data_6346 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C Resonance Assignments and Secondary Structure Determination Reveal that the Minimal Rac1 GTPase Binding Domain of Plexin-B1 Has a Ubiquitin Fold ; _BMRB_accession_number 6346 _BMRB_flat_file_name bmr6346.str _Entry_type original _Submission_date 2004-10-10 _Accession_date 2004-10-11 _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 Tong Yufeng . . 2 Buck Matthias . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 674 "13C chemical shifts" 517 "15N chemical shifts" 123 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-25 original author . stop_ _Original_release_date 2005-07-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N and 13C Resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15929008 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tong Yufeng . . 2 Buck Matthias . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 369 _Page_last 370 _Year 2005 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Vikis HG, Li W, He Z, Guan KL. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12457-62. ; _Citation_title 'The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11035813 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vikis 'H G' G. . 2 Li W . . 3 He Z . . 4 Guan 'K L' L. . 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 97 _Journal_issue 23 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 12457 _Page_last 12462 _Year 2000 _Details ; Semaphorin molecules serve as axon guidance signals that regulate the navigation of neuronal growth cones. Semaphorins have also been implicated in other biological processes, including the immune response. Plexins, acting either alone or in complex with neuropilins, have recently been identified as functional semaphorin receptors. However, the mechanisms of signal transduction by plexins remain largely unknown. We have demonstrated a direct interaction between plexin-B1 and activated Rac. Rac specifically interacts with the cytosolic domain of plexin-B1, but not with that of plexin-A3 or -C1. Neither RhoA nor Cdc42 interacts with plexin-B1, indicating that the Rac/plexin-B1 interaction is highly specific. The binding of GTP and the integrity of the Rac effector domain are required for the interaction with plexin-B1. Furthermore, we have identified that a Cdc42/Rac interactive binding (CRIB) motif in the cytosolic domain of plexin-B1 is essential for its interaction with active Rac. We have also observed that the semaphorin CD100, a ligand for plexin-B1, stimulates the interaction between plexin-B1 and active Rac. Our results support a model by which activated Rac plays a role in mediating semaphorin signals, resulting in reorganization of actin cytoskeletal structure. ; save_ ################################## # Molecular system description # ################################## save_plexin-B1_RBD-W1830F _Saveframe_category molecular_system _Mol_system_name 'h. plexin-B1 RBD-W1830F' _Abbreviation_common 'plexin-B1 RBD-W1830F' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'plexin-B1 RBD-W1830F' $plxb1_RBD-W1830F stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Rac1/Rnd1 small GTPase binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_plxb1_RBD-W1830F _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'plexin-B1 RBD' _Name_variant W1830F _Abbreviation_common 'plxb1 RBD-W1830F' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 122 _Mol_residue_sequence ; KKDVEYRPLTLNALLAVGPG AGEAQGVPVKVLDCDTISQA KEKMLDQLYKGVPLTQRPDP RTLDVEWRSGVAGHLILSDE DVTSEVQGLFRRLNTLQHYK VPDGATVALVPCLTKHVLRE NQ ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 LYS 2 -1 LYS 3 1743 ASP 4 1744 VAL 5 1745 GLU 6 1746 TYR 7 1747 ARG 8 1748 PRO 9 1749 LEU 10 1750 THR 11 1751 LEU 12 1752 ASN 13 1753 ALA 14 1754 LEU 15 1755 LEU 16 1756 ALA 17 1757 VAL 18 1758 GLY 19 1759 PRO 20 1760 GLY 21 1761 ALA 22 1762 GLY 23 1763 GLU 24 1764 ALA 25 1765 GLN 26 1766 GLY 27 1767 VAL 28 1768 PRO 29 1769 VAL 30 1770 LYS 31 1771 VAL 32 1772 LEU 33 1773 ASP 34 1774 CYS 35 1775 ASP 36 1776 THR 37 1777 ILE 38 1778 SER 39 1779 GLN 40 1780 ALA 41 1781 LYS 42 1782 GLU 43 1783 LYS 44 1784 MET 45 1785 LEU 46 1786 ASP 47 1787 GLN 48 1788 LEU 49 1789 TYR 50 1790 LYS 51 1791 GLY 52 1792 VAL 53 1793 PRO 54 1794 LEU 55 1795 THR 56 1796 GLN 57 1797 ARG 58 1798 PRO 59 1799 ASP 60 1800 PRO 61 1801 ARG 62 1802 THR 63 1803 LEU 64 1804 ASP 65 1805 VAL 66 1806 GLU 67 1807 TRP 68 1808 ARG 69 1809 SER 70 1810 GLY 71 1811 VAL 72 1812 ALA 73 1813 GLY 74 1814 HIS 75 1815 LEU 76 1816 ILE 77 1817 LEU 78 1818 SER 79 1819 ASP 80 1820 GLU 81 1821 ASP 82 1822 VAL 83 1823 THR 84 1824 SER 85 1825 GLU 86 1826 VAL 87 1827 GLN 88 1828 GLY 89 1829 LEU 90 1830 PHE 91 1831 ARG 92 1832 ARG 93 1833 LEU 94 1834 ASN 95 1835 THR 96 1836 LEU 97 1837 GLN 98 1838 HIS 99 1839 TYR 100 1840 LYS 101 1841 VAL 102 1842 PRO 103 1843 ASP 104 1844 GLY 105 1845 ALA 106 1846 THR 107 1847 VAL 108 1848 ALA 109 1849 LEU 110 1850 VAL 111 1851 PRO 112 1852 CYS 113 1853 LEU 114 1854 THR 115 1855 LYS 116 1856 HIS 117 1857 VAL 118 1858 LEU 119 1859 ARG 120 1860 GLU 121 1861 ASN 122 1862 GLN 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 PDB 2JPH "Nmr Solution Structure Of The Rho Gtpase Binding Domain Of Human Plexin-B1" 100.00 123 100.00 100.00 2.32e-82 PDB 2R2O "Crystal Structure Of The Effector Domain Of Human Plexin B1" 98.36 138 98.33 99.17 1.35e-78 PDB 2REX "Crystal Structure Of The Effector Domain Of Plxnb1 Bound With Rnd1 Gtpase" 98.36 121 99.17 100.00 9.93e-80 PDB 3HM6 "Crystal Structure Of The Cytoplasmic Domain Of Human Plexin B1" 100.00 644 97.54 100.00 2.22e-75 PDB 3SU8 "Crystal Structure Of A Truncated Intracellular Domain Of Plexin-B1 In Complex With Rac1" 100.00 611 97.54 100.00 1.63e-75 PDB 3SUA "Crystal Structure Of The Intracellular Domain Of Plexin-B1 In Complex With Rac1" 100.00 633 97.54 100.00 1.56e-75 DBJ BAA23703 "KIAA0407 [Homo sapiens]" 100.00 2143 97.54 100.00 1.39e-71 DBJ BAG10332 "plexin-B1 precursor [synthetic construct]" 100.00 2135 97.54 100.00 1.30e-71 DBJ BAG52423 "unnamed protein product [Homo sapiens]" 100.00 588 97.54 100.00 7.27e-76 DBJ BAG52582 "unnamed protein product [Homo sapiens]" 100.00 588 97.54 100.00 6.68e-76 EMBL CAB56222 "plexin-B1/SEP receptor [Homo sapiens]" 100.00 1952 97.54 100.00 1.34e-71 EMBL CAB57277 "semaphorin receptor [Homo sapiens]" 100.00 2135 97.54 100.00 1.41e-71 GB AAI46794 "Plexin B1 [Homo sapiens]" 100.00 2135 97.54 100.00 1.30e-71 GB EAW64864 "plexin B1, isoform CRA_a [Homo sapiens]" 100.00 1220 97.54 100.00 2.90e-72 GB EAW64865 "plexin B1, isoform CRA_b [Homo sapiens]" 100.00 2135 97.54 100.00 1.30e-71 GB EAW64866 "plexin B1, isoform CRA_c [Homo sapiens]" 100.00 1952 97.54 100.00 1.34e-71 REF NP_001123554 "plexin-B1 precursor [Homo sapiens]" 100.00 2135 97.54 100.00 1.30e-71 REF NP_002664 "plexin-B1 precursor [Homo sapiens]" 100.00 2135 97.54 100.00 1.30e-71 REF XP_003257054 "PREDICTED: LOW QUALITY PROTEIN: plexin-B1 [Nomascus leucogenys]" 100.00 2143 97.54 100.00 1.53e-71 REF XP_003926345 "PREDICTED: plexin-B1 isoform X2 [Saimiri boliviensis boliviensis]" 100.00 2137 97.54 100.00 1.41e-71 REF XP_004034120 "PREDICTED: plexin-B1 isoform 1 [Gorilla gorilla gorilla]" 100.00 2135 97.54 100.00 1.20e-71 SP O43157 "RecName: Full=Plexin-B1; AltName: Full=Semaphorin receptor SEP; Flags: Precursor [Homo sapiens]" 100.00 2135 97.54 100.00 1.30e-71 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $plxb1_RBD-W1830F Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $plxb1_RBD-W1830F 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $plxb1_RBD-W1830F 1.2 mM '[U-13C; U-15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $plxb1_RBD-W1830F 2 mM [U-13C] stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version 5.2.2 loop_ _Task 'Spectral Analysis' stop_ _Details . save_ save_nmrPipe _Saveframe_category software _Name NMRPipe _Version 2.3 loop_ _Task 'Data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model ICE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-13C_CT-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C CT-HSQC' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNHA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_H(CCCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH _Sample_label . save_ save_CC(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _Sample_label . save_ save_HCCH-TOSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOSY _Sample_label . save_ save_RD-HBCB(CGCD)HD_11 _Saveframe_category NMR_applied_experiment _Experiment_name RD-HBCB(CGCD)HD _Sample_label . save_ save_1H-TOCSY-relayed_RD-HCH-COSY_12 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-TOCSY-relayed RD-HCH-COSY' _Sample_label . save_ save_NOESY-15N-HSQC_13 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-15N-HSQC _Sample_label . save_ save_NOESY-13C-HSQC_14 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-13C-HSQC _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C CT-HSQC' _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 HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCCO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name RD-HBCB(CGCD)HD _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_12 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-TOCSY-relayed RD-HCH-COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_13 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_14 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-13C-HSQC _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 6.8 0.2 pH temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'plexin-B1 RBD-W1830F' _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 ASP N N 121.906 0.04 1 2 . 3 ASP H H 8.439 0.02 1 3 . 3 ASP CA C 54.397 0.24 1 4 . 3 ASP HA H 4.595 0.04 1 5 . 3 ASP CB C 40.560 0.24 1 6 . 3 ASP HB3 H 2.583 0.04 2 7 . 3 ASP HB2 H 2.715 0.04 2 8 . 3 ASP C C 175.973 0.10 1 9 . 4 VAL N N 118.586 0.04 1 10 . 4 VAL H H 8.024 0.02 1 11 . 4 VAL CA C 61.500 0.24 1 12 . 4 VAL HA H 4.123 0.04 1 13 . 4 VAL CB C 32.230 0.24 1 14 . 4 VAL HB H 2.000 0.04 1 15 . 4 VAL CG2 C 20.197 0.30 1 16 . 4 VAL HG2 H 0.880 0.04 4 17 . 4 VAL CG1 C 20.197 0.30 1 18 . 4 VAL HG1 H 0.880 0.04 4 19 . 4 VAL C C 175.790 0.10 1 20 . 5 GLU N N 123.998 0.04 1 21 . 5 GLU H H 8.470 0.02 1 22 . 5 GLU CA C 56.000 0.24 1 23 . 5 GLU HA H 4.308 0.04 1 24 . 5 GLU CB C 29.800 0.24 1 25 . 5 GLU HB3 H 1.903 0.04 1 26 . 5 GLU HB2 H 1.903 0.04 1 27 . 5 GLU CG C 35.688 0.28 1 28 . 5 GLU HG3 H 2.219 0.04 1 29 . 5 GLU HG2 H 2.219 0.04 1 30 . 5 GLU C C 175.665 0.10 1 31 . 6 TYR N N 119.758 0.04 1 32 . 6 TYR H H 7.768 0.02 1 33 . 6 TYR CA C 56.030 0.24 1 34 . 6 TYR HA H 4.966 0.04 1 35 . 6 TYR CB C 39.900 0.24 1 36 . 6 TYR HB3 H 3.044 0.04 1 37 . 6 TYR HB2 H 3.044 0.04 1 38 . 6 TYR C C 174.405 0.10 1 39 . 7 ARG N N 121.948 0.04 1 40 . 7 ARG H H 9.007 0.02 1 41 . 7 ARG CA C 52.358 0.24 1 42 . 7 ARG HA H 4.851 0.04 1 43 . 7 ARG CB C 30.887 0.24 1 44 . 7 ARG HB3 H 1.765 0.04 2 45 . 7 ARG HB2 H 1.671 0.04 2 46 . 7 ARG CG C 25.881 0.28 1 47 . 7 ARG HG3 H 1.575 0.04 1 48 . 7 ARG HG2 H 1.575 0.04 1 49 . 7 ARG CD C 42.692 0.28 1 50 . 7 ARG HD3 H 3.173 0.04 1 51 . 7 ARG HD2 H 3.173 0.04 1 52 . 7 ARG C C 174.405 0.10 1 53 . 8 PRO CA C 61.905 0.24 1 54 . 8 PRO HA H 5.069 0.04 1 55 . 8 PRO CB C 31.485 0.24 1 56 . 8 PRO HB3 H 2.194 0.04 2 57 . 8 PRO HB2 H 1.981 0.04 2 58 . 8 PRO CG C 26.195 0.28 1 59 . 8 PRO HG3 H 2.013 0.04 1 60 . 8 PRO HG2 H 2.013 0.04 1 61 . 8 PRO CD C 50.308 0.28 1 62 . 8 PRO HD3 H 3.730 0.04 1 63 . 8 PRO HD2 H 3.730 0.04 1 64 . 8 PRO C C 175.997 0.10 1 65 . 9 LEU N N 121.354 0.04 1 66 . 9 LEU H H 8.696 0.02 1 67 . 9 LEU CA C 53.370 0.24 1 68 . 9 LEU HA H 4.629 0.04 1 69 . 9 LEU CB C 44.580 0.24 1 70 . 9 LEU HB3 H 1.437 0.04 2 71 . 9 LEU HB2 H 1.250 0.04 2 72 . 9 LEU CG C 24.652 0.28 1 73 . 9 LEU HG H 0.744 0.04 1 74 . 9 LEU CD1 C 25.562 0.30 2 75 . 9 LEU HD1 H 0.596 0.04 4 76 . 9 LEU CD2 C 22.428 0.30 2 77 . 9 LEU HD2 H 0.596 0.04 4 78 . 9 LEU C C 175.509 0.10 1 79 . 10 THR N N 118.855 0.04 1 80 . 10 THR H H 9.123 0.02 1 81 . 10 THR CA C 61.810 0.24 1 82 . 10 THR HA H 4.988 0.04 1 83 . 10 THR CB C 68.380 0.24 1 84 . 10 THR HB H 4.046 0.04 1 85 . 10 THR CG2 C 21.180 0.30 1 86 . 10 THR HG2 H 1.080 0.04 1 87 . 10 THR C C 174.497 0.10 1 88 . 11 LEU N N 124.791 0.04 1 89 . 11 LEU H H 9.093 0.02 1 90 . 11 LEU CA C 52.060 0.24 1 91 . 11 LEU HA H 4.792 0.04 1 92 . 11 LEU CB C 41.960 0.24 1 93 . 11 LEU HB3 H 1.335 0.04 1 94 . 11 LEU HB2 H 1.335 0.04 1 95 . 11 LEU CG C 26.186 0.28 1 96 . 11 LEU HG H 1.536 0.04 1 97 . 11 LEU CD1 C 21.615 0.30 2 98 . 11 LEU HD1 H 0.670 0.04 4 99 . 11 LEU CD2 C 25.204 0.30 1 100 . 11 LEU HD2 H 1.335 0.04 2 101 . 11 LEU C C 175.492 0.10 1 102 . 12 ASN N N 121.481 0.04 1 103 . 12 ASN H H 8.892 0.02 1 104 . 12 ASN CA C 52.470 0.24 1 105 . 12 ASN HA H 4.813 0.04 1 106 . 12 ASN CB C 38.920 0.24 1 107 . 12 ASN HB3 H 2.614 0.04 2 108 . 12 ASN HB2 H 2.467 0.04 2 109 . 12 ASN CG C 176.740 0.28 1 110 . 12 ASN ND2 N 113.265 0.20 1 111 . 12 ASN HD21 H 6.951 0.04 2 112 . 12 ASN HD22 H 7.244 0.04 2 113 . 12 ASN C C 172.963 0.10 1 114 . 13 ALA N N 126.586 0.04 1 115 . 13 ALA H H 8.936 0.02 1 116 . 13 ALA CA C 50.490 0.24 1 117 . 13 ALA HA H 5.573 0.04 1 118 . 13 ALA CB C 21.310 0.24 1 119 . 13 ALA HB H 1.317 0.04 1 120 . 13 ALA C C 176.547 0.10 1 121 . 14 LEU N N 119.372 0.04 1 122 . 14 LEU H H 8.552 0.02 1 123 . 14 LEU CA C 53.350 0.24 1 124 . 14 LEU HA H 4.761 0.04 1 125 . 14 LEU CB C 44.230 0.24 1 126 . 14 LEU HB3 H 1.488 0.04 1 127 . 14 LEU HB2 H 1.488 0.04 1 128 . 14 LEU CG C 25.415 0.28 1 129 . 14 LEU HG H 0.739 0.04 1 130 . 14 LEU CD1 C 23.564 0.30 2 131 . 14 LEU HD1 H 0.739 0.04 4 132 . 14 LEU CD2 C 25.415 0.30 2 133 . 14 LEU HD2 H 0.739 0.04 4 134 . 14 LEU C C 175.195 0.10 1 135 . 15 LEU N N 122.996 0.04 1 136 . 15 LEU H H 8.750 0.02 1 137 . 15 LEU CA C 53.350 0.24 1 138 . 15 LEU HA H 4.644 0.04 1 139 . 15 LEU CB C 41.790 0.24 1 140 . 15 LEU HB3 H 1.922 0.04 2 141 . 15 LEU HB2 H 1.439 0.04 2 142 . 15 LEU CG C 26.483 0.28 1 143 . 15 LEU HG H 1.612 0.04 1 144 . 15 LEU CD1 C 23.490 0.30 1 145 . 15 LEU HD1 H 0.887 0.04 4 146 . 15 LEU CD2 C 23.490 0.30 1 147 . 15 LEU HD2 H 0.887 0.04 4 148 . 15 LEU C C 175.394 0.10 1 149 . 16 ALA N N 130.622 0.04 1 150 . 16 ALA H H 8.525 0.02 1 151 . 16 ALA CA C 50.860 0.24 1 152 . 16 ALA HA H 4.717 0.04 1 153 . 16 ALA CB C 18.086 0.24 1 154 . 16 ALA HB H 1.349 0.04 1 155 . 16 ALA C C 176.029 0.10 1 156 . 17 VAL N N 114.825 0.04 1 157 . 17 VAL H H 7.485 0.02 1 158 . 17 VAL CA C 60.660 0.24 1 159 . 17 VAL HA H 4.319 0.04 1 160 . 17 VAL CB C 33.140 0.24 1 161 . 17 VAL HB H 2.097 0.04 1 162 . 17 VAL CG2 C 20.445 0.30 2 163 . 17 VAL HG2 H 0.878 0.04 4 164 . 17 VAL CG1 C 18.688 0.30 2 165 . 17 VAL HG1 H 0.878 0.04 4 166 . 17 VAL C C 175.697 0.10 1 167 . 18 GLY N N 111.541 0.04 1 168 . 18 GLY H H 8.414 0.02 1 169 . 18 GLY CA C 44.110 0.24 1 170 . 18 GLY HA3 H 4.109 0.04 2 171 . 18 GLY HA2 H 4.318 0.04 2 172 . 18 GLY C C 175.697 0.10 1 173 . 19 PRO CA C 63.609 0.24 1 174 . 19 PRO HA H 4.470 0.04 1 175 . 19 PRO CB C 30.984 0.24 1 176 . 19 PRO HB3 H 2.330 0.04 2 177 . 19 PRO HB2 H 2.035 0.04 2 178 . 19 PRO CG C 26.204 0.28 1 179 . 19 PRO HG3 H 2.035 0.04 1 180 . 19 PRO HG2 H 2.035 0.04 1 181 . 19 PRO CD C 49.086 0.28 1 182 . 19 PRO HD3 H 3.692 0.04 1 183 . 19 PRO HD2 H 3.692 0.04 1 184 . 19 PRO C C 178.020 0.10 1 185 . 20 GLY N N 109.609 0.04 1 186 . 20 GLY H H 8.764 0.02 1 187 . 20 GLY CA C 45.070 0.24 1 188 . 20 GLY HA3 H 4.039 0.04 1 189 . 20 GLY HA2 H 4.039 0.04 1 190 . 20 GLY C C 174.797 0.10 1 191 . 21 ALA N N 123.255 0.04 1 192 . 21 ALA H H 7.903 0.02 1 193 . 21 ALA CA C 53.000 0.24 1 194 . 21 ALA HA H 4.233 0.04 1 195 . 21 ALA CB C 18.520 0.24 1 196 . 21 ALA HB H 1.381 0.04 1 197 . 21 ALA C C 178.447 0.10 1 198 . 22 GLY N N 106.559 0.04 1 199 . 22 GLY H H 8.519 0.02 1 200 . 22 GLY CA C 45.130 0.24 1 201 . 22 GLY HA3 H 3.967 0.04 1 202 . 22 GLY HA2 H 3.967 0.04 1 203 . 22 GLY C C 174.313 0.10 1 204 . 23 GLU N N 119.668 0.04 1 205 . 23 GLU H H 8.074 0.02 1 206 . 23 GLU CA C 55.720 0.24 1 207 . 23 GLU HA H 4.398 0.04 1 208 . 23 GLU CB C 29.460 0.24 1 209 . 23 GLU HB3 H 2.162 0.04 2 210 . 23 GLU HB2 H 1.951 0.04 2 211 . 23 GLU CG C 35.709 0.28 1 212 . 23 GLU HG3 H 2.281 0.04 1 213 . 23 GLU HG2 H 2.281 0.04 1 214 . 23 GLU C C 176.155 0.10 1 215 . 24 ALA N N 124.447 0.04 1 216 . 24 ALA H H 7.926 0.02 1 217 . 24 ALA CA C 52.000 0.24 1 218 . 24 ALA HA H 4.307 0.04 1 219 . 24 ALA CB C 18.890 0.24 1 220 . 24 ALA HB H 1.455 0.04 1 221 . 24 ALA C C 176.987 0.10 1 222 . 25 GLN N N 119.155 0.04 1 223 . 25 GLN H H 8.337 0.02 1 224 . 25 GLN CA C 54.750 0.24 1 225 . 25 GLN HA H 4.415 0.04 1 226 . 25 GLN CB C 29.320 0.24 1 227 . 25 GLN HB3 H 2.166 0.04 2 228 . 25 GLN HB2 H 2.022 0.04 2 229 . 25 GLN CG C 33.329 0.28 1 230 . 25 GLN HG3 H 2.448 0.04 1 231 . 25 GLN HG2 H 2.448 0.04 1 232 . 25 GLN CD C 180.713 0.28 1 233 . 25 GLN NE2 N 113.010 0.20 1 234 . 25 GLN HE21 H 6.893 0.04 2 235 . 25 GLN HE22 H 7.610 0.04 2 236 . 25 GLN C C 176.176 0.10 1 237 . 26 GLY N N 111.343 0.04 1 238 . 26 GLY H H 8.506 0.02 1 239 . 26 GLY CA C 44.800 0.24 1 240 . 26 GLY HA3 H 4.237 0.04 2 241 . 26 GLY HA2 H 3.743 0.04 2 242 . 26 GLY C C 173.583 0.10 1 243 . 27 VAL N N 120.282 0.04 1 244 . 27 VAL H H 8.877 0.02 1 245 . 27 VAL CA C 57.819 0.24 1 246 . 27 VAL HA H 4.778 0.04 1 247 . 27 VAL CB C 33.470 0.24 1 248 . 27 VAL HB H 2.073 0.04 1 249 . 27 VAL CG2 C 20.178 0.30 2 250 . 27 VAL HG2 H 0.925 0.04 4 251 . 27 VAL CG1 C 18.936 0.30 2 252 . 27 VAL HG1 H 0.844 0.04 4 253 . 27 VAL C C 173.583 0.10 1 254 . 28 PRO CA C 61.955 0.24 1 255 . 28 PRO HA H 5.125 0.04 1 256 . 28 PRO CB C 31.630 0.24 1 257 . 28 PRO HB3 H 2.087 0.04 2 258 . 28 PRO HB2 H 1.779 0.04 2 259 . 28 PRO CG C 26.730 0.28 1 260 . 28 PRO HG3 H 2.010 0.04 2 261 . 28 PRO HG2 H 2.140 0.04 2 262 . 28 PRO CD C 50.000 0.28 1 263 . 28 PRO HD3 H 3.790 0.04 1 264 . 28 PRO HD2 H 3.790 0.04 1 265 . 28 PRO C C 178.215 0.10 1 266 . 29 VAL N N 122.798 0.04 1 267 . 29 VAL H H 9.114 0.02 1 268 . 29 VAL CA C 60.330 0.24 1 269 . 29 VAL HA H 4.374 0.04 1 270 . 29 VAL CB C 34.200 0.24 1 271 . 29 VAL HB H 1.825 0.04 1 272 . 29 VAL CG2 C 21.518 0.30 2 273 . 29 VAL HG2 H 0.901 0.04 4 274 . 29 VAL CG1 C 20.204 0.30 2 275 . 29 VAL HG1 H 0.766 0.04 4 276 . 29 VAL C C 174.406 0.10 1 277 . 30 LYS N N 127.701 0.04 1 278 . 30 LYS H H 8.824 0.02 1 279 . 30 LYS CA C 55.930 0.24 1 280 . 30 LYS HA H 5.017 0.04 1 281 . 30 LYS CB C 31.160 0.24 1 282 . 30 LYS HB3 H 1.922 0.04 1 283 . 30 LYS HB2 H 1.922 0.04 1 284 . 30 LYS CG C 23.781 0.28 1 285 . 30 LYS HG3 H 1.496 0.04 1 286 . 30 LYS HG2 H 1.496 0.04 1 287 . 30 LYS CD C 28.358 0.28 1 288 . 30 LYS HD3 H 1.728 0.04 1 289 . 30 LYS HD2 H 1.728 0.04 1 290 . 30 LYS CE C 41.343 0.28 1 291 . 30 LYS HE3 H 2.967 0.04 1 292 . 30 LYS HE2 H 2.967 0.04 1 293 . 30 LYS C C 176.649 0.10 1 294 . 31 VAL N N 118.742 0.04 1 295 . 31 VAL H H 9.021 0.02 1 296 . 31 VAL CA C 58.700 0.24 1 297 . 31 VAL HA H 4.639 0.04 1 298 . 31 VAL CB C 33.610 0.24 1 299 . 31 VAL HB H 2.657 0.04 1 300 . 31 VAL CG2 C 20.799 0.30 2 301 . 31 VAL HG2 H 0.855 0.04 4 302 . 31 VAL CG1 C 18.778 0.30 2 303 . 31 VAL HG1 H 0.590 0.04 4 304 . 31 VAL C C 173.918 0.10 1 305 . 32 LEU N N 120.139 0.04 1 306 . 32 LEU H H 8.669 0.02 1 307 . 32 LEU CA C 52.760 0.24 1 308 . 32 LEU HA H 5.151 0.04 1 309 . 32 LEU CB C 44.340 0.24 1 310 . 32 LEU HB3 H 1.763 0.04 2 311 . 32 LEU HB2 H 1.449 0.04 2 312 . 32 LEU CG C 26.125 0.28 1 313 . 32 LEU HG H 0.799 0.04 1 314 . 32 LEU CD1 C 21.715 0.30 2 315 . 32 LEU HD1 H 0.624 0.04 4 316 . 32 LEU CD2 C 23.967 0.30 2 317 . 32 LEU HD2 H 0.624 0.04 4 318 . 32 LEU C C 178.133 0.10 1 319 . 33 ASP N N 121.569 0.04 1 320 . 33 ASP H H 9.206 0.02 1 321 . 33 ASP CA C 56.461 0.24 1 322 . 33 ASP HA H 4.156 0.04 1 323 . 33 ASP CB C 38.293 0.24 1 324 . 33 ASP HB3 H 2.814 0.04 2 325 . 33 ASP HB2 H 2.687 0.04 2 326 . 33 ASP C C 175.696 0.10 1 327 . 34 CYS N N 112.659 0.04 1 328 . 34 CYS H H 7.426 0.02 1 329 . 34 CYS CA C 55.713 0.24 1 330 . 34 CYS HA H 4.719 0.04 1 331 . 34 CYS CB C 27.623 0.24 1 332 . 34 CYS HB3 H 3.362 0.04 2 333 . 34 CYS HB2 H 2.683 0.04 2 334 . 34 CYS C C 173.750 0.10 1 335 . 35 ASP N N 125.614 0.04 1 336 . 35 ASP H H 7.914 0.02 1 337 . 35 ASP CA C 54.920 0.24 1 338 . 35 ASP HA H 4.734 0.04 1 339 . 35 ASP CB C 39.870 0.24 1 340 . 35 ASP HB3 H 2.950 0.04 2 341 . 35 ASP HB2 H 2.648 0.04 2 342 . 35 ASP C C 177.361 0.10 1 343 . 36 THR N N 110.929 0.04 1 344 . 36 THR H H 8.513 0.02 1 345 . 36 THR CA C 60.540 0.24 1 346 . 36 THR HA H 4.935 0.04 1 347 . 36 THR CB C 69.220 0.24 1 348 . 36 THR HB H 4.811 0.04 1 349 . 36 THR CG2 C 21.837 0.30 1 350 . 36 THR HG2 H 1.262 0.04 1 351 . 36 THR C C 174.890 0.10 1 352 . 37 ILE N N 120.178 0.04 1 353 . 37 ILE H H 7.770 0.02 1 354 . 37 ILE CA C 62.900 0.24 1 355 . 37 ILE HA H 3.626 0.04 1 356 . 37 ILE CB C 32.010 0.24 1 357 . 37 ILE HB H 2.405 0.04 1 358 . 37 ILE CG1 C 26.139 0.30 2 359 . 37 ILE HG13 H 1.746 0.04 9 360 . 37 ILE HG12 H 1.213 0.04 9 361 . 37 ILE CD1 C 7.345 0.30 1 362 . 37 ILE HD1 H 0.598 0.04 1 363 . 37 ILE CG2 C 17.051 0.30 2 364 . 37 ILE HG2 H 0.795 0.04 1 365 . 37 ILE C C 179.558 0.10 1 366 . 38 SER N N 117.593 0.04 1 367 . 38 SER H H 10.138 0.02 1 368 . 38 SER CA C 61.310 0.24 1 369 . 38 SER HA H 3.875 0.04 1 370 . 38 SER CB C 63.670 0.24 1 371 . 38 SER HB3 H 4.020 0.04 1 372 . 38 SER HB2 H 4.020 0.04 1 373 . 38 SER C C 177.577 0.10 1 374 . 39 GLN N N 122.318 0.04 1 375 . 39 GLN H H 7.849 0.02 1 376 . 39 GLN CA C 58.520 0.24 1 377 . 39 GLN HA H 4.104 0.04 1 378 . 39 GLN CB C 27.870 0.24 1 379 . 39 GLN HB3 H 1.773 0.04 1 380 . 39 GLN HB2 H 1.773 0.04 1 381 . 39 GLN CG C 34.208 0.28 1 382 . 39 GLN HG3 H 2.437 0.04 1 383 . 39 GLN HG2 H 2.437 0.04 1 384 . 39 GLN CD C 179.960 0.28 1 385 . 39 GLN NE2 N 110.399 0.20 1 386 . 39 GLN HE21 H 6.776 0.04 2 387 . 39 GLN HE22 H 7.500 0.04 2 388 . 39 GLN C C 179.669 0.10 1 389 . 40 ALA N N 123.102 0.04 1 390 . 40 ALA H H 9.106 0.02 1 391 . 40 ALA CA C 54.950 0.24 1 392 . 40 ALA HA H 4.005 0.04 1 393 . 40 ALA CB C 16.300 0.24 1 394 . 40 ALA HB H 1.459 0.04 1 395 . 40 ALA C C 179.037 0.10 1 396 . 41 LYS N N 119.399 0.04 1 397 . 41 LYS H H 9.134 0.02 1 398 . 41 LYS CA C 59.810 0.24 1 399 . 41 LYS HA H 3.901 0.04 1 400 . 41 LYS CB C 31.110 0.24 1 401 . 41 LYS HB3 H 1.790 0.04 1 402 . 41 LYS HB2 H 1.790 0.04 1 403 . 41 LYS CG C 23.444 0.28 1 404 . 41 LYS HG3 H 1.355 0.04 1 405 . 41 LYS HG2 H 1.355 0.04 1 406 . 41 LYS CD C 28.908 0.28 1 407 . 41 LYS HD3 H 2.107 0.04 1 408 . 41 LYS HD2 H 2.107 0.04 1 409 . 41 LYS CE C 41.018 0.28 1 410 . 41 LYS HE3 H 2.783 0.04 1 411 . 41 LYS HE2 H 2.783 0.04 1 412 . 41 LYS C C 178.031 0.10 1 413 . 42 GLU N N 118.170 0.04 1 414 . 42 GLU H H 7.765 0.02 1 415 . 42 GLU CA C 59.810 0.24 1 416 . 42 GLU HA H 3.921 0.04 1 417 . 42 GLU CB C 28.550 0.24 1 418 . 42 GLU HB3 H 2.243 0.04 1 419 . 42 GLU HB2 H 2.243 0.04 1 420 . 42 GLU CG C 35.527 0.28 1 421 . 42 GLU HG3 H 2.455 0.04 1 422 . 42 GLU HG2 H 2.455 0.04 1 423 . 42 GLU C C 178.866 0.10 1 424 . 43 LYS N N 118.411 0.04 1 425 . 43 LYS H H 7.611 0.02 1 426 . 43 LYS CA C 59.720 0.24 1 427 . 43 LYS HA H 4.185 0.04 1 428 . 43 LYS CB C 31.800 0.24 1 429 . 43 LYS HB3 H 1.985 0.04 1 430 . 43 LYS HB2 H 1.985 0.04 1 431 . 43 LYS CG C 26.348 0.28 1 432 . 43 LYS HG3 H 1.477 0.04 1 433 . 43 LYS HG2 H 1.477 0.04 1 434 . 43 LYS CD C 29.697 0.28 1 435 . 43 LYS HD3 H 1.786 0.04 1 436 . 43 LYS HD2 H 1.786 0.04 1 437 . 43 LYS CE C 41.503 0.28 1 438 . 43 LYS HE3 H 3.005 0.04 1 439 . 43 LYS HE2 H 3.005 0.04 1 440 . 43 LYS C C 180.556 0.10 1 441 . 44 MET N N 118.289 0.04 1 442 . 44 MET H H 8.605 0.02 1 443 . 44 MET CA C 59.550 0.24 1 444 . 44 MET HA H 3.939 0.04 1 445 . 44 MET CB C 33.410 0.24 1 446 . 44 MET HB3 H 1.931 0.04 2 447 . 44 MET HB2 H 2.440 0.04 2 448 . 44 MET CG C 31.044 0.28 1 449 . 44 MET HG3 H 2.796 0.04 1 450 . 44 MET HG2 H 2.796 0.04 1 451 . 44 MET CE C 16.695 0.28 1 452 . 44 MET HE H 1.841 0.04 1 453 . 44 MET C C 178.128 0.10 1 454 . 45 LEU N N 120.842 0.04 1 455 . 45 LEU H H 8.790 0.02 1 456 . 45 LEU CA C 58.700 0.24 1 457 . 45 LEU HA H 4.005 0.04 1 458 . 45 LEU CB C 40.960 0.24 1 459 . 45 LEU HB3 H 1.541 0.04 2 460 . 45 LEU HB2 H 2.071 0.04 2 461 . 45 LEU CG C 26.548 0.28 1 462 . 45 LEU HG H 1.769 0.04 1 463 . 45 LEU CD1 C 25.105 0.30 1 464 . 45 LEU HD1 H 0.853 0.04 4 465 . 45 LEU CD2 C 25.105 0.30 1 466 . 45 LEU HD2 H 0.853 0.04 4 467 . 45 LEU C C 178.246 0.10 1 468 . 46 ASP N N 116.555 0.04 1 469 . 46 ASP H H 7.958 0.02 1 470 . 46 ASP CA C 56.580 0.24 1 471 . 46 ASP HA H 4.423 0.04 1 472 . 46 ASP CB C 40.120 0.24 1 473 . 46 ASP HB3 H 2.841 0.04 2 474 . 46 ASP HB2 H 2.687 0.04 2 475 . 46 ASP C C 178.110 0.10 1 476 . 47 GLN N N 113.291 0.04 1 477 . 47 GLN H H 7.200 0.02 1 478 . 47 GLN CA C 56.550 0.24 1 479 . 47 GLN HA H 4.361 0.04 1 480 . 47 GLN CB C 28.660 0.24 1 481 . 47 GLN HB3 H 2.201 0.04 2 482 . 47 GLN HB2 H 2.000 0.04 2 483 . 47 GLN CG C 33.036 0.28 1 484 . 47 GLN HG3 H 2.598 0.04 1 485 . 47 GLN HG2 H 2.598 0.04 1 486 . 47 GLN CD C 179.605 0.28 1 487 . 47 GLN NE2 N 114.325 0.20 1 488 . 47 GLN HE21 H 7.241 0.04 2 489 . 47 GLN HE22 H 7.777 0.04 2 490 . 47 GLN C C 178.627 0.10 1 491 . 48 LEU N N 120.063 0.04 1 492 . 48 LEU H H 8.791 0.02 1 493 . 48 LEU CA C 56.880 0.24 1 494 . 48 LEU HA H 4.049 0.04 1 495 . 48 LEU CB C 41.280 0.24 1 496 . 48 LEU HB3 H 1.723 0.04 1 497 . 48 LEU HB2 H 1.723 0.04 1 498 . 48 LEU CG C 26.310 0.28 1 499 . 48 LEU HG H 1.208 0.04 1 500 . 48 LEU CD1 C 21.935 0.30 1 501 . 48 LEU HD1 H 0.728 0.04 4 502 . 48 LEU CD2 C 24.875 0.30 2 503 . 48 LEU HD2 H 0.878 0.04 4 504 . 48 LEU C C 177.730 0.10 1 505 . 49 TYR N N 114.825 0.04 1 506 . 49 TYR H H 8.124 0.02 1 507 . 49 TYR CA C 57.660 0.24 1 508 . 49 TYR HA H 4.474 0.04 1 509 . 49 TYR CB C 35.440 0.24 1 510 . 49 TYR HB3 H 3.318 0.04 2 511 . 49 TYR HB2 H 2.815 0.04 2 512 . 49 TYR C C 174.635 0.10 1 513 . 50 LYS N N 121.637 0.04 1 514 . 50 LYS H H 6.796 0.02 1 515 . 50 LYS CA C 58.690 0.24 1 516 . 50 LYS HA H 4.112 0.04 1 517 . 50 LYS CB C 31.160 0.24 1 518 . 50 LYS HB3 H 2.053 0.04 1 519 . 50 LYS HB2 H 2.053 0.04 1 520 . 50 LYS CG C 23.254 0.28 1 521 . 50 LYS HG3 H 1.512 0.04 1 522 . 50 LYS HG2 H 1.512 0.04 1 523 . 50 LYS CD C 28.526 0.28 1 524 . 50 LYS HD3 H 1.816 0.04 1 525 . 50 LYS HD2 H 1.816 0.04 1 526 . 50 LYS CE C 41.319 0.28 1 527 . 50 LYS HE3 H 3.072 0.04 1 528 . 50 LYS HE2 H 3.072 0.04 1 529 . 50 LYS C C 178.157 0.10 1 530 . 51 GLY N N 113.314 0.04 1 531 . 51 GLY H H 9.117 0.02 1 532 . 51 GLY CA C 45.000 0.24 1 533 . 51 GLY HA3 H 4.163 0.04 2 534 . 51 GLY HA2 H 3.810 0.04 2 535 . 51 GLY C C 173.931 0.10 1 536 . 52 VAL N N 122.847 0.04 1 537 . 52 VAL H H 8.112 0.02 1 538 . 52 VAL CA C 59.520 0.24 1 539 . 52 VAL HA H 4.559 0.04 1 540 . 52 VAL CB C 32.190 0.24 1 541 . 52 VAL HB H 2.388 0.04 1 542 . 52 VAL CG2 C 19.892 0.30 2 543 . 52 VAL HG2 H 1.106 0.04 4 544 . 52 VAL CG1 C 20.463 0.30 2 545 . 52 VAL HG1 H 0.993 0.04 4 546 . 52 VAL C C 173.937 0.10 1 547 . 53 PRO CA C 62.908 0.24 1 548 . 53 PRO HA H 4.470 0.04 1 549 . 53 PRO CB C 31.786 0.24 1 550 . 53 PRO HB3 H 1.840 0.04 1 551 . 53 PRO HB2 H 1.840 0.04 1 552 . 53 PRO CG C 27.103 0.28 1 553 . 53 PRO HG3 H 2.063 0.04 1 554 . 53 PRO HG2 H 2.063 0.04 1 555 . 53 PRO CD C 50.919 0.28 1 556 . 53 PRO HD3 H 4.099 0.04 2 557 . 53 PRO HD2 H 3.634 0.04 2 558 . 53 PRO C C 177.733 0.10 1 559 . 54 LEU N N 122.830 0.04 1 560 . 54 LEU H H 8.676 0.02 1 561 . 54 LEU CA C 58.400 0.24 1 562 . 54 LEU HA H 4.630 0.04 1 563 . 54 LEU CB C 40.580 0.24 1 564 . 54 LEU HB3 H 1.778 0.04 2 565 . 54 LEU HB2 H 1.639 0.04 2 566 . 54 LEU CG C 26.270 0.28 1 567 . 54 LEU HG H 1.778 0.04 1 568 . 54 LEU CD1 C 22.165 0.30 2 569 . 54 LEU HD1 H 0.946 0.04 4 570 . 54 LEU CD2 C 23.727 0.30 2 571 . 54 LEU HD2 H 0.946 0.04 4 572 . 54 LEU C C 179.461 0.10 1 573 . 55 THR N N 105.440 0.04 1 574 . 55 THR H H 7.651 0.02 1 575 . 55 THR CA C 66.820 0.24 1 576 . 55 THR HA H 4.154 0.04 1 577 . 55 THR CB C 68.140 0.24 1 578 . 55 THR HB H 4.392 0.04 1 579 . 55 THR CG2 C 21.616 0.30 1 580 . 55 THR HG2 H 1.341 0.04 1 581 . 55 THR C C 175.594 0.10 1 582 . 56 GLN N N 118.516 0.04 1 583 . 56 GLN H H 7.855 0.02 1 584 . 56 GLN CA C 54.650 0.24 1 585 . 56 GLN HA H 4.455 0.04 1 586 . 56 GLN CB C 28.880 0.24 1 587 . 56 GLN HB3 H 1.803 0.04 1 588 . 56 GLN HB2 H 1.803 0.04 1 589 . 56 GLN CG C 33.622 0.28 1 590 . 56 GLN HG3 H 2.353 0.04 1 591 . 56 GLN HG2 H 2.353 0.04 1 592 . 56 GLN CD C 180.090 0.28 1 593 . 56 GLN NE2 N 111.300 0.20 1 594 . 56 GLN HE21 H 6.895 0.04 2 595 . 56 GLN HE22 H 7.519 0.04 2 596 . 56 GLN C C 175.185 0.10 1 597 . 57 ARG N N 120.212 0.04 1 598 . 57 ARG H H 7.165 0.02 1 599 . 57 ARG CA C 53.630 0.24 1 600 . 57 ARG HA H 4.005 0.04 1 601 . 57 ARG CB C 30.100 0.24 1 602 . 57 ARG HB3 H 1.598 0.04 2 603 . 57 ARG HB2 H 1.352 0.04 2 604 . 57 ARG CG C 27.030 0.28 1 605 . 57 ARG HG3 H 1.760 0.04 2 606 . 57 ARG HG2 H 1.131 0.04 2 607 . 57 ARG CD C 44.300 0.28 1 608 . 57 ARG HD3 H 2.947 0.04 1 609 . 57 ARG HD2 H 2.947 0.04 1 610 . 57 ARG C C 175.185 0.10 1 611 . 58 PRO CA C 61.830 0.24 1 612 . 58 PRO HA H 4.370 0.04 1 613 . 58 PRO CB C 31.000 0.24 1 614 . 58 PRO HB3 H 2.122 0.04 2 615 . 58 PRO HB2 H 1.916 0.04 2 616 . 58 PRO CG C 26.294 0.28 1 617 . 58 PRO HG3 H 2.046 0.04 2 618 . 58 PRO CD C 49.641 0.28 1 619 . 58 PRO C C 175.257 0.10 1 620 . 59 ASP N N 121.322 0.04 1 621 . 59 ASP H H 8.459 0.02 1 622 . 59 ASP CA C 51.022 0.24 1 623 . 59 ASP HA H 4.674 0.04 1 624 . 59 ASP CB C 41.181 0.24 1 625 . 59 ASP HB3 H 2.737 0.04 1 626 . 59 ASP HB2 H 2.737 0.04 1 627 . 59 ASP C C 175.257 0.10 1 628 . 60 PRO CA C 64.899 0.24 1 629 . 60 PRO HA H 3.930 0.04 1 630 . 60 PRO CB C 31.539 0.24 1 631 . 60 PRO HB3 H 2.114 0.04 1 632 . 60 PRO HB2 H 2.114 0.04 1 633 . 60 PRO CG C 26.466 0.28 1 634 . 60 PRO HG3 H 2.114 0.04 1 635 . 60 PRO HG2 H 2.114 0.04 1 636 . 60 PRO CD C 50.729 0.28 1 637 . 60 PRO HD3 H 3.956 0.04 1 638 . 60 PRO HD2 H 3.956 0.04 1 639 . 60 PRO C C 177.654 0.10 1 640 . 61 ARG N N 115.474 0.04 1 641 . 61 ARG H H 8.545 0.02 1 642 . 61 ARG CA C 57.760 0.24 1 643 . 61 ARG HA H 4.205 0.04 1 644 . 61 ARG CB C 28.830 0.24 1 645 . 61 ARG HB3 H 1.929 0.04 1 646 . 61 ARG HB2 H 1.929 0.04 1 647 . 61 ARG CG C 26.260 0.28 1 648 . 61 ARG HG3 H 1.784 0.04 1 649 . 61 ARG HG2 H 1.784 0.04 1 650 . 61 ARG CD C 42.726 0.28 1 651 . 61 ARG HD3 H 3.266 0.04 1 652 . 61 ARG HD2 H 3.266 0.04 1 653 . 61 ARG C C 177.853 0.10 1 654 . 62 THR N N 107.274 0.04 1 655 . 62 THR H H 8.052 0.02 1 656 . 62 THR CA C 61.960 0.24 1 657 . 62 THR HA H 4.454 0.04 1 658 . 62 THR CB C 69.120 0.24 1 659 . 62 THR HB H 4.598 0.04 1 660 . 62 THR CG2 C 21.319 0.30 1 661 . 62 THR HG2 H 1.278 0.04 1 662 . 62 THR C C 173.739 0.10 1 663 . 63 LEU N N 122.831 0.04 1 664 . 63 LEU H H 7.440 0.02 1 665 . 63 LEU CA C 53.000 0.24 1 666 . 63 LEU HA H 5.255 0.04 1 667 . 63 LEU CB C 44.870 0.24 1 668 . 63 LEU HB3 H 1.577 0.04 2 669 . 63 LEU HB2 H 1.325 0.04 2 670 . 63 LEU CG C 26.210 0.28 1 671 . 63 LEU HG H 0.826 0.04 1 672 . 63 LEU CD1 C 22.505 0.30 1 673 . 63 LEU HD1 H 0.705 0.04 4 674 . 63 LEU CD2 C 22.505 0.30 1 675 . 63 LEU HD2 H 0.705 0.04 4 676 . 63 LEU C C 175.374 0.10 1 677 . 64 ASP N N 121.824 0.04 1 678 . 64 ASP H H 9.540 0.02 1 679 . 64 ASP CA C 51.910 0.24 1 680 . 64 ASP HA H 5.287 0.04 1 681 . 64 ASP CB C 44.630 0.24 1 682 . 64 ASP HB3 H 2.521 0.04 2 683 . 64 ASP HB2 H 2.292 0.04 2 684 . 64 ASP C C 175.260 0.10 1 685 . 65 VAL N N 118.373 0.04 1 686 . 65 VAL H H 8.756 0.02 1 687 . 65 VAL CA C 61.620 0.24 1 688 . 65 VAL HA H 4.422 0.04 1 689 . 65 VAL CB C 31.490 0.24 1 690 . 65 VAL HB H 2.004 0.04 1 691 . 65 VAL CG2 C 20.980 0.30 1 692 . 65 VAL HG2 H 0.833 0.04 2 693 . 65 VAL CG1 C 20.980 0.30 1 694 . 65 VAL HG1 H 0.694 0.04 2 695 . 65 VAL C C 173.459 0.10 1 696 . 66 GLU N N 128.434 0.04 1 697 . 66 GLU H H 9.637 0.02 1 698 . 66 GLU CA C 53.770 0.24 1 699 . 66 GLU HA H 5.106 0.04 1 700 . 66 GLU CB C 33.600 0.24 1 701 . 66 GLU HB3 H 2.236 0.04 1 702 . 66 GLU HB2 H 2.236 0.04 1 703 . 66 GLU CG C 37.722 0.28 1 704 . 66 GLU HG3 H 1.851 0.04 2 705 . 66 GLU HG2 H 1.645 0.04 2 706 . 66 GLU C C 175.295 0.10 1 707 . 67 TRP N N 129.401 0.04 1 708 . 67 TRP H H 9.633 0.02 1 709 . 67 TRP CA C 54.150 0.24 1 710 . 67 TRP HA H 5.287 0.04 1 711 . 67 TRP CB C 29.280 0.24 1 712 . 67 TRP HB3 H 3.562 0.04 2 713 . 67 TRP HB2 H 2.852 0.04 2 714 . 67 TRP NE1 N 127.081 0.20 1 715 . 67 TRP HE1 H 10.026 0.04 3 716 . 67 TRP C C 175.706 0.10 1 717 . 68 ARG N N 130.185 0.04 1 718 . 68 ARG H H 8.637 0.02 1 719 . 68 ARG CA C 54.920 0.24 1 720 . 68 ARG HA H 4.481 0.04 1 721 . 68 ARG CB C 28.050 0.24 1 722 . 68 ARG HB3 H 1.545 0.04 1 723 . 68 ARG HB2 H 1.545 0.04 1 724 . 68 ARG CG C 25.633 0.28 1 725 . 68 ARG HG3 H 0.622 0.04 1 726 . 68 ARG HG2 H 0.622 0.04 1 727 . 68 ARG CD C 42.918 0.28 1 728 . 68 ARG HD3 H 2.748 0.04 1 729 . 68 ARG HD2 H 2.748 0.04 1 730 . 68 ARG C C 175.020 0.10 1 731 . 69 SER N N 118.168 0.04 1 732 . 69 SER H H 7.514 0.02 1 733 . 69 SER CA C 58.050 0.24 1 734 . 69 SER HA H 4.167 0.04 1 735 . 69 SER CB C 63.030 0.24 1 736 . 69 SER HB3 H 3.191 0.04 2 737 . 69 SER HB2 H 2.772 0.04 2 738 . 69 SER C C 174.979 0.10 1 739 . 70 GLY N N 112.506 0.04 1 740 . 70 GLY H H 8.587 0.02 1 741 . 70 GLY CA C 45.130 0.24 1 742 . 70 GLY HA3 H 3.975 0.04 2 743 . 70 GLY HA2 H 3.828 0.04 2 744 . 70 GLY C C 174.771 0.10 1 745 . 71 VAL N N 119.246 0.04 1 746 . 71 VAL H H 8.045 0.02 1 747 . 71 VAL CA C 63.332 0.24 1 748 . 71 VAL HA H 4.063 0.04 1 749 . 71 VAL CB C 31.560 0.24 1 750 . 71 VAL HB H 2.055 0.04 1 751 . 71 VAL CG2 C 19.859 0.30 1 752 . 71 VAL HG2 H 0.953 0.04 4 753 . 71 VAL CG1 C 19.859 0.30 1 754 . 71 VAL HG1 H 0.953 0.04 4 755 . 71 VAL C C 176.568 0.10 1 756 . 72 ALA N N 122.727 0.04 1 757 . 72 ALA H H 8.047 0.02 1 758 . 72 ALA CA C 51.710 0.24 1 759 . 72 ALA HA H 4.325 0.04 1 760 . 72 ALA CB C 18.440 0.24 1 761 . 72 ALA HB H 1.267 0.04 1 762 . 72 ALA C C 177.209 0.10 1 763 . 73 GLY N N 107.031 0.04 1 764 . 73 GLY H H 7.636 0.02 1 765 . 73 GLY CA C 44.440 0.24 1 766 . 73 GLY HA3 H 3.978 0.04 2 767 . 73 GLY HA2 H 3.691 0.04 2 768 . 73 GLY C C 173.559 0.10 1 769 . 74 HIS N N 119.809 0.04 1 770 . 74 HIS H H 8.400 0.02 1 771 . 74 HIS CA C 54.260 0.24 1 772 . 74 HIS HA H 5.092 0.04 1 773 . 74 HIS CB C 29.400 0.24 1 774 . 74 HIS HB3 H 3.127 0.04 2 775 . 74 HIS HB2 H 2.878 0.04 2 776 . 74 HIS C C 174.392 0.10 1 777 . 75 LEU N N 124.921 0.04 1 778 . 75 LEU H H 8.545 0.02 1 779 . 75 LEU CA C 53.860 0.24 1 780 . 75 LEU HA H 4.736 0.04 1 781 . 75 LEU CB C 44.400 0.24 1 782 . 75 LEU HB3 H 1.723 0.04 2 783 . 75 LEU HB2 H 1.545 0.04 2 784 . 75 LEU CG C 25.800 0.28 1 785 . 75 LEU HG H 1.545 0.04 1 786 . 75 LEU CD1 C 23.757 0.30 1 787 . 75 LEU HD1 H 0.956 0.04 4 788 . 75 LEU CD2 C 23.757 0.30 1 789 . 75 LEU HD2 H 0.956 0.04 4 790 . 75 LEU C C 175.370 0.10 1 791 . 76 ILE N N 125.902 0.04 1 792 . 76 ILE H H 8.671 0.02 1 793 . 76 ILE CA C 58.890 0.24 1 794 . 76 ILE HA H 4.734 0.04 1 795 . 76 ILE CB C 35.200 0.24 1 796 . 76 ILE HB H 2.006 0.04 1 797 . 76 ILE CG1 C 26.126 0.30 2 798 . 76 ILE HG13 H 1.548 0.04 9 799 . 76 ILE HG12 H 1.548 0.04 9 800 . 76 ILE CD1 C 9.612 0.30 1 801 . 76 ILE HD1 H 0.814 0.04 1 802 . 76 ILE CG2 C 16.051 0.30 2 803 . 76 ILE HG2 H 0.814 0.04 4 804 . 76 ILE C C 176.284 0.10 1 805 . 77 LEU N N 129.042 0.04 1 806 . 77 LEU H H 8.963 0.02 1 807 . 77 LEU CA C 52.680 0.24 1 808 . 77 LEU HA H 4.281 0.04 1 809 . 77 LEU CB C 40.800 0.24 1 810 . 77 LEU HB3 H 1.573 0.04 1 811 . 77 LEU HB2 H 1.573 0.04 1 812 . 77 LEU CG C 25.044 0.28 1 813 . 77 LEU HG H 0.990 0.04 1 814 . 77 LEU CD1 C 19.029 0.30 2 815 . 77 LEU HD1 H -0.023 0.04 4 816 . 77 LEU CD2 C 23.715 0.30 2 817 . 77 LEU HD2 H 0.480 0.04 4 818 . 77 LEU C C 174.886 0.10 1 819 . 78 SER N N 114.779 0.04 1 820 . 78 SER H H 8.463 0.02 1 821 . 78 SER CA C 56.930 0.24 1 822 . 78 SER HA H 4.725 0.04 1 823 . 78 SER CB C 65.220 0.24 1 824 . 78 SER HB3 H 3.881 0.04 2 825 . 78 SER HB2 H 3.755 0.04 2 826 . 78 SER C C 173.243 0.10 1 827 . 79 ASP N N 122.267 0.04 1 828 . 79 ASP H H 8.814 0.02 1 829 . 79 ASP CA C 57.090 0.24 1 830 . 79 ASP HA H 4.707 0.04 1 831 . 79 ASP CB C 40.400 0.24 1 832 . 79 ASP HB3 H 2.788 0.04 1 833 . 79 ASP HB2 H 2.788 0.04 1 834 . 79 ASP C C 176.925 0.10 1 835 . 80 GLU N N 115.616 0.04 1 836 . 80 GLU H H 7.870 0.02 1 837 . 80 GLU CA C 54.820 0.24 1 838 . 80 GLU HA H 4.651 0.04 1 839 . 80 GLU CB C 32.020 0.24 1 840 . 80 GLU HB3 H 1.896 0.04 1 841 . 80 GLU HB2 H 1.896 0.04 1 842 . 80 GLU CG C 35.970 0.28 1 843 . 80 GLU HG3 H 2.121 0.04 1 844 . 80 GLU HG2 H 2.121 0.04 1 845 . 80 GLU C C 174.289 0.10 1 846 . 81 ASP N N 122.575 0.04 1 847 . 81 ASP H H 8.801 0.02 1 848 . 81 ASP CA C 52.863 0.24 1 849 . 81 ASP HA H 4.718 0.04 1 850 . 81 ASP CB C 41.063 0.24 1 851 . 81 ASP HB3 H 3.281 0.04 2 852 . 81 ASP HB2 H 2.996 0.04 2 853 . 81 ASP C C 177.301 0.10 1 854 . 82 VAL N N 115.895 0.04 1 855 . 82 VAL H H 8.171 0.02 1 856 . 82 VAL CA C 63.770 0.24 1 857 . 82 VAL HA H 4.247 0.04 1 858 . 82 VAL CB C 31.060 0.24 1 859 . 82 VAL HB H 2.365 0.04 1 860 . 82 VAL CG2 C 19.634 0.30 1 861 . 82 VAL HG2 H 1.089 0.04 4 862 . 82 VAL CG1 C 19.634 0.30 1 863 . 82 VAL HG1 H 1.089 0.04 4 864 . 82 VAL C C 176.625 0.10 1 865 . 83 THR N N 112.761 0.04 1 866 . 83 THR H H 8.320 0.02 1 867 . 83 THR CA C 61.910 0.24 1 868 . 83 THR HA H 4.523 0.04 1 869 . 83 THR CB C 69.610 0.24 1 870 . 83 THR HB H 3.959 0.04 1 871 . 83 THR CG2 C 21.030 0.30 1 872 . 83 THR HG2 H 1.369 0.04 1 873 . 83 THR C C 175.571 0.10 1 874 . 84 SER N N 118.812 0.04 1 875 . 84 SER H H 8.069 0.02 1 876 . 84 SER CA C 60.030 0.24 1 877 . 84 SER HA H 3.875 0.04 1 878 . 84 SER CB C 63.380 0.24 1 879 . 84 SER HB3 H 4.090 0.04 2 880 . 84 SER HB2 H 3.900 0.04 2 881 . 84 SER C C 174.082 0.10 1 882 . 85 GLU N N 124.532 0.04 1 883 . 85 GLU H H 8.763 0.02 1 884 . 85 GLU CA C 56.300 0.24 1 885 . 85 GLU HA H 4.369 0.04 1 886 . 85 GLU CB C 29.780 0.24 1 887 . 85 GLU HB3 H 2.032 0.04 1 888 . 85 GLU HB2 H 2.032 0.04 1 889 . 85 GLU CG C 35.672 0.28 1 890 . 85 GLU HG3 H 2.373 0.04 1 891 . 85 GLU HG2 H 2.373 0.04 1 892 . 85 GLU C C 175.836 0.10 1 893 . 86 VAL N N 122.113 0.04 1 894 . 86 VAL H H 8.394 0.02 1 895 . 86 VAL CA C 61.660 0.24 1 896 . 86 VAL HA H 4.329 0.04 1 897 . 86 VAL CB C 32.320 0.24 1 898 . 86 VAL HB H 2.038 0.04 1 899 . 86 VAL CG2 C 20.152 0.30 1 900 . 86 VAL HG2 H 0.921 0.04 4 901 . 86 VAL CG1 C 20.152 0.30 1 902 . 86 VAL HG1 H 0.921 0.04 4 903 . 86 VAL C C 175.983 0.10 1 904 . 87 GLN N N 125.737 0.04 1 905 . 87 GLN H H 8.635 0.02 1 906 . 87 GLN CA C 54.700 0.24 1 907 . 87 GLN HA H 4.504 0.04 1 908 . 87 GLN CB C 29.000 0.24 1 909 . 87 GLN HB3 H 2.071 0.04 2 910 . 87 GLN HB2 H 2.010 0.04 2 911 . 87 GLN CG C 33.036 0.28 1 912 . 87 GLN HG3 H 2.358 0.04 1 913 . 87 GLN HG2 H 2.358 0.04 1 914 . 87 GLN CD C 180.384 0.28 1 915 . 87 GLN NE2 N 111.855 0.20 1 916 . 87 GLN HE21 H 6.888 0.04 2 917 . 87 GLN HE22 H 7.594 0.04 2 918 . 87 GLN C C 175.859 0.10 1 919 . 88 GLY N N 113.634 0.04 1 920 . 88 GLY H H 8.752 0.02 1 921 . 88 GLY CA C 45.840 0.24 1 922 . 88 GLY HA3 H 4.046 0.04 2 923 . 88 GLY HA2 H 3.732 0.04 2 924 . 88 GLY C C 174.248 0.10 1 925 . 89 LEU N N 124.215 0.04 1 926 . 89 LEU H H 8.497 0.02 1 927 . 89 LEU CA C 54.740 0.24 1 928 . 89 LEU HA H 4.209 0.04 1 929 . 89 LEU CB C 41.000 0.24 1 930 . 89 LEU HB3 H 1.316 0.04 1 931 . 89 LEU HB2 H 1.316 0.04 1 932 . 89 LEU CG C 25.847 0.28 1 933 . 89 LEU HG H 1.507 0.04 1 934 . 89 LEU CD1 C 21.903 0.30 2 935 . 89 LEU HD1 H 0.848 0.04 4 936 . 89 LEU CD2 C 23.850 0.30 2 937 . 89 LEU HD2 H 0.844 0.04 4 938 . 89 LEU C C 176.797 0.10 1 939 . 90 PHE N N 118.520 0.04 1 940 . 90 PHE H H 7.946 0.02 1 941 . 90 PHE CA C 56.560 0.24 1 942 . 90 PHE HA H 4.826 0.04 1 943 . 90 PHE CB C 39.950 0.24 1 944 . 90 PHE HB3 H 3.220 0.04 2 945 . 90 PHE HB2 H 3.025 0.04 2 946 . 90 PHE HD1 H 7.137 0.04 2 947 . 90 PHE HE1 H 7.388 0.04 2 948 . 90 PHE HZ H 7.245 0.04 1 949 . 90 PHE C C 174.590 0.10 1 950 . 91 ARG N N 123.297 0.04 1 951 . 91 ARG H H 8.404 0.02 1 952 . 91 ARG CA C 54.700 0.24 1 953 . 91 ARG HA H 4.566 0.04 1 954 . 91 ARG CB C 30.260 0.24 1 955 . 91 ARG HB3 H 1.722 0.04 1 956 . 91 ARG HB2 H 1.722 0.04 1 957 . 91 ARG CG C 26.238 0.28 1 958 . 91 ARG HG3 H 1.547 0.04 1 959 . 91 ARG HG2 H 1.547 0.04 1 960 . 91 ARG CD C 42.688 0.28 1 961 . 91 ARG HD3 H 3.168 0.04 1 962 . 91 ARG HD2 H 3.168 0.04 1 963 . 91 ARG C C 175.488 0.10 1 964 . 92 ARG N N 124.534 0.04 1 965 . 92 ARG H H 8.541 0.02 1 966 . 92 ARG CA C 54.750 0.24 1 967 . 92 ARG HA H 4.400 0.04 1 968 . 92 ARG CB C 30.260 0.24 1 969 . 92 ARG HB3 H 1.759 0.04 1 970 . 92 ARG HB2 H 1.759 0.04 1 971 . 92 ARG CG C 25.965 0.28 1 972 . 92 ARG HG3 H 1.623 0.04 1 973 . 92 ARG HG2 H 1.623 0.04 1 974 . 92 ARG CD C 42.889 0.28 1 975 . 92 ARG HD3 H 3.226 0.04 1 976 . 92 ARG HD2 H 3.226 0.04 1 977 . 92 ARG C C 176.807 0.10 1 978 . 93 LEU N N 125.952 0.04 1 979 . 93 LEU H H 8.583 0.02 1 980 . 93 LEU CA C 54.730 0.24 1 981 . 93 LEU HA H 4.416 0.04 1 982 . 93 LEU CB C 40.860 0.24 1 983 . 93 LEU HB3 H 1.761 0.04 1 984 . 93 LEU HB2 H 1.761 0.04 1 985 . 93 LEU CG C 26.429 0.28 1 986 . 93 LEU HG H 1.356 0.04 1 987 . 93 LEU CD1 C 21.942 0.30 2 988 . 93 LEU HD1 H 0.876 0.04 4 989 . 93 LEU CD2 C 24.615 0.30 2 990 . 93 LEU HD2 H 0.990 0.04 4 991 . 93 LEU C C 177.632 0.10 1 992 . 94 ASN N N 122.701 0.04 1 993 . 94 ASN H H 9.760 0.02 1 994 . 94 ASN CA C 53.360 0.24 1 995 . 94 ASN HA H 4.114 0.04 1 996 . 94 ASN CB C 37.170 0.24 1 997 . 94 ASN HB3 H 3.774 0.04 2 998 . 94 ASN HB2 H 2.428 0.04 2 999 . 94 ASN CG C 175.502 0.28 1 1000 . 94 ASN ND2 N 109.235 0.20 1 1001 . 94 ASN HD21 H 6.036 0.04 2 1002 . 94 ASN HD22 H 7.430 0.04 2 1003 . 94 ASN C C 173.967 0.10 1 1004 . 95 THR N N 107.721 0.04 1 1005 . 95 THR H H 6.643 0.02 1 1006 . 95 THR CA C 58.240 0.24 1 1007 . 95 THR HA H 5.281 0.04 1 1008 . 95 THR CB C 72.570 0.24 1 1009 . 95 THR HB H 4.688 0.04 1 1010 . 95 THR CG2 C 21.090 0.30 1 1011 . 95 THR HG2 H 1.114 0.04 1 1012 . 95 THR C C 176.477 0.10 1 1013 . 96 LEU N N 118.751 0.04 1 1014 . 96 LEU H H 7.804 0.02 1 1015 . 96 LEU CA C 58.380 0.24 1 1016 . 96 LEU HA H 4.072 0.04 1 1017 . 96 LEU CB C 39.284 0.24 1 1018 . 96 LEU HB3 H 2.102 0.04 2 1019 . 96 LEU HB2 H 1.106 0.04 2 1020 . 96 LEU CG C 26.288 0.28 1 1021 . 96 LEU HG H 1.618 0.04 1 1022 . 96 LEU CD1 C 21.143 0.30 1 1023 . 96 LEU HD1 H 0.508 0.04 4 1024 . 96 LEU CD2 C 21.143 0.30 1 1025 . 96 LEU HD2 H 0.850 0.04 2 1026 . 96 LEU C C 179.891 0.10 1 1027 . 97 GLN N N 119.811 0.04 1 1028 . 97 GLN H H 8.663 0.02 1 1029 . 97 GLN CA C 58.350 0.24 1 1030 . 97 GLN HA H 4.187 0.04 1 1031 . 97 GLN CB C 27.610 0.24 1 1032 . 97 GLN HB3 H 1.947 0.04 1 1033 . 97 GLN HB2 H 1.947 0.04 1 1034 . 97 GLN CG C 33.036 0.28 1 1035 . 97 GLN HG3 H 2.416 0.04 2 1036 . 97 GLN HG2 H 2.277 0.04 2 1037 . 97 GLN CD C 179.944 0.28 1 1038 . 97 GLN NE2 N 111.367 0.20 1 1039 . 97 GLN HE21 H 6.793 0.04 2 1040 . 97 GLN HE22 H 7.492 0.04 2 1041 . 97 GLN C C 179.342 0.10 1 1042 . 98 HIS N N 121.347 0.04 1 1043 . 98 HIS H H 8.044 0.02 1 1044 . 98 HIS CA C 59.500 0.24 1 1045 . 98 HIS HA H 4.152 0.04 1 1046 . 98 HIS CB C 28.560 0.24 1 1047 . 98 HIS HB3 H 3.660 0.04 2 1048 . 98 HIS HB2 H 3.417 0.04 2 1049 . 98 HIS C C 176.489 0.10 1 1050 . 99 TYR N N 113.843 0.04 1 1051 . 99 TYR H H 7.090 0.02 1 1052 . 99 TYR CA C 59.240 0.24 1 1053 . 99 TYR HA H 4.284 0.04 1 1054 . 99 TYR CB C 39.980 0.24 1 1055 . 99 TYR HB3 H 3.351 0.04 2 1056 . 99 TYR HB2 H 2.539 0.04 2 1057 . 99 TYR C C 173.476 0.10 1 1058 . 100 LYS N N 113.743 0.04 1 1059 . 100 LYS H H 7.862 0.02 1 1060 . 100 LYS CA C 56.330 0.24 1 1061 . 100 LYS HA H 3.821 0.04 1 1062 . 100 LYS CB C 27.690 0.24 1 1063 . 100 LYS HB3 H 2.300 0.04 1 1064 . 100 LYS HB2 H 2.300 0.04 1 1065 . 100 LYS CG C 23.708 0.28 1 1066 . 100 LYS HG3 H 1.363 0.04 1 1067 . 100 LYS HG2 H 1.363 0.04 1 1068 . 100 LYS CD C 28.432 0.28 1 1069 . 100 LYS HD3 H 1.844 0.04 2 1070 . 100 LYS HD2 H 1.697 0.04 2 1071 . 100 LYS CE C 41.871 0.28 1 1072 . 100 LYS HE3 H 3.041 0.04 1 1073 . 100 LYS HE2 H 3.041 0.04 1 1074 . 100 LYS C C 176.147 0.10 1 1075 . 101 VAL N N 120.730 0.04 1 1076 . 101 VAL H H 6.860 0.02 1 1077 . 101 VAL CA C 60.400 0.24 1 1078 . 101 VAL HA H 2.921 0.04 1 1079 . 101 VAL CB C 31.010 0.24 1 1080 . 101 VAL HB H 1.228 0.04 1 1081 . 101 VAL CG2 C 20.482 0.30 2 1082 . 101 VAL HG2 H -0.111 0.04 4 1083 . 101 VAL CG1 C 19.340 0.30 2 1084 . 101 VAL HG1 H 0.034 0.04 4 1085 . 101 VAL C C 176.147 0.10 1 1086 . 102 PRO CA C 61.321 0.24 1 1087 . 102 PRO HA H 4.602 0.04 1 1088 . 102 PRO CB C 31.378 0.24 1 1089 . 102 PRO HB3 H 2.241 0.04 1 1090 . 102 PRO HB2 H 2.241 0.04 1 1091 . 102 PRO CG C 26.082 0.28 1 1092 . 102 PRO HG3 H 2.057 0.04 1 1093 . 102 PRO HG2 H 2.057 0.04 1 1094 . 102 PRO CD C 50.755 0.28 1 1095 . 102 PRO HD3 H 4.273 0.04 1 1096 . 102 PRO HD2 H 4.273 0.04 1 1097 . 102 PRO C C 175.612 0.10 1 1098 . 103 ASP N N 116.210 0.04 1 1099 . 103 ASP H H 8.242 0.02 1 1100 . 103 ASP CA C 55.660 0.24 1 1101 . 103 ASP HA H 4.318 0.04 1 1102 . 103 ASP CB C 40.330 0.24 1 1103 . 103 ASP HB3 H 2.634 0.04 1 1104 . 103 ASP HB2 H 2.634 0.04 1 1105 . 103 ASP C C 178.453 0.10 1 1106 . 104 GLY N N 115.149 0.04 1 1107 . 104 GLY H H 8.871 0.02 1 1108 . 104 GLY CA C 45.070 0.24 1 1109 . 104 GLY HA3 H 4.173 0.04 2 1110 . 104 GLY HA2 H 3.692 0.04 2 1111 . 104 GLY C C 174.277 0.10 1 1112 . 105 ALA N N 121.755 0.04 1 1113 . 105 ALA H H 7.512 0.02 1 1114 . 105 ALA CA C 52.550 0.24 1 1115 . 105 ALA HA H 4.249 0.04 1 1116 . 105 ALA CB C 19.550 0.24 1 1117 . 105 ALA HB H 1.364 0.04 1 1118 . 105 ALA C C 176.206 0.10 1 1119 . 106 THR N N 118.381 0.04 1 1120 . 106 THR H H 9.118 0.02 1 1121 . 106 THR CA C 62.200 0.24 1 1122 . 106 THR HA H 5.384 0.04 1 1123 . 106 THR CB C 68.670 0.24 1 1124 . 106 THR HB H 4.296 0.04 1 1125 . 106 THR CG2 C 20.824 0.30 1 1126 . 106 THR HG2 H 1.218 0.04 1 1127 . 106 THR C C 174.114 0.10 1 1128 . 107 VAL N N 124.759 0.04 1 1129 . 107 VAL H H 8.730 0.02 1 1130 . 107 VAL CA C 58.491 0.24 1 1131 . 107 VAL HA H 5.251 0.04 1 1132 . 107 VAL CB C 34.090 0.24 1 1133 . 107 VAL HB H 1.806 0.04 1 1134 . 107 VAL CG2 C 19.603 0.30 2 1135 . 107 VAL HG2 H 0.744 0.04 4 1136 . 107 VAL CG1 C 21.448 0.30 2 1137 . 107 VAL HG1 H 0.744 0.04 4 1138 . 107 VAL C C 172.822 0.10 1 1139 . 108 ALA N N 125.225 0.04 1 1140 . 108 ALA H H 9.629 0.02 1 1141 . 108 ALA CA C 48.694 0.24 1 1142 . 108 ALA HA H 5.488 0.04 1 1143 . 108 ALA CB C 21.380 0.24 1 1144 . 108 ALA HB H 1.125 0.04 1 1145 . 108 ALA C C 176.349 0.10 1 1146 . 109 LEU N N 120.521 0.04 1 1147 . 109 LEU H H 8.478 0.02 1 1148 . 109 LEU CA C 52.780 0.24 1 1149 . 109 LEU HA H 5.449 0.04 1 1150 . 109 LEU CB C 40.990 0.24 1 1151 . 109 LEU HB3 H 1.905 0.04 2 1152 . 109 LEU HB2 H 1.363 0.04 2 1153 . 109 LEU CG C 26.942 0.28 1 1154 . 109 LEU HG H 1.714 0.04 1 1155 . 109 LEU CD1 C 25.923 0.30 2 1156 . 109 LEU HD1 H 0.915 0.04 4 1157 . 109 LEU CD2 C 24.231 0.30 2 1158 . 109 LEU HD2 H 0.915 0.04 4 1159 . 109 LEU C C 175.404 0.10 1 1160 . 110 VAL N N 116.452 0.04 1 1161 . 110 VAL H H 8.670 0.02 1 1162 . 110 VAL CA C 56.600 0.24 1 1163 . 110 VAL HA H 4.943 0.04 1 1164 . 110 VAL CB C 32.300 0.24 1 1165 . 110 VAL HB H 2.250 0.04 1 1166 . 110 VAL CG2 C 18.196 0.30 1 1167 . 110 VAL HG2 H 0.702 0.04 2 1168 . 110 VAL CG1 C 21.333 0.30 1 1169 . 110 VAL HG1 H 0.845 0.04 2 1170 . 110 VAL C C 175.404 0.10 1 1171 . 111 PRO CA C 63.372 0.24 1 1172 . 111 PRO HA H 4.607 0.04 1 1173 . 111 PRO CB C 31.126 0.24 1 1174 . 111 PRO HB3 H 2.436 0.04 2 1175 . 111 PRO HB2 H 2.256 0.04 2 1176 . 111 PRO CG C 27.587 0.28 1 1177 . 111 PRO HG3 H 1.834 0.04 2 1178 . 111 PRO HG2 H 1.987 0.04 2 1179 . 111 PRO CD C 49.666 0.28 1 1180 . 111 PRO HD3 H 4.357 0.04 1 1181 . 111 PRO HD2 H 4.357 0.04 1 1182 . 111 PRO C C 177.192 0.10 1 1183 . 112 CYS N N 121.780 0.04 1 1184 . 112 CYS H H 8.278 0.02 1 1185 . 112 CYS CA C 58.230 0.24 1 1186 . 112 CYS HA H 4.479 0.04 1 1187 . 112 CYS CB C 26.790 0.24 1 1188 . 112 CYS HB3 H 2.604 0.04 1 1189 . 112 CYS HB2 H 2.604 0.04 1 1190 . 112 CYS C C 175.288 0.10 1 1191 . 113 LEU N N 126.976 0.04 1 1192 . 113 LEU H H 8.687 0.02 1 1193 . 113 LEU CA C 55.020 0.24 1 1194 . 113 LEU HA H 4.422 0.04 1 1195 . 113 LEU CB C 41.190 0.24 1 1196 . 113 LEU HB3 H 1.704 0.04 1 1197 . 113 LEU HB2 H 1.704 0.04 1 1198 . 113 LEU CG C 26.068 0.28 1 1199 . 113 LEU HG H 1.704 0.04 1 1200 . 113 LEU CD1 C 22.459 0.30 2 1201 . 113 LEU HD1 H 0.872 0.04 4 1202 . 113 LEU CD2 C 24.170 0.30 2 1203 . 113 LEU HD2 H 0.953 0.04 4 1204 . 113 LEU C C 177.704 0.10 1 1205 . 114 THR N N 115.028 0.04 1 1206 . 114 THR H H 8.062 0.02 1 1207 . 114 THR CA C 61.880 0.24 1 1208 . 114 THR HA H 4.279 0.04 1 1209 . 114 THR CB C 69.130 0.24 1 1210 . 114 THR HB H 4.151 0.04 1 1211 . 114 THR CG2 C 20.738 0.30 1 1212 . 114 THR HG2 H 1.178 0.04 1 1213 . 114 THR C C 174.172 0.10 1 1214 . 115 LYS N N 123.814 0.04 1 1215 . 115 LYS H H 8.275 0.02 1 1216 . 115 LYS CA C 55.650 0.24 1 1217 . 115 LYS HA H 4.318 0.04 1 1218 . 115 LYS CB C 32.050 0.24 1 1219 . 115 LYS HB3 H 1.730 0.04 1 1220 . 115 LYS HB2 H 1.730 0.04 1 1221 . 115 LYS CG C 23.690 0.28 1 1222 . 115 LYS HG3 H 1.363 0.04 1 1223 . 115 LYS HG2 H 1.363 0.04 1 1224 . 115 LYS CD C 28.210 0.28 1 1225 . 115 LYS HD3 H 1.730 0.04 1 1226 . 115 LYS HD2 H 1.730 0.04 1 1227 . 115 LYS CE C 41.525 0.28 1 1228 . 115 LYS HE3 H 3.008 0.04 1 1229 . 115 LYS HE2 H 3.008 0.04 1 1230 . 115 LYS C C 176.112 0.10 1 1231 . 116 HIS N N 121.214 0.04 1 1232 . 116 HIS H H 8.434 0.02 1 1233 . 116 HIS CA C 55.490 0.24 1 1234 . 116 HIS HA H 4.676 0.04 1 1235 . 116 HIS CB C 29.588 0.24 1 1236 . 116 HIS HB3 H 3.124 0.04 2 1237 . 116 HIS HB2 H 3.071 0.04 2 1238 . 116 HIS C C 174.982 0.10 1 1239 . 117 VAL N N 121.938 0.04 1 1240 . 117 VAL H H 8.193 0.02 1 1241 . 117 VAL CA C 61.880 0.24 1 1242 . 117 VAL HA H 4.101 0.04 1 1243 . 117 VAL CB C 31.960 0.24 1 1244 . 117 VAL HB H 2.048 0.04 1 1245 . 117 VAL CG2 C 19.859 0.30 1 1246 . 117 VAL HG2 H 0.923 0.04 4 1247 . 117 VAL CG1 C 19.859 0.30 1 1248 . 117 VAL HG1 H 0.923 0.04 4 1249 . 117 VAL C C 175.791 0.10 1 1250 . 118 LEU N N 126.291 0.04 1 1251 . 118 LEU H H 8.417 0.02 1 1252 . 118 LEU CA C 54.630 0.24 1 1253 . 118 LEU HA H 4.402 0.04 1 1254 . 118 LEU CB C 41.210 0.24 1 1255 . 118 LEU HB3 H 1.631 0.04 1 1256 . 118 LEU HB2 H 1.631 0.04 1 1257 . 118 LEU CG C 25.895 0.28 1 1258 . 118 LEU HG H 1.631 0.04 1 1259 . 118 LEU CD1 C 22.620 0.30 2 1260 . 118 LEU HD1 H 0.863 0.04 4 1261 . 118 LEU CD2 C 24.140 0.30 2 1262 . 118 LEU HD2 H 0.952 0.04 4 1263 . 118 LEU C C 177.073 0.10 1 1264 . 119 ARG N N 122.505 0.04 1 1265 . 119 ARG H H 8.412 0.02 1 1266 . 119 ARG CA C 55.720 0.24 1 1267 . 119 ARG HA H 4.368 0.04 1 1268 . 119 ARG CB C 29.960 0.24 1 1269 . 119 ARG HB3 H 1.832 0.04 1 1270 . 119 ARG HB2 H 1.832 0.04 1 1271 . 119 ARG CG C 26.009 0.28 1 1272 . 119 ARG HG3 H 1.646 0.04 1 1273 . 119 ARG HG2 H 1.646 0.04 1 1274 . 119 ARG CD C 42.700 0.28 1 1275 . 119 ARG HD3 H 3.222 0.04 1 1276 . 119 ARG HD2 H 3.222 0.04 1 1277 . 119 ARG C C 176.170 0.10 1 1278 . 120 GLU N N 121.690 0.04 1 1279 . 120 GLU H H 8.594 0.02 1 1280 . 120 GLU CA C 56.480 0.24 1 1281 . 120 GLU HA H 4.318 0.04 1 1282 . 120 GLU CB C 29.490 0.24 1 1283 . 120 GLU HB3 H 2.074 0.04 2 1284 . 120 GLU HB2 H 1.954 0.04 2 1285 . 120 GLU CG C 35.703 0.28 1 1286 . 120 GLU HG3 H 2.274 0.04 1 1287 . 120 GLU HG2 H 2.274 0.04 1 1288 . 120 GLU C C 176.210 0.10 1 1289 . 121 ASN N N 119.064 0.04 1 1290 . 121 ASN H H 8.544 0.02 1 1291 . 121 ASN CA C 53.030 0.24 1 1292 . 121 ASN HA H 4.718 0.04 1 1293 . 121 ASN CB C 38.300 0.24 1 1294 . 121 ASN HB3 H 2.864 0.04 2 1295 . 121 ASN HB2 H 2.731 0.04 2 1296 . 121 ASN CG C 177.407 0.28 1 1297 . 121 ASN ND2 N 113.080 0.20 1 1298 . 121 ASN HD21 H 6.947 0.04 2 1299 . 121 ASN HD22 H 7.660 0.04 2 1300 . 121 ASN C C 174.176 0.10 1 1301 . 122 GLN N N 124.833 0.04 1 1302 . 122 GLN H H 7.944 0.02 1 1303 . 122 GLN CA C 56.964 0.24 1 1304 . 122 GLN HA H 4.150 0.04 1 1305 . 122 GLN CB C 29.490 0.24 1 1306 . 122 GLN HB3 H 2.095 0.04 2 1307 . 122 GLN HB2 H 1.928 0.04 2 1308 . 122 GLN CG C 33.551 0.28 1 1309 . 122 GLN HG3 H 2.259 0.04 1 1310 . 122 GLN HG2 H 2.259 0.04 1 1311 . 122 GLN CD C 181.164 0.28 1 1312 . 122 GLN NE2 N 112.249 0.20 1 1313 . 122 GLN HE21 H 7.553 0.04 2 1314 . 122 GLN HE22 H 7.199 0.04 2 stop_ save_