data_18137 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR assignment of the monomeric DUF59 domain of human Fam96a ; _BMRB_accession_number 18137 _BMRB_flat_file_name bmr18137.str _Entry_type original _Submission_date 2011-12-12 _Accession_date 2011-12-12 _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 Mas Caroline . . 2 Chen Kai-En . . 3 Brereton Ian M. . 4 Martin Jennifer L. . 5 Hill Justine M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 103 "13C chemical shifts" 460 "15N chemical shifts" 105 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-26 update BMRB 'update entry citation' 2012-01-09 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone resonance assignments of the monomeric DUF59 domain of human Fam96a.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22618863 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mas Caroline . . 2 Chen Kai-En . . 3 Brereton Ian M. . 4 Martin Jennifer L. . 5 Hill Justine M. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 7 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 117 _Page_last 120 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Fam96a _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Fam96a $Fam96a stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Fam96a _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Fam96a _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 130 _Mol_residue_sequence ; SNARIMEEKALEVYDLIRTI RDPEKPNTLEELEVVSESCV EVQEINEEEYLVIIRFTPTV PHCSLATLIGLCLRVKLQRC LPFKHKLEIYISEGTHSTEE DINKQINDKERVAAAMENPN LREIVEQCVL ; loop_ _Residue_seq_code _Residue_label 1 SER 2 ASN 3 ALA 4 ARG 5 ILE 6 MET 7 GLU 8 GLU 9 LYS 10 ALA 11 LEU 12 GLU 13 VAL 14 TYR 15 ASP 16 LEU 17 ILE 18 ARG 19 THR 20 ILE 21 ARG 22 ASP 23 PRO 24 GLU 25 LYS 26 PRO 27 ASN 28 THR 29 LEU 30 GLU 31 GLU 32 LEU 33 GLU 34 VAL 35 VAL 36 SER 37 GLU 38 SER 39 CYS 40 VAL 41 GLU 42 VAL 43 GLN 44 GLU 45 ILE 46 ASN 47 GLU 48 GLU 49 GLU 50 TYR 51 LEU 52 VAL 53 ILE 54 ILE 55 ARG 56 PHE 57 THR 58 PRO 59 THR 60 VAL 61 PRO 62 HIS 63 CYS 64 SER 65 LEU 66 ALA 67 THR 68 LEU 69 ILE 70 GLY 71 LEU 72 CYS 73 LEU 74 ARG 75 VAL 76 LYS 77 LEU 78 GLN 79 ARG 80 CYS 81 LEU 82 PRO 83 PHE 84 LYS 85 HIS 86 LYS 87 LEU 88 GLU 89 ILE 90 TYR 91 ILE 92 SER 93 GLU 94 GLY 95 THR 96 HIS 97 SER 98 THR 99 GLU 100 GLU 101 ASP 102 ILE 103 ASN 104 LYS 105 GLN 106 ILE 107 ASN 108 ASP 109 LYS 110 GLU 111 ARG 112 VAL 113 ALA 114 ALA 115 ALA 116 MET 117 GLU 118 ASN 119 PRO 120 ASN 121 LEU 122 ARG 123 GLU 124 ILE 125 VAL 126 GLU 127 GLN 128 CYS 129 VAL 130 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-15 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18548 Fam96a 97.69 143 100.00 100.00 1.43e-83 PDB 2M5H "Nmr Structure Note: Solution Structure Of Monomeric Human Fam96a" 97.69 139 100.00 100.00 1.65e-83 PDB 3UX2 "Crystal Structure Of Domain-Swapped Fam96a Major Dimer" 100.00 130 98.46 98.46 4.44e-84 PDB 3UX3 "Crystal Structure Of Domain-Swapped Fam96a Minor Dimer" 100.00 130 100.00 100.00 2.96e-86 DBJ BAB15496 "unnamed protein product [Homo sapiens]" 97.69 160 100.00 100.00 5.18e-84 DBJ BAG35105 "unnamed protein product [Homo sapiens]" 97.69 160 100.00 100.00 5.18e-84 DBJ BAH14131 "unnamed protein product [Homo sapiens]" 50.77 102 100.00 100.00 2.50e-36 GB AAH08865 "Family with sequence similarity 96, member A [Homo sapiens]" 97.69 160 100.00 100.00 5.18e-84 GB AAI02257 "Family with sequence similarity 96, member A [Bos taurus]" 97.69 160 97.64 100.00 1.19e-82 GB AAI51429 "Family with sequence similarity 96, member A [Bos taurus]" 97.69 160 97.64 100.00 1.06e-82 GB ABQ82139 "FAM96A [Equus caballus]" 97.69 160 97.64 99.21 1.12e-82 GB AIC57308 "FAM96A, partial [synthetic construct]" 97.69 160 100.00 100.00 5.18e-84 REF NP_001014812 "MIP18 family protein FAM96A isoform b precursor [Homo sapiens]" 50.77 102 100.00 100.00 2.50e-36 REF NP_001030282 "MIP18 family protein FAM96A precursor [Bos taurus]" 97.69 160 97.64 100.00 1.19e-82 REF NP_001092912 "MIP18 family protein FAM96A precursor [Equus caballus]" 97.69 160 97.64 99.21 1.12e-82 REF NP_001276037 "MIP18 family protein FAM96A isoform b precursor [Homo sapiens]" 50.77 102 100.00 100.00 2.50e-36 REF NP_115607 "MIP18 family protein FAM96A isoform a precursor [Homo sapiens]" 97.69 160 100.00 100.00 5.18e-84 SP Q3T0U7 "RecName: Full=MIP18 family protein FAM96A" 97.69 160 97.64 100.00 1.19e-82 SP Q9H5X1 "RecName: Full=MIP18 family protein FAM96A" 97.69 160 100.00 100.00 5.18e-84 TPG DAA25322 "TPA: family with sequence similarity 96, member A [Bos taurus]" 97.69 160 97.64 100.00 1.06e-82 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Fam96a 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 $Fam96a 'recombinant technology' . Escherichia coli 'BL21 (DE3)' pMCSG7 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 $Fam96a 0.8 mM '[U-100% 13C; U-100% 15N]' 'Hepes buffer' 25 mM 'natural abundance' NaCl 150 mM 'natural abundance' DTT 2 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CCcpNMR _Saveframe_category software _Name CCcpNMR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_CC-TOCSY-CONH_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CC-TOCSY-CONH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details ; Hepes buffer 25mM pH7 NaCl 150 mM DTT 2 mM ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 150 . mM pH 7 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HN(CO)CA' '3D CC-TOCSY-CONH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Fam96a _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 3 ALA C C 178.789 0.011 1 2 3 3 ALA CA C 54.320 0.023 1 3 3 3 ALA CB C 18.970 0.037 1 4 4 4 ARG H H 8.300 0.009 1 5 4 4 ARG C C 177.713 0.017 1 6 4 4 ARG CA C 57.719 0.027 1 7 4 4 ARG CB C 29.934 0.049 1 8 4 4 ARG CG C 26.918 0.100 1 9 4 4 ARG CD C 43.110 0.100 1 10 4 4 ARG N N 119.140 0.031 1 11 5 5 ILE H H 7.857 0.005 1 12 5 5 ILE C C 177.829 0.029 1 13 5 5 ILE CA C 63.114 0.052 1 14 5 5 ILE CB C 37.730 0.048 1 15 5 5 ILE CG1 C 28.206 0.100 1 16 5 5 ILE CG2 C 17.580 0.100 1 17 5 5 ILE CD1 C 12.638 0.100 1 18 5 5 ILE N N 120.575 0.017 1 19 6 6 MET H H 8.156 0.022 1 20 6 6 MET C C 178.597 0.061 1 21 6 6 MET CA C 56.927 0.066 1 22 6 6 MET CB C 31.839 0.015 1 23 6 6 MET CG C 33.158 0.100 1 24 6 6 MET N N 120.445 0.168 1 25 7 7 GLU H H 8.232 0.019 1 26 7 7 GLU C C 178.797 0.027 1 27 7 7 GLU CA C 59.542 0.034 1 28 7 7 GLU CB C 29.626 0.016 1 29 7 7 GLU CG C 36.487 0.100 1 30 7 7 GLU N N 122.098 0.027 1 31 8 8 GLU H H 8.273 0.008 1 32 8 8 GLU C C 180.081 0.008 1 33 8 8 GLU CA C 59.744 0.059 1 34 8 8 GLU CB C 29.276 0.067 1 35 8 8 GLU CG C 36.552 0.100 1 36 8 8 GLU N N 119.820 0.109 1 37 9 9 LYS H H 8.106 0.002 1 38 9 9 LYS C C 178.386 0.006 1 39 9 9 LYS CA C 58.679 0.083 1 40 9 9 LYS CB C 32.231 0.005 1 41 9 9 LYS CG C 24.823 0.100 1 42 9 9 LYS CD C 27.688 0.100 1 43 9 9 LYS N N 119.117 0.023 1 44 10 10 ALA H H 8.031 0.029 1 45 10 10 ALA C C 179.974 0.004 1 46 10 10 ALA CA C 55.654 0.025 1 47 10 10 ALA CB C 17.829 0.024 1 48 10 10 ALA N N 121.403 0.193 1 49 11 11 LEU H H 7.823 0.002 1 50 11 11 LEU C C 179.136 0.024 1 51 11 11 LEU CA C 57.916 0.019 1 52 11 11 LEU CB C 41.311 0.080 1 53 11 11 LEU CG C 26.958 0.100 1 54 11 11 LEU CD1 C 23.255 0.100 2 55 11 11 LEU CD2 C 24.777 0.100 2 56 11 11 LEU N N 119.321 0.011 1 57 12 12 GLU H H 7.821 0.010 1 58 12 12 GLU C C 179.842 0.004 1 59 12 12 GLU CA C 59.617 0.058 1 60 12 12 GLU CB C 29.748 0.032 1 61 12 12 GLU CG C 36.296 0.100 1 62 12 12 GLU N N 121.376 0.074 1 63 13 13 VAL H H 7.987 0.021 1 64 13 13 VAL C C 178.281 0.006 1 65 13 13 VAL CA C 66.587 0.002 1 66 13 13 VAL CB C 31.642 0.020 1 67 13 13 VAL CG2 C 22.931 0.100 1 68 13 13 VAL N N 117.705 0.147 1 69 14 14 TYR H H 8.805 0.005 1 70 14 14 TYR C C 176.505 0.007 1 71 14 14 TYR CA C 62.225 0.015 1 72 14 14 TYR CB C 38.022 0.088 1 73 14 14 TYR N N 120.488 0.018 1 74 15 15 ASP H H 8.402 0.029 1 75 15 15 ASP C C 178.002 0.012 1 76 15 15 ASP CA C 57.244 0.019 1 77 15 15 ASP CB C 40.777 0.079 1 78 15 15 ASP N N 117.034 0.246 1 79 16 16 LEU H H 7.180 0.013 1 80 16 16 LEU C C 178.539 0.003 1 81 16 16 LEU CA C 56.621 0.050 1 82 16 16 LEU CB C 43.921 0.088 1 83 16 16 LEU CG C 26.852 0.100 1 84 16 16 LEU CD2 C 23.401 0.100 1 85 16 16 LEU N N 115.351 0.010 1 86 17 17 ILE C C 177.633 0.007 1 87 17 17 ILE CA C 62.744 0.044 1 88 17 17 ILE CB C 38.064 0.043 1 89 17 17 ILE CG2 C 18.251 0.100 1 90 17 17 ILE N N 110.567 0.069 1 91 18 18 ARG H H 7.964 0.007 1 92 18 18 ARG C C 174.733 0.001 1 93 18 18 ARG CA C 58.445 0.035 1 94 18 18 ARG CB C 27.945 0.068 1 95 18 18 ARG CG C 25.930 0.100 1 96 18 18 ARG CD C 44.085 0.100 1 97 18 18 ARG N N 119.030 0.077 1 98 19 19 THR H H 6.674 0.005 1 99 19 19 THR C C 175.424 0.010 1 100 19 19 THR CA C 60.890 0.018 1 101 19 19 THR CB C 68.951 0.011 1 102 19 19 THR CG2 C 22.370 0.100 1 103 19 19 THR N N 102.778 0.022 1 104 20 20 ILE H H 7.095 0.004 1 105 20 20 ILE C C 174.923 0.011 1 106 20 20 ILE CA C 63.024 0.017 1 107 20 20 ILE CB C 38.409 0.010 1 108 20 20 ILE CG1 C 29.899 0.100 1 109 20 20 ILE CG2 C 17.202 0.100 1 110 20 20 ILE CD1 C 14.647 0.100 1 111 20 20 ILE N N 124.741 0.029 1 112 21 21 ARG H H 8.403 0.005 1 113 21 21 ARG C C 175.071 0.022 1 114 21 21 ARG CA C 56.090 0.082 1 115 21 21 ARG CB C 31.248 0.065 1 116 21 21 ARG CG C 27.763 0.100 1 117 21 21 ARG CD C 43.259 0.100 1 118 21 21 ARG N N 127.675 0.043 1 119 22 22 ASP H H 8.173 0.018 1 120 22 22 ASP C C 174.776 0.100 1 121 22 22 ASP CA C 53.729 0.100 1 122 22 22 ASP CB C 44.486 0.100 1 123 22 22 ASP N N 122.546 0.226 1 124 26 26 PRO C C 175.264 0.004 1 125 26 26 PRO CA C 62.301 0.100 1 126 26 26 PRO CB C 28.229 0.100 1 127 26 26 PRO CG C 27.179 0.100 1 128 26 26 PRO CD C 49.406 0.100 1 129 27 27 ASN H H 8.404 0.006 1 130 27 27 ASN C C 173.632 0.001 1 131 27 27 ASN CA C 53.564 0.049 1 132 27 27 ASN CB C 45.671 0.096 1 133 27 27 ASN N N 118.871 0.297 1 134 28 28 THR H H 8.770 0.005 1 135 28 28 THR C C 176.454 0.007 1 136 28 28 THR CA C 60.356 0.077 1 137 28 28 THR CB C 71.620 0.070 1 138 28 28 THR CG2 C 21.929 0.100 1 139 28 28 THR N N 109.001 0.021 1 140 29 29 LEU H H 9.030 0.004 1 141 29 29 LEU C C 179.897 0.011 1 142 29 29 LEU CA C 57.684 0.022 1 143 29 29 LEU CB C 42.050 0.029 1 144 29 29 LEU CG C 25.928 0.100 1 145 29 29 LEU CD2 C 20.075 0.100 1 146 29 29 LEU N N 115.732 0.022 1 147 30 30 GLU H H 7.696 0.009 1 148 30 30 GLU C C 180.126 0.011 1 149 30 30 GLU CA C 59.249 0.007 1 150 30 30 GLU CB C 30.816 0.054 1 151 30 30 GLU CG C 35.913 0.100 1 152 30 30 GLU N N 117.535 0.029 1 153 31 31 GLU H H 8.044 0.003 1 154 31 31 GLU C C 178.647 0.005 1 155 31 31 GLU CA C 59.370 0.034 1 156 31 31 GLU CB C 30.043 0.057 1 157 31 31 GLU CG C 37.534 0.100 1 158 31 31 GLU N N 123.185 0.027 1 159 32 32 LEU H H 7.483 0.005 1 160 32 32 LEU C C 175.605 0.026 1 161 32 32 LEU CA C 54.412 0.043 1 162 32 32 LEU CB C 43.090 0.075 1 163 32 32 LEU CG C 27.225 0.100 1 164 32 32 LEU CD1 C 21.451 0.100 2 165 32 32 LEU CD2 C 26.627 0.100 2 166 32 32 LEU N N 114.982 0.026 1 167 33 33 GLU H H 8.023 0.013 1 168 33 33 GLU C C 175.632 0.021 1 169 33 33 GLU CA C 58.002 0.030 1 170 33 33 GLU CB C 26.630 0.011 1 171 33 33 GLU CG C 37.244 0.100 1 172 33 33 GLU N N 114.049 0.126 1 173 34 34 VAL H H 8.456 0.014 1 174 34 34 VAL C C 177.354 0.009 1 175 34 34 VAL CA C 63.589 0.020 1 176 34 34 VAL CB C 32.973 0.003 1 177 34 34 VAL CG2 C 22.589 0.100 1 178 34 34 VAL N N 119.804 0.186 1 179 35 35 VAL H H 6.947 0.004 1 180 35 35 VAL C C 173.164 0.003 1 181 35 35 VAL CA C 58.156 0.053 1 182 35 35 VAL CB C 35.517 0.009 1 183 35 35 VAL CG1 C 17.713 0.100 2 184 35 35 VAL CG2 C 21.743 0.100 2 185 35 35 VAL N N 104.527 0.024 1 186 36 36 SER H H 7.931 0.003 1 187 36 36 SER C C 174.789 0.007 1 188 36 36 SER CA C 57.655 0.065 1 189 36 36 SER CB C 65.640 0.034 1 190 36 36 SER N N 113.575 0.020 1 191 37 37 GLU H H 9.072 0.003 1 192 37 37 GLU C C 177.361 0.011 1 193 37 37 GLU CA C 60.318 0.039 1 194 37 37 GLU CB C 29.266 0.094 1 195 37 37 GLU CG C 36.499 0.100 1 196 37 37 GLU N N 123.170 0.040 1 197 38 38 SER H H 7.756 0.003 1 198 38 38 SER C C 175.284 0.100 1 199 38 38 SER CA C 59.132 0.016 1 200 38 38 SER CB C 63.262 0.071 1 201 38 38 SER N N 109.685 0.039 1 202 39 39 CYS H H 7.971 0.019 1 203 39 39 CYS C C 172.727 0.006 1 204 39 39 CYS CA C 59.757 0.043 1 205 39 39 CYS CB C 28.177 0.056 1 206 39 39 CYS N N 120.145 0.158 1 207 40 40 VAL H H 7.109 0.005 1 208 40 40 VAL C C 174.078 0.020 1 209 40 40 VAL CA C 61.113 0.035 1 210 40 40 VAL CB C 34.077 0.011 1 211 40 40 VAL CG2 C 22.033 0.100 1 212 40 40 VAL N N 120.125 0.031 1 213 41 41 GLU H H 9.261 0.003 1 214 41 41 GLU C C 174.124 0.023 1 215 41 41 GLU CA C 55.060 0.047 1 216 41 41 GLU CB C 33.671 0.052 1 217 41 41 GLU CG C 36.479 0.100 1 218 41 41 GLU N N 128.075 0.015 1 219 42 42 VAL H H 8.695 0.003 1 220 42 42 VAL C C 174.559 0.005 1 221 42 42 VAL CA C 60.695 0.024 1 222 42 42 VAL CB C 34.351 0.052 1 223 42 42 VAL CG2 C 22.099 0.100 1 224 42 42 VAL N N 123.930 0.022 1 225 43 43 GLN H H 9.375 0.004 1 226 43 43 GLN C C 175.243 0.008 1 227 43 43 GLN CA C 53.684 0.030 1 228 43 43 GLN CB C 32.733 0.055 1 229 43 43 GLN CG C 33.033 0.100 1 230 43 43 GLN N N 123.559 0.012 1 231 44 44 GLU H H 9.071 0.003 1 232 44 44 GLU C C 176.460 0.011 1 233 44 44 GLU CA C 57.254 0.008 1 234 44 44 GLU CB C 31.106 0.020 1 235 44 44 GLU CG C 36.850 0.100 1 236 44 44 GLU N N 124.783 0.036 1 237 45 45 ILE H H 8.316 0.020 1 238 45 45 ILE C C 175.811 0.003 1 239 45 45 ILE CA C 63.301 0.045 1 240 45 45 ILE CB C 38.822 0.041 1 241 45 45 ILE CG1 C 27.388 0.100 1 242 45 45 ILE CG2 C 17.725 0.100 1 243 45 45 ILE CD1 C 13.516 0.100 1 244 45 45 ILE N N 125.075 0.016 1 245 46 46 ASN H H 8.069 0.013 1 246 46 46 ASN C C 173.839 0.005 1 247 46 46 ASN CA C 52.402 0.009 1 248 46 46 ASN CB C 39.483 0.045 1 249 46 46 ASN N N 116.765 0.151 1 250 47 47 GLU H H 8.664 0.012 1 251 47 47 GLU C C 176.543 0.008 1 252 47 47 GLU CA C 59.154 0.044 1 253 47 47 GLU CB C 29.272 0.021 1 254 47 47 GLU CG C 36.388 0.100 1 255 47 47 GLU N N 116.895 0.116 1 256 48 48 GLU H H 8.703 0.005 1 257 48 48 GLU C C 174.329 0.005 1 258 48 48 GLU CA C 56.521 0.017 1 259 48 48 GLU CB C 30.677 0.014 1 260 48 48 GLU CG C 36.548 0.100 1 261 48 48 GLU N N 117.168 0.011 1 262 49 49 GLU H H 7.473 0.004 1 263 49 49 GLU C C 174.266 0.001 1 264 49 49 GLU CA C 56.055 0.025 1 265 49 49 GLU CB C 33.371 0.018 1 266 49 49 GLU CG C 36.703 0.100 1 267 49 49 GLU N N 119.285 0.310 1 268 50 50 TYR H H 8.082 0.016 1 269 50 50 TYR C C 174.106 0.008 1 270 50 50 TYR CA C 57.684 0.011 1 271 50 50 TYR CB C 41.528 0.036 1 272 50 50 TYR N N 122.260 0.179 1 273 51 51 LEU H H 9.562 0.003 1 274 51 51 LEU C C 174.454 0.013 1 275 51 51 LEU CA C 54.054 0.041 1 276 51 51 LEU CB C 44.284 0.030 1 277 51 51 LEU CG C 27.709 0.100 1 278 51 51 LEU CD1 C 26.267 0.100 2 279 51 51 LEU CD2 C 22.819 0.100 2 280 51 51 LEU N N 125.640 0.023 1 281 52 52 VAL H H 9.327 0.006 1 282 52 52 VAL C C 173.358 0.002 1 283 52 52 VAL CA C 61.155 0.034 1 284 52 52 VAL CB C 33.530 0.011 1 285 52 52 VAL CG1 C 20.807 0.100 2 286 52 52 VAL CG2 C 22.536 0.100 2 287 52 52 VAL N N 128.196 0.055 1 288 53 53 ILE H H 9.395 0.004 1 289 53 53 ILE C C 176.134 0.006 1 290 53 53 ILE CA C 59.916 0.016 1 291 53 53 ILE CB C 40.993 0.046 1 292 53 53 ILE CG1 C 27.886 0.100 1 293 53 53 ILE CG2 C 18.018 0.100 1 294 53 53 ILE N N 127.507 0.022 1 295 54 54 ILE H H 8.586 0.003 1 296 54 54 ILE C C 174.567 0.015 1 297 54 54 ILE CA C 59.548 0.011 1 298 54 54 ILE CB C 41.498 0.052 1 299 54 54 ILE CG1 C 27.755 0.100 1 300 54 54 ILE CG2 C 17.763 0.100 1 301 54 54 ILE N N 125.722 0.027 1 302 55 55 ARG H H 8.264 0.010 1 303 55 55 ARG C C 175.607 0.013 1 304 55 55 ARG CA C 54.024 0.024 1 305 55 55 ARG CB C 31.668 0.011 1 306 55 55 ARG CG C 28.775 0.100 1 307 55 55 ARG CD C 43.143 0.100 1 308 55 55 ARG N N 126.491 0.081 1 309 56 56 PHE H H 8.706 0.004 1 310 56 56 PHE C C 173.472 0.004 1 311 56 56 PHE CA C 55.036 0.002 1 312 56 56 PHE CB C 42.056 0.033 1 313 56 56 PHE N N 119.286 0.067 1 314 57 57 THR H H 9.348 0.007 1 315 57 57 THR C C 172.180 0.100 1 316 57 57 THR CB C 70.653 0.100 1 317 57 57 THR N N 118.565 0.048 1 318 59 59 THR C C 174.925 0.100 1 319 59 59 THR CA C 64.708 0.100 1 320 59 59 THR CB C 69.295 0.100 1 321 59 59 THR CG2 C 23.209 0.100 1 322 60 60 VAL H H 7.159 0.009 1 323 60 60 VAL CA C 68.223 0.100 1 324 60 60 VAL CB C 39.446 0.100 1 325 60 60 VAL N N 114.028 0.107 1 326 61 61 PRO C C 176.404 0.023 1 327 61 61 PRO CA C 65.263 0.007 1 328 61 61 PRO CB C 32.929 0.097 1 329 62 62 HIS H H 8.817 0.007 1 330 62 62 HIS C C 176.575 0.100 1 331 62 62 HIS CA C 56.774 0.100 1 332 62 62 HIS CB C 33.455 0.100 1 333 62 62 HIS N N 115.599 0.041 1 334 65 65 LEU C C 175.282 0.010 1 335 65 65 LEU CA C 53.340 0.100 1 336 65 65 LEU CB C 38.926 0.042 1 337 65 65 LEU CG C 20.853 0.100 1 338 66 66 ALA H H 8.472 0.013 1 339 66 66 ALA C C 178.896 0.100 1 340 66 66 ALA CA C 56.392 0.080 1 341 66 66 ALA CB C 18.873 0.066 1 342 66 66 ALA N N 124.870 0.144 1 343 67 67 THR H H 8.275 0.004 1 344 67 67 THR C C 176.125 0.031 1 345 67 67 THR CA C 66.639 0.082 1 346 67 67 THR CB C 68.315 0.019 1 347 67 67 THR CG2 C 21.405 0.100 1 348 67 67 THR N N 111.897 0.025 1 349 68 68 LEU H H 7.596 0.005 1 350 68 68 LEU C C 179.241 0.030 1 351 68 68 LEU CA C 58.602 0.005 1 352 68 68 LEU CB C 42.683 0.053 1 353 68 68 LEU CG C 27.763 0.100 1 354 68 68 LEU CD2 C 25.126 0.100 1 355 68 68 LEU N N 122.585 0.077 1 356 69 69 ILE H H 8.451 0.022 1 357 69 69 ILE C C 177.912 0.013 1 358 69 69 ILE CA C 66.460 0.018 1 359 69 69 ILE CB C 37.691 0.051 1 360 69 69 ILE CG2 C 16.932 0.100 1 361 69 69 ILE N N 120.513 0.139 1 362 70 70 GLY H H 8.125 0.007 1 363 70 70 GLY C C 175.210 0.013 1 364 70 70 GLY CA C 47.837 0.061 1 365 70 70 GLY N N 105.332 0.014 1 366 71 71 LEU H H 8.242 0.047 1 367 71 71 LEU C C 178.456 0.008 1 368 71 71 LEU CA C 58.022 0.073 1 369 71 71 LEU CB C 42.268 0.050 1 370 71 71 LEU CG C 26.123 0.100 1 371 71 71 LEU CD2 C 24.416 0.100 1 372 71 71 LEU N N 121.555 0.151 1 373 72 72 CYS H H 8.142 0.007 1 374 72 72 CYS C C 176.268 0.004 1 375 72 72 CYS CA C 64.255 0.030 1 376 72 72 CYS CB C 27.574 0.045 1 377 72 72 CYS N N 116.762 0.022 1 378 73 73 LEU H H 7.983 0.002 1 379 73 73 LEU C C 177.106 0.003 1 380 73 73 LEU CA C 58.397 0.009 1 381 73 73 LEU CB C 42.438 0.033 1 382 73 73 LEU CG C 29.994 0.100 1 383 73 73 LEU CD2 C 26.163 0.100 1 384 73 73 LEU N N 117.260 0.037 1 385 74 74 ARG H H 7.542 0.016 1 386 74 74 ARG C C 178.386 0.017 1 387 74 74 ARG CA C 59.957 0.049 1 388 74 74 ARG CG C 27.488 0.100 1 389 74 74 ARG CD C 43.140 0.100 1 390 74 74 ARG N N 115.846 0.049 1 391 75 75 VAL H H 8.723 0.004 1 392 75 75 VAL C C 178.031 0.009 1 393 75 75 VAL CA C 66.630 0.009 1 394 75 75 VAL CB C 31.672 0.062 1 395 75 75 VAL CG1 C 20.579 0.100 2 396 75 75 VAL CG2 C 23.143 0.100 2 397 75 75 VAL N N 118.843 0.028 1 398 76 76 LYS H H 8.272 0.009 1 399 76 76 LYS C C 178.597 0.017 1 400 76 76 LYS CA C 59.516 0.024 1 401 76 76 LYS CB C 32.853 0.094 1 402 76 76 LYS CG C 25.505 0.100 1 403 76 76 LYS CD C 29.867 0.100 1 404 76 76 LYS N N 118.091 0.192 1 405 77 77 LEU H H 7.517 0.011 1 406 77 77 LEU C C 178.580 0.016 1 407 77 77 LEU CA C 58.063 0.067 1 408 77 77 LEU CB C 40.139 0.053 1 409 77 77 LEU CG C 27.646 0.100 1 410 77 77 LEU CD2 C 26.494 0.100 1 411 77 77 LEU N N 115.856 0.018 1 412 78 78 GLN H H 8.638 0.013 1 413 78 78 GLN C C 179.017 0.034 1 414 78 78 GLN CA C 59.431 0.026 1 415 78 78 GLN CB C 28.327 0.030 1 416 78 78 GLN CG C 34.153 0.100 1 417 78 78 GLN N N 118.930 0.092 1 418 79 79 ARG H H 7.815 0.005 1 419 79 79 ARG C C 178.975 0.013 1 420 79 79 ARG CA C 59.027 0.077 1 421 79 79 ARG CB C 32.169 0.007 1 422 79 79 ARG CG C 27.717 0.100 1 423 79 79 ARG CD C 43.785 0.100 1 424 79 79 ARG N N 115.170 0.016 1 425 80 80 CYS H H 7.754 0.006 1 426 80 80 CYS C C 175.431 0.009 1 427 80 80 CYS CA C 60.534 0.032 1 428 80 80 CYS CB C 31.827 0.042 1 429 80 80 CYS N N 112.156 0.116 1 430 81 81 LEU H H 8.612 0.014 1 431 81 81 LEU C C 177.156 0.100 1 432 81 81 LEU CA C 53.292 0.100 1 433 81 81 LEU CB C 41.812 0.100 1 434 81 81 LEU N N 123.018 0.259 1 435 82 82 PRO C C 175.335 0.005 1 436 82 82 PRO CA C 63.862 0.028 1 437 82 82 PRO CB C 31.157 0.100 1 438 82 82 PRO CG C 27.076 0.100 1 439 83 83 PHE H H 6.366 0.006 1 440 83 83 PHE C C 174.457 0.019 1 441 83 83 PHE CA C 53.610 0.005 1 442 83 83 PHE CB C 40.805 0.064 1 443 83 83 PHE N N 113.719 0.019 1 444 84 84 LYS H H 9.220 0.003 1 445 84 84 LYS C C 176.553 0.014 1 446 84 84 LYS CA C 57.894 0.004 1 447 84 84 LYS CB C 32.397 0.018 1 448 84 84 LYS CG C 25.551 0.100 1 449 84 84 LYS CD C 29.333 0.100 1 450 84 84 LYS N N 124.547 0.032 1 451 85 85 HIS H H 8.521 0.017 1 452 85 85 HIS C C 173.662 0.020 1 453 85 85 HIS CA C 55.607 0.067 1 454 85 85 HIS CB C 32.341 0.076 1 455 85 85 HIS N N 119.761 0.100 1 456 86 86 LYS H H 8.750 0.005 1 457 86 86 LYS C C 175.173 1.287 1 458 86 86 LYS CA C 55.370 0.010 1 459 86 86 LYS CB C 35.588 0.016 1 460 86 86 LYS CG C 25.399 0.100 1 461 86 86 LYS CD C 29.229 0.100 1 462 86 86 LYS CE C 41.511 0.100 1 463 86 86 LYS N N 121.289 0.024 1 464 87 87 LEU H H 8.938 0.003 1 465 87 87 LEU C C 176.160 0.019 1 466 87 87 LEU CA C 53.633 0.003 1 467 87 87 LEU CB C 45.637 0.090 1 468 87 87 LEU CG C 27.640 0.100 1 469 87 87 LEU N N 125.303 0.018 1 470 88 88 GLU H H 9.349 0.004 1 471 88 88 GLU C C 173.337 0.009 1 472 88 88 GLU CA C 55.512 0.024 1 473 88 88 GLU CB C 33.091 0.041 1 474 88 88 GLU CG C 36.188 0.100 1 475 88 88 GLU N N 128.711 0.057 1 476 89 89 ILE H H 8.315 0.005 1 477 89 89 ILE C C 173.610 0.013 1 478 89 89 ILE CA C 58.705 0.043 1 479 89 89 ILE CB C 40.782 0.063 1 480 89 89 ILE CG1 C 27.139 0.100 1 481 89 89 ILE CG2 C 19.666 0.100 1 482 89 89 ILE N N 121.049 0.006 1 483 90 90 TYR H H 9.069 0.004 1 484 90 90 TYR C C 175.154 0.009 1 485 90 90 TYR CA C 55.280 0.013 1 486 90 90 TYR CB C 43.187 0.054 1 487 90 90 TYR N N 121.331 0.034 1 488 91 91 ILE H H 9.045 0.005 1 489 91 91 ILE C C 177.328 0.100 1 490 91 91 ILE CA C 59.647 0.100 1 491 91 91 ILE CB C 38.701 0.100 1 492 91 91 ILE N N 121.152 0.037 1 493 101 101 ASP C C 178.394 0.100 1 494 101 101 ASP CA C 59.061 0.100 1 495 101 101 ASP CB C 41.067 0.100 1 496 102 102 ILE H H 7.968 0.023 1 497 102 102 ILE C C 177.219 0.002 1 498 102 102 ILE CA C 65.035 0.014 1 499 102 102 ILE CB C 37.751 0.025 1 500 102 102 ILE CG2 C 17.760 0.100 1 501 102 102 ILE N N 121.586 0.225 1 502 103 103 ASN H H 8.499 0.005 1 503 103 103 ASN C C 178.550 0.012 1 504 103 103 ASN CA C 55.693 0.093 1 505 103 103 ASN CB C 38.126 0.059 1 506 103 103 ASN N N 117.787 0.016 1 507 104 104 LYS H H 7.824 0.020 1 508 104 104 LYS C C 179.087 0.022 1 509 104 104 LYS CA C 59.529 0.069 1 510 104 104 LYS CB C 32.521 0.064 1 511 104 104 LYS CG C 25.318 0.100 1 512 104 104 LYS CD C 29.360 0.100 1 513 104 104 LYS N N 119.416 0.188 1 514 105 105 GLN H H 7.848 0.022 1 515 105 105 GLN C C 178.183 0.013 1 516 105 105 GLN CA C 59.531 0.001 1 517 105 105 GLN CB C 29.079 0.019 1 518 105 105 GLN CG C 34.275 0.100 1 519 105 105 GLN N N 117.500 0.107 1 520 106 106 ILE H H 7.967 0.002 1 521 106 106 ILE C C 175.569 0.008 1 522 106 106 ILE CA C 62.970 0.012 1 523 106 106 ILE CB C 37.946 0.006 1 524 106 106 ILE CG1 C 25.322 0.100 1 525 106 106 ILE CG2 C 18.129 0.100 1 526 106 106 ILE N N 108.677 0.052 1 527 107 107 ASN H H 7.164 0.010 1 528 107 107 ASN C C 173.519 0.008 1 529 107 107 ASN CA C 53.958 0.040 1 530 107 107 ASN CB C 41.336 0.078 1 531 107 107 ASN N N 115.809 0.010 1 532 108 108 ASP H H 7.544 0.006 1 533 108 108 ASP C C 176.324 0.009 1 534 108 108 ASP CA C 54.215 0.079 1 535 108 108 ASP CB C 42.182 0.088 1 536 108 108 ASP N N 122.129 0.021 1 537 109 109 LYS H H 8.947 0.003 1 538 109 109 LYS C C 179.002 0.006 1 539 109 109 LYS CA C 60.309 0.036 1 540 109 109 LYS CB C 32.318 0.048 1 541 109 109 LYS CG C 24.710 0.100 1 542 109 109 LYS CD C 29.366 0.100 1 543 109 109 LYS N N 126.758 0.029 1 544 110 110 GLU H H 8.392 0.005 1 545 110 110 GLU C C 179.736 0.004 1 546 110 110 GLU CA C 59.274 0.097 1 547 110 110 GLU CB C 29.234 0.015 1 548 110 110 GLU CG C 36.857 0.100 1 549 110 110 GLU N N 119.453 0.053 1 550 111 111 ARG H H 8.042 0.005 1 551 111 111 ARG C C 180.142 0.016 1 552 111 111 ARG CA C 58.538 0.002 1 553 111 111 ARG CB C 29.856 0.063 1 554 111 111 ARG CG C 27.266 0.100 1 555 111 111 ARG CD C 43.063 0.100 1 556 111 111 ARG N N 121.632 0.019 1 557 112 112 VAL H H 8.524 0.008 1 558 112 112 VAL C C 177.190 0.007 1 559 112 112 VAL CA C 66.731 0.013 1 560 112 112 VAL CB C 31.954 0.004 1 561 112 112 VAL CG1 C 22.580 0.100 2 562 112 112 VAL CG2 C 20.753 0.100 2 563 112 112 VAL N N 122.469 0.171 1 564 113 113 ALA H H 7.679 0.007 1 565 113 113 ALA C C 180.414 0.009 1 566 113 113 ALA CA C 55.160 0.041 1 567 113 113 ALA CB C 17.913 0.013 1 568 113 113 ALA N N 120.053 0.150 1 569 114 114 ALA H H 7.779 0.012 1 570 114 114 ALA C C 181.004 0.002 1 571 114 114 ALA CA C 54.880 0.007 1 572 114 114 ALA CB C 18.138 0.014 1 573 114 114 ALA N N 118.594 0.218 1 574 115 115 ALA H H 7.908 0.010 1 575 115 115 ALA C C 179.314 0.011 1 576 115 115 ALA CA C 55.143 0.008 1 577 115 115 ALA CB C 18.544 0.066 1 578 115 115 ALA N N 122.157 0.261 1 579 116 116 MET H H 7.731 0.003 1 580 116 116 MET C C 177.621 0.010 1 581 116 116 MET CA C 55.456 0.032 1 582 116 116 MET CB C 30.947 0.047 1 583 116 116 MET CG C 32.748 0.100 1 584 116 116 MET N N 111.990 0.021 1 585 117 117 GLU H H 7.428 0.022 1 586 117 117 GLU C C 176.327 0.007 1 587 117 117 GLU CA C 56.443 0.040 1 588 117 117 GLU CB C 30.093 0.038 1 589 117 117 GLU CG C 36.266 0.017 1 590 117 117 GLU N N 117.032 0.091 1 591 118 118 ASN H H 7.605 0.004 1 592 118 118 ASN C C 174.110 0.100 1 593 118 118 ASN CA C 50.606 0.100 1 594 118 118 ASN CB C 39.110 0.100 1 595 118 118 ASN N N 121.678 0.036 1 596 119 119 PRO C C 178.525 0.004 1 597 119 119 PRO CA C 65.239 0.015 1 598 119 119 PRO CB C 32.186 0.033 1 599 119 119 PRO CG C 27.327 0.100 1 600 120 120 ASN H H 7.925 0.015 1 601 120 120 ASN C C 177.101 0.009 1 602 120 120 ASN CA C 56.057 0.039 1 603 120 120 ASN CB C 38.534 0.012 1 604 120 120 ASN N N 114.686 0.029 1 605 121 121 LEU H H 7.383 0.002 1 606 121 121 LEU C C 178.506 0.005 1 607 121 121 LEU CA C 57.328 0.047 1 608 121 121 LEU CB C 41.409 0.058 1 609 121 121 LEU CG C 27.264 0.100 1 610 121 121 LEU CD1 C 23.169 0.100 2 611 121 121 LEU CD2 C 25.287 0.100 2 612 121 121 LEU N N 119.598 0.014 1 613 122 122 ARG H H 8.559 0.020 1 614 122 122 ARG C C 177.660 0.008 1 615 122 122 ARG CA C 59.756 0.023 1 616 122 122 ARG CB C 29.958 0.008 1 617 122 122 ARG CG C 27.412 0.100 1 618 122 122 ARG CD C 43.149 0.100 1 619 122 122 ARG N N 119.151 0.048 1 620 123 123 GLU C C 178.950 0.008 1 621 123 123 GLU CA C 59.465 0.010 1 622 123 123 GLU CB C 29.596 0.028 1 623 123 123 GLU CG C 36.135 0.100 1 624 123 123 GLU N N 115.328 0.240 1 625 124 124 ILE H H 7.133 0.005 1 626 124 124 ILE C C 178.083 0.015 1 627 124 124 ILE CA C 64.614 0.060 1 628 124 124 ILE CB C 38.382 0.052 1 629 124 124 ILE CG1 C 28.457 0.100 1 630 124 124 ILE CG2 C 18.134 0.100 1 631 124 124 ILE CD1 C 13.188 0.100 1 632 124 124 ILE N N 119.226 0.019 1 633 125 125 VAL H H 8.059 0.019 1 634 125 125 VAL C C 178.338 0.006 1 635 125 125 VAL CA C 66.495 0.006 1 636 125 125 VAL CB C 32.097 0.003 1 637 125 125 VAL CG1 C 20.970 0.100 2 638 125 125 VAL CG2 C 22.979 0.100 2 639 125 125 VAL N N 120.531 0.093 1 640 126 126 GLU H H 8.437 0.002 1 641 126 126 GLU C C 179.571 0.008 1 642 126 126 GLU CA C 58.852 0.030 1 643 126 126 GLU CB C 28.573 0.032 1 644 126 126 GLU CG C 35.436 0.100 1 645 126 126 GLU N N 114.299 0.022 1 646 127 127 GLN H H 7.568 0.005 1 647 127 127 GLN C C 178.462 0.002 1 648 127 127 GLN CA C 58.204 0.018 1 649 127 127 GLN CB C 28.788 0.034 1 650 127 127 GLN CG C 34.044 0.100 1 651 127 127 GLN N N 116.069 0.085 1 652 128 128 CYS H H 8.083 0.003 1 653 128 128 CYS C C 176.696 0.009 1 654 128 128 CYS CA C 63.611 0.079 1 655 128 128 CYS CB C 29.147 0.029 1 656 128 128 CYS N N 116.558 0.019 1 657 129 129 VAL H H 7.622 0.004 1 658 129 129 VAL C C 174.896 0.007 1 659 129 129 VAL CA C 61.318 0.036 1 660 129 129 VAL CB C 31.622 0.042 1 661 129 129 VAL CG1 C 18.030 0.100 2 662 129 129 VAL CG2 C 21.761 0.100 2 663 129 129 VAL N N 108.669 0.040 1 664 130 130 LEU H H 6.905 0.006 1 665 130 130 LEU C C 182.564 0.100 1 666 130 130 LEU CA C 57.956 0.100 1 667 130 130 LEU CB C 42.947 0.100 1 668 130 130 LEU N N 128.048 0.017 1 stop_ save_