data_16555 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein ; _BMRB_accession_number 16555 _BMRB_flat_file_name bmr16555.str _Entry_type original _Submission_date 2009-10-15 _Accession_date 2009-10-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details n/a loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jung Jinwon . . 2 Byeon In-Ja L. . 3 Ahn Jinwoo . . 4 Concel Jason . . 5 Gronenborn Angela M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 472 "13C chemical shifts" 272 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-05-20 update BMRB 'complete entry citation' 2009-11-30 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 19921549 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jung Jinwon . . 2 Byeon In-Ja L. . 3 Ahn Jinwoo . . 4 Concel Jason . . 5 Gronenborn Angela M. . stop_ _Journal_abbreviation 'Biomol. NMR Assignments' _Journal_name_full 'Biomolecular NMR assignments' _Journal_volume 4 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 21 _Page_last 23 _Year 2010 _Details . loop_ _Keyword CA 'capsid protein' CTD 'C-terminal domain' HIV-1 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'CA-CTD dimer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'subunit 1' $HIV-1_Capsid_Protein 'subunit 2' $HIV-1_Capsid_Protein stop_ _System_molecular_weight 9827.3 _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'subunit 1' 1 'subunit 2' stop_ _Database_query_date . _Details homodimer save_ ######################## # Monomeric polymers # ######################## save_HIV-1_Capsid_Protein _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HIV-1_Capsid_Protein _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 88 _Mol_residue_sequence ; MYSPTSILDIRQGPKEPFRD YVDRFYKTLRAEQASQEVKN WMTETLLVQNANPDCKTILK ALGPAATLEEMMTACQGVGG PGHKARVL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 144 MET 2 145 TYR 3 146 SER 4 147 PRO 5 148 THR 6 149 SER 7 150 ILE 8 151 LEU 9 152 ASP 10 153 ILE 11 154 ARG 12 155 GLN 13 156 GLY 14 157 PRO 15 158 LYS 16 159 GLU 17 160 PRO 18 161 PHE 19 162 ARG 20 163 ASP 21 164 TYR 22 165 VAL 23 166 ASP 24 167 ARG 25 168 PHE 26 169 TYR 27 170 LYS 28 171 THR 29 172 LEU 30 173 ARG 31 174 ALA 32 175 GLU 33 176 GLN 34 177 ALA 35 178 SER 36 179 GLN 37 180 GLU 38 181 VAL 39 182 LYS 40 183 ASN 41 184 TRP 42 185 MET 43 186 THR 44 187 GLU 45 188 THR 46 189 LEU 47 190 LEU 48 191 VAL 49 192 GLN 50 193 ASN 51 194 ALA 52 195 ASN 53 196 PRO 54 197 ASP 55 198 CYS 56 199 LYS 57 200 THR 58 201 ILE 59 202 LEU 60 203 LYS 61 204 ALA 62 205 LEU 63 206 GLY 64 207 PRO 65 208 ALA 66 209 ALA 67 210 THR 68 211 LEU 69 212 GLU 70 213 GLU 71 214 MET 72 215 MET 73 216 THR 74 217 ALA 75 218 CYS 76 219 GLN 77 220 GLY 78 221 VAL 79 222 GLY 80 223 GLY 81 224 PRO 82 225 GLY 83 226 HIS 84 227 LYS 85 228 ALA 86 229 ARG 87 230 VAL 88 231 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-23 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" 97.73 87 98.84 98.84 1.79e-55 BMRB 17307 Capsid_protein_p24 95.45 105 97.62 97.62 2.43e-53 BMRB 19261 HIVcapsid 100.00 231 98.86 98.86 1.17e-56 BMRB 19575 HIV1_CA 100.00 231 98.86 98.86 1.17e-56 BMRB 25532 Gag 100.00 432 100.00 100.00 2.91e-55 PDB 1A43 "Structure Of The Hiv-1 Capsid Protein Dimerization Domain At 2.6a Resolution" 97.73 87 98.84 98.84 2.78e-56 PDB 1AUM "Hiv Capsid C-Terminal Domain (Cac146)" 79.55 70 98.57 98.57 2.56e-43 PDB 1BAJ "Hiv-1 Capsid Protein C-Terminal Fragment Plus Gag P2 Domain" 97.73 101 98.84 98.84 1.38e-56 PDB 1E6J "Crystal Structure Of Hiv-1 Capsid Protein (p24) In Complex With Fab13b5" 87.50 210 100.00 100.00 1.86e-48 PDB 1VU4 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VU5 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VU6 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VU7 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VU8 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VU9 "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUA "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUC "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUD "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUE "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUF "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUG "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUH "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUI "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUJ "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUK "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUL "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUM "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUN "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUO "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUP "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUQ "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUR "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUS "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUT "Atomic-level Structure Of The Entire Hiv-1 Capsid" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUU "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUV "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUW "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUX "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUY "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VUZ "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV0 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV1 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV2 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV3 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV4 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV5 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV6 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV7 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV8 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VV9 "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VVA "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VVB "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VVF "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VVG "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VVH "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 1VVI "Atomic-level Structure Of The Entire Hiv-1 Capsid (186 Hexamers + 12 Pentamers)" 100.00 231 100.00 100.00 2.52e-57 PDB 2BUO "Hiv-1 Capsid C-Terminal Domain In Complex With An Inhibitor Of Particle Assembly" 97.73 86 98.84 98.84 3.07e-56 PDB 2JO0 "The Solution Structure Of The Monomeric Species Of The C Terminal Domain Of The Ca Protein Of Hiv-1" 97.73 87 98.84 98.84 1.79e-55 PDB 2KOD "A High-Resolution Nmr Structure Of The Dimeric C-Terminal Domain Of Hiv-1 Ca" 100.00 88 100.00 100.00 8.57e-59 PDB 2L6E "Nmr Structure Of The Monomeric Mutant C-Terminal Domain Of Hiv-1 Capsid In Complex With Stapled Peptide Inhibitor" 95.45 105 97.62 97.62 2.43e-53 PDB 2M8L "Hiv Capsid Dimer Structure" 88.64 221 98.72 98.72 2.28e-48 PDB 2M8N "Hiv-1 Capsid Monomer Structure" 88.64 221 98.72 98.72 2.28e-48 PDB 2ONT "A Swapped Dimer Of The Hiv-1 Capsid C-terminal Domain" 86.36 76 97.37 97.37 2.45e-45 PDB 2XT1 "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain (146-231) In Complex With A Camelid Vhh" 97.73 86 98.84 98.84 3.07e-56 PDB 2XV6 "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain (146-220) In Complex With A Camelid Vhh." 85.23 75 98.67 98.67 3.58e-47 PDB 2XXM "Crystal Structure Of The Hiv-1 Capsid Protein C-Terminal Domain In Complex With A Camelid Vhh And The Cai Peptide" 85.23 75 98.67 98.67 3.58e-47 PDB 3DIK "Pseudo-Atomic Model Of The Hiv-1 Ca Hexameric Lattice" 86.36 219 98.68 98.68 9.32e-47 PDB 3DPH "Hiv-1 Capsid C-Terminal Domain Mutant (L211s)" 97.73 86 97.67 97.67 2.63e-55 PDB 3DS0 "Hiv-1 Capsid C-Terminal Domain Mutant (N183a) In Complex With An Inhibitor Of Particle Assembly (Cai)" 97.73 86 97.67 97.67 4.16e-55 PDB 3DS1 "Hiv-1 Capsid C-Terminal Domain Mutant (E187a) In Complex With An Inhibitor Of Particle Assembly (Cai)" 97.73 86 97.67 97.67 2.28e-55 PDB 3DS2 "Hiv-1 Capsid C-Terminal Domain Mutant (Y169a)" 97.73 86 97.67 97.67 4.30e-55 PDB 3DS3 "Hiv-1 Capsid C-Terminal Domain Mutant (Y169a) In Complex With An Inhibitor Of Particle Assembly (Cai)" 97.73 86 97.67 97.67 4.30e-55 PDB 3DS4 "Hiv-1 Capsid C-Terminal Domain Mutant (L211s) In Complex With An Inhibitor Of Particle Assembly (Cai)" 97.73 86 97.67 97.67 2.63e-55 PDB 3DS5 "Hiv-1 Capsid C-Terminal Domain Mutant (N183a)" 97.73 86 97.67 97.67 4.16e-55 PDB 3DTJ "Hiv-1 Capsid C-terminal Domain Mutant (e187a)" 97.73 86 97.67 97.67 2.28e-55 PDB 3J34 "Structure Of Hiv-1 Capsid Protein By Cryo-em" 100.00 231 100.00 100.00 2.52e-57 PDB 3J4F "Structure Of Hiv-1 Capsid Protein By Cryo-em" 100.00 231 100.00 100.00 2.52e-57 PDB 3LRY "Crystal Structure Of Synthetic Hiv-1 Capsid C-Terminal Domain (Cca)" 97.73 86 98.84 98.84 3.07e-56 PDB 3NTE "Crystal Structure Of The Wild-type Full-length Hiv-1 Capsid Protein" 88.64 221 100.00 100.00 5.12e-49 PDB 4COC "Hiv-1 Capsid C-terminal Domain Mutant (y169l)" 97.73 86 97.67 97.67 3.49e-55 PDB 4COP "Hiv-1 Capsid C-terminal Domain Mutant (y169s)" 97.73 86 97.67 97.67 3.38e-55 PDB 4D1K "Cryo-electron Microscopy Of Tubular Arrays Of Hiv-1 Gag Resolves Structures Essential For Immature Virus Assembly" 86.36 219 97.37 97.37 1.25e-45 PDB 4IPY "Hiv Capsid C-terminal Domain" 97.73 87 98.84 98.84 2.78e-56 PDB 4M0I "Crystal Structure Of Synthetic Hiv-1 Capsid C-terminal Domain (ctd) C198s Mutant" 97.73 86 97.67 97.67 3.73e-55 PDB 4USN "The Structure Of The Immature Hiv-1 Capsid In Intact Virus Particles At Sub-nm Resolution" 86.36 210 97.37 97.37 1.24e-45 PDB 4XFX "Structure Of The Native Full-length Hiv-1 Capsid Protein" 100.00 231 98.86 98.86 1.17e-56 PDB 4XFY "Structure Of The Native Full-length Dehydrated Hiv-1 Capsid Protein" 100.00 231 98.86 98.86 1.17e-56 PDB 4XFZ "Structure Of The Native Full-length Hiv-1 Capsid Protein In Complex With Pf-3450074 (pf74)" 100.00 231 98.86 98.86 1.17e-56 DBJ BAA00992 "gag polyprotein [Human immunodeficiency virus 1]" 100.00 500 100.00 100.00 1.41e-54 DBJ BAA12988 "Gag [Human immunodeficiency virus 1]" 100.00 512 100.00 100.00 2.42e-54 DBJ BAA12996 "Gag [Human immunodeficiency virus 1]" 100.00 512 100.00 100.00 2.27e-54 DBJ BAA93773 "gag protein [Human immunodeficiency virus 1]" 100.00 231 98.86 100.00 1.09e-56 DBJ BAA93774 "gag protein [Human immunodeficiency virus 1]" 100.00 231 98.86 100.00 1.10e-56 EMBL CAA06946 "gag polyprotein precursor [Human immunodeficiency virus 1]" 100.00 503 98.86 100.00 7.45e-54 EMBL CAA11880 "p24 [Human immunodeficiency virus 1]" 76.14 189 100.00 100.00 1.83e-40 EMBL CAA11884 "p24 [Human immunodeficiency virus 1]" 76.14 191 97.01 98.51 2.02e-39 EMBL CAA11886 "p24 [Human immunodeficiency virus 1]" 76.14 190 100.00 100.00 1.92e-40 EMBL CAA12915 "p24 core protein [Human immunodeficiency virus 1]" 54.55 113 97.92 97.92 4.69e-25 GB AAA44201 "gag polyprotein precursor [Human immunodeficiency virus 1]" 100.00 512 100.00 100.00 2.80e-54 GB AAA44224 "gag protein, partial [Human immunodeficiency virus 1]" 100.00 493 97.73 98.86 2.70e-53 GB AAA44225 "gag protein, partial [Human immunodeficiency virus 1]" 100.00 491 97.73 100.00 1.14e-53 GB AAA44306 "gag polyprotein [Human immunodeficiency virus 1]" 100.00 500 98.86 98.86 1.17e-53 GB AAA44652 "gag polyprotein precursor [Human immunodeficiency virus 1]" 100.00 512 100.00 100.00 2.74e-54 PIR FOVWLV "gag polyprotein - human immunodeficiency virus type 1 (isolate LAV-1a)" 100.00 500 100.00 100.00 1.67e-54 PRF 1102247B "protein gag" 100.00 512 100.00 100.00 2.80e-54 PRF 1103299C "gag gene" 100.00 478 100.00 100.00 8.58e-55 REF NP_057849 "Gag-Pol [Human immunodeficiency virus 1]" 100.00 1435 100.00 100.00 2.19e-52 REF NP_057850 "Pr55(Gag) [Human immunodeficiency virus 1]" 100.00 500 100.00 100.00 1.87e-54 REF NP_579880 "capsid [Human immunodeficiency virus 1]" 100.00 231 100.00 100.00 2.49e-57 SP P03347 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 100.00 512 100.00 100.00 2.80e-54 SP P03348 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 100.00 512 100.00 100.00 2.42e-54 SP P03349 "RecName: Full=Gag polyprotein; AltName: Full=Pr55Gag; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: RecName: " 100.00 502 98.86 100.00 6.60e-54 SP P03366 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 100.00 1447 100.00 100.00 2.18e-52 SP P03367 "RecName: Full=Gag-Pol polyprotein; AltName: Full=Pr160Gag-Pol; Contains: RecName: Full=Matrix protein p17; Short=MA; Contains: " 100.00 1447 100.00 100.00 1.96e-52 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HIV-1_Capsid_Protein 'Lentivirus human immunodeficiency virus' 11646 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 _Vector_name $HIV-1_Capsid_Protein 'recombinant technology' . Escherichia coli . pET21 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 $HIV-1_Capsid_Protein 2 mM '[U-100% 13C; U-100% 15N]' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' 'sodium phosphate' 25 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' DTT 2 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ 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' stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_3D_simultaneous_13C,15N-edited_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D simultaneous 13C,15N-edited NOESY' _Sample_label $sample_1 save_ save_3D_13C-edited_NOESY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-edited NOESY' _Sample_label $sample_1 save_ save_2D_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCACB' '3D HN(CO)CACB' '3D HNCA' '3D HN(CO)CA' '3D HBHA(CO)NH' '3D HCCH-TOCSY' '3D simultaneous 13C,15N-edited NOESY' '3D 13C-edited NOESY' '2D NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 145 2 TYR HA H 4.731 0.000 1 2 145 2 TYR HB2 H 2.931 0.000 1 3 145 2 TYR HB3 H 3.088 0.000 2 4 145 2 TYR HD1 H 7.109 0.000 3 5 145 2 TYR HE1 H 6.812 0.000 3 6 145 2 TYR CA C 58.014 0.000 1 7 145 2 TYR CB C 38.967 0.000 1 8 145 2 TYR CD1 C 132.735 0.000 3 9 145 2 TYR CE1 C 118.089 0.000 3 10 146 3 SER H H 8.041 0.000 1 11 146 3 SER HA H 4.691 0.000 1 12 146 3 SER HB2 H 3.671 0.000 1 13 146 3 SER HB3 H 3.772 0.000 2 14 146 3 SER CA C 55.320 0.000 1 15 146 3 SER CB C 63.943 0.000 1 16 146 3 SER N N 121.147 0.000 1 17 147 4 PRO HA H 4.412 0.000 1 18 147 4 PRO HB2 H 1.959 0.000 1 19 147 4 PRO HB3 H 2.296 0.000 2 20 147 4 PRO HD2 H 3.491 0.000 1 21 147 4 PRO HD3 H 3.683 0.000 2 22 147 4 PRO HG2 H 2.001 0.000 1 23 147 4 PRO CA C 63.062 0.000 1 24 147 4 PRO CB C 32.102 0.000 1 25 147 4 PRO CD C 50.586 0.000 1 26 147 4 PRO CG C 27.036 0.000 1 27 148 5 THR H H 8.174 0.000 1 28 148 5 THR HA H 4.641 0.000 1 29 148 5 THR HB H 4.224 0.000 1 30 148 5 THR HG2 H 1.194 0.000 1 31 148 5 THR CA C 60.991 0.000 1 32 148 5 THR CB C 70.053 0.000 1 33 148 5 THR CG2 C 20.850 0.000 1 34 148 5 THR N N 114.932 0.000 1 35 149 6 SER HA H 3.950 0.000 1 36 149 6 SER HB2 H 3.949 0.000 1 37 149 6 SER HB3 H 3.762 0.000 2 38 149 6 SER CB C 64.826 0.000 1 39 150 7 ILE H H 8.709 0.000 1 40 150 7 ILE HA H 3.954 0.000 1 41 150 7 ILE HB H 1.451 0.000 1 42 150 7 ILE HD1 H -0.210 0.000 1 43 150 7 ILE HG12 H 0.854 0.000 1 44 150 7 ILE HG13 H 0.994 0.000 2 45 150 7 ILE HG2 H 0.933 0.000 1 46 150 7 ILE CA C 60.718 0.000 1 47 150 7 ILE CB C 39.669 0.000 1 48 150 7 ILE CD1 C 14.795 0.000 1 49 150 7 ILE CG1 C 28.711 0.000 1 50 150 7 ILE CG2 C 17.501 0.000 1 51 150 7 ILE N N 125.960 0.000 1 52 151 8 LEU H H 7.614 0.000 1 53 151 8 LEU HA H 4.042 0.000 1 54 151 8 LEU HB2 H 1.747 0.000 1 55 151 8 LEU HB3 H 1.627 0.000 2 56 151 8 LEU HD1 H 1.159 0.000 2 57 151 8 LEU HD2 H 0.994 0.000 2 58 151 8 LEU HG H 1.805 0.000 1 59 151 8 LEU CA C 56.736 0.000 1 60 151 8 LEU CB C 40.960 0.000 1 61 151 8 LEU CD1 C 23.459 0.000 2 62 151 8 LEU CD2 C 25.705 0.000 2 63 151 8 LEU CG C 27.401 0.000 1 64 151 8 LEU N N 118.883 0.000 1 65 152 9 ASP H H 7.545 0.000 1 66 152 9 ASP HA H 4.760 0.000 1 67 152 9 ASP HB2 H 2.626 0.000 1 68 152 9 ASP HB3 H 2.967 0.000 2 69 152 9 ASP CA C 54.166 0.000 1 70 152 9 ASP CB C 41.993 0.000 1 71 152 9 ASP N N 114.458 0.000 1 72 153 10 ILE H H 7.391 0.000 1 73 153 10 ILE HA H 4.180 0.000 1 74 153 10 ILE HB H 2.441 0.000 1 75 153 10 ILE HD1 H 0.701 0.000 1 76 153 10 ILE HG12 H 1.279 0.000 1 77 153 10 ILE HG13 H 1.782 0.000 2 78 153 10 ILE HG2 H 0.984 0.000 1 79 153 10 ILE CA C 59.364 0.000 1 80 153 10 ILE CB C 33.977 0.000 1 81 153 10 ILE CD1 C 9.772 0.000 1 82 153 10 ILE CG1 C 27.068 0.000 1 83 153 10 ILE CG2 C 16.726 0.000 1 84 153 10 ILE N N 122.059 0.000 1 85 154 11 ARG H H 8.308 0.000 1 86 154 11 ARG HA H 4.930 0.000 1 87 154 11 ARG HB2 H 1.825 0.000 1 88 154 11 ARG HB3 H 1.654 0.000 2 89 154 11 ARG HD2 H 3.236 0.000 1 90 154 11 ARG HD3 H 3.207 0.000 2 91 154 11 ARG HG2 H 1.517 0.000 1 92 154 11 ARG CA C 53.999 0.000 1 93 154 11 ARG CB C 32.922 0.000 1 94 154 11 ARG CD C 43.012 0.000 1 95 154 11 ARG CG C 26.812 0.000 1 96 154 11 ARG N N 125.222 0.000 1 97 155 12 GLN H H 7.795 0.000 1 98 155 12 GLN HA H 3.895 0.000 1 99 155 12 GLN HB2 H 0.072 0.000 1 100 155 12 GLN HE21 H 7.616 0.000 2 101 155 12 GLN HE22 H 6.730 0.000 2 102 155 12 GLN HG2 H 3.212 0.000 1 103 155 12 GLN HG3 H 1.810 0.000 2 104 155 12 GLN CA C 55.815 0.000 1 105 155 12 GLN CB C 27.280 0.000 1 106 155 12 GLN CG C 32.559 0.000 1 107 155 12 GLN N N 127.507 0.000 1 108 155 12 GLN NE2 N 107.954 0.000 1 109 156 13 GLY H H 9.897 0.000 1 110 156 13 GLY HA2 H 4.004 0.000 1 111 156 13 GLY HA3 H 4.408 0.000 2 112 156 13 GLY CA C 44.889 0.000 1 113 156 13 GLY N N 116.784 0.000 1 114 157 14 PRO HA H 4.281 0.000 1 115 157 14 PRO HB2 H 2.017 0.000 1 116 157 14 PRO HB3 H 2.479 0.000 2 117 157 14 PRO HD2 H 3.811 0.000 1 118 157 14 PRO HD3 H 3.857 0.000 2 119 157 14 PRO HG2 H 2.180 0.000 1 120 157 14 PRO HG3 H 2.110 0.000 2 121 157 14 PRO CA C 65.684 0.000 1 122 157 14 PRO CB C 31.898 0.000 1 123 157 14 PRO CD C 50.246 0.000 1 124 157 14 PRO CG C 27.571 0.000 1 125 158 15 LYS H H 8.566 0.000 1 126 158 15 LYS HA H 4.569 0.000 1 127 158 15 LYS HB2 H 1.603 0.000 1 128 158 15 LYS HB3 H 2.122 0.000 2 129 158 15 LYS HD2 H 1.367 0.000 1 130 158 15 LYS HE2 H 2.988 0.000 1 131 158 15 LYS HG2 H 1.633 0.000 1 132 158 15 LYS HG3 H 1.719 0.000 2 133 158 15 LYS CA C 53.923 0.000 1 134 158 15 LYS CB C 32.320 0.000 1 135 158 15 LYS CD C 24.570 0.000 1 136 158 15 LYS CE C 41.986 0.000 1 137 158 15 LYS CG C 28.803 0.000 1 138 158 15 LYS N N 114.954 0.000 1 139 159 16 GLU H H 7.042 0.000 1 140 159 16 GLU HA H 4.595 0.000 1 141 159 16 GLU HB2 H 1.838 0.000 1 142 159 16 GLU HB3 H 2.265 0.000 2 143 159 16 GLU HG2 H 2.376 0.000 1 144 159 16 GLU HG3 H 2.657 0.000 2 145 159 16 GLU CA C 53.462 0.000 1 146 159 16 GLU CB C 31.87 0.000 1 147 159 16 GLU CG C 34.484 0.000 1 148 159 16 GLU N N 125.624 0.000 1 149 160 17 PRO HA H 4.437 0.000 1 150 160 17 PRO HB2 H 2.381 0.000 1 151 160 17 PRO HB3 H 2.132 0.000 2 152 160 17 PRO HD2 H 3.607 0.000 1 153 160 17 PRO HD3 H 3.564 0.000 2 154 160 17 PRO HG2 H 1.974 0.000 1 155 160 17 PRO HG3 H 1.854 0.000 2 156 160 17 PRO CA C 63.353 0.000 1 157 160 17 PRO CB C 32.700 0.000 1 158 160 17 PRO CD C 51.557 0.000 1 159 161 18 PHE H H 9.529 0.000 1 160 161 18 PHE HA H 4.460 0.000 1 161 161 18 PHE HB2 H 3.019 0.000 1 162 161 18 PHE HB3 H 3.571 0.000 2 163 161 18 PHE HD1 H 7.364 0.000 3 164 161 18 PHE HE1 H 7.006 0.000 3 165 161 18 PHE HZ H 6.934 0.000 1 166 161 18 PHE CA C 63.387 0.000 1 167 161 18 PHE CB C 39.262 0.000 1 168 161 18 PHE CD1 C 132.268 0.000 3 169 161 18 PHE CE1 C 131.077 0.000 3 170 161 18 PHE N N 128.271 0.000 1 171 162 19 ARG H H 9.087 0.000 1 172 162 19 ARG HA H 3.731 0.000 1 173 162 19 ARG HB2 H 1.739 0.000 1 174 162 19 ARG HB3 H 1.955 0.000 2 175 162 19 ARG HD2 H 3.191 0.000 1 176 162 19 ARG HD3 H 3.262 0.000 2 177 162 19 ARG HE H 7.340 0.000 1 178 162 19 ARG HG2 H 1.719 0.000 1 179 162 19 ARG HG3 H 1.758 0.000 2 180 162 19 ARG CA C 59.816 0.000 1 181 162 19 ARG CB C 29.920 0.000 1 182 162 19 ARG CD C 43.206 0.000 1 183 162 19 ARG CG C 27.280 0.000 1 184 162 19 ARG N N 115.694 0.000 1 185 162 19 ARG NE N 84.700 0.000 1 186 163 20 ASP H H 6.985 0.000 1 187 163 20 ASP HA H 4.444 0.000 1 188 163 20 ASP HB2 H 2.905 0.000 1 189 163 20 ASP CA C 57.001 0.000 1 190 163 20 ASP CB C 39.770 0.000 1 191 163 20 ASP N N 118.950 0.000 1 192 164 21 TYR H H 7.548 0.000 1 193 164 21 TYR HA H 4.390 0.000 1 194 164 21 TYR HB2 H 2.869 0.000 1 195 164 21 TYR HB3 H 3.208 0.000 2 196 164 21 TYR HD1 H 6.940 0.000 3 197 164 21 TYR HE1 H 6.449 0.000 3 198 164 21 TYR HH H 9.233 0.000 1 199 164 21 TYR CA C 59.495 0.000 1 200 164 21 TYR CB C 38.165 0.000 1 201 164 21 TYR CD1 C 133.754 0.000 3 202 164 21 TYR CE1 C 116.032 0.000 3 203 164 21 TYR N N 124.243 0.000 1 204 165 22 VAL H H 8.352 0.000 1 205 165 22 VAL HA H 2.780 0.000 1 206 165 22 VAL HB H 1.773 0.000 1 207 165 22 VAL HG1 H 0.811 0.000 2 208 165 22 VAL HG2 H 0.181 0.000 2 209 165 22 VAL CA C 66.685 0.000 1 210 165 22 VAL CB C 31.349 0.000 1 211 165 22 VAL CG1 C 22.188 0.000 2 212 165 22 VAL CG2 C 24.007 0.000 2 213 165 22 VAL N N 120.217 0.000 1 214 166 23 ASP H H 7.594 0.000 1 215 166 23 ASP HA H 4.445 0.000 1 216 166 23 ASP HB2 H 2.838 0.000 1 217 166 23 ASP HB3 H 2.729 0.000 2 218 166 23 ASP CA C 57.772 0.000 1 219 166 23 ASP CB C 40.945 0.000 1 220 166 23 ASP N N 118.227 0.000 1 221 167 24 ARG H H 7.876 0.000 1 222 167 24 ARG HA H 4.069 0.000 1 223 167 24 ARG HB2 H 2.095 0.000 1 224 167 24 ARG HB3 H 1.841 0.000 2 225 167 24 ARG HD2 H 3.396 0.000 1 226 167 24 ARG HD3 H 3.284 0.000 2 227 167 24 ARG HE H 9.452 0.000 1 228 167 24 ARG HG2 H 1.631 0.000 1 229 167 24 ARG HG3 H 1.983 0.000 2 230 167 24 ARG CA C 60.108 0.000 1 231 167 24 ARG CB C 30.525 0.000 1 232 167 24 ARG CD C 43.300 0.000 1 233 167 24 ARG CG C 29.000 0.000 1 234 167 24 ARG N N 119.139 0.000 1 235 167 24 ARG NE N 85.365 0.000 1 236 168 25 PHE H H 9.108 0.000 1 237 168 25 PHE HA H 3.636 0.000 1 238 168 25 PHE HB2 H 2.293 0.000 1 239 168 25 PHE HB3 H 2.978 0.000 2 240 168 25 PHE HD1 H 6.561 0.000 3 241 168 25 PHE HE1 H 6.862 0.000 3 242 168 25 PHE HZ H 6.540 0.000 1 243 168 25 PHE CA C 62.488 0.000 1 244 168 25 PHE CB C 39.028 0.000 1 245 168 25 PHE CD1 C 132.277 0.000 3 246 168 25 PHE CE1 C 130.561 0.000 3 247 168 25 PHE CZ C 128.936 0.000 1 248 168 25 PHE N N 124.237 0.000 1 249 169 26 TYR H H 9.097 0.000 1 250 169 26 TYR HA H 4.019 0.000 1 251 169 26 TYR HB2 H 3.114 0.000 1 252 169 26 TYR HB3 H 2.943 0.000 2 253 169 26 TYR HD1 H 7.381 0.000 3 254 169 26 TYR HE1 H 6.691 0.000 3 255 169 26 TYR CA C 63.234 0.000 1 256 169 26 TYR CB C 37.343 0.000 1 257 169 26 TYR CD1 C 132.724 0.000 3 258 169 26 TYR CE1 C 118.260 0.000 3 259 169 26 TYR N N 117.738 0.000 1 260 170 27 LYS H H 8.225 0.000 1 261 170 27 LYS HA H 4.004 0.000 1 262 170 27 LYS HB2 H 1.943 0.000 1 263 170 27 LYS HB3 H 1.882 0.000 2 264 170 27 LYS HE2 H 2.953 0.000 1 265 170 27 LYS HG2 H 1.574 0.000 1 266 170 27 LYS HG3 H 1.400 0.000 2 267 170 27 LYS CA C 60.184 0.000 1 268 170 27 LYS CB C 32.266 0.000 1 269 170 27 LYS CE C 41.870 0.000 1 270 170 27 LYS CG C 25.622 0.000 1 271 170 27 LYS N N 120.738 0.000 1 272 171 28 THR H H 7.615 0.000 1 273 171 28 THR HA H 3.882 0.000 1 274 171 28 THR HB H 3.967 0.000 1 275 171 28 THR HG2 H 1.004 0.000 1 276 171 28 THR CA C 67.117 0.000 1 277 171 28 THR CB C 68.165 0.000 1 278 171 28 THR CG2 C 21.489 0.000 1 279 171 28 THR N N 117.515 0.000 1 280 172 29 LEU H H 8.611 0.000 1 281 172 29 LEU HA H 3.606 0.000 1 282 172 29 LEU HB2 H 1.146 0.000 1 283 172 29 LEU HB3 H 1.707 0.000 2 284 172 29 LEU HD1 H 0.689 0.000 2 285 172 29 LEU HD2 H 0.697 0.000 2 286 172 29 LEU HG H 1.453 0.000 1 287 172 29 LEU CA C 57.840 0.000 1 288 172 29 LEU CB C 42.543 0.000 1 289 172 29 LEU CD1 C 25.746 0.000 2 290 172 29 LEU CD2 C 26.645 0.000 2 291 172 29 LEU CG C 26.305 0.000 1 292 172 29 LEU N N 124.197 0.000 1 293 173 30 ARG H H 7.755 0.000 1 294 173 30 ARG HA H 4.012 0.000 1 295 173 30 ARG HB2 H 1.923 0.000 1 296 173 30 ARG HB3 H 1.724 0.000 2 297 173 30 ARG HD2 H 3.219 0.000 1 298 173 30 ARG HD3 H 3.257 0.000 2 299 173 30 ARG HE H 7.155 0.000 1 300 173 30 ARG CA C 59.091 0.000 1 301 173 30 ARG CB C 29.940 0.000 1 302 173 30 ARG CD C 43.541 0.000 1 303 173 30 ARG N N 116.215 0.000 1 304 173 30 ARG NE N 84.650 0.000 1 305 174 31 ALA H H 7.138 0.000 1 306 174 31 ALA HA H 4.357 0.000 1 307 174 31 ALA HB H 1.491 0.000 1 308 174 31 ALA CA C 52.107 0.000 1 309 174 31 ALA CB C 19.291 0.000 1 310 174 31 ALA N N 118.911 0.000 1 311 175 32 GLU H H 7.453 0.000 1 312 175 32 GLU HA H 4.077 0.000 1 313 175 32 GLU HB2 H 1.994 0.000 1 314 175 32 GLU HG2 H 2.366 0.000 1 315 175 32 GLU HG3 H 2.108 0.000 2 316 175 32 GLU CA C 56.736 0.000 1 317 175 32 GLU CB C 30.190 0.000 1 318 175 32 GLU N N 120.518 0.000 1 319 176 33 GLN H H 8.819 0.000 1 320 176 33 GLN HA H 4.467 0.000 1 321 176 33 GLN HB2 H 2.038 0.000 1 322 176 33 GLN HB3 H 2.187 0.000 2 323 176 33 GLN HE21 H 7.465 0.000 2 324 176 33 GLN HE22 H 6.846 0.000 2 325 176 33 GLN HG2 H 2.363 0.000 1 326 176 33 GLN HG3 H 2.397 0.000 2 327 176 33 GLN CA C 54.909 0.000 1 328 176 33 GLN CB C 27.621 0.000 1 329 176 33 GLN CG C 33.554 0.000 1 330 176 33 GLN N N 123.933 0.000 1 331 176 33 GLN NE2 N 112.672 0.000 1 332 177 34 ALA H H 7.610 0.000 1 333 177 34 ALA HA H 4.536 0.000 1 334 177 34 ALA HB H 1.208 0.000 1 335 177 34 ALA CA C 51.066 0.000 1 336 177 34 ALA CB C 20.821 0.000 1 337 177 34 ALA N N 124.550 0.000 1 338 178 35 SER H H 8.659 0.000 1 339 178 35 SER HA H 4.408 0.000 1 340 178 35 SER HB2 H 4.071 0.000 1 341 178 35 SER HB3 H 4.409 0.000 2 342 178 35 SER CA C 57.391 0.000 1 343 178 35 SER CB C 64.733 0.000 1 344 178 35 SER N N 116.129 0.000 1 345 179 36 GLN H H 9.046 0.000 1 346 179 36 GLN HA H 3.859 0.000 1 347 179 36 GLN HB2 H 2.080 0.000 1 348 179 36 GLN HB3 H 2.240 0.000 2 349 179 36 GLN HE21 H 7.546 0.000 2 350 179 36 GLN HE22 H 7.034 0.000 2 351 179 36 GLN HG2 H 2.482 0.000 1 352 179 36 GLN HG3 H 2.420 0.000 2 353 179 36 GLN CA C 58.928 0.000 1 354 179 36 GLN CB C 27.966 0.000 1 355 179 36 GLN CG C 33.589 0.000 1 356 179 36 GLN N N 121.277 0.000 1 357 179 36 GLN NE2 N 114.329 0.000 1 358 180 37 GLU H H 8.667 0.000 1 359 180 37 GLU HA H 4.081 0.000 1 360 180 37 GLU HB2 H 2.065 0.000 1 361 180 37 GLU HB3 H 1.856 0.000 2 362 180 37 GLU HG2 H 2.323 0.000 1 363 180 37 GLU HG3 H 2.278 0.000 2 364 180 37 GLU CA C 60.001 0.000 1 365 180 37 GLU CB C 29.548 0.000 1 366 180 37 GLU CG C 36.603 0.000 1 367 180 37 GLU N N 118.270 0.000 1 368 181 38 VAL H H 7.349 0.000 1 369 181 38 VAL HA H 3.563 0.000 1 370 181 38 VAL HB H 2.001 0.000 1 371 181 38 VAL HG1 H 0.822 0.000 2 372 181 38 VAL HG2 H -0.040 0.000 2 373 181 38 VAL CA C 66.469 0.000 1 374 181 38 VAL CB C 30.788 0.000 1 375 181 38 VAL CG1 C 23.543 0.000 2 376 181 38 VAL CG2 C 20.019 0.000 2 377 181 38 VAL N N 120.988 0.000 1 378 182 39 LYS H H 8.658 0.000 1 379 182 39 LYS HA H 4.055 0.000 1 380 182 39 LYS HB2 H 1.500 0.000 1 381 182 39 LYS HB3 H 1.565 0.000 2 382 182 39 LYS HE2 H 3.003 0.000 1 383 182 39 LYS HE3 H 2.861 0.000 2 384 182 39 LYS HG2 H 1.531 0.000 1 385 182 39 LYS HG3 H 1.732 0.000 2 386 182 39 LYS CA C 60.664 0.000 1 387 182 39 LYS CB C 32.030 0.000 1 388 182 39 LYS N N 120.562 0.000 1 389 183 40 ASN H H 8.661 0.000 1 390 183 40 ASN HA H 4.489 0.000 1 391 183 40 ASN HB2 H 2.984 0.000 1 392 183 40 ASN HD21 H 7.785 0.000 2 393 183 40 ASN HD22 H 6.999 0.000 2 394 183 40 ASN CA C 55.866 0.000 1 395 183 40 ASN CB C 37.343 0.000 1 396 183 40 ASN N N 119.246 0.000 1 397 183 40 ASN ND2 N 111.459 0.000 1 398 184 41 TRP H H 7.679 0.000 1 399 184 41 TRP HA H 4.298 0.000 1 400 184 41 TRP HB2 H 3.354 0.000 1 401 184 41 TRP HB3 H 3.602 0.000 2 402 184 41 TRP HD1 H 7.438 0.000 1 403 184 41 TRP HE1 H 10.552 0.000 1 404 184 41 TRP HE3 H 7.146 0.000 1 405 184 41 TRP HH2 H 6.982 0.000 1 406 184 41 TRP HZ2 H 7.309 0.000 1 407 184 41 TRP HZ3 H 6.652 0.000 1 408 184 41 TRP CA C 62.154 0.000 1 409 184 41 TRP CB C 28.428 0.000 1 410 184 41 TRP CD1 C 126.932 0.000 1 411 184 41 TRP CE3 C 119.782 0.000 1 412 184 41 TRP CH2 C 122.484 0.000 1 413 184 41 TRP CZ2 C 114.629 0.000 1 414 184 41 TRP CZ3 C 121.319 0.000 1 415 184 41 TRP N N 122.953 0.000 1 416 184 41 TRP NE1 N 130.469 0.000 1 417 185 42 MET H H 9.080 0.000 1 418 185 42 MET HA H 3.452 0.000 1 419 185 42 MET HB2 H 3.003 0.000 2 420 185 42 MET HE H 1.408 0.000 1 421 185 42 MET HG2 H 2.390 0.000 2 422 185 42 MET CA C 60.108 0.000 1 423 185 42 MET N N 120.415 0.000 1 424 186 43 THR H H 8.174 0.000 1 425 186 43 THR HA H 3.809 0.000 1 426 186 43 THR HB H 4.387 0.000 1 427 186 43 THR HG2 H 1.244 0.000 1 428 186 43 THR CA C 66.416 0.000 1 429 186 43 THR CB C 68.708 0.000 1 430 186 43 THR CG2 C 22.657 0.000 1 431 186 43 THR N N 112.364 0.000 1 432 187 44 GLU H H 7.720 0.000 1 433 187 44 GLU HA H 4.075 0.000 1 434 187 44 GLU HB2 H 1.992 0.000 1 435 187 44 GLU HG2 H 2.386 0.000 1 436 187 44 GLU HG3 H 2.227 0.000 2 437 187 44 GLU CA C 58.258 0.000 1 438 187 44 GLU CB C 30.411 0.000 1 439 187 44 GLU CG C 36.441 0.000 1 440 187 44 GLU N N 118.729 0.000 1 441 188 45 THR H H 7.785 0.000 1 442 188 45 THR HA H 4.161 0.000 1 443 188 45 THR HB H 2.752 0.000 1 444 188 45 THR HG2 H 0.832 0.000 1 445 188 45 THR CA C 64.417 0.000 1 446 188 45 THR CB C 69.552 0.000 1 447 188 45 THR CG2 C 21.166 0.000 1 448 188 45 THR N N 111.783 0.000 1 449 189 46 LEU H H 7.539 0.000 1 450 189 46 LEU HA H 3.882 0.000 1 451 189 46 LEU HB2 H 1.965 0.000 1 452 189 46 LEU HB3 H 1.625 0.000 2 453 189 46 LEU HD1 H 0.945 0.000 2 454 189 46 LEU HD2 H 0.892 0.000 2 455 189 46 LEU HG H 1.641 0.000 1 456 189 46 LEU CA C 57.592 0.000 1 457 189 46 LEU CB C 41.740 0.000 1 458 189 46 LEU CD1 C 25.898 0.000 2 459 189 46 LEU CD2 C 24.721 0.000 2 460 189 46 LEU N N 120.964 0.000 1 461 190 47 LEU H H 6.927 0.000 1 462 190 47 LEU HA H 3.320 0.000 1 463 190 47 LEU HB2 H 1.433 0.000 1 464 190 47 LEU HB3 H 0.580 0.000 2 465 190 47 LEU HD1 H -0.059 0.000 2 466 190 47 LEU HD2 H 0.678 0.000 2 467 190 47 LEU HG H 0.993 0.000 1 468 190 47 LEU CA C 58.090 0.000 1 469 190 47 LEU CB C 41.571 0.000 1 470 190 47 LEU CD1 C 23.941 0.000 2 471 190 47 LEU CD2 C 25.674 0.000 2 472 190 47 LEU CG C 26.632 0.000 1 473 190 47 LEU N N 118.484 0.000 1 474 191 48 VAL H H 7.298 0.000 1 475 191 48 VAL HA H 3.541 0.000 1 476 191 48 VAL HB H 1.878 0.000 1 477 191 48 VAL HG1 H 0.676 0.000 2 478 191 48 VAL HG2 H 0.914 0.000 2 479 191 48 VAL CA C 65.641 0.000 1 480 191 48 VAL CB C 31.650 0.000 1 481 191 48 VAL CG1 C 22.699 0.000 2 482 191 48 VAL CG2 C 21.244 0.000 2 483 191 48 VAL N N 115.838 0.000 1 484 192 49 GLN H H 7.516 0.000 1 485 192 49 GLN HA H 3.851 0.000 1 486 192 49 GLN HB2 H 2.122 0.000 1 487 192 49 GLN HB3 H 1.978 0.000 2 488 192 49 GLN HE21 H 7.604 0.000 2 489 192 49 GLN HE22 H 6.971 0.000 2 490 192 49 GLN HG2 H 2.423 0.000 1 491 192 49 GLN CA C 58.782 0.000 1 492 192 49 GLN CB C 28.017 0.000 1 493 192 49 GLN CG C 32.864 0.000 1 494 192 49 GLN N N 116.669 0.000 1 495 192 49 GLN NE2 N 111.545 0.000 1 496 193 50 ASN H H 7.938 0.000 1 497 193 50 ASN HA H 4.941 0.000 1 498 193 50 ASN HB2 H 3.348 0.000 1 499 193 50 ASN HB3 H 3.654 0.000 2 500 193 50 ASN HD21 H 7.800 0.000 2 501 193 50 ASN HD22 H 6.280 0.000 2 502 193 50 ASN CA C 52.635 0.000 1 503 193 50 ASN CB C 38.126 0.000 1 504 193 50 ASN N N 114.871 0.000 1 505 193 50 ASN ND2 N 108.110 0.000 1 506 194 51 ALA H H 7.265 0.000 1 507 194 51 ALA HA H 4.249 0.000 1 508 194 51 ALA HB H 1.611 0.000 1 509 194 51 ALA CA C 51.843 0.000 1 510 194 51 ALA CB C 18.693 0.000 1 511 194 51 ALA N N 124.652 0.000 1 512 195 52 ASN H H 9.088 0.000 1 513 195 52 ASN HA H 4.634 0.000 1 514 195 52 ASN HB2 H 2.278 0.000 1 515 195 52 ASN HB3 H 3.228 0.000 2 516 195 52 ASN HD21 H 7.579 0.000 2 517 195 52 ASN HD22 H 7.004 0.000 2 518 195 52 ASN CA C 51.442 0.000 1 519 195 52 ASN CB C 35.186 0.000 1 520 195 52 ASN N N 119.264 0.000 1 521 195 52 ASN ND2 N 111.290 0.000 1 522 196 53 PRO HA H 4.129 0.000 1 523 196 53 PRO HB2 H 1.866 0.000 1 524 196 53 PRO HB3 H 2.401 0.000 2 525 196 53 PRO HD2 H 3.887 0.000 1 526 196 53 PRO HD3 H 3.836 0.000 2 527 196 53 PRO CA C 66.720 0.000 1 528 196 53 PRO CB C 31.947 0.000 1 529 196 53 PRO CD C 50.100 0.000 1 530 197 54 ASP H H 7.728 0.000 1 531 197 54 ASP HA H 4.404 0.000 1 532 197 54 ASP HB2 H 2.574 0.000 1 533 197 54 ASP CA C 57.234 0.000 1 534 197 54 ASP CB C 40.971 0.000 1 535 197 54 ASP N N 115.502 0.000 1 536 198 55 CYS H H 8.574 0.000 1 537 198 55 CYS HA H 4.275 0.000 1 538 198 55 CYS HB2 H 2.551 0.000 1 539 198 55 CYS HB3 H 3.252 0.000 2 540 198 55 CYS CA C 63.642 0.000 1 541 198 55 CYS CB C 27.622 0.000 1 542 198 55 CYS N N 116.555 0.000 1 543 199 56 LYS H H 9.499 0.000 1 544 199 56 LYS HA H 3.644 0.000 1 545 199 56 LYS HB2 H 1.814 0.000 1 546 199 56 LYS HB3 H 1.724 0.000 2 547 199 56 LYS HD2 H 1.658 0.000 1 548 199 56 LYS HG2 H 1.317 0.000 1 549 199 56 LYS HG3 H 1.421 0.000 2 550 199 56 LYS CA C 61.467 0.000 1 551 199 56 LYS CB C 32.343 0.000 1 552 199 56 LYS CD C 29.605 0.000 1 553 199 56 LYS CG C 25.551 0.000 1 554 199 56 LYS N N 121.805 0.000 1 555 200 57 THR H H 7.594 0.000 1 556 200 57 THR HA H 3.780 0.000 1 557 200 57 THR HB H 4.197 0.000 1 558 200 57 THR HG2 H 1.246 0.000 1 559 200 57 THR CA C 66.613 0.000 1 560 200 57 THR CB C 68.837 0.000 1 561 200 57 THR CG2 C 21.489 0.000 1 562 200 57 THR N N 112.995 0.000 1 563 201 58 ILE H H 6.791 0.000 1 564 201 58 ILE HA H 3.646 0.000 1 565 201 58 ILE HB H 1.889 0.000 1 566 201 58 ILE HD1 H 0.726 0.000 1 567 201 58 ILE HG12 H 1.687 0.000 1 568 201 58 ILE HG13 H 1.098 0.000 2 569 201 58 ILE HG2 H 0.881 0.000 1 570 201 58 ILE CA C 64.399 0.000 1 571 201 58 ILE CB C 38.332 0.000 1 572 201 58 ILE CD1 C 18.382 0.000 1 573 201 58 ILE CG1 C 28.958 0.000 1 574 201 58 ILE CG2 C 13.849 0.000 1 575 201 58 ILE N N 122.437 0.000 1 576 202 59 LEU H H 8.511 0.000 1 577 202 59 LEU HA H 3.747 0.000 1 578 202 59 LEU HB2 H 1.297 0.000 1 579 202 59 LEU HB3 H 1.742 0.000 2 580 202 59 LEU HD1 H 0.649 0.000 2 581 202 59 LEU HD2 H 0.569 0.000 2 582 202 59 LEU HG H 1.610 0.000 1 583 202 59 LEU CA C 57.610 0.000 1 584 202 59 LEU CB C 41.977 0.000 1 585 202 59 LEU CD1 C 25.843 0.000 2 586 202 59 LEU CD2 C 22.469 0.000 2 587 202 59 LEU CG C 26.236 0.000 1 588 202 59 LEU N N 118.897 0.000 1 589 203 60 LYS H H 8.454 0.000 1 590 203 60 LYS HA H 3.954 0.000 1 591 203 60 LYS HB2 H 1.799 0.000 1 592 203 60 LYS HD2 H 1.584 0.000 1 593 203 60 LYS HE2 H 2.858 0.000 1 594 203 60 LYS HG2 H 1.310 0.000 1 595 203 60 LYS HG3 H 1.499 0.000 2 596 203 60 LYS CA C 58.841 0.000 1 597 203 60 LYS CB C 31.681 0.000 1 598 203 60 LYS CD C 28.934 0.000 1 599 203 60 LYS CE C 41.731 0.000 1 600 203 60 LYS CG C 25.221 0.000 1 601 203 60 LYS N N 118.609 0.000 1 602 204 61 ALA H H 7.162 0.000 1 603 204 61 ALA HA H 4.264 0.000 1 604 204 61 ALA HB H 1.497 0.000 1 605 204 61 ALA CA C 53.304 0.000 1 606 204 61 ALA CB C 18.391 0.000 1 607 204 61 ALA N N 120.248 0.000 1 608 205 62 LEU H H 7.466 0.000 1 609 205 62 LEU HA H 4.180 0.000 1 610 205 62 LEU HB2 H 1.618 0.000 1 611 205 62 LEU HB3 H 1.856 0.000 2 612 205 62 LEU HD1 H 0.759 0.000 2 613 205 62 LEU HD2 H 0.768 0.000 2 614 205 62 LEU HG H 1.915 0.000 1 615 205 62 LEU CA C 56.084 0.000 1 616 205 62 LEU CB C 42.595 0.000 1 617 205 62 LEU CD1 C 22.814 0.000 2 618 205 62 LEU CD2 C 26.009 0.000 2 619 205 62 LEU CG C 26.088 0.000 1 620 205 62 LEU N N 118.117 0.000 1 621 206 63 GLY H H 7.502 0.000 1 622 206 63 GLY HA2 H 4.012 0.000 1 623 206 63 GLY HA3 H 4.316 0.000 2 624 206 63 GLY CA C 44.555 0.000 1 625 206 63 GLY N N 104.586 0.000 1 626 207 64 PRO HA H 4.351 0.000 1 627 207 64 PRO HB2 H 2.034 0.000 1 628 207 64 PRO HB3 H 2.259 0.000 2 629 207 64 PRO HD2 H 3.604 0.000 1 630 207 64 PRO HD3 H 3.718 0.000 2 631 207 64 PRO HG2 H 1.968 0.000 1 632 207 64 PRO HG3 H 2.047 0.000 2 633 207 64 PRO CA C 64.180 0.000 1 634 207 64 PRO CB C 31.986 0.000 1 635 207 64 PRO CD C 49.853 0.000 1 636 207 64 PRO CG C 26.948 0.000 1 637 208 65 ALA H H 8.395 0.000 1 638 208 65 ALA HA H 4.469 0.000 1 639 208 65 ALA HB H 1.377 0.000 1 640 208 65 ALA CA C 51.435 0.000 1 641 208 65 ALA CB C 18.354 0.000 1 642 208 65 ALA N N 121.525 0.000 1 643 209 66 ALA H H 7.168 0.000 1 644 209 66 ALA HA H 4.392 0.000 1 645 209 66 ALA HB H 1.337 0.000 1 646 209 66 ALA CA C 52.642 0.000 1 647 209 66 ALA CB C 19.873 0.000 1 648 209 66 ALA N N 122.862 0.000 1 649 210 67 THR H H 8.579 0.000 1 650 210 67 THR HA H 4.449 0.000 1 651 210 67 THR HB H 4.741 0.000 1 652 210 67 THR HG2 H 1.377 0.000 1 653 210 67 THR CA C 60.243 0.000 1 654 210 67 THR CB C 71.564 0.000 1 655 210 67 THR CG2 C 21.784 0.000 1 656 210 67 THR N N 113.347 0.000 1 657 211 68 LEU H H 8.881 0.000 1 658 211 68 LEU HA H 4.301 0.000 1 659 211 68 LEU HB2 H 1.740 0.000 1 660 211 68 LEU HB3 H 1.640 0.000 2 661 211 68 LEU HD1 H 1.015 0.000 2 662 211 68 LEU HD2 H 0.788 0.000 2 663 211 68 LEU HG H 1.618 0.000 1 664 211 68 LEU CA C 58.242 0.000 1 665 211 68 LEU CB C 41.154 0.000 1 666 211 68 LEU CD1 C 22.930 0.000 2 667 211 68 LEU CD2 C 24.878 0.000 2 668 211 68 LEU CG C 27.109 0.000 1 669 211 68 LEU N N 122.590 0.000 1 670 212 69 GLU H H 8.578 0.000 1 671 212 69 GLU HA H 3.981 0.000 1 672 212 69 GLU HB2 H 1.940 0.000 1 673 212 69 GLU HB3 H 2.042 0.000 2 674 212 69 GLU HG2 H 2.324 0.000 1 675 212 69 GLU HG3 H 2.256 0.000 2 676 212 69 GLU CA C 60.316 0.000 1 677 212 69 GLU CB C 28.958 0.000 1 678 212 69 GLU CG C 36.404 0.000 1 679 212 69 GLU N N 117.611 0.000 1 680 213 70 GLU H H 7.757 0.000 1 681 213 70 GLU HA H 3.981 0.000 1 682 213 70 GLU HB2 H 1.926 0.000 1 683 213 70 GLU HB3 H 2.433 0.000 2 684 213 70 GLU HG2 H 2.375 0.000 1 685 213 70 GLU HG3 H 2.294 0.000 2 686 213 70 GLU CA C 59.094 0.000 1 687 213 70 GLU CB C 29.559 0.000 1 688 213 70 GLU CG C 37.362 0.000 1 689 213 70 GLU N N 120.437 0.000 1 690 214 71 MET H H 8.552 0.000 1 691 214 71 MET HA H 3.600 0.000 1 692 214 71 MET HB2 H 1.832 0.000 1 693 214 71 MET HB3 H 2.525 0.000 2 694 214 71 MET HE H 2.009 0.000 1 695 214 71 MET HG2 H 2.118 0.000 1 696 214 71 MET HG3 H 2.835 0.000 2 697 214 71 MET CA C 60.168 0.000 1 698 214 71 MET CB C 33.002 0.000 1 699 214 71 MET CE C 17.527 0.000 1 700 214 71 MET CG C 32.574 0.000 1 701 214 71 MET N N 120.177 0.000 1 702 215 72 MET H H 8.783 0.000 1 703 215 72 MET HA H 4.207 0.000 1 704 215 72 MET HB2 H 2.512 0.000 1 705 215 72 MET HB3 H 2.991 0.000 2 706 215 72 MET HE H 2.049 0.000 1 707 215 72 MET HG2 H 2.157 0.000 1 708 215 72 MET HG3 H 2.398 0.000 2 709 215 72 MET CA C 59.427 0.000 1 710 215 72 MET CB C 32.669 0.000 1 711 215 72 MET CE C 16.836 0.000 1 712 215 72 MET CG C 32.630 0.000 1 713 215 72 MET N N 116.976 0.000 1 714 216 73 THR H H 8.360 0.000 1 715 216 73 THR HA H 3.908 0.000 1 716 216 73 THR HB H 4.168 0.000 1 717 216 73 THR HG2 H 1.229 0.000 1 718 216 73 THR CA C 66.522 0.000 1 719 216 73 THR CB C 68.618 0.000 1 720 216 73 THR CG2 C 21.686 0.000 1 721 216 73 THR N N 116.945 0.000 1 722 217 74 ALA H H 7.994 0.000 1 723 217 74 ALA HA H 4.157 0.000 1 724 217 74 ALA HB H 1.446 0.000 1 725 217 74 ALA CA C 54.812 0.000 1 726 217 74 ALA CB C 19.182 0.000 1 727 217 74 ALA N N 122.838 0.000 1 728 218 75 CYS H H 7.395 0.000 1 729 218 75 CYS HA H 4.395 0.000 1 730 218 75 CYS HB2 H 2.490 0.000 1 731 218 75 CYS HB3 H 3.004 0.000 2 732 218 75 CYS CA C 60.256 0.000 1 733 218 75 CYS CB C 28.290 0.000 1 734 218 75 CYS N N 110.937 0.000 1 735 219 76 GLN H H 7.529 0.000 1 736 219 76 GLN HA H 4.233 0.000 1 737 219 76 GLN HB2 H 2.214 0.000 1 738 219 76 GLN HB3 H 2.360 0.000 2 739 219 76 GLN HE21 H 7.552 0.000 2 740 219 76 GLN HE22 H 6.948 0.000 2 741 219 76 GLN HG2 H 2.605 0.000 1 742 219 76 GLN HG3 H 2.494 0.000 2 743 219 76 GLN CA C 58.342 0.000 1 744 219 76 GLN CB C 28.321 0.000 1 745 219 76 GLN CG C 33.202 0.000 1 746 219 76 GLN N N 122.453 0.000 1 747 219 76 GLN NE2 N 111.559 0.000 1 748 220 77 GLY H H 8.728 0.000 1 749 220 77 GLY HA2 H 3.929 0.000 1 750 220 77 GLY HA3 H 4.035 0.000 2 751 220 77 GLY CA C 45.275 0.000 1 752 220 77 GLY N N 109.969 0.000 1 753 221 78 VAL H H 7.355 0.000 1 754 221 78 VAL HA H 3.830 0.000 1 755 221 78 VAL HB H 2.024 0.000 1 756 221 78 VAL HG1 H 0.910 0.000 2 757 221 78 VAL CA C 63.520 0.000 1 758 221 78 VAL CB C 31.710 0.000 1 759 221 78 VAL CG1 C 21.697 0.000 2 760 221 78 VAL N N 120.419 0.000 1 761 222 79 GLY H H 8.743 0.000 1 762 222 79 GLY HA2 H 3.834 0.000 1 763 222 79 GLY HA3 H 4.111 0.000 2 764 222 79 GLY CA C 45.103 0.000 1 765 222 79 GLY N N 115.911 0.000 1 766 223 80 GLY H H 8.013 0.000 1 767 223 80 GLY HA2 H 4.104 0.000 1 768 223 80 GLY HA3 H 4.235 0.000 2 769 223 80 GLY CA C 44.500 0.000 1 770 223 80 GLY N N 108.167 0.000 1 771 224 81 PRO HA H 4.457 0.000 1 772 224 81 PRO HB2 H 1.970 0.000 1 773 224 81 PRO HB3 H 2.291 0.000 2 774 224 81 PRO HD2 H 3.681 0.000 1 775 224 81 PRO HG2 H 2.056 0.000 1 776 224 81 PRO CA C 63.618 0.000 1 777 224 81 PRO CB C 31.870 0.000 1 778 224 81 PRO CD C 49.560 0.000 1 779 224 81 PRO CG C 26.907 0.000 1 780 225 82 GLY H H 8.567 0.000 1 781 225 82 GLY HA2 H 3.933 0.000 1 782 225 82 GLY CA C 45.199 0.000 1 783 225 82 GLY N N 109.071 0.000 1 784 226 83 HIS H H 8.154 0.000 1 785 226 83 HIS HA H 4.591 0.000 1 786 226 83 HIS HB2 H 3.089 0.000 1 787 226 83 HIS HB3 H 3.142 0.000 2 788 226 83 HIS HD2 H 7.057 0.000 1 789 226 83 HIS HE1 H 7.977 0.000 1 790 226 83 HIS CA C 56.422 0.000 1 791 226 83 HIS CB C 30.665 0.000 1 792 226 83 HIS CD2 C 119.887 0.000 1 793 226 83 HIS CE1 C 138.038 0.000 1 794 226 83 HIS N N 119.653 0.000 1 795 227 84 LYS H H 8.259 0.000 1 796 227 84 LYS HA H 4.052 0.000 1 797 227 84 LYS HB2 H 2.116 0.000 1 798 227 84 LYS CA C 55.250 0.000 1 799 227 84 LYS CB C 32.871 0.000 1 800 227 84 LYS N N 123.422 0.000 1 801 228 85 ALA H H 8.279 0.000 1 802 228 85 ALA HA H 4.279 0.000 1 803 228 85 ALA HB H 1.385 0.000 1 804 228 85 ALA CA C 52.332 0.000 1 805 228 85 ALA CB C 19.217 0.000 1 806 228 85 ALA N N 125.435 0.000 1 807 229 86 ARG H H 8.314 0.000 1 808 229 86 ARG HA H 4.321 0.000 1 809 229 86 ARG HB2 H 1.807 0.000 1 810 229 86 ARG HB3 H 1.772 0.000 2 811 229 86 ARG HD2 H 3.193 0.000 1 812 229 86 ARG HG2 H 1.587 0.000 1 813 229 86 ARG HG3 H 1.646 0.000 2 814 229 86 ARG CA C 56.038 0.000 1 815 229 86 ARG CB C 30.478 0.000 1 816 229 86 ARG CD C 43.194 0.000 1 817 229 86 ARG CG C 26.794 0.000 1 818 229 86 ARG N N 120.961 0.000 1 819 230 87 VAL H H 8.234 0.000 1 820 230 87 VAL HA H 4.108 0.000 1 821 230 87 VAL HB H 2.063 0.000 1 822 230 87 VAL HG1 H 0.939 0.000 2 823 230 87 VAL CA C 62.421 0.000 1 824 230 87 VAL CB C 32.526 0.000 1 825 230 87 VAL CG1 C 20.831 0.000 2 826 230 87 VAL N N 122.991 0.000 1 827 231 88 LEU H H 7.909 0.000 1 828 231 88 LEU HA H 4.197 0.000 1 829 231 88 LEU HB2 H 1.575 0.000 1 830 231 88 LEU HD1 H 0.905 0.000 2 831 231 88 LEU HD2 H 0.848 0.000 2 832 231 88 LEU CA C 56.637 0.000 1 833 231 88 LEU CB C 43.255 0.000 1 834 231 88 LEU CD1 C 24.891 0.000 2 835 231 88 LEU N N 131.856 0.000 1 stop_ save_