data_19575 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HIV-1 capsid protein in tubular assemblies ; _BMRB_accession_number 19575 _BMRB_flat_file_name bmr19575.str _Entry_type original _Submission_date 2013-10-23 _Accession_date 2013-10-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Chemical shifts of full length, wild-type HIV-1 capsid protein in tubular assemblies formed under high ionic strength. Sequential assignments based on 2D and 3D magic-angle spinning NMR spectra and automated resonance assignment using the program MCASSIGN2. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bayro Marvin J. . 2 Chen Bo . . 3 Yau Wai-Ming . . 4 Tycko Robert . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 603 "15N chemical shifts" 188 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-04-24 update BMRB 'update entry citation' 2013-02-11 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Site-specific structural variations accompanying tubular assembly of the HIV-1 capsid protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 24370930 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bayro Marvin J. . 2 Chen Bo . . 3 Yau Wai-Ming . . 4 Tycko Robert . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 426 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1109 _Page_last 1127 _Year 2014 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Tubule _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Tubule $HIV1_CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details 'Tubules formed by self-assembly of a single protein, HIV-1 capsid.' save_ ######################## # Monomeric polymers # ######################## save_HIV1_CA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HIV1_CA _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _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_label 1 PRO 2 ILE 3 VAL 4 GLN 5 ASN 6 LEU 7 GLN 8 GLY 9 GLN 10 MET 11 VAL 12 HIS 13 GLN 14 ALA 15 ILE 16 SER 17 PRO 18 ARG 19 THR 20 LEU 21 ASN 22 ALA 23 TRP 24 VAL 25 LYS 26 VAL 27 VAL 28 GLU 29 GLU 30 LYS 31 ALA 32 PHE 33 SER 34 PRO 35 GLU 36 VAL 37 ILE 38 PRO 39 MET 40 PHE 41 SER 42 ALA 43 LEU 44 SER 45 GLU 46 GLY 47 ALA 48 THR 49 PRO 50 GLN 51 ASP 52 LEU 53 ASN 54 THR 55 MET 56 LEU 57 ASN 58 THR 59 VAL 60 GLY 61 GLY 62 HIS 63 GLN 64 ALA 65 ALA 66 MET 67 GLN 68 MET 69 LEU 70 LYS 71 GLU 72 THR 73 ILE 74 ASN 75 GLU 76 GLU 77 ALA 78 ALA 79 GLU 80 TRP 81 ASP 82 ARG 83 LEU 84 HIS 85 PRO 86 VAL 87 HIS 88 ALA 89 GLY 90 PRO 91 ILE 92 ALA 93 PRO 94 GLY 95 GLN 96 MET 97 ARG 98 GLU 99 PRO 100 ARG 101 GLY 102 SER 103 ASP 104 ILE 105 ALA 106 GLY 107 THR 108 THR 109 SER 110 THR 111 LEU 112 GLN 113 GLU 114 GLN 115 ILE 116 GLY 117 TRP 118 MET 119 THR 120 HIS 121 ASN 122 PRO 123 PRO 124 ILE 125 PRO 126 VAL 127 GLY 128 GLU 129 ILE 130 TYR 131 LYS 132 ARG 133 TRP 134 ILE 135 ILE 136 LEU 137 GLY 138 LEU 139 ASN 140 LYS 141 ILE 142 VAL 143 ARG 144 MET 145 TYR 146 SER 147 PRO 148 THR 149 SER 150 ILE 151 LEU 152 ASP 153 ILE 154 ARG 155 GLN 156 GLY 157 PRO 158 LYS 159 GLU 160 PRO 161 PHE 162 ARG 163 ASP 164 TYR 165 VAL 166 ASP 167 ARG 168 PHE 169 TYR 170 LYS 171 THR 172 LEU 173 ARG 174 ALA 175 GLU 176 GLN 177 ALA 178 SER 179 GLN 180 GLU 181 VAL 182 LYS 183 ASN 184 TRP 185 MET 186 THR 187 GLU 188 THR 189 LEU 190 LEU 191 VAL 192 GLN 193 ASN 194 ALA 195 ASN 196 PRO 197 ASP 198 CYS 199 LYS 200 THR 201 ILE 202 LEU 203 LYS 204 ALA 205 LEU 206 GLY 207 PRO 208 GLY 209 ALA 210 THR 211 LEU 212 GLU 213 GLU 214 MET 215 MET 216 THR 217 ALA 218 CYS 219 GLN 220 GLY 221 VAL 222 GLY 223 GLY 224 PRO 225 GLY 226 HIS 227 LYS 228 ALA 229 ARG 230 VAL 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 19261 HIVcapsid 100.00 231 100.00 100.00 1.27e-169 BMRB 19264 entity 100.00 231 99.13 99.13 2.67e-167 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 $HIV1_CA HIV-1 11676 Viruses . Lentivirus HIV-1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $HIV1_CA 'recombinant technology' . Escherichia coli BL21 DE3 . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_U-CA _Saveframe_category sample _Sample_type solid _Details 'Self-assembly under 1M NaCl.' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HIV1_CA 15 mM '[U-100% 13C; U-100% 15N]' NaCl 1 M 'natural abundance' stop_ save_ save_13-CA _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HIV1_CA 15 mM 'U-15N, [1,3-13C2]Glycerol' NaCl 1 M 'natural abundance' stop_ save_ save_2-CA _Saveframe_category sample _Sample_type solid _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HIV1_CA 15 mM 'U-15N; [2-13C]Glycerol' NaCl 1 M 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_MCASSIGN2 _Saveframe_category software _Name MCASSIGN2 _Version . loop_ _Vendor _Address _Electronic_address 'Robert Tycko' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model InfinityPlus _Field_strength 600 _Details 'Laboratory of Chemical Physics. NIDDK, National Institutes of Health.' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'Avance III' _Field_strength 900 _Details 'Courtesy of the MIT/Harvard Center for Magnetic Resonance. NIH grant EB-002026.' save_ ############################# # NMR applied experiments # ############################# save_3D_NCACX_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $U-CA save_ save_3D_NCOCX_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $U-CA save_ save_3D_NCACX_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCACX' _Sample_label $13-CA save_ save_3D_NCOCX_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCOCX' _Sample_label $13-CA save_ save_3D_CONCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CONCA' _Sample_label $13-CA save_ save_3D_CONCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CONCA' _Sample_label $2-CA save_ save_3D_NCXCY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCXCY' _Sample_label $U-CA save_ save_3D_NCXCY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NCXCY' _Sample_label $13-CA 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' 1 . M pH 8 . pH pressure 1 . atm temperature 273 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details ; 13C chemical shifts referenced relative to DSS. 15N chemical shifts referenced indirectly to liquid ammonia. ; 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 carbon' ppm 0.00 external direct . . . 0.251449530 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 NCACX' '3D NCOCX' '3D CONCA' '3D NCXCY' stop_ loop_ _Sample_label $U-CA $13-CA $2-CA stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Tubule _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 171.95 . . 2 1 1 PRO CA C 60.85 . . 3 1 1 PRO CB C 34.36 . . 4 1 1 PRO CG C 27.1 . . 5 1 1 PRO CD C 50.21 . . 6 1 1 PRO N N 49.48 . . 7 2 2 ILE C C 175.15 . . 8 2 2 ILE CA C 59.95 . . 9 2 2 ILE CB C 37.42 . . 10 2 2 ILE N N 120.68 . . 11 3 3 VAL CA C 60.55 . . 12 3 3 VAL CB C 32.15 . . 13 3 3 VAL N N 122.28 . . 14 4 4 GLN C C 177.05 . . 15 4 4 GLN CA C 54.92 . . 16 4 4 GLN CB C 31.08 . . 17 5 5 ASN C C 176.65 . . 18 5 5 ASN CA C 50.85 . . 19 5 5 ASN CB C 39.32 . . 20 5 5 ASN N N 124.98 . . 21 6 6 LEU CA C 57.02 . . 22 6 6 LEU CB C 41.04 . . 23 6 6 LEU N N 115.28 . . 24 14 14 ALA C C 177.85 . . 25 14 14 ALA CA C 51.74 . . 26 14 14 ALA CB C 18.77 . . 27 14 14 ALA N N 124.08 . . 28 15 15 ILE C C 173.85 . . 29 15 15 ILE CA C 61.81 . . 30 15 15 ILE CB C 38.52 . . 31 15 15 ILE CG1 C 28.94 . . 32 15 15 ILE CG2 C 16.26 . . 33 15 15 ILE N N 121.88 . . 34 16 16 SER C C 174.45 . . 35 16 16 SER CA C 55.5 . . 36 16 16 SER CB C 63.64 . . 37 16 16 SER N N 122.88 . . 38 17 17 PRO C C 177.85 . . 39 17 17 PRO CA C 65.05 . . 40 17 17 PRO CB C 31.46 . . 41 17 17 PRO CG C 27.67 . . 42 17 17 PRO CD C 50.63 . . 43 17 17 PRO N N 137.68 . . 44 18 18 ARG C C 178.95 . . 45 18 18 ARG CA C 58.96 . . 46 18 18 ARG CB C 29.67 . . 47 18 18 ARG N N 115.88 . . 48 19 19 THR C C 175.45 . . 49 19 19 THR CA C 66.34 . . 50 19 19 THR CB C 68.07 . . 51 19 19 THR CG2 C 22.93 . . 52 19 19 THR N N 119.78 . . 53 20 20 LEU C C 178.05 . . 54 20 20 LEU CA C 57.89 . . 55 20 20 LEU CB C 40.21 . . 56 20 20 LEU N N 120.28 . . 57 21 21 ASN C C 177.25 . . 58 21 21 ASN CA C 55.54 . . 59 21 21 ASN CB C 38.33 . . 60 21 21 ASN N N 115.18 . . 61 22 22 ALA C C 179.85 . . 62 22 22 ALA CA C 54.69 . . 63 22 22 ALA CB C 17.97 . . 64 22 22 ALA N N 121.38 . . 65 23 23 TRP C C 175.35 . . 66 23 23 TRP CA C 58.21 . . 67 23 23 TRP CB C 29.35 . . 68 23 23 TRP CG C 110.85 . . 69 23 23 TRP N N 119.28 . . 70 24 24 VAL C C 178.65 . . 71 24 24 VAL CA C 66.38 . . 72 24 24 VAL CB C 31.44 . . 73 24 24 VAL CG1 C 22.5 . . 74 24 24 VAL N N 115.98 . . 75 25 25 LYS C C 178.25 . . 76 25 25 LYS CA C 58.46 . . 77 25 25 LYS CB C 29.36 . . 78 25 25 LYS N N 118.08 . . 79 26 26 VAL C C 177.15 . . 80 26 26 VAL CA C 65.6 . . 81 26 26 VAL CB C 30.87 . . 82 26 26 VAL CG1 C 21.55 . . 83 26 26 VAL N N 119.68 . . 84 27 27 VAL C C 179.05 . . 85 27 27 VAL CA C 65.64 . . 86 27 27 VAL CB C 31.72 . . 87 27 27 VAL N N 119.98 . . 88 28 28 GLU C C 177.85 . . 89 28 28 GLU CA C 58.64 . . 90 28 28 GLU CB C 29.76 . . 91 28 28 GLU N N 117.58 . . 92 29 29 GLU C C 178.65 . . 93 29 29 GLU CA C 58.09 . . 94 29 29 GLU CB C 30.31 . . 95 29 29 GLU N N 115.98 . . 96 30 30 LYS C C 175.85 . . 97 30 30 LYS CA C 56.39 . . 98 30 30 LYS N N 116.68 . . 99 31 31 ALA N N 121.38 . . 100 32 32 PHE C C 176.75 . . 101 32 32 PHE CA C 56.8 . . 102 32 32 PHE CB C 39.5 . . 103 32 32 PHE N N 111.88 . . 104 33 33 SER C C 173.85 . . 105 33 33 SER CA C 57.6 . . 106 33 33 SER CB C 63.15 . . 107 33 33 SER N N 113.68 . . 108 34 34 PRO C C 178.35 . . 109 34 34 PRO CA C 66.03 . . 110 34 34 PRO CB C 31.82 . . 111 34 34 PRO CG C 27.64 . . 112 34 34 PRO CD C 50.22 . . 113 34 34 PRO N N 134.58 . . 114 35 35 GLU C C 179.05 . . 115 35 35 GLU CA C 58.87 . . 116 35 35 GLU CB C 29.58 . . 117 35 35 GLU N N 118.18 . . 118 36 36 VAL C C 176.45 . . 119 36 36 VAL CA C 65.37 . . 120 36 36 VAL CB C 31.55 . . 121 36 36 VAL CG1 C 21.41 . . 122 36 36 VAL N N 115.38 . . 123 37 37 ILE C C 175.05 . . 124 37 37 ILE CA C 67.52 . . 125 37 37 ILE CB C 34.52 . . 126 37 37 ILE CG1 C 30.36 . . 127 37 37 ILE CG2 C 18.25 . . 128 37 37 ILE N N 118.68 . . 129 38 38 PRO C C 179.15 . . 130 38 38 PRO CA C 64.82 . . 131 38 38 PRO CB C 30.21 . . 132 38 38 PRO CG C 27.82 . . 133 38 38 PRO CD C 49.01 . . 134 38 38 PRO N N 134.58 . . 135 39 39 MET C C 176.65 . . 136 39 39 MET CA C 57.64 . . 137 39 39 MET CB C 30.83 . . 138 39 39 MET N N 116.48 . . 139 40 40 PHE C C 178.55 . . 140 40 40 PHE CA C 61.56 . . 141 40 40 PHE CB C 37.87 . . 142 40 40 PHE N N 121.08 . . 143 41 41 SER C C 175.75 . . 144 41 41 SER CA C 62.05 . . 145 41 41 SER CB C 62.38 . . 146 41 41 SER N N 114.48 . . 147 42 42 ALA C C 180.25 . . 148 42 42 ALA CA C 54.14 . . 149 42 42 ALA CB C 18.99 . . 150 42 42 ALA N N 121.48 . . 151 43 43 LEU C C 175.85 . . 152 43 43 LEU CA C 55.65 . . 153 43 43 LEU CB C 41.9 . . 154 43 43 LEU N N 115.88 . . 155 44 44 SER C C 174.75 . . 156 44 44 SER CA C 56.87 . . 157 44 44 SER CB C 63.43 . . 158 44 44 SER N N 109.08 . . 159 45 45 GLU C C 178.05 . . 160 45 45 GLU CA C 57.96 . . 161 45 45 GLU CB C 29.11 . . 162 45 45 GLU CG C 35.28 . . 163 45 45 GLU N N 125.08 . . 164 46 46 GLY C C 174.05 . . 165 46 46 GLY CA C 45.72 . . 166 46 46 GLY N N 115.78 . . 167 47 47 ALA C C 178.15 . . 168 47 47 ALA CA C 52.87 . . 169 47 47 ALA CB C 20.08 . . 170 47 47 ALA N N 119.78 . . 171 48 48 THR C C 174.35 . . 172 48 48 THR CA C 59.49 . . 173 48 48 THR CB C 69.03 . . 174 48 48 THR CG2 C 21.86 . . 175 48 48 THR N N 108.88 . . 176 49 49 PRO C C 176.65 . . 177 49 49 PRO CA C 66.83 . . 178 49 49 PRO CB C 29.83 . . 179 49 49 PRO CG C 27.92 . . 180 49 49 PRO CD C 49.77 . . 181 49 49 PRO N N 132.68 . . 182 50 50 GLN C C 177.45 . . 183 50 50 GLN CA C 58.8 . . 184 50 50 GLN CB C 29.88 . . 185 50 50 GLN CG C 32.73 . . 186 50 50 GLN N N 116.28 . . 187 51 51 ASP C C 179.55 . . 188 51 51 ASP CA C 57.66 . . 189 51 51 ASP CB C 41.83 . . 190 51 51 ASP N N 117.68 . . 191 52 52 LEU C C 178.35 . . 192 52 52 LEU CA C 57.93 . . 193 52 52 LEU CB C 42.04 . . 194 52 52 LEU N N 120.38 . . 195 53 53 ASN C C 177.85 . . 196 53 53 ASN CA C 56.03 . . 197 53 53 ASN CB C 38.32 . . 198 53 53 ASN N N 115.58 . . 199 54 54 THR C C 176.25 . . 200 54 54 THR CA C 67.09 . . 201 54 54 THR CB C 67.94 . . 202 54 54 THR CG2 C 23.24 . . 203 54 54 THR N N 119.58 . . 204 55 55 MET C C 179.45 . . 205 55 55 MET CA C 60.02 . . 206 55 55 MET CB C 32.71 . . 207 55 55 MET N N 119.18 . . 208 56 56 LEU C C 178.05 . . 209 56 56 LEU CA C 58.7 . . 210 56 56 LEU CB C 41.55 . . 211 56 56 LEU CG C 26.78 . . 212 56 56 LEU N N 121.98 . . 213 57 57 ASN C C 176.75 . . 214 57 57 ASN CA C 54.55 . . 215 57 57 ASN CB C 38.1 . . 216 57 57 ASN N N 115.48 . . 217 58 58 THR C C 174.15 . . 218 58 58 THR CA C 63.17 . . 219 58 58 THR N N 107.98 . . 220 59 59 VAL C C 176.55 . . 221 59 59 VAL CA C 63.97 . . 222 59 59 VAL CB C 32.16 . . 223 59 59 VAL CG1 C 22.06 . . 224 59 59 VAL N N 120.88 . . 225 60 60 GLY C C 174.15 . . 226 60 60 GLY CA C 44.85 . . 227 60 60 GLY N N 116.38 . . 228 61 61 GLY C C 174.25 . . 229 61 61 GLY CA C 45.14 . . 230 62 62 HIS N N 119.48 . . 231 63 63 GLN C C 178.85 . . 232 63 63 GLN CA C 59.87 . . 233 63 63 GLN CB C 30.06 . . 234 63 63 GLN N N 119.98 . . 235 64 64 ALA C C 178.55 . . 236 64 64 ALA CA C 55.68 . . 237 64 64 ALA CB C 18.36 . . 238 64 64 ALA N N 124.18 . . 239 65 65 ALA C C 179.45 . . 240 65 65 ALA CA C 54.78 . . 241 65 65 ALA CB C 18.29 . . 242 65 65 ALA N N 121.08 . . 243 66 66 MET C C 179.05 . . 244 66 66 MET CA C 56.14 . . 245 66 66 MET CB C 29.9 . . 246 66 66 MET N N 113.08 . . 247 67 67 GLN N N 121.08 . . 248 69 69 LEU C C 181.25 . . 249 69 69 LEU CA C 57.24 . . 250 69 69 LEU CB C 41.53 . . 251 69 69 LEU N N 117.88 . . 252 70 70 LYS C C 178.35 . . 253 70 70 LYS CA C 58.76 . . 254 70 70 LYS CB C 31.52 . . 255 70 70 LYS N N 119.48 . . 256 71 71 GLU C C 178.65 . . 257 71 71 GLU CA C 58.78 . . 258 71 71 GLU N N 119.08 . . 259 72 72 THR C C 176.45 . . 260 72 72 THR CA C 66.87 . . 261 72 72 THR CB C 67.99 . . 262 72 72 THR N N 116.38 . . 263 73 73 ILE C C 176.65 . . 264 73 73 ILE CA C 65.58 . . 265 73 73 ILE CB C 37.61 . . 266 73 73 ILE CG2 C 18.03 . . 267 73 73 ILE N N 122.28 . . 268 74 74 ASN C C 177.95 . . 269 74 74 ASN CA C 55.69 . . 270 74 74 ASN CB C 37.53 . . 271 74 74 ASN N N 116.88 . . 272 75 75 GLU C C 177.95 . . 273 75 75 GLU CA C 57.92 . . 274 75 75 GLU CB C 29.27 . . 275 75 75 GLU N N 121.48 . . 276 76 76 GLU C C 179.25 . . 277 76 76 GLU CA C 57.74 . . 278 76 76 GLU CB C 26.73 . . 279 76 76 GLU N N 120.38 . . 280 77 77 ALA C C 178.55 . . 281 77 77 ALA CA C 54.55 . . 282 77 77 ALA CB C 17.44 . . 283 77 77 ALA N N 123.48 . . 284 78 78 ALA C C 181.25 . . 285 78 78 ALA CA C 54.4 . . 286 78 78 ALA CB C 17.65 . . 287 78 78 ALA N N 118.98 . . 288 79 79 GLU C C 178.05 . . 289 79 79 GLU CA C 58.57 . . 290 79 79 GLU CB C 28.9 . . 291 79 79 GLU N N 120.88 . . 292 80 80 TRP CA C 61.92 . . 293 80 80 TRP CB C 27.61 . . 294 80 80 TRP CG C 109.95 . . 295 80 80 TRP N N 121.38 . . 296 81 81 ASP C C 177.65 . . 297 81 81 ASP CA C 56.18 . . 298 81 81 ASP CB C 37.25 . . 299 81 81 ASP N N 116.88 . . 300 82 82 ARG C C 177.65 . . 301 82 82 ARG CA C 58.82 . . 302 82 82 ARG CB C 30.26 . . 303 82 82 ARG CG C 27.73 . . 304 82 82 ARG N N 119.78 . . 305 83 83 LEU C C 175.95 . . 306 83 83 LEU CA C 54.97 . . 307 83 83 LEU CB C 42.48 . . 308 83 83 LEU N N 116.58 . . 309 84 84 HIS C C 170.55 . . 310 84 84 HIS CA C 52.76 . . 311 84 84 HIS CB C 27.58 . . 312 84 84 HIS N N 116.68 . . 313 85 85 PRO C C 176.65 . . 314 85 85 PRO CA C 62.76 . . 315 85 85 PRO CB C 31.64 . . 316 85 85 PRO CG C 26.96 . . 317 85 85 PRO CD C 49.98 . . 318 85 85 PRO N N 137.78 . . 319 86 86 VAL C C 175.95 . . 320 86 86 VAL CA C 62.03 . . 321 86 86 VAL CB C 32.9 . . 322 86 86 VAL N N 120.58 . . 323 87 87 HIS C C 174.35 . . 324 87 87 HIS CA C 55.43 . . 325 87 87 HIS N N 122.38 . . 326 88 88 ALA C C 177.35 . . 327 88 88 ALA CA C 52.09 . . 328 88 88 ALA CB C 19.08 . . 329 88 88 ALA N N 127.28 . . 330 89 89 GLY C C 171.25 . . 331 89 89 GLY CA C 44.53 . . 332 89 89 GLY N N 108.68 . . 333 90 90 PRO N N 136.18 . . 334 91 91 ILE C C 175.55 . . 335 91 91 ILE CA C 59.9 . . 336 91 91 ILE N N 121.38 . . 337 92 92 ALA C C 174.85 . . 338 92 92 ALA CA C 50.53 . . 339 92 92 ALA CB C 17.88 . . 340 92 92 ALA N N 130.08 . . 341 93 93 PRO C C 178.05 . . 342 93 93 PRO CA C 63.62 . . 343 93 93 PRO CB C 32.42 . . 344 93 93 PRO N N 133.98 . . 345 94 94 GLY C C 174.25 . . 346 94 94 GLY CA C 45.35 . . 347 94 94 GLY N N 111.68 . . 348 95 95 GLN N N 119.68 . . 349 98 98 GLU C C 174.25 . . 350 98 98 GLU CA C 54.19 . . 351 98 98 GLU CB C 29.35 . . 352 98 98 GLU N N 122.88 . . 353 99 99 PRO C C 176.95 . . 354 99 99 PRO CA C 62.33 . . 355 99 99 PRO CB C 30.15 . . 356 99 99 PRO CG C 27.62 . . 357 99 99 PRO CD C 48.82 . . 358 99 99 PRO N N 134.08 . . 359 100 100 ARG C C 178.55 . . 360 100 100 ARG CA C 52.89 . . 361 100 100 ARG CB C 30.8 . . 362 100 100 ARG N N 120.98 . . 363 101 101 GLY C C 175.85 . . 364 101 101 GLY CA C 48.29 . . 365 101 101 GLY N N 116.48 . . 366 102 102 SER C C 176.65 . . 367 102 102 SER CA C 60.63 . . 368 102 102 SER CB C 61.72 . . 369 102 102 SER N N 114.58 . . 370 103 103 ASP C C 179.65 . . 371 103 103 ASP CA C 56.56 . . 372 103 103 ASP CB C 41.26 . . 373 103 103 ASP N N 122.48 . . 374 104 104 ILE C C 172.45 . . 375 104 104 ILE CA C 65.58 . . 376 104 104 ILE CB C 36.63 . . 377 104 104 ILE CG1 C 30.36 . . 378 104 104 ILE CG2 C 16.82 . . 379 104 104 ILE N N 125.58 . . 380 105 105 ALA C C 177.05 . . 381 105 105 ALA CA C 50.35 . . 382 105 105 ALA CB C 18.4 . . 383 105 105 ALA N N 111.68 . . 384 106 106 GLY C C 173.55 . . 385 106 106 GLY CA C 45.3 . . 386 106 106 GLY N N 101.98 . . 387 107 107 THR C C 176.95 . . 388 107 107 THR CA C 63.73 . . 389 107 107 THR CB C 68.66 . . 390 107 107 THR CG2 C 22.54 . . 391 107 107 THR N N 112.98 . . 392 108 108 THR C C 173.05 . . 393 108 108 THR CA C 60.69 . . 394 108 108 THR CB C 69.15 . . 395 108 108 THR CG2 C 20.23 . . 396 108 108 THR N N 105.68 . . 397 109 109 SER C C 173.85 . . 398 109 109 SER CA C 53.88 . . 399 109 109 SER CB C 66.64 . . 400 109 109 SER N N 111.98 . . 401 110 110 THR C C 175.55 . . 402 110 110 THR CA C 59.17 . . 403 110 110 THR CB C 71.09 . . 404 110 110 THR CG2 C 21.84 . . 405 110 110 THR N N 112.28 . . 406 111 111 LEU C C 178.25 . . 407 111 111 LEU CA C 57.8 . . 408 111 111 LEU CB C 40.56 . . 409 111 111 LEU N N 122.48 . . 410 112 112 GLN C C 179.55 . . 411 112 112 GLN CA C 59.39 . . 412 112 112 GLN CB C 27.67 . . 413 112 112 GLN CG C 34.06 . . 414 112 112 GLN N N 115.48 . . 415 113 113 GLU C C 179.15 . . 416 113 113 GLU CA C 58.12 . . 417 113 113 GLU CB C 26.94 . . 418 113 113 GLU N N 120.28 . . 419 114 114 GLN CA C 59.88 . . 420 114 114 GLN CB C 29.72 . . 421 114 114 GLN CG C 35.21 . . 422 114 114 GLN N N 119.38 . . 423 115 115 ILE C C 179.45 . . 424 115 115 ILE CA C 65.44 . . 425 115 115 ILE CB C 38.44 . . 426 115 115 ILE CG1 C 28.38 . . 427 115 115 ILE CG2 C 17 . . 428 115 115 ILE N N 117.98 . . 429 116 116 GLY C C 175.85 . . 430 116 116 GLY CA C 47 . . 431 116 116 GLY N N 110.48 . . 432 117 117 TRP C C 178.65 . . 433 117 117 TRP CA C 61.96 . . 434 117 117 TRP CB C 27.37 . . 435 117 117 TRP CG C 112.45 . . 436 117 117 TRP N N 121.18 . . 437 118 118 MET C C 177.25 . . 438 118 118 MET CA C 59.41 . . 439 118 118 MET CB C 34.82 . . 440 118 118 MET CG C 32.81 . . 441 118 118 MET N N 115.78 . . 442 119 119 THR C C 173.45 . . 443 119 119 THR CA C 60.75 . . 444 119 119 THR CB C 69.77 . . 445 119 119 THR CG2 C 21.38 . . 446 119 119 THR N N 104.18 . . 447 120 120 HIS C C 172.35 . . 448 120 120 HIS CA C 57.13 . . 449 120 120 HIS CB C 28.76 . . 450 120 120 HIS N N 123.78 . . 451 121 121 ASN C C 172.35 . . 452 121 121 ASN CA C 48.89 . . 453 121 121 ASN CB C 39.74 . . 454 121 121 ASN CG C 177.15 . . 455 121 121 ASN N N 118.78 . . 456 122 122 PRO C C 174.75 . . 457 122 122 PRO CA C 61.98 . . 458 122 122 PRO CB C 32.76 . . 459 122 122 PRO CG C 24.54 . . 460 122 122 PRO CD C 50.28 . . 461 122 122 PRO N N 138.48 . . 462 123 123 PRO C C 177.45 . . 463 123 123 PRO CA C 63.84 . . 464 123 123 PRO CB C 32.55 . . 465 123 123 PRO CG C 27.05 . . 466 123 123 PRO CD C 50.25 . . 467 123 123 PRO N N 134.18 . . 468 124 124 ILE C C 176.05 . . 469 124 124 ILE CA C 59.08 . . 470 124 124 ILE CB C 38.02 . . 471 124 124 ILE CG2 C 17.08 . . 472 124 124 ILE N N 122.68 . . 473 125 125 PRO C C 176.65 . . 474 125 125 PRO CA C 62.46 . . 475 125 125 PRO CB C 28.55 . . 476 125 125 PRO CG C 26.96 . . 477 125 125 PRO CD C 50.94 . . 478 125 125 PRO N N 136.48 . . 479 126 126 VAL C C 176.45 . . 480 126 126 VAL CA C 65.5 . . 481 126 126 VAL CB C 30.67 . . 482 126 126 VAL CG1 C 23.42 . . 483 126 126 VAL CG2 C 19.19 . . 484 126 126 VAL N N 115.28 . . 485 127 127 GLY C C 174.65 . . 486 127 127 GLY CA C 47.04 . . 487 127 127 GLY N N 106.48 . . 488 128 128 GLU C C 179.25 . . 489 128 128 GLU CA C 58.13 . . 490 128 128 GLU CB C 29.12 . . 491 128 128 GLU N N 121.48 . . 492 129 129 ILE C C 175.85 . . 493 129 129 ILE CA C 65 . . 494 129 129 ILE CB C 37.87 . . 495 129 129 ILE CG2 C 17.74 . . 496 129 129 ILE N N 120.58 . . 497 130 130 TYR C C 178.15 . . 498 130 130 TYR CA C 55.87 . . 499 130 130 TYR CB C 37.63 . . 500 130 130 TYR N N 116.58 . . 501 131 131 LYS N N 121.48 . . 502 133 133 TRP C C 178.05 . . 503 133 133 TRP CA C 58.36 . . 504 133 133 TRP CB C 29.84 . . 505 133 133 TRP CG C 112.15 . . 506 133 133 TRP N N 120.58 . . 507 134 134 ILE C C 177.95 . . 508 134 134 ILE CA C 65.05 . . 509 134 134 ILE CB C 38.13 . . 510 134 134 ILE CG1 C 29.44 . . 511 134 134 ILE CG2 C 17.81 . . 512 134 134 ILE N N 118.58 . . 513 135 135 ILE C C 177.55 . . 514 135 135 ILE CA C 66.16 . . 515 135 135 ILE CB C 37.46 . . 516 135 135 ILE CG1 C 30.94 . . 517 135 135 ILE CG2 C 17.3 . . 518 135 135 ILE N N 121.08 . . 519 136 136 LEU C C 180.85 . . 520 136 136 LEU CA C 58.54 . . 521 136 136 LEU CB C 41.31 . . 522 136 136 LEU CG C 26.82 . . 523 136 136 LEU N N 121.48 . . 524 137 137 GLY C C 175.65 . . 525 137 137 GLY CA C 47.44 . . 526 137 137 GLY N N 106.68 . . 527 138 138 LEU C C 178.35 . . 528 138 138 LEU CA C 57.82 . . 529 138 138 LEU CB C 41.93 . . 530 138 138 LEU CG C 26 . . 531 138 138 LEU N N 123.08 . . 532 139 139 ASN C C 178.05 . . 533 139 139 ASN CA C 56.45 . . 534 139 139 ASN CB C 38.4 . . 535 139 139 ASN N N 118.28 . . 536 140 140 LYS N N 118.28 . . 537 146 146 SER C C 174.55 . . 538 147 147 PRO C C 177.15 . . 539 147 147 PRO CA C 62.43 . . 540 147 147 PRO N N 133.78 . . 541 148 148 THR C C 176.05 . . 542 148 148 THR CA C 59.61 . . 543 148 148 THR CB C 70.43 . . 544 148 148 THR N N 112.88 . . 545 149 149 SER C C 174.55 . . 546 149 149 SER CA C 57.18 . . 547 149 149 SER CB C 64.75 . . 548 149 149 SER N N 116.88 . . 549 150 150 ILE C C 178.35 . . 550 150 150 ILE CA C 59.86 . . 551 150 150 ILE CB C 37.35 . . 552 150 150 ILE N N 121.18 . . 553 151 151 LEU C C 179.35 . . 554 151 151 LEU CA C 57.9 . . 555 151 151 LEU CB C 41.05 . . 556 151 151 LEU CG C 26.51 . . 557 151 151 LEU N N 117.48 . . 558 152 152 ASP C C 175.75 . . 559 152 152 ASP CA C 53.91 . . 560 152 152 ASP CB C 41.92 . . 561 152 152 ASP N N 115.48 . . 562 153 153 ILE C C 173.55 . . 563 153 153 ILE CA C 58.9 . . 564 153 153 ILE CB C 35.45 . . 565 153 153 ILE N N 122.08 . . 566 154 154 ARG C C 175.05 . . 567 154 154 ARG CA C 53.88 . . 568 154 154 ARG CB C 32.94 . . 569 154 154 ARG N N 125.28 . . 570 155 155 GLN C C 176.85 . . 571 155 155 GLN CA C 55.49 . . 572 155 155 GLN CB C 27.06 . . 573 155 155 GLN CG C 32.34 . . 574 155 155 GLN N N 127.48 . . 575 156 156 GLY C C 173.15 . . 576 156 156 GLY CA C 44.9 . . 577 156 156 GLY N N 116.98 . . 578 157 157 PRO C C 176.75 . . 579 157 157 PRO CA C 65.23 . . 580 157 157 PRO CB C 31.85 . . 581 157 157 PRO CG C 27.44 . . 582 157 157 PRO CD C 49.89 . . 583 157 157 PRO N N 136.88 . . 584 158 158 LYS C C 175.15 . . 585 158 158 LYS CA C 53.92 . . 586 158 158 LYS CB C 32.14 . . 587 158 158 LYS N N 114.98 . . 588 159 159 GLU C C 174.35 . . 589 159 159 GLU CA C 53.17 . . 590 159 159 GLU CB C 32.19 . . 591 159 159 GLU N N 125.18 . . 592 160 160 PRO C C 177.35 . . 593 160 160 PRO CA C 62.91 . . 594 160 160 PRO CB C 32.35 . . 595 160 160 PRO CG C 28.18 . . 596 160 160 PRO CD C 51.31 . . 597 160 160 PRO N N 143.58 . . 598 161 161 PHE C C 176.95 . . 599 161 161 PHE CA C 62.32 . . 600 161 161 PHE CB C 39.37 . . 601 161 161 PHE N N 127.58 . . 602 162 162 ARG C C 176.25 . . 603 162 162 ARG CA C 59.67 . . 604 162 162 ARG N N 115.88 . . 605 163 163 ASP C C 178.25 . . 606 163 163 ASP CA C 56.94 . . 607 163 163 ASP CB C 39.91 . . 608 163 163 ASP N N 116.68 . . 609 164 164 TYR C C 175.95 . . 610 164 164 TYR CA C 59.16 . . 611 164 164 TYR CG C 126.75 . . 612 164 164 TYR N N 123.28 . . 613 165 165 VAL CA C 66.19 . . 614 167 167 ARG C C 179.05 . . 615 168 168 PHE C C 176.85 . . 616 168 168 PHE CA C 62.24 . . 617 168 168 PHE CB C 39.63 . . 618 168 168 PHE N N 123.88 . . 619 169 169 TYR C C 179.15 . . 620 169 169 TYR CA C 63.47 . . 621 169 169 TYR CB C 37.89 . . 622 169 169 TYR N N 114.88 . . 623 170 170 LYS CA C 60.04 . . 624 170 170 LYS N N 123.58 . . 625 171 171 THR CA C 64.6 . . 626 171 171 THR CB C 68.94 . . 627 171 171 THR N N 111.98 . . 628 176 176 GLN C C 176.75 . . 629 176 176 GLN CA C 58.59 . . 630 177 177 ALA C C 177.35 . . 631 177 177 ALA CA C 52.09 . . 632 177 177 ALA CB C 19.1 . . 633 177 177 ALA N N 118.48 . . 634 178 178 SER C C 178.85 . . 635 178 178 SER CA C 58.6 . . 636 178 178 SER N N 113.58 . . 637 183 183 ASN C C 177.35 . . 638 183 183 ASN CA C 55.76 . . 639 183 183 ASN CB C 37.53 . . 640 183 183 ASN N N 116.98 . . 641 184 184 TRP C C 179.25 . . 642 184 184 TRP CA C 61.82 . . 643 184 184 TRP CB C 28.26 . . 644 184 184 TRP CG C 111.15 . . 645 184 184 TRP N N 122.38 . . 646 185 185 MET C C 179.55 . . 647 185 185 MET CA C 59.52 . . 648 185 185 MET CB C 31.79 . . 649 185 185 MET N N 115.88 . . 650 186 186 THR C C 178.25 . . 651 186 186 THR CA C 64.94 . . 652 186 186 THR CB C 68.84 . . 653 186 186 THR N N 110.18 . . 654 187 187 GLU C C 178.35 . . 655 187 187 GLU CA C 59.66 . . 656 187 187 GLU CB C 27.68 . . 657 187 187 GLU CG C 32.8 . . 658 187 187 GLU N N 116.18 . . 659 188 188 THR C C 174.05 . . 660 188 188 THR CA C 63.39 . . 661 188 188 THR CB C 69.24 . . 662 188 188 THR CG2 C 23.32 . . 663 188 188 THR N N 108.08 . . 664 189 189 LEU C C 178.05 . . 665 189 189 LEU CA C 58.56 . . 666 189 189 LEU CB C 40.02 . . 667 189 189 LEU N N 120.58 . . 668 190 190 LEU C C 179.35 . . 669 190 190 LEU CA C 57.75 . . 670 190 190 LEU CB C 41.69 . . 671 190 190 LEU N N 120.68 . . 672 191 191 VAL C C 176.75 . . 673 191 191 VAL CA C 65.2 . . 674 191 191 VAL CB C 31.99 . . 675 191 191 VAL CG1 C 22.56 . . 676 191 191 VAL N N 115.08 . . 677 192 192 GLN C C 177.05 . . 678 192 192 GLN CA C 58.25 . . 679 192 192 GLN CB C 28.21 . . 680 192 192 GLN N N 115.08 . . 681 193 193 ASN C C 175.15 . . 682 193 193 ASN CA C 52.33 . . 683 193 193 ASN CB C 38.15 . . 684 193 193 ASN N N 114.38 . . 685 194 194 ALA C C 175.25 . . 686 194 194 ALA CA C 51.68 . . 687 194 194 ALA CB C 18.58 . . 688 194 194 ALA N N 124.58 . . 689 195 195 ASN C C 173.25 . . 690 195 195 ASN CA C 51.39 . . 691 195 195 ASN CB C 35.97 . . 692 195 195 ASN N N 119.28 . . 693 196 196 PRO C C 178.25 . . 694 196 196 PRO CA C 66.43 . . 695 196 196 PRO CB C 32.02 . . 696 196 196 PRO CG C 27.06 . . 697 196 196 PRO CD C 49.62 . . 698 196 196 PRO N N 132.38 . . 699 197 197 ASP C C 178.85 . . 700 197 197 ASP CA C 56.78 . . 701 197 197 ASP CB C 40.28 . . 702 197 197 ASP N N 115.68 . . 703 198 198 CYS C C 178.65 . . 704 198 198 CYS CA C 59.65 . . 705 198 198 CYS CB C 35.14 . . 706 198 198 CYS N N 115.98 . . 707 199 199 LYS C C 177.55 . . 708 199 199 LYS CA C 60.8 . . 709 199 199 LYS CB C 32.22 . . 710 199 199 LYS N N 121.68 . . 711 200 200 THR C C 176.05 . . 712 200 200 THR CA C 66.51 . . 713 200 200 THR CB C 68.83 . . 714 200 200 THR CG2 C 21.5 . . 715 200 200 THR N N 112.08 . . 716 201 201 ILE C C 178.25 . . 717 201 201 ILE CA C 64.31 . . 718 201 201 ILE CB C 37.95 . . 719 201 201 ILE CG1 C 29.1 . . 720 201 201 ILE CG2 C 18.25 . . 721 201 201 ILE N N 122.98 . . 722 202 202 LEU C C 178.05 . . 723 202 202 LEU CA C 57.3 . . 724 202 202 LEU CB C 41.29 . . 725 202 202 LEU N N 118.18 . . 726 203 203 LYS C C 178.35 . . 727 203 203 LYS CA C 59.81 . . 728 203 203 LYS CB C 31.68 . . 729 203 203 LYS N N 119.68 . . 730 204 204 ALA C C 178.15 . . 731 204 204 ALA CA C 53.29 . . 732 204 204 ALA CB C 18.11 . . 733 204 204 ALA N N 120.08 . . 734 205 205 LEU C C 178.75 . . 735 205 205 LEU CA C 56.32 . . 736 205 205 LEU CB C 42.38 . . 737 205 205 LEU N N 116.98 . . 738 206 206 GLY C C 171.55 . . 739 206 206 GLY CA C 44.2 . . 740 206 206 GLY N N 104.08 . . 741 207 207 PRO C C 178.25 . . 742 207 207 PRO CA C 62.98 . . 743 207 207 PRO CB C 31.71 . . 744 207 207 PRO CG C 26.97 . . 745 207 207 PRO CD C 49.51 . . 746 207 207 PRO N N 132.48 . . 747 208 208 GLY C C 174.55 . . 748 208 208 GLY CA C 45.29 . . 749 208 208 GLY N N 109.98 . . 750 209 209 ALA C C 177.55 . . 751 209 209 ALA CA C 52.14 . . 752 209 209 ALA CB C 19.53 . . 753 209 209 ALA N N 123.48 . . 754 210 210 THR C C 175.15 . . 755 210 210 THR CA C 59.98 . . 756 210 210 THR CB C 70.26 . . 757 210 210 THR CG2 C 21.9 . . 758 210 210 THR N N 113.68 . . 759 211 211 LEU C C 179.35 . . 760 211 211 LEU CA C 58.18 . . 761 211 211 LEU CB C 40.36 . . 762 211 211 LEU CG C 26.94 . . 763 211 211 LEU N N 125.18 . . 764 212 212 GLU C C 179.35 . . 765 212 212 GLU CA C 59.82 . . 766 212 212 GLU CB C 28.99 . . 767 212 212 GLU N N 119.28 . . 768 213 213 GLU C C 178.35 . . 769 213 213 GLU CA C 58.66 . . 770 213 213 GLU N N 119.08 . . 771 214 214 MET C C 179.05 . . 772 214 214 MET CA C 59.66 . . 773 214 214 MET CB C 31.53 . . 774 214 214 MET N N 119.28 . . 775 215 215 MET C C 179.15 . . 776 215 215 MET CA C 58.58 . . 777 215 215 MET CB C 32.41 . . 778 215 215 MET N N 117.58 . . 779 216 216 THR C C 175.95 . . 780 216 216 THR CA C 65.87 . . 781 216 216 THR CB C 68.52 . . 782 216 216 THR N N 114.58 . . 783 217 217 ALA C C 178.85 . . 784 217 217 ALA CA C 54.76 . . 785 217 217 ALA CB C 18.6 . . 786 217 217 ALA N N 123.38 . . 787 218 218 CYS C C 174.45 . . 788 218 218 CYS CA C 56.57 . . 789 218 218 CYS CB C 40.36 . . 790 218 218 CYS N N 109.88 . . 791 219 219 GLN N N 121.78 . . stop_ save_