data_4981 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Identification of the phospholipid binding site of human beta2-glycoprotein I domain V by heteronuclear magnetic resonance ; _BMRB_accession_number 4981 _BMRB_flat_file_name bmr4981.str _Entry_type original _Submission_date 2001-03-27 _Accession_date 2001-04-03 _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 Hoshino Masaru . . 2 Hagihara Yoshihisa . . 3 Nishii Ichiro . . 4 Yamazaki Toshio . . 5 Kato Hisao . . 6 Goto Yuji . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 538 "13C chemical shifts" 389 "15N chemical shifts" 88 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-29 update author 'update chemical shift table' 2001-05-01 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Identification of the phospholipid binding site of human beta2-glycoprotein I domain V by heteronuclear magnetic resonance ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11124037 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hoshino Masaru . . 2 Hagihara Yoshihisa . . 3 Nishii Ichiro . . 4 Yamazaki Toshio . . 5 Kato Hisao . . 6 Goto Yuji . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 304 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 927 _Page_last 940 _Year 2000 _Details . loop_ _Keyword 'apolipoprotein H' 'short consensus repeat' 'complement control protein module' sushi-domain stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX Pipes. J. Biomol. NMR, 6, 277-293. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G.W. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Garrett, D.S., Powers, R., Gronenborn, A.M. & Clore, G.M. (1991). A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95, 214-220. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_beta2-GPI_domain_V _Saveframe_category molecular_system _Mol_system_name 'fifth domain of beta2-glycoprotein I' _Abbreviation_common 'beta2-GPI domain V' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'beta2-GPI domain V' $beta2-GPI_domain_V stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'lipid binding protein' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_beta2-GPI_domain_V _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'beta2-glycoprotein I' _Name_variant 'the fifth domain' _Abbreviation_common beta2-GPI _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 86 _Mol_residue_sequence ; TKASCKLPVKKATVVYQGER VKIQEKFKNGMLHGDKVSFF CKNKEKKCSYTEDAQCIDGT IEVPKCFKEHSSLAFWKTDA SDVKPC ; loop_ _Residue_seq_code _Residue_label 1 THR 2 LYS 3 ALA 4 SER 5 CYS 6 LYS 7 LEU 8 PRO 9 VAL 10 LYS 11 LYS 12 ALA 13 THR 14 VAL 15 VAL 16 TYR 17 GLN 18 GLY 19 GLU 20 ARG 21 VAL 22 LYS 23 ILE 24 GLN 25 GLU 26 LYS 27 PHE 28 LYS 29 ASN 30 GLY 31 MET 32 LEU 33 HIS 34 GLY 35 ASP 36 LYS 37 VAL 38 SER 39 PHE 40 PHE 41 CYS 42 LYS 43 ASN 44 LYS 45 GLU 46 LYS 47 LYS 48 CYS 49 SER 50 TYR 51 THR 52 GLU 53 ASP 54 ALA 55 GLN 56 CYS 57 ILE 58 ASP 59 GLY 60 THR 61 ILE 62 GLU 63 VAL 64 PRO 65 LYS 66 CYS 67 PHE 68 LYS 69 GLU 70 HIS 71 SER 72 SER 73 LEU 74 ALA 75 PHE 76 TRP 77 LYS 78 THR 79 ASP 80 ALA 81 SER 82 ASP 83 VAL 84 LYS 85 PRO 86 CYS 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 16639 beta2GPI 97.67 85 97.62 98.81 1.97e-52 PDB 1C1Z "Crystal Structure Of Human Beta-2-Glycoprotein-I (Apolipoprotein-H)" 98.84 326 100.00 100.00 4.07e-51 PDB 1G4F "Nmr Structure Of The Fifth Domain Of Human Beta2- Glycoprotein I" 100.00 86 100.00 100.00 1.01e-54 PDB 1G4G "Nmr Structure Of The Fifth Domain Of Human Beta2- Glycoprotein I" 100.00 86 100.00 100.00 1.01e-54 PDB 2KRI "Structure Of A Complex Between Domain V Of Beta2- Glycoprotein I And The Fourth Ligand-Binding Module From Ldlr Determined With" 97.67 85 98.81 98.81 5.28e-53 PDB 3OP8 "Crystal Structure Of The Domain V From Beta2-Glycoprotein I" 97.67 85 98.81 98.81 5.28e-53 PDB 4JHS "Crystal Structure Of A C-terminal Two Domain Fragment Of Human Beta-2- Glycoprotein 1" 98.84 180 98.82 100.00 4.21e-52 DBJ BAG36570 "unnamed protein product [Homo sapiens]" 98.84 345 98.82 100.00 1.51e-50 DBJ BAG60642 "unnamed protein product [Homo sapiens]" 98.84 274 98.82 100.00 3.93e-51 DBJ BAI46022 "apolipoprotein H [synthetic construct]" 98.84 345 100.00 100.00 4.39e-51 EMBL CAA37664 "beta-2-glycoprotein I [Homo sapiens]" 98.84 345 100.00 100.00 4.39e-51 EMBL CAA40977 "Apolipoprotein H (beta2-glycoprotein I) [Homo sapiens]" 98.84 345 98.82 100.00 1.58e-50 EMBL CAA41113 "Beta-2-glycoprotein I apolipoprotein H [Homo sapiens]" 98.84 345 100.00 100.00 4.39e-51 EMBL CAA72279 "beta-2-glycoprotein I [Homo sapiens]" 98.84 345 98.82 100.00 1.58e-50 GB AAA51766 "apolipoprotein H [Homo sapiens]" 98.84 345 98.82 100.00 1.58e-50 GB AAB21330 "beta 2-glycoprotein I [Homo sapiens]" 98.84 345 98.82 100.00 1.58e-50 GB AAH20703 "Apolipoprotein H (beta-2-glycoprotein I) [Homo sapiens]" 98.84 345 98.82 100.00 1.58e-50 GB AAH26283 "Apolipoprotein H (beta-2-glycoprotein I) [Homo sapiens]" 98.84 345 98.82 100.00 1.58e-50 GB AAK71538 "apolipoprotein H precursor [Pan troglodytes]" 98.84 345 98.82 100.00 1.65e-50 REF NP_000033 "beta-2-glycoprotein 1 precursor [Homo sapiens]" 98.84 345 98.82 100.00 1.58e-50 REF NP_001009118 "beta-2-glycoprotein 1 precursor [Pan troglodytes]" 98.84 345 98.82 100.00 1.65e-50 REF XP_001084366 "PREDICTED: beta-2-glycoprotein 1-like isoform 2 [Macaca mulatta]" 98.84 292 98.82 100.00 4.44e-51 REF XP_002748690 "PREDICTED: beta-2-glycoprotein 1 isoform X1 [Callithrix jacchus]" 98.84 372 97.65 98.82 1.24e-49 REF XP_002827786 "PREDICTED: beta-2-glycoprotein 1, partial [Pongo abelii]" 98.84 181 97.65 100.00 1.19e-51 SP P02749 "RecName: Full=Beta-2-glycoprotein 1; AltName: Full=APC inhibitor; AltName: Full=Activated protein C-binding protein; AltName: F" 98.84 345 98.82 100.00 1.58e-50 SP Q95LB0 "RecName: Full=Beta-2-glycoprotein 1; AltName: Full=Apolipoprotein H; Short=Apo-H; AltName: Full=Beta-2-glycoprotein I; Short=B2" 98.84 345 98.82 100.00 1.65e-50 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $beta2-GPI_domain_V human 9606 Eukaryota Metazoa Homo sapiens blood 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 $beta2-GPI_domain_V 'recombinant technology' 'P. pastoris' Pichia pastoris . . 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 $beta2-GPI_domain_V 1.0 mM [U-15N] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $beta2-GPI_domain_V 1.0 mM '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version 1.7 loop_ _Task processing stop_ _Details . _Citation_label $ref_1 save_ save_pipp _Saveframe_category software _Name pipp _Version 3.9.9 loop_ _Task processing stop_ _Details . _Citation_label $ref_2 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_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HN(CO)CAHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CAHA _Sample_label . save_ save_1H-13C-1H_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C-1H HCCH-TOCSY' _Sample_label . save_ save_1H-1H-15N_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY' _Sample_label . save_ save_13C-1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-1H-1H NOESY' _Sample_label . save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CAHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C-1H HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-1H-1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.1 n/a temperature 298 0.1 K 'ionic strength' 0.12 0.01 M 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-1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCACB CBCA(CO)NH HN(CO)CAHA '1H-13C-1H HCCH-TOCSY' '1H-1H-15N NOESY' '13C-1H-1H NOESY' HNCO stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'beta2-GPI domain V' _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 . 1 THR H H 8.23 0.03 1 2 . 1 THR HA H 4.14 0.03 1 3 . 1 THR HB H 4.09 0.03 1 4 . 1 THR HG2 H 1.19 0.03 1 5 . 1 THR C C 174.33 0.50 1 6 . 1 THR CA C 62.23 0.50 1 7 . 1 THR CB C 69.76 0.50 1 8 . 1 THR CG2 C 21.75 0.50 1 9 . 1 THR N N 117.44 0.25 1 10 . 2 LYS H H 8.61 0.03 1 11 . 2 LYS HA H 3.91 0.03 1 12 . 2 LYS HB2 H 1.29 0.03 1 13 . 2 LYS HB3 H 1.29 0.03 1 14 . 2 LYS HG2 H 0.85 0.03 1 15 . 2 LYS HG3 H 0.85 0.03 1 16 . 2 LYS HD2 H 1.29 0.03 2 17 . 2 LYS HD3 H 1.10 0.03 2 18 . 2 LYS HE2 H 2.77 0.03 1 19 . 2 LYS HE3 H 2.77 0.03 1 20 . 2 LYS C C 176.29 0.50 1 21 . 2 LYS CA C 55.57 0.50 1 22 . 2 LYS CB C 32.45 0.50 1 23 . 2 LYS CG C 24.95 0.50 1 24 . 2 LYS CD C 28.41 0.50 1 25 . 2 LYS CE C 42.02 0.50 1 26 . 2 LYS N N 124.28 0.25 1 27 . 3 ALA H H 8.75 0.03 1 28 . 3 ALA HA H 4.18 0.03 1 29 . 3 ALA HB H 1.27 0.03 1 30 . 3 ALA C C 176.99 0.50 1 31 . 3 ALA CA C 53.08 0.50 1 32 . 3 ALA CB C 19.01 0.50 1 33 . 3 ALA N N 126.54 0.25 1 34 . 4 SER H H 7.97 0.03 1 35 . 4 SER HA H 4.69 0.03 1 36 . 4 SER HB2 H 4.03 0.03 2 37 . 4 SER HB3 H 3.93 0.03 2 38 . 4 SER C C 173.52 0.50 1 39 . 4 SER CA C 57.85 0.50 1 40 . 4 SER CB C 64.44 0.50 1 41 . 4 SER N N 114.92 0.25 1 42 . 5 CYS H H 9.20 0.03 1 43 . 5 CYS HA H 4.78 0.03 1 44 . 5 CYS HB2 H 2.50 0.03 1 45 . 5 CYS HB3 H 3.02 0.03 1 46 . 5 CYS C C 174.35 0.50 1 47 . 5 CYS CA C 56.78 0.50 1 48 . 5 CYS CB C 44.26 0.50 1 49 . 5 CYS N N 117.05 0.25 1 50 . 6 LYS H H 8.49 0.03 1 51 . 6 LYS HA H 4.22 0.03 1 52 . 6 LYS HB2 H 1.70 0.03 1 53 . 6 LYS HB3 H 1.70 0.03 1 54 . 6 LYS HG2 H 1.43 0.03 1 55 . 6 LYS HG3 H 1.43 0.03 1 56 . 6 LYS HD2 H 1.65 0.03 1 57 . 6 LYS HD3 H 1.65 0.03 1 58 . 6 LYS HE2 H 2.97 0.03 1 59 . 6 LYS HE3 H 2.97 0.03 1 60 . 6 LYS C C 176.66 0.50 1 61 . 6 LYS CA C 55.63 0.50 1 62 . 6 LYS CB C 32.74 0.50 1 63 . 6 LYS CG C 25.02 0.50 1 64 . 6 LYS CD C 28.91 0.50 1 65 . 6 LYS CE C 41.81 0.50 1 66 . 6 LYS N N 124.52 0.25 1 67 . 7 LEU H H 8.64 0.03 1 68 . 7 LEU HA H 4.15 0.03 1 69 . 7 LEU HB2 H 1.51 0.03 1 70 . 7 LEU HB3 H 1.78 0.03 1 71 . 7 LEU HG H 1.70 0.03 1 72 . 7 LEU HD1 H 0.90 0.03 2 73 . 7 LEU HD2 H 0.85 0.03 2 74 . 7 LEU CA C 53.25 0.50 1 75 . 7 LEU CB C 41.92 0.50 1 76 . 7 LEU CG C 27.94 0.50 1 77 . 7 LEU CD1 C 25.16 0.50 1 78 . 7 LEU CD2 C 25.16 0.50 1 79 . 7 LEU N N 123.83 0.25 1 80 . 8 PRO HA H 4.55 0.03 1 81 . 8 PRO HB2 H 2.14 0.03 2 82 . 8 PRO HB3 H 2.00 0.03 2 83 . 8 PRO HG2 H 1.91 0.03 2 84 . 8 PRO HG3 H 1.74 0.03 2 85 . 8 PRO HD2 H 3.93 0.03 2 86 . 8 PRO HD3 H 3.45 0.03 2 87 . 8 PRO C C 175.36 0.50 1 88 . 8 PRO CA C 63.70 0.50 1 89 . 8 PRO CB C 31.57 0.50 1 90 . 8 PRO CG C 26.87 0.50 1 91 . 8 PRO CD C 50.42 0.50 1 92 . 9 VAL H H 6.82 0.03 1 93 . 9 VAL HA H 4.50 0.03 1 94 . 9 VAL HB H 2.20 0.03 1 95 . 9 VAL HG1 H 0.92 0.03 2 96 . 9 VAL HG2 H 0.75 0.03 2 97 . 9 VAL C C 173.69 0.50 1 98 . 9 VAL CA C 58.86 0.50 1 99 . 9 VAL CB C 35.28 0.50 1 100 . 9 VAL CG1 C 22.61 0.50 2 101 . 9 VAL CG2 C 19.82 0.50 2 102 . 9 VAL N N 113.15 0.25 1 103 . 10 LYS H H 8.73 0.03 1 104 . 10 LYS HA H 4.17 0.03 1 105 . 10 LYS HB2 H 1.83 0.03 1 106 . 10 LYS HB3 H 1.83 0.03 1 107 . 10 LYS HG2 H 1.53 0.03 2 108 . 10 LYS HG3 H 1.41 0.03 2 109 . 10 LYS HD2 H 1.67 0.03 1 110 . 10 LYS HD3 H 1.67 0.03 1 111 . 10 LYS HE2 H 2.98 0.03 1 112 . 10 LYS HE3 H 2.98 0.03 1 113 . 10 LYS C C 177.17 0.50 1 114 . 10 LYS CA C 58.16 0.50 1 115 . 10 LYS CB C 33.25 0.50 1 116 . 10 LYS CG C 25.27 0.50 1 117 . 10 LYS N N 120.99 0.25 1 118 . 11 LYS H H 7.50 0.03 1 119 . 11 LYS HA H 4.51 0.03 1 120 . 11 LYS HB2 H 1.71 0.03 1 121 . 11 LYS HB3 H 1.71 0.03 1 122 . 11 LYS HG2 H 1.33 0.03 2 123 . 11 LYS HG3 H 1.25 0.03 2 124 . 11 LYS HD2 H 1.61 0.03 1 125 . 11 LYS HD3 H 1.61 0.03 1 126 . 11 LYS HE2 H 2.91 0.03 1 127 . 11 LYS HE3 H 2.91 0.03 1 128 . 11 LYS C C 175.32 0.50 1 129 . 11 LYS CA C 55.62 0.50 1 130 . 11 LYS CB C 35.87 0.50 1 131 . 11 LYS CG C 24.98 0.50 1 132 . 11 LYS CD C 29.36 0.50 1 133 . 11 LYS CE C 41.85 0.50 1 134 . 11 LYS N N 115.85 0.25 1 135 . 12 ALA H H 8.24 0.03 1 136 . 12 ALA HA H 4.63 0.03 1 137 . 12 ALA HB H 1.61 0.03 1 138 . 12 ALA C C 175.91 0.50 1 139 . 12 ALA CA C 53.82 0.50 1 140 . 12 ALA CB C 21.83 0.50 1 141 . 12 ALA N N 122.77 0.25 1 142 . 13 THR H H 8.89 0.03 1 143 . 13 THR HA H 5.07 0.03 1 144 . 13 THR HB H 3.96 0.03 1 145 . 13 THR HG2 H 1.09 0.03 1 146 . 13 THR C C 173.10 0.50 1 147 . 13 THR CA C 63.06 0.50 1 148 . 13 THR CB C 68.96 0.50 1 149 . 13 THR CG2 C 21.35 0.50 1 150 . 13 THR N N 122.30 0.25 1 151 . 14 VAL H H 9.22 0.03 1 152 . 14 VAL HA H 5.07 0.03 1 153 . 14 VAL HB H 1.74 0.03 1 154 . 14 VAL HG1 H 0.41 0.03 2 155 . 14 VAL HG2 H 0.00 0.03 2 156 . 14 VAL C C 174.17 0.50 1 157 . 14 VAL CA C 58.00 0.50 1 158 . 14 VAL CB C 35.95 0.50 1 159 . 14 VAL CG1 C 28.10 0.50 2 160 . 14 VAL CG2 C 22.27 0.50 2 161 . 14 VAL N N 118.92 0.25 1 162 . 15 VAL H H 8.64 0.03 1 163 . 15 VAL HA H 4.78 0.03 1 164 . 15 VAL HB H 1.70 0.03 1 165 . 15 VAL HG1 H 0.79 0.03 2 166 . 15 VAL HG2 H 0.73 0.03 2 167 . 15 VAL C C 176.32 0.50 1 168 . 15 VAL CA C 61.72 0.50 1 169 . 15 VAL CB C 32.55 0.50 1 170 . 15 VAL CG1 C 22.10 0.50 2 171 . 15 VAL CG2 C 21.97 0.50 2 172 . 15 VAL N N 119.59 0.25 1 173 . 16 TYR H H 9.50 0.03 1 174 . 16 TYR HA H 5.10 0.03 1 175 . 16 TYR HB2 H 2.83 0.03 1 176 . 16 TYR HB3 H 2.83 0.03 1 177 . 16 TYR HD1 H 7.46 0.03 1 178 . 16 TYR HD2 H 7.46 0.03 1 179 . 16 TYR HE1 H 6.91 0.03 1 180 . 16 TYR HE2 H 6.91 0.03 1 181 . 16 TYR C C 174.68 0.50 1 182 . 16 TYR CA C 56.53 0.50 1 183 . 16 TYR CB C 41.95 0.50 1 184 . 16 TYR CD1 C 134.00 0.50 1 185 . 16 TYR CD2 C 134.00 0.50 1 186 . 16 TYR CE1 C 118.67 0.50 1 187 . 16 TYR CE2 C 118.67 0.50 1 188 . 16 TYR N N 128.22 0.25 1 189 . 17 GLN H H 9.38 0.03 1 190 . 17 GLN HA H 3.59 0.03 1 191 . 17 GLN HB2 H 1.58 0.03 1 192 . 17 GLN HB3 H 1.86 0.03 1 193 . 17 GLN HG2 H 1.51 0.03 2 194 . 17 GLN HG3 H 1.17 0.03 2 195 . 17 GLN HE21 H 7.03 0.03 2 196 . 17 GLN HE22 H 6.70 0.03 2 197 . 17 GLN C C 176.24 0.50 1 198 . 17 GLN CA C 56.61 0.50 1 199 . 17 GLN CB C 26.02 0.50 1 200 . 17 GLN CG C 32.94 0.50 1 201 . 17 GLN CD C 181.19 0.50 1 202 . 17 GLN N N 128.18 0.25 1 203 . 17 GLN NE2 N 111.57 0.25 1 204 . 18 GLY H H 8.29 0.03 1 205 . 18 GLY HA2 H 4.08 0.03 2 206 . 18 GLY HA3 H 3.39 0.03 2 207 . 18 GLY C C 173.22 0.50 1 208 . 18 GLY CA C 45.43 0.50 1 209 . 18 GLY N N 103.24 0.25 1 210 . 19 GLU H H 7.75 0.03 1 211 . 19 GLU HA H 4.69 0.03 1 212 . 19 GLU HB2 H 2.05 0.03 2 213 . 19 GLU HB3 H 1.89 0.03 2 214 . 19 GLU HG2 H 2.28 0.03 2 215 . 19 GLU HG3 H 2.19 0.03 2 216 . 19 GLU C C 174.89 0.50 1 217 . 19 GLU CA C 54.30 0.50 1 218 . 19 GLU CB C 33.13 0.50 1 219 . 19 GLU CG C 35.87 0.50 1 220 . 19 GLU N N 121.68 0.25 1 221 . 20 ARG H H 8.78 0.03 1 222 . 20 ARG HA H 4.92 0.03 1 223 . 20 ARG HB2 H 1.79 0.03 1 224 . 20 ARG HB3 H 1.56 0.03 1 225 . 20 ARG HG2 H 1.80 0.03 2 226 . 20 ARG HG3 H 1.41 0.03 2 227 . 20 ARG HD2 H 3.23 0.03 2 228 . 20 ARG HD3 H 3.06 0.03 2 229 . 20 ARG C C 176.53 0.50 1 230 . 20 ARG CA C 56.62 0.50 1 231 . 20 ARG CB C 30.65 0.50 1 232 . 20 ARG CG C 28.82 0.50 1 233 . 20 ARG CD C 43.74 0.50 1 234 . 20 ARG N N 124.20 0.25 1 235 . 21 VAL H H 9.46 0.03 1 236 . 21 VAL HA H 4.76 0.03 1 237 . 21 VAL HB H 2.08 0.03 1 238 . 21 VAL HG1 H 0.93 0.03 2 239 . 21 VAL HG2 H 0.64 0.03 2 240 . 21 VAL C C 174.10 0.50 1 241 . 21 VAL CA C 58.65 0.50 1 242 . 21 VAL CB C 35.85 0.50 1 243 . 21 VAL CG1 C 21.81 0.50 2 244 . 21 VAL CG2 C 19.61 0.50 2 245 . 21 VAL N N 119.52 0.25 1 246 . 22 LYS H H 8.78 0.03 1 247 . 22 LYS HA H 5.01 0.03 1 248 . 22 LYS HB2 H 1.66 0.03 1 249 . 22 LYS HB3 H 1.58 0.03 1 250 . 22 LYS HG2 H 1.53 0.03 2 251 . 22 LYS HG3 H 1.40 0.03 2 252 . 22 LYS HD2 H 1.63 0.03 2 253 . 22 LYS HD3 H 1.57 0.03 2 254 . 22 LYS HE2 H 2.91 0.03 1 255 . 22 LYS HE3 H 2.91 0.03 1 256 . 22 LYS C C 179.22 0.50 1 257 . 22 LYS CA C 55.07 0.50 1 258 . 22 LYS CB C 31.65 0.50 1 259 . 22 LYS CG C 25.25 0.50 1 260 . 22 LYS CD C 28.98 0.50 1 261 . 22 LYS CE C 42.00 0.50 1 262 . 22 LYS N N 121.26 0.25 1 263 . 23 ILE H H 9.32 0.03 1 264 . 23 ILE HA H 3.71 0.03 1 265 . 23 ILE HB H 1.79 0.03 1 266 . 23 ILE HG12 H 1.48 0.03 1 267 . 23 ILE HG13 H 1.48 0.03 1 268 . 23 ILE HG2 H 1.03 0.03 1 269 . 23 ILE HD1 H 0.65 0.03 1 270 . 23 ILE C C 175.16 0.50 1 271 . 23 ILE CA C 66.18 0.50 1 272 . 23 ILE CB C 38.10 0.50 1 273 . 23 ILE CG1 C 29.20 0.50 1 274 . 23 ILE CG2 C 17.36 0.50 1 275 . 23 ILE CD1 C 13.85 0.50 1 276 . 23 ILE N N 130.57 0.25 1 277 . 24 GLN H H 9.83 0.03 1 278 . 24 GLN HA H 4.15 0.03 1 279 . 24 GLN HB2 H 2.13 0.03 1 280 . 24 GLN HB3 H 2.38 0.03 1 281 . 24 GLN HG2 H 2.85 0.03 2 282 . 24 GLN HG3 H 2.19 0.03 2 283 . 24 GLN HE21 H 8.06 0.03 2 284 . 24 GLN HE22 H 7.20 0.03 2 285 . 24 GLN C C 175.53 0.50 1 286 . 24 GLN CA C 56.87 0.50 1 287 . 24 GLN CB C 26.08 0.50 1 288 . 24 GLN CG C 32.59 0.50 1 289 . 24 GLN CD C 181.31 0.50 1 290 . 24 GLN N N 119.74 0.25 1 291 . 24 GLN NE2 N 113.22 0.25 1 292 . 25 GLU H H 7.32 0.03 1 293 . 25 GLU HA H 4.38 0.03 1 294 . 25 GLU HB2 H 1.99 0.03 1 295 . 25 GLU HB3 H 2.08 0.03 1 296 . 25 GLU HG2 H 2.20 0.03 1 297 . 25 GLU HG3 H 2.20 0.03 1 298 . 25 GLU C C 177.18 0.50 1 299 . 25 GLU CA C 57.15 0.50 1 300 . 25 GLU CB C 30.75 0.50 1 301 . 25 GLU CG C 36.36 0.50 1 302 . 25 GLU N N 120.14 0.25 1 303 . 26 LYS H H 7.77 0.03 1 304 . 26 LYS HA H 3.92 0.03 1 305 . 26 LYS HB2 H 1.50 0.03 1 306 . 26 LYS HB3 H 1.06 0.03 1 307 . 26 LYS HG2 H 0.50 0.03 2 308 . 26 LYS HG3 H -0.18 0.03 2 309 . 26 LYS HD2 H 1.51 0.03 2 310 . 26 LYS HD3 H 1.39 0.03 2 311 . 26 LYS HE2 H 2.77 0.03 2 312 . 26 LYS HE3 H 2.57 0.03 2 313 . 26 LYS C C 176.23 0.50 1 314 . 26 LYS CA C 56.67 0.50 1 315 . 26 LYS CB C 32.17 0.50 1 316 . 26 LYS CG C 23.78 0.50 1 317 . 26 LYS CD C 27.23 0.50 1 318 . 26 LYS CE C 41.87 0.50 1 319 . 26 LYS N N 119.93 0.25 1 320 . 27 PHE H H 7.68 0.03 1 321 . 27 PHE HA H 4.94 0.03 1 322 . 27 PHE HB2 H 2.73 0.03 1 323 . 27 PHE HB3 H 3.05 0.03 1 324 . 27 PHE HD1 H 7.16 0.03 1 325 . 27 PHE HD2 H 7.16 0.03 1 326 . 27 PHE HE1 H 6.67 0.03 1 327 . 27 PHE HE2 H 6.67 0.03 1 328 . 27 PHE HZ H 5.50 0.03 1 329 . 27 PHE C C 176.28 0.50 1 330 . 27 PHE CA C 55.74 0.50 1 331 . 27 PHE CB C 37.19 0.50 1 332 . 27 PHE CD1 C 131.83 0.50 1 333 . 27 PHE CD2 C 131.83 0.50 1 334 . 27 PHE CE1 C 130.39 0.50 1 335 . 27 PHE CE2 C 130.39 0.50 1 336 . 27 PHE CZ C 129.04 0.50 1 337 . 27 PHE N N 115.75 0.25 1 338 . 28 LYS H H 6.95 0.03 1 339 . 28 LYS HA H 3.92 0.03 1 340 . 28 LYS HB2 H 1.91 0.03 1 341 . 28 LYS HB3 H 1.91 0.03 1 342 . 28 LYS HG2 H 1.38 0.03 1 343 . 28 LYS HG3 H 1.38 0.03 1 344 . 28 LYS HD2 H 1.72 0.03 1 345 . 28 LYS HD3 H 1.72 0.03 1 346 . 28 LYS HE2 H 3.03 0.03 1 347 . 28 LYS HE3 H 3.03 0.03 1 348 . 28 LYS C C 177.63 0.50 1 349 . 28 LYS CA C 59.71 0.50 1 350 . 28 LYS CB C 32.55 0.50 1 351 . 28 LYS CG C 24.13 0.50 1 352 . 28 LYS N N 120.54 0.25 1 353 . 29 ASN H H 8.68 0.03 1 354 . 29 ASN HA H 5.02 0.03 1 355 . 29 ASN HB2 H 2.63 0.03 1 356 . 29 ASN HB3 H 3.03 0.03 1 357 . 29 ASN HD21 H 7.63 0.03 2 358 . 29 ASN HD22 H 6.93 0.03 2 359 . 29 ASN C C 175.12 0.50 1 360 . 29 ASN CA C 52.46 0.50 1 361 . 29 ASN CB C 39.04 0.50 1 362 . 29 ASN CG C 178.06 0.50 1 363 . 29 ASN N N 116.07 0.25 1 364 . 29 ASN ND2 N 114.28 0.25 1 365 . 30 GLY H H 7.80 0.03 1 366 . 30 GLY HA2 H 4.48 0.03 2 367 . 30 GLY HA3 H 3.60 0.03 2 368 . 30 GLY C C 172.43 0.50 1 369 . 30 GLY CA C 44.10 0.50 1 370 . 30 GLY N N 109.08 0.25 1 371 . 31 MET H H 8.55 0.03 1 372 . 31 MET HA H 4.57 0.03 1 373 . 31 MET HB2 H 1.48 0.03 1 374 . 31 MET HB3 H 1.93 0.03 1 375 . 31 MET HG2 H 1.92 0.03 2 376 . 31 MET HG3 H 1.49 0.03 2 377 . 31 MET C C 174.57 0.50 1 378 . 31 MET CA C 54.40 0.50 1 379 . 31 MET CB C 37.11 0.50 1 380 . 31 MET CG C 31.31 0.50 1 381 . 31 MET N N 117.78 0.25 1 382 . 32 LEU H H 9.03 0.03 1 383 . 32 LEU HA H 4.40 0.03 1 384 . 32 LEU HB2 H 1.72 0.03 1 385 . 32 LEU HB3 H 1.41 0.03 1 386 . 32 LEU HG H 1.79 0.03 1 387 . 32 LEU HD1 H 0.98 0.03 2 388 . 32 LEU HD2 H 0.86 0.03 2 389 . 32 LEU C C 178.28 0.50 1 390 . 32 LEU CA C 53.99 0.50 1 391 . 32 LEU CB C 42.60 0.50 1 392 . 32 LEU CG C 27.18 0.50 1 393 . 32 LEU CD1 C 25.38 0.50 2 394 . 32 LEU CD2 C 22.70 0.50 2 395 . 32 LEU N N 123.92 0.25 1 396 . 33 HIS H H 8.45 0.03 1 397 . 33 HIS HA H 4.02 0.03 1 398 . 33 HIS HB2 H 2.67 0.03 1 399 . 33 HIS HB3 H 2.97 0.03 1 400 . 33 HIS HD2 H 6.90 0.03 1 401 . 33 HIS HE1 H 7.81 0.03 1 402 . 33 HIS C C 177.38 0.50 1 403 . 33 HIS CA C 59.87 0.50 1 404 . 33 HIS CB C 30.72 0.50 1 405 . 33 HIS CD2 C 118.44 0.50 1 406 . 33 HIS CE1 C 138.62 0.50 1 407 . 33 HIS N N 121.68 0.25 1 408 . 34 GLY H H 9.00 0.03 1 409 . 34 GLY HA2 H 4.23 0.03 2 410 . 34 GLY HA3 H 3.20 0.03 2 411 . 34 GLY C C 175.28 0.50 1 412 . 34 GLY CA C 44.51 0.50 1 413 . 34 GLY N N 118.59 0.25 1 414 . 35 ASP H H 8.33 0.03 1 415 . 35 ASP HA H 4.69 0.03 1 416 . 35 ASP HB2 H 2.85 0.03 2 417 . 35 ASP HB3 H 2.19 0.03 2 418 . 35 ASP C C 174.48 0.50 1 419 . 35 ASP CA C 56.33 0.50 1 420 . 35 ASP CB C 41.67 0.50 1 421 . 35 ASP N N 124.44 0.25 1 422 . 36 LYS H H 8.49 0.03 1 423 . 36 LYS HA H 5.20 0.03 1 424 . 36 LYS HB2 H 1.74 0.03 2 425 . 36 LYS HB3 H 1.55 0.03 2 426 . 36 LYS HG2 H 1.33 0.03 2 427 . 36 LYS HG3 H 1.24 0.03 2 428 . 36 LYS HD2 H 1.55 0.03 1 429 . 36 LYS HD3 H 1.55 0.03 1 430 . 36 LYS HE2 H 2.82 0.03 1 431 . 36 LYS HE3 H 2.82 0.03 1 432 . 36 LYS C C 175.23 0.50 1 433 . 36 LYS CA C 54.92 0.50 1 434 . 36 LYS CB C 36.26 0.50 1 435 . 36 LYS CG C 24.63 0.50 1 436 . 36 LYS CD C 29.36 0.50 1 437 . 36 LYS CE C 41.37 0.50 1 438 . 36 LYS N N 123.91 0.25 1 439 . 37 VAL H H 8.63 0.03 1 440 . 37 VAL HA H 5.21 0.03 1 441 . 37 VAL HB H 1.66 0.03 1 442 . 37 VAL HG1 H 0.66 0.03 2 443 . 37 VAL HG2 H 0.33 0.03 2 444 . 37 VAL C C 174.30 0.50 1 445 . 37 VAL CA C 58.19 0.50 1 446 . 37 VAL CB C 35.79 0.50 1 447 . 37 VAL CG1 C 23.31 0.50 2 448 . 37 VAL CG2 C 18.75 0.50 2 449 . 37 VAL N N 115.82 0.25 1 450 . 38 SER H H 8.70 0.03 1 451 . 38 SER HA H 5.27 0.03 1 452 . 38 SER HB2 H 3.28 0.03 1 453 . 38 SER HB3 H 3.50 0.03 1 454 . 38 SER C C 173.27 0.50 1 455 . 38 SER CA C 57.08 0.50 1 456 . 38 SER CB C 63.23 0.50 1 457 . 38 SER N N 115.34 0.25 1 458 . 39 PHE H H 8.81 0.03 1 459 . 39 PHE HA H 4.42 0.03 1 460 . 39 PHE HB2 H 2.61 0.03 1 461 . 39 PHE HB3 H 2.88 0.03 1 462 . 39 PHE HD1 H 6.74 0.03 1 463 . 39 PHE HD2 H 6.74 0.03 1 464 . 39 PHE HE1 H 6.48 0.03 1 465 . 39 PHE HE2 H 6.48 0.03 1 466 . 39 PHE HZ H 6.45 0.03 1 467 . 39 PHE C C 174.51 0.50 1 468 . 39 PHE CA C 57.33 0.50 1 469 . 39 PHE CB C 41.37 0.50 1 470 . 39 PHE CD1 C 132.26 0.50 1 471 . 39 PHE CD2 C 132.26 0.50 1 472 . 39 PHE CE1 C 129.88 0.50 1 473 . 39 PHE CE2 C 129.88 0.50 1 474 . 39 PHE CZ C 127.39 0.50 1 475 . 39 PHE N N 123.64 0.25 1 476 . 40 PHE H H 9.79 0.03 1 477 . 40 PHE HA H 4.71 0.03 1 478 . 40 PHE HB2 H 3.04 0.03 1 479 . 40 PHE HB3 H 2.49 0.03 1 480 . 40 PHE HD1 H 7.24 0.03 1 481 . 40 PHE HD2 H 7.24 0.03 1 482 . 40 PHE HE1 H 6.99 0.03 1 483 . 40 PHE HE2 H 6.99 0.03 1 484 . 40 PHE HZ H 6.96 0.03 1 485 . 40 PHE C C 175.42 0.50 1 486 . 40 PHE CA C 58.19 0.50 1 487 . 40 PHE CB C 40.82 0.50 1 488 . 40 PHE CD1 C 132.44 0.50 1 489 . 40 PHE CD2 C 132.44 0.50 1 490 . 40 PHE CE1 C 130.81 0.50 1 491 . 40 PHE CE2 C 130.81 0.50 1 492 . 40 PHE CZ C 129.88 0.50 1 493 . 40 PHE N N 118.22 0.25 1 494 . 41 CYS H H 9.12 0.03 1 495 . 41 CYS HA H 4.43 0.03 1 496 . 41 CYS HB2 H 1.69 0.03 1 497 . 41 CYS HB3 H 2.85 0.03 1 498 . 41 CYS C C 171.34 0.50 1 499 . 41 CYS CA C 53.04 0.50 1 500 . 41 CYS CB C 43.56 0.50 1 501 . 41 CYS N N 120.67 0.25 1 502 . 42 LYS H H 8.73 0.03 1 503 . 42 LYS HA H 4.62 0.03 1 504 . 42 LYS HB2 H 1.63 0.03 1 505 . 42 LYS HB3 H 1.46 0.03 1 506 . 42 LYS HG2 H 1.15 0.03 2 507 . 42 LYS HG3 H 0.94 0.03 2 508 . 42 LYS HD2 H 1.37 0.03 2 509 . 42 LYS HD3 H 1.27 0.03 2 510 . 42 LYS HE2 H 2.50 0.03 1 511 . 42 LYS HE3 H 2.50 0.03 1 512 . 42 LYS C C 176.38 0.50 1 513 . 42 LYS CA C 55.83 0.50 1 514 . 42 LYS CB C 34.86 0.50 1 515 . 42 LYS CG C 25.60 0.50 1 516 . 42 LYS CD C 29.27 0.50 1 517 . 42 LYS CE C 41.55 0.50 1 518 . 42 LYS N N 120.25 0.25 1 519 . 43 ASN H H 9.52 0.03 1 520 . 43 ASN HA H 5.03 0.03 1 521 . 43 ASN HB2 H 2.70 0.03 1 522 . 43 ASN HB3 H 3.51 0.03 1 523 . 43 ASN HD21 H 7.47 0.03 2 524 . 43 ASN HD22 H 7.12 0.03 2 525 . 43 ASN C C 176.15 0.50 1 526 . 43 ASN CA C 52.84 0.50 1 527 . 43 ASN CB C 38.89 0.50 1 528 . 43 ASN CG C 176.40 0.50 1 529 . 43 ASN N N 125.79 0.25 1 530 . 43 ASN ND2 N 114.06 0.25 1 531 . 44 LYS H H 9.05 0.03 1 532 . 44 LYS HA H 4.05 0.03 1 533 . 44 LYS HB2 H 1.91 0.03 1 534 . 44 LYS HB3 H 1.91 0.03 1 535 . 44 LYS HG2 H 1.53 0.03 2 536 . 44 LYS HG3 H 1.44 0.03 2 537 . 44 LYS HD2 H 1.72 0.03 1 538 . 44 LYS HD3 H 1.72 0.03 1 539 . 44 LYS HE2 H 3.01 0.03 1 540 . 44 LYS HE3 H 3.01 0.03 1 541 . 44 LYS C C 178.11 0.50 1 542 . 44 LYS CA C 59.60 0.50 1 543 . 44 LYS CB C 32.65 0.50 1 544 . 44 LYS CG C 25.06 0.50 1 545 . 44 LYS CD C 29.16 0.50 1 546 . 44 LYS CE C 41.77 0.50 1 547 . 44 LYS N N 127.20 0.25 1 548 . 45 GLU H H 8.44 0.03 1 549 . 45 GLU HA H 4.13 0.03 1 550 . 45 GLU HB2 H 2.18 0.03 2 551 . 45 GLU HB3 H 2.09 0.03 2 552 . 45 GLU HG2 H 2.31 0.03 1 553 . 45 GLU HG3 H 2.31 0.03 1 554 . 45 GLU C C 178.37 0.50 1 555 . 45 GLU CA C 59.40 0.50 1 556 . 45 GLU CB C 29.77 0.50 1 557 . 45 GLU CG C 36.78 0.50 1 558 . 45 GLU N N 119.86 0.25 1 559 . 46 LYS H H 7.78 0.03 1 560 . 46 LYS HA H 4.28 0.03 1 561 . 46 LYS HB2 H 1.99 0.03 1 562 . 46 LYS HB3 H 1.55 0.03 1 563 . 46 LYS HG2 H 1.45 0.03 2 564 . 46 LYS HG3 H 1.33 0.03 2 565 . 46 LYS HE2 H 2.93 0.03 1 566 . 46 LYS HE3 H 2.93 0.03 1 567 . 46 LYS C C 175.42 0.50 1 568 . 46 LYS CA C 55.82 0.50 1 569 . 46 LYS CB C 34.50 0.50 1 570 . 46 LYS CG C 25.36 0.50 1 571 . 46 LYS CE C 41.80 0.50 1 572 . 46 LYS N N 116.80 0.25 1 573 . 47 LYS H H 7.92 0.03 1 574 . 47 LYS HA H 3.79 0.03 1 575 . 47 LYS HB2 H 1.67 0.03 1 576 . 47 LYS HB3 H 1.94 0.03 1 577 . 47 LYS HG2 H 1.18 0.03 1 578 . 47 LYS HG3 H 1.18 0.03 1 579 . 47 LYS HD2 H 1.57 0.03 2 580 . 47 LYS HD3 H 1.49 0.03 2 581 . 47 LYS HE2 H 2.88 0.03 1 582 . 47 LYS HE3 H 2.88 0.03 1 583 . 47 LYS C C 173.87 0.50 1 584 . 47 LYS CA C 56.89 0.50 1 585 . 47 LYS CB C 29.18 0.50 1 586 . 47 LYS CG C 24.93 0.50 1 587 . 47 LYS CD C 29.21 0.50 1 588 . 47 LYS CE C 41.93 0.50 1 589 . 47 LYS N N 118.45 0.25 1 590 . 48 CYS H H 7.92 0.03 1 591 . 48 CYS HA H 5.41 0.03 1 592 . 48 CYS HB2 H 3.40 0.03 1 593 . 48 CYS HB3 H 2.95 0.03 1 594 . 48 CYS C C 171.99 0.50 1 595 . 48 CYS CA C 53.76 0.50 1 596 . 48 CYS CB C 44.13 0.50 1 597 . 48 CYS N N 113.84 0.25 1 598 . 49 SER H H 9.52 0.03 1 599 . 49 SER HA H 5.64 0.03 1 600 . 49 SER HB2 H 3.98 0.03 1 601 . 49 SER HB3 H 3.90 0.03 1 602 . 49 SER C C 172.27 0.50 1 603 . 49 SER CA C 56.63 0.50 1 604 . 49 SER CB C 67.98 0.50 1 605 . 49 SER N N 118.64 0.25 1 606 . 50 TYR H H 8.93 0.03 1 607 . 50 TYR HA H 5.23 0.03 1 608 . 50 TYR HB2 H 3.24 0.03 1 609 . 50 TYR HB3 H 2.88 0.03 1 610 . 50 TYR HD1 H 7.02 0.03 1 611 . 50 TYR HD2 H 7.02 0.03 1 612 . 50 TYR HE1 H 6.70 0.03 1 613 . 50 TYR HE2 H 6.70 0.03 1 614 . 50 TYR C C 172.45 0.50 1 615 . 50 TYR CA C 55.50 0.50 1 616 . 50 TYR CB C 40.58 0.50 1 617 . 50 TYR CD1 C 134.11 0.50 1 618 . 50 TYR CD2 C 134.11 0.50 1 619 . 50 TYR CE1 C 118.05 0.50 1 620 . 50 TYR CE2 C 118.05 0.50 1 621 . 50 TYR N N 121.02 0.25 1 622 . 51 THR H H 8.20 0.03 1 623 . 51 THR HA H 5.55 0.03 1 624 . 51 THR HB H 3.68 0.03 1 625 . 51 THR HG2 H 0.25 0.03 1 626 . 51 THR C C 174.80 0.50 1 627 . 51 THR CA C 58.82 0.50 1 628 . 51 THR CB C 72.24 0.50 1 629 . 51 THR CG2 C 20.56 0.50 1 630 . 51 THR N N 108.72 0.25 1 631 . 52 GLU H H 8.58 0.03 1 632 . 52 GLU HA H 4.62 0.03 1 633 . 52 GLU HB2 H 1.96 0.03 2 634 . 52 GLU HB3 H 1.71 0.03 2 635 . 52 GLU HG2 H 2.48 0.03 2 636 . 52 GLU HG3 H 2.42 0.03 2 637 . 52 GLU C C 175.61 0.50 1 638 . 52 GLU CA C 56.11 0.50 1 639 . 52 GLU CB C 34.68 0.50 1 640 . 52 GLU CG C 37.01 0.50 1 641 . 52 GLU N N 120.47 0.25 1 642 . 53 ASP H H 8.66 0.03 1 643 . 53 ASP HA H 5.41 0.03 1 644 . 53 ASP HB2 H 2.65 0.03 1 645 . 53 ASP HB3 H 2.37 0.03 1 646 . 53 ASP C C 176.10 0.50 1 647 . 53 ASP CA C 54.53 0.50 1 648 . 53 ASP CB C 42.45 0.50 1 649 . 53 ASP N N 124.94 0.25 1 650 . 54 ALA H H 9.23 0.03 1 651 . 54 ALA HA H 4.72 0.03 1 652 . 54 ALA HB H 1.43 0.03 1 653 . 54 ALA C C 174.17 0.50 1 654 . 54 ALA CA C 51.64 0.50 1 655 . 54 ALA CB C 23.77 0.50 1 656 . 54 ALA N N 122.91 0.25 1 657 . 55 GLN H H 8.65 0.03 1 658 . 55 GLN HA H 5.22 0.03 1 659 . 55 GLN HB2 H 1.61 0.03 1 660 . 55 GLN HB3 H 1.93 0.03 1 661 . 55 GLN HG2 H 1.96 0.03 1 662 . 55 GLN HG3 H 1.96 0.03 1 663 . 55 GLN HE21 H 7.49 0.03 2 664 . 55 GLN HE22 H 6.87 0.03 2 665 . 55 GLN C C 174.01 0.50 1 666 . 55 GLN CA C 53.50 0.50 1 667 . 55 GLN CB C 33.16 0.50 1 668 . 55 GLN CG C 33.19 0.50 1 669 . 55 GLN CD C 179.91 0.50 1 670 . 55 GLN N N 121.29 0.25 1 671 . 55 GLN NE2 N 112.69 0.25 1 672 . 56 CYS H H 8.48 0.03 1 673 . 56 CYS HA H 4.63 0.03 1 674 . 56 CYS HB2 H 2.66 0.03 1 675 . 56 CYS HB3 H 3.02 0.03 1 676 . 56 CYS C C 173.03 0.50 1 677 . 56 CYS CA C 55.10 0.50 1 678 . 56 CYS CB C 39.12 0.50 1 679 . 56 CYS N N 123.88 0.25 1 680 . 57 ILE H H 9.05 0.03 1 681 . 57 ILE HA H 4.53 0.03 1 682 . 57 ILE HB H 1.92 0.03 1 683 . 57 ILE HG12 H 0.89 0.03 1 684 . 57 ILE HG13 H 1.37 0.03 1 685 . 57 ILE HG2 H 0.95 0.03 1 686 . 57 ILE HD1 H 0.71 0.03 1 687 . 57 ILE C C 176.33 0.50 1 688 . 57 ILE CA C 59.33 0.50 1 689 . 57 ILE CB C 39.06 0.50 1 690 . 57 ILE CG1 C 26.36 0.50 1 691 . 57 ILE CG2 C 17.53 0.50 1 692 . 57 ILE CD1 C 11.45 0.50 1 693 . 57 ILE N N 133.80 0.25 1 694 . 58 ASP H H 12.40 0.03 1 695 . 58 ASP HA H 4.54 0.03 1 696 . 58 ASP HB2 H 2.36 0.03 1 697 . 58 ASP HB3 H 3.04 0.03 1 698 . 58 ASP C C 176.77 0.50 1 699 . 58 ASP CA C 54.68 0.50 1 700 . 58 ASP CB C 40.76 0.50 1 701 . 58 ASP N N 135.53 0.25 1 702 . 59 GLY H H 6.99 0.03 1 703 . 59 GLY HA2 H 4.13 0.03 2 704 . 59 GLY HA3 H 3.75 0.03 2 705 . 59 GLY C C 174.76 0.50 1 706 . 59 GLY CA C 46.11 0.50 1 707 . 59 GLY N N 104.34 0.25 1 708 . 60 THR H H 8.14 0.03 1 709 . 60 THR HA H 4.61 0.03 1 710 . 60 THR HB H 4.06 0.03 1 711 . 60 THR HG2 H 1.17 0.03 1 712 . 60 THR C C 172.11 0.50 1 713 . 60 THR CA C 62.00 0.50 1 714 . 60 THR CB C 71.37 0.50 1 715 . 60 THR CG2 C 21.60 0.50 1 716 . 60 THR N N 120.13 0.25 1 717 . 61 ILE H H 8.54 0.03 1 718 . 61 ILE HA H 4.67 0.03 1 719 . 61 ILE HB H 1.62 0.03 1 720 . 61 ILE HG12 H 0.58 0.03 1 721 . 61 ILE HG13 H 1.35 0.03 1 722 . 61 ILE HG2 H 0.87 0.03 1 723 . 61 ILE HD1 H 0.59 0.03 1 724 . 61 ILE C C 172.21 0.50 1 725 . 61 ILE CA C 59.31 0.50 1 726 . 61 ILE CB C 41.51 0.50 1 727 . 61 ILE CG1 C 29.31 0.50 1 728 . 61 ILE CG2 C 15.61 0.50 1 729 . 61 ILE CD1 C 14.95 0.50 1 730 . 61 ILE N N 126.16 0.25 1 731 . 62 GLU H H 8.43 0.03 1 732 . 62 GLU HA H 4.45 0.03 1 733 . 62 GLU HB2 H 1.89 0.03 2 734 . 62 GLU HB3 H 1.79 0.03 2 735 . 62 GLU HG2 H 2.16 0.03 2 736 . 62 GLU HG3 H 2.08 0.03 2 737 . 62 GLU C C 175.55 0.50 1 738 . 62 GLU CA C 54.44 0.50 1 739 . 62 GLU CB C 30.36 0.50 1 740 . 62 GLU CG C 35.83 0.50 1 741 . 62 GLU N N 128.95 0.25 1 742 . 63 VAL H H 8.42 0.03 1 743 . 63 VAL HA H 3.47 0.03 1 744 . 63 VAL HB H 1.60 0.03 1 745 . 63 VAL HG1 H 0.64 0.03 2 746 . 63 VAL HG2 H 0.28 0.03 2 747 . 63 VAL CA C 60.53 0.50 1 748 . 63 VAL CB C 31.96 0.50 1 749 . 63 VAL CG1 C 21.87 0.50 2 750 . 63 VAL CG2 C 20.47 0.50 2 751 . 63 VAL N N 127.27 0.25 1 752 . 64 PRO HA H 4.32 0.03 1 753 . 64 PRO HB2 H 2.58 0.03 2 754 . 64 PRO HB3 H 1.82 0.03 2 755 . 64 PRO HG2 H 1.90 0.03 2 756 . 64 PRO HG3 H 1.82 0.03 2 757 . 64 PRO HD2 H 3.44 0.03 2 758 . 64 PRO HD3 H 2.58 0.03 2 759 . 64 PRO C C 177.98 0.50 1 760 . 64 PRO CA C 63.33 0.50 1 761 . 64 PRO CB C 32.73 0.50 1 762 . 64 PRO CG C 27.99 0.50 1 763 . 64 PRO CD C 51.33 0.50 1 764 . 65 LYS H H 8.87 0.03 1 765 . 65 LYS HA H 3.91 0.03 1 766 . 65 LYS HB2 H 1.85 0.03 1 767 . 65 LYS HB3 H 1.85 0.03 1 768 . 65 LYS HG2 H 1.57 0.03 2 769 . 65 LYS HG3 H 1.50 0.03 2 770 . 65 LYS HD2 H 1.71 0.03 1 771 . 65 LYS HD3 H 1.71 0.03 1 772 . 65 LYS HE2 H 3.01 0.03 1 773 . 65 LYS HE3 H 3.01 0.03 1 774 . 65 LYS C C 178.60 0.50 1 775 . 65 LYS CA C 59.39 0.50 1 776 . 65 LYS CB C 32.08 0.50 1 777 . 65 LYS CG C 25.14 0.50 1 778 . 65 LYS CD C 29.09 0.50 1 779 . 65 LYS CE C 41.81 0.50 1 780 . 65 LYS N N 126.41 0.25 1 781 . 66 CYS H H 8.70 0.03 1 782 . 66 CYS HA H 4.44 0.03 1 783 . 66 CYS HB2 H 3.54 0.03 2 784 . 66 CYS HB3 H 3.07 0.03 2 785 . 66 CYS C C 174.80 0.50 1 786 . 66 CYS CA C 56.61 0.50 1 787 . 66 CYS CB C 37.29 0.50 1 788 . 66 CYS N N 115.00 0.25 1 789 . 67 PHE H H 7.67 0.03 1 790 . 67 PHE HA H 4.29 0.03 1 791 . 67 PHE HB2 H 2.79 0.03 2 792 . 67 PHE HB3 H 2.61 0.03 2 793 . 67 PHE HD1 H 7.21 0.03 1 794 . 67 PHE HD2 H 7.21 0.03 1 795 . 67 PHE HE1 H 7.55 0.03 1 796 . 67 PHE HE2 H 7.55 0.03 1 797 . 67 PHE HZ H 7.53 0.03 1 798 . 67 PHE CA C 60.08 0.50 1 799 . 67 PHE CB C 39.66 0.50 1 800 . 67 PHE CD1 C 132.20 0.50 1 801 . 67 PHE CD2 C 132.20 0.50 1 802 . 67 PHE CE1 C 132.22 0.50 1 803 . 67 PHE CE2 C 132.22 0.50 1 804 . 67 PHE CZ C 129.75 0.50 1 805 . 67 PHE N N 125.28 0.25 1 806 . 68 LYS H H 7.56 0.03 1 807 . 68 LYS HA H 4.03 0.03 1 808 . 68 LYS HB2 H 1.64 0.03 1 809 . 68 LYS HB3 H 1.64 0.03 1 810 . 68 LYS HG2 H 1.32 0.03 1 811 . 68 LYS HG3 H 1.32 0.03 1 812 . 68 LYS HE2 H 2.92 0.03 1 813 . 68 LYS HE3 H 2.92 0.03 1 814 . 68 LYS CA C 56.03 0.50 1 815 . 68 LYS CB C 33.52 0.50 1 816 . 68 LYS CG C 24.69 0.50 1 817 . 68 LYS CE C 41.74 0.50 1 818 . 68 LYS N N 124.43 0.25 1 819 . 69 GLU H H 8.07 0.03 1 820 . 69 GLU HA H 4.00 0.03 1 821 . 69 GLU HB2 H 1.94 0.03 1 822 . 69 GLU HB3 H 1.94 0.03 1 823 . 69 GLU HG2 H 2.38 0.03 2 824 . 69 GLU HG3 H 2.21 0.03 2 825 . 69 GLU C C 176.72 0.50 1 826 . 69 GLU CA C 57.23 0.50 1 827 . 69 GLU CB C 30.32 0.50 1 828 . 69 GLU CG C 36.55 0.50 1 829 . 69 GLU N N 122.23 0.25 1 830 . 70 HIS H H 8.25 0.03 1 831 . 70 HIS HA H 4.51 0.03 1 832 . 70 HIS HB2 H 3.03 0.03 1 833 . 70 HIS HB3 H 3.03 0.03 1 834 . 70 HIS HD2 H 6.96 0.03 1 835 . 70 HIS HE1 H 7.84 0.03 1 836 . 70 HIS CA C 56.66 0.50 1 837 . 70 HIS CB C 30.46 0.50 1 838 . 70 HIS CD2 C 119.98 0.50 1 839 . 70 HIS CE1 C 138.00 0.50 1 840 . 70 HIS N N 121.36 0.25 1 841 . 71 SER H H 8.10 0.03 1 842 . 71 SER HA H 4.29 0.03 1 843 . 71 SER HB2 H 3.80 0.03 2 844 . 71 SER HB3 H 3.62 0.03 2 845 . 71 SER CA C 58.81 0.50 1 846 . 71 SER CB C 63.84 0.50 1 847 . 71 SER N N 117.52 0.25 1 848 . 72 SER H H 8.39 0.03 1 849 . 72 SER HA H 4.36 0.03 1 850 . 72 SER HB2 H 3.92 0.03 2 851 . 72 SER HB3 H 3.87 0.03 2 852 . 72 SER C C 174.58 0.50 1 853 . 72 SER CA C 59.21 0.50 1 854 . 72 SER CB C 63.57 0.50 1 855 . 72 SER N N 118.91 0.25 1 856 . 73 LEU H H 7.92 0.03 1 857 . 73 LEU HA H 4.27 0.03 1 858 . 73 LEU HB2 H 1.59 0.03 1 859 . 73 LEU HB3 H 1.50 0.03 1 860 . 73 LEU HG H 1.60 0.03 1 861 . 73 LEU HD1 H 0.88 0.03 2 862 . 73 LEU HD2 H 0.84 0.03 2 863 . 73 LEU C C 177.54 0.50 1 864 . 73 LEU CA C 55.42 0.50 1 865 . 73 LEU CB C 42.07 0.50 1 866 . 73 LEU CG C 27.00 0.50 1 867 . 73 LEU CD1 C 25.14 0.50 2 868 . 73 LEU CD2 C 23.19 0.50 2 869 . 73 LEU N N 123.28 0.25 1 870 . 74 ALA H H 7.93 0.03 1 871 . 74 ALA HA H 3.97 0.03 1 872 . 74 ALA HB H 1.05 0.03 1 873 . 74 ALA C C 177.92 0.50 1 874 . 74 ALA CA C 52.87 0.50 1 875 . 74 ALA CB C 18.57 0.50 1 876 . 74 ALA N N 124.00 0.25 1 877 . 75 PHE H H 7.73 0.03 1 878 . 75 PHE HA H 4.38 0.03 1 879 . 75 PHE HB2 H 3.07 0.03 2 880 . 75 PHE HB3 H 2.97 0.03 2 881 . 75 PHE HD1 H 7.11 0.03 1 882 . 75 PHE HD2 H 7.11 0.03 1 883 . 75 PHE HE1 H 7.30 0.03 0 884 . 75 PHE HE2 H 7.30 0.03 1 885 . 75 PHE HZ H 7.29 0.03 1 886 . 75 PHE C C 175.32 0.50 1 887 . 75 PHE CA C 58.33 0.50 1 888 . 75 PHE CB C 38.94 0.50 1 889 . 75 PHE CD1 C 131.94 0.50 1 890 . 75 PHE CD2 C 131.94 0.50 1 891 . 75 PHE CE1 C 131.70 0.50 1 892 . 75 PHE CE2 C 131.70 0.50 1 893 . 75 PHE CZ C 130.09 0.50 1 894 . 75 PHE N N 117.71 0.25 1 895 . 76 TRP H H 7.54 0.03 1 896 . 76 TRP HA H 4.60 0.03 1 897 . 76 TRP HB2 H 3.18 0.03 2 898 . 76 TRP HB3 H 3.11 0.03 2 899 . 76 TRP HD1 H 7.12 0.03 1 900 . 76 TRP HE1 H 10.22 0.03 1 901 . 76 TRP HE3 H 7.34 0.03 1 902 . 76 TRP HZ3 H 7.04 0.03 1 903 . 76 TRP HH2 H 7.15 0.03 1 904 . 76 TRP HZ2 H 7.43 0.03 1 905 . 76 TRP CA C 56.64 0.50 1 906 . 76 TRP CB C 28.92 0.50 1 907 . 76 TRP CD1 C 126.63 0.50 1 908 . 76 TRP CE3 C 120.87 0.50 1 909 . 76 TRP CZ3 C 122.18 0.50 1 910 . 76 TRP CH2 C 124.68 0.50 1 911 . 76 TRP CZ2 C 114.73 0.50 1 912 . 76 TRP N N 120.87 0.25 1 913 . 76 TRP NE1 N 130.69 0.25 1 914 . 77 LYS H H 7.87 0.03 1 915 . 77 LYS HA H 4.14 0.03 1 916 . 77 LYS HB2 H 1.65 0.03 2 917 . 77 LYS HB3 H 1.56 0.03 2 918 . 77 LYS HG2 H 1.14 0.03 1 919 . 77 LYS HG3 H 1.14 0.03 1 920 . 77 LYS HD2 H 1.54 0.03 1 921 . 77 LYS HD3 H 1.54 0.03 1 922 . 77 LYS HE2 H 2.87 0.03 1 923 . 77 LYS HE3 H 2.87 0.03 1 924 . 77 LYS C C 176.45 0.50 1 925 . 77 LYS CA C 56.77 0.50 1 926 . 77 LYS CB C 32.94 0.50 1 927 . 77 LYS CG C 24.84 0.50 1 928 . 77 LYS CD C 28.87 0.50 1 929 . 77 LYS CE C 41.78 0.50 1 930 . 77 LYS N N 122.81 0.25 1 931 . 78 THR H H 7.79 0.03 1 932 . 78 THR HA H 4.08 0.03 1 933 . 78 THR HB H 3.84 0.03 1 934 . 78 THR HG2 H 1.15 0.03 1 935 . 78 THR C C 173.67 0.50 1 936 . 78 THR CA C 62.13 0.50 1 937 . 78 THR CB C 70.05 0.50 1 938 . 78 THR CG2 C 21.93 0.50 1 939 . 78 THR N N 115.44 0.25 1 940 . 79 ASP H H 8.78 0.03 1 941 . 79 ASP HA H 4.41 0.03 1 942 . 79 ASP HB2 H 2.58 0.03 1 943 . 79 ASP HB3 H 2.58 0.03 1 944 . 79 ASP C C 177.21 0.50 1 945 . 79 ASP CA C 54.62 0.50 1 946 . 79 ASP CB C 42.29 0.50 1 947 . 79 ASP N N 126.12 0.25 1 948 . 80 ALA H H 8.68 0.03 1 949 . 80 ALA HA H 3.79 0.03 1 950 . 80 ALA HB H 1.20 0.03 1 951 . 80 ALA C C 177.73 0.50 1 952 . 80 ALA CA C 54.69 0.50 1 953 . 80 ALA CB C 18.71 0.50 1 954 . 80 ALA N N 126.29 0.25 1 955 . 81 SER H H 8.17 0.03 1 956 . 81 SER HA H 3.12 0.03 1 957 . 81 SER HB2 H 3.33 0.03 2 958 . 81 SER HB3 H 3.17 0.03 2 959 . 81 SER C C 174.56 0.50 1 960 . 81 SER CA C 60.08 0.50 1 961 . 81 SER CB C 62.75 0.50 1 962 . 81 SER N N 111.10 0.25 1 963 . 82 ASP H H 7.88 0.03 1 964 . 82 ASP HA H 4.69 0.03 1 965 . 82 ASP HB2 H 2.51 0.03 1 966 . 82 ASP HB3 H 2.77 0.03 1 967 . 82 ASP C C 175.56 0.50 1 968 . 82 ASP CA C 54.44 0.50 1 969 . 82 ASP CB C 41.76 0.50 1 970 . 82 ASP N N 122.29 0.25 1 971 . 83 VAL H H 7.18 0.03 1 972 . 83 VAL HA H 4.08 0.03 1 973 . 83 VAL HB H 2.04 0.03 1 974 . 83 VAL HG1 H 0.95 0.03 2 975 . 83 VAL HG2 H 0.81 0.03 2 976 . 83 VAL C C 175.53 0.50 1 977 . 83 VAL CA C 61.54 0.50 1 978 . 83 VAL CB C 33.21 0.50 1 979 . 83 VAL CG1 C 21.64 0.50 2 980 . 83 VAL CG2 C 21.84 0.50 2 981 . 83 VAL N N 121.16 0.25 1 982 . 84 LYS H H 8.59 0.03 1 983 . 84 LYS HA H 4.48 0.03 1 984 . 84 LYS HB2 H 1.91 0.03 1 985 . 84 LYS HB3 H 1.91 0.03 1 986 . 84 LYS HG2 H 1.61 0.03 2 987 . 84 LYS HG3 H 1.51 0.03 2 988 . 84 LYS HD2 H 1.73 0.03 1 989 . 84 LYS HD3 H 1.73 0.03 1 990 . 84 LYS HE2 H 3.03 0.03 1 991 . 84 LYS HE3 H 3.03 0.03 1 992 . 84 LYS CA C 55.10 0.50 1 993 . 84 LYS CB C 32.19 0.50 1 994 . 84 LYS CG C 24.08 0.50 1 995 . 84 LYS CD C 29.28 0.50 1 996 . 84 LYS CE C 41.92 0.50 1 997 . 84 LYS N N 130.34 0.25 1 998 . 85 PRO HA H 5.17 0.03 1 999 . 85 PRO HB2 H 2.47 0.03 2 1000 . 85 PRO HB3 H 2.03 0.03 2 1001 . 85 PRO HG2 H 2.14 0.03 2 1002 . 85 PRO HG3 H 2.04 0.03 2 1003 . 85 PRO HD2 H 3.87 0.03 2 1004 . 85 PRO HD3 H 3.67 0.03 2 1005 . 85 PRO C C 178.61 0.50 1 1006 . 85 PRO CA C 62.73 0.50 1 1007 . 85 PRO CB C 32.21 0.50 1 1008 . 85 PRO CG C 27.93 0.50 1 1009 . 85 PRO CD C 51.01 0.50 1 1010 . 86 CYS H H 9.74 0.03 1 1011 . 86 CYS HA H 4.41 0.03 1 1012 . 86 CYS HB2 H 2.79 0.03 1 1013 . 86 CYS HB3 H 3.29 0.03 1 1014 . 86 CYS CA C 56.67 0.50 1 1015 . 86 CYS CB C 40.75 0.50 1 stop_ save_