data_17829 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; FVIII C2 Domain ; _BMRB_accession_number 17829 _BMRB_flat_file_name bmr17829.str _Entry_type original _Submission_date 2011-08-03 _Accession_date 2011-08-03 _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 Nuzzio Kristin M. . 2 Cullinan David B. . 3 Novakovic Valerie A. . 4 Boettcher John M. . 5 Rienstra Chad M. . 6 Gilbert Gary E. . 7 Baleja James D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 145 "13C chemical shifts" 440 "15N chemical shifts" 145 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-03-25 update BMRB 'update entry citation' 2012-03-01 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_C2_Domain_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Backbone resonance assignments of the C2 domain of coagulation factor VIII.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 22392338 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Nuzzio Kristin M. . 2 Cullinan David B. . 3 Novakovic Valerie A. . 4 Boettcher John M. . 5 Rienstra Chad M. . 6 Gilbert Gary E. . 7 Baleja James D. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 7 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 31 _Page_last 34 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'C2 Domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label C2_Domain $C2_Domain 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_C2_Domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common C2_Domain _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 163 _Mol_residue_sequence ; GSHMCSMPLGMESKAISDAQ ITASSYFTNMFATWSPSKAR LHLQGRSNAWRPQVNNPKEW LQVDFQKTMKVTGVTTQGVK SLLTSMYVKEFLISSSQDGH QWTLFFQNGKVKVFQGNQDS FTPVVNSLDPPLLTRYLRIH PQSWVHQIALRMEVLGCEAQ DLY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 . GLY 2 . SER 3 . HIS 4 . MET 5 2174 CYS 6 2175 SER 7 2176 MET 8 2177 PRO 9 2178 LEU 10 2179 GLY 11 2180 MET 12 2181 GLU 13 2182 SER 14 2183 LYS 15 2184 ALA 16 2185 ILE 17 2186 SER 18 2187 ASP 19 2188 ALA 20 2189 GLN 21 2190 ILE 22 2191 THR 23 2192 ALA 24 2193 SER 25 2194 SER 26 2195 TYR 27 2196 PHE 28 2197 THR 29 2198 ASN 30 2199 MET 31 2200 PHE 32 2201 ALA 33 2202 THR 34 2203 TRP 35 2204 SER 36 2205 PRO 37 2206 SER 38 2207 LYS 39 2208 ALA 40 2209 ARG 41 2210 LEU 42 2211 HIS 43 2212 LEU 44 2213 GLN 45 2214 GLY 46 2215 ARG 47 2216 SER 48 2217 ASN 49 2218 ALA 50 2219 TRP 51 2220 ARG 52 2221 PRO 53 2222 GLN 54 2223 VAL 55 2224 ASN 56 2225 ASN 57 2226 PRO 58 2227 LYS 59 2228 GLU 60 2229 TRP 61 2230 LEU 62 2231 GLN 63 2232 VAL 64 2233 ASP 65 2234 PHE 66 2235 GLN 67 2236 LYS 68 2237 THR 69 2238 MET 70 2239 LYS 71 2240 VAL 72 2241 THR 73 2242 GLY 74 2243 VAL 75 2244 THR 76 2245 THR 77 2246 GLN 78 2247 GLY 79 2248 VAL 80 2249 LYS 81 2250 SER 82 2251 LEU 83 2252 LEU 84 2253 THR 85 2254 SER 86 2255 MET 87 2256 TYR 88 2257 VAL 89 2258 LYS 90 2259 GLU 91 2260 PHE 92 2261 LEU 93 2262 ILE 94 2263 SER 95 2264 SER 96 2265 SER 97 2266 GLN 98 2267 ASP 99 2268 GLY 100 2269 HIS 101 2270 GLN 102 2271 TRP 103 2272 THR 104 2273 LEU 105 2274 PHE 106 2275 PHE 107 2276 GLN 108 2277 ASN 109 2278 GLY 110 2279 LYS 111 2280 VAL 112 2281 LYS 113 2282 VAL 114 2283 PHE 115 2284 GLN 116 2285 GLY 117 2286 ASN 118 2287 GLN 119 2288 ASP 120 2289 SER 121 2290 PHE 122 2291 THR 123 2292 PRO 124 2293 VAL 125 2294 VAL 126 2295 ASN 127 2296 SER 128 2297 LEU 129 2298 ASP 130 2299 PRO 131 2300 PRO 132 2301 LEU 133 2302 LEU 134 2303 THR 135 2304 ARG 136 2305 TYR 137 2306 LEU 138 2307 ARG 139 2308 ILE 140 2309 HIS 141 2310 PRO 142 2311 GLN 143 2312 SER 144 2313 TRP 145 2314 VAL 146 2315 HIS 147 2316 GLN 148 2317 ILE 149 2318 ALA 150 2319 LEU 151 2320 ARG 152 2321 MET 153 2322 GLU 154 2323 VAL 155 2324 LEU 156 2325 GLY 157 2326 CYS 158 2327 GLU 159 2328 ALA 160 2329 GLN 161 2330 ASP 162 2331 LEU 163 2332 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 1D7P "Crystal Structure Of The C2 Domain Of Human Factor Viii At 1.5 A Resolution At 1.5 A" 95.71 159 99.36 99.36 5.73e-111 PDB 1IQD "Human Factor Viii C2 Domain Complexed To Human Monoclonal Bo2c11 Fab" 95.71 156 99.36 99.36 5.28e-111 PDB 3HNB "Factor Viii Trp2313-His2315 Segment Is Involved In Membrane Shown By Crystal Structure Of Complex Between Factor Viii C And An " 95.09 159 100.00 100.00 5.48e-111 PDB 3HNY "Factor Viii Trp2313-His2315 Segment Is Involved In Membrane Binding As Shown By Crystal Structure Of Complex Between Factor Vii" 95.09 159 100.00 100.00 5.48e-111 PDB 3HOB "Factor Viii Trp2313-His2315 Segment Is Involved In Membrane Shown By Crystal Structure Of Complex Between Factor Viii C And An " 95.09 159 100.00 100.00 5.48e-111 PDB 4KI5 "Cystal Structure Of Human Factor Viii C2 Domain In A Ternary Complex With Murine Inhbitory Antibodies 3e6 And G99" 101.84 183 98.19 98.19 2.19e-115 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $C2_Domain 'E. coli' 562 Bacteria . Escherichia coli 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 $C2_Domain 'recombinant technology' . Escherichia coli . BL21 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 $C2_Domain 0.8 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' EDTA 50 uM 'natural abundance' NaN3 0.01 % 'natural abundance' DSS 20 uM 'natural abundance' imidazole 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _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' 0.05 . 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 0.00 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 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 '3D HNCACB' 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 C2_Domain _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 2174 5 CYS C C 173.305 0.000 1 2 2174 5 CYS CA C 57.241 0.000 1 3 2174 5 CYS CB C 45.537 0.118 1 4 2175 6 SER H H 8.255 0.011 1 5 2175 6 SER C C 172.849 0.000 1 6 2175 6 SER CA C 57.368 0.216 1 7 2175 6 SER CB C 63.371 0.003 1 8 2175 6 SER N N 118.173 0.132 1 9 2176 7 MET H H 8.534 0.013 1 10 2176 7 MET CA C 54.227 0.013 1 11 2176 7 MET CB C 33.021 0.000 1 12 2176 7 MET N N 123.490 0.029 1 13 2177 8 PRO C C 179.000 0.000 1 14 2177 8 PRO CA C 63.355 0.099 1 15 2177 8 PRO CB C 32.665 0.016 1 16 2178 9 LEU H H 9.180 0.011 1 17 2178 9 LEU C C 176.933 0.000 1 18 2178 9 LEU CA C 56.267 0.145 1 19 2178 9 LEU CB C 42.719 0.169 1 20 2178 9 LEU N N 124.342 0.153 1 21 2179 10 GLY H H 7.268 0.010 1 22 2179 10 GLY C C 176.618 0.000 1 23 2179 10 GLY CA C 47.758 0.197 1 24 2179 10 GLY N N 103.551 0.032 1 25 2180 11 MET H H 10.777 0.005 1 26 2180 11 MET C C 179.187 0.000 1 27 2180 11 MET CA C 57.188 0.069 1 28 2180 11 MET CB C 32.552 0.163 1 29 2180 11 MET N N 125.553 0.067 1 30 2181 12 GLU H H 9.406 0.013 1 31 2181 12 GLU C C 179.219 0.000 1 32 2181 12 GLU CA C 60.420 0.073 1 33 2181 12 GLU CB C 30.706 0.091 1 34 2181 12 GLU N N 123.415 0.074 1 35 2182 13 SER H H 9.252 0.014 1 36 2182 13 SER C C 175.588 0.000 1 37 2182 13 SER CA C 59.915 0.090 1 38 2182 13 SER CB C 64.901 0.087 1 39 2182 13 SER N N 114.965 0.097 1 40 2183 14 LYS H H 7.250 0.012 1 41 2183 14 LYS C C 175.228 0.000 1 42 2183 14 LYS CA C 59.793 0.097 1 43 2183 14 LYS CB C 29.571 0.137 1 44 2183 14 LYS N N 113.528 0.077 1 45 2184 15 ALA H H 7.976 0.021 1 46 2184 15 ALA C C 180.681 0.000 1 47 2184 15 ALA CA C 55.437 0.000 1 48 2184 15 ALA CB C 19.061 0.000 1 49 2184 15 ALA N N 123.432 0.048 1 50 2185 16 ILE H H 7.696 0.012 1 51 2185 16 ILE C C 175.419 0.000 1 52 2185 16 ILE CA C 62.036 0.034 1 53 2185 16 ILE N N 117.733 0.064 1 54 2186 17 SER H H 8.101 0.017 1 55 2186 17 SER C C 174.508 0.000 1 56 2186 17 SER CA C 59.442 0.000 1 57 2186 17 SER CB C 65.882 0.133 1 58 2186 17 SER N N 127.543 0.061 1 59 2187 18 ASP H H 8.850 0.015 1 60 2187 18 ASP C C 177.659 0.000 1 61 2187 18 ASP CA C 58.919 0.000 1 62 2187 18 ASP CB C 40.421 0.080 1 63 2187 18 ASP N N 121.826 0.100 1 64 2188 19 ALA H H 7.880 0.012 1 65 2188 19 ALA C C 178.999 0.000 1 66 2188 19 ALA CA C 54.300 0.076 1 67 2188 19 ALA CB C 19.400 0.000 1 68 2188 19 ALA N N 117.970 0.025 1 69 2189 20 GLN H H 7.466 0.020 1 70 2189 20 GLN C C 174.876 0.000 1 71 2189 20 GLN CA C 57.879 0.109 1 72 2189 20 GLN CB C 31.745 0.092 1 73 2189 20 GLN N N 115.376 0.064 1 74 2190 21 ILE H H 7.578 0.012 1 75 2190 21 ILE C C 174.877 0.000 1 76 2190 21 ILE CA C 61.236 0.181 1 77 2190 21 ILE CB C 39.687 0.040 1 78 2190 21 ILE N N 124.624 0.132 1 79 2191 22 THR H H 9.049 0.014 1 80 2191 22 THR C C 172.132 0.000 1 81 2191 22 THR CA C 59.901 0.158 1 82 2191 22 THR CB C 74.053 0.084 1 83 2191 22 THR N N 117.060 0.029 1 84 2192 23 ALA H H 8.192 0.012 1 85 2192 23 ALA C C 176.906 0.000 1 86 2192 23 ALA CA C 52.121 0.078 1 87 2192 23 ALA CB C 25.396 0.118 1 88 2192 23 ALA N N 118.150 0.055 1 89 2193 24 SER H H 7.572 0.011 1 90 2193 24 SER C C 175.218 0.000 1 91 2193 24 SER CA C 61.178 0.223 1 92 2193 24 SER N N 117.317 0.043 1 93 2194 25 SER H H 7.578 0.014 1 94 2194 25 SER C C 172.351 0.000 1 95 2194 25 SER CA C 59.154 0.252 1 96 2194 25 SER CB C 65.172 0.136 1 97 2194 25 SER N N 112.429 0.053 1 98 2195 26 TYR H H 8.302 0.013 1 99 2195 26 TYR C C 172.793 0.000 1 100 2195 26 TYR CA C 57.353 0.053 1 101 2195 26 TYR CB C 40.823 0.000 1 102 2195 26 TYR N N 113.322 0.035 1 103 2196 27 PHE H H 8.236 0.181 1 104 2196 27 PHE C C 174.505 0.000 1 105 2196 27 PHE CA C 58.246 0.112 1 106 2196 27 PHE CB C 40.198 0.118 1 107 2196 27 PHE N N 123.775 0.049 1 108 2197 28 THR H H 7.864 0.012 1 109 2197 28 THR C C 171.756 0.000 1 110 2197 28 THR CA C 61.500 0.000 1 111 2197 28 THR CB C 71.078 0.058 1 112 2197 28 THR N N 123.689 0.030 1 113 2198 29 ASN H H 8.604 0.013 1 114 2198 29 ASN CA C 52.675 0.031 1 115 2198 29 ASN CB C 39.634 0.000 1 116 2198 29 ASN N N 124.718 0.109 1 117 2199 30 MET C C 175.900 0.000 1 118 2199 30 MET CA C 58.691 0.000 1 119 2199 30 MET CB C 31.839 0.000 1 120 2200 31 PHE H H 7.935 0.010 1 121 2200 31 PHE C C 175.055 0.000 1 122 2200 31 PHE CA C 58.733 0.027 1 123 2200 31 PHE CB C 40.423 0.000 1 124 2200 31 PHE N N 117.648 0.033 1 125 2201 32 ALA H H 7.962 0.013 1 126 2201 32 ALA C C 175.330 0.000 1 127 2201 32 ALA CA C 53.078 0.110 1 128 2201 32 ALA CB C 22.611 0.028 1 129 2201 32 ALA N N 123.419 0.050 1 130 2202 33 THR H H 7.978 0.012 1 131 2202 33 THR C C 173.887 0.000 1 132 2202 33 THR CA C 62.211 0.070 1 133 2202 33 THR CB C 71.397 0.098 1 134 2202 33 THR N N 116.570 0.117 1 135 2203 34 TRP H H 9.172 0.013 1 136 2203 34 TRP C C 175.895 0.000 1 137 2203 34 TRP CA C 55.861 0.109 1 138 2203 34 TRP CB C 27.200 0.028 1 139 2203 34 TRP N N 101.970 0.059 1 140 2204 35 SER H H 6.858 0.012 1 141 2204 35 SER CA C 57.571 0.028 1 142 2204 35 SER CB C 62.577 0.000 1 143 2204 35 SER N N 111.206 0.034 1 144 2205 36 PRO C C 176.068 0.000 1 145 2205 36 PRO CA C 66.167 0.149 1 146 2205 36 PRO CB C 31.671 0.068 1 147 2206 37 SER H H 7.158 0.011 1 148 2206 37 SER C C 174.164 0.000 1 149 2206 37 SER CA C 60.013 0.022 1 150 2206 37 SER CB C 62.774 0.091 1 151 2206 37 SER N N 104.894 0.076 1 152 2207 38 LYS H H 7.786 0.012 1 153 2207 38 LYS C C 176.980 0.000 1 154 2207 38 LYS CA C 55.400 0.125 1 155 2207 38 LYS CB C 31.732 0.000 1 156 2207 38 LYS N N 121.432 0.058 1 157 2208 39 ALA H H 7.609 0.014 1 158 2208 39 ALA C C 177.948 0.000 1 159 2208 39 ALA CA C 52.325 0.017 1 160 2208 39 ALA CB C 19.127 0.075 1 161 2208 39 ALA N N 123.890 0.191 1 162 2209 40 ARG H H 8.244 0.013 1 163 2209 40 ARG C C 175.218 0.000 1 164 2209 40 ARG CA C 56.242 0.151 1 165 2209 40 ARG CB C 33.296 0.189 1 166 2209 40 ARG N N 122.450 0.036 1 167 2210 41 LEU H H 7.211 0.015 1 168 2210 41 LEU C C 175.297 0.000 1 169 2210 41 LEU CA C 56.833 0.202 1 170 2210 41 LEU CB C 43.911 0.000 1 171 2210 41 LEU N N 126.227 0.122 1 172 2211 42 HIS H H 8.978 0.013 1 173 2211 42 HIS C C 175.550 0.000 1 174 2211 42 HIS CA C 59.420 0.040 1 175 2211 42 HIS CB C 28.551 0.046 1 176 2211 42 HIS N N 115.373 0.084 1 177 2212 43 LEU H H 8.173 0.012 1 178 2212 43 LEU C C 177.443 0.000 1 179 2212 43 LEU CA C 58.336 0.115 1 180 2212 43 LEU CB C 43.202 0.111 1 181 2212 43 LEU N N 126.739 0.038 1 182 2213 44 GLN H H 8.388 0.014 1 183 2213 44 GLN C C 175.724 0.000 1 184 2213 44 GLN CA C 54.852 0.098 1 185 2213 44 GLN CB C 31.610 0.000 1 186 2213 44 GLN N N 125.147 0.054 1 187 2214 45 GLY H H 8.263 0.012 1 188 2214 45 GLY CA C 45.033 0.011 1 189 2214 45 GLY N N 109.473 0.061 1 190 2215 46 ARG H H 8.308 0.000 1 191 2215 46 ARG C C 177.125 0.000 1 192 2215 46 ARG CA C 57.540 0.000 1 193 2215 46 ARG CB C 31.252 0.074 1 194 2215 46 ARG N N 122.526 0.000 1 195 2216 47 SER H H 8.178 0.014 1 196 2216 47 SER C C 173.817 0.000 1 197 2216 47 SER CA C 56.711 0.000 1 198 2216 47 SER CB C 61.784 0.106 1 199 2216 47 SER N N 116.842 0.072 1 200 2217 48 ASN H H 8.338 0.013 1 201 2217 48 ASN C C 170.935 0.000 1 202 2217 48 ASN CA C 54.116 0.000 1 203 2217 48 ASN CB C 35.858 0.000 1 204 2217 48 ASN N N 118.802 0.091 1 205 2218 49 ALA H H 7.496 0.014 1 206 2218 49 ALA C C 176.451 0.000 1 207 2218 49 ALA CA C 52.285 0.043 1 208 2218 49 ALA CB C 21.988 0.144 1 209 2218 49 ALA N N 115.369 0.050 1 210 2219 50 TRP H H 7.751 0.014 1 211 2219 50 TRP C C 176.539 0.000 1 212 2219 50 TRP CA C 57.779 0.122 1 213 2219 50 TRP CB C 30.842 0.158 1 214 2219 50 TRP N N 116.276 0.071 1 215 2220 51 ARG H H 7.209 0.011 1 216 2220 51 ARG CA C 52.886 0.122 1 217 2220 51 ARG CB C 34.612 0.000 1 218 2220 51 ARG N N 127.525 0.076 1 219 2221 52 PRO C C 175.272 0.000 1 220 2221 52 PRO CA C 61.959 0.000 1 221 2222 53 GLN H H 8.589 0.013 1 222 2222 53 GLN C C 174.848 0.000 1 223 2222 53 GLN CA C 59.488 0.055 1 224 2222 53 GLN CB C 29.238 0.098 1 225 2222 53 GLN N N 119.450 0.038 1 226 2223 54 VAL H H 6.553 0.010 1 227 2223 54 VAL C C 173.361 0.000 1 228 2223 54 VAL CA C 59.333 0.135 1 229 2223 54 VAL CB C 35.294 0.032 1 230 2223 54 VAL N N 110.425 0.102 1 231 2224 55 ASN H H 8.314 0.013 1 232 2224 55 ASN C C 172.433 0.000 1 233 2224 55 ASN CA C 53.088 0.021 1 234 2224 55 ASN CB C 38.732 0.155 1 235 2224 55 ASN N N 119.298 0.063 1 236 2225 56 ASN H H 6.613 0.011 1 237 2225 56 ASN CA C 52.877 0.077 1 238 2225 56 ASN CB C 40.478 0.000 1 239 2225 56 ASN N N 121.702 0.055 1 240 2226 57 PRO C C 176.356 0.000 1 241 2226 57 PRO CA C 64.779 0.027 1 242 2226 57 PRO CB C 32.634 0.179 1 243 2227 58 LYS H H 8.646 0.012 1 244 2227 58 LYS C C 176.942 0.000 1 245 2227 58 LYS CA C 57.198 0.000 1 246 2227 58 LYS CB C 32.261 0.000 1 247 2227 58 LYS N N 119.713 0.030 1 248 2228 59 GLU H H 7.606 0.013 1 249 2228 59 GLU C C 175.644 0.000 1 250 2228 59 GLU CA C 56.124 0.120 1 251 2228 59 GLU CB C 30.846 0.019 1 252 2228 59 GLU N N 121.944 0.065 1 253 2229 60 TRP H H 8.815 0.014 1 254 2229 60 TRP C C 172.447 0.000 1 255 2229 60 TRP CA C 55.980 0.065 1 256 2229 60 TRP CB C 32.169 0.121 1 257 2229 60 TRP N N 114.763 0.056 1 258 2230 61 LEU H H 7.517 0.010 1 259 2230 61 LEU C C 174.029 0.000 1 260 2230 61 LEU CA C 54.040 0.129 1 261 2230 61 LEU CB C 45.339 0.039 1 262 2230 61 LEU N N 121.457 0.130 1 263 2231 62 GLN H H 9.507 0.012 1 264 2231 62 GLN CA C 54.127 0.024 1 265 2231 62 GLN CB C 34.715 0.000 1 266 2231 62 GLN N N 128.162 0.062 1 267 2232 63 VAL C C 173.508 0.000 1 268 2232 63 VAL CA C 61.449 0.110 1 269 2232 63 VAL CB C 35.680 0.012 1 270 2233 64 ASP H H 8.109 0.013 1 271 2233 64 ASP C C 177.107 0.000 1 272 2233 64 ASP CA C 51.816 0.106 1 273 2233 64 ASP CB C 43.056 0.126 1 274 2233 64 ASP N N 124.587 0.070 1 275 2234 65 PHE H H 8.944 0.012 1 276 2234 65 PHE C C 176.746 0.000 1 277 2234 65 PHE CA C 61.000 0.000 1 278 2234 65 PHE CB C 40.355 0.071 1 279 2234 65 PHE N N 123.740 0.087 1 280 2235 66 GLN H H 8.808 0.014 1 281 2235 66 GLN C C 172.981 0.000 1 282 2235 66 GLN CA C 59.587 0.085 1 283 2235 66 GLN CB C 26.678 0.030 1 284 2235 66 GLN N N 111.474 0.102 1 285 2236 67 LYS H H 7.797 0.012 1 286 2236 67 LYS C C 173.848 0.000 1 287 2236 67 LYS CA C 54.981 0.064 1 288 2236 67 LYS CB C 34.159 0.070 1 289 2236 67 LYS N N 116.211 0.017 1 290 2237 68 THR H H 8.337 0.012 1 291 2237 68 THR C C 173.290 0.000 1 292 2237 68 THR CA C 65.381 0.074 1 293 2237 68 THR CB C 68.841 0.032 1 294 2237 68 THR N N 116.492 0.042 1 295 2238 69 MET H H 8.580 0.013 1 296 2238 69 MET CA C 52.855 0.062 1 297 2238 69 MET CB C 34.175 0.000 1 298 2238 69 MET N N 127.248 0.078 1 299 2239 70 LYS H H 8.358 0.000 1 300 2239 70 LYS C C 174.153 0.000 1 301 2239 70 LYS CA C 56.201 0.135 1 302 2239 70 LYS CB C 33.611 0.000 1 303 2239 70 LYS N N 122.526 0.000 1 304 2240 71 VAL H H 9.322 0.012 1 305 2240 71 VAL C C 175.903 0.000 1 306 2240 71 VAL CA C 63.016 0.141 1 307 2240 71 VAL CB C 33.719 0.081 1 308 2240 71 VAL N N 127.667 0.034 1 309 2241 72 THR H H 9.260 0.014 1 310 2241 72 THR C C 176.413 0.000 1 311 2241 72 THR CA C 61.178 0.129 1 312 2241 72 THR CB C 70.645 0.052 1 313 2241 72 THR N N 115.976 0.089 1 314 2242 73 GLY H H 8.159 0.014 1 315 2242 73 GLY C C 170.557 0.000 1 316 2242 73 GLY CA C 47.378 0.147 1 317 2242 73 GLY N N 112.592 0.052 1 318 2243 74 VAL H H 8.688 0.013 1 319 2243 74 VAL C C 172.887 0.000 1 320 2243 74 VAL CA C 61.070 0.173 1 321 2243 74 VAL CB C 36.720 0.072 1 322 2243 74 VAL N N 116.788 0.057 1 323 2244 75 THR H H 9.004 0.012 1 324 2244 75 THR C C 174.683 0.000 1 325 2244 75 THR CA C 61.225 0.080 1 326 2244 75 THR CB C 70.057 0.063 1 327 2244 75 THR N N 124.430 0.112 1 328 2245 76 THR H H 8.659 0.012 1 329 2245 76 THR C C 173.821 0.000 1 330 2245 76 THR CA C 60.695 0.203 1 331 2245 76 THR CB C 73.419 0.033 1 332 2245 76 THR N N 113.910 0.047 1 333 2246 77 GLN H H 8.979 0.014 1 334 2246 77 GLN C C 175.405 0.000 1 335 2246 77 GLN CA C 55.189 0.156 1 336 2246 77 GLN CB C 28.293 0.000 1 337 2246 77 GLN N N 126.548 0.089 1 338 2247 78 GLY H H 8.659 0.016 1 339 2247 78 GLY C C 172.470 0.000 1 340 2247 78 GLY CA C 44.909 0.122 1 341 2247 78 GLY N N 113.042 0.182 1 342 2248 79 VAL H H 9.226 0.017 1 343 2248 79 VAL C C 171.763 0.000 1 344 2248 79 VAL CA C 63.075 0.088 1 345 2248 79 VAL CB C 36.344 0.009 1 346 2248 79 VAL N N 120.600 0.029 1 347 2249 80 LYS H H 8.064 0.012 1 348 2249 80 LYS CA C 55.350 0.056 1 349 2249 80 LYS CB C 35.488 0.000 1 350 2249 80 LYS N N 126.366 0.058 1 351 2250 81 SER H H 9.235 0.000 1 352 2250 81 SER C C 174.337 0.000 1 353 2250 81 SER CA C 57.681 0.000 1 354 2250 81 SER CB C 65.237 0.000 1 355 2250 81 SER N N 128.269 0.000 1 356 2251 82 LEU H H 9.220 0.014 1 357 2251 82 LEU C C 171.237 0.000 1 358 2251 82 LEU CA C 57.643 0.088 1 359 2251 82 LEU CB C 42.323 0.000 1 360 2251 82 LEU N N 128.405 0.133 1 361 2252 83 LEU H H 8.756 0.008 1 362 2252 83 LEU C C 177.450 0.000 1 363 2252 83 LEU CA C 56.286 0.000 1 364 2252 83 LEU CB C 41.973 0.016 1 365 2252 83 LEU N N 118.603 0.067 1 366 2253 84 THR H H 8.137 0.011 1 367 2253 84 THR C C 176.076 0.000 1 368 2253 84 THR CA C 63.023 0.017 1 369 2253 84 THR CB C 70.682 0.000 1 370 2253 84 THR N N 118.176 0.028 1 371 2254 85 SER H H 8.404 0.020 1 372 2254 85 SER C C 173.026 0.000 1 373 2254 85 SER CA C 59.776 0.153 1 374 2254 85 SER CB C 64.938 0.051 1 375 2254 85 SER N N 122.037 0.042 1 376 2255 86 MET H H 8.818 0.013 1 377 2255 86 MET C C 173.997 0.000 1 378 2255 86 MET CA C 55.695 0.034 1 379 2255 86 MET CB C 36.070 0.015 1 380 2255 86 MET N N 124.193 0.043 1 381 2256 87 TYR H H 7.544 0.013 1 382 2256 87 TYR C C 172.942 0.000 1 383 2256 87 TYR CA C 57.211 0.162 1 384 2256 87 TYR CB C 39.204 0.178 1 385 2256 87 TYR N N 115.921 0.065 1 386 2257 88 VAL H H 9.990 0.013 1 387 2257 88 VAL C C 175.147 0.000 1 388 2257 88 VAL CA C 63.784 0.087 1 389 2257 88 VAL CB C 33.086 0.076 1 390 2257 88 VAL N N 121.909 0.040 1 391 2258 89 LYS H H 8.782 0.011 1 392 2258 89 LYS C C 177.804 0.000 1 393 2258 89 LYS CA C 58.521 0.098 1 394 2258 89 LYS CB C 34.964 0.113 1 395 2258 89 LYS N N 128.384 0.039 1 396 2259 90 GLU H H 7.616 0.010 1 397 2259 90 GLU C C 176.084 0.000 1 398 2259 90 GLU CA C 55.483 0.106 1 399 2259 90 GLU CB C 36.392 0.078 1 400 2259 90 GLU N N 118.314 0.049 1 401 2260 91 PHE H H 8.702 0.014 1 402 2260 91 PHE C C 173.944 0.000 1 403 2260 91 PHE CA C 57.218 0.008 1 404 2260 91 PHE CB C 42.338 0.000 1 405 2260 91 PHE N N 118.407 0.070 1 406 2261 92 LEU H H 8.441 0.013 1 407 2261 92 LEU C C 176.554 0.000 1 408 2261 92 LEU CA C 53.111 0.152 1 409 2261 92 LEU CB C 44.017 0.037 1 410 2261 92 LEU N N 122.783 0.037 1 411 2262 93 ILE H H 9.615 0.014 1 412 2262 93 ILE C C 175.108 0.000 1 413 2262 93 ILE CA C 59.814 0.120 1 414 2262 93 ILE CB C 41.800 0.100 1 415 2262 93 ILE N N 122.541 0.069 1 416 2263 94 SER H H 9.333 0.012 1 417 2263 94 SER C C 172.969 0.000 1 418 2263 94 SER CA C 58.594 0.129 1 419 2263 94 SER CB C 67.644 0.073 1 420 2263 94 SER N N 119.989 0.050 1 421 2264 95 SER H H 8.906 0.012 1 422 2264 95 SER C C 172.968 0.000 1 423 2264 95 SER CA C 57.903 0.116 1 424 2264 95 SER CB C 67.350 0.016 1 425 2264 95 SER N N 113.026 0.042 1 426 2265 96 SER H H 7.450 0.013 1 427 2265 96 SER C C 173.350 0.000 1 428 2265 96 SER CA C 57.849 0.045 1 429 2265 96 SER CB C 64.415 0.176 1 430 2265 96 SER N N 112.021 0.075 1 431 2266 97 GLN H H 9.001 0.022 1 432 2266 97 GLN C C 176.246 0.000 1 433 2266 97 GLN CA C 56.114 0.119 1 434 2266 97 GLN CB C 29.550 0.057 1 435 2266 97 GLN N N 124.161 0.138 1 436 2267 98 ASP H H 7.816 0.008 1 437 2267 98 ASP C C 176.566 0.000 1 438 2267 98 ASP CA C 53.546 0.000 1 439 2267 98 ASP CB C 42.751 0.097 1 440 2267 98 ASP N N 116.520 0.057 1 441 2268 99 GLY H H 7.892 0.014 1 442 2268 99 GLY CA C 45.311 0.064 1 443 2268 99 GLY N N 112.737 0.074 1 444 2269 100 HIS H H 8.184 0.001 1 445 2269 100 HIS C C 173.915 0.000 1 446 2269 100 HIS CA C 57.222 0.000 1 447 2269 100 HIS CB C 32.198 0.000 1 448 2269 100 HIS N N 119.636 0.044 1 449 2270 101 GLN H H 9.019 0.020 1 450 2270 101 GLN C C 175.949 0.000 1 451 2270 101 GLN CA C 55.746 0.148 1 452 2270 101 GLN CB C 30.084 0.000 1 453 2270 101 GLN N N 122.294 0.112 1 454 2271 102 TRP H H 9.103 0.013 1 455 2271 102 TRP C C 176.094 0.000 1 456 2271 102 TRP CA C 57.527 0.148 1 457 2271 102 TRP CB C 32.320 0.146 1 458 2271 102 TRP N N 131.208 0.027 1 459 2272 103 THR H H 9.235 0.003 1 460 2272 103 THR C C 175.382 0.000 1 461 2272 103 THR CA C 61.924 0.204 1 462 2272 103 THR CB C 71.589 0.077 1 463 2272 103 THR N N 119.821 0.128 1 464 2273 104 LEU H H 9.144 0.013 1 465 2273 104 LEU C C 175.824 0.000 1 466 2273 104 LEU CA C 56.301 0.079 1 467 2273 104 LEU CB C 44.299 0.033 1 468 2273 104 LEU N N 133.455 0.061 1 469 2274 105 PHE H H 9.174 0.012 1 470 2274 105 PHE C C 175.322 0.000 1 471 2274 105 PHE CA C 61.104 0.180 1 472 2274 105 PHE CB C 39.944 0.070 1 473 2274 105 PHE N N 123.747 0.056 1 474 2275 106 PHE H H 8.079 0.011 1 475 2275 106 PHE C C 174.848 0.000 1 476 2275 106 PHE CA C 56.543 0.090 1 477 2275 106 PHE CB C 42.910 0.023 1 478 2275 106 PHE N N 132.037 0.044 1 479 2276 107 GLN H H 8.860 0.013 1 480 2276 107 GLN C C 172.622 0.000 1 481 2276 107 GLN CA C 56.537 0.035 1 482 2276 107 GLN CB C 33.326 0.000 1 483 2276 107 GLN N N 117.981 0.060 1 484 2277 108 ASN H H 8.170 0.010 1 485 2277 108 ASN C C 175.412 0.000 1 486 2277 108 ASN CA C 55.406 0.013 1 487 2277 108 ASN CB C 37.615 0.050 1 488 2277 108 ASN N N 119.553 0.014 1 489 2278 109 GLY H H 8.771 0.014 1 490 2278 109 GLY C C 173.300 0.000 1 491 2278 109 GLY CA C 46.600 0.096 1 492 2278 109 GLY N N 103.672 0.058 1 493 2279 110 LYS H H 7.412 0.012 1 494 2279 110 LYS CA C 54.487 0.025 1 495 2279 110 LYS CB C 36.426 0.000 1 496 2279 110 LYS N N 119.739 0.036 1 497 2280 111 VAL C C 175.245 0.000 1 498 2280 111 VAL CA C 64.439 0.088 1 499 2280 111 VAL CB C 32.277 0.027 1 500 2281 112 LYS H H 8.348 0.013 1 501 2281 112 LYS C C 173.758 0.000 1 502 2281 112 LYS CA C 56.128 0.159 1 503 2281 112 LYS CB C 34.155 0.164 1 504 2281 112 LYS N N 130.442 0.055 1 505 2282 113 VAL H H 8.257 0.012 1 506 2282 113 VAL C C 176.308 0.000 1 507 2282 113 VAL CA C 62.342 0.161 1 508 2282 113 VAL CB C 31.186 0.100 1 509 2282 113 VAL N N 128.775 0.080 1 510 2283 114 PHE H H 8.892 0.012 1 511 2283 114 PHE C C 175.544 0.000 1 512 2283 114 PHE CA C 59.028 0.103 1 513 2283 114 PHE CB C 38.650 0.116 1 514 2283 114 PHE N N 129.526 0.041 1 515 2284 115 GLN H H 8.982 0.013 1 516 2284 115 GLN C C 175.524 0.000 1 517 2284 115 GLN CA C 56.114 0.123 1 518 2284 115 GLN CB C 29.026 0.084 1 519 2284 115 GLN N N 122.183 0.126 1 520 2285 116 GLY H H 8.646 0.012 1 521 2285 116 GLY C C 172.426 0.000 1 522 2285 116 GLY CA C 44.922 0.022 1 523 2285 116 GLY N N 115.131 0.075 1 524 2286 117 ASN H H 8.077 0.014 1 525 2286 117 ASN C C 172.530 0.000 1 526 2286 117 ASN CA C 57.346 0.130 1 527 2286 117 ASN CB C 43.189 0.168 1 528 2286 117 ASN N N 118.876 0.034 1 529 2287 118 GLN H H 8.525 0.009 1 530 2287 118 GLN C C 173.043 0.000 1 531 2287 118 GLN CA C 55.373 0.176 1 532 2287 118 GLN CB C 31.193 0.146 1 533 2287 118 GLN N N 115.032 0.073 1 534 2288 119 ASP H H 6.840 0.012 1 535 2288 119 ASP C C 175.711 0.000 1 536 2288 119 ASP CA C 53.395 0.149 1 537 2288 119 ASP CB C 41.512 0.121 1 538 2288 119 ASP N N 116.907 0.025 1 539 2289 120 SER H H 8.180 0.011 1 540 2289 120 SER C C 172.443 0.000 1 541 2289 120 SER CA C 60.219 0.098 1 542 2289 120 SER CB C 65.810 0.231 1 543 2289 120 SER N N 109.289 0.070 1 544 2290 121 PHE H H 7.143 0.008 1 545 2290 121 PHE C C 176.030 0.000 1 546 2290 121 PHE CA C 57.600 0.148 1 547 2290 121 PHE CB C 42.445 0.155 1 548 2290 121 PHE N N 116.595 0.087 1 549 2291 122 THR H H 9.757 0.012 1 550 2291 122 THR CA C 63.567 0.052 1 551 2291 122 THR CB C 68.781 0.000 1 552 2291 122 THR N N 130.204 0.053 1 553 2292 123 PRO C C 176.242 0.000 1 554 2292 123 PRO CB C 32.549 0.105 1 555 2293 124 VAL H H 8.594 0.012 1 556 2293 124 VAL C C 175.033 0.000 1 557 2293 124 VAL CA C 62.406 0.000 1 558 2293 124 VAL CB C 35.491 0.064 1 559 2293 124 VAL N N 125.357 0.138 1 560 2294 125 VAL H H 9.032 0.013 1 561 2294 125 VAL C C 175.929 0.000 1 562 2294 125 VAL CA C 62.560 0.178 1 563 2294 125 VAL CB C 33.316 0.075 1 564 2294 125 VAL N N 132.215 0.035 1 565 2295 126 ASN H H 9.564 0.012 1 566 2295 126 ASN C C 174.374 0.000 1 567 2295 126 ASN CA C 53.228 0.096 1 568 2295 126 ASN CB C 44.040 0.047 1 569 2295 126 ASN N N 129.231 0.067 1 570 2296 127 SER H H 8.821 0.012 1 571 2296 127 SER C C 173.820 0.000 1 572 2296 127 SER CA C 59.199 0.167 1 573 2296 127 SER CB C 64.973 0.246 1 574 2296 127 SER N N 119.642 0.070 1 575 2297 128 LEU H H 8.104 0.012 1 576 2297 128 LEU CA C 59.295 0.000 1 577 2297 128 LEU CB C 42.180 0.000 1 578 2297 128 LEU N N 127.203 0.175 1 579 2298 129 ASP H H 7.916 0.000 1 580 2298 129 ASP N N 123.326 0.000 1 581 2300 131 PRO C C 176.423 0.000 1 582 2300 131 PRO CA C 63.374 0.068 1 583 2300 131 PRO CB C 33.672 0.000 1 584 2301 132 LEU H H 8.349 0.014 1 585 2301 132 LEU C C 175.581 0.000 1 586 2301 132 LEU CA C 54.073 0.180 1 587 2301 132 LEU CB C 46.740 0.058 1 588 2301 132 LEU N N 122.070 0.055 1 589 2302 133 LEU H H 8.418 0.012 1 590 2302 133 LEU C C 176.610 0.000 1 591 2302 133 LEU CA C 54.020 0.110 1 592 2302 133 LEU CB C 41.581 0.041 1 593 2302 133 LEU N N 127.182 0.049 1 594 2303 134 THR H H 9.102 0.012 1 595 2303 134 THR C C 171.224 0.000 1 596 2303 134 THR CA C 61.364 0.125 1 597 2303 134 THR CB C 70.473 0.078 1 598 2303 134 THR N N 118.464 0.044 1 599 2304 135 ARG H H 7.524 0.011 1 600 2304 135 ARG C C 172.983 0.000 1 601 2304 135 ARG CA C 57.789 0.055 1 602 2304 135 ARG CB C 32.081 0.165 1 603 2304 135 ARG N N 127.683 0.118 1 604 2305 136 TYR H H 8.181 0.011 1 605 2305 136 TYR C C 176.593 0.000 1 606 2305 136 TYR CA C 56.443 0.106 1 607 2305 136 TYR CB C 43.712 0.090 1 608 2305 136 TYR N N 114.400 0.071 1 609 2306 137 LEU H H 8.933 0.010 1 610 2306 137 LEU C C 174.365 0.000 1 611 2306 137 LEU CA C 54.762 0.043 1 612 2306 137 LEU CB C 40.797 0.000 1 613 2306 137 LEU N N 125.193 0.102 1 614 2307 138 ARG H H 9.352 0.014 1 615 2307 138 ARG C C 174.319 0.000 1 616 2307 138 ARG CA C 55.338 0.176 1 617 2307 138 ARG CB C 35.551 0.050 1 618 2307 138 ARG N N 125.892 0.053 1 619 2308 139 ILE H H 8.657 0.011 1 620 2308 139 ILE CA C 57.080 0.000 1 621 2308 139 ILE CB C 40.744 0.000 1 622 2308 139 ILE N N 120.112 0.160 1 623 2310 141 PRO C C 174.883 0.000 1 624 2310 141 PRO CA C 64.466 0.113 1 625 2310 141 PRO CB C 33.149 0.000 1 626 2311 142 GLN H H 9.359 0.014 1 627 2311 142 GLN C C 174.875 0.000 1 628 2311 142 GLN CA C 56.614 0.062 1 629 2311 142 GLN CB C 32.635 0.051 1 630 2311 142 GLN N N 122.028 0.047 1 631 2312 143 SER H H 7.936 0.012 1 632 2312 143 SER C C 174.523 0.000 1 633 2312 143 SER CA C 58.341 0.083 1 634 2312 143 SER CB C 65.180 0.085 1 635 2312 143 SER N N 111.601 0.075 1 636 2313 144 TRP H H 8.052 0.012 1 637 2313 144 TRP CA C 57.293 0.095 1 638 2313 144 TRP CB C 31.143 0.000 1 639 2313 144 TRP N N 121.891 0.039 1 640 2314 145 VAL C C 175.788 0.000 1 641 2314 145 VAL CA C 63.371 0.144 1 642 2314 145 VAL CB C 32.161 0.080 1 643 2315 146 HIS H H 8.783 0.017 1 644 2315 146 HIS C C 175.193 0.000 1 645 2315 146 HIS CA C 62.761 0.199 1 646 2315 146 HIS CB C 28.251 0.196 1 647 2315 146 HIS N N 119.554 0.145 1 648 2316 147 GLN H H 9.251 0.019 1 649 2316 147 GLN C C 173.312 0.000 1 650 2316 147 GLN CA C 54.352 0.097 1 651 2316 147 GLN CB C 32.740 0.000 1 652 2316 147 GLN N N 119.855 0.088 1 653 2317 148 ILE H H 6.575 0.013 1 654 2317 148 ILE C C 173.499 0.000 1 655 2317 148 ILE CA C 63.654 0.064 1 656 2317 148 ILE CB C 37.240 0.039 1 657 2317 148 ILE N N 118.845 0.033 1 658 2318 149 ALA H H 5.928 0.012 1 659 2318 149 ALA C C 175.796 0.000 1 660 2318 149 ALA CA C 51.492 0.070 1 661 2318 149 ALA CB C 23.714 0.065 1 662 2318 149 ALA N N 126.921 0.038 1 663 2319 150 LEU H H 8.488 0.012 1 664 2319 150 LEU C C 174.818 0.000 1 665 2319 150 LEU CA C 54.954 0.107 1 666 2319 150 LEU CB C 50.456 0.132 1 667 2319 150 LEU N N 119.708 0.037 1 668 2320 151 ARG H H 8.563 0.012 1 669 2320 151 ARG C C 174.877 0.000 1 670 2320 151 ARG CA C 57.227 0.071 1 671 2320 151 ARG CB C 36.108 0.112 1 672 2320 151 ARG N N 122.970 0.078 1 673 2321 152 MET H H 7.727 0.013 1 674 2321 152 MET C C 173.910 0.000 1 675 2321 152 MET CA C 55.846 0.159 1 676 2321 152 MET CB C 38.471 0.185 1 677 2321 152 MET N N 118.491 0.154 1 678 2322 153 GLU H H 8.973 0.015 1 679 2322 153 GLU C C 173.307 0.000 1 680 2322 153 GLU CA C 54.995 0.210 1 681 2322 153 GLU CB C 27.868 0.000 1 682 2322 153 GLU N N 119.398 0.103 1 683 2323 154 VAL H H 9.237 0.012 1 684 2323 154 VAL C C 172.488 0.000 1 685 2323 154 VAL CA C 62.097 0.181 1 686 2323 154 VAL CB C 34.871 0.051 1 687 2323 154 VAL N N 126.528 0.025 1 688 2324 155 LEU H H 8.662 0.011 1 689 2324 155 LEU C C 176.964 0.000 1 690 2324 155 LEU CA C 52.821 0.130 1 691 2324 155 LEU CB C 44.441 0.186 1 692 2324 155 LEU N N 127.656 0.047 1 693 2325 156 GLY H H 8.893 0.014 1 694 2325 156 GLY C C 172.270 0.000 1 695 2325 156 GLY CA C 48.845 0.161 1 696 2325 156 GLY N N 109.227 0.094 1 697 2326 157 CYS H H 9.116 0.014 1 698 2326 157 CYS C C 172.433 0.000 1 699 2326 157 CYS CA C 56.874 0.117 1 700 2326 157 CYS CB C 41.731 0.185 1 701 2326 157 CYS N N 115.779 0.048 1 702 2327 158 GLU H H 8.378 0.012 1 703 2327 158 GLU C C 176.600 0.000 1 704 2327 158 GLU CA C 57.635 0.094 1 705 2327 158 GLU CB C 30.279 0.012 1 706 2327 158 GLU N N 119.596 0.092 1 707 2328 159 ALA H H 8.382 0.012 1 708 2328 159 ALA C C 176.890 0.000 1 709 2328 159 ALA CA C 53.183 0.052 1 710 2328 159 ALA CB C 20.086 0.188 1 711 2328 159 ALA N N 125.004 0.073 1 712 2329 160 GLN H H 7.985 0.011 1 713 2329 160 GLN C C 175.230 0.000 1 714 2329 160 GLN CA C 56.161 0.056 1 715 2329 160 GLN CB C 30.268 0.044 1 716 2329 160 GLN N N 119.019 0.061 1 717 2330 161 ASP H H 8.217 0.011 1 718 2330 161 ASP C C 175.619 0.000 1 719 2330 161 ASP CA C 55.124 0.175 1 720 2330 161 ASP CB C 41.444 0.009 1 721 2330 161 ASP N N 121.648 0.029 1 722 2331 162 LEU H H 7.966 0.012 1 723 2331 162 LEU C C 175.902 0.000 1 724 2331 162 LEU CA C 55.579 0.098 1 725 2331 162 LEU CB C 42.852 0.097 1 726 2331 162 LEU N N 122.451 0.090 1 727 2332 163 TYR H H 7.523 0.011 1 728 2332 163 TYR CA C 59.416 0.052 1 729 2332 163 TYR CB C 39.862 0.000 1 730 2332 163 TYR N N 125.606 0.022 1 stop_ save_