data_7128 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Fibronecting 1F3-2F3 backbone chemical shift assignments ; _BMRB_accession_number 7128 _BMRB_flat_file_name bmr7128.str _Entry_type original _Submission_date 2006-05-23 _Accession_date 2006-05-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'Backbone 1H, 15N and 13C chemical shift assignments of the first two type III domains of human fibronectin' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vakonakis Ioannis . . 2 Campbell Iain D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 175 "13C chemical shifts" 322 "15N chemical shifts" 175 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-05-29 original author . stop_ _Original_release_date 2007-05-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17464288 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vakonakis Ioannis . . 2 Staunton David . . 3 Rooney Luke . . 4 Campbell Iain D. . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 26 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2575 _Page_last 2583 _Year 2007 _Details . loop_ _Keyword 'Protein complex' 'Protein structure' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 1F3-2F3 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 1F3-2F3 $Fibronectin_1F3-2F3 stop_ _System_molecular_weight 22097 _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 1F3-2F3 stop_ loop_ _Biological_function 'Structural protein' stop_ _Database_query_date . _Details 'Single polypeptide comprising the first two type III domains of human Fibronectin and the intervening linker' save_ ######################## # Monomeric polymers # ######################## save_Fibronectin_1F3-2F3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 1F3-2F3 _Molecular_mass 22097 _Mol_thiol_state 'not present' loop_ _Biological_function 'Structural protein' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 201 _Mol_residue_sequence ; SGPVEVFITETPSQPNSHPI QWNAPQPSHISKYILRWRPK NSVGRWKEATIPGHLNSYTI KGLKPGVVYEGQLISIQQYG HQEVTRFDFTTTSTSTPVTS NTVTGETTPFSPLVATSESV TEITASSFVVSWVSASDTVS GFRVEYELSEEGDEPQYLDL PSTATSVNIPDLLPGRKYIV NVYQISEDGEQSLILSTSQT T ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 SER 2 2 GLY 3 3 PRO 4 4 VAL 5 5 GLU 6 6 VAL 7 7 PHE 8 8 ILE 9 9 THR 10 10 GLU 11 11 THR 12 12 PRO 13 13 SER 14 14 GLN 15 15 PRO 16 16 ASN 17 17 SER 18 18 HIS 19 19 PRO 20 20 ILE 21 21 GLN 22 22 TRP 23 23 ASN 24 24 ALA 25 25 PRO 26 26 GLN 27 27 PRO 28 28 SER 29 29 HIS 30 30 ILE 31 31 SER 32 32 LYS 33 33 TYR 34 34 ILE 35 35 LEU 36 36 ARG 37 37 TRP 38 38 ARG 39 39 PRO 40 40 LYS 41 41 ASN 42 42 SER 43 43 VAL 44 44 GLY 45 45 ARG 46 46 TRP 47 47 LYS 48 48 GLU 49 49 ALA 50 50 THR 51 51 ILE 52 52 PRO 53 53 GLY 54 54 HIS 55 55 LEU 56 56 ASN 57 57 SER 58 58 TYR 59 59 THR 60 60 ILE 61 61 LYS 62 62 GLY 63 63 LEU 64 64 LYS 65 65 PRO 66 66 GLY 67 67 VAL 68 68 VAL 69 69 TYR 70 70 GLU 71 71 GLY 72 72 GLN 73 73 LEU 74 74 ILE 75 75 SER 76 76 ILE 77 77 GLN 78 78 GLN 79 79 TYR 80 80 GLY 81 81 HIS 82 82 GLN 83 83 GLU 84 84 VAL 85 85 THR 86 86 ARG 87 87 PHE 88 88 ASP 89 89 PHE 90 90 THR 91 91 THR 92 92 THR 93 93 SER 94 94 THR 95 95 SER 96 96 THR 97 97 PRO 98 98 VAL 99 99 THR 100 100 SER 101 101 ASN 102 102 THR 103 103 VAL 104 104 THR 105 105 GLY 106 106 GLU 107 107 THR 108 108 THR 109 109 PRO 110 110 PHE 111 111 SER 112 112 PRO 113 113 LEU 114 114 VAL 115 115 ALA 116 116 THR 117 117 SER 118 118 GLU 119 119 SER 120 120 VAL 121 121 THR 122 122 GLU 123 123 ILE 124 124 THR 125 125 ALA 126 126 SER 127 127 SER 128 128 PHE 129 129 VAL 130 130 VAL 131 131 SER 132 132 TRP 133 133 VAL 134 134 SER 135 135 ALA 136 136 SER 137 137 ASP 138 138 THR 139 139 VAL 140 140 SER 141 141 GLY 142 142 PHE 143 143 ARG 144 144 VAL 145 145 GLU 146 146 TYR 147 147 GLU 148 148 LEU 149 149 SER 150 150 GLU 151 151 GLU 152 152 GLY 153 153 ASP 154 154 GLU 155 155 PRO 156 156 GLN 157 157 TYR 158 158 LEU 159 159 ASP 160 160 LEU 161 161 PRO 162 162 SER 163 163 THR 164 164 ALA 165 165 THR 166 166 SER 167 167 VAL 168 168 ASN 169 169 ILE 170 170 PRO 171 171 ASP 172 172 LEU 173 173 LEU 174 174 PRO 175 175 GLY 176 176 ARG 177 177 LYS 178 178 TYR 179 179 ILE 180 180 VAL 181 181 ASN 182 182 VAL 183 183 TYR 184 184 GLN 185 185 ILE 186 186 SER 187 187 GLU 188 188 ASP 189 189 GLY 190 190 GLU 191 191 GLN 192 192 SER 193 193 LEU 194 194 ILE 195 195 LEU 196 196 SER 197 197 THR 198 198 SER 199 199 GLN 200 200 THR 201 201 THR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 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 2HA1 "Complex Of The First And Second Type Iii Domains Of Human Fibronectin In Solution" 100.00 201 100.00 100.00 3.65e-140 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue $Fibronectin_1F3-2F3 Human 9606 Eukaryota Metazoa Homo sapiens 'Extracellular matrix' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name _Vendor_name $Fibronectin_1F3-2F3 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) RP+ plamid pGEX-6P-3 Amersham stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'U-15N 1F3-2F3, 150mM NaCl, 20mM NaPi, pH 7.0, 5% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Fibronectin_1F3-2F3 1.2 mM [U-15N] NaCl 150 mM . NaPi 20 mM . D2O 5 % . H2O 95 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'U-13C, 15N 1F3-2F3, 150mM NaCl, 20mM NaPi pH 7.0, 5% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Fibronectin_1F3-2F3 1 mM '[U-13C; U-15N]' NaCl 150 mM . NaPi 20 mM . D2O 5 % . H2O 95 % . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name 'Omega Spectrometer Operating Software' _Version 'Beta 6.0.3b2' loop_ _Vendor _Address _Electronic_address GE/Bruker . . stop_ loop_ _Task 'Data collection' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version '2.3 Rev 2005.319.11.22' loop_ _Vendor _Address _Electronic_address NIH/NIDDK . . stop_ loop_ _Task 'Data processing' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name PIPP _Version 4.3.7 loop_ _Vendor _Address _Electronic_address NIH ; Dan Garrett NIH/NIDDK/LCP Bldg5, Rm B1-27 5 Center Dr MSC 0510 Bethesda, MD, USA ; . stop_ loop_ _Task 'Data analysis' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'Data collection' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_750MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer 'home build' _Model . _Field_strength 750 _Details 'Home build consoles controlled by GE/Bruker Omega software & computers' save_ save_500MHz_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance II' _Field_strength 500 _Details 'Bruker Avance II spectrometer console with cryoprobe, Oxford 500 MHz Magnet' save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label $sample_1 save_ save_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_2 save_ save_CBCANH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label $sample_2 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_2 save_ save_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details '150mM NaCl, 20mM NaPi pH 7.0, 5% D2O, 30C' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 420 20 mM pH 7 0.1 pH pressure 1 0 atm temperature 303 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details 'Backbone chemical shift assignments' loop_ _Experiment_label 15N_HSQC CBCA(CO)NH CBCANH HNCA HN(CO)CA stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 1F3-2F3 _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 1 1 SER CA C 58.40 0.10 1 2 1 1 SER CB C 64.24 0.10 1 3 2 2 GLY H H 8.27 0.02 1 4 2 2 GLY CA C 44.71 0.10 1 5 2 2 GLY N N 110.86 0.10 1 6 3 3 PRO CA C 63.18 0.10 1 7 3 3 PRO CB C 32.61 0.10 1 8 4 4 VAL H H 8.09 0.02 1 9 4 4 VAL CA C 62.42 0.10 1 10 4 4 VAL CB C 32.61 0.10 1 11 4 4 VAL N N 120.04 0.10 1 12 5 5 GLU H H 8.20 0.02 1 13 5 5 GLU CA C 55.71 0.10 1 14 5 5 GLU N N 126.09 0.10 1 15 6 6 VAL H H 8.04 0.02 1 16 6 6 VAL CA C 61.15 0.10 1 17 6 6 VAL N N 122.01 0.10 1 18 7 7 PHE H H 8.89 0.02 1 19 7 7 PHE CA C 56.33 0.10 1 20 7 7 PHE N N 125.07 0.10 1 21 12 12 PRO CA C 64.80 0.10 1 22 13 13 SER H H 8.21 0.02 1 23 13 13 SER CA C 60.08 0.10 1 24 13 13 SER N N 113.38 0.10 1 25 16 16 ASN CA C 53.50 0.10 1 26 17 17 SER H H 7.60 0.02 1 27 17 17 SER CA C 57.21 0.10 1 28 17 17 SER N N 113.20 0.10 1 29 18 18 HIS H H 8.66 0.02 1 30 18 18 HIS CA C 54.32 0.10 1 31 18 18 HIS N N 121.26 0.10 1 32 19 19 PRO CA C 62.30 0.10 1 33 20 20 ILE H H 8.77 0.02 1 34 20 20 ILE CA C 59.27 0.10 1 35 20 20 ILE N N 124.23 0.10 1 36 21 21 GLN H H 8.25 0.02 1 37 21 21 GLN CA C 53.96 0.10 1 38 21 21 GLN N N 123.63 0.10 1 39 22 22 TRP H H 7.66 0.02 1 40 22 22 TRP CA C 55.21 0.10 1 41 22 22 TRP N N 117.90 0.10 1 42 23 23 ASN H H 8.61 0.02 1 43 23 23 ASN CA C 52.33 0.10 1 44 23 23 ASN CB C 40.37 0.10 1 45 23 23 ASN N N 117.38 0.10 1 46 24 24 ALA H H 8.60 0.02 1 47 24 24 ALA CA C 49.83 0.10 1 48 24 24 ALA CB C 19.50 0.10 1 49 24 24 ALA N N 127.42 0.10 1 50 25 25 PRO CA C 64.18 0.10 1 51 25 25 PRO CB C 32.10 0.10 1 52 26 26 GLN H H 8.20 0.02 1 53 26 26 GLN CA C 53.77 0.10 1 54 26 26 GLN CB C 28.77 0.10 1 55 26 26 GLN N N 115.88 0.10 1 56 29 29 HIS CA C 55.31 0.10 1 57 29 29 HIS CB C 29.66 0.10 1 58 30 30 ILE H H 8.02 0.02 1 59 30 30 ILE CA C 60.71 0.10 1 60 30 30 ILE N N 123.04 0.10 1 61 31 31 SER H H 8.98 0.02 1 62 31 31 SER CA C 59.78 0.10 1 63 31 31 SER CB C 64.18 0.10 1 64 31 31 SER N N 121.96 0.10 1 65 32 32 LYS H H 7.51 0.02 1 66 32 32 LYS CA C 55.46 0.10 1 67 32 32 LYS CB C 35.00 0.10 1 68 32 32 LYS N N 117.84 0.10 1 69 33 33 TYR H H 9.21 0.02 1 70 33 33 TYR CA C 55.80 0.10 1 71 33 33 TYR N N 117.22 0.10 1 72 34 34 ILE H H 9.20 0.02 1 73 34 34 ILE CA C 60.33 0.10 1 74 34 34 ILE N N 121.22 0.10 1 75 35 35 LEU H H 9.04 0.02 1 76 35 35 LEU CA C 52.86 0.10 1 77 35 35 LEU CB C 45.68 0.10 1 78 35 35 LEU N N 130.43 0.10 1 79 36 36 ARG H H 9.36 0.02 1 80 36 36 ARG HE H 6.99 0.02 1 81 36 36 ARG CA C 53.84 0.10 1 82 36 36 ARG N N 123.15 0.10 1 83 36 36 ARG NE N 83.48 0.10 1 84 37 37 TRP H H 8.99 0.02 1 85 37 37 TRP HE1 H 10.12 0.02 1 86 37 37 TRP CA C 58.13 0.10 1 87 37 37 TRP N N 119.83 0.10 1 88 37 37 TRP NE1 N 128.98 0.10 1 89 38 38 ARG H H 8.88 0.02 1 90 38 38 ARG HE H 6.53 0.02 1 91 38 38 ARG CA C 54.52 0.10 1 92 38 38 ARG N N 116.36 0.10 1 93 38 38 ARG NE N 87.19 0.10 1 94 39 39 PRO CA C 63.59 0.10 1 95 39 39 PRO CB C 31.26 0.10 1 96 40 40 LYS H H 9.07 0.02 1 97 40 40 LYS CA C 58.14 0.10 1 98 40 40 LYS CB C 32.95 0.10 1 99 40 40 LYS N N 126.87 0.10 1 100 41 41 ASN H H 8.71 0.02 1 101 41 41 ASN CA C 54.46 0.10 1 102 41 41 ASN CB C 37.27 0.10 1 103 41 41 ASN N N 118.02 0.10 1 104 42 42 SER H H 7.58 0.02 1 105 42 42 SER CA C 57.55 0.10 1 106 42 42 SER CB C 64.95 0.10 1 107 42 42 SER N N 113.34 0.10 1 108 43 43 VAL H H 8.05 0.02 1 109 43 43 VAL CA C 61.10 0.10 1 110 43 43 VAL CB C 31.29 0.10 1 111 43 43 VAL N N 115.52 0.10 1 112 44 44 GLY H H 7.93 0.02 1 113 44 44 GLY CA C 44.40 0.10 1 114 44 44 GLY N N 110.29 0.10 1 115 45 45 ARG H H 8.15 0.02 1 116 45 45 ARG CA C 56.16 0.10 1 117 45 45 ARG CB C 31.14 0.10 1 118 45 45 ARG N N 118.73 0.10 1 119 46 46 TRP H H 8.28 0.02 1 120 46 46 TRP HE1 H 10.04 0.02 1 121 46 46 TRP CA C 57.73 0.10 1 122 46 46 TRP CB C 29.45 0.10 1 123 46 46 TRP N N 121.90 0.10 1 124 46 46 TRP NE1 N 130.41 0.10 1 125 47 47 LYS H H 8.40 0.02 1 126 47 47 LYS CA C 55.84 0.10 1 127 47 47 LYS CB C 32.18 0.10 1 128 47 47 LYS N N 124.47 0.10 1 129 48 48 GLU H H 7.75 0.02 1 130 48 48 GLU CA C 54.59 0.10 1 131 48 48 GLU CB C 34.98 0.10 1 132 48 48 GLU N N 116.76 0.10 1 133 49 49 ALA H H 9.32 0.02 1 134 49 49 ALA CA C 51.45 0.10 1 135 49 49 ALA CB C 22.42 0.10 1 136 49 49 ALA N N 125.99 0.10 1 137 50 50 THR H H 8.43 0.02 1 138 50 50 THR CA C 62.15 0.10 1 139 50 50 THR CB C 69.73 0.10 1 140 50 50 THR N N 116.57 0.10 1 141 51 51 ILE H H 9.52 0.02 1 142 51 51 ILE CA C 58.74 0.10 1 143 51 51 ILE N N 129.69 0.10 1 144 52 52 PRO CA C 63.50 0.10 1 145 52 52 PRO CB C 33.38 0.10 1 146 53 53 GLY H H 7.65 0.02 1 147 53 53 GLY CA C 47.04 0.10 1 148 53 53 GLY N N 103.90 0.10 1 149 54 54 HIS H H 7.73 0.02 1 150 54 54 HIS CA C 56.37 0.10 1 151 54 54 HIS CB C 29.98 0.10 1 152 54 54 HIS N N 114.01 0.10 1 153 55 55 LEU H H 7.70 0.02 1 154 55 55 LEU CA C 54.31 0.10 1 155 55 55 LEU CB C 43.41 0.10 1 156 55 55 LEU N N 123.77 0.10 1 157 56 56 ASN H H 7.66 0.02 1 158 56 56 ASN CA C 51.06 0.10 1 159 56 56 ASN N N 114.48 0.10 1 160 57 57 SER H H 6.39 0.02 1 161 57 57 SER CA C 56.41 0.10 1 162 57 57 SER CB C 65.97 0.10 1 163 57 57 SER N N 108.37 0.10 1 164 58 58 TYR H H 8.51 0.02 1 165 58 58 TYR CA C 58.80 0.10 1 166 58 58 TYR CB C 42.59 0.10 1 167 58 58 TYR N N 120.15 0.10 1 168 59 59 THR H H 7.37 0.02 1 169 59 59 THR CA C 62.04 0.10 1 170 59 59 THR N N 123.23 0.10 1 171 60 60 ILE H H 7.87 0.02 1 172 60 60 ILE CA C 62.12 0.10 1 173 60 60 ILE CB C 38.68 0.10 1 174 60 60 ILE N N 128.50 0.10 1 175 61 61 LYS H H 8.36 0.02 1 176 61 61 LYS CA C 55.06 0.10 1 177 61 61 LYS N N 127.50 0.10 1 178 62 62 GLY H H 8.43 0.02 1 179 62 62 GLY CA C 46.69 0.10 1 180 62 62 GLY N N 108.51 0.10 1 181 63 63 LEU H H 8.20 0.02 1 182 63 63 LEU CA C 54.20 0.10 1 183 63 63 LEU N N 119.65 0.10 1 184 64 64 LYS H H 8.42 0.02 1 185 64 64 LYS CA C 59.82 0.10 1 186 64 64 LYS N N 122.15 0.10 1 187 65 65 PRO CA C 63.22 0.10 1 188 66 66 GLY H H 8.46 0.02 1 189 66 66 GLY CA C 46.03 0.10 1 190 66 66 GLY N N 111.50 0.10 1 191 67 67 VAL H H 7.31 0.02 1 192 67 67 VAL CA C 61.88 0.10 1 193 67 67 VAL CB C 33.97 0.10 1 194 67 67 VAL N N 121.42 0.10 1 195 68 68 VAL H H 8.03 0.02 1 196 68 68 VAL CA C 62.07 0.10 1 197 68 68 VAL CB C 31.72 0.10 1 198 68 68 VAL N N 125.59 0.10 1 199 69 69 TYR H H 9.47 0.02 1 200 69 69 TYR CA C 57.79 0.10 1 201 69 69 TYR N N 129.00 0.10 1 202 70 70 GLU H H 9.04 0.02 1 203 70 70 GLU CA C 54.30 0.10 1 204 70 70 GLU N N 118.19 0.10 1 205 71 71 GLY H H 9.13 0.02 1 206 71 71 GLY CA C 43.27 0.10 1 207 71 71 GLY N N 108.92 0.10 1 208 72 72 GLN H H 9.17 0.02 1 209 72 72 GLN CA C 54.22 0.10 1 210 72 72 GLN N N 118.97 0.10 1 211 73 73 LEU H H 9.27 0.02 1 212 73 73 LEU CA C 53.40 0.10 1 213 73 73 LEU N N 124.46 0.10 1 214 74 74 ILE H H 10.02 0.02 1 215 74 74 ILE CA C 60.33 0.10 1 216 74 74 ILE N N 131.77 0.10 1 217 75 75 SER H H 9.17 0.02 1 218 75 75 SER CA C 56.61 0.10 1 219 75 75 SER N N 122.41 0.10 1 220 76 76 ILE H H 8.24 0.02 1 221 76 76 ILE CA C 60.85 0.10 1 222 76 76 ILE N N 125.36 0.10 1 223 77 77 GLN H H 8.56 0.02 1 224 77 77 GLN CA C 55.22 0.10 1 225 77 77 GLN CB C 30.07 0.10 1 226 77 77 GLN N N 125.71 0.10 1 227 78 78 GLN H H 8.55 0.02 1 228 78 78 GLN CA C 58.23 0.10 1 229 78 78 GLN N N 120.90 0.10 1 230 79 79 TYR H H 8.16 0.02 1 231 79 79 TYR CA C 57.90 0.10 1 232 79 79 TYR N N 115.46 0.10 1 233 80 80 GLY H H 7.95 0.02 1 234 80 80 GLY CA C 45.62 0.10 1 235 80 80 GLY N N 106.83 0.10 1 236 81 81 HIS H H 7.55 0.02 1 237 81 81 HIS CA C 56.93 0.10 1 238 81 81 HIS CB C 31.15 0.10 1 239 81 81 HIS N N 120.26 0.10 1 240 82 82 GLN H H 8.06 0.02 1 241 82 82 GLN CA C 54.37 0.10 1 242 82 82 GLN N N 122.24 0.10 1 243 83 83 GLU H H 8.20 0.02 1 244 83 83 GLU CA C 55.00 0.10 1 245 83 83 GLU CB C 33.08 0.10 1 246 83 83 GLU N N 121.12 0.10 1 247 84 84 VAL H H 8.77 0.02 1 248 84 84 VAL CA C 61.74 0.10 1 249 84 84 VAL N N 122.78 0.10 1 250 85 85 THR H H 9.00 0.02 1 251 85 85 THR CA C 62.28 0.10 1 252 85 85 THR N N 126.34 0.10 1 253 86 86 ARG H H 9.01 0.02 1 254 86 86 ARG CA C 55.50 0.10 1 255 86 86 ARG CB C 32.53 0.10 1 256 86 86 ARG N N 127.45 0.10 1 257 87 87 PHE H H 8.14 0.02 1 258 87 87 PHE CA C 56.25 0.10 1 259 87 87 PHE CB C 40.00 0.10 1 260 87 87 PHE N N 118.63 0.10 1 261 88 88 ASP H H 8.62 0.02 1 262 88 88 ASP CA C 52.80 0.10 1 263 88 88 ASP CB C 43.53 0.10 1 264 88 88 ASP N N 120.14 0.10 1 265 89 89 PHE H H 9.26 0.02 1 266 89 89 PHE CA C 57.06 0.10 1 267 89 89 PHE N N 115.65 0.10 1 268 90 90 THR H H 8.67 0.02 1 269 90 90 THR CA C 59.99 0.10 1 270 90 90 THR N N 112.82 0.10 1 271 91 91 THR H H 8.03 0.02 1 272 91 91 THR CA C 60.02 0.10 1 273 91 91 THR N N 119.12 0.10 1 274 97 97 PRO CA C 63.09 0.10 1 275 97 97 PRO CB C 32.35 0.10 1 276 98 98 VAL H H 8.43 0.02 1 277 98 98 VAL CA C 62.28 0.10 1 278 98 98 VAL CB C 33.22 0.10 1 279 98 98 VAL N N 120.76 0.10 1 280 100 100 SER CA C 58.09 0.10 1 281 100 100 SER CB C 64.21 0.10 1 282 101 101 ASN H H 8.52 0.02 1 283 101 101 ASN CA C 53.38 0.10 1 284 101 101 ASN CB C 39.20 0.10 1 285 101 101 ASN N N 120.89 0.10 1 286 102 102 THR H H 8.16 0.02 1 287 102 102 THR CA C 62.08 0.10 1 288 102 102 THR CB C 69.93 0.10 1 289 102 102 THR N N 114.82 0.10 1 290 103 103 VAL H H 8.24 0.02 1 291 103 103 VAL CA C 62.46 0.10 1 292 103 103 VAL CB C 32.72 0.10 1 293 103 103 VAL N N 122.72 0.10 1 294 104 104 THR H H 8.21 0.02 1 295 104 104 THR CA C 61.98 0.10 1 296 104 104 THR CB C 69.93 0.10 1 297 104 104 THR N N 117.26 0.10 1 298 105 105 GLY H H 8.32 0.02 1 299 105 105 GLY CA C 45.39 0.10 1 300 105 105 GLY N N 111.09 0.10 1 301 106 106 GLU H H 8.26 0.02 1 302 106 106 GLU CA C 56.59 0.10 1 303 106 106 GLU CB C 30.62 0.10 1 304 106 106 GLU N N 120.62 0.10 1 305 107 107 THR H H 8.27 0.02 1 306 107 107 THR CA C 61.79 0.10 1 307 107 107 THR CB C 69.98 0.10 1 308 107 107 THR N N 115.40 0.10 1 309 108 108 THR H H 8.23 0.02 1 310 108 108 THR CA C 59.77 0.10 1 311 108 108 THR CB C 69.90 0.10 1 312 108 108 THR N N 118.93 0.10 1 313 109 109 PRO CA C 63.26 0.10 1 314 109 109 PRO CB C 32.03 0.10 1 315 110 110 PHE H H 8.20 0.02 1 316 110 110 PHE CA C 57.73 0.10 1 317 110 110 PHE CB C 39.68 0.10 1 318 110 110 PHE N N 120.40 0.10 1 319 111 111 SER H H 8.01 0.02 1 320 111 111 SER CA C 55.73 0.10 1 321 111 111 SER CB C 63.85 0.10 1 322 111 111 SER N N 119.42 0.10 1 323 112 112 PRO CA C 63.20 0.10 1 324 112 112 PRO CB C 32.17 0.10 1 325 113 113 LEU H H 8.16 0.02 1 326 113 113 LEU CA C 55.41 0.10 1 327 113 113 LEU CB C 42.30 0.10 1 328 113 113 LEU N N 121.65 0.10 1 329 114 114 VAL H H 7.94 0.02 1 330 114 114 VAL CA C 61.98 0.10 1 331 114 114 VAL CB C 32.96 0.10 1 332 114 114 VAL N N 120.87 0.10 1 333 115 115 ALA H H 8.35 0.02 1 334 115 115 ALA CA C 52.43 0.10 1 335 115 115 ALA CB C 19.50 0.10 1 336 115 115 ALA N N 127.98 0.10 1 337 116 116 THR H H 8.14 0.02 1 338 116 116 THR CA C 61.68 0.10 1 339 116 116 THR CB C 70.00 0.10 1 340 116 116 THR N N 113.45 0.10 1 341 117 117 SER H H 8.33 0.02 1 342 117 117 SER CA C 58.48 0.10 1 343 117 117 SER CB C 64.00 0.10 1 344 117 117 SER N N 117.64 0.10 1 345 118 118 GLU H H 8.46 0.02 1 346 118 118 GLU CA C 56.79 0.10 1 347 118 118 GLU CB C 30.37 0.10 1 348 118 118 GLU N N 122.57 0.10 1 349 119 119 SER H H 8.28 0.02 1 350 119 119 SER CA C 58.46 0.10 1 351 119 119 SER CB C 63.93 0.10 1 352 119 119 SER N N 116.56 0.10 1 353 120 120 VAL H H 8.12 0.02 1 354 120 120 VAL CA C 62.29 0.10 1 355 120 120 VAL CB C 32.79 0.10 1 356 120 120 VAL N N 121.86 0.10 1 357 121 121 THR H H 8.25 0.02 1 358 121 121 THR CA C 61.90 0.10 1 359 121 121 THR CB C 70.03 0.10 1 360 121 121 THR N N 117.95 0.10 1 361 122 122 GLU H H 8.36 0.02 1 362 122 122 GLU CA C 56.48 0.10 1 363 122 122 GLU CB C 30.42 0.10 1 364 122 122 GLU N N 123.33 0.10 1 365 123 123 ILE H H 8.22 0.02 1 366 123 123 ILE CA C 61.21 0.10 1 367 123 123 ILE CB C 38.78 0.10 1 368 123 123 ILE N N 122.27 0.10 1 369 124 124 THR H H 8.31 0.02 1 370 124 124 THR CA C 61.40 0.10 1 371 124 124 THR CB C 70.08 0.10 1 372 124 124 THR N N 118.96 0.10 1 373 125 125 ALA H H 8.26 0.02 1 374 125 125 ALA CA C 52.48 0.10 1 375 125 125 ALA CB C 20.08 0.10 1 376 125 125 ALA N N 125.69 0.10 1 377 126 126 SER H H 8.41 0.02 1 378 126 126 SER CA C 58.01 0.10 1 379 126 126 SER CB C 64.64 0.10 1 380 126 126 SER N N 115.32 0.10 1 381 127 127 SER H H 8.05 0.02 1 382 127 127 SER CA C 57.62 0.10 1 383 127 127 SER CB C 65.64 0.10 1 384 127 127 SER N N 115.19 0.10 1 385 128 128 PHE H H 7.78 0.02 1 386 128 128 PHE CA C 56.75 0.10 1 387 128 128 PHE CB C 40.59 0.10 1 388 128 128 PHE N N 118.04 0.10 1 389 129 129 VAL H H 8.23 0.02 1 390 129 129 VAL CA C 60.87 0.10 1 391 129 129 VAL CB C 33.85 0.10 1 392 129 129 VAL N N 122.70 0.10 1 393 130 130 VAL H H 8.38 0.02 1 394 130 130 VAL CA C 60.61 0.10 1 395 130 130 VAL CB C 34.73 0.10 1 396 130 130 VAL N N 126.07 0.10 1 397 131 131 SER H H 8.12 0.02 1 398 131 131 SER CA C 57.26 0.10 1 399 131 131 SER CB C 66.16 0.10 1 400 131 131 SER N N 119.04 0.10 1 401 132 132 TRP H H 7.75 0.02 1 402 132 132 TRP HE1 H 6.54 0.02 1 403 132 132 TRP CA C 56.27 0.10 1 404 132 132 TRP CB C 30.70 0.10 1 405 132 132 TRP N N 118.68 0.10 1 406 132 132 TRP NE1 N 126.62 0.10 1 407 133 133 VAL H H 8.04 0.02 1 408 133 133 VAL CA C 61.19 0.10 1 409 133 133 VAL CB C 34.00 0.10 1 410 133 133 VAL N N 116.75 0.10 1 411 134 134 SER H H 8.61 0.02 1 412 134 134 SER CA C 58.09 0.10 1 413 134 134 SER CB C 64.36 0.10 1 414 134 134 SER N N 119.20 0.10 1 415 135 135 ALA H H 8.95 0.02 1 416 135 135 ALA CA C 52.14 0.10 1 417 135 135 ALA CB C 19.95 0.10 1 418 135 135 ALA N N 128.31 0.10 1 419 136 136 SER H H 8.02 0.02 1 420 136 136 SER CA C 57.75 0.10 1 421 136 136 SER CB C 64.23 0.10 1 422 136 136 SER N N 113.58 0.10 1 423 137 137 ASP H H 8.53 0.02 1 424 137 137 ASP CA C 54.85 0.10 1 425 137 137 ASP CB C 41.19 0.10 1 426 137 137 ASP N N 122.44 0.10 1 427 138 138 THR H H 8.11 0.02 1 428 138 138 THR CA C 61.01 0.10 1 429 138 138 THR CB C 69.09 0.10 1 430 138 138 THR N N 111.32 0.10 1 431 139 139 VAL H H 7.57 0.02 1 432 139 139 VAL CA C 61.84 0.10 1 433 139 139 VAL CB C 33.66 0.10 1 434 139 139 VAL N N 120.54 0.10 1 435 140 140 SER H H 9.10 0.02 1 436 140 140 SER CA C 59.02 0.10 1 437 140 140 SER CB C 64.71 0.10 1 438 140 140 SER N N 119.09 0.10 1 439 141 141 GLY H H 7.37 0.02 1 440 141 141 GLY CA C 44.63 0.10 1 441 141 141 GLY N N 107.91 0.10 1 442 142 142 PHE H H 8.36 0.02 1 443 142 142 PHE CA C 56.69 0.10 1 444 142 142 PHE CB C 43.77 0.10 1 445 142 142 PHE N N 114.27 0.10 1 446 143 143 ARG H H 9.27 0.02 1 447 143 143 ARG HE H 8.26 0.02 1 448 143 143 ARG CA C 54.93 0.10 1 449 143 143 ARG CB C 34.09 0.10 1 450 143 143 ARG N N 123.69 0.10 1 451 143 143 ARG NE N 85.40 0.10 1 452 144 144 VAL H H 9.50 0.02 1 453 144 144 VAL CA C 61.40 0.10 1 454 144 144 VAL CB C 33.43 0.10 1 455 144 144 VAL N N 128.51 0.10 1 456 145 145 GLU H H 9.59 0.02 1 457 145 145 GLU CA C 53.90 0.10 1 458 145 145 GLU CB C 34.66 0.10 1 459 145 145 GLU N N 129.12 0.10 1 460 146 146 TYR H H 8.92 0.02 1 461 146 146 TYR CA C 55.09 0.10 1 462 146 146 TYR CB C 41.73 0.10 1 463 146 146 TYR N N 120.81 0.10 1 464 147 147 GLU H H 8.84 0.02 1 465 147 147 GLU CA C 54.24 0.10 1 466 147 147 GLU CB C 33.40 0.10 1 467 147 147 GLU N N 118.35 0.10 1 468 148 148 LEU H H 9.15 0.02 1 469 148 148 LEU CA C 55.20 0.10 1 470 148 148 LEU CB C 42.82 0.10 1 471 148 148 LEU N N 125.16 0.10 1 472 149 149 SER H H 8.40 0.02 1 473 149 149 SER CA C 60.04 0.10 1 474 149 149 SER CB C 63.23 0.10 1 475 149 149 SER N N 117.32 0.10 1 476 150 150 GLU H H 8.21 0.02 1 477 150 150 GLU CA C 57.06 0.10 1 478 150 150 GLU CB C 30.01 0.10 1 479 150 150 GLU N N 119.18 0.10 1 480 151 151 GLU H H 7.98 0.02 1 481 151 151 GLU CA C 56.88 0.10 1 482 151 151 GLU CB C 30.36 0.10 1 483 151 151 GLU N N 118.90 0.10 1 484 152 152 GLY H H 8.48 0.02 1 485 152 152 GLY CA C 45.94 0.10 1 486 152 152 GLY N N 109.16 0.10 1 487 153 153 ASP H H 8.22 0.02 1 488 153 153 ASP CA C 53.73 0.10 1 489 153 153 ASP CB C 42.33 0.10 1 490 153 153 ASP N N 120.76 0.10 1 491 154 154 GLU H H 8.37 0.02 1 492 154 154 GLU CA C 54.12 0.10 1 493 154 154 GLU CB C 30.14 0.10 1 494 154 154 GLU N N 121.14 0.10 1 495 155 155 PRO CA C 63.02 0.10 1 496 155 155 PRO CB C 32.42 0.10 1 497 156 156 GLN H H 7.96 0.02 1 498 156 156 GLN CA C 54.18 0.10 1 499 156 156 GLN CB C 31.60 0.10 1 500 156 156 GLN N N 119.21 0.10 1 501 157 157 TYR H H 8.05 0.02 1 502 157 157 TYR CA C 56.46 0.10 1 503 157 157 TYR CB C 42.96 0.10 1 504 157 157 TYR N N 114.52 0.10 1 505 158 158 LEU H H 9.26 0.02 1 506 158 158 LEU CA C 54.50 0.10 1 507 158 158 LEU CB C 46.08 0.10 1 508 158 158 LEU N N 121.98 0.10 1 509 159 159 ASP H H 8.70 0.02 1 510 159 159 ASP CA C 54.39 0.10 1 511 159 159 ASP CB C 42.76 0.10 1 512 159 159 ASP N N 123.54 0.10 1 513 160 160 LEU H H 9.24 0.02 1 514 160 160 LEU CA C 51.84 0.10 1 515 160 160 LEU CB C 44.87 0.10 1 516 160 160 LEU N N 124.00 0.10 1 517 161 161 PRO CA C 62.33 0.10 1 518 161 161 PRO CB C 33.61 0.10 1 519 162 162 SER H H 8.79 0.02 1 520 162 162 SER CA C 61.12 0.10 1 521 162 162 SER CB C 63.42 0.10 1 522 162 162 SER N N 112.95 0.10 1 523 163 163 THR H H 7.09 0.02 1 524 163 163 THR CA C 61.19 0.10 1 525 163 163 THR CB C 69.20 0.10 1 526 163 163 THR N N 107.44 0.10 1 527 164 164 ALA H H 7.88 0.02 1 528 164 164 ALA CA C 52.95 0.10 1 529 164 164 ALA CB C 21.26 0.10 1 530 164 164 ALA N N 126.33 0.10 1 531 165 165 THR H H 8.02 0.02 1 532 165 165 THR CA C 59.63 0.10 1 533 165 165 THR CB C 69.82 0.10 1 534 165 165 THR N N 108.42 0.10 1 535 166 166 SER H H 6.75 0.02 1 536 166 166 SER CA C 56.73 0.10 1 537 166 166 SER CB C 65.34 0.10 1 538 166 166 SER N N 111.91 0.10 1 539 167 167 VAL H H 8.62 0.02 1 540 167 167 VAL CA C 60.69 0.10 1 541 167 167 VAL CB C 34.95 0.10 1 542 167 167 VAL N N 117.33 0.10 1 543 168 168 ASN H H 8.13 0.02 1 544 168 168 ASN CA C 51.77 0.10 1 545 168 168 ASN CB C 39.80 0.10 1 546 168 168 ASN N N 125.13 0.10 1 547 169 169 ILE H H 8.69 0.02 1 548 169 169 ILE CA C 58.55 0.10 1 549 169 169 ILE CB C 37.09 0.10 1 550 169 169 ILE N N 127.35 0.10 1 551 170 170 PRO CA C 62.28 0.10 1 552 170 170 PRO CB C 33.31 0.10 1 553 171 171 ASP H H 8.27 0.02 1 554 171 171 ASP CA C 55.12 0.10 1 555 171 171 ASP CB C 39.29 0.10 1 556 171 171 ASP N N 113.40 0.10 1 557 172 172 LEU H H 8.11 0.02 1 558 172 172 LEU CA C 53.97 0.10 1 559 172 172 LEU CB C 41.22 0.10 1 560 172 172 LEU N N 117.96 0.10 1 561 173 173 LEU H H 8.35 0.02 1 562 173 173 LEU CA C 52.93 0.10 1 563 173 173 LEU CB C 42.28 0.10 1 564 173 173 LEU N N 123.09 0.10 1 565 174 174 PRO CA C 62.96 0.10 1 566 174 174 PRO CB C 32.58 0.10 1 567 175 175 GLY H H 8.34 0.02 1 568 175 175 GLY CA C 47.25 0.10 1 569 175 175 GLY N N 111.09 0.10 1 570 176 176 ARG H H 8.02 0.02 1 571 176 176 ARG CA C 52.45 0.10 1 572 176 176 ARG CB C 33.36 0.10 1 573 176 176 ARG N N 118.43 0.10 1 574 177 177 LYS H H 8.09 0.02 1 575 177 177 LYS CA C 56.03 0.10 1 576 177 177 LYS CB C 34.03 0.10 1 577 177 177 LYS N N 120.46 0.10 1 578 178 178 TYR H H 9.12 0.02 1 579 178 178 TYR CA C 57.72 0.10 1 580 178 178 TYR CB C 42.20 0.10 1 581 178 178 TYR N N 125.70 0.10 1 582 179 179 ILE H H 9.29 0.02 1 583 179 179 ILE CA C 60.21 0.10 1 584 179 179 ILE CB C 39.11 0.10 1 585 179 179 ILE N N 121.99 0.10 1 586 180 180 VAL H H 8.65 0.02 1 587 180 180 VAL CA C 60.91 0.10 1 588 180 180 VAL CB C 34.58 0.10 1 589 180 180 VAL N N 126.04 0.10 1 590 181 181 ASN H H 9.40 0.02 1 591 181 181 ASN CA C 51.66 0.10 1 592 181 181 ASN CB C 42.80 0.10 1 593 181 181 ASN N N 125.11 0.10 1 594 182 182 VAL H H 9.00 0.02 1 595 182 182 VAL CA C 61.57 0.10 1 596 182 182 VAL CB C 32.95 0.10 1 597 182 182 VAL N N 121.16 0.10 1 598 183 183 TYR H H 9.53 0.02 1 599 183 183 TYR CA C 56.05 0.10 1 600 183 183 TYR CB C 40.70 0.10 1 601 183 183 TYR N N 125.45 0.10 1 602 184 184 GLN H H 9.38 0.02 1 603 184 184 GLN CA C 54.68 0.10 1 604 184 184 GLN CB C 32.26 0.10 1 605 184 184 GLN N N 121.81 0.10 1 606 185 185 ILE H H 8.28 0.02 1 607 185 185 ILE CA C 59.63 0.10 1 608 185 185 ILE CB C 37.86 0.10 1 609 185 185 ILE N N 126.12 0.10 1 610 186 186 SER H H 8.90 0.02 1 611 186 186 SER CA C 57.89 0.10 1 612 186 186 SER CB C 65.30 0.10 1 613 186 186 SER N N 122.79 0.10 1 614 187 187 GLU H H 8.96 0.02 1 615 187 187 GLU CA C 59.42 0.10 1 616 187 187 GLU CB C 29.51 0.10 1 617 187 187 GLU N N 122.77 0.10 1 618 188 188 ASP H H 7.90 0.02 1 619 188 188 ASP CA C 53.59 0.10 1 620 188 188 ASP CB C 40.56 0.10 1 621 188 188 ASP N N 115.61 0.10 1 622 189 189 GLY H H 7.98 0.02 1 623 189 189 GLY CA C 45.33 0.10 1 624 189 189 GLY N N 108.21 0.10 1 625 190 190 GLU H H 7.77 0.02 1 626 190 190 GLU CA C 56.58 0.10 1 627 190 190 GLU CB C 30.28 0.10 1 628 190 190 GLU N N 120.98 0.10 1 629 191 191 GLN H H 8.81 0.02 1 630 191 191 GLN CA C 54.52 0.10 1 631 191 191 GLN CB C 31.13 0.10 1 632 191 191 GLN N N 124.12 0.10 1 633 192 192 SER H H 8.86 0.02 1 634 192 192 SER CA C 57.10 0.10 1 635 192 192 SER CB C 65.34 0.10 1 636 192 192 SER N N 116.89 0.10 1 637 193 193 LEU H H 9.04 0.02 1 638 193 193 LEU CA C 56.22 0.10 1 639 193 193 LEU CB C 42.52 0.10 1 640 193 193 LEU N N 129.33 0.10 1 641 194 194 ILE H H 8.97 0.02 1 642 194 194 ILE CA C 61.30 0.10 1 643 194 194 ILE CB C 40.02 0.10 1 644 194 194 ILE N N 121.61 0.10 1 645 195 195 LEU H H 7.33 0.02 1 646 195 195 LEU CA C 56.08 0.10 1 647 195 195 LEU CB C 45.41 0.10 1 648 195 195 LEU N N 122.64 0.10 1 649 196 196 SER H H 8.45 0.02 1 650 196 196 SER CA C 56.94 0.10 1 651 196 196 SER CB C 65.16 0.10 1 652 196 196 SER N N 120.57 0.10 1 653 197 197 THR H H 9.37 0.02 1 654 197 197 THR CA C 59.64 0.10 1 655 197 197 THR CB C 70.09 0.10 1 656 197 197 THR N N 121.85 0.10 1 657 198 198 SER H H 8.37 0.02 1 658 198 198 SER CA C 56.63 0.10 1 659 198 198 SER CB C 65.84 0.10 1 660 198 198 SER N N 117.60 0.10 1 661 199 199 GLN H H 8.89 0.02 1 662 199 199 GLN CA C 54.74 0.10 1 663 199 199 GLN CB C 32.44 0.10 1 664 199 199 GLN N N 121.96 0.10 1 665 200 200 THR H H 8.35 0.02 1 666 200 200 THR CA C 61.07 0.10 1 667 200 200 THR CB C 70.22 0.10 1 668 200 200 THR N N 118.88 0.10 1 669 201 201 THR H H 8.95 0.02 1 670 201 201 THR CA C 62.21 0.10 1 671 201 201 THR CB C 70.27 0.10 1 672 201 201 THR N N 122.79 0.10 1 stop_ save_