data_19261 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HIV capsid dimer structure ; _BMRB_accession_number 19261 _BMRB_flat_file_name bmr19261.str _Entry_type original _Submission_date 2013-05-23 _Accession_date 2013-05-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'HIV capsid dimer structure. This is equilibrium with a monomer (deposited separately) at NMR conditions.' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Deshmukh Lalit . . 2 Schwieters Charles D. . 3 Grishaev Alexander . . 4 Clore 'G. Marius' . . 5 Ghirlando Rodolfo . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 178 "13C chemical shifts" 563 "15N chemical shifts" 178 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-02-05 update BMRB 'update entry citation' 2013-12-09 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24066695 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Deshmukh Lalit . . 2 Schwieters Charles D. . 3 Grishaev Alexander . . 4 Ghirlando Rodolfo . . 5 Baber James L. . 6 Clore 'G. Marius' . . stop_ _Journal_abbreviation 'J. Am. Chem. Soc.' _Journal_name_full 'Journal of the American Chemical Society' _Journal_volume 135 _Journal_issue 43 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16133 _Page_last 16147 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HIV capsid dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'HIV capsid, 1' $HIVcapsid 'HIV capsid, 2' $HIVcapsid 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_HIVcapsid _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HIVcapsid _Molecular_mass 24654.443 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 231 _Mol_residue_sequence ; PIVQNLQGQMVHQAISPRTL NAWVKVVEEKAFSPEVIPMF SALSEGATPQDLNTMLNTVG GHQAAMQMLKETINEEAAEW DRLHPVHAGPIAPGQMREPR GSDIAGTTSTLQEQIGWMTH NPPIPVGEIYKRWIILGLNK IVRMYSPTSILDIRQGPKEP FRDYVDRFYKTLRAEQASQE VKNWMTETLLVQNANPDCKT ILKALGPGATLEEMMTACQG VGGPGHKARVL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 PRO 2 2 ILE 3 3 VAL 4 4 GLN 5 5 ASN 6 6 LEU 7 7 GLN 8 8 GLY 9 9 GLN 10 10 MET 11 11 VAL 12 12 HIS 13 13 GLN 14 14 ALA 15 15 ILE 16 16 SER 17 17 PRO 18 18 ARG 19 19 THR 20 20 LEU 21 21 ASN 22 22 ALA 23 23 TRP 24 24 VAL 25 25 LYS 26 26 VAL 27 27 VAL 28 28 GLU 29 29 GLU 30 30 LYS 31 31 ALA 32 32 PHE 33 33 SER 34 34 PRO 35 35 GLU 36 36 VAL 37 37 ILE 38 38 PRO 39 39 MET 40 40 PHE 41 41 SER 42 42 ALA 43 43 LEU 44 44 SER 45 45 GLU 46 46 GLY 47 47 ALA 48 48 THR 49 49 PRO 50 50 GLN 51 51 ASP 52 52 LEU 53 53 ASN 54 54 THR 55 55 MET 56 56 LEU 57 57 ASN 58 58 THR 59 59 VAL 60 60 GLY 61 61 GLY 62 62 HIS 63 63 GLN 64 64 ALA 65 65 ALA 66 66 MET 67 67 GLN 68 68 MET 69 69 LEU 70 70 LYS 71 71 GLU 72 72 THR 73 73 ILE 74 74 ASN 75 75 GLU 76 76 GLU 77 77 ALA 78 78 ALA 79 79 GLU 80 80 TRP 81 81 ASP 82 82 ARG 83 83 LEU 84 84 HIS 85 85 PRO 86 86 VAL 87 87 HIS 88 88 ALA 89 89 GLY 90 90 PRO 91 91 ILE 92 92 ALA 93 93 PRO 94 94 GLY 95 95 GLN 96 96 MET 97 97 ARG 98 98 GLU 99 99 PRO 100 100 ARG 101 101 GLY 102 102 SER 103 103 ASP 104 104 ILE 105 105 ALA 106 106 GLY 107 107 THR 108 108 THR 109 109 SER 110 110 THR 111 111 LEU 112 112 GLN 113 113 GLU 114 114 GLN 115 115 ILE 116 116 GLY 117 117 TRP 118 118 MET 119 119 THR 120 120 HIS 121 121 ASN 122 122 PRO 123 123 PRO 124 124 ILE 125 125 PRO 126 126 VAL 127 127 GLY 128 128 GLU 129 129 ILE 130 130 TYR 131 131 LYS 132 132 ARG 133 133 TRP 134 134 ILE 135 135 ILE 136 136 LEU 137 137 GLY 138 138 LEU 139 139 ASN 140 140 LYS 141 141 ILE 142 142 VAL 143 143 ARG 144 144 MET 145 145 TYR 146 146 SER 147 147 PRO 148 148 THR 149 149 SER 150 150 ILE 151 151 LEU 152 152 ASP 153 153 ILE 154 154 ARG 155 155 GLN 156 156 GLY 157 157 PRO 158 158 LYS 159 159 GLU 160 160 PRO 161 161 PHE 162 162 ARG 163 163 ASP 164 164 TYR 165 165 VAL 166 166 ASP 167 167 ARG 168 168 PHE 169 169 TYR 170 170 LYS 171 171 THR 172 172 LEU 173 173 ARG 174 174 ALA 175 175 GLU 176 176 GLN 177 177 ALA 178 178 SER 179 179 GLN 180 180 GLU 181 181 VAL 182 182 LYS 183 183 ASN 184 184 TRP 185 185 MET 186 186 THR 187 187 GLU 188 188 THR 189 189 LEU 190 190 LEU 191 191 VAL 192 192 GLN 193 193 ASN 194 194 ALA 195 195 ASN 196 196 PRO 197 197 ASP 198 198 CYS 199 199 LYS 200 200 THR 201 201 ILE 202 202 LEU 203 203 LYS 204 204 ALA 205 205 LEU 206 206 GLY 207 207 PRO 208 208 GLY 209 209 ALA 210 210 THR 211 211 LEU 212 212 GLU 213 213 GLU 214 214 MET 215 215 MET 216 216 THR 217 217 ALA 218 218 CYS 219 219 GLN 220 220 GLY 221 221 VAL 222 222 GLY 223 223 GLY 224 224 PRO 225 225 GLY 226 226 HIS 227 227 LYS 228 228 ALA 229 229 ARG 230 230 VAL 231 231 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-22 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 17738 HIV-1_CA 100.00 240 99.13 99.13 6.39e-167 BMRB 19264 entity 100.00 231 99.13 99.13 2.67e-167 BMRB 19575 HIV1_CA 100.00 231 100.00 100.00 1.27e-169 BMRB 25532 Gag 100.00 432 98.27 99.57 4.95e-166 PDB 1AFV "Hiv-1 Capsid Protein (P24) Complex With Fab25.3" 65.37 151 100.00 100.00 2.15e-104 PDB 1AK4 "Human Cyclophilin A Bound To The Amino-Terminal Domain Of Hiv-1 Capsid" 62.77 145 100.00 100.00 5.06e-100 PDB 1E6J "Crystal Structure Of Hiv-1 Capsid Protein (p24) In Complex With Fab13b5" 90.91 210 98.57 99.52 2.63e-151 PDB 1GWP "Structure Of The N-terminal Domain Of The Mature Hiv-1 Capsid Protein" 65.37 151 100.00 100.00 2.15e-104 PDB 1L6N "Structure Of The N-Terminal 283-Residue Fragment Of The Hiv- 1 Gag Polyprotein" 65.37 289 100.00 100.00 8.30e-104 PDB 1M9C "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type Complex." 63.20 146 100.00 100.00 8.46e-101 PDB 1M9E "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a Complex" 63.20 146 99.32 99.32 1.41e-99 PDB 1M9F "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m Complex" 63.20 146 98.63 98.63 1.36e-98 PDB 1M9X "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m,G89a Complex" 63.20 146 97.95 97.95 5.39e-98 PDB 1M9Y "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex" 63.20 146 98.63 98.63 7.57e-99 PDB 1VU4 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VU5 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VU6 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VU7 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VU8 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VU9 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUA "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUC "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUD "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUE "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUF "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUG "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUH "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUI "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUJ "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUK "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUL "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUM "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUN "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUO "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUP "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUQ "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUR "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUS "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUT "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUU "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUV "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUW "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUX "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUY "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VUZ "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV0 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV1 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV2 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV3 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV4 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV5 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV6 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV7 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV8 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VV9 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VVA "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VVB "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VVF "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VVG "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VVH "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 1VVI "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 99.13 99.13 4.90e-168 PDB 2GOL "Xray Structure Of Gag278" 63.20 146 100.00 100.00 8.46e-101 PDB 2JPR "Joint Refinement Of The Hiv-1 Ca-Ntd In Complex With The Assembly Inhibitor Cap-1" 62.34 145 100.00 100.00 7.90e-99 PDB 2LF4 "Structure Of A Monomeric Mutant Of The Hiv-1 Capsid Protein" 100.00 240 99.13 99.13 6.39e-167 PDB 2M8L "Hiv Capsid Dimer Structure" 95.67 221 100.00 100.00 9.71e-162 PDB 2M8N "Hiv-1 Capsid Monomer Structure" 95.67 221 100.00 100.00 9.71e-162 PDB 2M8P "The Structure Of The W184am185a Mutant Of The Hiv-1 Capsid Protein" 95.67 221 99.10 99.10 2.21e-159 PDB 2PWM "Crystal Structure Of Hiv-1 Ca146 A92e Real Cell" 63.20 146 99.32 99.32 6.30e-100 PDB 2PWO "Crystal Structure Of Hiv-1 Ca146 A92e Psuedo Cell" 63.20 146 99.32 99.32 6.30e-100 PDB 2PXR "Crystal Structure Of Hiv-1 Ca146 In The Presence Of Cap-1" 63.20 146 100.00 100.00 8.46e-101 PDB 2X2D "Acetyl-Cypa:hiv-1 N-Term Capsid Domain Complex" 63.20 147 100.00 100.00 9.97e-101 PDB 2X83 "Evolutionary Basis Of Hiv Restriction By The Antiretroviral Trimcyp" 63.20 146 100.00 100.00 8.46e-101 PDB 3DIK "Pseudo-Atomic Model Of The Hiv-1 Ca Hexameric Lattice" 94.81 219 100.00 100.00 2.93e-160 PDB 3GV2 "X-Ray Structure Of Hexameric Hiv-1 Ca" 96.54 342 99.10 99.10 5.90e-160 PDB 3H47 "X-Ray Structure Of Hexameric Hiv-1 Ca" 100.00 231 98.27 98.27 3.22e-165 PDB 3H4E "X-Ray Structure Of Hexameric Hiv-1 Ca" 100.00 231 98.27 98.27 3.22e-165 PDB 3J34 "Structure Of Hiv-1 Capsid Protein By Cryo-em" 100.00 231 99.13 99.13 4.90e-168 PDB 3J4F "Structure Of Hiv-1 Capsid Protein By Cryo-em" 100.00 231 99.13 99.13 4.90e-168 PDB 3MGE "X-Ray Structure Of Hexameric Hiv-1 Ca" 100.00 231 98.27 98.27 1.08e-165 PDB 3NTE "Crystal Structure Of The Wild-type Full-length Hiv-1 Capsid Protein" 95.67 221 98.19 99.55 3.03e-159 PDB 3P05 "X-Ray Structure Of Pentameric Hiv-1 Ca" 100.00 231 98.27 98.27 2.99e-165 PDB 3P0A "X-Ray Structure Of Pentameric Hiv-1 Ca" 100.00 231 97.84 97.84 6.97e-164 PDB 4ARG "Structure Of The Immature Retroviral Capsid At 8a Resolution By Cryo-Electron Microscopy" 55.84 129 100.00 100.00 6.06e-88 PDB 4B4N "Cpsf6 Defines A Conserved Capsid Interface That Modulates Hiv-1 Replication" 63.20 146 100.00 100.00 8.46e-101 PDB 4D1K "Cryo-electron Microscopy Of Tubular Arrays Of Hiv-1 Gag Resolves Structures Essential For Immature Virus Assembly" 94.81 219 99.54 99.54 8.61e-159 PDB 4E91 "Crystal Structure Of The N-terminal Domain Of Hiv-1 Capsid In Complex With Inhibitor Bd3" 63.20 146 100.00 100.00 8.46e-101 PDB 4E92 "Crystal Structure Of The N-terminal Domain Of Hiv-1 Capsid In Complex With Inhibitor Bm4" 63.20 146 100.00 100.00 8.46e-101 PDB 4INB "Crystal Structure Of The N-terminal Domain Of Hiv-1 Capsid In Complex With Benzodiazepine Inhibitor" 63.20 146 100.00 100.00 8.46e-101 PDB 4J93 "Crystal Structure Of The N-terminal Domain Of Hiv-1 Capsid In Complex With Inhibitor Bi-1" 63.20 146 100.00 100.00 8.46e-101 PDB 4LQW "Crystal Structure Of Hiv-1 Capsid N-terminal Domain In Complex With Nup358 Cyclophilin" 63.20 146 100.00 100.00 8.46e-101 PDB 4NX4 "Re-refinement Of Cap-1 Hiv-ca Complex" 63.20 146 100.00 100.00 8.46e-101 PDB 4QNB "Disulfide Stabilized Hiv-1 Ca Hexamer In Complex With Phenyl-l- Phenylalaninamide Inhibitor" 100.00 231 98.27 98.27 3.22e-165 PDB 4U0A "Hexameric Hiv-1 Ca In Complex With Cpsf6 Peptide, P6 Crystal Form" 100.00 231 98.27 98.27 3.22e-165 PDB 4U0B "Hexamer Hiv-1 Ca In Complex With Cpsf6 Peptide, P212121 Crystal Form" 100.00 231 98.27 98.27 3.22e-165 PDB 4U0C "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P6 Crystal Form" 100.00 231 98.27 98.27 3.22e-165 PDB 4U0D "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P212121 Crystal Form" 100.00 231 98.27 98.27 3.22e-165 PDB 4U0E "Hexameric Hiv-1 Ca In Complex With Pf3450074" 100.00 231 98.27 98.27 3.22e-165 PDB 4U0F "Hexameric Hiv-1 Ca In Complex With Bi-2" 100.00 231 98.27 98.27 3.22e-165 PDB 4USN "The Structure Of The Immature Hiv-1 Capsid In Intact Virus Particles At Sub-nm Resolution" 90.91 210 99.52 99.52 4.14e-152 PDB 4WYM "Structural Basis Of Hiv-1 Capsid Recognition By Cpsf6" 100.00 231 98.27 98.27 3.22e-165 PDB 4XFX "Structure Of The Native Full-length Hiv-1 Capsid Protein" 100.00 231 100.00 100.00 1.27e-169 PDB 4XFY "Structure Of The Native Full-length Dehydrated Hiv-1 Capsid Protein" 100.00 231 100.00 100.00 1.27e-169 PDB 4XFZ "Structure Of The Native Full-length Hiv-1 Capsid Protein In Complex With Pf-3450074 (pf74)" 100.00 231 100.00 100.00 1.27e-169 DBJ BAA00992 "gag polyprotein [Human immunodeficiency virus 1]" 100.00 500 99.13 99.57 2.36e-165 DBJ BAA12988 "Gag [Human immunodeficiency virus 1]" 100.00 512 98.27 99.57 5.70e-164 DBJ BAA12996 "Gag [Human immunodeficiency virus 1]" 100.00 512 98.27 99.57 6.86e-164 DBJ BAA93773 "gag protein [Human immunodeficiency virus 1]" 100.00 231 98.27 99.13 2.84e-166 DBJ BAA93774 "gag protein [Human immunodeficiency virus 1]" 100.00 231 96.97 97.84 3.30e-163 EMBL CAA06946 "gag polyprotein precursor [Human immunodeficiency virus 1]" 100.00 503 96.97 98.27 4.71e-161 EMBL CAA11884 "p24 [Human immunodeficiency virus 1]" 82.68 191 98.95 100.00 2.97e-137 EMBL CAA11886 "p24 [Human immunodeficiency virus 1]" 81.82 190 97.35 98.41 1.53e-133 EMBL CAA25902 "gag precursor polypeptide [Human immunodeficiency virus 1]" 78.79 316 98.35 100.00 8.85e-128 EMBL CAA65355 "p24 protein [Human immunodeficiency virus 1]" 91.77 212 98.11 99.06 1.30e-150 GB AAA44201 "gag polyprotein precursor [Human immunodeficiency virus 1]" 100.00 512 98.27 99.57 6.35e-164 GB AAA44225 "gag protein, partial [Human immunodeficiency virus 1]" 100.00 491 97.40 99.57 1.07e-163 GB AAA44306 "gag polyprotein [Human immunodeficiency virus 1]" 100.00 500 97.40 98.70 7.26e-163 GB AAA44652 "gag polyprotein precursor [Human immunodeficiency virus 1]" 100.00 512 98.27 99.57 7.24e-164 GB AAA44691 "gag protein, partial [Human immunodeficiency virus 1]" 100.00 490 96.97 98.70 1.18e-162 PIR FOVWLV "gag polyprotein - human immunodeficiency virus type 1 (isolate LAV-1a)" 100.00 500 98.27 99.57 2.06e-164 PRF 1102247B "protein gag" 100.00 512 98.27 99.57 6.35e-164 PRF 1103299C "gag gene" 100.00 478 98.27 99.57 3.67e-165 REF NP_057849 "Gag-Pol [Human immunodeficiency virus 1]" 100.00 1435 98.27 99.57 7.53e-154 REF NP_057850 "Pr55(Gag) [Human immunodeficiency virus 1]" 100.00 500 98.27 99.57 3.71e-164 REF NP_579880 "capsid [Human immunodeficiency virus 1]" 100.00 231 98.27 99.57 4.88e-167 SP P03347 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 100.00 512 98.27 99.57 6.35e-164 SP P03348 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 100.00 512 98.27 99.57 5.70e-164 SP P03349 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 100.00 502 98.27 99.57 4.19e-164 SP P03366 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 100.00 1447 98.27 99.57 7.41e-154 SP P03367 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 100.00 1447 98.27 99.57 7.49e-154 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HIVcapsid HIV 12721 Viruses . Lentivirus 'Human immunodeficiency virus' 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 $HIVcapsid 'recombinant technology' . Escherichia coli BL21 pET11a 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 $HIVcapsid 0.5 mM '[U-13C; U-15N; U-2H]' EDTA 1 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' H2O 95 % 'natural abundance' D2O 5 % '[U-100% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version 2.32 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_CCPN-Analysis _Saveframe_category software _Name CCPN-Analysis _Version 2.2.2 loop_ _Vendor _Address _Electronic_address '(CCPN-Analysis)-Vranken, Boucher, Stevens..Laue.' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _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_1 save_ save_2D_1H-13C_HSQC_aliphatic_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aromatic_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aromatic' _Sample_label $sample_1 save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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_HNCA_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_TROSY-Artsy_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TROSY-Artsy' _Sample_label $sample_1 save_ save_2D_1H-15N_R1_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N R1' _Sample_label $sample_1 save_ save_2D_1H-15N_R1_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N R1' _Sample_label $sample_1 save_ save_2D_1H-15N_R1r_13 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N R1r' _Sample_label $sample_1 save_ save_2D_1H-15N_R1r_14 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N R1r' _Sample_label $sample_1 save_ save_2D_1H-15N_HetNOE_15 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HetNOE' _Sample_label $sample_1 save_ save_2D_1H-15N_HetNOE_16 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HetNOE' _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 pH 6.5 . pH pressure 1 . atm temperature 308 . 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 water C 13 protons ppm 4.7 internal indirect . . . 1 water H 1 protons ppm 4.7 internal direct . . . 1 water N 15 protons ppm 4.7 internal indirect . . . 1 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 HNCO' '3D HNCACB' '3D HNCA' '3D HN(CO)CA' 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 'HIV capsid, 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 1 1 PRO C C 171.899 0.200 . 2 1 1 PRO CA C 61.047 0.200 . 3 1 1 PRO CB C 33.066 0.200 . 4 2 2 ILE H H 8.833 0.020 . 5 2 2 ILE C C 175.076 0.200 . 6 2 2 ILE CA C 60.065 0.002 . 7 2 2 ILE CB C 36.922 0.008 . 8 2 2 ILE N N 121.797 0.200 . 9 3 3 VAL H H 8.866 0.020 . 10 3 3 VAL C C 173.600 0.200 . 11 3 3 VAL CA C 58.889 0.003 . 12 3 3 VAL CB C 34.329 0.200 . 13 3 3 VAL N N 123.386 0.200 . 14 4 4 GLN H H 8.295 0.020 . 15 4 4 GLN C C 176.878 0.200 . 16 4 4 GLN CA C 54.598 0.003 . 17 4 4 GLN CB C 29.830 0.009 . 18 4 4 GLN N N 122.509 0.200 . 19 5 5 ASN H H 8.826 0.020 . 20 5 5 ASN C C 177.265 0.200 . 21 5 5 ASN CA C 50.735 0.006 . 22 5 5 ASN CB C 38.044 0.003 . 23 5 5 ASN N N 124.919 0.200 . 24 6 6 LEU H H 8.122 0.020 . 25 6 6 LEU C C 178.117 0.200 . 26 6 6 LEU CA C 57.091 0.007 . 27 6 6 LEU CB C 40.486 0.011 . 28 6 6 LEU N N 119.054 0.200 . 29 7 7 GLN H H 7.508 0.020 . 30 7 7 GLN C C 176.219 0.200 . 31 7 7 GLN CA C 55.744 0.033 . 32 7 7 GLN CB C 27.704 0.004 . 33 7 7 GLN N N 116.418 0.200 . 34 8 8 GLY H H 8.030 0.020 . 35 8 8 GLY C C 174.173 0.200 . 36 8 8 GLY CA C 44.989 0.041 . 37 8 8 GLY N N 108.195 0.200 . 38 9 9 GLN H H 7.856 0.020 . 39 9 9 GLN C C 175.131 0.200 . 40 9 9 GLN CA C 53.889 0.018 . 41 9 9 GLN CB C 28.735 0.001 . 42 9 9 GLN N N 120.479 0.200 . 43 10 10 MET H H 8.403 0.020 . 44 10 10 MET C C 175.928 0.200 . 45 10 10 MET CA C 53.759 0.006 . 46 10 10 MET CB C 30.347 0.002 . 47 10 10 MET N N 121.290 0.001 . 48 11 11 VAL H H 9.036 0.020 . 49 11 11 VAL C C 174.208 0.200 . 50 11 11 VAL CA C 59.235 0.048 . 51 11 11 VAL CB C 34.606 0.004 . 52 11 11 VAL N N 120.364 0.200 . 53 12 12 HIS H H 8.642 0.020 . 54 12 12 HIS CA C 56.827 0.001 . 55 12 12 HIS CB C 31.713 0.200 . 56 12 12 HIS N N 121.877 0.200 . 57 13 13 GLN H H 7.905 0.020 . 58 13 13 GLN C C 173.703 0.200 . 59 13 13 GLN CA C 53.626 0.001 . 60 13 13 GLN CB C 31.524 0.030 . 61 13 13 GLN N N 126.102 0.200 . 62 14 14 ALA H H 8.248 0.020 . 63 14 14 ALA C C 178.115 0.200 . 64 14 14 ALA CA C 51.739 0.004 . 65 14 14 ALA CB C 18.009 0.004 . 66 14 14 ALA N N 125.798 0.200 . 67 15 15 ILE H H 8.207 0.020 . 68 15 15 ILE C C 174.670 0.200 . 69 15 15 ILE CA C 61.604 0.001 . 70 15 15 ILE CB C 37.613 0.057 . 71 15 15 ILE N N 121.853 0.200 . 72 16 16 SER H H 8.391 0.020 . 73 16 16 SER C C 174.298 0.200 . 74 16 16 SER CA C 55.823 0.047 . 75 16 16 SER CB C 63.057 0.200 . 76 16 16 SER N N 123.681 0.200 . 77 17 17 PRO C C 178.827 0.200 . 78 17 17 PRO CA C 65.038 0.200 . 79 17 17 PRO CB C 31.142 0.200 . 80 18 18 ARG H H 7.914 0.020 . 81 18 18 ARG C C 179.351 0.200 . 82 18 18 ARG CA C 58.853 0.041 . 83 18 18 ARG CB C 28.926 0.001 . 84 18 18 ARG N N 116.467 0.200 . 85 19 19 THR H H 7.620 0.020 . 86 19 19 THR C C 175.796 0.200 . 87 19 19 THR CA C 65.919 0.002 . 88 19 19 THR CB C 67.762 0.014 . 89 19 19 THR N N 119.838 0.001 . 90 20 20 LEU H H 7.963 0.020 . 91 20 20 LEU C C 178.591 0.200 . 92 20 20 LEU CA C 57.802 0.017 . 93 20 20 LEU CB C 40.426 0.005 . 94 20 20 LEU N N 121.383 0.200 . 95 21 21 ASN H H 8.518 0.020 . 96 21 21 ASN C C 177.526 0.200 . 97 21 21 ASN CA C 55.679 0.022 . 98 21 21 ASN CB C 37.657 0.200 . 99 21 21 ASN N N 116.284 0.200 . 100 22 22 ALA H H 7.686 0.020 . 101 22 22 ALA CA C 54.486 0.013 . 102 22 22 ALA CB C 17.409 0.200 . 103 22 22 ALA N N 122.464 0.001 . 104 23 23 TRP C C 175.906 0.200 . 105 23 23 TRP CA C 58.118 0.200 . 106 24 24 VAL H H 8.211 0.020 . 107 24 24 VAL C C 178.306 0.200 . 108 24 24 VAL CA C 66.121 0.034 . 109 24 24 VAL CB C 30.675 0.200 . 110 24 24 VAL N N 118.364 0.200 . 111 25 25 LYS H H 7.664 0.020 . 112 25 25 LYS C C 178.704 0.200 . 113 25 25 LYS CA C 58.386 0.200 . 114 25 25 LYS CB C 30.792 0.200 . 115 25 25 LYS N N 118.058 0.200 . 116 26 26 VAL C C 177.469 0.200 . 117 26 26 VAL CA C 65.601 0.200 . 118 27 27 VAL H H 7.267 0.020 . 119 27 27 VAL C C 179.017 0.200 . 120 27 27 VAL CA C 65.332 0.018 . 121 27 27 VAL N N 120.450 0.001 . 122 28 28 GLU H H 8.152 0.020 . 123 28 28 GLU C C 178.548 0.200 . 124 28 28 GLU CA C 58.829 0.026 . 125 28 28 GLU CB C 28.996 0.022 . 126 28 28 GLU N N 120.013 0.001 . 127 29 29 GLU H H 8.016 0.020 . 128 29 29 GLU C C 178.425 0.200 . 129 29 29 GLU CA C 58.074 0.008 . 130 29 29 GLU CB C 29.963 0.200 . 131 29 29 GLU N N 116.341 0.001 . 132 30 30 LYS H H 8.305 0.020 . 133 30 30 LYS C C 176.723 0.200 . 134 30 30 LYS CA C 54.979 0.003 . 135 30 30 LYS CB C 31.428 0.044 . 136 30 30 LYS N N 115.917 0.200 . 137 31 31 ALA H H 7.776 0.020 . 138 31 31 ALA C C 174.002 0.200 . 139 31 31 ALA CA C 52.659 0.006 . 140 31 31 ALA CB C 16.561 0.036 . 141 31 31 ALA N N 123.568 0.200 . 142 32 32 PHE H H 7.165 0.020 . 143 32 32 PHE C C 174.655 0.200 . 144 32 32 PHE CA C 57.609 0.022 . 145 32 32 PHE CB C 36.684 0.016 . 146 32 32 PHE N N 113.734 0.001 . 147 33 33 SER H H 7.103 0.020 . 148 33 33 SER C C 173.330 0.200 . 149 33 33 SER CA C 56.575 0.200 . 150 33 33 SER CB C 62.710 0.200 . 151 33 33 SER N N 114.771 0.200 . 152 34 34 PRO C C 178.587 0.200 . 153 34 34 PRO CA C 65.758 0.200 . 154 34 34 PRO CB C 30.853 0.200 . 155 35 35 GLU H H 8.524 0.020 . 156 35 35 GLU C C 177.344 0.200 . 157 35 35 GLU CA C 58.325 0.029 . 158 35 35 GLU CB C 28.896 0.200 . 159 35 35 GLU N N 116.146 0.001 . 160 36 36 VAL H H 8.182 0.020 . 161 36 36 VAL C C 176.812 0.200 . 162 36 36 VAL CA C 64.662 0.001 . 163 36 36 VAL CB C 30.815 0.031 . 164 36 36 VAL N N 117.234 0.001 . 165 37 37 ILE H H 7.438 0.020 . 166 37 37 ILE C C 175.364 0.200 . 167 37 37 ILE CA C 67.294 0.200 . 168 37 37 ILE CB C 34.073 0.200 . 169 37 37 ILE N N 119.576 0.001 . 170 38 38 PRO C C 180.208 0.200 . 171 38 38 PRO CA C 64.949 0.200 . 172 38 38 PRO CB C 29.647 0.200 . 173 39 39 MET H H 7.018 0.020 . 174 39 39 MET C C 177.328 0.200 . 175 39 39 MET CA C 57.774 0.013 . 176 39 39 MET CB C 31.107 0.200 . 177 39 39 MET N N 116.366 0.200 . 178 40 40 PHE H H 8.748 0.020 . 179 40 40 PHE C C 178.739 0.200 . 180 40 40 PHE CA C 61.458 0.083 . 181 40 40 PHE CB C 37.615 0.010 . 182 40 40 PHE N N 120.980 0.200 . 183 41 41 SER H H 8.327 0.020 . 184 41 41 SER C C 175.784 0.200 . 185 41 41 SER CA C 61.979 0.031 . 186 41 41 SER N N 114.837 0.200 . 187 42 42 ALA H H 7.703 0.020 . 188 42 42 ALA C C 180.423 0.200 . 189 42 42 ALA CA C 54.191 0.200 . 190 42 42 ALA CB C 17.418 0.200 . 191 42 42 ALA N N 122.409 0.001 . 192 43 43 LEU C C 176.663 0.200 . 193 43 43 LEU CA C 55.701 0.200 . 194 44 44 SER H H 7.083 0.020 . 195 44 44 SER C C 174.789 0.200 . 196 44 44 SER CA C 57.060 0.004 . 197 44 44 SER CB C 62.801 0.023 . 198 44 44 SER N N 109.630 0.001 . 199 45 45 GLU H H 7.005 0.020 . 200 45 45 GLU C C 178.209 0.200 . 201 45 45 GLU CA C 57.828 0.005 . 202 45 45 GLU CB C 28.286 0.015 . 203 45 45 GLU N N 125.573 0.200 . 204 46 46 GLY H H 9.218 0.020 . 205 46 46 GLY C C 174.335 0.200 . 206 46 46 GLY CA C 45.438 0.027 . 207 46 46 GLY N N 115.883 0.200 . 208 47 47 ALA H H 7.425 0.020 . 209 47 47 ALA C C 178.457 0.200 . 210 47 47 ALA CA C 52.699 0.003 . 211 47 47 ALA CB C 19.300 0.006 . 212 47 47 ALA N N 120.289 0.200 . 213 48 48 THR H H 8.714 0.020 . 214 48 48 THR C C 174.625 0.200 . 215 48 48 THR CA C 59.497 0.200 . 216 48 48 THR CB C 68.913 0.200 . 217 48 48 THR N N 109.456 0.200 . 218 49 49 PRO C C 176.943 0.200 . 219 49 49 PRO CA C 66.751 0.200 . 220 49 49 PRO CB C 29.736 0.200 . 221 50 50 GLN H H 8.343 0.020 . 222 50 50 GLN C C 178.919 0.200 . 223 50 50 GLN CA C 59.693 0.035 . 224 50 50 GLN CB C 28.084 0.045 . 225 50 50 GLN N N 116.430 0.200 . 226 51 51 ASP H H 7.911 0.020 . 227 51 51 ASP C C 178.224 0.200 . 228 51 51 ASP CA C 57.243 0.054 . 229 51 51 ASP CB C 40.659 0.006 . 230 51 51 ASP N N 120.777 0.200 . 231 52 52 LEU H H 8.047 0.020 . 232 52 52 LEU C C 178.982 0.200 . 233 52 52 LEU CA C 57.719 0.035 . 234 52 52 LEU CB C 39.370 0.002 . 235 52 52 LEU N N 120.348 0.001 . 236 53 53 ASN H H 8.598 0.020 . 237 53 53 ASN C C 178.149 0.200 . 238 53 53 ASN CA C 56.040 0.010 . 239 53 53 ASN CB C 36.716 0.028 . 240 53 53 ASN N N 118.184 0.001 . 241 54 54 THR H H 8.376 0.020 . 242 54 54 THR C C 177.093 0.200 . 243 54 54 THR CA C 66.747 0.033 . 244 54 54 THR CB C 67.605 0.001 . 245 54 54 THR N N 120.221 0.200 . 246 55 55 MET H H 7.899 0.020 . 247 55 55 MET C C 179.471 0.200 . 248 55 55 MET CA C 59.922 0.027 . 249 55 55 MET CB C 32.091 0.007 . 250 55 55 MET N N 120.351 0.001 . 251 56 56 LEU H H 8.531 0.020 . 252 56 56 LEU C C 178.977 0.200 . 253 56 56 LEU CA C 57.792 0.007 . 254 56 56 LEU CB C 40.223 0.004 . 255 56 56 LEU N N 121.056 0.200 . 256 57 57 ASN H H 8.376 0.020 . 257 57 57 ASN C C 177.102 0.200 . 258 57 57 ASN CA C 54.773 0.012 . 259 57 57 ASN CB C 37.592 0.014 . 260 57 57 ASN N N 116.462 0.200 . 261 58 58 THR H H 7.485 0.020 . 262 58 58 THR C C 174.958 0.200 . 263 58 58 THR CA C 63.640 0.013 . 264 58 58 THR CB C 69.069 0.013 . 265 58 58 THR N N 111.759 0.200 . 266 59 59 VAL H H 7.304 0.020 . 267 59 59 VAL C C 175.994 0.200 . 268 59 59 VAL CA C 62.564 0.055 . 269 59 59 VAL CB C 30.523 0.067 . 270 59 59 VAL N N 120.111 0.200 . 271 60 60 GLY H H 8.192 0.020 . 272 60 60 GLY C C 174.472 0.200 . 273 60 60 GLY CA C 44.892 0.028 . 274 60 60 GLY N N 113.268 0.200 . 275 61 61 GLY H H 8.208 0.020 . 276 61 61 GLY C C 173.931 0.200 . 277 61 61 GLY CA C 44.891 0.043 . 278 61 61 GLY N N 108.982 0.200 . 279 62 62 HIS H H 8.250 0.020 . 280 62 62 HIS CA C 55.375 0.004 . 281 62 62 HIS CB C 28.338 0.003 . 282 62 62 HIS N N 119.366 0.200 . 283 63 63 GLN H H 8.314 0.020 . 284 63 63 GLN C C 178.616 0.200 . 285 63 63 GLN CA C 60.120 0.018 . 286 63 63 GLN CB C 27.520 0.200 . 287 63 63 GLN N N 120.109 0.200 . 288 64 64 ALA H H 8.641 0.020 . 289 64 64 ALA C C 180.645 0.200 . 290 64 64 ALA CA C 54.781 0.039 . 291 64 64 ALA CB C 16.830 0.200 . 292 64 64 ALA N N 122.074 0.001 . 293 65 65 ALA H H 7.947 0.020 . 294 65 65 ALA C C 179.165 0.200 . 295 65 65 ALA CA C 54.300 0.022 . 296 65 65 ALA CB C 17.403 0.024 . 297 65 65 ALA N N 122.037 0.200 . 298 66 66 MET H H 8.328 0.020 . 299 66 66 MET C C 179.427 0.200 . 300 66 66 MET CA C 56.210 0.200 . 301 66 66 MET CB C 29.680 0.025 . 302 66 66 MET N N 115.905 0.200 . 303 67 67 GLN H H 8.177 0.020 . 304 67 67 GLN C C 178.381 0.200 . 305 67 67 GLN CA C 58.494 0.042 . 306 67 67 GLN CB C 26.902 0.007 . 307 67 67 GLN N N 120.620 0.200 . 308 68 68 MET H H 7.565 0.020 . 309 68 68 MET C C 179.669 0.200 . 310 68 68 MET CA C 58.422 0.053 . 311 68 68 MET CB C 31.717 0.011 . 312 68 68 MET N N 119.708 0.200 . 313 69 69 LEU H H 8.292 0.020 . 314 69 69 LEU C C 178.454 0.200 . 315 69 69 LEU CA C 58.509 0.054 . 316 69 69 LEU CB C 40.712 0.200 . 317 69 69 LEU N N 123.233 0.200 . 318 70 70 LYS H H 8.309 0.020 . 319 70 70 LYS C C 178.891 0.200 . 320 70 70 LYS CA C 59.369 0.052 . 321 70 70 LYS CB C 30.800 0.007 . 322 70 70 LYS N N 119.545 0.200 . 323 71 71 GLU H H 8.167 0.020 . 324 71 71 GLU C C 179.463 0.200 . 325 71 71 GLU CA C 59.085 0.006 . 326 71 71 GLU CB C 28.395 0.200 . 327 71 71 GLU N N 119.052 0.001 . 328 72 72 THR H H 7.798 0.020 . 329 72 72 THR C C 175.916 0.200 . 330 72 72 THR CA C 66.929 0.002 . 331 72 72 THR CB C 68.245 0.014 . 332 72 72 THR N N 117.959 0.200 . 333 73 73 ILE H H 8.264 0.020 . 334 73 73 ILE C C 176.862 0.200 . 335 73 73 ILE CA C 65.578 0.006 . 336 73 73 ILE CB C 37.005 0.015 . 337 73 73 ILE N N 122.304 0.200 . 338 74 74 ASN H H 8.168 0.020 . 339 74 74 ASN C C 178.642 0.200 . 340 74 74 ASN CA C 55.608 0.057 . 341 74 74 ASN CB C 36.993 0.003 . 342 74 74 ASN N N 116.969 0.200 . 343 75 75 GLU H H 7.917 0.020 . 344 75 75 GLU C C 179.549 0.200 . 345 75 75 GLU CA C 58.922 0.011 . 346 75 75 GLU CB C 28.408 0.059 . 347 75 75 GLU N N 122.119 0.200 . 348 76 76 GLU H H 8.093 0.020 . 349 76 76 GLU C C 179.419 0.200 . 350 76 76 GLU CA C 57.666 0.013 . 351 76 76 GLU CB C 26.090 0.028 . 352 76 76 GLU N N 120.864 0.200 . 353 77 77 ALA H H 8.252 0.020 . 354 77 77 ALA C C 178.886 0.200 . 355 77 77 ALA CA C 54.409 0.013 . 356 77 77 ALA CB C 16.646 0.200 . 357 77 77 ALA N N 124.313 0.200 . 358 78 78 ALA H H 7.448 0.020 . 359 78 78 ALA C C 181.363 0.200 . 360 78 78 ALA CA C 54.216 0.024 . 361 78 78 ALA CB C 16.780 0.001 . 362 78 78 ALA N N 119.677 0.001 . 363 79 79 GLU H H 7.703 0.020 . 364 79 79 GLU C C 178.435 0.200 . 365 79 79 GLU CA C 58.108 0.012 . 366 79 79 GLU CB C 28.086 0.200 . 367 79 79 GLU N N 121.439 0.200 . 368 80 80 TRP H H 8.403 0.020 . 369 80 80 TRP C C 179.638 0.200 . 370 80 80 TRP CA C 61.332 0.031 . 371 80 80 TRP CB C 28.839 0.200 . 372 80 80 TRP N N 121.542 0.001 . 373 81 81 ASP H H 8.160 0.020 . 374 81 81 ASP C C 178.560 0.200 . 375 81 81 ASP CA C 57.136 0.007 . 376 81 81 ASP CB C 38.998 0.010 . 377 81 81 ASP N N 120.032 0.200 . 378 82 82 ARG H H 7.773 0.020 . 379 82 82 ARG C C 178.218 0.200 . 380 82 82 ARG CA C 58.773 0.010 . 381 82 82 ARG CB C 29.634 0.013 . 382 82 82 ARG N N 121.010 0.200 . 383 83 83 LEU H H 7.524 0.020 . 384 83 83 LEU C C 176.303 0.200 . 385 83 83 LEU CA C 54.728 0.013 . 386 83 83 LEU CB C 41.595 0.003 . 387 83 83 LEU N N 117.073 0.200 . 388 84 84 HIS H H 7.605 0.020 . 389 84 84 HIS CA C 52.667 0.200 . 390 84 84 HIS CB C 26.492 0.200 . 391 84 84 HIS N N 117.332 0.200 . 392 85 85 PRO C C 177.121 0.200 . 393 85 85 PRO CA C 62.693 0.200 . 394 85 85 PRO CB C 30.970 0.200 . 395 86 86 VAL H H 8.128 0.020 . 396 86 86 VAL C C 176.285 0.200 . 397 86 86 VAL CA C 61.702 0.003 . 398 86 86 VAL CB C 31.980 0.024 . 399 86 86 VAL N N 121.026 0.200 . 400 87 87 HIS H H 8.764 0.020 . 401 87 87 HIS CA C 55.413 0.011 . 402 87 87 HIS CB C 29.192 0.033 . 403 87 87 HIS N N 125.331 0.200 . 404 88 88 ALA H H 8.390 0.020 . 405 88 88 ALA C C 177.486 0.200 . 406 88 88 ALA CA C 51.838 0.001 . 407 88 88 ALA CB C 18.382 0.010 . 408 88 88 ALA N N 127.669 0.200 . 409 89 89 GLY H H 7.941 0.020 . 410 89 89 GLY C C 171.236 0.200 . 411 89 89 GLY CA C 43.948 0.046 . 412 89 89 GLY N N 109.329 0.200 . 413 90 90 PRO C C 176.958 0.200 . 414 90 90 PRO CA C 62.511 0.200 . 415 90 90 PRO CB C 31.228 0.200 . 416 91 91 ILE H H 8.241 0.020 . 417 91 91 ILE C C 175.783 0.200 . 418 91 91 ILE CA C 59.715 0.027 . 419 91 91 ILE CB C 37.690 0.001 . 420 91 91 ILE N N 122.182 0.200 . 421 92 92 ALA H H 8.263 0.020 . 422 92 92 ALA C C 175.049 0.200 . 423 92 92 ALA CA C 50.053 0.034 . 424 92 92 ALA CB C 17.025 0.200 . 425 92 92 ALA N N 130.752 0.200 . 426 93 93 PRO C C 178.175 0.200 . 427 93 93 PRO CA C 63.531 0.200 . 428 93 93 PRO CB C 30.598 0.200 . 429 94 94 GLY H H 8.613 0.020 . 430 94 94 GLY C C 174.269 0.200 . 431 94 94 GLY CA C 44.950 0.043 . 432 94 94 GLY N N 112.274 0.200 . 433 95 95 GLN H H 7.788 0.020 . 434 95 95 GLN C C 175.195 0.200 . 435 95 95 GLN CA C 54.181 0.052 . 436 95 95 GLN CB C 28.964 0.200 . 437 95 95 GLN N N 120.049 0.200 . 438 96 96 MET H H 8.414 0.020 . 439 96 96 MET C C 176.075 0.200 . 440 96 96 MET CA C 54.302 0.200 . 441 96 96 MET CB C 33.487 0.022 . 442 96 96 MET N N 121.542 0.200 . 443 97 97 ARG H H 8.668 0.020 . 444 97 97 ARG C C 174.886 0.200 . 445 97 97 ARG CA C 54.851 0.010 . 446 97 97 ARG CB C 29.102 0.200 . 447 97 97 ARG N N 123.895 0.001 . 448 98 98 GLU H H 8.640 0.020 . 449 98 98 GLU C C 174.698 0.200 . 450 98 98 GLU CA C 53.934 0.200 . 451 98 98 GLU CB C 28.870 0.200 . 452 98 98 GLU N N 123.454 0.200 . 453 99 99 PRO C C 177.310 0.200 . 454 99 99 PRO CA C 62.255 0.200 . 455 100 100 ARG H H 9.705 0.020 . 456 100 100 ARG C C 178.541 0.200 . 457 100 100 ARG CA C 52.791 0.001 . 458 100 100 ARG CB C 29.651 0.200 . 459 100 100 ARG N N 122.249 0.200 . 460 101 101 GLY H H 11.576 0.020 . 461 101 101 GLY C C 176.082 0.200 . 462 101 101 GLY CA C 47.978 0.002 . 463 101 101 GLY N N 117.171 0.200 . 464 102 102 SER H H 9.200 0.020 . 465 102 102 SER C C 176.928 0.200 . 466 102 102 SER CA C 60.505 0.054 . 467 102 102 SER CB C 61.273 0.051 . 468 102 102 SER N N 115.107 0.200 . 469 103 103 ASP H H 7.313 0.020 . 470 103 103 ASP C C 179.792 0.200 . 471 103 103 ASP CA C 56.436 0.014 . 472 103 103 ASP CB C 40.660 0.006 . 473 103 103 ASP N N 123.327 0.200 . 474 104 104 ILE H H 7.376 0.020 . 475 104 104 ILE C C 172.708 0.200 . 476 104 104 ILE CA C 65.268 0.020 . 477 104 104 ILE CB C 35.733 0.006 . 478 104 104 ILE N N 126.089 0.200 . 479 105 105 ALA H H 6.905 0.020 . 480 105 105 ALA C C 177.245 0.200 . 481 105 105 ALA CA C 50.158 0.006 . 482 105 105 ALA CB C 17.583 0.200 . 483 105 105 ALA N N 112.574 0.200 . 484 106 106 GLY H H 6.901 0.020 . 485 106 106 GLY C C 173.806 0.200 . 486 106 106 GLY CA C 44.935 0.061 . 487 106 106 GLY N N 102.545 0.200 . 488 107 107 THR H H 8.167 0.020 . 489 107 107 THR C C 176.994 0.200 . 490 107 107 THR CA C 63.491 0.024 . 491 107 107 THR CB C 68.163 0.200 . 492 107 107 THR N N 113.545 0.200 . 493 108 108 THR H H 7.078 0.020 . 494 108 108 THR C C 173.286 0.200 . 495 108 108 THR CA C 60.644 0.007 . 496 108 108 THR CB C 68.841 0.017 . 497 108 108 THR N N 106.587 0.200 . 498 109 109 SER H H 7.063 0.020 . 499 109 109 SER C C 174.072 0.200 . 500 109 109 SER CA C 53.759 0.024 . 501 109 109 SER CB C 65.925 0.004 . 502 109 109 SER N N 112.545 0.200 . 503 110 110 THR H H 8.787 0.020 . 504 110 110 THR C C 175.876 0.200 . 505 110 110 THR CA C 59.109 0.005 . 506 110 110 THR CB C 70.769 0.027 . 507 110 110 THR N N 113.000 0.200 . 508 111 111 LEU H H 8.744 0.020 . 509 111 111 LEU C C 178.190 0.200 . 510 111 111 LEU CA C 57.509 0.002 . 511 111 111 LEU CB C 39.984 0.037 . 512 111 111 LEU N N 122.955 0.200 . 513 112 112 GLN H H 8.087 0.020 . 514 112 112 GLN C C 179.694 0.200 . 515 112 112 GLN CA C 59.104 0.015 . 516 112 112 GLN CB C 26.831 0.012 . 517 112 112 GLN N N 116.038 0.200 . 518 113 113 GLU H H 7.597 0.020 . 519 113 113 GLU C C 177.739 0.200 . 520 113 113 GLU CA C 58.363 0.007 . 521 113 113 GLU CB C 28.268 0.007 . 522 113 113 GLU N N 121.141 0.200 . 523 114 114 GLN H H 7.939 0.020 . 524 114 114 GLN C C 178.242 0.200 . 525 114 114 GLN CA C 59.584 0.003 . 526 114 114 GLN CB C 26.944 0.011 . 527 114 114 GLN N N 118.191 0.200 . 528 115 115 ILE H H 8.568 0.020 . 529 115 115 ILE C C 179.560 0.200 . 530 115 115 ILE CA C 65.128 0.019 . 531 115 115 ILE CB C 37.374 0.002 . 532 115 115 ILE N N 118.450 0.200 . 533 116 116 GLY H H 8.096 0.020 . 534 116 116 GLY C C 176.068 0.200 . 535 116 116 GLY CA C 46.753 0.014 . 536 116 116 GLY N N 111.333 0.200 . 537 117 117 TRP H H 8.209 0.020 . 538 117 117 TRP C C 178.922 0.200 . 539 117 117 TRP CA C 61.621 0.083 . 540 117 117 TRP CB C 26.857 0.038 . 541 117 117 TRP N N 121.898 0.001 . 542 118 118 MET H H 8.444 0.020 . 543 118 118 MET C C 177.388 0.200 . 544 118 118 MET CA C 59.236 0.012 . 545 118 118 MET CB C 33.926 0.012 . 546 118 118 MET N N 116.542 0.200 . 547 119 119 THR H H 7.846 0.020 . 548 119 119 THR C C 173.698 0.200 . 549 119 119 THR CA C 60.733 0.022 . 550 119 119 THR CB C 69.513 0.006 . 551 119 119 THR N N 105.059 0.200 . 552 120 120 HIS H H 7.164 0.020 . 553 120 120 HIS CA C 56.833 0.030 . 554 120 120 HIS CB C 28.064 0.005 . 555 120 120 HIS N N 123.771 0.200 . 556 121 121 ASN H H 7.343 0.020 . 557 121 121 ASN C C 172.676 0.200 . 558 121 121 ASN CA C 48.856 0.200 . 559 121 121 ASN CB C 39.097 0.200 . 560 121 121 ASN N N 119.903 0.200 . 561 123 123 PRO C C 177.534 0.200 . 562 123 123 PRO CA C 63.741 0.200 . 563 123 123 PRO CB C 31.775 0.200 . 564 124 124 ILE H H 8.169 0.020 . 565 124 124 ILE C C 176.283 0.200 . 566 124 124 ILE CA C 58.730 0.200 . 567 124 124 ILE CB C 37.233 0.200 . 568 124 124 ILE N N 122.849 0.200 . 569 125 125 PRO C C 176.868 0.200 . 570 125 125 PRO CA C 62.385 0.200 . 571 125 125 PRO CB C 27.782 0.200 . 572 126 126 VAL H H 8.970 0.020 . 573 126 126 VAL C C 176.590 0.200 . 574 126 126 VAL CA C 65.363 0.015 . 575 126 126 VAL CB C 29.835 0.005 . 576 126 126 VAL N N 116.294 0.200 . 577 127 127 GLY H H 7.652 0.020 . 578 127 127 GLY C C 174.703 0.200 . 579 127 127 GLY CA C 46.749 0.016 . 580 127 127 GLY N N 106.447 0.200 . 581 128 128 GLU H H 7.487 0.020 . 582 128 128 GLU C C 179.564 0.200 . 583 128 128 GLU CA C 57.803 0.067 . 584 128 128 GLU CB C 28.431 0.008 . 585 128 128 GLU N N 121.623 0.200 . 586 129 129 ILE H H 7.989 0.020 . 587 129 129 ILE C C 176.160 0.200 . 588 129 129 ILE CA C 64.812 0.011 . 589 129 129 ILE CB C 37.048 0.006 . 590 129 129 ILE N N 121.512 0.200 . 591 130 130 TYR H H 7.165 0.020 . 592 130 130 TYR C C 178.253 0.200 . 593 130 130 TYR CA C 55.781 0.020 . 594 130 130 TYR CB C 35.821 0.003 . 595 130 130 TYR N N 117.173 0.200 . 596 131 131 LYS H H 7.893 0.020 . 597 131 131 LYS C C 177.704 0.200 . 598 131 131 LYS CA C 59.987 0.041 . 599 131 131 LYS CB C 31.065 0.090 . 600 131 131 LYS N N 116.783 0.200 . 601 132 132 ARG H H 7.444 0.020 . 602 132 132 ARG C C 179.163 0.200 . 603 132 132 ARG CA C 59.443 0.042 . 604 132 132 ARG CB C 28.311 0.200 . 605 132 132 ARG N N 118.109 0.200 . 606 133 133 TRP H H 7.848 0.020 . 607 133 133 TRP C C 178.412 0.200 . 608 133 133 TRP CA C 57.982 0.017 . 609 133 133 TRP CB C 28.473 0.003 . 610 133 133 TRP N N 122.208 0.200 . 611 134 134 ILE H H 8.366 0.020 . 612 134 134 ILE C C 178.229 0.200 . 613 134 134 ILE CA C 64.967 0.016 . 614 134 134 ILE CB C 36.899 0.200 . 615 134 134 ILE N N 119.377 0.200 . 616 135 135 ILE H H 8.721 0.020 . 617 135 135 ILE C C 178.458 0.200 . 618 135 135 ILE CA C 65.759 0.011 . 619 135 135 ILE CB C 36.560 0.013 . 620 135 135 ILE N N 121.583 0.200 . 621 136 136 LEU H H 8.195 0.020 . 622 136 136 LEU C C 180.667 0.200 . 623 136 136 LEU CA C 58.390 0.040 . 624 136 136 LEU CB C 40.278 0.021 . 625 136 136 LEU N N 122.910 0.200 . 626 137 137 GLY H H 8.105 0.020 . 627 137 137 GLY C C 175.559 0.200 . 628 137 137 GLY CA C 47.061 0.020 . 629 137 137 GLY N N 108.295 0.200 . 630 138 138 LEU H H 9.333 0.020 . 631 138 138 LEU C C 178.850 0.200 . 632 138 138 LEU CA C 57.568 0.037 . 633 138 138 LEU CB C 40.986 0.009 . 634 138 138 LEU N N 123.082 0.200 . 635 139 139 ASN H H 8.607 0.020 . 636 139 139 ASN C C 177.742 0.200 . 637 139 139 ASN CA C 56.583 0.012 . 638 139 139 ASN CB C 38.574 0.008 . 639 139 139 ASN N N 117.938 0.001 . 640 140 140 LYS H H 7.489 0.020 . 641 140 140 LYS C C 178.941 0.200 . 642 140 140 LYS CA C 59.532 0.013 . 643 140 140 LYS CB C 31.590 0.008 . 644 140 140 LYS N N 119.634 0.200 . 645 141 141 ILE H H 7.820 0.020 . 646 141 141 ILE C C 178.242 0.200 . 647 141 141 ILE CA C 64.715 0.051 . 648 141 141 ILE CB C 37.361 0.200 . 649 141 141 ILE N N 120.495 0.200 . 650 142 142 VAL H H 8.420 0.020 . 651 142 142 VAL C C 178.837 0.200 . 652 142 142 VAL CA C 65.102 0.004 . 653 142 142 VAL CB C 30.802 0.200 . 654 142 142 VAL N N 118.963 0.200 . 655 143 143 ARG H H 7.513 0.020 . 656 143 143 ARG C C 177.905 0.200 . 657 143 143 ARG CA C 58.020 0.014 . 658 143 143 ARG CB C 29.103 0.200 . 659 143 143 ARG N N 118.110 0.001 . 660 144 144 MET H H 7.708 0.020 . 661 144 144 MET CA C 57.002 0.200 . 662 144 144 MET CB C 31.937 0.200 . 663 144 144 MET N N 118.063 0.200 . 664 150 150 ILE C C 175.950 0.200 . 665 150 150 ILE CA C 54.937 0.200 . 666 151 151 LEU H H 8.088 0.020 . 667 151 151 LEU C C 179.081 0.200 . 668 151 151 LEU CA C 57.887 0.040 . 669 151 151 LEU CB C 40.276 0.127 . 670 151 151 LEU N N 121.739 0.001 . 671 152 152 ASP H H 8.280 0.020 . 672 152 152 ASP CA C 54.733 0.200 . 673 152 152 ASP CB C 37.577 0.200 . 674 152 152 ASP N N 116.919 0.200 . 675 154 154 ARG C C 175.767 0.200 . 676 154 154 ARG CA C 53.765 0.200 . 677 154 154 ARG CB C 31.828 0.200 . 678 155 155 GLN H H 7.702 0.020 . 679 155 155 GLN C C 177.138 0.200 . 680 155 155 GLN CA C 55.402 0.004 . 681 155 155 GLN CB C 26.369 0.023 . 682 155 155 GLN N N 127.597 0.200 . 683 156 156 GLY H H 9.766 0.020 . 684 156 156 GLY C C 173.487 0.200 . 685 156 156 GLY CA C 44.620 0.023 . 686 156 156 GLY N N 116.971 0.200 . 687 157 157 PRO C C 177.024 0.200 . 688 157 157 PRO CA C 65.236 0.200 . 689 158 158 LYS H H 8.449 0.020 . 690 158 158 LYS C C 175.647 0.200 . 691 158 158 LYS CA C 53.552 0.045 . 692 158 158 LYS CB C 31.288 0.200 . 693 158 158 LYS N N 115.398 0.200 . 694 159 159 GLU H H 6.965 0.020 . 695 159 159 GLU C C 174.613 0.200 . 696 159 159 GLU CA C 53.094 0.200 . 697 159 159 GLU CB C 30.960 0.200 . 698 159 159 GLU N N 126.015 0.200 . 699 160 160 PRO C C 177.549 0.200 . 700 160 160 PRO CA C 62.981 0.200 . 701 160 160 PRO CB C 31.569 0.200 . 702 161 161 PHE H H 9.365 0.020 . 703 161 161 PHE C C 176.802 0.200 . 704 161 161 PHE CA C 62.509 0.061 . 705 161 161 PHE CB C 38.425 0.008 . 706 161 161 PHE N N 128.330 0.200 . 707 162 162 ARG H H 8.955 0.020 . 708 162 162 ARG C C 177.306 0.200 . 709 162 162 ARG CA C 59.309 0.008 . 710 162 162 ARG CB C 28.973 0.004 . 711 162 162 ARG N N 115.935 0.200 . 712 163 163 ASP H H 6.915 0.020 . 713 163 163 ASP C C 178.200 0.200 . 714 163 163 ASP CA C 56.673 0.006 . 715 163 163 ASP CB C 39.404 0.010 . 716 163 163 ASP N N 119.341 0.200 . 717 164 164 TYR H H 7.449 0.020 . 718 164 164 TYR C C 176.010 0.200 . 719 164 164 TYR CA C 59.022 0.008 . 720 164 164 TYR CB C 37.334 0.027 . 721 164 164 TYR N N 124.517 0.200 . 722 165 165 VAL H H 8.233 0.020 . 723 165 165 VAL C C 177.809 0.200 . 724 165 165 VAL CA C 66.119 0.003 . 725 165 165 VAL CB C 30.516 0.103 . 726 165 165 VAL N N 120.308 0.200 . 727 166 166 ASP H H 7.477 0.020 . 728 166 166 ASP C C 178.967 0.200 . 729 166 166 ASP CA C 57.397 0.012 . 730 166 166 ASP CB C 40.402 0.019 . 731 166 166 ASP N N 118.556 0.200 . 732 167 167 ARG H H 7.763 0.020 . 733 167 167 ARG C C 179.130 0.200 . 734 167 167 ARG CA C 59.632 0.021 . 735 167 167 ARG CB C 29.301 0.200 . 736 167 167 ARG N N 119.305 0.200 . 737 168 168 PHE H H 8.964 0.020 . 738 168 168 PHE CA C 61.879 0.200 . 739 168 168 PHE N N 124.615 0.200 . 740 193 193 ASN C C 175.073 0.200 . 741 193 193 ASN CA C 52.412 0.200 . 742 193 193 ASN CB C 37.527 0.200 . 743 194 194 ALA H H 7.170 0.020 . 744 194 194 ALA C C 175.707 0.200 . 745 194 194 ALA CA C 51.299 0.112 . 746 194 194 ALA CB C 17.885 0.003 . 747 194 194 ALA N N 124.930 0.200 . 748 195 195 ASN H H 8.983 0.020 . 749 195 195 ASN C C 172.979 0.200 . 750 195 195 ASN CA C 50.967 0.200 . 751 195 195 ASN CB C 34.808 0.200 . 752 195 195 ASN N N 119.594 0.001 . 753 196 196 PRO C C 178.957 0.200 . 754 196 196 PRO CA C 66.313 0.200 . 755 196 196 PRO CB C 31.188 0.200 . 756 197 197 ASP H H 7.625 0.020 . 757 197 197 ASP C C 179.114 0.200 . 758 197 197 ASP CA C 56.882 0.010 . 759 197 197 ASP CB C 40.320 0.009 . 760 197 197 ASP N N 115.874 0.200 . 761 198 198 CYS H H 8.464 0.020 . 762 198 198 CYS C C 176.465 0.200 . 763 198 198 CYS CA C 63.169 0.200 . 764 198 198 CYS CB C 27.167 0.060 . 765 198 198 CYS N N 116.924 0.200 . 766 199 199 LYS H H 9.412 0.020 . 767 199 199 LYS C C 178.115 0.200 . 768 199 199 LYS CA C 60.964 0.003 . 769 199 199 LYS CB C 31.361 0.021 . 770 199 199 LYS N N 122.133 0.200 . 771 200 200 THR H H 7.494 0.020 . 772 200 200 THR C C 176.415 0.200 . 773 200 200 THR CA C 66.219 0.022 . 774 200 200 THR CB C 68.297 0.038 . 775 200 200 THR N N 113.262 0.200 . 776 201 201 ILE H H 6.728 0.020 . 777 201 201 ILE C C 178.415 0.200 . 778 201 201 ILE CA C 63.967 0.009 . 779 201 201 ILE CB C 37.242 0.016 . 780 201 201 ILE N N 122.732 0.200 . 781 202 202 LEU H H 8.385 0.020 . 782 202 202 LEU C C 180.658 0.200 . 783 202 202 LEU CA C 57.064 0.052 . 784 202 202 LEU CB C 40.987 0.200 . 785 202 202 LEU N N 119.251 0.001 . 786 203 203 LYS H H 8.395 0.020 . 787 203 203 LYS C C 178.347 0.200 . 788 203 203 LYS CA C 58.297 0.009 . 789 203 203 LYS CB C 30.704 0.006 . 790 203 203 LYS N N 119.240 0.200 . 791 204 204 ALA H H 7.115 0.020 . 792 204 204 ALA C C 178.811 0.200 . 793 204 204 ALA CA C 52.939 0.007 . 794 204 204 ALA CB C 17.462 0.019 . 795 204 204 ALA N N 120.584 0.200 . 796 205 205 LEU H H 7.352 0.020 . 797 205 205 LEU C C 178.468 0.200 . 798 205 205 LEU CA C 55.890 0.017 . 799 205 205 LEU CB C 41.404 0.022 . 800 205 205 LEU N N 118.684 0.200 . 801 206 206 GLY H H 7.381 0.020 . 802 206 206 GLY C C 171.732 0.200 . 803 206 206 GLY CA C 43.912 0.055 . 804 206 206 GLY N N 104.984 0.200 . 805 207 207 PRO C C 178.227 0.200 . 806 207 207 PRO CA C 63.017 0.200 . 807 207 207 PRO CB C 30.945 0.200 . 808 208 208 GLY H H 8.686 0.020 . 809 208 208 GLY C C 174.622 0.200 . 810 208 208 GLY CA C 44.911 0.004 . 811 208 208 GLY N N 110.320 0.200 . 812 209 209 ALA H H 7.150 0.020 . 813 209 209 ALA C C 177.737 0.200 . 814 209 209 ALA CA C 52.003 0.003 . 815 209 209 ALA CB C 18.744 0.005 . 816 209 209 ALA N N 123.707 0.200 . 817 210 210 THR H H 8.527 0.020 . 818 210 210 THR C C 175.876 0.200 . 819 210 210 THR CA C 60.024 0.004 . 820 210 210 THR CB C 70.901 0.200 . 821 210 210 THR N N 113.619 0.200 . 822 211 211 LEU H H 8.744 0.020 . 823 211 211 LEU C C 179.156 0.200 . 824 211 211 LEU CA C 57.708 0.070 . 825 211 211 LEU CB C 40.105 0.008 . 826 211 211 LEU N N 122.955 0.200 . 827 212 212 GLU H H 8.475 0.020 . 828 212 212 GLU C C 179.562 0.200 . 829 212 212 GLU CA C 59.890 0.014 . 830 212 212 GLU CB C 28.175 0.200 . 831 212 212 GLU N N 117.895 0.200 . 832 213 213 GLU H H 7.697 0.020 . 833 213 213 GLU C C 180.145 0.200 . 834 213 213 GLU CA C 58.972 0.015 . 835 213 213 GLU CB C 28.702 0.019 . 836 213 213 GLU N N 120.952 0.200 . 837 214 214 MET H H 8.425 0.020 . 838 214 214 MET C C 177.479 0.200 . 839 214 214 MET CA C 59.799 0.003 . 840 214 214 MET CB C 32.189 0.050 . 841 214 214 MET N N 120.336 0.200 . 842 215 215 MET H H 8.724 0.020 . 843 215 215 MET C C 179.727 0.200 . 844 215 215 MET CA C 58.940 0.030 . 845 215 215 MET CB C 31.779 0.029 . 846 215 215 MET N N 117.288 0.200 . 847 216 216 THR H H 8.249 0.020 . 848 216 216 THR C C 176.723 0.200 . 849 216 216 THR CA C 66.075 0.004 . 850 216 216 THR CB C 68.086 0.009 . 851 216 216 THR N N 117.071 0.200 . 852 217 217 ALA H H 7.888 0.020 . 853 217 217 ALA C C 179.598 0.200 . 854 217 217 ALA CA C 54.428 0.002 . 855 217 217 ALA CB C 18.026 0.001 . 856 217 217 ALA N N 123.326 0.200 . 857 218 218 CYS H H 7.323 0.020 . 858 218 218 CYS C C 175.569 0.200 . 859 218 218 CYS CA C 59.945 0.005 . 860 218 218 CYS CB C 27.627 0.200 . 861 218 218 CYS N N 111.345 0.200 . 862 219 219 GLN H H 7.449 0.020 . 863 219 219 GLN C C 176.515 0.200 . 864 219 219 GLN CA C 57.867 0.022 . 865 219 219 GLN CB C 27.685 0.025 . 866 219 219 GLN N N 122.489 0.200 . 867 220 220 GLY H H 8.537 0.020 . 868 220 220 GLY C C 174.537 0.200 . 869 220 220 GLY CA C 44.908 0.005 . 870 220 220 GLY N N 109.961 0.200 . 871 221 221 VAL H H 7.277 0.020 . 872 221 221 VAL C C 177.014 0.200 . 873 221 221 VAL CA C 62.928 0.002 . 874 221 221 VAL CB C 30.784 0.006 . 875 221 221 VAL N N 120.644 0.200 . 876 222 222 GLY H H 8.564 0.020 . 877 222 222 GLY C C 174.142 0.200 . 878 222 222 GLY CA C 44.634 0.061 . 879 222 222 GLY N N 115.571 0.200 . 880 223 223 GLY H H 7.914 0.020 . 881 223 223 GLY C C 172.071 0.200 . 882 223 223 GLY CA C 44.124 0.017 . 883 223 223 GLY N N 108.695 0.200 . 884 224 224 PRO C C 177.859 0.200 . 885 224 224 PRO CA C 63.230 0.200 . 886 224 224 PRO CB C 31.122 0.200 . 887 225 225 GLY H H 8.415 0.020 . 888 225 225 GLY C C 174.067 0.200 . 889 225 225 GLY CA C 44.876 0.046 . 890 225 225 GLY N N 109.290 0.200 . 891 226 226 HIS H H 8.049 0.020 . 892 226 226 HIS CA C 55.859 0.050 . 893 226 226 HIS CB C 28.879 0.200 . 894 226 226 HIS N N 119.896 0.001 . 895 227 227 LYS H H 8.119 0.020 . 896 227 227 LYS C C 175.898 0.200 . 897 227 227 LYS CA C 55.628 0.015 . 898 227 227 LYS CB C 31.893 0.052 . 899 227 227 LYS N N 123.533 0.001 . 900 228 228 ALA H H 8.147 0.020 . 901 228 228 ALA C C 177.383 0.200 . 902 228 228 ALA CA C 51.938 0.005 . 903 228 228 ALA CB C 18.400 0.011 . 904 228 228 ALA N N 125.611 0.200 . 905 229 229 ARG H H 8.166 0.020 . 906 229 229 ARG C C 175.894 0.200 . 907 229 229 ARG CA C 55.627 0.003 . 908 229 229 ARG CB C 29.898 0.005 . 909 229 229 ARG N N 121.107 0.200 . 910 230 230 VAL H H 8.090 0.020 . 911 230 230 VAL C C 175.019 0.200 . 912 230 230 VAL CA C 61.973 0.036 . 913 230 230 VAL CB C 31.729 0.005 . 914 230 230 VAL N N 123.017 0.200 . 915 231 231 LEU H H 7.756 0.020 . 916 231 231 LEU C C 182.069 0.200 . 917 231 231 LEU CA C 56.348 0.200 . 918 231 231 LEU CB C 42.383 0.200 . 919 231 231 LEU N N 131.803 0.200 . stop_ save_