data_17307 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of the monomeric mutant C-terminal domain of HIV-1 Capsid in complex with stapled peptide Inhibitor ; _BMRB_accession_number 17307 _BMRB_flat_file_name bmr17307.str _Entry_type new _Submission_date 2010-11-18 _Accession_date 2010-11-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhattacharya Shibani . . 2 Zhang Hongtao . . 3 Debnath Asim K. . 4 Cowburn David . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 601 "13C chemical shifts" 377 "15N chemical shifts" 94 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-12-16 original author . stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 18417468 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bhattacharya Shibani . . 2 Zhang Hongtao . . 3 Debnath Asim K. . 4 Cowburn David . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 283 _Journal_issue 24 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 16247 _Page_last 16278 _Year 2008 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HIV-1 Capsid in complex with stapled peptide Inhibitor' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Capsid_protein_p24 $Capsid_protein_p24 NYAD-13_Peptide_Inhibitor $NYAD-13_Peptide_Inhibitor 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_Capsid_protein_p24 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Capsid_protein_p24 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MTSILDIRQGPKEPFRDYVD RFYKTLRAEQASQEVKNAAT ETLLVQNANPDCKTILKALG PAATLEEMMTACQGVGGPGH KARVL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 127 MET 2 128 GLY 3 129 SER 4 130 SER 5 131 HIS 6 132 HIS 7 133 HIS 8 134 HIS 9 135 HIS 10 136 HIS 11 137 SER 12 138 SER 13 139 GLY 14 140 LEU 15 141 VAL 16 142 PRO 17 143 ARG 18 144 GLY 19 145 SER 20 146 HIS 21 147 MET 22 148 THR 23 149 SER 24 150 ILE 25 151 LEU 26 152 ASP 27 153 ILE 28 154 ARG 29 155 GLN 30 156 GLY 31 157 PRO 32 158 LYS 33 159 GLU 34 160 PRO 35 161 PHE 36 162 ARG 37 163 ASP 38 164 TYR 39 165 VAL 40 166 ASP 41 167 ARG 42 168 PHE 43 169 TYR 44 170 LYS 45 171 THR 46 172 LEU 47 173 ARG 48 174 ALA 49 175 GLU 50 176 GLN 51 177 ALA 52 178 SER 53 179 GLN 54 180 GLU 55 181 VAL 56 182 LYS 57 183 ASN 58 184 ALA 59 185 ALA 60 186 THR 61 187 GLU 62 188 THR 63 189 LEU 64 190 LEU 65 191 VAL 66 192 GLN 67 193 ASN 68 194 ALA 69 195 ASN 70 196 PRO 71 197 ASP 72 198 CYS 73 199 LYS 74 200 THR 75 201 ILE 76 202 LEU 77 203 LYS 78 204 ALA 79 205 LEU 80 206 GLY 81 207 PRO 82 208 ALA 83 209 ALA 84 210 THR 85 211 LEU 86 212 GLU 87 213 GLU 88 214 MET 89 215 MET 90 216 THR 91 217 ALA 92 218 CYS 93 219 GLN 94 220 GLY 95 221 VAL 96 222 GLY 97 223 GLY 98 224 PRO 99 225 GLY 100 226 HIS 101 227 LYS 102 228 ALA 103 229 ARG 104 230 VAL 105 231 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-04-17 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 15137 "CAC monomer" 80.00 87 98.81 98.81 4.34e-54 BMRB 16555 HIV-1_Capsid_Protein 80.00 88 97.62 97.62 2.61e-53 BMRB 17738 HIV-1_CA 80.00 240 98.81 98.81 3.31e-52 BMRB 19264 entity 80.00 231 98.81 98.81 1.26e-52 BMRB 25532 Gag 80.00 432 97.62 97.62 8.83e-50 PDB 1E6J "Crystal Structure Of Hiv-1 Capsid Protein (p24) In Complex With Fab13b5" 69.52 210 97.26 97.26 2.53e-43 PDB 1VU4 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VU5 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VU6 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VU7 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VU8 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VU9 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUA "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUC "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUD "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUE "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUF "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUG "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUH "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUI "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUJ "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUK "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUL "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUM "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUN "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUO "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUP "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUQ "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUR "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUS "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUT "Atomic-level Structure Of The Entire Hiv-1 Capsid" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUU "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUV "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUW "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUX "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUY "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VUZ "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV0 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV1 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV2 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV3 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV4 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV5 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV6 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV7 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV8 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VV9 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VVA "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VVB "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VVF "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VVG "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VVH "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 1VVI "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 80.00 231 97.62 97.62 6.51e-52 PDB 2JO0 "The Solution Structure Of The Monomeric Species Of The C Terminal Domain Of The Ca Protein Of Hiv-1" 80.00 87 98.81 98.81 4.34e-54 PDB 2JYG "Solution Structure Of The W184aM185A MUTANT OF THE CARBOXY- Terminal Dimerization Domain Of The Hiv-1 Capsid Protein" 80.00 84 98.81 98.81 4.11e-54 PDB 2JYL "Solution Structure Of A Double Mutant Of The Carboxy- Terminal Dimerization Domain Of The Hiv-1 Capsid Protein" 100.00 105 99.05 99.05 9.04e-71 PDB 2KOD "A High-Resolution Nmr Structure Of The Dimeric C-Terminal Domain Of Hiv-1 Ca" 80.00 88 97.62 97.62 2.61e-53 PDB 2L6E "Nmr Structure Of The Monomeric Mutant C-Terminal Domain Of Hiv-1 Capsid In Complex With Stapled Peptide Inhibitor" 100.00 105 100.00 100.00 1.58e-71 PDB 2LF4 "Structure Of A Monomeric Mutant Of The Hiv-1 Capsid Protein" 80.00 240 98.81 98.81 3.31e-52 PDB 2M8P "The Structure Of The W184am185a Mutant Of The Hiv-1 Capsid Protein" 70.48 221 98.65 98.65 1.29e-44 PDB 3GV2 "X-Ray Structure Of Hexameric Hiv-1 Ca" 72.38 342 98.68 98.68 3.86e-43 PDB 3H47 "X-Ray Structure Of Hexameric Hiv-1 Ca" 80.00 231 98.81 98.81 2.60e-52 PDB 3H4E "X-Ray Structure Of Hexameric Hiv-1 Ca" 80.00 231 98.81 98.81 2.60e-52 PDB 3J34 "Structure Of Hiv-1 Capsid Protein By Cryo-em" 80.00 231 97.62 97.62 6.51e-52 PDB 3J4F "Structure Of Hiv-1 Capsid Protein By Cryo-em" 80.00 231 97.62 97.62 6.51e-52 PDB 3MGE "X-Ray Structure Of Hexameric Hiv-1 Ca" 80.00 231 98.81 98.81 2.80e-52 PDB 3NTE "Crystal Structure Of The Wild-type Full-length Hiv-1 Capsid Protein" 70.48 221 97.30 97.30 5.83e-44 PDB 3P05 "X-Ray Structure Of Pentameric Hiv-1 Ca" 80.00 231 98.81 98.81 2.74e-52 PDB 3P0A "X-Ray Structure Of Pentameric Hiv-1 Ca" 80.00 231 98.81 98.81 2.46e-52 PDB 4ARG "Structure Of The Immature Retroviral Capsid At 8a Resolution By Cryo-Electron Microscopy" 65.71 69 98.55 98.55 2.08e-42 PDB 4QNB "Disulfide Stabilized Hiv-1 Ca Hexamer In Complex With Phenyl-l- Phenylalaninamide Inhibitor" 80.00 231 98.81 98.81 2.60e-52 PDB 4U0A "Hexameric Hiv-1 Ca In Complex With Cpsf6 Peptide, P6 Crystal Form" 80.00 231 98.81 98.81 2.60e-52 PDB 4U0B "Hexamer Hiv-1 Ca In Complex With Cpsf6 Peptide, P212121 Crystal Form" 80.00 231 98.81 98.81 2.60e-52 PDB 4U0C "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P6 Crystal Form" 80.00 231 98.81 98.81 2.60e-52 PDB 4U0D "Hexameric Hiv-1 Ca In Complex With Nup153 Peptide, P212121 Crystal Form" 80.00 231 98.81 98.81 2.60e-52 PDB 4U0E "Hexameric Hiv-1 Ca In Complex With Pf3450074" 80.00 231 98.81 98.81 2.60e-52 PDB 4U0F "Hexameric Hiv-1 Ca In Complex With Bi-2" 80.00 231 98.81 98.81 2.60e-52 PDB 4WYM "Structural Basis Of Hiv-1 Capsid Recognition By Cpsf6" 80.00 231 98.81 98.81 2.60e-52 DBJ BAA00992 "gag polyprotein [Human immunodeficiency virus 1]" 80.00 500 97.62 97.62 3.20e-49 DBJ BAA12988 "Gag [Human immunodeficiency virus 1]" 80.00 512 97.62 97.62 4.68e-49 DBJ BAA12996 "Gag [Human immunodeficiency virus 1]" 80.00 512 97.62 97.62 4.49e-49 DBJ BAA93785 "gag protein [Human immunodeficiency virus 1]" 80.00 231 97.62 97.62 6.24e-52 DBJ BAA93786 "gag protein [Human immunodeficiency virus 1]" 80.00 231 97.62 97.62 7.10e-52 EMBL CAA82791 "gag [Human immunodeficiency virus 1]" 77.14 146 97.53 97.53 2.71e-50 EMBL CAA82793 "gag [Human immunodeficiency virus 1]" 77.14 146 97.53 97.53 2.71e-50 EMBL CAB85858 "P24 [Human immunodeficiency virus 1]" 80.00 225 97.62 97.62 8.02e-52 EMBL CAB85866 "P24 [Human immunodeficiency virus 1]" 80.00 221 97.62 97.62 4.60e-52 EMBL CAB87157 "p24 [Human immunodeficiency virus 1]" 75.24 226 97.47 97.47 1.96e-48 GB AAA44201 "gag polyprotein precursor [Human immunodeficiency virus 1]" 80.00 512 97.62 97.62 4.98e-49 GB AAA44306 "gag polyprotein [Human immunodeficiency virus 1]" 79.05 500 97.59 97.59 1.77e-48 GB AAA44652 "gag polyprotein precursor [Human immunodeficiency virus 1]" 80.00 512 97.62 97.62 4.63e-49 GB AAA76686 "gag [Human immunodeficiency virus 1]" 80.00 500 97.62 97.62 4.15e-49 GB AAB04036 "gag [Human immunodeficiency virus 1]" 80.00 500 97.62 97.62 3.78e-49 PIR FOVWLV "gag polyprotein - human immunodeficiency virus type 1 (isolate LAV-1a)" 80.00 500 97.62 97.62 3.74e-49 PRF 1102247B "protein gag" 80.00 512 97.62 97.62 4.98e-49 PRF 1103299C "gag gene" 80.00 478 97.62 97.62 3.09e-49 REF NP_057849 "Gag-Pol [Human immunodeficiency virus 1]" 80.00 1435 97.62 97.62 6.88e-47 REF NP_057850 "Pr55(Gag) [Human immunodeficiency virus 1]" 80.00 500 97.62 97.62 4.07e-49 REF NP_579880 "capsid [Human immunodeficiency virus 1]" 80.00 231 97.62 97.62 5.91e-52 SP P03347 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 80.00 512 97.62 97.62 4.98e-49 SP P03348 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 80.00 512 97.62 97.62 4.68e-49 SP P03366 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 80.00 1447 97.62 97.62 9.30e-47 SP P03367 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 80.00 1447 97.62 97.62 9.30e-47 SP P04585 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 80.00 1435 97.62 97.62 6.88e-47 stop_ save_ save_NYAD-13_Peptide_Inhibitor _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NYAD-13_Peptide_Inhibitor _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 14 _Mol_residue_sequence ITFXDLLXYYGKKK loop_ _Residue_seq_code _Residue_label 1 ILE 2 THR 3 PHE 4 MK8 5 ASP 6 LEU 7 LEU 8 MK8 9 TYR 10 TYR 11 GLY 12 LYS 13 LYS 14 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ###################### # Polymer residues # ###################### save_chem_comp_MK8 _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common 2-METHYL-L-NORLEUCINE _BMRB_code . _PDB_code MK8 _Standard_residue_derivative . _Molecular_mass 145.199 _Mol_paramagnetic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 9 13:49:29 2009 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? N N N . 0 . ? CA CA C . 0 . ? C C C . 0 . ? O O O . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD CD C . 0 . ? CE CE C . 0 . ? OXT OXT O . 0 . ? HC1 HC1 H . 0 . ? HC2 HC2 H . 0 . ? HC3 HC3 H . 0 . ? H H H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG2 HG2 H . 0 . ? HG3 HG3 H . 0 . ? HD2 HD2 H . 0 . ? HD3 HD3 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? HE3 HE3 H . 0 . ? HO1 HO1 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 N ? ? SING C1 HC1 ? ? SING C1 HC2 ? ? SING C1 HC3 ? ? SING N CA ? ? SING N H ? ? SING CA C ? ? SING CA CB ? ? SING CA HA ? ? DOUB C O ? ? SING C OXT ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD ? ? SING CG HG2 ? ? SING CG HG3 ? ? SING CD CE ? ? SING CD HD2 ? ? SING CD HD3 ? ? SING CE HE1 ? ? SING CE HE2 ? ? SING CE HE3 ? ? SING OXT HO1 ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _ICTVdb_decimal_code _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Capsid_protein_p24 HIV-1 00.061.1.06.009. 11676 virus . . . $NYAD-13_Peptide_Inhibitor . . . . . . . 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 $Capsid_protein_p24 'recombinant technology' . . . . pET14b $NYAD-13_Peptide_Inhibitor 'chemical synthesis' . . . . . 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 $Capsid_protein_p24 600 uM '[U-100% 13C; U-100% 15N]' $NYAD-13_Peptide_Inhibitor 900 uM 'natural abundance' DTT 2 mM 'natural abundance' 'ammonium acetate' 100 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Capsid_protein_p24 600 uM '[U-100% 13C; U-100% 15N]' $NYAD-13_Peptide_Inhibitor 900 uM 'natural abundance' DTT 2 mM 'natural abundance' 'ammonium acetate' 100 mM 'natural abundance' D2O 100 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_ARIA _Saveframe_category software _Name ARIA _Version 2.2 loop_ _Vendor _Address _Electronic_address 'Linge, O'Donoghue and Nilges' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CARA _Saveframe_category software _Name CARA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Keller, Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 1.3 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task processing 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 900 _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_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _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_CBCA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-13C_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C NOESY' _Sample_label $sample_2 save_ save_2D_f1,f2_filtered_1H-1H_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D f1,f2 filtered 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_f2_filtered_1H-1H_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D f2 filtered 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _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 temperature 298 . K pH 7.0 . pH pressure 1 . atm 'ionic strength' 100 . mM stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 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_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '2D f1,f2 filtered 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Capsid_protein_p24 _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 1 138 12 SER C C 174.857 0.50 1 2 138 12 SER CA C 58.484 0.50 1 3 138 12 SER CB C 63.629 0.50 1 4 139 13 GLY H H 8.350 0.05 1 5 139 13 GLY HA2 H 3.868 0.05 2 6 139 13 GLY HA3 H 3.868 0.05 2 7 139 13 GLY C C 173.693 0.50 1 8 139 13 GLY CA C 44.887 0.50 1 9 139 13 GLY N N 110.492 0.10 1 10 140 14 LEU H H 7.997 0.05 1 11 140 14 LEU C C 176.969 0.50 1 12 140 14 LEU CA C 54.924 0.50 1 13 140 14 LEU CB C 42.230 0.50 1 14 140 14 LEU N N 121.445 0.10 1 15 141 15 VAL H H 8.053 0.05 1 16 141 15 VAL C C 174.228 0.50 1 17 141 15 VAL CA C 59.845 0.50 1 18 141 15 VAL CB C 32.488 0.50 1 19 141 15 VAL N N 122.487 0.10 1 20 142 16 PRO HA H 4.304 0.05 1 21 142 16 PRO HB2 H 1.774 0.05 2 22 142 16 PRO HB3 H 2.181 0.05 2 23 142 16 PRO C C 176.712 0.50 1 24 142 16 PRO CA C 62.802 0.50 1 25 142 16 PRO CB C 31.889 0.50 1 26 143 17 ARG H H 8.447 0.05 1 27 143 17 ARG C C 176.899 0.50 1 28 143 17 ARG CA C 56.302 0.50 1 29 143 17 ARG CB C 30.520 0.50 1 30 143 17 ARG N N 121.958 0.10 1 31 144 18 GLY H H 8.442 0.05 1 32 144 18 GLY C C 173.971 0.50 1 33 144 18 GLY CA C 45.084 0.50 1 34 144 18 GLY N N 110.366 0.10 1 35 145 19 SER H H 8.182 0.05 1 36 145 19 SER C C 174.142 0.50 1 37 145 19 SER CA C 58.298 0.50 1 38 145 19 SER CB C 63.838 0.50 1 39 145 19 SER N N 115.802 0.10 1 40 147 21 MET HA H 4.326 0.05 1 41 147 21 MET HB2 H 1.887 0.05 2 42 147 21 MET HB3 H 1.927 0.05 2 43 147 21 MET HG2 H 2.259 0.05 2 44 147 21 MET C C 174.721 0.50 1 45 147 21 MET CA C 55.469 0.50 1 46 147 21 MET CB C 27.140 0.50 1 47 148 22 THR H H 8.160 0.05 1 48 148 22 THR HA H 4.142 0.05 1 49 148 22 THR HB H 4.011 0.05 1 50 148 22 THR HG2 H 1.077 0.05 1 51 148 22 THR C C 174.828 0.50 1 52 148 22 THR CA C 62.899 0.50 1 53 148 22 THR CB C 69.806 0.50 1 54 148 22 THR CG2 C 21.971 0.50 1 55 148 22 THR N N 115.799 0.10 1 56 149 23 SER H H 8.679 0.05 1 57 149 23 SER HA H 4.377 0.05 1 58 149 23 SER HB2 H 3.627 0.05 2 59 149 23 SER HB3 H 3.821 0.05 2 60 149 23 SER C C 176.841 0.50 1 61 149 23 SER CA C 58.503 0.50 1 62 149 23 SER CB C 64.096 0.50 1 63 149 23 SER N N 119.924 0.10 1 64 150 24 ILE H H 8.420 0.05 1 65 150 24 ILE HA H 3.901 0.05 1 66 150 24 ILE HB H 1.347 0.05 1 67 150 24 ILE HG12 H 0.587 0.05 2 68 150 24 ILE HG13 H 0.971 0.05 2 69 150 24 ILE HG2 H 0.609 0.05 1 70 150 24 ILE HD1 H -0.160 0.05 1 71 150 24 ILE C C 175.063 0.50 1 72 150 24 ILE CA C 59.515 0.50 1 73 150 24 ILE CB C 39.192 0.50 1 74 150 24 ILE CG1 C 28.770 0.50 1 75 150 24 ILE CG2 C 18.881 0.50 1 76 150 24 ILE CD1 C 14.811 0.50 1 77 150 24 ILE N N 123.568 0.10 1 78 151 25 LEU H H 7.290 0.05 1 79 151 25 LEU HA H 3.861 0.05 1 80 151 25 LEU HB2 H 1.426 0.05 2 81 151 25 LEU HB3 H 1.532 0.05 2 82 151 25 LEU HG H 1.496 0.05 1 83 151 25 LEU HD1 H 0.792 0.05 2 84 151 25 LEU HD2 H 0.798 0.05 2 85 151 25 LEU C C 177.612 0.50 1 86 151 25 LEU CA C 56.972 0.50 1 87 151 25 LEU CB C 41.727 0.50 1 88 151 25 LEU CG C 27.342 0.50 1 89 151 25 LEU CD1 C 23.151 0.50 2 90 151 25 LEU CD2 C 25.247 0.50 2 91 151 25 LEU N N 119.449 0.10 1 92 152 26 ASP H H 7.434 0.05 1 93 152 26 ASP HA H 4.642 0.05 1 94 152 26 ASP HB2 H 2.528 0.05 2 95 152 26 ASP HB3 H 2.826 0.05 2 96 152 26 ASP C C 175.941 0.50 1 97 152 26 ASP CA C 53.940 0.50 1 98 152 26 ASP CB C 41.918 0.50 1 99 152 26 ASP N N 114.499 0.10 1 100 153 27 ILE H H 7.292 0.05 1 101 153 27 ILE HA H 4.096 0.05 1 102 153 27 ILE HB H 2.316 0.05 1 103 153 27 ILE HG12 H 1.167 0.05 2 104 153 27 ILE HG13 H 1.657 0.05 2 105 153 27 ILE HG2 H 0.895 0.05 1 106 153 27 ILE HD1 H 0.590 0.05 1 107 153 27 ILE C C 173.436 0.50 1 108 153 27 ILE CA C 59.353 0.50 1 109 153 27 ILE CB C 34.367 0.50 1 110 153 27 ILE CG1 C 27.021 0.50 1 111 153 27 ILE CG2 C 16.869 0.50 1 112 153 27 ILE CD1 C 9.753 0.50 1 113 153 27 ILE N N 121.966 0.10 1 114 154 28 ARG H H 8.288 0.05 1 115 154 28 ARG HA H 4.850 0.05 1 116 154 28 ARG HB2 H 1.598 0.05 2 117 154 28 ARG HB3 H 1.772 0.05 2 118 154 28 ARG HG2 H 1.446 0.05 2 119 154 28 ARG HG3 H 1.439 0.05 2 120 154 28 ARG HD2 H 3.109 0.05 2 121 154 28 ARG HD3 H 3.148 0.05 2 122 154 28 ARG C C 175.513 0.50 1 123 154 28 ARG CA C 53.826 0.50 1 124 154 28 ARG CB C 33.044 0.50 1 125 154 28 ARG CG C 27.008 0.50 1 126 154 28 ARG CD C 43.263 0.50 1 127 154 28 ARG N N 125.105 0.10 1 128 155 29 GLN H H 7.726 0.05 1 129 155 29 GLN HA H 3.882 0.05 1 130 155 29 GLN HB2 H 0.126 0.05 2 131 155 29 GLN HB3 H 1.757 0.05 2 132 155 29 GLN HG2 H 3.121 0.05 2 133 155 29 GLN HG3 H 2.097 0.05 2 134 155 29 GLN HE21 H 6.654 0.05 2 135 155 29 GLN HE22 H 7.606 0.05 2 136 155 29 GLN C C 177.055 0.50 1 137 155 29 GLN CA C 55.955 0.50 1 138 155 29 GLN CB C 27.520 0.50 1 139 155 29 GLN CG C 32.815 0.50 1 140 155 29 GLN N N 127.515 0.10 1 141 155 29 GLN NE2 N 108.264 0.10 1 142 156 30 GLY H H 9.826 0.05 1 143 156 30 GLY HA2 H 3.915 0.05 2 144 156 30 GLY HA3 H 4.322 0.05 2 145 156 30 GLY C C 173.350 0.50 1 146 156 30 GLY CA C 45.079 0.50 1 147 156 30 GLY N N 116.820 0.10 1 148 157 31 PRO HA H 4.199 0.05 1 149 157 31 PRO HB2 H 1.932 0.05 2 150 157 31 PRO HB3 H 2.399 0.05 2 151 157 31 PRO HG2 H 2.024 0.05 2 152 157 31 PRO HG3 H 2.096 0.05 2 153 157 31 PRO HD2 H 4.243 0.05 2 154 157 31 PRO HD3 H 3.761 0.05 2 155 157 31 PRO C C 176.844 0.50 1 156 157 31 PRO CA C 65.616 0.50 1 157 157 31 PRO CB C 32.104 0.50 1 158 157 31 PRO CG C 27.564 0.50 1 159 157 31 PRO CD C 51.636 0.50 1 160 158 32 LYS H H 8.488 0.05 1 161 158 32 LYS HA H 4.489 0.05 1 162 158 32 LYS HB2 H 1.524 0.05 2 163 158 32 LYS HB3 H 2.036 0.05 2 164 158 32 LYS HG2 H 1.257 0.05 2 165 158 32 LYS HG3 H 1.288 0.05 2 166 158 32 LYS HD2 H 1.632 0.05 2 167 158 32 LYS HD3 H 1.642 0.05 2 168 158 32 LYS HE2 H 2.908 0.05 2 169 158 32 LYS HE3 H 2.908 0.05 2 170 158 32 LYS C C 175.534 0.50 1 171 158 32 LYS CA C 53.921 0.50 1 172 158 32 LYS CB C 32.594 0.50 1 173 158 32 LYS CG C 24.973 0.50 1 174 158 32 LYS CD C 28.876 0.50 1 175 158 32 LYS CE C 42.101 0.50 1 176 158 32 LYS N N 114.885 0.10 1 177 159 33 GLU H H 6.961 0.05 1 178 159 33 GLU HA H 4.522 0.05 1 179 159 33 GLU HB2 H 1.779 0.05 2 180 159 33 GLU HB3 H 2.198 0.05 2 181 159 33 GLU HG2 H 2.310 0.05 2 182 159 33 GLU HG3 H 2.597 0.05 2 183 159 33 GLU C C 174.549 0.50 1 184 159 33 GLU CA C 53.426 0.50 1 185 159 33 GLU CB C 32.085 0.50 1 186 159 33 GLU CG C 34.646 0.50 1 187 159 33 GLU N N 125.703 0.10 1 188 160 34 PRO HA H 4.382 0.05 1 189 160 34 PRO HB2 H 1.813 0.05 2 190 160 34 PRO HB3 H 2.499 0.05 2 191 160 34 PRO HG2 H 1.946 0.05 2 192 160 34 PRO HG3 H 2.174 0.05 2 193 160 34 PRO HD2 H 3.765 0.05 2 194 160 34 PRO HD3 H 4.246 0.05 2 195 160 34 PRO C C 177.313 0.50 1 196 160 34 PRO CA C 63.553 0.50 1 197 160 34 PRO CB C 32.608 0.50 1 198 160 34 PRO CG C 28.462 0.50 1 199 160 34 PRO CD C 51.893 0.50 1 200 161 35 PHE H H 9.499 0.05 1 201 161 35 PHE HA H 4.431 0.05 1 202 161 35 PHE HB2 H 2.924 0.05 2 203 161 35 PHE HB3 H 3.505 0.05 2 204 161 35 PHE HD1 H 7.256 0.05 1 205 161 35 PHE HD2 H 7.256 0.05 1 206 161 35 PHE HE1 H 6.889 0.05 1 207 161 35 PHE HE2 H 6.889 0.05 1 208 161 35 PHE HZ H 6.784 0.05 1 209 161 35 PHE C C 176.732 0.50 1 210 161 35 PHE CA C 63.050 0.50 1 211 161 35 PHE CB C 39.705 0.50 1 212 161 35 PHE CD1 C 131.826 0.50 3 213 161 35 PHE CE1 C 131.292 0.50 3 214 161 35 PHE CZ C 129.364 0.50 1 215 161 35 PHE N N 128.653 0.10 1 216 162 36 ARG H H 9.056 0.05 1 217 162 36 ARG HA H 3.662 0.05 1 218 162 36 ARG HB2 H 1.727 0.05 2 219 162 36 ARG HB3 H 1.913 0.05 2 220 162 36 ARG HG2 H 1.703 0.05 2 221 162 36 ARG HG3 H 1.636 0.05 2 222 162 36 ARG HD2 H 3.208 0.05 2 223 162 36 ARG HD3 H 3.225 0.05 2 224 162 36 ARG C C 177.526 0.50 1 225 162 36 ARG CA C 59.550 0.50 1 226 162 36 ARG CB C 30.055 0.50 1 227 162 36 ARG CG C 27.102 0.50 1 228 162 36 ARG CD C 43.391 0.50 1 229 162 36 ARG N N 115.338 0.10 1 230 163 37 ASP H H 6.961 0.05 1 231 163 37 ASP HA H 4.420 0.05 1 232 163 37 ASP HB2 H 2.855 0.05 2 233 163 37 ASP HB3 H 2.855 0.05 2 234 163 37 ASP C C 177.783 0.50 1 235 163 37 ASP CA C 56.976 0.50 1 236 163 37 ASP CB C 40.215 0.50 1 237 163 37 ASP N N 119.761 0.10 1 238 164 38 TYR H H 7.491 0.05 1 239 164 38 TYR HA H 4.345 0.05 1 240 164 38 TYR HB2 H 2.814 0.05 2 241 164 38 TYR HB3 H 3.141 0.05 2 242 164 38 TYR HD1 H 6.483 0.05 3 243 164 38 TYR HD2 H 6.762 0.05 3 244 164 38 TYR HE1 H 6.461 0.05 3 245 164 38 TYR HE2 H 6.571 0.05 3 246 164 38 TYR HH H 9.331 0.05 1 247 164 38 TYR C C 176.070 0.50 1 248 164 38 TYR CA C 59.514 0.50 1 249 164 38 TYR CB C 38.318 0.50 1 250 164 38 TYR CD1 C 134.024 0.50 3 251 164 38 TYR CD2 C 131.818 0.50 3 252 164 38 TYR CE1 C 115.754 0.50 3 253 164 38 TYR CE2 C 117.865 0.50 3 254 164 38 TYR N N 124.282 0.10 1 255 165 39 VAL H H 8.123 0.05 1 256 165 39 VAL HA H 2.627 0.05 1 257 165 39 VAL HB H 1.508 0.05 1 258 165 39 VAL HG1 H 0.701 0.05 2 259 165 39 VAL HG2 H -0.099 0.05 2 260 165 39 VAL C C 177.119 0.50 1 261 165 39 VAL CA C 66.643 0.50 1 262 165 39 VAL CB C 30.586 0.50 1 263 165 39 VAL CG1 C 22.135 0.50 2 264 165 39 VAL CG2 C 23.466 0.50 2 265 165 39 VAL N N 119.770 0.10 1 266 166 40 ASP H H 7.368 0.05 1 267 166 40 ASP HA H 4.327 0.05 1 268 166 40 ASP HB2 H 2.730 0.05 2 269 166 40 ASP HB3 H 2.867 0.05 2 270 166 40 ASP C C 177.933 0.50 1 271 166 40 ASP CA C 58.019 0.50 1 272 166 40 ASP CB C 41.744 0.50 1 273 166 40 ASP N N 118.631 0.10 1 274 167 41 ARG H H 7.692 0.05 1 275 167 41 ARG HA H 3.957 0.05 1 276 167 41 ARG HB2 H 1.721 0.05 2 277 167 41 ARG HB3 H 2.025 0.05 2 278 167 41 ARG HG2 H 1.488 0.05 2 279 167 41 ARG HG3 H 1.968 0.05 2 280 167 41 ARG HD2 H 3.218 0.05 2 281 167 41 ARG HD3 H 3.302 0.05 2 282 167 41 ARG HE H 9.335 0.05 1 283 167 41 ARG C C 179.304 0.50 1 284 167 41 ARG CA C 60.222 0.50 1 285 167 41 ARG CB C 30.583 0.50 1 286 167 41 ARG CG C 28.964 0.50 1 287 167 41 ARG CD C 43.662 0.50 1 288 167 41 ARG N N 117.887 0.10 1 289 167 41 ARG NE N 110.375 0.10 1 290 168 42 PHE H H 8.827 0.05 1 291 168 42 PHE HA H 3.524 0.05 1 292 168 42 PHE HB2 H 2.276 0.05 2 293 168 42 PHE HB3 H 3.063 0.05 2 294 168 42 PHE HD1 H 6.835 0.05 1 295 168 42 PHE HD2 H 6.835 0.05 1 296 168 42 PHE HE1 H 7.259 0.05 1 297 168 42 PHE HE2 H 7.259 0.05 1 298 168 42 PHE HZ H 7.066 0.05 1 299 168 42 PHE C C 176.563 0.50 1 300 168 42 PHE CA C 62.058 0.50 1 301 168 42 PHE CB C 39.765 0.50 1 302 168 42 PHE CD1 C 132.043 0.50 3 303 168 42 PHE CE1 C 131.884 0.50 3 304 168 42 PHE CZ C 128.642 0.50 1 305 168 42 PHE N N 125.379 0.10 1 306 169 43 TYR H H 9.333 0.05 1 307 169 43 TYR HA H 4.119 0.05 1 308 169 43 TYR HB2 H 2.996 0.05 2 309 169 43 TYR HB3 H 3.102 0.05 2 310 169 43 TYR HD1 H 6.600 0.05 1 311 169 43 TYR HD2 H 6.600 0.05 1 312 169 43 TYR HE1 H 6.198 0.05 1 313 169 43 TYR HE2 H 6.198 0.05 1 314 169 43 TYR C C 176.648 0.50 1 315 169 43 TYR CA C 61.210 0.50 1 316 169 43 TYR CB C 38.669 0.50 1 317 169 43 TYR CD1 C 133.463 0.50 3 318 169 43 TYR CE1 C 117.170 0.50 3 319 169 43 TYR N N 118.920 0.10 1 320 170 44 LYS H H 8.474 0.05 1 321 170 44 LYS HA H 3.162 0.05 1 322 170 44 LYS HB2 H 1.606 0.05 2 323 170 44 LYS HB3 H 1.717 0.05 2 324 170 44 LYS HG2 H 1.151 0.05 2 325 170 44 LYS HG3 H 1.512 0.05 2 326 170 44 LYS HD2 H 1.462 0.05 2 327 170 44 LYS HE2 H 2.835 0.05 2 328 170 44 LYS HE3 H 2.835 0.05 2 329 170 44 LYS C C 179.797 0.50 1 330 170 44 LYS CA C 60.036 0.50 1 331 170 44 LYS CB C 32.321 0.50 1 332 170 44 LYS CG C 26.510 0.50 1 333 170 44 LYS CD C 29.394 0.50 1 334 170 44 LYS CE C 42.020 0.50 1 335 170 44 LYS N N 118.073 0.10 1 336 171 45 THR H H 7.697 0.05 1 337 171 45 THR HA H 3.688 0.05 1 338 171 45 THR HB H 3.883 0.05 1 339 171 45 THR HG2 H 0.812 0.05 1 340 171 45 THR C C 175.920 0.50 1 341 171 45 THR CA C 66.635 0.50 1 342 171 45 THR CB C 68.111 0.50 1 343 171 45 THR CG2 C 20.690 0.50 1 344 171 45 THR N N 116.102 0.10 1 345 172 46 LEU H H 8.154 0.05 1 346 172 46 LEU HA H 3.735 0.05 1 347 172 46 LEU HB2 H 1.270 0.05 2 348 172 46 LEU HB3 H 1.400 0.05 2 349 172 46 LEU HG H 1.151 0.05 1 350 172 46 LEU HD1 H 0.661 0.05 2 351 172 46 LEU HD2 H 0.814 0.05 2 352 172 46 LEU C C 179.489 0.50 1 353 172 46 LEU CA C 56.978 0.50 1 354 172 46 LEU CB C 42.230 0.50 1 355 172 46 LEU CG C 26.510 0.50 1 356 172 46 LEU CD1 C 24.984 0.50 2 357 172 46 LEU CD2 C 27.012 0.50 2 358 172 46 LEU N N 121.910 0.10 1 359 173 47 ARG H H 8.907 0.05 1 360 173 47 ARG HA H 3.699 0.05 1 361 173 47 ARG HB2 H 1.450 0.05 2 362 173 47 ARG HB3 H 1.450 0.05 2 363 173 47 ARG HG2 H 1.396 0.05 2 364 173 47 ARG HG3 H 1.395 0.05 2 365 173 47 ARG HD2 H 2.632 0.05 2 366 173 47 ARG HD3 H 2.907 0.05 2 367 173 47 ARG C C 176.263 0.50 1 368 173 47 ARG CA C 59.510 0.50 1 369 173 47 ARG CB C 29.459 0.50 1 370 173 47 ARG CG C 26.675 0.50 1 371 173 47 ARG CD C 43.270 0.50 1 372 173 47 ARG N N 119.050 0.10 1 373 174 48 ALA H H 6.717 0.05 1 374 174 48 ALA HA H 4.087 0.05 1 375 174 48 ALA HB H 1.334 0.05 1 376 174 48 ALA C C 177.698 0.50 1 377 174 48 ALA CA C 52.911 0.50 1 378 174 48 ALA CB C 19.303 0.50 1 379 174 48 ALA N N 118.213 0.10 1 380 175 49 GLU H H 6.965 0.05 1 381 175 49 GLU HA H 4.016 0.05 1 382 175 49 GLU HB2 H 1.743 0.05 2 383 175 49 GLU HB3 H 1.853 0.05 2 384 175 49 GLU HG2 H 2.061 0.05 2 385 175 49 GLU HG3 H 2.165 0.05 2 386 175 49 GLU C C 176.413 0.50 1 387 175 49 GLU CA C 56.696 0.50 1 388 175 49 GLU CB C 30.315 0.50 1 389 175 49 GLU CG C 35.900 0.50 1 390 175 49 GLU N N 118.654 0.10 1 391 176 50 GLN H H 8.676 0.05 1 392 176 50 GLN HA H 4.287 0.05 1 393 176 50 GLN HB2 H 1.896 0.05 2 394 176 50 GLN HB3 H 1.969 0.05 2 395 176 50 GLN HG2 H 2.260 0.05 2 396 176 50 GLN HG3 H 2.225 0.05 2 397 176 50 GLN HE21 H 6.749 0.05 2 398 176 50 GLN HE22 H 7.371 0.05 2 399 176 50 GLN C C 173.950 0.50 1 400 176 50 GLN CA C 54.959 0.50 1 401 176 50 GLN CB C 27.075 0.50 1 402 176 50 GLN CG C 33.621 0.50 1 403 176 50 GLN N N 124.161 0.10 1 404 176 50 GLN NE2 N 112.537 0.10 1 405 177 51 ALA H H 7.438 0.05 1 406 177 51 ALA HA H 4.422 0.05 1 407 177 51 ALA HB H 1.153 0.05 1 408 177 51 ALA C C 175.449 0.50 1 409 177 51 ALA CA C 50.877 0.50 1 410 177 51 ALA CB C 21.933 0.50 1 411 177 51 ALA N N 125.232 0.10 1 412 178 52 SER H H 8.499 0.05 1 413 178 52 SER HA H 4.303 0.05 1 414 178 52 SER HB2 H 3.981 0.05 2 415 178 52 SER HB3 H 4.329 0.05 2 416 178 52 SER C C 174.607 0.50 1 417 178 52 SER CA C 57.433 0.50 1 418 178 52 SER CB C 64.863 0.50 1 419 178 52 SER N N 115.865 0.10 1 420 179 53 GLN H H 9.036 0.05 1 421 179 53 GLN HA H 3.712 0.05 1 422 179 53 GLN HB2 H 2.061 0.05 2 423 179 53 GLN HB3 H 2.171 0.05 2 424 179 53 GLN HG2 H 2.446 0.05 2 425 179 53 GLN HG3 H 2.469 0.05 2 426 179 53 GLN HE21 H 6.538 0.05 2 427 179 53 GLN HE22 H 7.756 0.05 2 428 179 53 GLN C C 177.848 0.50 1 429 179 53 GLN CA C 59.756 0.50 1 430 179 53 GLN CB C 28.542 0.50 1 431 179 53 GLN CG C 34.124 0.50 1 432 179 53 GLN N N 121.381 0.10 1 433 179 53 GLN NE2 N 111.339 0.10 1 434 180 54 GLU H H 8.859 0.05 1 435 180 54 GLU HA H 4.081 0.05 1 436 180 54 GLU HB2 H 1.944 0.05 2 437 180 54 GLU HB3 H 2.062 0.05 2 438 180 54 GLU HG2 H 2.277 0.05 2 439 180 54 GLU HG3 H 2.392 0.05 2 440 180 54 GLU C C 179.732 0.50 1 441 180 54 GLU CA C 60.527 0.50 1 442 180 54 GLU CB C 29.030 0.50 1 443 180 54 GLU CG C 36.892 0.50 1 444 180 54 GLU N N 118.202 0.10 1 445 181 55 VAL H H 7.488 0.05 1 446 181 55 VAL HA H 3.670 0.05 1 447 181 55 VAL HB H 2.078 0.05 1 448 181 55 VAL HG1 H 0.779 0.05 2 449 181 55 VAL HG2 H 0.936 0.05 2 450 181 55 VAL C C 178.897 0.50 1 451 181 55 VAL CA C 66.241 0.50 1 452 181 55 VAL CB C 31.311 0.50 1 453 181 55 VAL CG1 C 21.138 0.50 2 454 181 55 VAL CG2 C 23.456 0.50 2 455 181 55 VAL N N 122.732 0.10 1 456 182 56 LYS H H 8.043 0.05 1 457 182 56 LYS HA H 3.718 0.05 1 458 182 56 LYS HB2 H 0.851 0.05 2 459 182 56 LYS HB3 H 1.429 0.05 2 460 182 56 LYS HG2 H 0.486 0.05 2 461 182 56 LYS HG3 H 1.396 0.05 2 462 182 56 LYS HD2 H 0.285 0.05 2 463 182 56 LYS HD3 H 0.844 0.05 2 464 182 56 LYS HE2 H 2.385 0.05 2 465 182 56 LYS HE3 H 2.841 0.05 2 466 182 56 LYS C C 179.690 0.50 1 467 182 56 LYS CA C 61.036 0.50 1 468 182 56 LYS CB C 32.066 0.50 1 469 182 56 LYS CG C 27.051 0.50 1 470 182 56 LYS CD C 29.553 0.50 1 471 182 56 LYS CE C 42.803 0.50 1 472 182 56 LYS N N 120.099 0.10 1 473 183 57 ASN H H 9.126 0.05 1 474 183 57 ASN HA H 4.545 0.05 1 475 183 57 ASN HB2 H 3.000 0.05 2 476 183 57 ASN HB3 H 3.143 0.05 2 477 183 57 ASN HD21 H 7.100 0.05 2 478 183 57 ASN HD22 H 7.863 0.05 2 479 183 57 ASN C C 176.391 0.50 1 480 183 57 ASN CA C 57.089 0.50 1 481 183 57 ASN CB C 37.710 0.50 1 482 183 57 ASN N N 121.279 0.10 1 483 183 57 ASN ND2 N 111.822 0.10 1 484 184 58 ALA H H 7.874 0.05 1 485 184 58 ALA HA H 4.274 0.05 1 486 184 58 ALA HB H 1.484 0.05 1 487 184 58 ALA C C 180.546 0.50 1 488 184 58 ALA CA C 55.333 0.50 1 489 184 58 ALA CB C 17.881 0.50 1 490 184 58 ALA N N 123.274 0.10 1 491 185 59 ALA H H 8.301 0.05 1 492 185 59 ALA HA H 4.084 0.05 1 493 185 59 ALA HB H 1.421 0.05 1 494 185 59 ALA C C 179.497 0.50 1 495 185 59 ALA CA C 54.983 0.50 1 496 185 59 ALA CB C 18.389 0.50 1 497 185 59 ALA N N 120.391 0.10 1 498 186 60 THR H H 8.006 0.05 1 499 186 60 THR HA H 4.299 0.05 1 500 186 60 THR HB H 3.971 0.05 1 501 186 60 THR HG2 H 0.999 0.05 1 502 186 60 THR C C 175.941 0.50 1 503 186 60 THR CA C 69.162 0.50 1 504 186 60 THR CB C 68.652 0.50 1 505 186 60 THR CG2 C 21.936 0.50 1 506 186 60 THR N N 115.081 0.10 1 507 187 61 GLU H H 8.356 0.05 1 508 187 61 GLU HA H 4.271 0.05 1 509 187 61 GLU HB2 H 2.049 0.05 2 510 187 61 GLU HB3 H 2.211 0.05 2 511 187 61 GLU HG2 H 2.346 0.05 2 512 187 61 GLU HG3 H 2.400 0.05 2 513 187 61 GLU C C 178.362 0.50 1 514 187 61 GLU CA C 59.380 0.50 1 515 187 61 GLU CB C 30.581 0.50 1 516 187 61 GLU CG C 36.665 0.50 1 517 187 61 GLU N N 120.496 0.10 1 518 188 62 THR H H 7.735 0.05 1 519 188 62 THR HA H 4.333 0.05 1 520 188 62 THR HB H 4.056 0.05 1 521 188 62 THR HG2 H 1.191 0.05 1 522 188 62 THR C C 176.177 0.50 1 523 188 62 THR CA C 64.175 0.50 1 524 188 62 THR CB C 70.594 0.50 1 525 188 62 THR CG2 C 21.930 0.50 1 526 188 62 THR N N 109.398 0.10 1 527 189 63 LEU H H 8.307 0.05 1 528 189 63 LEU HA H 4.307 0.05 1 529 189 63 LEU HB2 H 1.769 0.05 2 530 189 63 LEU HB3 H 2.219 0.05 2 531 189 63 LEU HG H 1.861 0.05 1 532 189 63 LEU HD1 H 0.803 0.05 2 533 189 63 LEU HD2 H 0.811 0.05 2 534 189 63 LEU C C 177.505 0.50 1 535 189 63 LEU CA C 57.442 0.50 1 536 189 63 LEU CB C 42.758 0.50 1 537 189 63 LEU CD1 C 22.246 0.50 2 538 189 63 LEU CD2 C 27.002 0.50 2 539 189 63 LEU N N 119.343 0.10 1 540 190 64 LEU H H 7.154 0.05 1 541 190 64 LEU HA H 3.457 0.05 1 542 190 64 LEU HB2 H 0.741 0.05 2 543 190 64 LEU HB3 H 1.580 0.05 2 544 190 64 LEU HG H 0.973 0.05 1 545 190 64 LEU HD1 H -0.113 0.05 2 546 190 64 LEU HD2 H 0.503 0.05 2 547 190 64 LEU C C 179.668 0.50 1 548 190 64 LEU CA C 59.519 0.50 1 549 190 64 LEU CB C 41.431 0.50 1 550 190 64 LEU CG C 27.016 0.50 1 551 190 64 LEU CD1 C 23.960 0.50 2 552 190 64 LEU CD2 C 25.494 0.50 2 553 190 64 LEU N N 119.351 0.10 1 554 191 65 VAL H H 8.198 0.05 1 555 191 65 VAL HA H 3.600 0.05 1 556 191 65 VAL HB H 1.888 0.05 1 557 191 65 VAL HG1 H 0.787 0.05 2 558 191 65 VAL HG2 H 0.885 0.05 2 559 191 65 VAL C C 177.226 0.50 1 560 191 65 VAL CA C 65.834 0.50 1 561 191 65 VAL CB C 31.597 0.50 1 562 191 65 VAL CG1 C 21.455 0.50 2 563 191 65 VAL CG2 C 22.686 0.50 2 564 191 65 VAL N N 116.234 0.10 1 565 192 66 GLN H H 7.483 0.05 1 566 192 66 GLN HA H 3.786 0.05 1 567 192 66 GLN HB2 H 1.942 0.05 2 568 192 66 GLN HB3 H 2.152 0.05 2 569 192 66 GLN HG2 H 2.333 0.05 2 570 192 66 GLN HG3 H 2.433 0.05 2 571 192 66 GLN HE21 H 6.778 0.05 2 572 192 66 GLN HE22 H 7.476 0.05 2 573 192 66 GLN C C 177.141 0.50 1 574 192 66 GLN CA C 59.346 0.50 1 575 192 66 GLN CB C 29.525 0.50 1 576 192 66 GLN CG C 34.122 0.50 1 577 192 66 GLN N N 117.020 0.10 1 578 192 66 GLN NE2 N 111.411 0.10 1 579 193 67 ASN H H 8.148 0.05 1 580 193 67 ASN HA H 4.890 0.05 1 581 193 67 ASN HB2 H 3.510 0.05 2 582 193 67 ASN HB3 H 3.515 0.05 2 583 193 67 ASN HD21 H 6.437 0.05 2 584 193 67 ASN HD22 H 7.963 0.05 2 585 193 67 ASN C C 175.299 0.50 1 586 193 67 ASN CA C 52.858 0.50 1 587 193 67 ASN CB C 37.686 0.50 1 588 193 67 ASN N N 114.759 0.10 1 589 193 67 ASN ND2 N 109.661 0.10 1 590 194 68 ALA H H 7.246 0.05 1 591 194 68 ALA HA H 4.175 0.05 1 592 194 68 ALA HB H 1.522 0.05 1 593 194 68 ALA C C 175.513 0.50 1 594 194 68 ALA CA C 51.899 0.50 1 595 194 68 ALA CB C 18.885 0.50 1 596 194 68 ALA N N 124.657 0.10 1 597 195 69 ASN H H 9.040 0.05 1 598 195 69 ASN HA H 4.544 0.05 1 599 195 69 ASN HB2 H 2.202 0.05 2 600 195 69 ASN HB3 H 3.161 0.05 2 601 195 69 ASN HD21 H 6.938 0.05 2 602 195 69 ASN HD22 H 7.543 0.05 2 603 195 69 ASN C C 172.686 0.50 1 604 195 69 ASN CA C 51.456 0.50 1 605 195 69 ASN CB C 35.636 0.50 1 606 195 69 ASN N N 119.360 0.10 1 607 195 69 ASN ND2 N 111.454 0.10 1 608 196 70 PRO HA H 4.042 0.05 1 609 196 70 PRO HB2 H 1.793 0.05 2 610 196 70 PRO HB3 H 2.324 0.05 2 611 196 70 PRO HG2 H 1.927 0.05 2 612 196 70 PRO HG3 H 2.109 0.05 2 613 196 70 PRO HD2 H 3.749 0.05 2 614 196 70 PRO HD3 H 3.811 0.05 2 615 196 70 PRO C C 178.850 0.50 1 616 196 70 PRO CA C 66.639 0.50 1 617 196 70 PRO CB C 32.259 0.50 1 618 196 70 PRO CG C 27.667 0.50 1 619 196 70 PRO CD C 49.778 0.50 1 620 197 71 ASP H H 7.646 0.05 1 621 197 71 ASP HA H 4.320 0.05 1 622 197 71 ASP HB2 H 2.481 0.05 2 623 197 71 ASP HB3 H 2.485 0.05 2 624 197 71 ASP C C 179.132 0.50 1 625 197 71 ASP CA C 57.459 0.50 1 626 197 71 ASP CB C 41.237 0.50 1 627 197 71 ASP N N 115.358 0.10 1 628 198 72 CYS H H 8.529 0.05 1 629 198 72 CYS HA H 4.195 0.05 1 630 198 72 CYS HB2 H 2.478 0.05 2 631 198 72 CYS HB3 H 3.193 0.05 2 632 198 72 CYS C C 176.244 0.50 1 633 198 72 CYS CA C 63.683 0.50 1 634 198 72 CYS CB C 27.773 0.50 1 635 198 72 CYS N N 116.452 0.10 1 636 199 73 LYS H H 9.482 0.05 1 637 199 73 LYS HA H 3.595 0.05 1 638 199 73 LYS HB2 H 1.652 0.05 2 639 199 73 LYS HB3 H 1.743 0.05 2 640 199 73 LYS HG2 H 1.288 0.05 2 641 199 73 LYS HG3 H 1.384 0.05 2 642 199 73 LYS HD2 H 1.603 0.05 2 643 199 73 LYS HD3 H 1.601 0.05 2 644 199 73 LYS HE2 H 2.922 0.05 2 645 199 73 LYS HE3 H 2.939 0.05 2 646 199 73 LYS C C 178.040 0.50 1 647 199 73 LYS CA C 61.551 0.50 1 648 199 73 LYS CB C 32.361 0.50 1 649 199 73 LYS CG C 25.520 0.50 1 650 199 73 LYS CD C 29.530 0.50 1 651 199 73 LYS CE C 42.250 0.50 1 652 199 73 LYS N N 121.822 0.10 1 653 200 74 THR H H 7.530 0.05 1 654 200 74 THR HA H 3.713 0.05 1 655 200 74 THR HB H 4.110 0.05 1 656 200 74 THR HG2 H 1.166 0.05 1 657 200 74 THR C C 178.044 0.50 1 658 200 74 THR CA C 66.651 0.50 1 659 200 74 THR CB C 68.800 0.50 1 660 200 74 THR CG2 C 21.377 0.50 1 661 200 74 THR N N 113.304 0.10 1 662 201 75 ILE H H 6.716 0.05 1 663 201 75 ILE HA H 3.566 0.05 1 664 201 75 ILE HB H 1.784 0.05 1 665 201 75 ILE HG12 H 0.998 0.05 2 666 201 75 ILE HG13 H 1.612 0.05 2 667 201 75 ILE HG2 H 0.644 0.05 1 668 201 75 ILE HD1 H 0.799 0.05 1 669 201 75 ILE C C 178.190 0.50 1 670 201 75 ILE CA C 64.584 0.50 1 671 201 75 ILE CB C 38.685 0.50 1 672 201 75 ILE CG1 C 29.066 0.50 1 673 201 75 ILE CG2 C 18.538 0.50 1 674 201 75 ILE CD1 C 14.199 0.50 1 675 201 75 ILE N N 122.676 0.10 1 676 202 76 LEU H H 8.529 0.05 1 677 202 76 LEU HA H 3.666 0.05 1 678 202 76 LEU HB2 H 1.179 0.05 2 679 202 76 LEU HB3 H 1.708 0.05 2 680 202 76 LEU HG H 1.516 0.05 1 681 202 76 LEU HD1 H 0.452 0.05 2 682 202 76 LEU HD2 H 0.561 0.05 2 683 202 76 LEU C C 180.760 0.50 1 684 202 76 LEU CA C 57.665 0.50 1 685 202 76 LEU CB C 42.251 0.50 1 686 202 76 LEU CG C 26.477 0.50 1 687 202 76 LEU CD1 C 22.441 0.50 2 688 202 76 LEU CD2 C 26.008 0.50 2 689 202 76 LEU N N 118.876 0.10 1 690 203 77 LYS H H 8.488 0.05 1 691 203 77 LYS HA H 3.889 0.05 1 692 203 77 LYS HB2 H 1.753 0.05 2 693 203 77 LYS HB3 H 1.756 0.05 2 694 203 77 LYS HG2 H 1.330 0.05 2 695 203 77 LYS HG3 H 1.472 0.05 2 696 203 77 LYS HD2 H 1.551 0.05 2 697 203 77 LYS HD3 H 1.551 0.05 2 698 203 77 LYS HE2 H 2.811 0.05 2 699 203 77 LYS HE3 H 2.811 0.05 2 700 203 77 LYS C C 178.747 0.50 1 701 203 77 LYS CA C 59.063 0.50 1 702 203 77 LYS CB C 32.081 0.50 1 703 203 77 LYS CG C 25.489 0.50 1 704 203 77 LYS CD C 29.118 0.50 1 705 203 77 LYS CE C 41.617 0.50 1 706 203 77 LYS N N 119.619 0.10 1 707 204 78 ALA H H 7.101 0.05 1 708 204 78 ALA HA H 4.116 0.05 1 709 204 78 ALA HB H 1.414 0.05 1 710 204 78 ALA C C 178.940 0.50 1 711 204 78 ALA CA C 53.916 0.50 1 712 204 78 ALA CB C 18.160 0.50 1 713 204 78 ALA N N 120.564 0.10 1 714 205 79 LEU H H 7.440 0.05 1 715 205 79 LEU HA H 4.057 0.05 1 716 205 79 LEU HB2 H 1.507 0.05 2 717 205 79 LEU HB3 H 1.774 0.05 2 718 205 79 LEU HG H 1.232 0.05 1 719 205 79 LEU HD1 H 0.665 0.05 2 720 205 79 LEU HD2 H 0.645 0.05 2 721 205 79 LEU C C 178.811 0.50 1 722 205 79 LEU CA C 56.259 0.50 1 723 205 79 LEU CB C 42.722 0.50 1 724 205 79 LEU CD1 C 22.954 0.50 2 725 205 79 LEU CD2 C 26.000 0.50 2 726 205 79 LEU N N 117.578 0.10 1 727 206 80 GLY H H 7.178 0.05 1 728 206 80 GLY HA2 H 3.915 0.05 2 729 206 80 GLY HA3 H 4.278 0.05 2 730 206 80 GLY CA C 44.784 0.50 1 731 206 80 GLY N N 103.570 0.10 1 732 207 81 PRO HA H 4.370 0.05 1 733 207 81 PRO HB2 H 1.952 0.05 2 734 207 81 PRO HB3 H 2.230 0.05 2 735 207 81 PRO HG2 H 1.993 0.05 2 736 207 81 PRO HG3 H 1.914 0.05 2 737 207 81 PRO HD2 H 3.530 0.05 2 738 207 81 PRO HD3 H 3.664 0.05 2 739 207 81 PRO C C 177.633 0.50 1 740 207 81 PRO CA C 64.609 0.50 1 741 207 81 PRO CB C 32.075 0.50 1 742 207 81 PRO CG C 26.909 0.50 1 743 207 81 PRO CD C 49.887 0.50 1 744 208 82 ALA H H 8.365 0.05 1 745 208 82 ALA HA H 4.438 0.05 1 746 208 82 ALA HB H 1.297 0.05 1 747 208 82 ALA C C 176.991 0.50 1 748 208 82 ALA CA C 51.398 0.50 1 749 208 82 ALA CB C 18.402 0.50 1 750 208 82 ALA N N 122.470 0.10 1 751 209 83 ALA H H 6.896 0.05 1 752 209 83 ALA HA H 4.249 0.05 1 753 209 83 ALA HB H 1.221 0.05 1 754 209 83 ALA C C 177.676 0.50 1 755 209 83 ALA CA C 52.896 0.50 1 756 209 83 ALA CB C 20.370 0.50 1 757 209 83 ALA N N 122.515 0.10 1 758 210 84 THR H H 8.461 0.05 1 759 210 84 THR HA H 4.337 0.05 1 760 210 84 THR HB H 4.669 0.05 1 761 210 84 THR HG2 H 1.243 0.05 1 762 210 84 THR C C 175.492 0.50 1 763 210 84 THR CA C 60.023 0.50 1 764 210 84 THR CB C 71.063 0.50 1 765 210 84 THR CG2 C 21.832 0.50 1 766 210 84 THR N N 113.111 0.10 1 767 211 85 LEU H H 9.126 0.05 1 768 211 85 LEU HA H 4.066 0.05 1 769 211 85 LEU HB2 H 1.164 0.05 2 770 211 85 LEU HB3 H 1.339 0.05 2 771 211 85 LEU HG H 0.973 0.05 1 772 211 85 LEU HD1 H 0.203 0.05 2 773 211 85 LEU HD2 H 0.650 0.05 2 774 211 85 LEU C C 178.790 0.50 1 775 211 85 LEU CA C 57.994 0.50 1 776 211 85 LEU CB C 41.233 0.50 1 777 211 85 LEU CG C 27.016 0.50 1 778 211 85 LEU CD1 C 25.999 0.50 2 779 211 85 LEU CD2 C 23.256 0.50 2 780 211 85 LEU N N 122.385 0.10 1 781 212 86 GLU H H 8.756 0.05 1 782 212 86 GLU HA H 3.829 0.05 1 783 212 86 GLU HB2 H 1.882 0.05 2 784 212 86 GLU HB3 H 2.002 0.05 2 785 212 86 GLU HG2 H 2.338 0.05 2 786 212 86 GLU HG3 H 2.269 0.05 2 787 212 86 GLU C C 179.390 0.50 1 788 212 86 GLU CA C 60.541 0.50 1 789 212 86 GLU CB C 29.274 0.50 1 790 212 86 GLU CG C 36.894 0.50 1 791 212 86 GLU N N 117.734 0.10 1 792 213 87 GLU H H 7.601 0.05 1 793 213 87 GLU HA H 3.856 0.05 1 794 213 87 GLU HB2 H 2.322 0.05 2 795 213 87 GLU HB3 H 2.323 0.05 2 796 213 87 GLU HG2 H 2.190 0.05 2 797 213 87 GLU HG3 H 2.258 0.05 2 798 213 87 GLU C C 180.054 0.50 1 799 213 87 GLU CA C 59.515 0.50 1 800 213 87 GLU CB C 29.587 0.50 1 801 213 87 GLU CG C 37.493 0.50 1 802 213 87 GLU N N 119.749 0.10 1 803 214 88 MET H H 8.295 0.05 1 804 214 88 MET HA H 3.457 0.05 1 805 214 88 MET HB2 H 1.710 0.05 2 806 214 88 MET HB3 H 1.943 0.05 2 807 214 88 MET HG2 H 2.775 0.05 2 808 214 88 MET HG3 H 2.273 0.05 2 809 214 88 MET HE H 1.851 0.05 1 810 214 88 MET C C 177.226 0.50 1 811 214 88 MET CA C 60.108 0.50 1 812 214 88 MET CB C 33.082 0.50 1 813 214 88 MET CG C 32.966 0.50 1 814 214 88 MET CE C 17.868 0.50 1 815 214 88 MET N N 120.343 0.10 1 816 215 89 MET H H 8.627 0.05 1 817 215 89 MET HA H 4.081 0.05 1 818 215 89 MET HB2 H 1.979 0.05 2 819 215 89 MET HB3 H 2.258 0.05 2 820 215 89 MET HG2 H 2.528 0.05 2 821 215 89 MET HG3 H 2.610 0.05 2 822 215 89 MET HE H 1.646 0.05 1 823 215 89 MET C C 179.817 0.50 1 824 215 89 MET CA C 58.514 0.50 1 825 215 89 MET CB C 32.095 0.50 1 826 215 89 MET CG C 33.320 0.50 1 827 215 89 MET CE C 17.842 0.50 1 828 215 89 MET N N 116.854 0.10 1 829 216 90 THR H H 8.181 0.05 1 830 216 90 THR HA H 3.803 0.05 1 831 216 90 THR HB H 4.053 0.05 1 832 216 90 THR HG2 H 1.138 0.05 1 833 216 90 THR C C 177.226 0.50 1 834 216 90 THR CA C 66.544 0.50 1 835 216 90 THR CB C 68.687 0.50 1 836 216 90 THR CG2 C 21.616 0.50 1 837 216 90 THR N N 116.265 0.10 1 838 217 91 ALA H H 7.979 0.05 1 839 217 91 ALA HA H 4.066 0.05 1 840 217 91 ALA HB H 1.341 0.05 1 841 217 91 ALA C C 179.561 0.50 1 842 217 91 ALA CA C 54.924 0.50 1 843 217 91 ALA CB C 19.380 0.50 1 844 217 91 ALA N N 122.877 0.10 1 845 218 92 CYS H H 7.376 0.05 1 846 218 92 CYS HA H 4.317 0.05 1 847 218 92 CYS HB2 H 2.460 0.05 2 848 218 92 CYS HB3 H 2.970 0.05 2 849 218 92 CYS C C 175.427 0.50 1 850 218 92 CYS CA C 60.325 0.50 1 851 218 92 CYS CB C 28.306 0.50 1 852 218 92 CYS N N 110.620 0.10 1 853 219 93 GLN H H 7.399 0.05 1 854 219 93 GLN HA H 4.147 0.05 1 855 219 93 GLN HB2 H 2.125 0.05 2 856 219 93 GLN HB3 H 2.280 0.05 2 857 219 93 GLN HG2 H 2.381 0.05 2 858 219 93 GLN HG3 H 2.514 0.05 2 859 219 93 GLN HE21 H 6.857 0.05 2 860 219 93 GLN HE22 H 7.492 0.05 2 861 219 93 GLN C C 176.477 0.50 1 862 219 93 GLN CA C 58.501 0.50 1 863 219 93 GLN CB C 28.529 0.50 1 864 219 93 GLN CG C 33.335 0.50 1 865 219 93 GLN N N 122.626 0.10 1 866 219 93 GLN NE2 N 111.659 0.10 1 867 220 94 GLY H H 8.687 0.05 1 868 220 94 GLY HA2 H 3.842 0.05 2 869 220 94 GLY HA3 H 3.937 0.05 2 870 220 94 GLY C C 174.399 0.50 1 871 220 94 GLY CA C 45.303 0.50 1 872 220 94 GLY N N 110.387 0.10 1 873 221 95 VAL H H 7.284 0.05 1 874 221 95 VAL HA H 3.835 0.05 1 875 221 95 VAL HB H 1.949 0.05 1 876 221 95 VAL HG1 H 0.844 0.05 2 877 221 95 VAL HG2 H 0.813 0.05 2 878 221 95 VAL C C 177.077 0.50 1 879 221 95 VAL CA C 63.568 0.50 1 880 221 95 VAL CB C 31.719 0.50 1 881 221 95 VAL CG1 C 21.932 0.50 2 882 221 95 VAL CG2 C 21.381 0.50 2 883 221 95 VAL N N 120.427 0.10 1 884 222 96 GLY H H 8.742 0.05 1 885 222 96 GLY HA2 H 3.745 0.05 2 886 222 96 GLY HA3 H 4.032 0.05 2 887 222 96 GLY C C 173.922 0.50 1 888 222 96 GLY CA C 45.259 0.50 1 889 222 96 GLY N N 116.137 0.10 1 890 223 97 GLY H H 7.932 0.05 1 891 223 97 GLY HA2 H 4.117 0.05 2 892 223 97 GLY HA3 H 4.038 0.05 2 893 223 97 GLY C C 171.979 0.50 1 894 223 97 GLY CA C 44.770 0.50 1 895 223 97 GLY N N 108.039 0.10 1 896 224 98 PRO HA H 4.382 0.05 1 897 224 98 PRO HB2 H 1.790 0.05 2 898 224 98 PRO HB3 H 2.214 0.05 2 899 224 98 PRO HG2 H 1.904 0.05 2 900 224 98 PRO HG3 H 1.965 0.05 2 901 224 98 PRO HD2 H 3.596 0.05 2 902 224 98 PRO HD3 H 3.773 0.05 2 903 224 98 PRO C C 177.763 0.50 1 904 224 98 PRO CA C 63.556 0.50 1 905 224 98 PRO CB C 32.069 0.50 1 906 224 98 PRO CG C 27.010 0.50 1 907 224 98 PRO CD C 50.647 0.50 1 908 225 99 GLY H H 8.452 0.05 1 909 225 99 GLY HA2 H 3.844 0.05 2 910 225 99 GLY HA3 H 3.828 0.05 2 911 225 99 GLY C C 173.928 0.50 1 912 225 99 GLY CA C 45.301 0.50 1 913 225 99 GLY N N 109.147 0.10 1 914 226 100 HIS H H 8.119 0.05 1 915 226 100 HIS HA H 4.513 0.05 1 916 226 100 HIS HB2 H 3.054 0.05 2 917 226 100 HIS HB3 H 3.054 0.05 2 918 226 100 HIS C C 174.935 0.50 1 919 226 100 HIS CA C 56.171 0.50 1 920 226 100 HIS CB C 30.348 0.50 1 921 226 100 HIS N N 119.497 0.10 1 922 227 101 LYS H H 8.225 0.05 1 923 227 101 LYS HA H 4.195 0.05 1 924 227 101 LYS HB2 H 1.615 0.05 2 925 227 101 LYS HB3 H 1.704 0.05 2 926 227 101 LYS HG2 H 1.297 0.05 2 927 227 101 LYS HG3 H 1.292 0.05 2 928 227 101 LYS HD2 H 1.739 0.05 2 929 227 101 LYS HD3 H 1.739 0.05 2 930 227 101 LYS HE2 H 2.897 0.05 2 931 227 101 LYS HE3 H 2.897 0.05 2 932 227 101 LYS C C 175.839 0.50 1 933 227 101 LYS CA C 55.944 0.50 1 934 227 101 LYS CB C 32.708 0.50 1 935 227 101 LYS CG C 24.441 0.50 1 936 227 101 LYS CD C 29.038 0.50 1 937 227 101 LYS CE C 41.859 0.50 1 938 227 101 LYS N N 123.248 0.10 1 939 228 102 ALA H H 8.261 0.05 1 940 228 102 ALA HA H 4.195 0.05 1 941 228 102 ALA HB H 1.287 0.05 1 942 228 102 ALA C C 177.334 0.50 1 943 228 102 ALA CA C 52.251 0.50 1 944 228 102 ALA CB C 19.160 0.50 1 945 228 102 ALA N N 125.618 0.10 1 946 229 103 ARG H H 8.289 0.05 1 947 229 103 ARG HA H 4.235 0.05 1 948 229 103 ARG HB2 H 1.704 0.05 2 949 229 103 ARG HB3 H 1.704 0.05 2 950 229 103 ARG HG2 H 1.553 0.05 2 951 229 103 ARG HG3 H 1.553 0.05 2 952 229 103 ARG HD2 H 3.099 0.05 2 953 229 103 ARG HD3 H 3.099 0.05 2 954 229 103 ARG C C 175.797 0.50 1 955 229 103 ARG CA C 55.810 0.50 1 956 229 103 ARG CB C 30.618 0.50 1 957 229 103 ARG CG C 26.505 0.50 1 958 229 103 ARG CD C 43.193 0.50 1 959 229 103 ARG N N 121.125 0.10 1 960 230 104 VAL H H 8.220 0.05 1 961 230 104 VAL HA H 4.007 0.05 1 962 230 104 VAL HB H 1.962 0.05 1 963 230 104 VAL HG1 H 0.851 0.05 2 964 230 104 VAL HG2 H 0.851 0.05 2 965 230 104 VAL C C 174.994 0.50 1 966 230 104 VAL CA C 62.305 0.50 1 967 230 104 VAL CB C 32.685 0.50 1 968 230 104 VAL CG1 C 20.350 0.50 2 969 230 104 VAL CG2 C 20.900 0.50 2 970 230 104 VAL N N 123.242 0.10 1 971 231 105 LEU H H 7.889 0.05 1 972 231 105 LEU N N 131.960 0.10 1 stop_ save_ save_assigned_chem_shift_list_1_2 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D 1H-15N NOESY' '3D 1H-13C NOESY' '2D f1,f2 filtered 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name NYAD-13_Peptide_Inhibitor _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 ILE H H 9.014 0.05 1 2 1 1 ILE HA H 4.090 0.05 1 3 1 1 ILE HB H 2.040 0.05 1 4 1 1 ILE HG12 H 1.277 0.05 2 5 1 1 ILE HG13 H 1.277 0.05 2 6 1 1 ILE HG2 H 1.001 0.05 1 7 1 1 ILE HD1 H 0.788 0.05 1 8 2 2 THR H H 8.702 0.05 1 9 2 2 THR HA H 4.535 0.05 1 10 2 2 THR HB H 4.875 0.05 1 11 2 2 THR HG2 H 1.284 0.05 1 12 3 3 PHE H H 8.703 0.05 1 13 3 3 PHE HA H 4.365 0.05 1 14 3 3 PHE HB2 H 3.087 0.05 2 15 3 3 PHE HB3 H 3.135 0.05 2 16 3 3 PHE HD1 H 7.300 0.05 1 17 3 3 PHE HD2 H 7.300 0.05 1 18 3 3 PHE HE1 H 7.300 0.05 1 19 3 3 PHE HE2 H 7.300 0.05 1 20 3 3 PHE HZ H 7.139 0.05 1 21 4 4 MK8 H H 8.038 0.05 1 22 4 4 MK8 HB H 1.667 0.05 2 23 4 4 MK8 HB1 H 1.418 0.05 1 24 4 4 MK8 HG H 1.018 0.05 2 25 4 4 MK8 HD H 2.006 0.05 2 26 4 4 MK8 HE H 5.375 0.05 1 27 4 4 MK8 HBA H 1.972 0.05 2 28 4 4 MK8 HDA H 1.589 0.05 2 29 4 4 MK8 HGA H 1.587 0.05 2 30 5 5 ASP H H 7.243 0.05 1 31 5 5 ASP HA H 4.278 0.05 1 32 5 5 ASP HB2 H 2.630 0.05 2 33 5 5 ASP HB3 H 3.054 0.05 2 34 6 6 LEU H H 7.519 0.05 1 35 6 6 LEU HA H 3.805 0.05 1 36 6 6 LEU HB2 H 1.407 0.05 2 37 6 6 LEU HB3 H 1.917 0.05 2 38 6 6 LEU HG H 1.179 0.05 1 39 6 6 LEU HD1 H 0.799 0.05 2 40 6 6 LEU HD2 H 0.797 0.05 2 41 7 7 LEU H H 7.389 0.05 1 42 7 7 LEU HA H 3.816 0.05 1 43 7 7 LEU HB2 H 1.685 0.05 2 44 7 7 LEU HB3 H 1.397 0.05 2 45 7 7 LEU HG H 1.399 0.05 1 46 7 7 LEU HD1 H 0.881 0.05 2 47 7 7 LEU HD2 H 0.914 0.05 2 48 8 8 MK8 H H 8.396 0.05 1 49 8 8 MK8 HB H 1.556 0.05 2 50 8 8 MK8 HB1 H 1.353 0.05 1 51 8 8 MK8 HG H 1.003 0.05 2 52 8 8 MK8 HD H 1.616 0.05 2 53 8 8 MK8 HE H 5.486 0.05 1 54 8 8 MK8 HBA H 1.394 0.05 2 55 8 8 MK8 HDA H 2.245 0.05 2 56 8 8 MK8 HGA H 1.169 0.05 2 57 9 9 TYR H H 7.583 0.05 1 58 9 9 TYR HA H 3.892 0.05 1 59 9 9 TYR HB2 H 2.765 0.05 1 60 9 9 TYR HB3 H 2.977 0.05 1 61 9 9 TYR HD1 H 6.226 0.05 1 62 9 9 TYR HD2 H 6.226 0.05 1 63 9 9 TYR HE1 H 6.340 0.05 1 64 9 9 TYR HE2 H 6.340 0.05 1 65 10 10 TYR H H 7.962 0.05 1 66 10 10 TYR HA H 3.883 0.05 1 67 10 10 TYR HB2 H 2.325 0.05 1 68 10 10 TYR HB3 H 2.920 0.05 1 69 10 10 TYR HD1 H 6.766 0.05 1 70 10 10 TYR HD2 H 6.766 0.05 1 71 10 10 TYR HE1 H 6.490 0.05 1 72 10 10 TYR HE2 H 6.490 0.05 1 73 11 11 GLY H H 8.314 0.05 1 74 11 11 GLY HA2 H 3.704 0.05 2 75 11 11 GLY HA3 H 4.030 0.05 2 76 12 12 LYS H H 7.561 0.05 1 77 12 12 LYS HA H 4.168 0.05 1 78 12 12 LYS HB2 H 1.690 0.05 2 79 12 12 LYS HB3 H 1.753 0.05 2 80 12 12 LYS HG2 H 1.351 0.05 2 81 12 12 LYS HG3 H 1.434 0.05 2 82 12 12 LYS HD2 H 1.548 0.05 2 83 12 12 LYS HD3 H 1.547 0.05 2 84 12 12 LYS HE2 H 2.876 0.05 2 85 12 12 LYS HE3 H 2.927 0.05 2 86 13 13 LYS H H 7.874 0.05 1 87 13 13 LYS HA H 4.160 0.05 1 88 13 13 LYS HB2 H 1.634 0.05 2 89 13 13 LYS HB3 H 1.729 0.05 2 90 13 13 LYS HG2 H 1.289 0.05 2 91 13 13 LYS HD2 H 1.524 0.05 2 92 13 13 LYS HE2 H 2.787 0.05 2 93 13 13 LYS HE3 H 2.792 0.05 2 94 14 14 LYS H H 8.106 0.05 1 95 14 14 LYS HA H 4.145 0.05 1 96 14 14 LYS HB2 H 1.712 0.05 2 97 14 14 LYS HG2 H 1.357 0.05 2 98 14 14 LYS HG3 H 1.357 0.05 2 99 14 14 LYS HD2 H 1.627 0.05 2 100 14 14 LYS HD3 H 1.627 0.05 2 stop_ save_