data_18178 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of AGR2 residues 41-175 ; _BMRB_accession_number 18178 _BMRB_flat_file_name bmr18178.str _Entry_type original _Submission_date 2012-01-04 _Accession_date 2012-01-04 _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 Patel Pryank . . 2 Clarke Christopher J. . 3 Barraclough Dong L. . 4 Rudland Philip S. . 5 Barraclough Roger . . 6 Lian Lu-Yun . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 199 "13C chemical shifts" 480 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-03-12 update BMRB 'update entry citation' 2013-01-07 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 18179 'E60A mutant AGR2' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23274113 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Patel Pryank . . 2 Clarke Christopher . . 3 Barraclough 'Dong Liu' . . 4 Jowitt 'Thomas Adam' . . 5 Rudland 'Philip Spencer' . . 6 Barraclough Roger . . 7 Lian Lu-Yun . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 425 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 929 _Page_last 943 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'AGR2 residues 41-175' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $AGR2 entity_2 $AGR2 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_AGR2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common AGR2 _Molecular_mass 15615.084 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 140 _Mol_residue_sequence ; IDPFTPQTLSRGWGDQLIWT QTYEEALYKSKTSNKPLMII HHLDECPHSQALKKVFAENK EIQKLAEQFVLLNLVYETTD KHLSPDGQYVPRIMFVDPSL TVRADITGRYSNRLYAYEPA DTALLLDNMKKALKLLKTEL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . ILE 2 . ASP 3 . PRO 4 . PHE 5 . THR 6 41 PRO 7 42 GLN 8 43 THR 9 44 LEU 10 45 SER 11 46 ARG 12 47 GLY 13 48 TRP 14 49 GLY 15 50 ASP 16 51 GLN 17 52 LEU 18 53 ILE 19 54 TRP 20 55 THR 21 56 GLN 22 57 THR 23 58 TYR 24 59 GLU 25 60 GLU 26 61 ALA 27 62 LEU 28 63 TYR 29 64 LYS 30 65 SER 31 66 LYS 32 67 THR 33 68 SER 34 69 ASN 35 70 LYS 36 71 PRO 37 72 LEU 38 73 MET 39 74 ILE 40 75 ILE 41 76 HIS 42 77 HIS 43 78 LEU 44 79 ASP 45 80 GLU 46 81 CYS 47 82 PRO 48 83 HIS 49 84 SER 50 85 GLN 51 86 ALA 52 87 LEU 53 88 LYS 54 89 LYS 55 90 VAL 56 91 PHE 57 92 ALA 58 93 GLU 59 94 ASN 60 95 LYS 61 96 GLU 62 97 ILE 63 98 GLN 64 99 LYS 65 100 LEU 66 101 ALA 67 102 GLU 68 103 GLN 69 104 PHE 70 105 VAL 71 106 LEU 72 107 LEU 73 108 ASN 74 109 LEU 75 110 VAL 76 111 TYR 77 112 GLU 78 113 THR 79 114 THR 80 115 ASP 81 116 LYS 82 117 HIS 83 118 LEU 84 119 SER 85 120 PRO 86 121 ASP 87 122 GLY 88 123 GLN 89 124 TYR 90 125 VAL 91 126 PRO 92 127 ARG 93 128 ILE 94 129 MET 95 130 PHE 96 131 VAL 97 132 ASP 98 133 PRO 99 134 SER 100 135 LEU 101 136 THR 102 137 VAL 103 138 ARG 104 139 ALA 105 140 ASP 106 141 ILE 107 142 THR 108 143 GLY 109 144 ARG 110 145 TYR 111 146 SER 112 147 ASN 113 148 ARG 114 149 LEU 115 150 TYR 116 151 ALA 117 152 TYR 118 153 GLU 119 154 PRO 120 155 ALA 121 156 ASP 122 157 THR 123 158 ALA 124 159 LEU 125 160 LEU 126 161 LEU 127 162 ASP 128 163 ASN 129 164 MET 130 165 LYS 131 166 LYS 132 167 ALA 133 168 LEU 134 169 LYS 135 170 LEU 136 171 LEU 137 172 LYS 138 173 THR 139 174 GLU 140 175 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 18179 AGR2_E60A 100.00 140 99.29 99.29 2.36e-97 PDB 2LNS "Solution Structure Of Agr2 Residues 41-175" 100.00 140 100.00 100.00 4.29e-98 PDB 2LNT "Solution Structure Of E60a Mutant Agr2" 100.00 140 99.29 99.29 2.36e-97 DBJ BAD96787 "anterior gradient 2 homolog [Homo sapiens]" 98.57 175 97.83 97.83 4.10e-93 DBJ BAG35784 "unnamed protein product [Homo sapiens]" 98.57 175 97.83 98.55 6.42e-94 EMBL CAH92219 "hypothetical protein [Pongo abelii]" 98.57 175 97.83 97.83 5.94e-94 GB AAC77358 "secreted cement gland protein XAG-2 homolog [Homo sapiens]" 98.57 175 98.55 98.55 2.96e-94 GB AAC82614 "secreted cement gland protein XAG-2 homolog [Homo sapiens]" 98.57 175 98.55 98.55 2.96e-94 GB AAF22484 "putative secreted protein XAG [Homo sapiens]" 98.57 175 98.55 98.55 2.96e-94 GB AAH15503 "Anterior gradient homolog 2 (Xenopus laevis) [Homo sapiens]" 98.57 175 98.55 98.55 2.96e-94 GB AAL54870 "XAG-2 homolog long protein [Homo sapiens]" 98.57 175 98.55 98.55 2.96e-94 REF NP_001127525 "anterior gradient protein 2 homolog precursor [Pongo abelii]" 98.57 175 97.83 97.83 5.94e-94 REF NP_001181233 "anterior gradient protein 2 homolog precursor [Macaca mulatta]" 98.57 175 97.83 98.55 6.70e-94 REF NP_006399 "anterior gradient protein 2 homolog precursor [Homo sapiens]" 98.57 175 98.55 98.55 2.96e-94 REF XP_002751578 "PREDICTED: anterior gradient protein 2 homolog [Callithrix jacchus]" 98.57 175 97.83 98.55 4.24e-94 REF XP_002751579 "PREDICTED: anterior gradient protein 2 homolog [Callithrix jacchus]" 98.57 175 97.83 98.55 4.24e-94 SP O95994 "RecName: Full=Anterior gradient protein 2 homolog; Short=AG-2; Short=hAG-2; AltName: Full=HPC8; AltName: Full=Secreted cement g" 98.57 175 98.55 98.55 2.96e-94 SP Q5R7P1 "RecName: Full=Anterior gradient protein 2 homolog; Flags: Precursor" 98.57 175 97.83 97.83 5.94e-94 TPG DAA30743 "TPA: anterior gradient 2 homolog [Bos taurus]" 96.43 175 97.04 99.26 4.83e-92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $AGR2 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 $AGR2 'recombinant technology' . Escherichia coli . pET-151D stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '13C/15N/2H AGR2' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AGR2 1 mM '[U-13C; U-15N; U-2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' MES 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details '13CH3 ILV labelled' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AGR2 1 mM '[U-13C; U-15N; U-2H]' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' MES 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type 'filamentous virus' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AGR2 1 mM [U-15N] 'Pf1 phage' 10 mg 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' MES 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AGR2 1 mM [U-15N] PEG:Hexanol 5 % 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' MES 20 mM 'natural abundance' NaCl 100 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CNSSOLVE _Saveframe_category software _Name CNSSOLVE _Version . loop_ _Vendor _Address _Electronic_address 'Brunger, Adams, Clore, Gros, Nilges and Read' . . stop_ loop_ _Task refinement 'structure solution' stop_ _Details . save_ save_Analysis _Saveframe_category software _Name Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_3D_HN(COCA)CB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(COCA)CB' _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_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_2 save_ save_3D_1H-13C_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_IPAP_11 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP _Sample_label $sample_3 save_ save_IPAP_12 _Saveframe_category NMR_applied_experiment _Experiment_name IPAP _Sample_label $sample_4 save_ save_3D_HN(CA)CO_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 . M pH 6.5 . 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 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0 na 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC' '3D HN(COCA)CB' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name entity_1 _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 41 6 PRO C C 177.082 0.000 1 2 41 6 PRO CA C 62.552 0.016 1 3 41 6 PRO CB C 31.250 0.000 1 4 42 7 GLN H H 8.364 0.002 1 5 42 7 GLN C C 177.981 0.014 1 6 42 7 GLN CA C 56.032 0.017 1 7 42 7 GLN CB C 30.915 0.070 1 8 42 7 GLN N N 120.179 0.058 1 9 43 8 THR H H 8.350 0.003 1 10 43 8 THR C C 175.020 0.033 1 11 43 8 THR CA C 59.007 0.027 1 12 43 8 THR CB C 70.140 0.038 1 13 43 8 THR N N 114.869 0.058 1 14 44 9 LEU H H 7.370 0.007 1 15 44 9 LEU HD1 H 0.687 0.006 1 16 44 9 LEU HD2 H 0.709 0.005 1 17 44 9 LEU C C 178.673 0.022 1 18 44 9 LEU CA C 56.229 0.064 1 19 44 9 LEU CB C 41.446 0.062 1 20 44 9 LEU CG C 27.097 0.008 1 21 44 9 LEU CD1 C 24.237 0.042 1 22 44 9 LEU CD2 C 25.080 0.061 1 23 44 9 LEU N N 118.668 0.064 1 24 45 10 SER H H 8.783 0.004 1 25 45 10 SER C C 174.912 0.000 1 26 45 10 SER CA C 58.310 0.049 1 27 45 10 SER CB C 64.467 0.019 1 28 45 10 SER N N 112.616 0.060 1 29 46 11 ARG H H 7.608 0.003 1 30 46 11 ARG C C 174.775 0.000 1 31 46 11 ARG CA C 57.196 0.064 1 32 46 11 ARG CB C 26.615 0.035 1 33 46 11 ARG N N 109.560 0.046 1 34 47 12 GLY H H 7.511 0.003 1 35 47 12 GLY C C 175.372 0.021 1 36 47 12 GLY CA C 44.588 0.056 1 37 47 12 GLY N N 102.730 0.049 1 38 48 13 TRP H H 7.825 0.003 1 39 48 13 TRP C C 176.507 0.000 1 40 48 13 TRP CA C 59.620 0.027 1 41 48 13 TRP CB C 28.558 0.035 1 42 48 13 TRP N N 121.740 0.054 1 43 49 14 GLY H H 7.528 0.006 1 44 49 14 GLY C C 176.293 0.000 1 45 49 14 GLY CA C 48.517 0.036 1 46 49 14 GLY N N 101.240 0.044 1 47 50 15 ASP H H 9.473 0.005 1 48 50 15 ASP C C 177.113 0.000 1 49 50 15 ASP CA C 57.501 0.037 1 50 50 15 ASP CB C 39.458 0.028 1 51 50 15 ASP N N 130.670 0.053 1 52 51 16 GLN H H 8.765 0.002 1 53 51 16 GLN HE21 H 7.409 0.003 1 54 51 16 GLN HE22 H 7.123 0.005 1 55 51 16 GLN C C 175.548 0.032 1 56 51 16 GLN CA C 55.057 0.013 1 57 51 16 GLN CB C 26.916 0.032 1 58 51 16 GLN CG C 33.162 0.000 1 59 51 16 GLN CD C 180.949 0.026 1 60 51 16 GLN N N 116.513 0.037 1 61 51 16 GLN NE2 N 112.880 0.004 1 62 52 17 LEU H H 7.292 0.009 1 63 52 17 LEU HD1 H 0.732 0.012 1 64 52 17 LEU HD2 H 0.789 0.015 1 65 52 17 LEU C C 175.291 0.025 1 66 52 17 LEU CA C 52.872 0.038 1 67 52 17 LEU CB C 41.335 0.028 1 68 52 17 LEU CG C 25.894 0.024 1 69 52 17 LEU CD1 C 22.347 0.043 1 70 52 17 LEU CD2 C 25.775 0.169 1 71 52 17 LEU N N 120.429 0.067 1 72 53 18 ILE H H 8.273 0.010 1 73 53 18 ILE HD1 H 0.704 0.004 1 74 53 18 ILE C C 176.343 0.000 1 75 53 18 ILE CA C 59.297 0.047 1 76 53 18 ILE CB C 35.455 0.036 1 77 53 18 ILE CG1 C 25.933 0.000 1 78 53 18 ILE CG2 C 16.490 0.000 1 79 53 18 ILE CD1 C 11.295 0.036 1 80 53 18 ILE N N 118.709 0.056 1 81 54 19 TRP H H 9.483 0.004 1 82 54 19 TRP C C 176.626 0.004 1 83 54 19 TRP CA C 56.104 0.017 1 84 54 19 TRP CB C 30.536 0.022 1 85 54 19 TRP N N 130.785 0.053 1 86 55 20 THR H H 8.818 0.004 1 87 55 20 THR C C 173.318 0.039 1 88 55 20 THR CA C 61.975 0.013 1 89 55 20 THR CB C 69.738 0.000 1 90 55 20 THR N N 117.137 0.043 1 91 56 21 GLN H H 9.286 0.003 1 92 56 21 GLN C C 175.566 0.025 1 93 56 21 GLN CA C 59.182 0.028 1 94 56 21 GLN CB C 28.699 0.027 1 95 56 21 GLN N N 124.248 0.048 1 96 57 22 THR H H 7.191 0.004 1 97 57 22 THR C C 174.797 0.026 1 98 57 22 THR CA C 57.913 0.028 1 99 57 22 THR CB C 72.144 0.016 1 100 57 22 THR N N 102.859 0.048 1 101 58 23 TYR H H 9.563 0.005 1 102 58 23 TYR C C 176.917 0.017 1 103 58 23 TYR CA C 58.838 0.023 1 104 58 23 TYR CB C 37.955 0.023 1 105 58 23 TYR N N 123.004 0.047 1 106 59 24 GLU H H 9.964 0.003 1 107 59 24 GLU C C 179.450 0.000 1 108 59 24 GLU CA C 59.779 0.036 1 109 59 24 GLU CB C 26.475 0.042 1 110 59 24 GLU N N 116.310 0.058 1 111 60 25 GLU H H 7.176 0.005 1 112 60 25 GLU C C 177.636 0.000 1 113 60 25 GLU CA C 57.738 0.041 1 114 60 25 GLU CB C 28.894 0.011 1 115 60 25 GLU N N 121.906 0.062 1 116 61 26 ALA H H 8.211 0.004 1 117 61 26 ALA C C 179.565 0.001 1 118 61 26 ALA CA C 54.974 0.028 1 119 61 26 ALA CB C 18.007 0.042 1 120 61 26 ALA N N 122.967 0.047 1 121 62 27 LEU H H 8.423 0.005 1 122 62 27 LEU HD1 H 0.184 0.006 1 123 62 27 LEU HD2 H 0.561 0.008 1 124 62 27 LEU C C 178.879 0.014 1 125 62 27 LEU CA C 57.046 0.038 1 126 62 27 LEU CB C 40.927 0.018 1 127 62 27 LEU CD1 C 24.929 0.014 1 128 62 27 LEU CD2 C 22.208 0.081 1 129 62 27 LEU N N 117.697 0.046 1 130 63 28 TYR H H 6.951 0.004 1 131 63 28 TYR C C 179.740 0.007 1 132 63 28 TYR CA C 61.096 0.016 1 133 63 28 TYR CB C 37.014 0.045 1 134 63 28 TYR N N 118.808 0.055 1 135 64 29 LYS H H 8.789 0.003 1 136 64 29 LYS C C 179.820 0.000 1 137 64 29 LYS CA C 58.815 0.030 1 138 64 29 LYS CB C 31.538 0.012 1 139 64 29 LYS N N 120.900 0.051 1 140 65 30 SER H H 8.547 0.003 1 141 65 30 SER C C 176.913 0.000 1 142 65 30 SER CA C 61.094 0.025 1 143 65 30 SER CB C 63.219 0.020 1 144 65 30 SER N N 118.160 0.054 1 145 66 31 LYS H H 8.027 0.005 1 146 66 31 LYS C C 180.181 0.001 1 147 66 31 LYS CA C 58.686 0.027 1 148 66 31 LYS CB C 31.286 0.028 1 149 66 31 LYS N N 117.215 0.047 1 150 67 32 THR H H 7.855 0.003 1 151 67 32 THR C C 176.580 0.024 1 152 67 32 THR CA C 64.458 0.026 1 153 67 32 THR CB C 68.750 0.024 1 154 67 32 THR N N 109.818 0.067 1 155 68 33 SER H H 7.970 0.005 1 156 68 33 SER C C 174.922 0.037 1 157 68 33 SER CA C 58.781 0.018 1 158 68 33 SER CB C 64.416 0.010 1 159 68 33 SER N N 115.227 0.056 1 160 69 34 ASN H H 8.047 0.003 1 161 69 34 ASN HD21 H 7.372 0.003 1 162 69 34 ASN HD22 H 6.424 0.006 1 163 69 34 ASN C C 173.476 0.044 1 164 69 34 ASN CA C 53.879 0.037 1 165 69 34 ASN CB C 37.874 0.038 1 166 69 34 ASN CG C 177.979 0.016 1 167 69 34 ASN N N 121.291 0.057 1 168 69 34 ASN ND2 N 110.282 0.000 1 169 70 35 LYS H H 7.593 0.004 1 170 70 35 LYS C C 173.628 0.000 1 171 70 35 LYS CA C 52.978 0.023 1 172 70 35 LYS CB C 32.954 0.000 1 173 70 35 LYS N N 117.181 0.052 1 174 71 36 PRO C C 172.506 0.000 1 175 71 36 PRO CA C 61.842 0.000 1 176 71 36 PRO CB C 31.036 0.000 1 177 72 37 LEU H H 8.907 0.004 1 178 72 37 LEU HD1 H 0.681 0.004 1 179 72 37 LEU HD2 H 0.687 0.005 1 180 72 37 LEU C C 174.764 0.000 1 181 72 37 LEU CA C 52.206 0.000 1 182 72 37 LEU CB C 43.927 0.000 1 183 72 37 LEU CD1 C 24.653 0.029 1 184 72 37 LEU CD2 C 26.694 0.028 1 185 72 37 LEU N N 122.686 0.047 1 186 73 38 MET H H 8.953 0.003 1 187 73 38 MET C C 172.821 0.000 1 188 73 38 MET CA C 54.285 0.000 1 189 73 38 MET CB C 34.353 0.007 1 190 73 38 MET N N 128.570 0.054 1 191 74 39 ILE H H 8.723 0.004 1 192 74 39 ILE HD1 H 0.736 0.005 1 193 74 39 ILE C C 175.426 0.000 1 194 74 39 ILE CA C 59.032 0.000 1 195 74 39 ILE CB C 39.420 0.000 1 196 74 39 ILE CG1 C 26.480 0.000 1 197 74 39 ILE CD1 C 16.341 0.039 1 198 74 39 ILE N N 123.777 0.038 1 199 75 40 ILE H H 8.579 0.006 1 200 75 40 ILE HD1 H -0.072 0.009 1 201 75 40 ILE C C 175.404 0.000 1 202 75 40 ILE CA C 59.953 0.052 1 203 75 40 ILE CB C 38.907 0.013 1 204 75 40 ILE CG1 C 25.999 0.063 1 205 75 40 ILE CD1 C 14.065 0.058 1 206 75 40 ILE N N 126.599 0.051 1 207 76 41 HIS H H 9.162 0.004 1 208 76 41 HIS C C 174.829 0.022 1 209 76 41 HIS CA C 55.881 0.043 1 210 76 41 HIS CB C 28.547 0.025 1 211 76 41 HIS N N 128.289 0.055 1 212 77 42 HIS H H 8.874 0.003 1 213 77 42 HIS C C 171.293 0.022 1 214 77 42 HIS CA C 54.323 0.078 1 215 77 42 HIS CB C 33.828 0.010 1 216 77 42 HIS N N 120.585 0.056 1 217 78 43 LEU H H 7.179 0.010 1 218 78 43 LEU HD1 H 0.822 0.005 1 219 78 43 LEU HD2 H 0.988 0.005 1 220 78 43 LEU C C 178.219 0.015 1 221 78 43 LEU CA C 53.682 0.070 1 222 78 43 LEU CB C 45.615 0.070 1 223 78 43 LEU CG C 26.508 0.000 1 224 78 43 LEU CD1 C 25.393 0.046 1 225 78 43 LEU CD2 C 23.641 0.041 1 226 78 43 LEU N N 114.371 0.056 1 227 79 44 ASP H H 8.724 0.008 1 228 79 44 ASP C C 178.234 0.000 1 229 79 44 ASP CA C 57.048 0.059 1 230 79 44 ASP CB C 40.117 0.006 1 231 79 44 ASP N N 123.175 0.052 1 232 80 45 GLU H H 9.132 0.004 1 233 80 45 GLU C C 175.390 0.024 1 234 80 45 GLU CA C 56.149 0.010 1 235 80 45 GLU CB C 27.750 0.024 1 236 80 45 GLU N N 115.392 0.049 1 237 81 46 CYS H H 7.138 0.003 1 238 81 46 CYS C C 175.696 0.000 1 239 81 46 CYS CA C 55.858 0.000 1 240 81 46 CYS CB C 29.724 0.000 1 241 81 46 CYS N N 125.617 0.057 1 242 82 47 PRO C C 180.699 0.013 1 243 82 47 PRO CA C 64.034 0.001 1 244 83 48 HIS H H 8.800 0.009 1 245 83 48 HIS C C 179.864 0.009 1 246 83 48 HIS CA C 58.718 0.066 1 247 83 48 HIS CB C 28.738 0.000 1 248 83 48 HIS N N 125.288 0.110 1 249 84 49 SER H H 11.465 0.005 1 250 84 49 SER C C 175.786 0.000 1 251 84 49 SER CA C 63.396 0.048 1 252 84 49 SER CB C 64.599 0.060 1 253 84 49 SER N N 129.791 0.075 1 254 85 50 GLN H H 8.163 0.004 1 255 85 50 GLN HE21 H 7.001 0.004 1 256 85 50 GLN HE22 H 6.686 0.003 1 257 85 50 GLN C C 178.630 0.025 1 258 85 50 GLN CA C 57.662 0.051 1 259 85 50 GLN CB C 26.440 0.028 1 260 85 50 GLN CG C 33.327 0.001 1 261 85 50 GLN CD C 180.670 0.016 1 262 85 50 GLN N N 117.882 0.053 1 263 85 50 GLN NE2 N 111.695 0.002 1 264 86 51 ALA H H 7.795 0.005 1 265 86 51 ALA C C 180.910 0.024 1 266 86 51 ALA CA C 54.254 0.057 1 267 86 51 ALA CB C 17.555 0.000 1 268 86 51 ALA N N 121.776 0.056 1 269 87 52 LEU H H 7.916 0.009 1 270 87 52 LEU HD1 H 0.771 0.003 1 271 87 52 LEU HD2 H 1.104 0.007 1 272 87 52 LEU C C 176.496 0.034 1 273 87 52 LEU CA C 56.577 0.065 1 274 87 52 LEU CB C 40.946 0.060 1 275 87 52 LEU CD1 C 21.766 0.040 1 276 87 52 LEU CD2 C 25.929 0.011 1 277 87 52 LEU N N 118.785 0.083 1 278 88 53 LYS H H 7.909 0.003 1 279 88 53 LYS C C 177.116 0.010 1 280 88 53 LYS CA C 58.522 0.017 1 281 88 53 LYS CB C 30.562 0.010 1 282 88 53 LYS N N 120.545 0.070 1 283 89 54 LYS H H 6.932 0.006 1 284 89 54 LYS C C 179.007 0.002 1 285 89 54 LYS CA C 58.812 0.056 1 286 89 54 LYS CB C 31.635 0.024 1 287 89 54 LYS N N 114.600 0.050 1 288 90 55 VAL H H 6.766 0.007 1 289 90 55 VAL HG1 H 1.072 0.008 1 290 90 55 VAL HG2 H 1.217 0.005 1 291 90 55 VAL C C 178.423 0.021 1 292 90 55 VAL CA C 63.912 0.037 1 293 90 55 VAL CB C 30.586 0.046 1 294 90 55 VAL CG1 C 21.993 0.045 1 295 90 55 VAL CG2 C 21.131 0.046 1 296 90 55 VAL N N 110.508 0.046 1 297 91 56 PHE H H 8.693 0.006 1 298 91 56 PHE C C 177.911 0.002 1 299 91 56 PHE CA C 61.331 0.022 1 300 91 56 PHE CB C 41.010 0.065 1 301 91 56 PHE N N 123.851 0.052 1 302 92 57 ALA H H 8.706 0.004 1 303 92 57 ALA C C 180.148 0.004 1 304 92 57 ALA CA C 53.768 0.034 1 305 92 57 ALA CB C 17.661 0.044 1 306 92 57 ALA N N 118.354 0.055 1 307 93 58 GLU H H 7.114 0.003 1 308 93 58 GLU C C 175.951 0.011 1 309 93 58 GLU CA C 55.445 0.050 1 310 93 58 GLU CB C 29.629 0.017 1 311 93 58 GLU N N 112.053 0.046 1 312 94 59 ASN H H 7.249 0.004 1 313 94 59 ASN HD21 H 7.561 0.006 1 314 94 59 ASN HD22 H 7.041 0.007 1 315 94 59 ASN C C 174.422 0.026 1 316 94 59 ASN CA C 53.611 0.020 1 317 94 59 ASN CB C 38.023 0.007 1 318 94 59 ASN N N 120.186 0.056 1 319 94 59 ASN ND2 N 112.601 0.006 1 320 95 60 LYS H H 8.649 0.002 1 321 95 60 LYS C C 179.401 0.017 1 322 95 60 LYS CA C 58.814 0.009 1 323 95 60 LYS CB C 31.138 0.013 1 324 95 60 LYS N N 127.094 0.052 1 325 96 61 GLU H H 7.960 0.003 1 326 96 61 GLU C C 179.955 0.029 1 327 96 61 GLU CA C 59.426 0.017 1 328 96 61 GLU CB C 28.366 0.014 1 329 96 61 GLU N N 119.095 0.041 1 330 97 62 ILE H H 8.465 0.005 1 331 97 62 ILE HD1 H 0.662 0.006 1 332 97 62 ILE C C 177.489 0.022 1 333 97 62 ILE CA C 65.266 0.029 1 334 97 62 ILE CB C 36.729 0.005 1 335 97 62 ILE CG1 C 29.455 0.000 1 336 97 62 ILE CG2 C 14.913 0.000 1 337 97 62 ILE CD1 C 13.014 0.078 1 338 97 62 ILE N N 122.469 0.045 1 339 98 63 GLN H H 8.023 0.004 1 340 98 63 GLN C C 178.476 0.011 1 341 98 63 GLN CA C 58.038 0.033 1 342 98 63 GLN CB C 27.988 0.017 1 343 98 63 GLN N N 115.266 0.042 1 344 99 64 LYS H H 7.548 0.002 1 345 99 64 LYS C C 180.132 0.018 1 346 99 64 LYS CA C 57.345 0.032 1 347 99 64 LYS CB C 31.020 0.014 1 348 99 64 LYS N N 116.152 0.051 1 349 100 65 LEU H H 7.907 0.004 1 350 100 65 LEU HD1 H 0.887 0.005 1 351 100 65 LEU HD2 H 0.886 0.004 1 352 100 65 LEU C C 178.767 0.000 1 353 100 65 LEU CA C 56.583 0.036 1 354 100 65 LEU CB C 40.767 0.000 1 355 100 65 LEU CD1 C 23.701 0.112 1 356 100 65 LEU CD2 C 27.862 0.014 1 357 100 65 LEU N N 122.371 0.059 1 358 101 66 ALA H H 8.470 0.008 1 359 101 66 ALA C C 177.824 0.000 1 360 101 66 ALA CA C 54.203 0.038 1 361 101 66 ALA CB C 16.828 0.000 1 362 101 66 ALA N N 119.317 0.137 1 363 102 67 GLU H H 7.014 0.006 1 364 102 67 GLU C C 178.662 0.020 1 365 102 67 GLU CA C 57.826 0.023 1 366 102 67 GLU CB C 29.052 0.018 1 367 102 67 GLU N N 112.370 0.058 1 368 103 68 GLN H H 8.162 0.004 1 369 103 68 GLN HE21 H 7.620 0.007 1 370 103 68 GLN HE22 H 6.700 0.009 1 371 103 68 GLN C C 173.459 0.052 1 372 103 68 GLN CA C 55.610 0.046 1 373 103 68 GLN CB C 27.844 0.058 1 374 103 68 GLN CG C 33.676 0.000 1 375 103 68 GLN CD C 180.109 0.016 1 376 103 68 GLN N N 116.027 0.048 1 377 103 68 GLN NE2 N 112.487 0.002 1 378 104 69 PHE H H 7.647 0.004 1 379 104 69 PHE C C 177.709 0.000 1 380 104 69 PHE CA C 56.810 0.027 1 381 104 69 PHE CB C 39.974 0.000 1 382 104 69 PHE N N 116.764 0.054 1 383 105 70 VAL H H 8.932 0.007 1 384 105 70 VAL HG1 H 0.981 0.004 1 385 105 70 VAL HG2 H 0.672 0.008 1 386 105 70 VAL C C 174.511 0.010 1 387 105 70 VAL CA C 62.808 0.032 1 388 105 70 VAL CB C 30.646 0.026 1 389 105 70 VAL CG1 C 22.239 0.032 1 390 105 70 VAL CG2 C 21.120 0.047 1 391 105 70 VAL N N 120.752 0.000 1 392 106 71 LEU H H 8.450 0.007 1 393 106 71 LEU HD1 H 0.478 0.004 1 394 106 71 LEU HD2 H -0.090 0.005 1 395 106 71 LEU C C 175.393 0.000 1 396 106 71 LEU CA C 53.338 0.005 1 397 106 71 LEU CB C 43.767 0.000 1 398 106 71 LEU CD1 C 23.863 0.037 1 399 106 71 LEU CD2 C 27.060 0.013 1 400 106 71 LEU N N 128.637 0.049 1 401 107 72 LEU H H 8.313 0.004 1 402 107 72 LEU HD1 H 0.703 0.008 1 403 107 72 LEU C C 174.424 0.000 1 404 107 72 LEU CA C 53.213 0.059 1 405 107 72 LEU CB C 46.228 0.005 1 406 107 72 LEU CD1 C 26.505 0.043 1 407 107 72 LEU N N 123.849 0.009 1 408 108 73 ASN H H 9.844 0.002 1 409 108 73 ASN C C 172.081 0.062 1 410 108 73 ASN CA C 51.790 0.059 1 411 108 73 ASN CB C 41.416 0.034 1 412 108 73 ASN N N 124.978 0.062 1 413 109 74 LEU H H 8.511 0.004 1 414 109 74 LEU HD1 H 0.449 0.006 1 415 109 74 LEU HD2 H 0.881 0.005 1 416 109 74 LEU C C 175.859 0.004 1 417 109 74 LEU CA C 52.919 0.071 1 418 109 74 LEU CB C 46.467 0.002 1 419 109 74 LEU CD1 C 26.880 0.018 1 420 109 74 LEU CD2 C 24.018 0.071 1 421 109 74 LEU N N 121.862 0.101 1 422 110 75 VAL H H 8.681 0.007 1 423 110 75 VAL HG1 H 0.075 0.004 1 424 110 75 VAL HG2 H 0.769 0.003 1 425 110 75 VAL C C 175.323 0.048 1 426 110 75 VAL CA C 58.659 0.021 1 427 110 75 VAL CB C 30.253 0.028 1 428 110 75 VAL CG1 C 19.830 0.048 1 429 110 75 VAL CG2 C 18.390 0.046 1 430 110 75 VAL N N 111.424 0.063 1 431 111 76 TYR H H 7.200 0.003 1 432 111 76 TYR C C 174.858 0.024 1 433 111 76 TYR CA C 57.160 0.024 1 434 111 76 TYR CB C 41.452 0.019 1 435 111 76 TYR N N 124.309 0.052 1 436 112 77 GLU H H 7.321 0.003 1 437 112 77 GLU C C 178.110 0.000 1 438 112 77 GLU CA C 57.273 0.009 1 439 112 77 GLU CB C 28.812 0.000 1 440 112 77 GLU N N 125.982 0.059 1 441 113 78 THR H H 8.256 0.002 1 442 113 78 THR C C 175.758 0.000 1 443 113 78 THR CA C 61.621 0.000 1 444 113 78 THR CB C 70.448 0.000 1 445 113 78 THR N N 117.894 0.004 1 446 114 79 THR H H 8.435 0.002 1 447 114 79 THR C C 174.674 0.000 1 448 114 79 THR CA C 60.840 0.057 1 449 114 79 THR CB C 68.228 0.057 1 450 114 79 THR N N 107.131 0.069 1 451 115 80 ASP H H 7.846 0.003 1 452 115 80 ASP C C 178.268 0.016 1 453 115 80 ASP CA C 52.811 0.047 1 454 115 80 ASP CB C 40.720 0.024 1 455 115 80 ASP N N 121.256 0.049 1 456 116 81 LYS H H 8.800 0.009 1 457 116 81 LYS C C 179.359 0.016 1 458 116 81 LYS CA C 57.462 0.049 1 459 116 81 LYS CB C 30.250 0.000 1 460 116 81 LYS N N 128.564 0.057 1 461 117 82 HIS H H 8.702 0.007 1 462 117 82 HIS C C 176.206 0.029 1 463 117 82 HIS CA C 57.529 0.053 1 464 117 82 HIS CB C 27.280 0.004 1 465 117 82 HIS N N 117.867 0.178 1 466 118 83 LEU H H 7.306 0.005 1 467 118 83 LEU HD1 H 0.510 0.010 1 468 118 83 LEU HD2 H 0.550 0.009 1 469 118 83 LEU C C 176.369 0.008 1 470 118 83 LEU CA C 53.560 0.022 1 471 118 83 LEU CB C 40.759 0.025 1 472 118 83 LEU CG C 26.166 0.000 1 473 118 83 LEU CD1 C 26.138 0.017 1 474 118 83 LEU CD2 C 23.708 0.025 1 475 118 83 LEU N N 113.534 0.056 1 476 119 84 SER H H 7.252 0.005 1 477 119 84 SER C C 174.190 0.000 1 478 119 84 SER CA C 55.128 0.031 1 479 119 84 SER CB C 61.634 0.000 1 480 119 84 SER N N 111.737 0.057 1 481 120 85 PRO C C 178.288 0.000 1 482 120 85 PRO CA C 64.797 0.025 1 483 120 85 PRO CB C 31.183 0.057 1 484 121 86 ASP H H 8.883 0.003 1 485 121 86 ASP C C 175.037 0.031 1 486 121 86 ASP CA C 51.638 0.073 1 487 121 86 ASP CB C 39.655 0.011 1 488 121 86 ASP N N 117.572 0.044 1 489 122 87 GLY H H 6.948 0.003 1 490 122 87 GLY C C 173.695 0.026 1 491 122 87 GLY CA C 43.375 0.028 1 492 122 87 GLY N N 106.669 0.056 1 493 123 88 GLN H H 8.203 0.002 1 494 123 88 GLN C C 174.512 0.025 1 495 123 88 GLN CA C 54.168 0.071 1 496 123 88 GLN CB C 26.442 0.030 1 497 123 88 GLN N N 118.297 0.045 1 498 124 89 TYR H H 5.919 0.004 1 499 124 89 TYR C C 173.676 0.021 1 500 124 89 TYR CA C 54.260 0.063 1 501 124 89 TYR CB C 38.154 0.007 1 502 124 89 TYR N N 117.012 0.056 1 503 125 90 VAL H H 8.276 0.005 1 504 125 90 VAL HG1 H 0.567 0.005 1 505 125 90 VAL HG2 H 0.935 0.004 1 506 125 90 VAL C C 173.584 0.000 1 507 125 90 VAL CA C 57.497 0.066 1 508 125 90 VAL CB C 34.383 0.000 1 509 125 90 VAL CG1 C 22.301 0.105 1 510 125 90 VAL CG2 C 18.082 0.047 1 511 125 90 VAL N N 109.046 0.056 1 512 126 91 PRO C C 176.439 0.000 1 513 126 91 PRO CA C 61.711 0.018 1 514 126 91 PRO CB C 33.249 0.000 1 515 127 92 ARG H H 8.685 0.006 1 516 127 92 ARG C C 175.561 0.000 1 517 127 92 ARG CA C 55.356 0.000 1 518 127 92 ARG CB C 31.219 0.000 1 519 127 92 ARG N N 121.468 0.063 1 520 128 93 ILE H H 9.060 0.004 1 521 128 93 ILE HD1 H 0.764 0.004 1 522 128 93 ILE C C 173.726 0.000 1 523 128 93 ILE CA C 60.669 0.000 1 524 128 93 ILE CB C 37.976 0.000 1 525 128 93 ILE CG1 C 26.042 0.000 1 526 128 93 ILE CG2 C 16.559 0.000 1 527 128 93 ILE CD1 C 12.833 0.075 1 528 128 93 ILE N N 127.776 0.000 1 529 129 94 MET H H 8.513 0.004 1 530 129 94 MET C C 174.465 0.000 1 531 129 94 MET CA C 50.838 0.036 1 532 129 94 MET CB C 33.661 0.000 1 533 129 94 MET N N 122.209 0.039 1 534 130 95 PHE H H 8.538 0.003 1 535 130 95 PHE C C 175.112 0.000 1 536 130 95 PHE CA C 55.976 0.023 1 537 130 95 PHE CB C 41.078 0.035 1 538 130 95 PHE N N 117.585 0.057 1 539 131 96 VAL H H 9.863 0.003 1 540 131 96 VAL HG1 H 0.807 0.007 1 541 131 96 VAL HG2 H 0.838 0.006 1 542 131 96 VAL C C 174.612 0.006 1 543 131 96 VAL CA C 60.865 0.049 1 544 131 96 VAL CB C 34.108 0.009 1 545 131 96 VAL CG1 C 20.057 0.033 1 546 131 96 VAL CG2 C 21.931 0.071 1 547 131 96 VAL N N 122.666 0.044 1 548 132 97 ASP H H 8.397 0.004 1 549 132 97 ASP C C 175.227 0.000 1 550 132 97 ASP CA C 52.633 0.032 1 551 132 97 ASP CB C 44.823 0.000 1 552 132 97 ASP N N 127.691 0.048 1 553 133 98 PRO C C 176.032 0.000 1 554 133 98 PRO CA C 64.753 0.052 1 555 133 98 PRO CB C 31.155 0.039 1 556 134 99 SER H H 8.161 0.002 1 557 134 99 SER C C 175.632 0.000 1 558 134 99 SER CA C 59.832 0.016 1 559 134 99 SER CB C 63.762 0.010 1 560 134 99 SER N N 110.967 0.045 1 561 135 100 LEU H H 9.193 0.006 1 562 135 100 LEU HD1 H 0.798 0.004 1 563 135 100 LEU HD2 H 0.820 0.006 1 564 135 100 LEU C C 176.198 0.012 1 565 135 100 LEU CA C 56.074 0.028 1 566 135 100 LEU CB C 35.932 0.008 1 567 135 100 LEU CD1 C 22.519 0.046 1 568 135 100 LEU CD2 C 25.557 0.141 1 569 135 100 LEU N N 118.152 0.048 1 570 136 101 THR H H 6.989 0.007 1 571 136 101 THR C C 174.057 0.034 1 572 136 101 THR CA C 61.580 0.030 1 573 136 101 THR CB C 69.849 0.039 1 574 136 101 THR N N 115.651 0.060 1 575 137 102 VAL H H 8.994 0.005 1 576 137 102 VAL HG1 H 0.763 0.004 1 577 137 102 VAL HG2 H 0.881 0.006 1 578 137 102 VAL C C 177.458 0.023 1 579 137 102 VAL CA C 63.625 0.055 1 580 137 102 VAL CB C 30.951 0.033 1 581 137 102 VAL CG1 C 20.031 0.012 1 582 137 102 VAL CG2 C 22.379 0.043 1 583 137 102 VAL N N 128.649 0.056 1 584 138 103 ARG H H 9.367 0.007 1 585 138 103 ARG C C 177.685 0.000 1 586 138 103 ARG CA C 50.447 0.054 1 587 138 103 ARG CB C 24.188 0.005 1 588 138 103 ARG N N 128.197 0.042 1 589 139 104 ALA H H 8.318 0.004 1 590 139 104 ALA C C 177.749 0.000 1 591 139 104 ALA CA C 53.022 0.067 1 592 139 104 ALA CB C 17.265 0.018 1 593 139 104 ALA N N 130.271 0.056 1 594 140 105 ASP H H 9.629 0.003 1 595 140 105 ASP C C 175.448 0.035 1 596 140 105 ASP CA C 53.735 0.033 1 597 140 105 ASP CB C 38.561 0.018 1 598 140 105 ASP N N 113.430 0.057 1 599 141 106 ILE H H 7.527 0.003 1 600 141 106 ILE HD1 H 0.454 0.005 1 601 141 106 ILE C C 175.076 0.020 1 602 141 106 ILE CA C 62.021 0.017 1 603 141 106 ILE CB C 35.194 0.012 1 604 141 106 ILE CG1 C 26.153 0.000 1 605 141 106 ILE CG2 C 18.361 0.000 1 606 141 106 ILE CD1 C 12.453 0.059 1 607 141 106 ILE N N 122.759 0.059 1 608 142 107 THR H H 7.794 0.010 1 609 142 107 THR C C 176.229 0.027 1 610 142 107 THR CA C 58.802 0.027 1 611 142 107 THR CB C 71.240 0.033 1 612 142 107 THR N N 117.199 0.064 1 613 143 108 GLY H H 8.879 0.004 1 614 143 108 GLY C C 174.709 0.035 1 615 143 108 GLY CA C 43.792 0.022 1 616 143 108 GLY N N 109.586 0.047 1 617 144 109 ARG H H 8.132 0.006 1 618 144 109 ARG C C 176.906 0.018 1 619 144 109 ARG CA C 55.626 0.061 1 620 144 109 ARG CB C 29.907 0.028 1 621 144 109 ARG N N 116.047 0.055 1 622 145 110 TYR H H 8.827 0.003 1 623 145 110 TYR C C 177.027 0.000 1 624 145 110 TYR CA C 56.834 0.073 1 625 145 110 TYR CB C 36.495 0.025 1 626 145 110 TYR N N 122.752 0.060 1 627 146 111 SER H H 8.598 0.005 1 628 146 111 SER C C 175.287 0.000 1 629 146 111 SER CA C 60.280 0.040 1 630 146 111 SER CB C 62.075 0.005 1 631 146 111 SER N N 119.780 0.057 1 632 147 112 ASN H H 8.356 0.002 1 633 147 112 ASN HD21 H 7.502 0.002 1 634 147 112 ASN HD22 H 6.708 0.004 1 635 147 112 ASN C C 173.978 0.034 1 636 147 112 ASN CA C 52.888 0.062 1 637 147 112 ASN CB C 36.874 0.018 1 638 147 112 ASN CG C 178.076 0.019 1 639 147 112 ASN N N 115.945 0.045 1 640 147 112 ASN ND2 N 113.017 0.141 1 641 148 113 ARG H H 6.738 0.005 1 642 148 113 ARG C C 176.648 0.014 1 643 148 113 ARG CA C 54.805 0.010 1 644 148 113 ARG CB C 29.903 0.008 1 645 148 113 ARG N N 121.457 0.049 1 646 149 114 LEU H H 9.922 0.009 1 647 149 114 LEU HD1 H 0.668 0.008 1 648 149 114 LEU HD2 H 0.708 0.007 1 649 149 114 LEU C C 176.112 0.022 1 650 149 114 LEU CA C 57.150 0.040 1 651 149 114 LEU CB C 42.097 0.027 1 652 149 114 LEU CD1 C 22.980 0.024 1 653 149 114 LEU CD2 C 25.534 0.078 1 654 149 114 LEU N N 125.677 0.054 1 655 150 115 TYR H H 8.258 0.003 1 656 150 115 TYR C C 174.825 0.022 1 657 150 115 TYR CA C 55.560 0.075 1 658 150 115 TYR CB C 37.965 0.009 1 659 150 115 TYR N N 115.012 0.049 1 660 151 116 ALA H H 7.482 0.004 1 661 151 116 ALA C C 177.864 0.019 1 662 151 116 ALA CA C 51.129 0.043 1 663 151 116 ALA CB C 20.351 0.012 1 664 151 116 ALA N N 121.080 0.052 1 665 152 117 TYR H H 6.857 0.008 1 666 152 117 TYR C C 174.050 0.034 1 667 152 117 TYR CA C 57.671 0.020 1 668 152 117 TYR CB C 41.937 0.010 1 669 152 117 TYR N N 115.067 0.060 1 670 153 118 GLU H H 9.536 0.006 1 671 153 118 GLU C C 176.201 0.000 1 672 153 118 GLU CA C 53.729 0.024 1 673 153 118 GLU CB C 28.636 0.000 1 674 153 118 GLU N N 122.450 0.053 1 675 154 119 PRO C C 176.899 0.005 1 676 154 119 PRO CA C 65.756 0.037 1 677 154 119 PRO CB C 30.755 0.018 1 678 155 120 ALA H H 7.732 0.005 1 679 155 120 ALA C C 178.871 0.011 1 680 155 120 ALA CA C 52.672 0.052 1 681 155 120 ALA CB C 17.901 0.018 1 682 155 120 ALA N N 114.498 0.036 1 683 156 121 ASP H H 8.502 0.002 1 684 156 121 ASP C C 177.113 0.018 1 685 156 121 ASP CA C 54.375 0.057 1 686 156 121 ASP CB C 41.607 0.003 1 687 156 121 ASP N N 117.305 0.057 1 688 157 122 THR H H 7.417 0.004 1 689 157 122 THR C C 176.398 0.000 1 690 157 122 THR CA C 66.146 0.040 1 691 157 122 THR CB C 67.291 0.014 1 692 157 122 THR N N 111.209 0.043 1 693 158 123 ALA H H 8.625 0.003 1 694 158 123 ALA C C 180.369 0.018 1 695 158 123 ALA CA C 55.003 0.022 1 696 158 123 ALA CB C 16.650 0.027 1 697 158 123 ALA N N 123.521 0.057 1 698 159 124 LEU H H 7.431 0.007 1 699 159 124 LEU HD1 H 0.888 0.004 1 700 159 124 LEU HD2 H 0.948 0.011 1 701 159 124 LEU C C 178.678 0.032 1 702 159 124 LEU CA C 56.880 0.062 1 703 159 124 LEU CB C 40.857 0.000 1 704 159 124 LEU CD1 C 26.428 0.081 1 705 159 124 LEU CD2 C 23.563 0.022 1 706 159 124 LEU N N 121.062 0.050 1 707 160 125 LEU H H 8.436 0.008 1 708 160 125 LEU HD1 H 0.442 0.006 1 709 160 125 LEU HD2 H 0.686 0.012 1 710 160 125 LEU C C 178.508 0.016 1 711 160 125 LEU CA C 57.947 0.030 1 712 160 125 LEU CB C 39.786 0.058 1 713 160 125 LEU CD1 C 21.622 0.054 1 714 160 125 LEU CD2 C 25.453 0.166 1 715 160 125 LEU N N 119.561 0.077 1 716 161 126 LEU H H 8.101 0.004 1 717 161 126 LEU HD1 H 0.771 0.004 1 718 161 126 LEU HD2 H 0.769 0.004 1 719 161 126 LEU C C 179.246 0.008 1 720 161 126 LEU CA C 57.917 0.091 1 721 161 126 LEU CB C 41.010 0.050 1 722 161 126 LEU CD1 C 25.281 0.050 1 723 161 126 LEU CD2 C 24.660 0.059 1 724 161 126 LEU N N 119.747 0.044 1 725 162 127 ASP H H 7.865 0.002 1 726 162 127 ASP C C 179.621 0.046 1 727 162 127 ASP CA C 57.219 0.024 1 728 162 127 ASP CB C 39.870 0.016 1 729 162 127 ASP N N 118.731 0.041 1 730 163 128 ASN H H 8.714 0.006 1 731 163 128 ASN HD21 H 7.970 0.002 1 732 163 128 ASN HD22 H 6.956 0.011 1 733 163 128 ASN C C 177.513 0.000 1 734 163 128 ASN CA C 54.064 0.080 1 735 163 128 ASN CB C 36.187 0.027 1 736 163 128 ASN CG C 175.776 0.024 1 737 163 128 ASN N N 121.966 0.075 1 738 163 128 ASN ND2 N 111.452 0.000 1 739 164 129 MET H H 8.694 0.010 1 740 164 129 MET C C 178.663 0.000 1 741 164 129 MET CA C 59.059 0.015 1 742 164 129 MET CB C 33.742 0.000 1 743 164 129 MET N N 122.224 0.097 1 744 165 130 LYS H H 7.753 0.004 1 745 165 130 LYS C C 180.385 0.000 1 746 165 130 LYS CA C 60.025 0.031 1 747 165 130 LYS CB C 30.867 0.000 1 748 165 130 LYS N N 116.977 0.041 1 749 166 131 LYS H H 7.918 0.005 1 750 166 131 LYS C C 179.593 0.012 1 751 166 131 LYS CA C 59.679 0.000 1 752 166 131 LYS CB C 31.918 0.000 1 753 166 131 LYS N N 120.316 0.050 1 754 167 132 ALA H H 7.795 0.004 1 755 167 132 ALA C C 177.994 0.034 1 756 167 132 ALA CA C 53.695 0.020 1 757 167 132 ALA CB C 17.347 0.000 1 758 167 132 ALA N N 122.128 0.040 1 759 168 133 LEU H H 7.004 0.010 1 760 168 133 LEU HD1 H 0.251 0.003 1 761 168 133 LEU HD2 H 0.728 0.007 1 762 168 133 LEU C C 177.695 0.001 1 763 168 133 LEU CA C 55.413 0.075 1 764 168 133 LEU CB C 41.048 0.039 1 765 168 133 LEU CD1 C 22.930 0.034 1 766 168 133 LEU CD2 C 25.975 0.054 1 767 168 133 LEU N N 113.535 0.057 1 768 169 134 LYS H H 7.184 0.003 1 769 169 134 LYS C C 174.639 0.022 1 770 169 134 LYS CA C 54.990 0.035 1 771 169 134 LYS CB C 28.705 0.011 1 772 169 134 LYS N N 122.848 0.049 1 773 170 135 LEU H H 7.300 0.005 1 774 170 135 LEU HD1 H 0.668 0.005 1 775 170 135 LEU HD2 H 0.822 0.004 1 776 170 135 LEU C C 178.839 0.011 1 777 170 135 LEU CA C 54.406 0.080 1 778 170 135 LEU CB C 39.889 0.022 1 779 170 135 LEU CD1 C 21.118 0.047 1 780 170 135 LEU CD2 C 25.683 0.044 1 781 170 135 LEU N N 120.223 0.048 1 782 171 136 LEU H H 8.608 0.005 1 783 171 136 LEU HD1 H 0.726 0.009 1 784 171 136 LEU HD2 H 0.741 0.002 1 785 171 136 LEU C C 178.609 0.022 1 786 171 136 LEU CA C 55.289 0.078 1 787 171 136 LEU CB C 40.676 0.060 1 788 171 136 LEU CD1 C 25.167 0.027 1 789 171 136 LEU CD2 C 21.313 0.019 1 790 171 136 LEU N N 119.810 0.059 1 791 172 137 LYS H H 8.450 0.003 1 792 172 137 LYS C C 176.728 0.017 1 793 172 137 LYS CA C 55.451 0.053 1 794 172 137 LYS CB C 31.752 0.002 1 795 172 137 LYS N N 120.729 0.052 1 796 173 138 THR H H 8.086 0.003 1 797 173 138 THR C C 174.592 0.021 1 798 173 138 THR CA C 61.468 0.029 1 799 173 138 THR CB C 69.237 0.011 1 800 173 138 THR N N 116.281 0.048 1 801 174 139 GLU H H 8.277 0.006 1 802 174 139 GLU C C 175.505 0.022 1 803 174 139 GLU CA C 55.752 0.057 1 804 174 139 GLU CB C 29.506 0.006 1 805 174 139 GLU N N 123.493 0.056 1 806 175 140 LEU H H 7.848 0.002 1 807 175 140 LEU HD1 H 0.764 0.004 1 808 175 140 LEU HD2 H 0.811 0.002 1 809 175 140 LEU C C 182.820 0.000 1 810 175 140 LEU CA C 56.185 0.027 1 811 175 140 LEU CB C 42.227 0.048 1 812 175 140 LEU CD1 C 23.325 0.013 1 813 175 140 LEU CD2 C 25.006 0.045 1 814 175 140 LEU N N 128.735 0.047 1 stop_ save_