data_5366 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF THE VAM7P PX DOMAIN ; _BMRB_accession_number 5366 _BMRB_flat_file_name bmr5366.str _Entry_type original _Submission_date 2002-05-08 _Accession_date 2002-05-08 _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 Lu J. . . 2 Garcia . J . 3 Dulubova I. . . 4 Sudhof T. C. . 5 Rizo J. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 791 "13C chemical shifts" 575 "15N chemical shifts" 127 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-25 original author . stop_ _Original_release_date 2003-02-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of the Vam7P PX Domain' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21989951 _PubMed_ID 11993989 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu J. . . 2 Garcia J. J. . 3 Dulubova I. . . 4 Sudhof T. C. . 5 Rizo J. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 19 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5956 _Page_last 5962 _Year 2002 _Details . loop_ _Keyword 'phosphoinositide binding' 'PX domain' Vam7p stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Lu J., Garcia J., Dulubova I, Sudhof TC, Rizo J. Solution structure of the Vam7p PX Domain Biochemistry, 2002 May 14:41(19):5956-62 ; _Citation_title 'Solution structure of the Vam7p PX domain.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11993989 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lu Jun . . 2 Garcia Jesus . . 3 Dulubova Irina . . 4 Sudhof 'Thomas C' C. . 5 Rizo Josep . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 41 _Journal_issue 19 _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 5956 _Page_last 5962 _Year 2002 _Details ; PX domains have been recently found to act as phosphoinositide binding modules. In the yeast SNARE protein Vam7p, the PX domain binds to PtdIns(3)P and is required for vacuolar targeting. To gain insight into how PX domains function, the solution structure of the ligand-free Vam7p PX domain has been determined by NMR spectroscopy. The Vam7p PX domain has the same overall alpha/beta fold observed in the structures of the ligand-free p47(phox) PX domain and the PtdIns(3)P-bound p40(phox) PX domain, exhibiting several similarities and differences with these two PX domains. Most striking is the similarity between the Vam7p and p40(phox) PX domains in a subset of secondary structure elements despite the low level of sequence identity between them, suggesting that these elements form a conserved core in the PX domain fold. These similarities and the observation that a putative PtdIns(3)P binding site is already formed in the apo Vam7p PX domains suggest that ligand binding does not induce major conformational changes, contrary to what was previously thought. The proposed ligand binding site of the Vam7p PX domain includes basic side chains from the conserved structural core that also participate in PtdIns(3)P binding to the p40(phox) PX domain, and basic side chains from a variable loop that probably inserts into the membrane. These results indicate that PX domains contain a combination of conserved and variable features that allow them to have a common function and at the same time exhibit distinct specificities, mechanisms of regulation, or modes of interaction with effector molecules. ; save_ ################################## # Molecular system description # ################################## save_system_Vam7P _Saveframe_category molecular_system _Mol_system_name 'Vacuolar morphogenesis protein' _Abbreviation_common Vam7P _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Vacuolar morphogenesis protein' $Vam7P stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Vam7P _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common vam7p _Abbreviation_common vam7p _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; KMSEKLRKMSEKLRIKVDDV KINPKYVLYGVSTPNKRLYK RYSEFWKLKTRLERDVGSTI PYDFPEKPGVLDRRWQRRYD DPEMIDERRIGLERFLNELY NDRFDSRWRDTKIAQDFLQL SKPN ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 MET 3 SER 4 GLU 5 LYS 6 LEU 7 ARG 8 LYS 9 MET 10 SER 11 GLU 12 LYS 13 LEU 14 ARG 15 ILE 16 LYS 17 VAL 18 ASP 19 ASP 20 VAL 21 LYS 22 ILE 23 ASN 24 PRO 25 LYS 26 TYR 27 VAL 28 LEU 29 TYR 30 GLY 31 VAL 32 SER 33 THR 34 PRO 35 ASN 36 LYS 37 ARG 38 LEU 39 TYR 40 LYS 41 ARG 42 TYR 43 SER 44 GLU 45 PHE 46 TRP 47 LYS 48 LEU 49 LYS 50 THR 51 ARG 52 LEU 53 GLU 54 ARG 55 ASP 56 VAL 57 GLY 58 SER 59 THR 60 ILE 61 PRO 62 TYR 63 ASP 64 PHE 65 PRO 66 GLU 67 LYS 68 PRO 69 GLY 70 VAL 71 LEU 72 ASP 73 ARG 74 ARG 75 TRP 76 GLN 77 ARG 78 ARG 79 TYR 80 ASP 81 ASP 82 PRO 83 GLU 84 MET 85 ILE 86 ASP 87 GLU 88 ARG 89 ARG 90 ILE 91 GLY 92 LEU 93 GLU 94 ARG 95 PHE 96 LEU 97 ASN 98 GLU 99 LEU 100 TYR 101 ASN 102 ASP 103 ARG 104 PHE 105 ASP 106 SER 107 ARG 108 TRP 109 ARG 110 ASP 111 THR 112 LYS 113 ILE 114 ALA 115 GLN 116 ASP 117 PHE 118 LEU 119 GLN 120 LEU 121 SER 122 LYS 123 PRO 124 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-10-26 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 1KMD "Solution Structure Of The Vam7p Px Domain" 94.35 117 100.00 100.00 5.37e-77 GB EGA86963 "Vam7p [Saccharomyces cerevisiae VL3]" 93.55 308 99.14 99.14 4.87e-77 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Vam7P 'baker's yeast' 4932 Eukaryota . Saccharomyces cerevisiae 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 $Vam7P '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 $Vam7P 0.5 mM [U-15N] 'Mes buffer' 20 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Vam7P 0.5 mM '[U-15N; U-13C]' 'Mes buffer' 20 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Vam7P 0.5 mM [U-15N] 'Mes buffer' 20 mM . D2O 100 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Vam7P 0.5 mM '[U-10% 13C]' 'Mes buffer' 20 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task processing stop_ _Details 'DeLaglio, F. et al.' save_ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1 loop_ _Task collection stop_ _Details Varian save_ save_NMRView _Saveframe_category software _Name NMRView _Version 4.1.2 loop_ _Task 'data analysis' stop_ _Details 'Johnson, B. and Blevins R.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task refinement stop_ _Details 'Brunger, A.T. et al.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 6.2 0.2 n/a pressure 1 . atm temperature 298 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Vacuolar morphogenesis protein' _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 . 8 LYS N N 123.503 0.15 1 2 . 8 LYS H H 8.366 0.03 1 3 . 8 LYS CA C 56.563 0.12 1 4 . 8 LYS HA H 4.275 0.03 1 5 . 8 LYS CB C 33.449 0.12 1 6 . 8 LYS HB2 H 1.790 0.03 1 7 . 8 LYS HB3 H 1.790 0.03 1 8 . 8 LYS CG C 25.126 0.12 1 9 . 8 LYS HG2 H 1.431 0.03 2 10 . 8 LYS HG3 H 1.382 0.03 2 11 . 8 LYS CD C 29.405 0.12 1 12 . 8 LYS HD2 H 1.620 0.03 1 13 . 8 LYS HD3 H 1.620 0.03 1 14 . 8 LYS CE C 42.441 0.12 1 15 . 8 LYS HE2 H 2.960 0.03 1 16 . 8 LYS HE3 H 2.960 0.03 1 17 . 8 LYS C C 174.577 0.12 1 18 . 9 MET N N 122.457 0.15 1 19 . 9 MET H H 8.503 0.03 1 20 . 9 MET CA C 55.884 0.12 1 21 . 9 MET HA H 4.463 0.03 1 22 . 9 MET CB C 33.311 0.12 1 23 . 9 MET HB2 H 2.065 0.03 2 24 . 9 MET HB3 H 1.985 0.03 2 25 . 9 MET CG C 32.565 0.12 1 26 . 9 MET HG2 H 2.592 0.03 2 27 . 9 MET HG3 H 2.520 0.03 2 28 . 9 MET CE C 17.481 0.12 1 29 . 9 MET HE H 2.072 0.03 1 30 . 9 MET C C 174.210 0.12 1 31 . 10 SER N N 117.245 0.15 1 32 . 10 SER H H 8.349 0.03 1 33 . 10 SER CA C 58.636 0.12 1 34 . 10 SER HA H 4.408 0.03 1 35 . 10 SER CB C 64.194 0.12 1 36 . 10 SER HB2 H 3.840 0.03 1 37 . 10 SER HB3 H 3.840 0.03 1 38 . 10 SER C C 172.247 0.12 1 39 . 11 GLU N N 123.041 0.15 1 40 . 11 GLU H H 8.376 0.03 1 41 . 11 GLU CA C 56.442 0.12 1 42 . 11 GLU HA H 4.273 0.03 1 43 . 11 GLU CB C 30.977 0.12 1 44 . 11 GLU HB2 H 2.009 0.03 2 45 . 11 GLU HB3 H 1.909 0.03 2 46 . 11 GLU CG C 36.501 0.12 1 47 . 11 GLU HG2 H 2.230 0.03 1 48 . 11 GLU HG3 H 2.230 0.03 1 49 . 11 GLU C C 174.187 0.12 1 50 . 12 LYS N N 122.908 0.15 1 51 . 12 LYS H H 8.328 0.03 1 52 . 12 LYS CA C 56.908 0.12 1 53 . 12 LYS HA H 4.207 0.03 1 54 . 12 LYS CB C 33.630 0.12 1 55 . 12 LYS HB2 H 1.670 0.03 1 56 . 12 LYS HB3 H 1.670 0.03 1 57 . 12 LYS CG C 25.455 0.12 1 58 . 12 LYS HG2 H 1.382 0.03 2 59 . 12 LYS HG3 H 1.302 0.03 2 60 . 12 LYS CD C 29.537 0.12 1 61 . 12 LYS HD2 H 1.615 0.03 1 62 . 12 LYS HD3 H 1.615 0.03 1 63 . 12 LYS CE C 42.638 0.12 1 64 . 12 LYS HE2 H 2.937 0.03 1 65 . 12 LYS HE3 H 2.937 0.03 1 66 . 12 LYS C C 174.045 0.12 1 67 . 13 LEU N N 126.488 0.15 1 68 . 13 LEU H H 9.122 0.03 1 69 . 13 LEU CA C 54.516 0.12 1 70 . 13 LEU HA H 4.388 0.03 1 71 . 13 LEU CB C 43.628 0.12 1 72 . 13 LEU HB2 H 1.540 0.03 2 73 . 13 LEU HB3 H 1.400 0.03 2 74 . 13 LEU CG C 27.693 0.12 1 75 . 13 LEU HG H 1.350 0.03 1 76 . 13 LEU CD1 C 24.599 0.12 1 77 . 13 LEU HD1 H 0.824 0.03 1 78 . 13 LEU CD2 C 25.850 0.12 1 79 . 13 LEU HD2 H 0.690 0.03 1 80 . 13 LEU C C 173.146 0.12 1 81 . 14 ARG N N 126.967 0.15 1 82 . 14 ARG H H 8.242 0.03 1 83 . 14 ARG CA C 56.310 0.12 1 84 . 14 ARG HA H 4.303 0.03 1 85 . 14 ARG CB C 30.148 0.12 1 86 . 14 ARG HB2 H 1.690 0.03 2 87 . 14 ARG HB3 H 1.623 0.03 2 88 . 14 ARG CG C 27.693 0.12 1 89 . 14 ARG HG2 H 1.520 0.03 2 90 . 14 ARG HG3 H 1.390 0.03 2 91 . 14 ARG CD C 43.692 0.12 1 92 . 14 ARG HD2 H 3.110 0.03 1 93 . 14 ARG HD3 H 3.110 0.03 1 94 . 14 ARG C C 172.815 0.12 1 95 . 15 ILE N N 127.640 0.15 1 96 . 15 ILE H H 8.297 0.03 1 97 . 15 ILE CA C 60.224 0.12 1 98 . 15 ILE HA H 4.638 0.03 1 99 . 15 ILE CB C 40.432 0.12 1 100 . 15 ILE HB H 1.420 0.03 1 101 . 15 ILE CG1 C 28.747 0.12 1 102 . 15 ILE HG12 H 1.359 0.03 2 103 . 15 ILE HG13 H 0.620 0.03 2 104 . 15 ILE CD1 C 15.843 0.12 1 105 . 15 ILE HD1 H 0.480 0.03 1 106 . 15 ILE CG2 C 19.220 0.12 1 107 . 15 ILE HG2 H 0.703 0.03 1 108 . 15 ILE C C 173.879 0.12 1 109 . 16 LYS N N 126.513 0.15 1 110 . 16 LYS H H 8.607 0.03 1 111 . 16 LYS CA C 53.992 0.12 1 112 . 16 LYS HA H 4.790 0.03 1 113 . 16 LYS CB C 36.116 0.12 1 114 . 16 LYS HB2 H 1.710 0.03 2 115 . 16 LYS HB3 H 1.550 0.03 2 116 . 16 LYS CG C 24.731 0.12 1 117 . 16 LYS HG2 H 1.300 0.03 2 118 . 16 LYS HG3 H 1.242 0.03 2 119 . 16 LYS CD C 28.944 0.12 1 120 . 16 LYS HD2 H 1.611 0.03 1 121 . 16 LYS HD3 H 1.611 0.03 1 122 . 16 LYS CE C 42.112 0.12 1 123 . 16 LYS HE2 H 2.935 0.03 2 124 . 16 LYS HE3 H 2.847 0.03 2 125 . 16 LYS C C 173.702 0.12 1 126 . 17 VAL N N 125.895 0.15 1 127 . 17 VAL H H 9.906 0.03 1 128 . 17 VAL CA C 61.421 0.12 1 129 . 17 VAL HA H 5.282 0.03 1 130 . 17 VAL CB C 30.644 0.12 1 131 . 17 VAL HB H 2.306 0.03 1 132 . 17 VAL CG2 C 21.138 0.12 1 133 . 17 VAL HG2 H 0.847 0.03 1 134 . 17 VAL CG1 C 23.830 0.12 1 135 . 17 VAL HG1 H 1.082 0.03 1 136 . 17 VAL C C 173.382 0.12 1 137 . 18 ASP N N 122.046 0.15 1 138 . 18 ASP H H 8.278 0.03 1 139 . 18 ASP CA C 53.651 0.12 1 140 . 18 ASP HA H 4.705 0.03 1 141 . 18 ASP CB C 41.528 0.12 1 142 . 18 ASP HB2 H 2.947 0.03 2 143 . 18 ASP HB3 H 2.382 0.03 2 144 . 18 ASP C C 173.643 0.12 1 145 . 19 ASP N N 116.786 0.15 1 146 . 19 ASP H H 7.809 0.03 1 147 . 19 ASP CA C 54.536 0.12 1 148 . 19 ASP HA H 4.977 0.03 1 149 . 19 ASP CB C 45.273 0.12 1 150 . 19 ASP HB2 H 2.263 0.03 2 151 . 19 ASP HB3 H 2.659 0.03 2 152 . 19 ASP C C 172.117 0.12 1 153 . 20 VAL N N 121.355 0.15 1 154 . 20 VAL H H 7.969 0.03 1 155 . 20 VAL CA C 61.599 0.12 1 156 . 20 VAL HA H 4.827 0.03 1 157 . 20 VAL CB C 35.793 0.12 1 158 . 20 VAL HB H 1.788 0.03 1 159 . 20 VAL CG2 C 20.900 0.12 1 160 . 20 VAL HG2 H 0.795 0.03 1 161 . 20 VAL CG1 C 22.080 0.12 1 162 . 20 VAL HG1 H 0.588 0.03 1 163 . 20 VAL C C 173.160 0.12 1 164 . 21 LYS N N 125.678 0.15 1 165 . 21 LYS H H 9.073 0.03 1 166 . 21 LYS CA C 54.753 0.12 1 167 . 21 LYS HA H 4.634 0.03 1 168 . 21 LYS CB C 35.504 0.12 1 169 . 21 LYS HB2 H 1.610 0.03 2 170 . 21 LYS HB3 H 1.520 0.03 2 171 . 21 LYS CG C 24.862 0.12 1 172 . 21 LYS HG2 H 1.240 0.03 2 173 . 21 LYS HG3 H 1.140 0.03 2 174 . 21 LYS CD C 29.339 0.12 1 175 . 21 LYS HD2 H 1.420 0.03 2 176 . 21 LYS HD3 H 1.230 0.03 2 177 . 21 LYS CE C 41.980 0.12 1 178 . 21 LYS HE2 H 2.658 0.03 2 179 . 21 LYS HE3 H 2.603 0.03 2 180 . 21 LYS C C 172.767 0.12 1 181 . 22 ILE N N 125.492 0.15 1 182 . 22 ILE H H 8.900 0.03 1 183 . 22 ILE CA C 62.234 0.12 1 184 . 22 ILE HA H 4.148 0.03 1 185 . 22 ILE CB C 38.649 0.12 1 186 . 22 ILE HB H 1.760 0.03 1 187 . 22 ILE CG1 C 28.549 0.12 1 188 . 22 ILE HG12 H 1.460 0.03 2 189 . 22 ILE HG13 H 0.880 0.03 2 190 . 22 ILE CD1 C 13.960 0.12 1 191 . 22 ILE HD1 H 0.739 0.03 1 192 . 22 ILE CG2 C 18.608 0.12 1 193 . 22 ILE HG2 H 0.765 0.03 1 194 . 22 ILE C C 173.016 0.12 1 195 . 23 ASN N N 128.436 0.15 1 196 . 23 ASN H H 8.177 0.03 1 197 . 23 ASN CA C 51.568 0.12 1 198 . 23 ASN HA H 5.070 0.03 1 199 . 23 ASN CB C 39.500 0.12 1 200 . 23 ASN HB2 H 2.464 0.03 2 201 . 23 ASN HB3 H 2.528 0.03 2 202 . 23 ASN ND2 N 112.825 0.15 1 203 . 23 ASN HD22 H 7.148 0.03 2 204 . 23 ASN HD21 H 5.968 0.03 2 205 . 23 ASN C C 171.200 0.12 1 206 . 24 PRO CA C 65.929 0.12 1 207 . 24 PRO HA H 4.217 0.03 1 208 . 24 PRO CB C 32.762 0.12 1 209 . 24 PRO HB2 H 2.363 0.03 2 210 . 24 PRO HB3 H 1.718 0.03 2 211 . 24 PRO CG C 28.286 0.12 1 212 . 24 PRO HG2 H 2.025 0.03 2 213 . 24 PRO HG3 H 1.910 0.03 2 214 . 24 PRO CD C 51.100 0.12 1 215 . 24 PRO HD2 H 3.732 0.03 2 216 . 24 PRO HD3 H 3.500 0.03 2 217 . 24 PRO C C 174.281 0.12 1 218 . 25 LYS N N 112.287 0.15 1 219 . 25 LYS H H 8.204 0.03 1 220 . 25 LYS CA C 56.227 0.12 1 221 . 25 LYS HA H 4.044 0.03 1 222 . 25 LYS CB C 34.667 0.12 1 223 . 25 LYS HB2 H 1.590 0.03 2 224 . 25 LYS HB3 H 1.770 0.03 2 225 . 25 LYS CG C 25.455 0.12 1 226 . 25 LYS HG2 H 1.310 0.03 2 227 . 25 LYS HG3 H 1.185 0.03 2 228 . 25 LYS CD C 29.076 0.12 1 229 . 25 LYS HD2 H 1.620 0.03 1 230 . 25 LYS HD3 H 1.620 0.03 1 231 . 25 LYS CE C 42.507 0.12 1 232 . 25 LYS HE2 H 2.925 0.03 1 233 . 25 LYS HE3 H 2.925 0.03 1 234 . 25 LYS C C 173.784 0.12 1 235 . 26 TYR N N 114.182 0.15 1 236 . 26 TYR H H 7.303 0.03 1 237 . 26 TYR CA C 56.797 0.12 1 238 . 26 TYR HA H 4.984 0.03 1 239 . 26 TYR CB C 40.306 0.12 1 240 . 26 TYR HB2 H 3.390 0.03 2 241 . 26 TYR HB3 H 2.917 0.03 2 242 . 26 TYR CD1 C 134.260 0.12 1 243 . 26 TYR HD1 H 6.830 0.03 1 244 . 26 TYR CE1 C 117.774 0.12 1 245 . 26 TYR HE1 H 6.690 0.03 1 246 . 26 TYR CE2 C 117.774 0.12 1 247 . 26 TYR HE2 H 6.690 0.03 1 248 . 26 TYR CD2 C 134.260 0.12 1 249 . 26 TYR HD2 H 6.830 0.03 1 250 . 26 TYR C C 170.804 0.12 1 251 . 27 VAL N N 119.462 0.15 1 252 . 27 VAL H H 8.350 0.03 1 253 . 27 VAL CA C 62.103 0.12 1 254 . 27 VAL HA H 4.556 0.03 1 255 . 27 VAL CB C 34.441 0.12 1 256 . 27 VAL HB H 2.030 0.03 1 257 . 27 VAL CG2 C 23.050 0.12 1 258 . 27 VAL HG2 H 0.983 0.03 1 259 . 27 VAL CG1 C 21.660 0.12 1 260 . 27 VAL HG1 H 0.439 0.03 1 261 . 27 VAL C C 173.843 0.12 1 262 . 28 LEU N N 125.700 0.15 1 263 . 28 LEU H H 9.072 0.03 1 264 . 28 LEU CA C 53.461 0.12 1 265 . 28 LEU HA H 4.943 0.03 1 266 . 28 LEU CB C 46.413 0.12 1 267 . 28 LEU HB2 H 1.458 0.03 2 268 . 28 LEU HB3 H 1.868 0.03 2 269 . 28 LEU CG C 26.800 0.12 1 270 . 28 LEU HG H 1.660 0.03 1 271 . 28 LEU CD1 C 25.989 0.12 1 272 . 28 LEU HD1 H 0.862 0.03 1 273 . 28 LEU CD2 C 24.800 0.12 1 274 . 28 LEU HD2 H 0.920 0.03 1 275 . 28 LEU C C 172.799 0.12 1 276 . 29 TYR N N 121.897 0.15 1 277 . 29 TYR H H 9.497 0.03 1 278 . 29 TYR CA C 58.494 0.12 1 279 . 29 TYR HA H 4.610 0.03 1 280 . 29 TYR CB C 39.692 0.12 1 281 . 29 TYR HB2 H 3.222 0.03 2 282 . 29 TYR HB3 H 2.771 0.03 2 283 . 29 TYR CD1 C 132.910 0.12 1 284 . 29 TYR HD1 H 7.140 0.03 1 285 . 29 TYR CE1 C 117.365 0.12 1 286 . 29 TYR HE1 H 6.870 0.03 1 287 . 29 TYR CE2 C 117.365 0.12 1 288 . 29 TYR HE2 H 6.870 0.03 1 289 . 29 TYR CD2 C 132.910 0.12 1 290 . 29 TYR HD2 H 7.140 0.03 1 291 . 29 TYR C C 173.419 0.12 1 292 . 30 GLY N N 113.452 0.15 1 293 . 30 GLY H H 9.297 0.03 1 294 . 30 GLY CA C 47.055 0.12 1 295 . 30 GLY HA2 H 3.550 0.03 2 296 . 30 GLY HA3 H 2.626 0.03 2 297 . 30 GLY C C 168.600 0.12 1 298 . 31 VAL N N 125.754 0.15 1 299 . 31 VAL H H 8.951 0.03 1 300 . 31 VAL CA C 61.798 0.12 1 301 . 31 VAL HA H 4.401 0.03 1 302 . 31 VAL CB C 32.960 0.12 1 303 . 31 VAL HB H 2.095 0.03 1 304 . 31 VAL CG2 C 22.120 0.12 1 305 . 31 VAL HG2 H 1.083 0.03 1 306 . 31 VAL CG1 C 22.990 0.12 1 307 . 31 VAL HG1 H 0.788 0.03 1 308 . 31 VAL C C 173.148 0.12 1 309 . 32 SER N N 124.317 0.15 1 310 . 32 SER H H 9.705 0.03 1 311 . 32 SER CA C 58.041 0.12 1 312 . 32 SER HA H 5.170 0.03 1 313 . 32 SER CB C 64.632 0.12 1 314 . 32 SER HB2 H 3.820 0.03 2 315 . 32 SER HB3 H 3.745 0.03 2 316 . 32 SER C C 172.484 0.12 1 317 . 33 THR N N 117.250 0.15 1 318 . 33 THR H H 8.551 0.03 1 319 . 33 THR CA C 59.633 0.12 1 320 . 33 THR HA H 4.978 0.03 1 321 . 33 THR CB C 68.275 0.12 1 322 . 33 THR HB H 4.543 0.03 1 323 . 33 THR CG2 C 22.520 0.12 1 324 . 33 THR HG2 H 1.102 0.03 1 325 . 34 PRO CA C 66.080 0.12 1 326 . 34 PRO HA H 4.268 0.03 1 327 . 34 PRO CB C 32.160 0.12 1 328 . 34 PRO HB2 H 2.388 0.03 2 329 . 34 PRO HB3 H 1.730 0.03 2 330 . 34 PRO CG C 29.076 0.12 1 331 . 34 PRO HG2 H 2.201 0.03 2 332 . 34 PRO HG3 H 1.981 0.03 2 333 . 34 PRO CD C 50.700 0.12 1 334 . 34 PRO HD2 H 3.990 0.03 2 335 . 34 PRO HD3 H 3.610 0.03 2 336 . 34 PRO C C 174.790 0.12 1 337 . 35 ASN N N 110.465 0.15 1 338 . 35 ASN H H 7.907 0.03 1 339 . 35 ASN CA C 53.729 0.12 1 340 . 35 ASN HA H 4.790 0.03 1 341 . 35 ASN CB C 40.903 0.12 1 342 . 35 ASN HB2 H 2.664 0.03 2 343 . 35 ASN HB3 H 2.783 0.03 2 344 . 35 ASN ND2 N 112.695 0.15 1 345 . 35 ASN HD22 H 6.965 0.03 2 346 . 35 ASN HD21 H 7.578 0.03 2 347 . 35 ASN C C 172.495 0.12 1 348 . 36 LYS N N 118.232 0.15 1 349 . 36 LYS H H 7.567 0.03 1 350 . 36 LYS CA C 56.300 0.12 1 351 . 36 LYS HA H 4.555 0.03 1 352 . 36 LYS CB C 35.870 0.12 1 353 . 36 LYS HB2 H 1.750 0.03 2 354 . 36 LYS HB3 H 1.640 0.03 2 355 . 36 LYS CG C 24.270 0.12 1 356 . 36 LYS HG2 H 1.250 0.03 2 357 . 36 LYS HG3 H 1.192 0.03 2 358 . 36 LYS CD C 29.405 0.12 1 359 . 36 LYS HD2 H 1.620 0.03 1 360 . 36 LYS HD3 H 1.620 0.03 1 361 . 36 LYS CE C 42.375 0.12 1 362 . 36 LYS HE2 H 2.948 0.03 1 363 . 36 LYS HE3 H 2.948 0.03 1 364 . 36 LYS C C 171.595 0.12 1 365 . 37 ARG N N 122.910 0.15 1 366 . 37 ARG H H 8.324 0.03 1 367 . 37 ARG CA C 55.389 0.12 1 368 . 37 ARG HA H 5.200 0.03 1 369 . 37 ARG CB C 32.388 0.12 1 370 . 37 ARG HB2 H 1.718 0.03 2 371 . 37 ARG HB3 H 1.598 0.03 2 372 . 37 ARG CG C 27.891 0.12 1 373 . 37 ARG HG2 H 1.095 0.03 2 374 . 37 ARG HG3 H 0.926 0.03 2 375 . 37 ARG CD C 43.995 0.12 1 376 . 37 ARG HD2 H 3.003 0.03 2 377 . 37 ARG HD3 H 2.850 0.03 2 378 . 37 ARG NE N 124.840 0.15 1 379 . 37 ARG HE H 7.580 0.03 1 380 . 37 ARG C C 172.874 0.12 1 381 . 38 LEU N N 127.475 0.15 1 382 . 38 LEU H H 8.869 0.03 1 383 . 38 LEU CA C 53.575 0.12 1 384 . 38 LEU HA H 4.692 0.03 1 385 . 38 LEU CB C 45.361 0.12 1 386 . 38 LEU HB2 H 1.404 0.03 1 387 . 38 LEU HB3 H 1.404 0.03 1 388 . 38 LEU CG C 27.400 0.12 1 389 . 38 LEU HG H 1.420 0.03 1 390 . 38 LEU CD1 C 26.580 0.12 1 391 . 38 LEU HD1 H 0.668 0.03 1 392 . 38 LEU CD2 C 24.467 0.12 1 393 . 38 LEU HD2 H 0.755 0.03 1 394 . 38 LEU C C 173.016 0.12 1 395 . 39 TYR N N 120.435 0.15 1 396 . 39 TYR H H 8.831 0.03 1 397 . 39 TYR CA C 58.582 0.12 1 398 . 39 TYR HA H 5.310 0.03 1 399 . 39 TYR CB C 40.210 0.12 1 400 . 39 TYR HB2 H 2.864 0.03 2 401 . 39 TYR HB3 H 2.698 0.03 2 402 . 39 TYR CD1 C 132.770 0.12 1 403 . 39 TYR HD1 H 6.890 0.03 1 404 . 39 TYR CE1 C 117.840 0.12 1 405 . 39 TYR HE1 H 6.620 0.03 1 406 . 39 TYR HH H 5.310 0.03 1 407 . 39 TYR CE2 C 117.840 0.12 1 408 . 39 TYR HE2 H 6.620 0.03 1 409 . 39 TYR CD2 C 132.770 0.12 1 410 . 39 TYR HD2 H 6.890 0.03 1 411 . 39 TYR C C 174.574 0.12 1 412 . 40 LYS N N 122.295 0.15 1 413 . 40 LYS H H 9.118 0.03 1 414 . 40 LYS CA C 53.923 0.12 1 415 . 40 LYS HA H 4.935 0.03 1 416 . 40 LYS CB C 39.215 0.12 1 417 . 40 LYS HB2 H 1.460 0.03 2 418 . 40 LYS HB3 H 1.830 0.03 2 419 . 40 LYS CG C 24.731 0.12 1 420 . 40 LYS HG2 H 1.060 0.03 2 421 . 40 LYS HG3 H 0.720 0.03 2 422 . 40 LYS CD C 30.000 0.12 1 423 . 40 LYS HD2 H 1.330 0.03 2 424 . 40 LYS HD3 H 0.690 0.03 2 425 . 40 LYS CE C 42.000 0.12 1 426 . 40 LYS HE2 H 1.970 0.03 2 427 . 40 LYS HE3 H 1.100 0.03 2 428 . 40 LYS C C 174.825 0.12 1 429 . 41 ARG N N 123.309 0.15 1 430 . 41 ARG H H 9.526 0.03 1 431 . 41 ARG CA C 56.024 0.12 1 432 . 41 ARG HA H 5.302 0.03 1 433 . 41 ARG CB C 32.461 0.12 1 434 . 41 ARG HB2 H 2.472 0.03 2 435 . 41 ARG HB3 H 1.920 0.03 2 436 . 41 ARG CG C 28.220 0.12 1 437 . 41 ARG HG2 H 1.812 0.03 2 438 . 41 ARG HG3 H 1.718 0.03 2 439 . 41 ARG CD C 43.758 0.12 1 440 . 41 ARG HD2 H 2.765 0.03 1 441 . 41 ARG HD3 H 2.765 0.03 1 442 . 41 ARG C C 176.765 0.12 1 443 . 42 TYR N N 124.784 0.15 1 444 . 42 TYR H H 10.479 0.03 1 445 . 42 TYR CA C 63.447 0.12 1 446 . 42 TYR HA H 4.559 0.03 1 447 . 42 TYR CB C 39.121 0.12 1 448 . 42 TYR HB2 H 3.500 0.03 2 449 . 42 TYR HB3 H 3.380 0.03 2 450 . 42 TYR CD1 C 132.400 0.12 1 451 . 42 TYR HD1 H 6.920 0.03 1 452 . 42 TYR CE1 C 117.690 0.12 1 453 . 42 TYR HE1 H 6.500 0.03 1 454 . 42 TYR CE2 C 117.690 0.12 1 455 . 42 TYR HE2 H 6.500 0.03 1 456 . 42 TYR CD2 C 132.400 0.12 1 457 . 42 TYR HD2 H 6.920 0.03 1 458 . 42 TYR C C 176.647 0.12 1 459 . 43 SER N N 112.455 0.15 1 460 . 43 SER H H 9.237 0.03 1 461 . 43 SER CA C 61.528 0.12 1 462 . 43 SER HA H 4.190 0.03 1 463 . 43 SER CB C 62.484 0.12 1 464 . 43 SER C C 175.235 0.12 1 465 . 44 GLU N N 121.118 0.15 1 466 . 44 GLU H H 7.895 0.03 1 467 . 44 GLU CA C 60.195 0.12 1 468 . 44 GLU HA H 4.200 0.03 1 469 . 44 GLU CB C 30.247 0.12 1 470 . 44 GLU HB2 H 2.480 0.03 2 471 . 44 GLU HB3 H 2.242 0.03 2 472 . 44 GLU C C 178.150 0.12 1 473 . 45 PHE N N 119.234 0.15 1 474 . 45 PHE H H 8.117 0.03 1 475 . 45 PHE CA C 61.816 0.12 1 476 . 45 PHE HA H 4.227 0.03 1 477 . 45 PHE CB C 39.083 0.12 1 478 . 45 PHE HB2 H 3.370 0.03 2 479 . 45 PHE HB3 H 2.920 0.03 2 480 . 45 PHE CD1 C 133.215 0.12 1 481 . 45 PHE HD1 H 7.580 0.03 1 482 . 45 PHE CE1 C 131.922 0.12 1 483 . 45 PHE HE1 H 7.440 0.03 1 484 . 45 PHE CZ C 129.310 0.12 1 485 . 45 PHE HZ H 7.150 0.03 1 486 . 45 PHE CE2 C 131.922 0.12 1 487 . 45 PHE HE2 H 7.440 0.03 1 488 . 45 PHE CD2 C 133.215 0.12 1 489 . 45 PHE HD2 H 7.580 0.03 1 490 . 45 PHE C C 174.825 0.12 1 491 . 46 TRP N N 119.973 0.15 1 492 . 46 TRP H H 7.741 0.03 1 493 . 46 TRP CA C 60.737 0.12 1 494 . 46 TRP HA H 3.782 0.03 1 495 . 46 TRP CB C 29.407 0.12 1 496 . 46 TRP HB2 H 3.223 0.03 2 497 . 46 TRP HB3 H 2.870 0.03 2 498 . 46 TRP CD1 C 126.763 0.12 1 499 . 46 TRP HD1 H 7.020 0.03 1 500 . 46 TRP NE1 N 129.597 0.15 1 501 . 46 TRP HE1 H 10.050 0.03 1 502 . 46 TRP CZ2 C 115.096 0.12 1 503 . 46 TRP HZ2 H 7.400 0.03 1 504 . 46 TRP CH2 C 124.550 0.12 1 505 . 46 TRP HH2 H 7.080 0.03 1 506 . 46 TRP CZ3 C 121.664 0.12 1 507 . 46 TRP HZ3 H 6.888 0.03 1 508 . 46 TRP CE3 C 120.371 0.12 1 509 . 46 TRP HE3 H 7.100 0.03 1 510 . 46 TRP C C 175.964 0.12 1 511 . 47 LYS N N 119.188 0.15 1 512 . 47 LYS H H 8.316 0.03 1 513 . 47 LYS CA C 59.605 0.12 1 514 . 47 LYS HA H 3.823 0.03 1 515 . 47 LYS CB C 32.627 0.12 1 516 . 47 LYS HB2 H 1.944 0.03 2 517 . 47 LYS HB3 H 1.840 0.03 2 518 . 47 LYS CG C 26.047 0.12 1 519 . 47 LYS HG2 H 1.650 0.03 2 520 . 47 LYS HG3 H 1.466 0.03 2 521 . 47 LYS CD C 29.800 0.12 1 522 . 47 LYS HD2 H 1.720 0.03 2 523 . 47 LYS HD3 H 1.670 0.03 2 524 . 47 LYS CE C 42.441 0.12 1 525 . 47 LYS HE2 H 2.973 0.03 1 526 . 47 LYS HE3 H 2.973 0.03 1 527 . 47 LYS C C 176.079 0.12 1 528 . 48 LEU N N 120.170 0.15 1 529 . 48 LEU H H 7.240 0.03 1 530 . 48 LEU CA C 58.856 0.12 1 531 . 48 LEU HA H 3.901 0.03 1 532 . 48 LEU CB C 40.890 0.12 1 533 . 48 LEU HB2 H 1.868 0.03 2 534 . 48 LEU HB3 H 1.070 0.03 2 535 . 48 LEU CG C 26.900 0.12 1 536 . 48 LEU HG H 1.150 0.03 1 537 . 48 LEU CD1 C 23.550 0.12 1 538 . 48 LEU HD1 H 0.530 0.03 1 539 . 48 LEU CD2 C 24.430 0.12 1 540 . 48 LEU HD2 H 0.025 0.03 1 541 . 48 LEU C C 174.849 0.12 1 542 . 49 LYS N N 117.887 0.15 1 543 . 49 LYS H H 7.384 0.03 1 544 . 49 LYS CA C 60.969 0.12 1 545 . 49 LYS HA H 3.506 0.03 1 546 . 49 LYS CB C 32.413 0.12 1 547 . 49 LYS HB2 H 1.210 0.03 2 548 . 49 LYS HB3 H 1.100 0.03 2 549 . 49 LYS CG C 24.731 0.12 1 550 . 49 LYS HG2 H 0.760 0.03 2 551 . 49 LYS HG3 H 0.720 0.03 2 552 . 49 LYS CD C 29.142 0.12 1 553 . 49 LYS HD2 H 0.500 0.03 2 554 . 49 LYS HD3 H 0.450 0.03 2 555 . 49 LYS CE C 42.046 0.12 1 556 . 49 LYS HE2 H 2.290 0.03 1 557 . 49 LYS HE3 H 2.290 0.03 1 558 . 49 LYS C C 175.286 0.12 1 559 . 50 THR N N 130.830 0.15 1 560 . 50 THR H H 7.893 0.03 1 561 . 50 THR CA C 65.793 0.12 1 562 . 50 THR HA H 3.772 0.03 1 563 . 50 THR CB C 69.135 0.12 1 564 . 50 THR HB H 3.870 0.03 1 565 . 50 THR CG2 C 21.702 0.12 1 566 . 50 THR HG2 H 0.755 0.03 1 567 . 50 THR C C 175.700 0.12 1 568 . 51 ARG N N 123.327 0.15 1 569 . 51 ARG H H 8.487 0.03 1 570 . 51 ARG CA C 59.468 0.12 1 571 . 51 ARG HA H 4.010 0.03 1 572 . 51 ARG CB C 30.265 0.12 1 573 . 51 ARG HB2 H 1.900 0.03 1 574 . 51 ARG HB3 H 1.900 0.03 1 575 . 51 ARG CG C 28.220 0.12 1 576 . 51 ARG HG2 H 1.810 0.03 2 577 . 51 ARG HG3 H 1.650 0.03 2 578 . 51 ARG CD C 43.560 0.12 1 579 . 51 ARG HD2 H 3.190 0.03 2 580 . 51 ARG HD3 H 3.100 0.03 2 581 . 51 ARG C C 177.238 0.12 1 582 . 52 LEU N N 119.809 0.15 1 583 . 52 LEU H H 8.620 0.03 1 584 . 52 LEU CA C 58.791 0.12 1 585 . 52 LEU HA H 4.118 0.03 1 586 . 52 LEU CB C 42.507 0.12 1 587 . 52 LEU HB2 H 2.383 0.03 2 588 . 52 LEU HB3 H 1.755 0.03 2 589 . 52 LEU CG C 27.200 0.12 1 590 . 52 LEU HG H 2.000 0.03 1 591 . 52 LEU CD1 C 27.957 0.12 1 592 . 52 LEU HD1 H 0.880 0.03 1 593 . 52 LEU CD2 C 26.113 0.12 1 594 . 52 LEU HD2 H 1.115 0.03 1 595 . 52 LEU C C 176.883 0.12 1 596 . 53 GLU N N 116.958 0.15 1 597 . 53 GLU H H 8.007 0.03 1 598 . 53 GLU CA C 60.646 0.12 1 599 . 53 GLU HA H 4.476 0.03 1 600 . 53 GLU CB C 29.704 0.12 1 601 . 53 GLU HB2 H 2.088 0.03 2 602 . 53 GLU HB3 H 1.898 0.03 2 603 . 53 GLU CG C 38.300 0.12 1 604 . 53 GLU HG2 H 2.800 0.03 2 605 . 53 GLU HG3 H 2.640 0.03 2 606 . 53 GLU C C 178.527 0.12 1 607 . 54 ARG N N 119.813 0.15 1 608 . 54 ARG H H 7.754 0.03 1 609 . 54 ARG CA C 58.880 0.12 1 610 . 54 ARG HA H 4.062 0.03 1 611 . 54 ARG CB C 30.388 0.12 1 612 . 54 ARG HB2 H 1.980 0.03 2 613 . 54 ARG HB3 H 1.915 0.03 2 614 . 54 ARG CG C 27.364 0.12 1 615 . 54 ARG HG2 H 1.780 0.03 2 616 . 54 ARG HG3 H 1.650 0.03 2 617 . 54 ARG CD C 43.692 0.12 1 618 . 54 ARG HD2 H 3.178 0.03 1 619 . 54 ARG HD3 H 3.178 0.03 1 620 . 54 ARG C C 176.019 0.12 1 621 . 55 ASP N N 120.180 0.15 1 622 . 55 ASP H H 8.344 0.03 1 623 . 55 ASP CA C 57.746 0.12 1 624 . 55 ASP HA H 4.364 0.03 1 625 . 55 ASP CB C 42.178 0.12 1 626 . 55 ASP HB2 H 2.680 0.03 2 627 . 55 ASP HB3 H 2.640 0.03 2 628 . 55 ASP C C 176.197 0.12 1 629 . 56 VAL N N 118.524 0.15 1 630 . 56 VAL H H 8.665 0.03 1 631 . 56 VAL CA C 64.523 0.12 1 632 . 56 VAL HA H 3.555 0.03 1 633 . 56 VAL CB C 32.205 0.12 1 634 . 56 VAL HB H 1.625 0.03 1 635 . 56 VAL CG2 C 23.122 0.12 1 636 . 56 VAL HG2 H 0.338 0.03 1 637 . 56 VAL CG1 C 21.495 0.12 1 638 . 56 VAL HG1 H -0.105 0.03 1 639 . 56 VAL C C 175.752 0.12 1 640 . 57 GLY N N 107.39 0.15 1 641 . 57 GLY H H 7.755 0.03 1 642 . 57 GLY CA C 46.181 0.12 1 643 . 57 GLY HA2 H 4.094 0.03 2 644 . 57 GLY HA3 H 3.744 0.03 2 645 . 57 GLY C C 172.247 0.12 1 646 . 58 SER N N 112.664 0.15 1 647 . 58 SER H H 7.443 0.03 1 648 . 58 SER CA C 57.082 0.12 1 649 . 58 SER HA H 4.728 0.03 1 650 . 58 SER CB C 66.211 0.12 1 651 . 58 SER HB2 H 3.875 0.03 2 652 . 58 SER HB3 H 3.722 0.03 2 653 . 58 SER C C 170.270 0.12 1 654 . 59 THR N N 115.632 0.15 1 655 . 59 THR H H 8.108 0.03 1 656 . 59 THR CA C 62.785 0.12 1 657 . 59 THR HA H 4.112 0.03 1 658 . 59 THR CB C 69.700 0.12 1 659 . 59 THR HB H 3.884 0.03 1 660 . 59 THR CG2 C 22.380 0.12 1 661 . 59 THR HG2 H 1.180 0.03 1 662 . 59 THR C C 172.614 0.12 1 663 . 60 ILE N N 130.351 0.15 1 664 . 60 ILE H H 9.829 0.03 1 665 . 60 ILE CA C 59.629 0.12 1 666 . 60 ILE HA H 3.380 0.03 1 667 . 60 ILE CB C 39.960 0.12 1 668 . 60 ILE HB H 1.287 0.03 1 669 . 60 ILE CG1 C 29.800 0.12 1 670 . 60 ILE HG12 H 0.340 0.03 2 671 . 60 ILE HG13 H 0.160 0.03 2 672 . 60 ILE CD1 C 16.040 0.12 1 673 . 60 ILE HD1 H 0.730 0.03 1 674 . 60 ILE CG2 C 18.060 0.12 1 675 . 60 ILE HG2 H 0.750 0.03 1 676 . 60 ILE C C 173.300 0.12 1 677 . 61 PRO CA C 63.509 0.12 1 678 . 61 PRO HA H 4.275 0.03 1 679 . 61 PRO CB C 31.512 0.12 1 680 . 61 PRO HB2 H 1.862 0.03 2 681 . 61 PRO HB3 H 1.580 0.03 2 682 . 61 PRO CG C 26.311 0.12 1 683 . 61 PRO HG2 H 1.730 0.03 2 684 . 61 PRO HG3 H 0.498 0.03 2 685 . 61 PRO CD C 51.700 0.12 1 686 . 61 PRO HD2 H 3.170 0.03 1 687 . 61 PRO HD3 H 3.170 0.03 1 688 . 61 PRO C C 173.702 0.12 1 689 . 62 TYR N N 119.266 0.15 1 690 . 62 TYR H H 5.626 0.03 1 691 . 62 TYR CA C 55.169 0.12 1 692 . 62 TYR HA H 4.700 0.03 1 693 . 62 TYR CB C 39.993 0.12 1 694 . 62 TYR HB2 H 3.521 0.03 2 695 . 62 TYR HB3 H 2.405 0.03 2 696 . 62 TYR CD1 C 132.219 0.12 1 697 . 62 TYR HD1 H 6.590 0.03 1 698 . 62 TYR CE1 C 118.190 0.12 1 699 . 62 TYR HE1 H 6.460 0.03 1 700 . 62 TYR CE2 C 118.190 0.12 1 701 . 62 TYR HE2 H 6.460 0.03 1 702 . 62 TYR CD2 C 132.219 0.12 1 703 . 62 TYR HD2 H 6.590 0.03 1 704 . 62 TYR C C 173.160 0.12 1 705 . 63 ASP N N 122.850 0.15 1 706 . 63 ASP H H 9.138 0.03 1 707 . 63 ASP CA C 55.629 0.12 1 708 . 63 ASP HA H 4.441 0.03 1 709 . 63 ASP CB C 41.339 0.12 1 710 . 63 ASP HB2 H 2.620 0.03 1 711 . 63 ASP HB3 H 2.620 0.03 1 712 . 63 ASP C C 172.696 0.12 1 713 . 64 PHE N N 125.560 0.15 1 714 . 64 PHE H H 8.376 0.03 1 715 . 64 PHE CA C 55.941 0.12 1 716 . 64 PHE HA H 4.410 0.03 1 717 . 64 PHE CB C 42.747 0.12 1 718 . 64 PHE HB2 H 2.920 0.03 2 719 . 64 PHE HB3 H 2.510 0.03 2 720 . 64 PHE CD1 C 131.590 0.12 1 721 . 64 PHE HD1 H 6.170 0.03 1 722 . 64 PHE CE1 C 131.270 0.12 1 723 . 64 PHE HE1 H 6.730 0.03 1 724 . 64 PHE CZ C 128.221 0.12 1 725 . 64 PHE HZ H 6.460 0.03 1 726 . 64 PHE CE2 C 131.270 0.12 1 727 . 64 PHE HE2 H 6.730 0.03 1 728 . 64 PHE CD2 C 131.590 0.12 1 729 . 64 PHE HD2 H 6.170 0.03 1 730 . 64 PHE C C 172.300 0.12 1 731 . 65 PRO CA C 63.509 0.12 1 732 . 65 PRO HA H 4.418 0.03 1 733 . 65 PRO CB C 30.788 0.12 1 734 . 65 PRO HB2 H 1.960 0.03 2 735 . 65 PRO HB3 H 1.900 0.03 2 736 . 65 PRO CG C 27.759 0.12 1 737 . 65 PRO HG2 H 1.382 0.03 1 738 . 65 PRO HG3 H 1.382 0.03 1 739 . 65 PRO CD C 49.450 0.12 1 740 . 65 PRO HD2 H 2.750 0.03 2 741 . 65 PRO HD3 H 1.530 0.03 2 742 . 65 PRO C C 172.465 0.12 1 743 . 66 GLU N N 122.582 0.15 1 744 . 66 GLU H H 7.953 0.03 1 745 . 66 GLU CA C 56.530 0.12 1 746 . 66 GLU HA H 4.348 0.03 1 747 . 66 GLU CB C 31.775 0.12 1 748 . 66 GLU HB2 H 2.047 0.03 2 749 . 66 GLU HB3 H 1.977 0.03 2 750 . 66 GLU CG C 36.318 0.12 1 751 . 66 GLU HG2 H 2.232 0.03 1 752 . 66 GLU HG3 H 2.232 0.03 1 753 . 66 GLU C C 173.502 0.12 1 754 . 67 LYS N N 124.535 0.15 1 755 . 67 LYS H H 8.530 0.03 1 756 . 67 LYS CA C 54.540 0.12 1 757 . 67 LYS HA H 4.430 0.03 1 758 . 67 LYS CB C 32.950 0.12 1 759 . 67 LYS HB2 H 1.710 0.03 2 760 . 67 LYS HB3 H 1.605 0.03 2 761 . 67 LYS CG C 24.800 0.12 1 762 . 67 LYS HG2 H 1.320 0.03 1 763 . 67 LYS HG3 H 1.320 0.03 1 764 . 67 LYS CD C 29.500 0.12 1 765 . 67 LYS HD2 H 1.580 0.03 1 766 . 67 LYS HD3 H 1.580 0.03 1 767 . 67 LYS CE C 42.100 0.12 1 768 . 67 LYS HE2 H 2.830 0.03 1 769 . 67 LYS HE3 H 2.830 0.03 1 770 . 67 LYS C C 172.300 0.12 1 771 . 68 PRO CA C 63.638 0.12 1 772 . 68 PRO HA H 4.350 0.03 1 773 . 68 PRO CB C 32.414 0.12 1 774 . 68 PRO HB2 H 2.200 0.03 2 775 . 68 PRO HB3 H 1.837 0.03 2 776 . 68 PRO CG C 27.825 0.12 1 777 . 68 PRO HG2 H 1.880 0.03 2 778 . 68 PRO HG3 H 1.810 0.03 2 779 . 68 PRO CD C 50.736 0.12 1 780 . 68 PRO HD2 H 3.618 0.03 2 781 . 68 PRO HD3 H 3.374 0.03 2 782 . 68 PRO C C 175.345 0.12 1 783 . 69 GLY N N 109.77 0.15 1 784 . 69 GLY H H 8.603 0.03 1 785 . 69 GLY CA C 45.642 0.12 1 786 . 69 GLY HA2 H 3.927 0.03 1 787 . 69 GLY HA3 H 3.927 0.03 1 788 . 69 GLY C C 172.401 0.12 1 789 . 70 VAL N N 118.266 0.15 1 790 . 70 VAL H H 7.771 0.03 1 791 . 70 VAL CA C 63.127 0.12 1 792 . 70 VAL HA H 3.864 0.03 1 793 . 70 VAL CB C 32.755 0.12 1 794 . 70 VAL HB H 1.968 0.03 1 795 . 70 VAL CG2 C 20.958 0.12 1 796 . 70 VAL HG2 H 0.822 0.03 1 797 . 70 VAL CG1 C 21.437 0.12 1 798 . 70 VAL HG1 H 0.822 0.03 1 799 . 70 VAL C C 174.326 0.12 1 800 . 71 LEU N N 123.828 0.15 1 801 . 71 LEU H H 8.280 0.03 1 802 . 71 LEU CA C 55.523 0.12 1 803 . 71 LEU HA H 4.283 0.03 1 804 . 71 LEU CB C 42.175 0.12 1 805 . 71 LEU HB2 H 1.600 0.03 2 806 . 71 LEU HB3 H 1.540 0.03 2 807 . 71 LEU CG C 27.364 0.12 1 808 . 71 LEU HG H 1.530 0.03 1 809 . 71 LEU CD1 C 25.323 0.12 1 810 . 71 LEU HD1 H 0.848 0.03 1 811 . 71 LEU CD2 C 23.743 0.12 1 812 . 71 LEU HD2 H 0.778 0.03 1 813 . 71 LEU C C 174.813 0.12 1 814 . 72 ASP N N 121.783 0.15 1 815 . 72 ASP H H 8.079 0.03 1 816 . 72 ASP CA C 54.444 0.12 1 817 . 72 ASP HA H 4.541 0.03 1 818 . 72 ASP CB C 42.466 0.12 1 819 . 72 ASP HB2 H 2.779 0.03 2 820 . 72 ASP HB3 H 2.613 0.03 2 821 . 72 ASP C C 174.896 0.12 1 822 . 73 ARG N N 123.128 0.15 1 823 . 73 ARG H H 8.472 0.03 1 824 . 73 ARG CA C 57.805 0.12 1 825 . 73 ARG HA H 4.114 0.03 1 826 . 73 ARG CB C 30.219 0.12 1 827 . 73 ARG HB2 H 1.810 0.03 2 828 . 73 ARG HB3 H 1.740 0.03 2 829 . 73 ARG CG C 27.496 0.12 1 830 . 73 ARG HG2 H 1.600 0.03 1 831 . 73 ARG HG3 H 1.600 0.03 1 832 . 73 ARG CD C 43.560 0.12 1 833 . 73 ARG HD2 H 3.140 0.03 1 834 . 73 ARG HD3 H 3.140 0.03 1 835 . 73 ARG C C 175.381 0.12 1 836 . 74 ARG N N 119.831 0.15 1 837 . 74 ARG H H 8.483 0.03 1 838 . 74 ARG CA C 57.979 0.12 1 839 . 74 ARG HA H 4.002 0.03 1 840 . 74 ARG CB C 30.313 0.12 1 841 . 74 ARG HB2 H 1.420 0.03 1 842 . 74 ARG HB3 H 1.420 0.03 1 843 . 74 ARG CG C 27.232 0.12 1 844 . 74 ARG HG2 H 1.300 0.03 1 845 . 74 ARG HG3 H 1.300 0.03 1 846 . 74 ARG CD C 43.758 0.12 1 847 . 74 ARG HD2 H 3.020 0.03 2 848 . 74 ARG HD3 H 2.900 0.03 2 849 . 74 ARG C C 174.979 0.12 1 850 . 75 TRP N N 118.812 0.15 1 851 . 75 TRP H H 7.721 0.03 1 852 . 75 TRP CA C 57.327 0.12 1 853 . 75 TRP HA H 4.720 0.03 1 854 . 75 TRP CB C 29.802 0.12 1 855 . 75 TRP HB2 H 3.380 0.03 2 856 . 75 TRP HB3 H 3.230 0.03 2 857 . 75 TRP CD1 C 127.490 0.12 1 858 . 75 TRP HD1 H 7.240 0.03 1 859 . 75 TRP NE1 N 129.149 0.15 1 860 . 75 TRP HE1 H 10.070 0.03 1 861 . 75 TRP CZ2 C 114.720 0.12 1 862 . 75 TRP HZ2 H 7.410 0.03 1 863 . 75 TRP CH2 C 124.540 0.12 1 864 . 75 TRP HH2 H 7.118 0.03 1 865 . 75 TRP CZ3 C 122.040 0.12 1 866 . 75 TRP HZ3 H 7.068 0.03 1 867 . 75 TRP CE3 C 121.140 0.12 1 868 . 75 TRP HE3 H 7.526 0.03 1 869 . 75 TRP C C 174.126 0.12 1 870 . 76 GLN N N 119.642 0.15 1 871 . 76 GLN H H 7.885 0.03 1 872 . 76 GLN CA C 56.134 0.12 1 873 . 76 GLN HA H 4.214 0.03 1 874 . 76 GLN CB C 29.122 0.12 1 875 . 76 GLN HB2 H 2.070 0.03 2 876 . 76 GLN HB3 H 1.840 0.03 2 877 . 76 GLN CG C 34.145 0.12 1 878 . 76 GLN HG2 H 2.152 0.03 1 879 . 76 GLN HG3 H 2.152 0.03 1 880 . 76 GLN NE2 N 112.075 0.15 1 881 . 76 GLN HE22 H 7.390 0.03 2 882 . 76 GLN HE21 H 6.803 0.03 2 883 . 76 GLN C C 173.773 0.12 1 884 . 77 ARG N N 120.933 0.15 1 885 . 77 ARG H H 7.705 0.03 1 886 . 77 ARG CA C 56.230 0.12 1 887 . 77 ARG HA H 4.340 0.03 1 888 . 77 ARG CB C 32.223 0.12 1 889 . 77 ARG HB2 H 1.832 0.03 1 890 . 77 ARG HB3 H 1.832 0.03 1 891 . 77 ARG CG C 27.957 0.12 1 892 . 77 ARG HG2 H 1.640 0.03 1 893 . 77 ARG HG3 H 1.640 0.03 1 894 . 77 ARG CD C 43.889 0.12 1 895 . 77 ARG HD2 H 3.158 0.03 2 896 . 77 ARG HD3 H 3.062 0.03 2 897 . 77 ARG C C 174.033 0.12 1 898 . 78 ARG N N 121.577 0.15 1 899 . 78 ARG H H 8.674 0.03 1 900 . 78 ARG CA C 56.832 0.12 1 901 . 78 ARG HA H 4.327 0.03 1 902 . 78 ARG CB C 32.162 0.12 1 903 . 78 ARG HB2 H 1.826 0.03 1 904 . 78 ARG HB3 H 1.826 0.03 1 905 . 78 ARG CG C 28.352 0.12 1 906 . 78 ARG HG2 H 1.710 0.03 1 907 . 78 ARG HG3 H 1.710 0.03 1 908 . 78 ARG CD C 43.823 0.12 1 909 . 78 ARG HD2 H 3.290 0.03 2 910 . 78 ARG HD3 H 3.162 0.03 2 911 . 78 ARG C C 175.937 0.12 1 912 . 79 TYR N N 120.104 0.15 1 913 . 79 TYR H H 8.583 0.03 1 914 . 79 TYR CA C 59.856 0.12 1 915 . 79 TYR HA H 4.237 0.03 1 916 . 79 TYR CB C 37.865 0.12 1 917 . 79 TYR HB2 H 3.080 0.03 1 918 . 79 TYR HB3 H 3.080 0.03 1 919 . 79 TYR CD1 C 133.310 0.12 1 920 . 79 TYR HD1 H 7.000 0.03 1 921 . 79 TYR CE1 C 117.850 0.12 1 922 . 79 TYR HE1 H 6.600 0.03 1 923 . 79 TYR CE2 C 117.850 0.12 1 924 . 79 TYR HE2 H 6.600 0.03 1 925 . 79 TYR CD2 C 133.310 0.12 1 926 . 79 TYR HD2 H 7.000 0.03 1 927 . 79 TYR C C 171.405 0.12 1 928 . 80 ASP N N 116.621 0.15 1 929 . 80 ASP H H 7.527 0.03 1 930 . 80 ASP CA C 51.335 0.12 1 931 . 80 ASP HA H 4.072 0.03 1 932 . 80 ASP CB C 39.234 0.12 1 933 . 80 ASP HB2 H 2.495 0.03 2 934 . 80 ASP HB3 H 1.219 0.03 2 935 . 80 ASP C C 173.193 0.12 1 936 . 81 ASP N N 121.702 0.15 1 937 . 81 ASP H H 7.240 0.03 1 938 . 81 ASP CA C 53.050 0.12 1 939 . 81 ASP HA H 4.480 0.03 1 940 . 81 ASP CB C 42.932 0.12 1 941 . 81 ASP HB2 H 2.730 0.03 1 942 . 81 ASP HB3 H 2.730 0.03 1 943 . 81 ASP C C 173.200 0.12 1 944 . 82 PRO CA C 65.556 0.12 1 945 . 82 PRO HA H 4.067 0.03 1 946 . 82 PRO CB C 32.422 0.12 1 947 . 82 PRO HB2 H 2.280 0.03 2 948 . 82 PRO HB3 H 1.970 0.03 2 949 . 82 PRO CG C 27.759 0.12 1 950 . 82 PRO HG2 H 2.016 0.03 1 951 . 82 PRO HG3 H 2.016 0.03 1 952 . 82 PRO CD C 51.300 0.12 1 953 . 82 PRO HD2 H 3.990 0.03 2 954 . 82 PRO HD3 H 3.740 0.03 2 955 . 82 PRO C C 177.273 0.12 1 956 . 83 GLU N N 118.731 0.15 1 957 . 83 GLU H H 8.050 0.03 1 958 . 83 GLU CA C 59.194 0.12 1 959 . 83 GLU HA H 4.127 0.03 1 960 . 83 GLU CB C 29.894 0.12 1 961 . 83 GLU HB2 H 2.041 0.03 2 962 . 83 GLU HB3 H 2.040 0.03 2 963 . 83 GLU CG C 37.416 0.12 1 964 . 83 GLU HG2 H 2.334 0.03 2 965 . 83 GLU HG3 H 2.209 0.03 2 966 . 83 GLU C C 176.847 0.12 1 967 . 84 MET N N 121.357 0.15 1 968 . 84 MET H H 7.968 0.03 1 969 . 84 MET CA C 58.654 0.12 1 970 . 84 MET HA H 4.000 0.03 1 971 . 84 MET CB C 33.271 0.12 1 972 . 84 MET HB2 H 2.196 0.03 2 973 . 84 MET HB3 H 1.790 0.03 2 974 . 84 MET CG C 32.170 0.12 1 975 . 84 MET HG2 H 2.445 0.03 2 976 . 84 MET HG3 H 2.180 0.03 2 977 . 84 MET CE C 18.195 0.12 1 978 . 84 MET HE H 1.957 0.03 1 979 . 84 MET C C 176.400 0.12 1 980 . 85 ILE N N 119.154 0.15 1 981 . 85 ILE H H 8.228 0.03 1 982 . 85 ILE CA C 65.043 0.12 1 983 . 85 ILE HA H 3.865 0.03 1 984 . 85 ILE CB C 38.392 0.12 1 985 . 85 ILE HB H 1.766 0.03 1 986 . 85 ILE CG1 C 28.900 0.12 1 987 . 85 ILE HG12 H 1.630 0.03 2 988 . 85 ILE HG13 H 1.100 0.03 2 989 . 85 ILE CD1 C 14.110 0.12 1 990 . 85 ILE HD1 H 0.656 0.03 1 991 . 85 ILE CG2 C 18.740 0.12 1 992 . 85 ILE HG2 H 0.958 0.03 1 993 . 85 ILE C C 176.113 0.12 1 994 . 86 ASP N N 119.625 0.15 1 995 . 86 ASP H H 7.945 0.03 1 996 . 86 ASP CA C 58.369 0.12 1 997 . 86 ASP HA H 4.520 0.03 1 998 . 86 ASP CB C 41.763 0.12 1 999 . 86 ASP HB2 H 2.758 0.03 2 1000 . 86 ASP HB3 H 2.645 0.03 2 1001 . 86 ASP C C 175.854 0.12 1 1002 . 87 GLU N N 117.737 0.15 1 1003 . 87 GLU H H 7.885 0.03 1 1004 . 87 GLU CA C 59.763 0.12 1 1005 . 87 GLU HA H 3.972 0.03 1 1006 . 87 GLU CB C 30.091 0.12 1 1007 . 87 GLU HB2 H 2.180 0.03 2 1008 . 87 GLU HB3 H 2.058 0.03 2 1009 . 87 GLU CG C 36.763 0.12 1 1010 . 87 GLU HG2 H 2.395 0.03 2 1011 . 87 GLU HG3 H 2.204 0.03 2 1012 . 87 GLU C C 178.609 0.12 1 1013 . 88 ARG N N 120.997 0.15 1 1014 . 88 ARG H H 8.378 0.03 1 1015 . 88 ARG CA C 60.906 0.12 1 1016 . 88 ARG HA H 3.700 0.03 1 1017 . 88 ARG CB C 30.388 0.12 1 1018 . 88 ARG HB2 H 2.110 0.03 2 1019 . 88 ARG HB3 H 1.480 0.03 2 1020 . 88 ARG CG C 28.944 0.12 1 1021 . 88 ARG HG2 H 1.590 0.03 2 1022 . 88 ARG HG3 H 1.130 0.03 2 1023 . 88 ARG CD C 44.153 0.12 1 1024 . 88 ARG HD2 H 2.760 0.03 2 1025 . 88 ARG HD3 H 2.290 0.03 2 1026 . 88 ARG NE N 125.350 0.15 1 1027 . 88 ARG HE H 6.720 0.03 1 1028 . 88 ARG C C 175.038 0.12 1 1029 . 89 ARG N N 120.950 0.15 1 1030 . 89 ARG H H 9.162 0.03 1 1031 . 89 ARG CA C 61.229 0.12 1 1032 . 89 ARG HA H 3.650 0.03 1 1033 . 89 ARG CB C 31.062 0.12 1 1034 . 89 ARG HB2 H 2.325 0.03 2 1035 . 89 ARG HB3 H 2.064 0.03 2 1036 . 89 ARG CG C 27.298 0.12 1 1037 . 89 ARG HG2 H 1.775 0.03 2 1038 . 89 ARG HG3 H 1.651 0.03 2 1039 . 89 ARG CD C 43.494 0.12 1 1040 . 89 ARG HD2 H 3.450 0.03 2 1041 . 89 ARG HD3 H 3.060 0.03 2 1042 . 89 ARG NE N 121.266 0.15 1 1043 . 89 ARG HE H 7.363 0.03 1 1044 . 89 ARG C C 175.736 0.12 1 1045 . 90 ILE N N 117.402 0.15 1 1046 . 90 ILE H H 8.003 0.03 1 1047 . 90 ILE CA C 64.781 0.12 1 1048 . 90 ILE HA H 3.717 0.03 1 1049 . 90 ILE CB C 38.899 0.12 1 1050 . 90 ILE HB H 1.806 0.03 1 1051 . 90 ILE CG1 C 29.800 0.12 1 1052 . 90 ILE HG12 H 1.670 0.03 2 1053 . 90 ILE HG13 H 1.153 0.03 2 1054 . 90 ILE CD1 C 13.838 0.12 1 1055 . 90 ILE HD1 H 0.829 0.03 1 1056 . 90 ILE CG2 C 17.620 0.12 1 1057 . 90 ILE HG2 H 0.928 0.03 1 1058 . 90 ILE C C 177.368 0.12 1 1059 . 91 GLY N N 108.48 0.15 1 1060 . 91 GLY H H 8.054 0.03 1 1061 . 91 GLY CA C 47.349 0.12 1 1062 . 91 GLY HA2 H 3.855 0.03 2 1063 . 91 GLY HA3 H 3.553 0.03 2 1064 . 91 GLY C C 175.050 0.12 1 1065 . 92 LEU N N 123.658 0.15 1 1066 . 92 LEU H H 9.013 0.03 1 1067 . 92 LEU CA C 57.786 0.12 1 1068 . 92 LEU HA H 3.793 0.03 1 1069 . 92 LEU CB C 41.267 0.12 1 1070 . 92 LEU HB2 H 1.638 0.03 2 1071 . 92 LEU HB3 H 0.533 0.03 2 1072 . 92 LEU CG C 25.475 0.12 1 1073 . 92 LEU HG H 1.438 0.03 1 1074 . 92 LEU CD1 C 24.100 0.12 1 1075 . 92 LEU HD1 H -0.546 0.03 1 1076 . 92 LEU CD2 C 21.702 0.12 1 1077 . 92 LEU HD2 H -0.182 0.03 1 1078 . 92 LEU C C 176.161 0.12 1 1079 . 93 GLU N N 120.267 0.15 1 1080 . 93 GLU H H 8.139 0.03 1 1081 . 93 GLU CA C 61.770 0.12 1 1082 . 93 GLU HA H 3.675 0.03 1 1083 . 93 GLU CB C 31.437 0.12 1 1084 . 93 GLU HB2 H 2.334 0.03 2 1085 . 93 GLU HB3 H 2.230 0.03 2 1086 . 93 GLU CG C 38.853 0.12 1 1087 . 93 GLU HG2 H 2.150 0.03 2 1088 . 93 GLU HG3 H 2.080 0.03 2 1089 . 93 GLU C C 176.776 0.12 1 1090 . 94 ARG N N 120.838 0.15 1 1091 . 94 ARG H H 8.159 0.03 1 1092 . 94 ARG CA C 60.258 0.12 1 1093 . 94 ARG HA H 4.180 0.03 1 1094 . 94 ARG CB C 30.145 0.12 1 1095 . 94 ARG HB2 H 2.012 0.03 2 1096 . 94 ARG HB3 H 1.930 0.03 2 1097 . 94 ARG CG C 27.562 0.12 1 1098 . 94 ARG HG2 H 1.800 0.03 2 1099 . 94 ARG HG3 H 1.645 0.03 2 1100 . 94 ARG CD C 43.955 0.12 1 1101 . 94 ARG HD2 H 3.265 0.03 2 1102 . 94 ARG HD3 H 3.216 0.03 2 1103 . 94 ARG NE N 125.664 0.15 1 1104 . 94 ARG HE H 7.380 0.03 1 1105 . 94 ARG C C 175.700 0.12 1 1106 . 95 PHE N N 119.626 0.15 1 1107 . 95 PHE H H 7.955 0.03 1 1108 . 95 PHE CA C 61.494 0.12 1 1109 . 95 PHE HA H 4.328 0.03 1 1110 . 95 PHE CB C 39.654 0.12 1 1111 . 95 PHE HB2 H 3.593 0.03 2 1112 . 95 PHE HB3 H 3.085 0.03 2 1113 . 95 PHE CD1 C 129.840 0.12 1 1114 . 95 PHE HD1 H 7.290 0.03 1 1115 . 95 PHE CE1 C 130.510 0.12 1 1116 . 95 PHE HE1 H 7.160 0.03 1 1117 . 95 PHE CZ C 128.790 0.12 1 1118 . 95 PHE HZ H 6.800 0.03 1 1119 . 95 PHE CE2 C 130.510 0.12 1 1120 . 95 PHE HE2 H 7.160 0.03 1 1121 . 95 PHE CD2 C 129.840 0.12 1 1122 . 95 PHE HD2 H 7.290 0.03 1 1123 . 95 PHE C C 174.056 0.12 1 1124 . 96 LEU N N 115.181 0.15 1 1125 . 96 LEU H H 8.513 0.03 1 1126 . 96 LEU CA C 57.813 0.12 1 1127 . 96 LEU HA H 3.825 0.03 1 1128 . 96 LEU CB C 43.100 0.12 1 1129 . 96 LEU HB2 H 2.000 0.03 2 1130 . 96 LEU HB3 H 1.465 0.03 2 1131 . 96 LEU CG C 28.088 0.12 1 1132 . 96 LEU HG H 1.112 0.03 1 1133 . 96 LEU CD1 C 28.125 0.12 1 1134 . 96 LEU HD1 H 1.110 0.03 1 1135 . 96 LEU CD2 C 23.480 0.12 1 1136 . 96 LEU HD2 H 1.250 0.03 1 1137 . 96 LEU C C 176.835 0.12 1 1138 . 97 ASN N N 115.652 0.15 1 1139 . 97 ASN H H 8.033 0.03 1 1140 . 97 ASN CA C 58.571 0.12 1 1141 . 97 ASN HA H 4.222 0.03 1 1142 . 97 ASN CB C 40.005 0.12 1 1143 . 97 ASN HB2 H 2.877 0.03 2 1144 . 97 ASN HB3 H 2.577 0.03 2 1145 . 97 ASN ND2 N 116.209 0.15 1 1146 . 97 ASN HD22 H 8.049 0.03 2 1147 . 97 ASN HD21 H 7.471 0.03 2 1148 . 97 ASN C C 175.937 0.12 1 1149 . 98 GLU N N 119.221 0.15 1 1150 . 98 GLU H H 8.115 0.03 1 1151 . 98 GLU CA C 59.752 0.12 1 1152 . 98 GLU HA H 3.790 0.03 1 1153 . 98 GLU CB C 29.188 0.12 1 1154 . 98 GLU HB2 H 1.710 0.03 2 1155 . 98 GLU HB3 H 1.641 0.03 2 1156 . 98 GLU CG C 37.350 0.12 1 1157 . 98 GLU HG2 H 2.542 0.03 2 1158 . 98 GLU HG3 H 2.112 0.03 2 1159 . 98 GLU C C 175.227 0.12 1 1160 . 99 LEU N N 118.861 0.15 1 1161 . 99 LEU H H 7.268 0.03 1 1162 . 99 LEU CA C 58.758 0.12 1 1163 . 99 LEU HA H 3.173 0.03 1 1164 . 99 LEU CB C 42.717 0.12 1 1165 . 99 LEU HB2 H 0.610 0.03 2 1166 . 99 LEU HB3 H 1.050 0.03 2 1167 . 99 LEU CG C 27.298 0.12 1 1168 . 99 LEU HG H 0.926 0.03 1 1169 . 99 LEU CD1 C 27.200 0.12 1 1170 . 99 LEU HD1 H 0.375 0.03 1 1171 . 99 LEU CD2 C 23.600 0.12 1 1172 . 99 LEU HD2 H -0.103 0.03 1 1173 . 99 LEU C C 177.308 0.12 1 1174 . 100 TYR N N 111.046 0.15 1 1175 . 100 TYR H H 7.965 0.03 1 1176 . 100 TYR CA C 62.782 0.12 1 1177 . 100 TYR HA H 3.900 0.03 1 1178 . 100 TYR CB C 38.179 0.12 1 1179 . 100 TYR HB2 H 2.990 0.03 2 1180 . 100 TYR HB3 H 2.628 0.03 2 1181 . 100 TYR CD1 C 133.300 0.12 1 1182 . 100 TYR HD1 H 7.350 0.03 1 1183 . 100 TYR CE1 C 117.710 0.12 1 1184 . 100 TYR HE1 H 6.560 0.03 1 1185 . 100 TYR CE2 C 117.710 0.12 1 1186 . 100 TYR HE2 H 6.560 0.03 1 1187 . 100 TYR CD2 C 133.300 0.12 1 1188 . 100 TYR HD2 H 7.350 0.03 1 1189 . 100 TYR C C 174.126 0.12 1 1190 . 101 ASN N N 113.396 0.15 1 1191 . 101 ASN H H 7.215 0.03 1 1192 . 101 ASN CA C 53.420 0.12 1 1193 . 101 ASN HA H 5.025 0.03 1 1194 . 101 ASN CB C 40.509 0.12 1 1195 . 101 ASN HB2 H 2.930 0.03 2 1196 . 101 ASN HB3 H 2.864 0.03 2 1197 . 101 ASN ND2 N 112.972 0.15 1 1198 . 101 ASN HD22 H 7.430 0.03 2 1199 . 101 ASN HD21 H 6.947 0.03 2 1200 . 101 ASN C C 172.602 0.12 1 1201 . 102 ASP N N 120.689 0.15 1 1202 . 102 ASP H H 6.829 0.03 1 1203 . 102 ASP CA C 55.926 0.12 1 1204 . 102 ASP HA H 4.550 0.03 1 1205 . 102 ASP CB C 40.781 0.12 1 1206 . 102 ASP HB2 H 3.178 0.03 2 1207 . 102 ASP HB3 H 3.099 0.03 2 1208 . 102 ASP C C 174.861 0.12 1 1209 . 103 ARG N N 125.581 0.15 1 1210 . 103 ARG H H 8.503 0.03 1 1211 . 103 ARG CA C 56.945 0.12 1 1212 . 103 ARG HA H 4.100 0.03 1 1213 . 103 ARG CB C 30.680 0.12 1 1214 . 103 ARG HB2 H 1.526 0.03 2 1215 . 103 ARG HB3 H 1.462 0.03 2 1216 . 103 ARG CG C 27.101 0.12 1 1217 . 103 ARG HG2 H 1.400 0.03 2 1218 . 103 ARG HG3 H 1.290 0.03 2 1219 . 103 ARG CD C 43.758 0.12 1 1220 . 103 ARG HD2 H 3.050 0.03 1 1221 . 103 ARG HD3 H 3.050 0.03 1 1222 . 103 ARG C C 174.754 0.12 1 1223 . 104 PHE N N 119.814 0.15 1 1224 . 104 PHE H H 8.765 0.03 1 1225 . 104 PHE CA C 59.420 0.12 1 1226 . 104 PHE HA H 4.631 0.03 1 1227 . 104 PHE CB C 40.455 0.12 1 1228 . 104 PHE HB2 H 3.101 0.03 2 1229 . 104 PHE HB3 H 3.299 0.03 2 1230 . 104 PHE CD1 C 132.050 0.12 1 1231 . 104 PHE HD1 H 7.380 0.03 1 1232 . 104 PHE CE1 C 130.820 0.12 1 1233 . 104 PHE HE1 H 7.380 0.03 1 1234 . 104 PHE CZ C 129.620 0.12 1 1235 . 104 PHE HZ H 7.300 0.03 1 1236 . 104 PHE CE2 C 130.820 0.12 1 1237 . 104 PHE HE2 H 7.380 0.03 1 1238 . 104 PHE CD2 C 132.050 0.12 1 1239 . 104 PHE HD2 H 7.380 0.03 1 1240 . 104 PHE C C 173.757 0.12 1 1241 . 105 ASP N N 121.210 0.15 1 1242 . 105 ASP H H 7.885 0.03 1 1243 . 105 ASP CA C 52.895 0.12 1 1244 . 105 ASP HA H 4.888 0.03 1 1245 . 105 ASP CB C 40.895 0.12 1 1246 . 105 ASP HB2 H 3.481 0.03 2 1247 . 105 ASP HB3 H 2.509 0.03 2 1248 . 105 ASP C C 172.892 0.12 1 1249 . 106 SER N N 117.450 0.15 1 1250 . 106 SER H H 8.475 0.03 1 1251 . 106 SER CA C 58.584 0.12 1 1252 . 106 SER HA H 4.500 0.03 1 1253 . 106 SER CB C 64.428 0.12 1 1254 . 106 SER HB2 H 4.036 0.03 2 1255 . 106 SER HB3 H 3.725 0.03 2 1256 . 106 SER C C 172.413 0.12 1 1257 . 107 ARG N N 117.969 0.15 1 1258 . 107 ARG H H 7.753 0.03 1 1259 . 107 ARG CA C 59.151 0.12 1 1260 . 107 ARG HA H 3.680 0.03 1 1261 . 107 ARG CB C 31.046 0.12 1 1262 . 107 ARG HB2 H 1.042 0.03 2 1263 . 107 ARG HB3 H 0.892 0.03 2 1264 . 107 ARG CG C 25.982 0.12 1 1265 . 107 ARG HG2 H 1.460 0.03 1 1266 . 107 ARG HG3 H 1.460 0.03 1 1267 . 107 ARG CD C 43.758 0.12 1 1268 . 107 ARG HD2 H 3.050 0.03 1 1269 . 107 ARG HD3 H 3.050 0.03 1 1270 . 107 ARG NE N 125.070 0.15 1 1271 . 107 ARG HE H 8.614 0.03 1 1272 . 107 ARG C C 175.535 0.12 1 1273 . 108 TRP N N 115.689 0.15 1 1274 . 108 TRP H H 6.462 0.03 1 1275 . 108 TRP CA C 57.782 0.12 1 1276 . 108 TRP HA H 3.923 0.03 1 1277 . 108 TRP CB C 29.007 0.12 1 1278 . 108 TRP HB2 H 3.553 0.03 2 1279 . 108 TRP HB3 H 3.150 0.03 2 1280 . 108 TRP CD1 C 130.320 0.12 1 1281 . 108 TRP HD1 H 7.780 0.03 1 1282 . 108 TRP NE1 N 130.018 0.15 1 1283 . 108 TRP HE1 H 10.170 0.03 1 1284 . 108 TRP CZ2 C 115.020 0.12 1 1285 . 108 TRP HZ2 H 7.210 0.03 1 1286 . 108 TRP CH2 C 125.340 0.12 1 1287 . 108 TRP HH2 H 6.990 0.03 1 1288 . 108 TRP CZ3 C 121.400 0.12 1 1289 . 108 TRP HZ3 H 6.660 0.03 1 1290 . 108 TRP CE3 C 119.910 0.12 1 1291 . 108 TRP HE3 H 7.410 0.03 1 1292 . 108 TRP C C 175.928 0.12 1 1293 . 109 ARG N N 117.265 0.15 1 1294 . 109 ARG H H 8.446 0.03 1 1295 . 109 ARG CA C 57.908 0.12 1 1296 . 109 ARG HA H 3.646 0.03 1 1297 . 109 ARG CB C 29.545 0.12 1 1298 . 109 ARG HB2 H 1.770 0.03 2 1299 . 109 ARG HB3 H 1.675 0.03 2 1300 . 109 ARG CG C 26.179 0.12 1 1301 . 109 ARG HG2 H 1.926 0.03 2 1302 . 109 ARG HG3 H 1.578 0.03 2 1303 . 109 ARG CD C 44.416 0.12 1 1304 . 109 ARG HD2 H 3.140 0.03 1 1305 . 109 ARG HD3 H 3.140 0.03 1 1306 . 109 ARG NE N 127.140 0.15 1 1307 . 109 ARG HE H 7.420 0.03 1 1308 . 109 ARG C C 173.654 0.12 1 1309 . 110 ASP N N 118.446 0.15 1 1310 . 110 ASP H H 7.662 0.03 1 1311 . 110 ASP CA C 55.205 0.12 1 1312 . 110 ASP HA H 4.618 0.03 1 1313 . 110 ASP CB C 40.701 0.12 1 1314 . 110 ASP HB2 H 2.667 0.03 2 1315 . 110 ASP HB3 H 2.565 0.03 2 1316 . 110 ASP C C 175.476 0.12 1 1317 . 111 THR N N 130.618 0.15 1 1318 . 111 THR H H 7.269 0.03 1 1319 . 111 THR CA C 61.958 0.12 1 1320 . 111 THR HA H 4.180 0.03 1 1321 . 111 THR CB C 71.821 0.12 1 1322 . 111 THR HB H 4.470 0.03 1 1323 . 111 THR CG2 C 22.361 0.12 1 1324 . 111 THR HG2 H 1.430 0.03 1 1325 . 111 THR C C 172.945 0.12 1 1326 . 112 LYS N N 123.658 0.15 1 1327 . 112 LYS H H 8.598 0.03 1 1328 . 112 LYS CA C 59.495 0.12 1 1329 . 112 LYS HA H 3.982 0.03 1 1330 . 112 LYS CB C 32.291 0.12 1 1331 . 112 LYS HB2 H 1.815 0.03 1 1332 . 112 LYS HB3 H 1.815 0.03 1 1333 . 112 LYS CG C 25.257 0.12 1 1334 . 112 LYS HG2 H 1.490 0.03 2 1335 . 112 LYS HG3 H 1.425 0.03 2 1336 . 112 LYS CD C 29.405 0.12 1 1337 . 112 LYS HD2 H 1.720 0.03 2 1338 . 112 LYS HD3 H 1.620 0.03 2 1339 . 112 LYS CE C 42.572 0.12 1 1340 . 112 LYS HE2 H 3.020 0.03 1 1341 . 112 LYS HE3 H 3.020 0.03 1 1342 . 112 LYS C C 176.989 0.12 1 1343 . 113 ILE N N 114.720 0.15 1 1344 . 113 ILE H H 7.717 0.03 1 1345 . 113 ILE CA C 64.313 0.12 1 1346 . 113 ILE HA H 3.947 0.03 1 1347 . 113 ILE CB C 38.876 0.12 1 1348 . 113 ILE HB H 1.689 0.03 1 1349 . 113 ILE CG1 C 28.681 0.12 1 1350 . 113 ILE HG12 H 1.606 0.03 2 1351 . 113 ILE HG13 H 1.186 0.03 2 1352 . 113 ILE CD1 C 14.620 0.12 1 1353 . 113 ILE HD1 H 0.888 0.03 1 1354 . 113 ILE CG2 C 18.608 0.12 1 1355 . 113 ILE HG2 H 0.892 0.03 1 1356 . 113 ILE C C 176.550 0.12 1 1357 . 114 ALA N N 123.209 0.15 1 1358 . 114 ALA H H 8.103 0.03 1 1359 . 114 ALA CA C 55.477 0.12 1 1360 . 114 ALA HA H 4.160 0.03 1 1361 . 114 ALA CB C 18.943 0.12 1 1362 . 114 ALA HB H 1.495 0.03 1 1363 . 114 ALA C C 179.860 0.12 1 1364 . 115 GLN N N 121.073 0.15 1 1365 . 115 GLN H H 8.272 0.03 1 1366 . 115 GLN CA C 59.832 0.12 1 1367 . 115 GLN HA H 4.103 0.03 1 1368 . 115 GLN CB C 28.792 0.12 1 1369 . 115 GLN HB2 H 2.206 0.03 1 1370 . 115 GLN HB3 H 2.206 0.03 1 1371 . 115 GLN CG C 34.475 0.12 1 1372 . 115 GLN HG2 H 2.575 0.03 1 1373 . 115 GLN HG3 H 2.575 0.03 1 1374 . 115 GLN NE2 N 112.731 0.15 1 1375 . 115 GLN HE22 H 7.648 0.03 2 1376 . 115 GLN HE21 H 6.762 0.03 2 1377 . 115 GLN C C 176.528 0.12 1 1378 . 116 ASP N N 118.985 0.15 1 1379 . 116 ASP H H 9.021 0.03 1 1380 . 116 ASP CA C 56.975 0.12 1 1381 . 116 ASP HA H 4.476 0.03 1 1382 . 116 ASP CB C 40.595 0.12 1 1383 . 116 ASP HB2 H 2.795 0.03 2 1384 . 116 ASP HB3 H 2.634 0.03 2 1385 . 116 ASP C C 177.935 0.12 1 1386 . 117 PHE N N 121.940 0.15 1 1387 . 117 PHE H H 8.014 0.03 1 1388 . 117 PHE CA C 62.843 0.12 1 1389 . 117 PHE HA H 4.150 0.03 1 1390 . 117 PHE CB C 39.658 0.12 1 1391 . 117 PHE HB2 H 3.417 0.03 2 1392 . 117 PHE HB3 H 3.128 0.03 2 1393 . 117 PHE CD1 C 133.320 0.12 1 1394 . 117 PHE HD1 H 7.340 0.03 1 1395 . 117 PHE CE1 C 130.842 0.12 1 1396 . 117 PHE HE1 H 6.972 0.03 1 1397 . 117 PHE CZ C 128.720 0.12 1 1398 . 117 PHE HZ H 5.888 0.03 1 1399 . 117 PHE CE2 C 130.842 0.12 1 1400 . 117 PHE HE2 H 6.972 0.03 1 1401 . 117 PHE CD2 C 133.320 0.12 1 1402 . 117 PHE HD2 H 7.340 0.03 1 1403 . 117 PHE C C 173.702 0.12 1 1404 . 118 LEU N N 110.934 0.15 1 1405 . 118 LEU H H 6.302 0.03 1 1406 . 118 LEU CA C 53.261 0.12 1 1407 . 118 LEU HA H 4.352 0.03 1 1408 . 118 LEU CB C 42.080 0.12 1 1409 . 118 LEU HB2 H 1.595 0.03 2 1410 . 118 LEU HB3 H 1.292 0.03 2 1411 . 118 LEU CG C 26.900 0.12 1 1412 . 118 LEU HG H 1.830 0.03 1 1413 . 118 LEU CD1 C 26.179 0.12 1 1414 . 118 LEU HD1 H 0.230 0.03 1 1415 . 118 LEU CD2 C 23.282 0.12 1 1416 . 118 LEU HD2 H 0.533 0.03 1 1417 . 118 LEU C C 171.845 0.12 1 1418 . 119 GLN N N 115.677 0.15 1 1419 . 119 GLN H H 7.716 0.03 1 1420 . 119 GLN CA C 56.913 0.12 1 1421 . 119 GLN HA H 3.975 0.03 1 1422 . 119 GLN CB C 26.202 0.12 1 1423 . 119 GLN HB2 H 2.110 0.03 2 1424 . 119 GLN HB3 H 1.900 0.03 2 1425 . 119 GLN CG C 34.475 0.12 1 1426 . 119 GLN HG2 H 2.353 0.03 2 1427 . 119 GLN HG3 H 2.165 0.03 2 1428 . 119 GLN NE2 N 111.740 0.15 1 1429 . 119 GLN HE22 H 7.531 0.03 2 1430 . 119 GLN HE21 H 6.771 0.03 2 1431 . 119 GLN C C 173.855 0.12 1 1432 . 120 LEU N N 117.273 0.15 1 1433 . 120 LEU H H 8.212 0.03 1 1434 . 120 LEU CA C 55.615 0.12 1 1435 . 120 LEU HA H 4.220 0.03 1 1436 . 120 LEU CB C 42.799 0.12 1 1437 . 120 LEU HB2 H 1.688 0.03 2 1438 . 120 LEU HB3 H 1.568 0.03 2 1439 . 120 LEU CG C 26.900 0.12 1 1440 . 120 LEU HG H 1.540 0.03 1 1441 . 120 LEU CD1 C 26.377 0.12 1 1442 . 120 LEU HD1 H 0.900 0.03 1 1443 . 120 LEU CD2 C 22.887 0.12 1 1444 . 120 LEU HD2 H 0.759 0.03 1 1445 . 120 LEU C C 175.960 0.12 1 1446 . 121 SER N N 114.436 0.15 1 1447 . 121 SER H H 8.038 0.03 1 1448 . 121 SER CA C 58.126 0.12 1 1449 . 121 SER HA H 4.450 0.03 1 1450 . 121 SER CB C 64.363 0.12 1 1451 . 121 SER HB2 H 3.808 0.03 1 1452 . 121 SER HB3 H 3.808 0.03 1 1453 . 121 SER C C 171.900 0.12 1 1454 . 122 LYS N N 123.828 0.15 1 1455 . 122 LYS H H 8.236 0.03 1 1456 . 122 LYS CA C 54.600 0.12 1 1457 . 122 LYS HA H 4.620 0.03 1 1458 . 122 LYS CB C 33.130 0.12 1 1459 . 122 LYS HB2 H 1.820 0.03 2 1460 . 122 LYS HB3 H 1.720 0.03 2 1461 . 122 LYS CG C 25.000 0.12 1 1462 . 122 LYS HG2 H 1.440 0.03 1 1463 . 122 LYS HG3 H 1.440 0.03 1 1464 . 122 LYS CD C 29.500 0.12 1 1465 . 122 LYS HD2 H 1.660 0.03 1 1466 . 122 LYS HD3 H 1.660 0.03 1 1467 . 122 LYS CE C 42.500 0.12 1 1468 . 122 LYS HE2 H 2.970 0.03 1 1469 . 122 LYS HE3 H 2.970 0.03 1 1470 . 122 LYS C C 172.800 0.12 1 1471 . 123 PRO CA C 63.817 0.12 1 1472 . 123 PRO HA H 4.402 0.03 1 1473 . 123 PRO CB C 32.210 0.12 1 1474 . 123 PRO HB2 H 2.259 0.03 2 1475 . 123 PRO HB3 H 1.938 0.03 2 1476 . 123 PRO CG C 27.618 0.12 1 1477 . 123 PRO HG2 H 1.980 0.03 1 1478 . 123 PRO HG3 H 1.980 0.03 1 1479 . 123 PRO CD C 50.937 0.12 1 1480 . 123 PRO HD2 H 3.780 0.03 2 1481 . 123 PRO HD3 H 3.650 0.03 2 1482 . 123 PRO C C 173.867 0.12 1 1483 . 124 ASN N N 123.826 0.15 1 1484 . 124 ASN H H 7.943 0.03 1 1485 . 124 ASN CA C 55.061 0.12 1 1486 . 124 ASN HA H 4.415 0.03 1 1487 . 124 ASN CB C 40.577 0.12 1 1488 . 124 ASN HB2 H 2.710 0.03 1 1489 . 124 ASN HB3 H 2.710 0.03 1 1490 . 124 ASN ND2 N 112.723 0.15 1 1491 . 124 ASN HD22 H 7.486 0.03 2 1492 . 124 ASN HD21 H 6.791 0.03 2 1493 . 124 ASN C C 177.500 0.12 1 stop_ save_