 . 42 LYS N N 120.6 0.05 1 402 . 43 SER H H 7.69 0.02 1 403 . 43 SER HA H 4.18 0.02 1 404 . 43 SER HB2 H 4.06 0.02 2 405 . 43 SER HB3 H 3.86 0.02 2 406 . 43 SER CA C 61.87 0.05 5 407 . 43 SER N N 113.6 0.05 1 408 . 44 LYS H H 7.89 0.02 1 409 . 44 LYS HA H 4.07 0.02 1 410 . 44 LYS HB2 H 2.22 0.02 1 411 . 44 LYS HB3 H 2.15 0.02 1 412 . 44 LYS HG2 H 1.72 0.02 2 413 . 44 LYS HG3 H 1.78 0.02 2 414 . 44 LYS HD2 H 1.43 0.02 2 415 . 44 LYS HD3 H 1.52 0.02 2 416 . 44 LYS HE2 H 3.08 0.02 1 417 . 44 LYS HE3 H 3.08 0.02 1 418 . 44 LYS CA C 58.70 0.05 1 419 . 44 LYS CB C 29.87 0.05 1 420 . 44 LYS CG C 29.87 0.05 1 421 . 44 LYS CD C 25.66 0.05 1 422 . 44 LYS CE C 43.23 0.05 1 423 . 44 LYS N N 112.7 0.05 1 424 . 45 LEU H H 7.56 0.02 1 425 . 45 LEU HA H 4.60 0.02 1 426 . 45 LEU HB2 H 1.68 0.02 1 427 . 45 LEU HB3 H 1.43 0.02 1 428 . 45 LEU HG H 1.4 0.02 1 429 . 45 LEU HD1 H 1.03 0.02 1 430 . 45 LEU HD2 H 1.03 0.02 1 431 . 45 LEU CA C 54.13 0.05 1 432 . 45 LEU CB C 42.00 0.05 1 433 . 45 LEU CG C 28.47 0.05 1 434 . 45 LEU CD1 C 27.06 0.05 1 435 . 45 LEU CD2 C 27.06 0.05 1 436 . 45 LEU N N 119.8 0.05 1 437 . 46 PRO HA H 4.58 0.02 1 438 . 46 PRO HB2 H 2.62 0.02 1 439 . 46 PRO HB3 H 2.62 0.02 1 440 . 46 PRO HG2 H 1.85 0.02 1 441 . 46 PRO HG3 H 1.85 0.02 1 442 . 46 PRO HD2 H 3.66 0.02 2 443 . 46 PRO HD3 H 3.96 0.02 2 444 . 46 PRO CA C 63.27 0.05 1 445 . 46 PRO CB C 33.39 0.05 1 446 . 46 PRO CG C 33.39 0.05 1 447 . 46 PRO CD C 51.32 0.05 1 448 . 47 ILE H H 8.65 0.02 1 449 . 47 ILE HA H 3.97 0.02 1 450 . 47 ILE HB H 2.00 0.02 1 451 . 47 ILE HG12 H 1.45 0.02 2 452 . 47 ILE HG13 H 1.52 0.02 2 453 . 47 ILE HG2 H 1.05 0.02 1 454 . 47 ILE HD1 H 0.92 0.02 1 455 . 47 ILE CA C 65.38 0.05 1 456 . 47 ILE CB C 38.00 0.05 1 457 . 47 ILE CG1 C 29.17 0.05 1 458 . 47 ILE CG2 C 17.92 0.05 1 459 . 47 ILE CD1 C 13.00 0.05 1 460 . 47 ILE N N 124.3 0.05 1 461 . 48 LEU H H 8.85 0.02 1 462 . 48 LEU HA H 4.28 0.02 1 463 . 48 LEU HB2 H 1.83 0.02 1 464 . 48 LEU HB3 H 1.58 0.02 1 465 . 48 LEU HG H 1.62 0.02 1 466 . 48 LEU HD1 H 1.03 0.02 1 467 . 48 LEU HD2 H 1.00 0.02 1 468 . 48 LEU CA C 59.05 0.05 1 469 . 48 LEU CB C 43.23 0.05 1 470 . 48 LEU CG C 27.77 0.05 1 471 . 48 LEU CD1 C 24.95 0.05 1 472 . 48 LEU CD2 C 24.25 0.05 1 473 . 48 LEU N N 120.5 0.05 1 474 . 49 GLU H H 7.22 0.02 1 475 . 49 GLU HA H 4.22 0.02 1 476 . 49 GLU HB2 H 2.07 0.02 1 477 . 49 GLU HB3 H 2.19 0.02 1 478 . 49 GLU HG2 H 2.48 0.02 1 479 . 49 GLU HG3 H 2.48 0.02 1 480 . 49 GLU CA C 60.46 0.05 1 481 . 49 GLU CB C 29.87 0.05 1 482 . 49 GLU CG C 38.31 0.05 1 483 . 49 GLU N N 117.8 0.05 1 484 . 50 LEU H H 8.03 0.02 1 485 . 50 LEU HA H 4.02 0.02 1 486 . 50 LEU HB2 H 1.52 0.02 1 487 . 50 LEU HB3 H 1.88 0.02 1 488 . 50 LEU HG H 1.61 0.02 1 489 . 50 LEU HD1 H 0.92 0.02 1 490 . 50 LEU HD2 H 0.86 0.02 1 491 . 50 LEU CA C 59.05 0.05 1 492 . 50 LEU CB C 41.83 0.05 1 493 . 50 LEU CG C 27.77 0.05 1 494 . 50 LEU CD1 C 26.36 0.05 1 495 . 50 LEU CD2 C 24.25 0.05 1 496 . 50 LEU N N 119.6 0.05 1 497 . 51 SER H H 8.73 0.02 1 498 . 51 SER HA H 4.42 0.02 1 499 . 51 SER HB2 H 4.12 0.02 1 500 . 51 SER HB3 H 4.12 0.02 1 501 . 51 SER CA C 62.57 0.05 1 502 . 51 SER CB C 63.27 0.05 1 503 . 51 SER N N 115.6 0.05 1 504 . 52 HIS H H 7.63 0.02 1 505 . 52 HIS HA H 4.61 0.02 1 506 . 52 HIS HB2 H 3.33 0.02 2 507 . 52 HIS HB3 H 3.42 0.02 2 508 . 52 HIS HD2 H 6.74 0.02 1 509 . 52 HIS HE1 H 8.08 0.02 1 510 . 52 HIS CA C 59.76 0.05 1 511 . 52 HIS CB C 31.98 0.05 1 512 . 52 HIS N N 122.3 0.05 1 513 . 53 ILE H H 8.33 0.02 1 514 . 53 ILE HA H 3.34 0.02 1 515 . 53 ILE HB H 1.91 0.02 1 516 . 53 ILE HG12 H 0.84 0.02 2 517 . 53 ILE HG13 H 0.74 0.02 2 518 . 53 ILE HG2 H 0.73 0.02 1 519 . 53 ILE HD1 H 0.74 0.02 1 520 . 53 ILE CA C 67.14 0.05 1 521 . 53 ILE CB C 39.02 0.05 1 522 . 53 ILE CG1 C 31.98 0.05 1 523 . 53 ILE CG2 C 17.22 0.05 1 524 . 53 ILE CD1 C 14.41 0.05 1 525 . 53 ILE N N 118.7 0.05 1 526 . 54 TRP H H 8.70 0.02 1 527 . 54 TRP HA H 3.90 0.02 1 528 . 54 TRP HB2 H 3.56 0.02 1 529 . 54 TRP HB3 H 3.46 0.02 1 530 . 54 TRP HD1 H 7.27 0.02 1 531 . 54 TRP HE1 H 10.20 0.02 1 532 . 54 TRP HE3 H 7.52 0.02 1 533 . 54 TRP HZ2 H 7.23 0.02 1 534 . 54 TRP HZ3 H 6.98 0.02 1 535 . 54 TRP HH2 H 6.93 0.02 1 536 . 54 TRP CA C 61.87 0.05 1 537 . 54 TRP CB C 29.17 0.05 1 538 . 54 TRP N N 122.3 0.05 1 539 . 54 TRP NE1 N 129.1 0.05 1 540 . 55 GLU H H 7.93 0.02 1 541 . 55 GLU HA H 3.98 0.02 1 542 . 55 GLU HB2 H 2.23 0.02 2 543 . 55 GLU HB3 H 2.32 0.02 2 544 . 55 GLU HG2 H 2.51 0.02 2 545 . 55 GLU HG3 H 2.56 0.02 2 546 . 55 GLU CA C 59.76 0.05 1 547 . 55 GLU CB C 29.87 0.05 1 548 . 55 GLU CG C 37.61 0.05 1 549 . 55 GLU N N 116.4 0.05 1 550 . 56 LEU H H 7.76 0.02 1 551 . 56 LEU HA H 4.50 0.02 1 552 . 56 LEU HB2 H 1.18 0.02 1 553 . 56 LEU HB3 H 1.69 0.02 1 554 . 56 LEU HG H 1.18 0.02 1 555 . 56 LEU HD1 H 0.48 0.02 1 556 . 56 LEU HD2 H 0.58 0.02 1 557 . 56 LEU CA C 57.65 0.05 1 558 . 56 LEU CB C 43.93 0.05 1 559 . 56 LEU CG C 27.77 0.05 1 560 . 56 LEU CD1 C 25.66 0.05 1 561 . 56 LEU CD2 C 23.55 0.05 1 562 . 56 LEU N N 116.0 0.05 1 563 . 57 SER H H 7.50 0.02 1 564 . 57 SER HA H 4.18 0.02 1 565 . 57 SER HB2 H 3.66 0.02 1 566 . 57 SER HB3 H 3.40 0.02 1 567 . 57 SER CA C 61.87 0.05 1 568 . 57 SER CB C 64.68 0.05 1 569 . 57 SER N N 115.6 0.05 1 570 . 58 ASP H H 7.97 0.02 1 571 . 58 ASP HA H 4.46 0.02 1 572 . 58 ASP HB2 H 2.40 0.02 1 573 . 58 ASP HB3 H 1.30 0.02 1 574 . 58 ASP CA C 52.01 0.05 1 575 . 58 ASP CB C 37.61 0.05 1 576 . 58 ASP N N 115.6 0.05 1 577 . 59 PHE H H 7.97 0.02 1 578 . 59 PHE HA H 4.36 0.02 1 579 . 59 PHE HB2 H 3.37 0.02 1 580 . 59 PHE HB3 H 3.26 0.02 1 581 . 59 PHE HD1 H 7.33 0.02 1 582 . 59 PHE HD2 H 7.33 0.02 1 583 . 59 PHE CA C 59.76 0.05 1 584 . 59 PHE CB C 40.42 0.05 1 585 . 59 PHE N N 125.9 0.05 1 586 . 60 ASP H H 8.19 0.02 1 587 . 60 ASP HA H 4.63 0.02 1 588 . 60 ASP HB2 H 2.67 0.02 1 589 . 60 ASP HB3 H 3.14 0.02 1 590 . 60 ASP CA C 52.73 0.05 1 591 . 60 ASP CB C 40.42 0.05 1 592 . 60 ASP N N 112.6 0.05 1 593 . 61 LYS H H 7.74 0.02 1 594 . 61 LYS HA H 3.93 0.02 1 595 . 61 LYS HB2 H 2.08 0.02 2 596 . 61 LYS HB3 H 2.03 0.02 2 597 . 61 LYS HG2 H 1.82 0.02 1 598 . 61 LYS HG3 H 1.82 0.02 1 599 . 61 LYS HD2 H 1.78 0.02 1 600 . 61 LYS HD3 H 1.78 0.02 1 601 . 61 LYS HE2 H 3.10 0.02 2 602 . 61 LYS HE3 H 3.20 0.02 2 603 . 61 LYS CA C 58.35 0.05 1 604 . 61 LYS CB C 29.87 0.05 1 605 . 61 LYS CG C 29.87 0.05 1 606 . 61 LYS CD C 25.66 0.05 1 607 . 61 LYS CE C 43.23 0.05 1 608 . 61 LYS N N 114.0 0.05 1 609 . 62 ASP H H 8.32 0.02 1 610 . 62 ASP HA H 4.68 0.02 1 611 . 62 ASP HB2 H 2.46 0.02 1 612 . 62 ASP HB3 H 2.99 0.02 1 613 . 62 ASP CA C 54.13 0.05 1 614 . 62 ASP CB C 41.83 0.05 1 615 . 62 ASP N N 118.1 0.05 1 616 . 63 GLY H H 10.66 0.02 1 617 . 63 GLY HA2 H 4.38 0.02 2 618 . 63 GLY HA3 H 3.92 0.02 2 619 . 63 GLY CA C 46.75 0.05 1 620 . 63 GLY N N 113.7 0.05 1 621 . 64 ALA H H 8.36 0.02 1 622 . 64 ALA HA H 5.10 0.02 1 623 . 64 ALA HB H 1.28 0.02 1 624 . 64 ALA CA C 51.37 0.05 1 625 . 64 ALA CB C 23.55 0.05 1 626 . 64 ALA N N 123.2 0.05 1 627 . 65 LEU H H 9.22 0.02 1 628 . 65 LEU HA H 6.15 0.02 1 629 . 65 LEU HB2 H 1.85 0.02 1 630 . 65 LEU HB3 H 2.11 0.02 1 631 . 65 LEU HG H 1.86 0.02 1 632 . 65 LEU HD1 H 1.13 0.02 1 633 . 65 LEU HD2 H 0.26 0.02 1 634 . 65 LEU CA C 53.43 0.05 1 635 . 65 LEU CB C 43.64 0.05 1 636 . 65 LEU CD1 C 28.47 0.05 1 637 . 65 LEU CD2 C 22.14 0.05 1 638 . 65 LEU N N 119.4 0.05 1 639 . 66 THR H H 9.10 0.02 1 640 . 66 THR HA H 4.80 0.02 1 641 . 66 THR HB H 4.31 0.02 1 642 . 66 THR HG1 H 5.65 0.02 1 643 . 66 THR HG2 H 1.48 0.02 1 644 . 66 THR CA C 61.16 0.05 1 645 . 66 THR CB C 68.90 0.05 1 646 . 66 THR CG2 C 18.62 0.05 1 647 . 66 THR N N 114.3 0.05 1 648 . 67 LEU H H 9.11 0.02 1 649 . 67 LEU HA H 3.60 0.02 1 650 . 67 LEU HB2 H 1.66 0.02 1 651 . 67 LEU HB3 H 1.66 0.02 1 652 . 67 LEU HG H 1.31 0.02 1 653 . 67 LEU HD1 H 0.41 0.02 1 654 . 67 LEU HD2 H 0.85 0.02 1 655 . 67 LEU CA C 59.76 0.05 1 656 . 67 LEU CB C 41.83 0.05 1 657 . 67 LEU CG C 27.77 0.05 1 658 . 67 LEU CD1 C 24.25 0.05 1 659 . 67 LEU CD2 C 26.30 0.05 1 660 . 67 LEU N N 120.9 0.05 1 661 . 68 ASP H H 8.64 0.02 1 662 . 68 ASP HA H 4.48 0.02 1 663 . 68 ASP HB2 H 2.81 0.02 1 664 . 68 ASP HB3 H 2.73 0.02 1 665 . 68 ASP CA C 59.76 0.05 1 666 . 68 ASP CB C 41.83 0.05 1 667 . 68 ASP N N 118.1 0.05 1 668 . 69 GLU H H 7.52 0.02 1 669 . 69 GLU HA H 3.87 0.02 1 670 . 69 GLU HB2 H 1.69 0.02 1 671 . 69 GLU HB3 H 1.69 0.02 1 672 . 69 GLU HG2 H 2.25 0.02 2 673 . 69 GLU HG3 H 1.69 0.02 2 674 . 69 GLU CA C 59.76 0.05 1 675 . 69 GLU CB C 33.30 0.05 1 676 . 69 GLU CG C 37.61 0.05 1 677 . 69 GLU N N 121.1 0.05 1 678 . 70 PHE H H 9.31 0.02 1 679 . 70 PHE HA H 4.34 0.02 1 680 . 70 PHE HB2 H 3.83 0.02 1 681 . 70 PHE HB3 H 3.33 0.02 1 682 . 70 PHE HD1 H 6.58 0.02 1 683 . 70 PHE HD2 H 6.58 0.02 1 684 . 70 PHE HE1 H 7.09 0.02 1 685 . 70 PHE HE2 H 7.09 0.02 1 686 . 70 PHE HZ H 6.58 0.02 1 687 . 70 PHE CA C 62.57 0.05 1 688 . 70 PHE CB C 40.05 0.05 1 689 . 70 PHE N N 119.1 0.05 1 690 . 71 CYS H H 8.87 0.02 1 691 . 71 CYS HA H 4.07 0.02 1 692 . 71 CYS HB2 H 2.81 0.02 1 693 . 71 CYS HB3 H 3.45 0.02 1 694 . 71 CYS CA C 65.38 0.05 1 695 . 71 CYS CB C 27.77 0.05 1 696 . 71 CYS N N 116.3 0.05 1 697 . 72 ALA H H 7.53 0.02 1 698 . 72 ALA HA H 4.11 0.02 1 699 . 72 ALA HB H 1.71 0.02 1 700 . 72 ALA CA C 56.94 0.05 1 701 . 72 ALA CB C 17.92 0.05 1 702 . 72 ALA N N 120.2 0.05 1 703 . 73 ALA H H 8.17 0.02 1 704 . 73 ALA HA H 3.69 0.02 1 705 . 73 ALA HB H 0.98 0.02 1 706 . 73 ALA CA C 55.54 0.05 1 707 . 73 ALA CB C 18.62 0.05 1 708 . 73 ALA N N 119.0 0.05 1 709 . 74 PHE H H 8.72 0.02 1 710 . 74 PHE HA H 3.90 0.02 1 711 . 74 PHE HB2 H 2.58 0.02 2 712 . 74 PHE HB3 H 2.32 0.02 2 713 . 74 PHE HD1 H 7.43 0.02 1 714 . 74 PHE HD2 H 7.43 0.02 1 715 . 74 PHE HE1 H 7.63 0.02 1 716 . 74 PHE HE2 H 7.63 0.02 1 717 . 74 PHE HZ H 7.76 0.02 1 718 . 74 PHE CA C 60.46 0.05 1 719 . 74 PHE CB C 39.02 0.05 1 720 . 74 PHE N N 118.0 0.05 1 721 . 75 HIS H H 8.22 0.02 1 722 . 75 HIS HA H 4.68 0.02 1 723 . 75 HIS HB2 H 3.29 0.02 1 724 . 75 HIS HB3 H 3.52 0.02 1 725 . 75 HIS HD2 H 7.18 0.02 1 726 . 75 HIS HE1 H 8.10 0.02 1 727 . 75 HIS CA C 61.16 0.05 1 728 . 75 HIS CB C 32.69 0.05 1 729 . 75 HIS N N 118.9 0.05 1 730 . 76 LEU H H 8.17 0.02 1 731 . 76 LEU HA H 4.18 0.02 1 732 . 76 LEU HB2 H 2.18 0.02 2 733 . 76 LEU HB3 H 1.12 0.02 2 734 . 76 LEU HG H 1.93 0.02 1 735 . 76 LEU HD1 H 0.68 0.02 1 736 . 76 LEU HD2 H 0.51 0.02 1 737 . 76 LEU CA C 59.41 0.05 1 738 . 76 LEU CB C 43.93 0.05 1 739 . 76 LEU CG C 27.77 0.05 1 740 . 76 LEU CD1 C 27.77 0.05 1 741 . 76 LEU CD2 C 24.95 0.05 1 742 . 76 LEU N N 119.8 0.05 1 743 . 77 VAL H H 8.47 0.02 1 744 . 77 VAL HA H 3.43 0.02 1 745 . 77 VAL HB H 2.43 0.02 1 746 . 77 VAL HG1 H 1.02 0.02 1 747 . 77 VAL HG2 H 0.79 0.02 1 748 . 77 VAL CA C 68.19 0.05 1 749 . 77 VAL CB C 31.98 0.05 1 750 . 77 VAL CG1 C 22.14 0.05 1 751 . 77 VAL CG2 C 24.25 0.05 1 752 . 77 VAL N N 120.7 0.05 1 753 . 78 VAL H H 8.81 0.02 1 754 . 78 VAL HA H 3.60 0.02 1 755 . 78 VAL HB H 2.32 0.02 1 756 . 78 VAL HG1 H 1.09 0.02 1 757 . 78 VAL HG2 H 1.47 0.02 1 758 . 78 VAL CA C 68.19 0.05 1 759 . 78 VAL CB C 31.98 0.05 1 760 . 78 VAL CG1 C 22.14 0.05 1 761 . 78 VAL CG2 C 24.25 0.05 1 762 . 78 VAL N N 119.7 0.05 1 763 . 79 ALA H H 8.22 0.02 1 764 . 79 ALA HA H 4.22 0.02 1 765 . 79 ALA HB H 1.52 0.02 1 766 . 79 ALA CA C 56.24 0.05 1 767 . 79 ALA CB C 18.52 0.05 1 768 . 79 ALA N N 121.4 0.05 1 769 . 80 ARG H H 8.63 0.02 1 770 . 80 ARG HA H 4.63 0.02 1 771 . 80 ARG HB2 H 2.35 0.02 1 772 . 80 ARG HB3 H 2.03 0.02 1 773 . 80 ARG HG2 H 1.90 0.02 2 774 . 80 ARG HG3 H 1.78 0.02 2 775 . 80 ARG HD2 H 3.96 0.02 2 776 . 80 ARG HD3 H 3.06 0.02 2 777 . 80 ARG CA C 57.30 0.05 1 778 . 80 ARG CB C 29.87 0.05 1 779 . 80 ARG CG C 27.06 0.05 1 780 . 80 ARG CD C 44.64 0.05 1 781 . 80 ARG N N 119.1 0.05 1 782 . 81 LYS H H 9.23 0.02 1 783 . 81 LYS HA H 4.17 0.02 1 784 . 81 LYS HB2 H 2.15 0.02 2 785 . 81 LYS HB3 H 2.06 0.02 2 786 . 81 LYS HG2 H 1.86 0.02 2 787 . 81 LYS HG3 H 1.81 0.02 2 788 . 81 LYS HD2 H 1.69 0.02 2 789 . 81 LYS HD3 H 1.81 0.02 2 790 . 81 LYS HE2 H 3.13 0.02 2 791 . 81 LYS HE3 H 3.22 0.02 2 792 . 81 LYS CA C 59.76 0.05 1 793 . 81 LYS CB C 31.98 0.05 1 794 . 81 LYS CG C 29.17 0.05 1 795 . 81 LYS CD C 25.66 0.05 1 796 . 81 LYS CE C 42.53 0.05 1 797 . 81 LYS N N 123.1 0.05 1 798 . 82 ASN H H 7.89 0.02 1 799 . 82 ASN HA H 4.83 0.02 1 800 . 82 ASN HB2 H 3.00 0.02 2 801 . 82 ASN HB3 H 3.08 0.02 2 802 . 82 ASN HD21 H 6.93 0.02 2 803 . 82 ASN HD22 H 7.37 0.02 2 804 . 82 ASN CA C 54.13 0.05 1 805 . 82 ASN CB C 40.42 0.05 1 806 . 82 ASN N N 116.2 0.05 1 807 . 82 ASN ND2 N 112.3 0.05 1 808 . 83 GLY H H 8.04 0.02 1 809 . 83 GLY HA2 H 4.19 0.02 2 810 . 83 GLY HA3 H 3.71 0.02 2 811 . 83 GLY CA C 46.50 0.05 1 812 . 83 GLY N N 106.5 0.05 1 813 . 84 TYR H H 8.03 0.02 1 814 . 84 TYR HA H 4.59 0.02 1 815 . 84 TYR HB2 H 3.08 0.02 1 816 . 84 TYR HB3 H 2.59 0.02 1 817 . 84 TYR HD1 H 7.10 0.02 1 818 . 84 TYR HD2 H 7.10 0.02 1 819 . 84 TYR HE1 H 6.71 0.02 1 820 . 84 TYR HE2 H 6.71 0.02 1 821 . 84 TYR CA C 59.05 0.05 1 822 . 84 TYR CB C 39.02 0.05 1 823 . 84 TYR N N 120.8 0.05 1 824 . 85 ASP H H 8.42 0.02 1 825 . 85 ASP HA H 4.61 0.02 1 826 . 85 ASP HB2 H 2.71 0.02 1 827 . 85 ASP HB3 H 2.63 0.02 1 828 . 85 ASP CA C 54.84 0.05 1 829 . 85 ASP CB C 41.83 0.05 1 830 . 85 ASP N N 119.8 0.05 1 831 . 86 LEU H H 8.75 0.02 1 832 . 86 LEU HA H 4.80 0.02 1 833 . 86 LEU HB2 H 1.26 0.02 1 834 . 86 LEU HB3 H 1.73 0.02 1 835 . 86 LEU HG H 1.26 0.02 1 836 . 86 LEU HD1 H 1.01 0.02 2 837 . 86 LEU HD2 H 1.00 0.02 2 838 . 86 LEU CA C 52.73 0.05 1 839 . 86 LEU CB C 43.23 0.05 1 840 . 86 LEU CD1 C 25.66 0.05 1 841 . 86 LEU CD2 C 25.66 0.05 1 842 . 86 LEU N N 121.2 0.05 1 843 . 87 PRO HA H 4.72 0.02 1 844 . 87 PRO HB2 H 2.18 0.02 2 845 . 87 PRO HB3 H 2.31 0.02 2 846 . 87 PRO HG2 H 1.58 0.02 2 847 . 87 PRO HG3 H 1.32 0.02 2 848 . 87 PRO HD2 H 3.32 0.02 2 849 . 87 PRO HD3 H 3.96 0.02 2 850 . 87 PRO CA C 62.57 0.05 1 851 . 87 PRO CB C 31.98 0.05 1 852 . 87 PRO CG C 27.06 0.05 1 853 . 87 PRO CD C 50.62 0.05 1 854 . 88 GLU HA H 4.21 0.02 1 855 . 88 GLU HB2 H 2.11 0.02 1 856 . 88 GLU HB3 H 2.11 0.02 1 857 . 88 GLU HG2 H 2.34 0.02 2 858 . 88 GLU HG3 H 2.46 0.02 2 859 . 88 GLU CA C 59.41 0.05 1 860 . 88 GLU CB C 31.28 0.05 1 861 . 88 GLU CG C 36.91 0.05 1 862 . 89 LYS H H 7.55 0.02 1 863 . 89 LYS HA H 4.46 0.02 1 864 . 89 LYS HB2 H 1.76 0.02 1 865 . 89 LYS HB3 H 1.60 0.02 1 866 . 89 LYS HG2 H 1.60 0.02 1 867 . 89 LYS HG3 H 1.60 0.02 1 868 . 89 LYS HD2 H 1.38 0.02 1 869 . 89 LYS HD3 H 1.38 0.02 1 870 . 89 LYS HE2 H 3.10 0.02 1 871 . 89 LYS HE3 H 3.10 0.02 1 872 . 89 LYS CA C 54.13 0.05 1 873 . 89 LYS CB C 36.20 0.05 1 874 . 89 LYS CG C 29.86 0.05 1 875 . 89 LYS CD C 24.95 0.05 1 876 . 89 LYS CE C 43.23 0.05 1 877 . 89 LYS N N 114.5 0.05 1 878 . 90 LEU H H 8.87 0.02 1 879 . 90 LEU HA H 3.98 0.02 1 880 . 90 LEU HB2 H 1.72 0.02 1 881 . 90 LEU HB3 H 1.72 0.02 1 882 . 90 LEU HG H 1.13 0.02 1 883 . 90 LEU HD1 H 0.87 0.02 1 884 . 90 LEU HD2 H 0.81 0.02 1 885 . 90 LEU CA C 54.13 0.05 1 886 . 90 LEU CB C 43.23 0.05 1 887 . 90 LEU CG C 26.36 0.05 1 888 . 90 LEU CD1 C 24.95 0.05 1 889 . 90 LEU CD2 C 27.77 0.05 1 890 . 90 LEU N N 124.7 0.05 1 891 . 91 PRO HA H 4.33 0.02 1 892 . 91 PRO HB2 H 2.28 0.02 2 893 . 91 PRO HB3 H 1.64 0.02 2 894 . 91 PRO HG2 H 1.20 0.02 2 895 . 91 PRO HG3 H 0.88 0.02 2 896 . 91 PRO HD2 H 3.10 0.02 2 897 . 91 PRO HD3 H 3.78 0.02 2 898 . 91 PRO CA C 63.27 0.05 1 899 . 91 PRO CB C 33.39 0.05 1 900 . 91 PRO CG C 27.00 0.05 1 901 . 91 PRO CD C 51.00 0.05 1 902 . 92 GLU H H 8.95 0.02 1 903 . 92 GLU HA H 3.99 0.02 1 904 . 92 GLU HB2 H 2.14 0.02 2 905 . 92 GLU HB3 H 2.33 0.02 2 906 . 92 GLU HG2 H 2.43 0.02 1 907 . 92 GLU HG3 H 2.43 0.02 1 908 . 92 GLU CA C 61.16 0.05 1 909 . 92 GLU CB C 29.87 0.05 1 910 . 92 GLU CG C 37.61 0.05 1 911 . 92 GLU N N 124.4 0.05 1 912 . 93 SER H H 7.77 0.02 1 913 . 93 SER HA H 4.32 0.02 1 914 . 93 SER HB2 H 3.99 0.02 1 915 . 93 SER HB3 H 3.99 0.02 1 916 . 93 SER CA C 56.21 0.05 1 917 . 93 SER N N 120.3 0.05 1 918 . 94 LEU H H 7.78 0.02 1 919 . 94 LEU HA H 4.53 0.02 1 920 . 94 LEU HB2 H 1.81 0.02 1 921 . 94 LEU HB3 H 1.65 0.02 1 922 . 94 LEU HG H 1.70 0.02 1 923 . 94 LEU HD1 H 0.98 0.02 1 924 . 94 LEU HD2 H 1.03 0.02 1 925 . 94 LEU CA C 55.54 0.05 1 926 . 94 LEU CB C 43.94 0.05 1 927 . 94 LEU CG C 28.47 0.05 1 928 . 94 LEU CD1 C 26.36 0.05 1 929 . 94 LEU CD2 C 24.95 0.05 1 930 . 94 LEU N N 119.8 0.05 1 931 . 95 MET H H 7.26 0.02 1 932 . 95 MET HA H 4.33 0.02 1 933 . 95 MET HB2 H 1.94 0.02 1 934 . 95 MET HB3 H 1.84 0.02 1 935 . 95 MET HG2 H 2.40 0.02 2 936 . 95 MET HG3 H 2.25 0.02 2 937 . 95 MET CA C 54.13 0.05 1 938 . 95 MET CB C 33.39 0.05 1 939 . 95 MET CG C 33.39 0.05 1 940 . 95 MET N N 118.8 0.05 1 941 . 96 PRO HA H 4.45 0.02 1 942 . 96 PRO HB2 H 2.28 0.02 1 943 . 96 PRO HB3 H 2.28 0.02 1 944 . 96 PRO HG2 H 1.92 0.02 2 945 . 96 PRO HG3 H 1.99 0.02 2 946 . 96 PRO HD2 H 3.31 0.02 2 947 . 96 PRO HD3 H 3.55 0.02 2 948 . 96 PRO CA C 64.20 0.05 1 949 . 96 PRO CB C 31.98 0.05 1 950 . 96 PRO CG C 28.47 0.05 1 951 . 96 PRO CD C 51.32 0.05 1 952 . 97 LYS H H 8.00 0.02 1 953 . 97 LYS HA H 4.20 0.02 1 954 . 97 LYS HB2 H 1.88 0.02 1 955 . 97 LYS HB3 H 1.75 0.02 1 956 . 97 LYS HG2 H 1.48 0.02 1 957 . 97 LYS HG3 H 1.48 0.02 1 958 . 97 LYS HE2 H 3.04 0.02 1 959 . 97 LYS HE3 H 3.04 0.02 1 960 . 97 LYS CA C 57.65 0.05 1 961 . 97 LYS CB C 34.80 0.05 1 962 . 97 LYS CG C 24.95 0.05 1 963 . 97 LYS CE C 43.23 0.05 1 964 . 97 LYS N N 126.4 0.05 1 stop_ save_