data_16771 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Integrin beta3 subunit in a disulfide linked alphaIIb-beta3 cytosolic domain ; _BMRB_accession_number 16771 _BMRB_flat_file_name bmr16771.str _Entry_type new _Submission_date 2010-03-10 _Accession_date 2010-03-10 _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 Metcalf Douglas G. . 2 Kielec Joseph M. . 3 Valentine Kathleen G. . 4 Wand 'A Joshua' . . 5 Bennett Joel S. . 6 William DeGrado F. . 7 Moore David T. . 8 Molnar Kathleen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 323 "13C chemical shifts" 231 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-05-19 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21156831 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Metcalf Douglas G. . 2 Moore David T. . 3 Wu Yibing . . 4 Kielec Joseph M. . 5 Molnar Kathleen . . 6 Valentine Kathleen G. . 7 Wand 'A. Joshua' . . 8 Bennett Joel S. . 9 DeGrado William F. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 107 _Journal_issue 52 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 22481 _Page_last 22486 _Year 2010 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name alphaIIb_beta3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label alphaIIb $alphaIIb beta3 $beta3 stop_ _System_molecular_weight 11694.1 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_alphaIIb _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common alphaIIb _Molecular_mass 2994.3 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 25 _Mol_residue_sequence ; SPECWKVGFFKRNRPPLEED DEEGE ; loop_ _Residue_seq_code _Residue_label 1 SER 2 PRO 3 GLU 4 CYS 5 TRP 6 LYS 7 VAL 8 GLY 9 PHE 10 PHE 11 LYS 12 ARG 13 ASN 14 ARG 15 PRO 16 PRO 17 LEU 18 GLU 19 GLU 20 ASP 21 ASP 22 GLU 23 GLU 24 GLY 25 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-24 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 1DPK "Solution Structure Of The Cytoplasmic Domain Of The Integrin Alpha-Iib Subunit" 80.00 20 100.00 100.00 9.23e-04 PDB 1M8O "Platelet Integrin Alfaiib-Beta3 Cytoplasmic Domain" 80.00 20 100.00 100.00 9.23e-04 PDB 1S4W "Nmr Structure Of The Cytoplasmic Domain Of Integrin Aiib In Dpc Micelles" 80.00 20 100.00 100.00 9.23e-04 PDB 2MTP "The Structure Of Filamin Repeat 21 Bound To Integrin" 84.00 21 100.00 100.00 5.66e-05 DBJ BAG37735 "unnamed protein product [Homo sapiens]" 84.00 1039 100.00 100.00 1.96e-05 DBJ BAI46167 "integrin, alpha 2b [synthetic construct]" 84.00 1039 100.00 100.00 1.92e-05 EMBL CAA29987 "platelet glycoprotein IIb (648 AA) [Homo sapiens]" 84.00 648 100.00 100.00 2.40e-05 GB AAA52597 "glycoprotein IIb, partial [Homo sapiens]" 84.00 172 100.00 100.00 3.48e-05 GB AAA53150 "platelet Glycoprotein IIb (GPIIb), partial [Homo sapiens]" 84.00 1039 100.00 100.00 1.81e-05 GB AAA60114 "platelet membrane glycoprotein IIb [Homo sapiens]" 84.00 1039 100.00 100.00 1.90e-05 GB AAA65936 "glycoprotein IIb, partial [Papio cynocephalus]" 84.00 604 100.00 100.00 2.58e-05 GB AAI17444 "Integrin, alpha 2b (platelet glycoprotein IIb of IIb/IIIa complex, antigen CD41) [Homo sapiens]" 84.00 1039 100.00 100.00 1.92e-05 REF NP_000410 "integrin alpha-IIb preproprotein [Homo sapiens]" 84.00 1039 100.00 100.00 1.92e-05 REF NP_001014929 "integrin alpha-IIb [Bos taurus]" 52.00 937 100.00 100.00 4.36e+00 REF NP_001075262 "integrin alpha-IIb precursor [Equus caballus]" 52.00 1036 100.00 100.00 5.32e+00 REF XP_001114526 "PREDICTED: integrin alpha-IIb [Macaca mulatta]" 84.00 1039 100.00 100.00 1.76e-05 REF XP_001150497 "PREDICTED: integrin alpha-IIb isoform X2 [Pan troglodytes]" 84.00 1108 100.00 100.00 1.60e-05 SP P08514 "RecName: Full=Integrin alpha-IIb; AltName: Full=GPalpha IIb; Short=GPIIb; AltName: Full=Platelet membrane glycoprotein IIb; Alt" 84.00 1039 100.00 100.00 1.92e-05 SP P53711 "RecName: Full=Integrin alpha-IIb; AltName: Full=GPalpha IIb; Short=GPIIb; AltName: Full=Platelet membrane glycoprotein IIb; Alt" 84.00 604 100.00 100.00 2.58e-05 TPG DAA18359 "TPA: integrin alpha 2b [Bos taurus]" 52.00 937 100.00 100.00 4.61e+00 stop_ save_ save_beta3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta3 _Molecular_mass 8699.9 _Mol_thiol_state 'all disulfide bound' _Details . _Residue_count 75 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MSPECLIWKLLITIHDRKEF AKFEEERARAKWDTANNPLY KEATSTFTNITYRGT ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 688 MET 2 689 GLY 3 690 SER 4 691 SER 5 692 HIS 6 693 HIS 7 694 HIS 8 695 HIS 9 696 HIS 10 697 HIS 11 698 SER 12 699 SER 13 700 GLY 14 701 LEU 15 702 VAL 16 703 PRO 17 704 ARG 18 705 GLY 19 706 SER 20 707 HIS 21 708 MET 22 709 SER 23 710 PRO 24 711 GLU 25 712 CYS 26 713 LEU 27 714 ILE 28 715 TRP 29 716 LYS 30 717 LEU 31 718 LEU 32 719 ILE 33 720 THR 34 721 ILE 35 722 HIS 36 723 ASP 37 724 ARG 38 725 LYS 39 726 GLU 40 727 PHE 41 728 ALA 42 729 LYS 43 730 PHE 44 731 GLU 45 732 GLU 46 733 GLU 47 734 ARG 48 735 ALA 49 736 ARG 50 737 ALA 51 738 LYS 52 739 TRP 53 740 ASP 54 741 THR 55 742 ALA 56 743 ASN 57 744 ASN 58 745 PRO 59 746 LEU 60 747 TYR 61 748 LYS 62 749 GLU 63 750 ALA 64 751 THR 65 752 SER 66 753 THR 67 754 PHE 68 755 THR 69 756 ASN 70 757 ILE 71 758 THR 72 759 TYR 73 760 ARG 74 761 GLY 75 762 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 15552 beta3_integrin 62.67 49 100.00 100.00 1.06e-24 BMRB 16496 B3TMCD 68.00 79 98.04 98.04 2.74e-28 PDB 1M8O "Platelet Integrin Alfaiib-Beta3 Cytoplasmic Domain" 62.67 47 100.00 100.00 7.49e-25 PDB 2KNC "Platelet Integrin Alfaiib-Beta3 Transmembrane-Cytoplasmic Heterocomplex" 68.00 79 98.04 98.04 2.74e-28 PDB 2KV9 "Integrin Beta3 Subunit In A Disulfide Linked Alphaiib-Beta3 Cytosolic Domain" 100.00 75 100.00 100.00 6.50e-48 DBJ BAE34283 "unnamed protein product [Mus musculus]" 66.67 787 100.00 100.00 2.19e-26 DBJ BAJ17755 "integrin, beta 3 [synthetic construct]" 66.67 788 100.00 100.00 2.19e-26 EMBL CAD29521 "integrin beta3 subunit [Rattus norvegicus]" 66.67 787 100.00 100.00 2.19e-26 GB AAA35927 "plate glycoprotein IIIa (GPIIIa) [Homo sapiens]" 66.67 788 100.00 100.00 2.19e-26 GB AAA52589 "glycoprotein IIIa precursor [Homo sapiens]" 66.67 788 100.00 100.00 2.19e-26 GB AAA52600 "platelet glycoprotein IIIa, partial [Homo sapiens]" 66.67 761 100.00 100.00 2.06e-26 GB AAA60122 "glycoprotein IIIa [Homo sapiens]" 66.67 788 100.00 100.00 2.19e-26 GB AAB27096 "beta 3 integrin, GPIIIA [rats, Peptide Partial, 723 aa]" 66.67 723 100.00 100.00 1.87e-26 REF NP_000203 "integrin beta-3 precursor [Homo sapiens]" 66.67 788 100.00 100.00 2.19e-26 REF NP_001003162 "integrin beta-3 precursor [Canis lupus familiaris]" 66.67 784 100.00 100.00 2.18e-26 REF NP_001075271 "integrin beta-3 precursor [Equus caballus]" 66.67 784 100.00 100.00 2.18e-26 REF NP_001075535 "integrin beta-3 precursor [Oryctolagus cuniculus]" 66.67 788 100.00 100.00 2.19e-26 REF NP_001193419 "integrin beta-3 precursor [Bos taurus]" 66.67 784 100.00 100.00 2.18e-26 SP O54890 "RecName: Full=Integrin beta-3; AltName: Full=Platelet membrane glycoprotein IIIa; Short=GPIIIa; AltName: CD_antigen=CD61; Flags" 66.67 787 100.00 100.00 2.19e-26 SP P05106 "RecName: Full=Integrin beta-3; AltName: Full=Platelet membrane glycoprotein IIIa; Short=GPIIIa; AltName: CD_antigen=CD61; Flags" 66.67 788 100.00 100.00 2.19e-26 TPG DAA18403 "TPA: integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61) [Bos taurus]" 66.67 784 100.00 100.00 2.18e-26 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide alphaIIb 4 CYS SG beta3 25 CYS SG stop_ loop_ _Deleted_atom_mol_system_component_name _Deleted_atom_residue_seq_code _Deleted_atom_residue_label _Deleted_atom_name alphaIIb 4 CYS HG beta3 25 CYS HG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $alphaIIb . . . . . . 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 _Details $alphaIIb 'recombinant technology' . Escherichia coli BL21 pET-16b 'The alphaIIb subunit was expressed in the pET-16b vector as a C-terminal fusion with the designed protein alpha3D, a small, highly stable peptide that expresses well in E. coli and is unrelated to integrin alphaIIb. The alphaIIb fragment was subsequently cleaved from the fusion protein using thrombin.' $beta3 'recombinant technology' . Escherichia coli BL21 pET-15b 'The beta3 subunit was expressed as a C-terminal fusion to the pET-15b histidine tag.' 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 'sodium phosphate' 5 mM 'natural abundance' DPC 100 mM '[U-99% 2H]' 'sodium azide' 0.02 % 'natural abundance' TFA 25 mM 'natural abundance' $beta3 1 mM '[U-99% 13C; U-99% 15N]' $alphaIIb 1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '10% 13C used to distinguish pro-chiral methyls in valine and leucine side chains.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 5 mM 'natural abundance' DPC 100 mM '[U-99% 2H]' 'sodium azide' 0.02 % 'natural abundance' TFA 25 mM 'natural abundance' $beta3 1 mM '[U-10% 13C; U-99% 15N]' $alphaIIb 1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task 'structure solution' refinement stop_ _Details . save_ save_Felix _Saveframe_category software _Name Felix _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_4D_(13C)HSQC-NOESY-(13C)HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '4D (13C)HSQC-NOESY-(13C)HSQC' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 310 . K pH 6.0 . pH pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 . 'separate tube (no insert) similar to the experimental sample tube' . 1.0 DSS C 13 'methyl protons' ppm 0.00 na indirect . 'separate tube (no insert) similar to the experimental sample tube' . 0.25 DSS N 15 'methyl protons' ppm 0.00 na indirect . 'separate tube (no insert) similar to the experimental sample tube' . 0.1 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '3D HNCO' '3D HNCACB' '3D HCCH-TOCSY' '3D 1H-15N NOESY' '3D 1H-15N TOCSY' '3D 1H-13C NOESY' '2D 1H-15N HSQC' '2D 1H-13C HSQC' '4D (13C)HSQC-NOESY-(13C)HSQC' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name beta3 _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 1 713 26 LEU H H 8.2 . 1 2 713 26 LEU HA H 4.12 . 1 3 713 26 LEU HB2 H 1.86 . 2 4 713 26 LEU HB3 H 1.68 . 2 5 713 26 LEU HD1 H 0.92 . 1 6 713 26 LEU HD2 H 0.91 . 1 7 713 26 LEU HG H 1.7 . 1 8 713 26 LEU C C 173.7 . 1 9 713 26 LEU CA C 58.6 . 1 10 713 26 LEU CB C 42.14 . 1 11 713 26 LEU CD1 C 25.14 . 1 12 713 26 LEU CD2 C 24.67 . 1 13 713 26 LEU CG C 27.46 . 1 14 713 26 LEU N N 122.7 . 1 15 714 27 ILE H H 8.2 . 1 16 714 27 ILE HA H 3.68 . 1 17 714 27 ILE HB H 1.95 . 1 18 714 27 ILE HD1 H 0.82 . 1 19 714 27 ILE HG12 H 1.68 . 2 20 714 27 ILE HG13 H 1.17 . 2 21 714 27 ILE HG2 H 0.86 . 1 22 714 27 ILE C C 174.8 . 1 23 714 27 ILE CA C 64.7 . 1 24 714 27 ILE CB C 37.46 . 1 25 714 27 ILE CD1 C 12.99 . 1 26 714 27 ILE CG1 C 29.5 . 1 27 714 27 ILE CG2 C 17.95 . 1 28 714 27 ILE N N 117.4 . 1 29 715 28 TRP H H 7.84 . 1 30 715 28 TRP HA H 4.36 . 1 31 715 28 TRP HB2 H 3.46 . 2 32 715 28 TRP HB3 H 3.31 . 2 33 715 28 TRP HD1 H 7.11 . 1 34 715 28 TRP HE3 H 7.33 . 1 35 715 28 TRP HZ3 H 6.82 . 1 36 715 28 TRP C C 175 . 1 37 715 28 TRP CA C 60.6 . 1 38 715 28 TRP CB C 29.86 . 1 39 715 28 TRP CD1 C 126.9 . 1 40 715 28 TRP CE3 C 120.8 . 1 41 715 28 TRP CZ3 C 121.2 . 1 42 715 28 TRP N N 120.2 . 1 43 716 29 LYS H H 8.06 . 1 44 716 29 LYS HA H 3.81 . 1 45 716 29 LYS HB2 H 1.99 . 2 46 716 29 LYS HB3 H 1.9 . 2 47 716 29 LYS HD2 H 1.64 . 1 48 716 29 LYS HD3 H 1.64 . 1 49 716 29 LYS HE2 H 2.87 . 1 50 716 29 LYS HE3 H 2.87 . 1 51 716 29 LYS HG2 H 1.51 . 2 52 716 29 LYS HG3 H 1.4 . 2 53 716 29 LYS C C 175.9 . 1 54 716 29 LYS CA C 59.3 . 1 55 716 29 LYS CB C 32.44 . 1 56 716 29 LYS CD C 29.41 . 1 57 716 29 LYS CE C 42.3 . 1 58 716 29 LYS CG C 25.63 . 1 59 716 29 LYS N N 116.4 . 1 60 717 30 LEU H H 8.19 . 1 61 717 30 LEU HA H 3.97 . 1 62 717 30 LEU HB2 H 1.88 . 2 63 717 30 LEU HB3 H 1.74 . 2 64 717 30 LEU HD1 H 0.86 . 1 65 717 30 LEU HD2 H 0.83 . 1 66 717 30 LEU HG H 1.68 . 1 67 717 30 LEU C C 174.1 . 1 68 717 30 LEU CA C 58.59 . 1 69 717 30 LEU CB C 41.87 . 1 70 717 30 LEU CD1 C 24.59 . 1 71 717 30 LEU CD2 C 24.92 . 1 72 717 30 LEU CG C 27.27 . 1 73 717 30 LEU N N 121.5 . 1 74 718 31 LEU H H 8.18 . 1 75 718 31 LEU HA H 3.88 . 1 76 718 31 LEU HB2 H 1.81 . 2 77 718 31 LEU HB3 H 1.29 . 2 78 718 31 LEU HD1 H 0.79 . 1 79 718 31 LEU HD2 H 0.74 . 1 80 718 31 LEU HG H 1.86 . 1 81 718 31 LEU C C 172.9 . 1 82 718 31 LEU CA C 58.49 . 1 83 718 31 LEU CB C 41.37 . 1 84 718 31 LEU CD1 C 25.89 . 1 85 718 31 LEU CD2 C 23.12 . 1 86 718 31 LEU CG C 26.97 . 1 87 718 31 LEU N N 118.9 . 1 88 719 32 ILE H H 8.12 . 1 89 719 32 ILE HA H 3.61 . 1 90 719 32 ILE HB H 1.67 . 1 91 719 32 ILE HD1 H 0.5 . 1 92 719 32 ILE HG12 H 1.16 . 2 93 719 32 ILE HG13 H 0.92 . 2 94 719 32 ILE HG2 H 0.66 . 1 95 719 32 ILE C C 174 . 1 96 719 32 ILE CA C 64.05 . 1 97 719 32 ILE CB C 37.41 . 1 98 719 32 ILE CD1 C 12.84 . 1 99 719 32 ILE CG1 C 28.14 . 1 100 719 32 ILE CG2 C 17.9 . 1 101 719 32 ILE N N 117.2 . 1 102 720 33 THR H H 7.66 . 1 103 720 33 THR HA H 3.97 . 1 104 720 33 THR HB H 4.37 . 1 105 720 33 THR HG2 H 1.2 . 1 106 720 33 THR C C 66.96 . 1 107 720 33 THR CA C 68.75 . 1 108 720 33 THR CB C 21.62 . 1 109 720 33 THR CG2 C 175.6 . 1 110 720 33 THR N N 116.82 . 1 111 721 34 ILE H H 7.92 . 1 112 721 34 ILE HA H 3.7 . 1 113 721 34 ILE HB H 1.89 . 1 114 721 34 ILE HD1 H 0.74 . 1 115 721 34 ILE HG12 H 1.66 . 2 116 721 34 ILE HG13 H 1.08 . 2 117 721 34 ILE HG2 H 0.78 . 1 118 721 34 ILE C C 175.2 . 1 119 721 34 ILE CA C 64.73 . 1 120 721 34 ILE CB C 38.1 . 1 121 721 34 ILE CD1 C 13.78 . 1 122 721 34 ILE CG1 C 28.78 . 1 123 721 34 ILE CG2 C 17.92 . 1 124 721 34 ILE N N 119.3 . 1 125 722 35 HIS H H 8.04 . 1 126 722 35 HIS HA H 3.99 . 1 127 722 35 HIS HB2 H 3.28 . 2 128 722 35 HIS HB3 H 3.06 . 2 129 722 35 HIS HD2 H 7.07 . 1 130 722 35 HIS HE1 H 8.52 . 1 131 722 35 HIS C C 176.9 . 1 132 722 35 HIS CA C 58.56 . 1 133 722 35 HIS CB C 28.95 . 1 134 722 35 HIS CD2 C 120.5 . 1 135 722 35 HIS CE1 C 137 . 1 136 722 35 HIS N N 117.3 . 1 137 723 36 ASP H H 8.01 . 1 138 723 36 ASP HA H 4.53 . 1 139 723 36 ASP HB2 H 2.77 . 2 140 723 36 ASP HB3 H 2.7 . 2 141 723 36 ASP C C 175 . 1 142 723 36 ASP CA C 55.03 . 1 143 723 36 ASP CB C 41.23 . 1 144 723 36 ASP N N 117.5 . 1 145 724 37 ARG H H 7.88 . 1 146 724 37 ARG HA H 4.3 . 1 147 724 37 ARG HB2 H 2.21 . 2 148 724 37 ARG HB3 H 1.99 . 2 149 724 37 ARG HD2 H 3.24 . 2 150 724 37 ARG HD3 H 3.14 . 2 151 724 37 ARG HE H 7.86 . 1 152 724 37 ARG HG2 H 1.9 . 2 153 724 37 ARG HG3 H 1.73 . 2 154 724 37 ARG HH11 H 7.05 . 1 155 724 37 ARG HH12 H 7.05 . 1 156 724 37 ARG HH21 H 7.05 . 1 157 724 37 ARG HH22 H 7.05 . 1 158 724 37 ARG C C 174 . 1 159 724 37 ARG CA C 56.29 . 1 160 724 37 ARG CB C 29.88 . 1 161 724 37 ARG CD C 42.86 . 1 162 724 37 ARG CG C 27.33 . 1 163 724 37 ARG N N 120.2 . 1 164 724 37 ARG NE N 84.01 . 1 165 724 37 ARG NH1 N 72.53 . 1 166 724 37 ARG NH2 N 72.53 . 1 167 725 38 LYS H H 8.54 . 1 168 725 38 LYS HA H 4.13 . 1 169 725 38 LYS HB2 H 1.86 . 1 170 725 38 LYS HB3 H 1.86 . 1 171 725 38 LYS HD2 H 1.67 . 1 172 725 38 LYS HD3 H 1.67 . 1 173 725 38 LYS HE2 H 2.98 . 1 174 725 38 LYS HE3 H 2.98 . 1 175 725 38 LYS HG2 H 1.46 . 1 176 725 38 LYS HG3 H 1.46 . 1 177 725 38 LYS C C 173.7 . 1 178 725 38 LYS CA C 58.7 . 1 179 725 38 LYS CB C 32.09 . 1 180 725 38 LYS CD C 29.26 . 1 181 725 38 LYS CE C 42.3 . 1 182 725 38 LYS CG C 24.9 . 1 183 725 38 LYS N N 122.2 . 1 184 726 39 GLU H H 8.78 . 1 185 726 39 GLU HA H 4.07 . 1 186 726 39 GLU HB2 H 1.94 . 2 187 726 39 GLU HB3 H 1.9 . 2 188 726 39 GLU HG2 H 2.26 . 1 189 726 39 GLU HG3 H 2.26 . 1 190 726 39 GLU C C 174.1 . 1 191 726 39 GLU CA C 59.05 . 1 192 726 39 GLU CB C 29.22 . 1 193 726 39 GLU CG C 36.48 . 1 194 726 39 GLU N N 118.8 . 1 195 727 40 PHE H H 7.88 . 1 196 727 40 PHE HA H 4.37 . 1 197 727 40 PHE HB2 H 3.27 . 2 198 727 40 PHE HB3 H 3.14 . 2 199 727 40 PHE HD1 H 7.2 . 1 200 727 40 PHE HD2 H 7.2 . 1 201 727 40 PHE C C 175.1 . 1 202 727 40 PHE CA C 60.14 . 1 203 727 40 PHE CB C 39.42 . 1 204 727 40 PHE CD1 C 132 . 1 205 727 40 PHE CD2 C 132 . 1 206 727 40 PHE N N 118.7 . 1 207 728 41 ALA H H 7.87 . 1 208 728 41 ALA HA H 4.14 . 1 209 728 41 ALA HB H 1.47 . 1 210 728 41 ALA C C 172.5 . 1 211 728 41 ALA CA C 54.8 . 1 212 728 41 ALA CB C 18.7 . 1 213 728 41 ALA N N 121.9 . 1 214 729 42 LYS H H 7.85 . 1 215 729 42 LYS HA H 4.15 . 1 216 729 42 LYS HB2 H 1.82 . 1 217 729 42 LYS HB3 H 1.82 . 1 218 729 42 LYS HD2 H 1.66 . 1 219 729 42 LYS HD3 H 1.66 . 1 220 729 42 LYS HE2 H 2.92 . 1 221 729 42 LYS HE3 H 2.92 . 1 222 729 42 LYS HG2 H 1.41 . 2 223 729 42 LYS HG3 H 1.36 . 2 224 729 42 LYS C C 174 . 1 225 729 42 LYS CA C 58.14 . 1 226 729 42 LYS CB C 32.37 . 1 227 729 42 LYS CD C 29.2 . 1 228 729 42 LYS CE C 42.3 . 1 229 729 42 LYS CG C 25 . 1 230 729 42 LYS N N 117.7 . 1 231 730 43 PHE H H 7.83 . 1 232 730 43 PHE HA H 4.32 . 1 233 730 43 PHE HB2 H 3.15 . 2 234 730 43 PHE HB3 H 3.09 . 2 235 730 43 PHE HD1 H 7.13 . 1 236 730 43 PHE HD2 H 7.13 . 1 237 730 43 PHE C C 175.1 . 1 238 730 43 PHE CA C 60.31 . 1 239 730 43 PHE CB C 39.24 . 1 240 730 43 PHE CD1 C 132.1 . 1 241 730 43 PHE CD2 C 132.1 . 1 242 730 43 PHE N N 119.7 . 1 243 731 44 GLU H H 8.17 . 1 244 731 44 GLU HA H 3.94 . 1 245 731 44 GLU HB2 H 2.01 . 1 246 731 44 GLU HB3 H 2.01 . 1 247 731 44 GLU HG2 H 2.25 . 2 248 731 44 GLU HG3 H 2.16 . 2 249 731 44 GLU C C 173.8 . 1 250 731 44 GLU CA C 58.5 . 1 251 731 44 GLU CB C 29.5 . 1 252 731 44 GLU CG C 35.52 . 1 253 731 44 GLU N N 118.9 . 1 254 732 45 GLU H H 8.06 . 1 255 732 45 GLU HA H 4.03 . 1 256 732 45 GLU HB2 H 2.1 . 1 257 732 45 GLU HB3 H 2.1 . 1 258 732 45 GLU HG2 H 2.36 . 2 259 732 45 GLU HG3 H 2.23 . 2 260 732 45 GLU C C 173.7 . 1 261 732 45 GLU CA C 58.87 . 1 262 732 45 GLU CB C 29.8 . 1 263 732 45 GLU CG C 36.12 . 1 264 732 45 GLU N N 120.1 . 1 265 733 46 GLU H H 8.06 . 1 266 733 46 GLU HA H 4.07 . 1 267 733 46 GLU HB2 H 2.01 . 1 268 733 46 GLU HB3 H 2.01 . 1 269 733 46 GLU HG2 H 2.32 . 1 270 733 46 GLU HG3 H 2.32 . 1 271 733 46 GLU C C 173.5 . 1 272 733 46 GLU CA C 58.47 . 1 273 733 46 GLU CB C 29.3 . 1 274 733 46 GLU CG C 35.91 . 1 275 733 46 GLU N N 119 . 1 276 734 47 ARG H H 8.04 . 1 277 734 47 ARG HA H 3.91 . 1 278 734 47 ARG HB2 H 1.72 . 2 279 734 47 ARG HB3 H 1.59 . 2 280 734 47 ARG HD2 H 3.02 . 2 281 734 47 ARG HD3 H 2.97 . 2 282 734 47 ARG HE H 7.63 . 1 283 734 47 ARG HG2 H 1.48 . 1 284 734 47 ARG HG3 H 1.48 . 1 285 734 47 ARG HH11 H 6.9 . 1 286 734 47 ARG HH12 H 6.9 . 1 287 734 47 ARG HH21 H 6.9 . 1 288 734 47 ARG HH22 H 6.9 . 1 289 734 47 ARG C C 174.4 . 1 290 734 47 ARG CA C 58.31 . 1 291 734 47 ARG CB C 30.23 . 1 292 734 47 ARG CD C 43.5 . 1 293 734 47 ARG CG C 27.28 . 1 294 734 47 ARG N N 119.4 . 1 295 734 47 ARG NE N 84.3 . 1 296 734 47 ARG NH1 N 72.4 . 1 297 734 47 ARG NH2 N 72.4 . 1 298 735 48 ALA H H 7.78 . 1 299 735 48 ALA HA H 4.13 . 1 300 735 48 ALA HB H 1.43 . 1 301 735 48 ALA C C 173.3 . 1 302 735 48 ALA CA C 54.1 . 1 303 735 48 ALA CB C 18.9 . 1 304 735 48 ALA N N 121 . 1 305 736 49 ARG H H 7.73 . 1 306 736 49 ARG HA H 4.11 . 1 307 736 49 ARG HB2 H 1.84 . 2 308 736 49 ARG HB3 H 1.8 . 2 309 736 49 ARG HD2 H 3.16 . 2 310 736 49 ARG HD3 H 3.26 . 2 311 736 49 ARG HE H 7.44 . 1 312 736 49 ARG HG2 H 1.68 . 2 313 736 49 ARG HG3 H 1.61 . 2 314 736 49 ARG C C 175.3 . 1 315 736 49 ARG CA C 57.27 . 1 316 736 49 ARG CB C 30.87 . 1 317 736 49 ARG CD C 43.65 . 1 318 736 49 ARG CG C 27.57 . 1 319 736 49 ARG N N 117 . 1 320 736 49 ARG NE N 84.9 . 1 321 737 50 ALA H H 7.69 . 1 322 737 50 ALA HA H 4.16 . 1 323 737 50 ALA HB H 1.24 . 1 324 737 50 ALA C C 174.5 . 1 325 737 50 ALA CA C 53.1 . 1 326 737 50 ALA CB C 19.2 . 1 327 737 50 ALA N N 122.1 . 1 328 738 51 LYS H H 7.86 . 1 329 738 51 LYS HA H 4.21 . 1 330 738 51 LYS HB2 H 1.75 . 2 331 738 51 LYS HB3 H 1.71 . 2 332 738 51 LYS HD2 H 1.61 . 1 333 738 51 LYS HD3 H 1.61 . 1 334 738 51 LYS HE2 H 2.93 . 1 335 738 51 LYS HE3 H 2.93 . 1 336 738 51 LYS HG2 H 1.34 . 2 337 738 51 LYS HG3 H 1.28 . 2 338 738 51 LYS C C 175.5 . 1 339 738 51 LYS CA C 56.4 . 1 340 738 51 LYS CB C 32.71 . 1 341 738 51 LYS CD C 29.16 . 1 342 738 51 LYS CE C 42.23 . 1 343 738 51 LYS CG C 24.83 . 1 344 738 51 LYS N N 118.1 . 1 345 739 52 TRP H H 8.01 . 1 346 739 52 TRP HA H 4.65 . 1 347 739 52 TRP HB2 H 3.24 . 2 348 739 52 TRP HB3 H 3.16 . 2 349 739 52 TRP HD1 H 7.2 . 1 350 739 52 TRP HE1 H 10.37 . 1 351 739 52 TRP HE3 H 7.48 . 1 352 739 52 TRP HH2 H 7.07 . 1 353 739 52 TRP HZ2 H 7.35 . 1 354 739 52 TRP C C 176.2 . 1 355 739 52 TRP CA C 57.2 . 1 356 739 52 TRP CB C 30 . 1 357 739 52 TRP CD1 C 127 . 1 358 739 52 TRP CE3 C 120.8 . 1 359 739 52 TRP CH2 C 124.4 . 1 360 739 52 TRP CZ2 C 114.5 . 1 361 739 52 TRP N N 120.9 . 1 362 739 52 TRP NE1 N 129.9 . 1 363 740 53 ASP H H 8.34 . 1 364 740 53 ASP HA H 4.63 . 1 365 740 53 ASP HB2 H 2.69 . 2 366 740 53 ASP HB3 H 2.6 . 2 367 740 53 ASP C C 175.3 . 1 368 740 53 ASP CA C 54.23 . 1 369 740 53 ASP CB C 41.28 . 1 370 740 53 ASP N N 121.5 . 1 371 741 54 THR H H 7.99 . 1 372 741 54 THR HA H 4.04 . 1 373 741 54 THR HB H 4.09 . 1 374 741 54 THR HG2 H 1.07 . 1 375 741 54 THR C C 176.9 . 1 376 741 54 THR CA C 63.3 . 1 377 741 54 THR CB C 69.36 . 1 378 741 54 THR CG2 C 22.26 . 1 379 741 54 THR N N 113.92 . 1 380 742 55 ALA H H 8.11 . 1 381 742 55 ALA HA H 4.11 . 1 382 742 55 ALA HB H 1.34 . 1 383 742 55 ALA C C 174.2 . 1 384 742 55 ALA CA C 53.6 . 1 385 742 55 ALA CB C 19.2 . 1 386 742 55 ALA N N 123.3 . 1 387 743 56 ASN H H 7.95 . 1 388 743 56 ASN HA H 4.71 . 1 389 743 56 ASN HB2 H 2.8 . 2 390 743 56 ASN HB3 H 2.63 . 2 391 743 56 ASN HD21 H 7.76 . 2 392 743 56 ASN HD22 H 6.82 . 2 393 743 56 ASN C C 177.5 . 1 394 743 56 ASN CA C 53.05 . 1 395 743 56 ASN CB C 39.34 . 1 396 743 56 ASN N N 114.8 . 1 397 743 56 ASN ND2 N 114 . 1 398 744 57 ASN H H 7.89 . 1 399 744 57 ASN HA H 4.88 . 1 400 744 57 ASN HB2 H 2.85 . 2 401 744 57 ASN HB3 H 2.76 . 2 402 744 57 ASN HD21 H 7.91 . 2 403 744 57 ASN HD22 H 6.44 . 2 404 744 57 ASN CA C 51.94 . 1 405 744 57 ASN CB C 39.72 . 1 406 744 57 ASN N N 120 . 1 407 744 57 ASN ND2 N 112.7 . 1 408 745 58 PRO HA H 4.36 . 1 409 745 58 PRO HB2 H 2.37 . 2 410 745 58 PRO HB3 H 1.9 . 2 411 745 58 PRO HD2 H 3.83 . 2 412 745 58 PRO HD3 H 3.67 . 2 413 745 58 PRO HG2 H 2.03 . 2 414 745 58 PRO HG3 H 1.94 . 2 415 745 58 PRO C C 174 . 1 416 745 58 PRO CA C 64.82 . 1 417 745 58 PRO CB C 32.48 . 1 418 745 58 PRO CD C 51.1 . 1 419 745 58 PRO CG C 27.64 . 1 420 746 59 LEU H H 8.15 . 1 421 746 59 LEU HA H 4.15 . 1 422 746 59 LEU HB2 H 1.68 . 2 423 746 59 LEU HB3 H 1.51 . 2 424 746 59 LEU HD1 H 0.93 . 1 425 746 59 LEU HD2 H 0.86 . 1 426 746 59 LEU HG H 1.64 . 1 427 746 59 LEU C C 173.9 . 1 428 746 59 LEU CA C 57.43 . 1 429 746 59 LEU CB C 42.01 . 1 430 746 59 LEU CD1 C 25.16 . 1 431 746 59 LEU CD2 C 24.44 . 1 432 746 59 LEU CG C 27.56 . 1 433 746 59 LEU N N 119 . 1 434 747 60 TYR H H 7.75 . 1 435 747 60 TYR HA H 4.23 . 1 436 747 60 TYR HB2 H 3.17 . 2 437 747 60 TYR HB3 H 2.97 . 2 438 747 60 TYR HD1 H 6.96 . 1 439 747 60 TYR HD2 H 6.96 . 1 440 747 60 TYR HE1 H 6.74 . 1 441 747 60 TYR HE2 H 6.74 . 1 442 747 60 TYR C C 174.5 . 1 443 747 60 TYR CA C 60.27 . 1 444 747 60 TYR CB C 38.59 . 1 445 747 60 TYR CD1 C 132.77 . 1 446 747 60 TYR CD2 C 132.77 . 1 447 747 60 TYR CE1 C 118.49 . 1 448 747 60 TYR CE2 C 118.49 . 1 449 747 60 TYR N N 118.34 . 1 450 748 61 LYS H H 7.95 . 1 451 748 61 LYS HA H 4.04 . 1 452 748 61 LYS HB2 H 1.86 . 1 453 748 61 LYS HB3 H 1.86 . 1 454 748 61 LYS HD2 H 1.68 . 1 455 748 61 LYS HD3 H 1.68 . 1 456 748 61 LYS HE2 H 2.98 . 1 457 748 61 LYS HE3 H 2.98 . 1 458 748 61 LYS HG2 H 1.49 . 2 459 748 61 LYS HG3 H 1.42 . 2 460 748 61 LYS C C 173.6 . 1 461 748 61 LYS CA C 58.73 . 1 462 748 61 LYS CB C 32.59 . 1 463 748 61 LYS CD C 29.41 . 1 464 748 61 LYS CE C 42.3 . 1 465 748 61 LYS CG C 25.11 . 1 466 748 61 LYS N N 120.3 . 1 467 749 62 GLU H H 8.12 . 1 468 749 62 GLU HA H 4.18 . 1 469 749 62 GLU HB2 H 2.08 . 1 470 749 62 GLU HB3 H 2.08 . 1 471 749 62 GLU HG2 H 2.34 . 1 472 749 62 GLU HG3 H 2.34 . 1 473 749 62 GLU C C 173.6 . 1 474 749 62 GLU CA C 58.18 . 1 475 749 62 GLU CB C 29.32 . 1 476 749 62 GLU CG C 35.24 . 1 477 749 62 GLU N N 119.6 . 1 478 750 63 ALA H H 8.37 . 1 479 750 63 ALA HA H 4.11 . 1 480 750 63 ALA HB H 1.44 . 1 481 750 63 ALA C C 173.3 . 1 482 750 63 ALA CA C 54.9 . 1 483 750 63 ALA CB C 19 . 1 484 750 63 ALA N N 122.9 . 1 485 751 64 THR H H 8.04 . 1 486 751 64 THR HA H 4.02 . 1 487 751 64 THR HB H 4.21 . 1 488 751 64 THR HG2 H 1.09 . 1 489 751 64 THR C C 175.4 . 1 490 751 64 THR CA C 64.85 . 1 491 751 64 THR CB C 69.07 . 1 492 751 64 THR CG2 C 22.18 . 1 493 751 64 THR N N 109.72 . 1 494 752 65 SER H H 8 . 1 495 752 65 SER HA H 4.35 . 1 496 752 65 SER HB2 H 3.95 . 2 497 752 65 SER HB3 H 3.93 . 2 498 752 65 SER C C 176.2 . 1 499 752 65 SER CA C 60.67 . 1 500 752 65 SER CB C 63.43 . 1 501 752 65 SER N N 117.55 . 1 502 753 66 THR H H 7.89 . 1 503 753 66 THR HA H 4.06 . 1 504 753 66 THR HB H 4.06 . 1 505 753 66 THR HG2 H 1.03 . 1 506 753 66 THR C C 176.8 . 1 507 753 66 THR CA C 65.49 . 1 508 753 66 THR CB C 69.17 . 1 509 753 66 THR CG2 C 21.74 . 1 510 753 66 THR N N 117.1 . 1 511 754 67 PHE H H 8.06 . 1 512 754 67 PHE HA H 4.44 . 1 513 754 67 PHE HB2 H 3.23 . 2 514 754 67 PHE HB3 H 3.05 . 2 515 754 67 PHE HD1 H 7.19 . 1 516 754 67 PHE HD2 H 7.19 . 1 517 754 67 PHE C C 175.5 . 1 518 754 67 PHE CA C 59.71 . 1 519 754 67 PHE CB C 39.45 . 1 520 754 67 PHE CD1 C 131.6 . 1 521 754 67 PHE CD2 C 131.6 . 1 522 754 67 PHE N N 119.5 . 1 523 755 68 THR H H 7.91 . 1 524 755 68 THR HA H 4.1 . 1 525 755 68 THR HB H 4.25 . 1 526 755 68 THR HG2 H 1.23 . 1 527 755 68 THR C C 177.2 . 1 528 755 68 THR CA C 64.27 . 1 529 755 68 THR CB C 69.41 . 1 530 755 68 THR CG2 C 21.99 . 1 531 755 68 THR N N 112.7 . 1 532 756 69 ASN H H 8.1 . 1 533 756 69 ASN HA H 4.68 . 1 534 756 69 ASN HB2 H 2.87 . 2 535 756 69 ASN HB3 H 2.82 . 2 536 756 69 ASN HD21 H 7.61 . 2 537 756 69 ASN HD22 H 6.82 . 2 538 756 69 ASN C C 176.3 . 1 539 756 69 ASN CA C 54.33 . 1 540 756 69 ASN CB C 39.08 . 1 541 756 69 ASN N N 119.3 . 1 542 756 69 ASN ND2 N 112.6 . 1 543 757 70 ILE H H 7.77 . 1 544 757 70 ILE HA H 4.11 . 1 545 757 70 ILE HB H 1.9 . 1 546 757 70 ILE HD1 H 0.84 . 1 547 757 70 ILE HG12 H 1.57 . 2 548 757 70 ILE HG13 H 1.21 . 2 549 757 70 ILE HG2 H 0.87 . 1 550 757 70 ILE C C 176.2 . 1 551 757 70 ILE CA C 62.39 . 1 552 757 70 ILE CB C 38.78 . 1 553 757 70 ILE CD1 C 13.88 . 1 554 757 70 ILE CG1 C 28 . 1 555 757 70 ILE CG2 C 17.94 . 1 556 757 70 ILE N N 118.9 . 1 557 758 71 THR H H 7.86 . 1 558 758 71 THR HA H 4.26 . 1 559 758 71 THR HB H 4.09 . 1 560 758 71 THR HG2 H 1.03 . 1 561 758 71 THR C C 177.9 . 1 562 758 71 THR CA C 62.21 . 1 563 758 71 THR CB C 69.89 . 1 564 758 71 THR CG2 C 21.74 . 1 565 758 71 THR N N 114.76 . 1 566 759 72 TYR H H 7.98 . 1 567 759 72 TYR HA H 4.52 . 1 568 759 72 TYR HB2 H 2.99 . 1 569 759 72 TYR HB3 H 2.99 . 1 570 759 72 TYR HD1 H 7.08 . 1 571 759 72 TYR HD2 H 7.08 . 1 572 759 72 TYR HE1 H 6.78 . 1 573 759 72 TYR HE2 H 6.78 . 1 574 759 72 TYR C C 176.5 . 1 575 759 72 TYR CA C 58.48 . 1 576 759 72 TYR CB C 39.05 . 1 577 759 72 TYR CD1 C 133.26 . 1 578 759 72 TYR CD2 C 133.26 . 1 579 759 72 TYR CE1 C 118.4 . 1 580 759 72 TYR CE2 C 118.4 . 1 581 759 72 TYR N N 122.17 . 1 582 760 73 ARG H H 8.07 . 1 583 760 73 ARG HA H 4.29 . 1 584 760 73 ARG HB2 H 1.85 . 2 585 760 73 ARG HB3 H 1.71 . 2 586 760 73 ARG HD2 H 3.15 . 1 587 760 73 ARG HD3 H 3.15 . 1 588 760 73 ARG HE H 7.28 . 1 589 760 73 ARG HG2 H 1.57 . 1 590 760 73 ARG HG3 H 1.57 . 1 591 760 73 ARG HH11 H 6.82 . 1 592 760 73 ARG HH12 H 6.82 . 1 593 760 73 ARG HH21 H 6.82 . 1 594 760 73 ARG HH22 H 6.82 . 1 595 760 73 ARG C C 175.8 . 1 596 760 73 ARG CA C 56.15 . 1 597 760 73 ARG CB C 31.18 . 1 598 760 73 ARG CD C 43.57 . 1 599 760 73 ARG CG C 27.25 . 1 600 760 73 ARG N N 122.6 . 1 601 760 73 ARG NE N 85 . 1 602 760 73 ARG NH1 N 72.1 . 1 603 760 73 ARG NH2 N 72.1 . 1 604 761 74 GLY H H 7.77 . 1 605 761 74 GLY HA2 H 3.91 . 1 606 761 74 GLY HA3 H 3.91 . 1 607 761 74 GLY C C 178.7 . 1 608 761 74 GLY CA C 45.54 . 1 609 761 74 GLY N N 109 . 1 610 762 75 THR H H 7.56 . 1 611 762 75 THR HA H 4.14 . 1 612 762 75 THR HB H 4.23 . 1 613 762 75 THR HG2 H 1.14 . 1 614 762 75 THR CA C 63.21 . 1 615 762 75 THR CB C 70.85 . 1 616 762 75 THR CG2 C 22.33 . 1 stop_ save_