data_6099 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N chemical shift assignments for the activation domain of the transcriptional activator VP16 ; _BMRB_accession_number 6099 _BMRB_flat_file_name bmr6099.str _Entry_type original _Submission_date 2004-02-13 _Accession_date 2004-02-13 _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 Jonker Henry . . 2 Folkers Gert . . 3 Wechselberger Rainer . . 4 Boelens Rolf . . 5 Kaptein Rob . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 276 "13C chemical shifts" 224 "15N chemical shifts" 73 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-09-28 original author . stop_ _Original_release_date 2004-09-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural and functional studies on transcriptional activation - Interactions of the cofactor PC4 and activator VP16 ; _Citation_status published _Citation_type thesis _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jonker Henry . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Thesis_institution 'Utrecht University' _Thesis_institution_city Utrecht _Thesis_institution_country 'The Netherlands' _Page_first . _Page_last . _Year 2003 _Details . loop_ _Keyword 'PC4 cofactor VP16 activator transcription' stop_ save_ ################################## # Molecular system description # ################################## save_system_VP16 _Saveframe_category molecular_system _Mol_system_name VP16ad _Abbreviation_common VP16 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'VP16 activation domain' $VP16 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_VP16 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'herpes simplex virion protein 16' _Abbreviation_common VP16 _Molecular_mass 8394 _Mol_thiol_state 'not present' _Details 'The amino terminal domain of VP16 contains two strong activation regions.' ############################## # Polymer residue sequence # ############################## _Residue_count 80 _Mol_residue_sequence ; STAPPTDVSLGDELHLDGED VAMAHADALDDFDLDMLGDG DSPGPGFTPHDSAPYGALDT ADFEFEQMFTDALGIDEYGG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 411 SER 2 412 THR 3 413 ALA 4 414 PRO 5 415 PRO 6 416 THR 7 417 ASP 8 418 VAL 9 419 SER 10 420 LEU 11 421 GLY 12 422 ASP 13 423 GLU 14 424 LEU 15 425 HIS 16 426 LEU 17 427 ASP 18 428 GLY 19 429 GLU 20 430 ASP 21 431 VAL 22 432 ALA 23 433 MET 24 434 ALA 25 435 HIS 26 436 ALA 27 437 ASP 28 438 ALA 29 439 LEU 30 440 ASP 31 441 ASP 32 442 PHE 33 443 ASP 34 444 LEU 35 445 ASP 36 446 MET 37 447 LEU 38 448 GLY 39 449 ASP 40 450 GLY 41 451 ASP 42 452 SER 43 453 PRO 44 454 GLY 45 455 PRO 46 456 GLY 47 457 PHE 48 458 THR 49 459 PRO 50 460 HIS 51 461 ASP 52 462 SER 53 463 ALA 54 464 PRO 55 465 TYR 56 466 GLY 57 467 ALA 58 468 LEU 59 469 ASP 60 470 THR 61 471 ALA 62 472 ASP 63 473 PHE 64 474 GLU 65 475 PHE 66 476 GLU 67 477 GLN 68 478 MET 69 479 PHE 70 480 THR 71 481 ASP 72 482 ALA 73 483 LEU 74 484 GLY 75 485 ILE 76 486 ASP 77 487 GLU 78 488 TYR 79 489 GLY 80 490 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 DBJ BAL03259 "XVE fusion protein [Moss transformation vector pPGX6]" 100.00 483 97.50 98.75 4.72e-44 DBJ BAM21067 "XVE fusion protein [Moss transformation vector pPGX1]" 100.00 483 97.50 98.75 4.72e-44 DBJ BAM21069 "XVE fusion protein [Moss transformation vector pPGX2]" 100.00 483 97.50 98.75 4.72e-44 DBJ BAM21071 "XVE fusion protein [Moss transformation vector pPGX8]" 100.00 483 97.50 98.75 4.72e-44 DBJ BAM21075 "XVE fusion protein [Moss transformation vector pPIG1b-LGXH]" 100.00 483 97.50 98.75 4.72e-44 EMBL CAA26913 "unnamed protein product [Human herpesvirus 1]" 100.00 490 98.75 98.75 2.04e-43 EMBL CAA32298 "tegument protein [Human herpesvirus 1]" 100.00 490 98.75 98.75 2.04e-43 EMBL CAI26306 "tTAV protein [synthetic construct]" 100.00 338 98.75 98.75 1.04e-44 EMBL CAQ68373 "GAL4-VP16-GR [Cloning vector pDEX00]" 100.00 433 97.50 98.75 1.31e-48 GB AAA45766 "alpha trans inducing factor [Human herpesvirus 1]" 100.00 479 98.75 98.75 1.40e-43 GB AAB72093 "chimeric tumour suppressor [synthetic construct]" 100.00 363 97.50 98.75 1.18e-44 GB AAF89185 "GAL4/SV40/VP16 fusion protein [Cloning Vector pACT]" 57.50 89 100.00 100.00 1.88e-10 GB AAG02187 "synthetic VP16-glucocorticoid/ecdysone receptor VgEcR [Cloning vector pFB-ERV]" 97.50 756 98.72 98.72 1.96e-43 GB AAG36984 "XVE fusion protein [plant expression vector pER8]" 100.00 483 97.50 98.75 4.72e-44 REF NP_044650 "transactivating tegument protein VP16 [Human herpesvirus 1]" 100.00 490 98.75 98.75 2.04e-43 SP P04486 "RecName: Full=Tegument protein VP16; AltName: Full=Alpha trans-inducing protein; AltName: Full=Alpha-TIF; AltName: Full=ICP25; " 100.00 490 98.75 98.75 1.94e-43 SP P06492 "RecName: Full=Tegument protein VP16; AltName: Full=Alpha trans-inducing protein; AltName: Full=Alpha-TIF; AltName: Full=ICP25; " 100.00 490 98.75 98.75 2.04e-43 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $VP16 'Herpes Simplex Virus' 10298 Viruses . Herpes simplex 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 _Details $VP16 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)pLysS . ; Overexpression of a GST fusion protein. The GST moiety was removed by thrombin cleavage. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_VP16_298K_LS _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $VP16 . mM 0.5 1 '[U-13C; U-15N]' KCl 50 mM . . . KHxPO4 50 mM . . . D5-Glycin 2 M . . . 'Protease Inhibitor cocktail' . mM . . . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3 loop_ _Task analyses assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details . save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 500 _Details . save_ save_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_Spectrometer_was_locked_on_deuterated_glycine._1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Spectrometer was locked on deuterated glycine.' _Sample_label $sample_VP16_298K_LS save_ save_Triple_resonance_probes._2 _Saveframe_category NMR_applied_experiment _Experiment_name 'Triple resonance probes.' _Sample_label $sample_VP16_298K_LS save_ ####################### # Sample conditions # ####################### save_condition_VP16_298K_LS _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.6 0.1 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 _Indirect_shift_ratio_citation_label _Reference_correction_type _Correction_value_citation_label H2O C 13 protons ppm 4.7 internal indirect . . . 0.251449530 $entry_citation temperature $entry_citation H2O H 1 protons ppm 4.7 internal direct . internal . 1.000000000 $entry_citation temperature $entry_citation H2O N 15 protons ppm 4.7 internal indirect . . . 0.101329118 $entry_citation temperature $entry_citation 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_chemical_shift_VP16_298K_LS _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_VP16_298K_LS stop_ _Sample_conditions_label $condition_VP16_298K_LS _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'VP16 activation domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 THR H H 8.12 . 1 2 . 2 THR N N 114 . 1 3 . 2 THR CA C 61.8 . 1 4 . 2 THR HA H 4.25 . 1 5 . 2 THR C C 173.9 . 1 6 . 2 THR CB C 69.9 . 1 7 . 2 THR HB H 4.16 . 1 8 . 3 ALA H H 8.1 . 1 9 . 3 ALA N N 127.8 . 1 10 . 3 ALA CA C 50.5 . 1 11 . 3 ALA HA H 4.58 . 1 12 . 3 ALA C C 174.8 . 1 13 . 3 ALA CB C 18.6 . 1 14 . 3 ALA HB H 1.31 . 1 15 . 5 PRO CA C 63.1 . 1 16 . 5 PRO HA H 4.46 . 1 17 . 5 PRO C C 177.1 . 1 18 . 5 PRO CB C 32.1 . 1 19 . 5 PRO HB2 H 1.91 . 1 20 . 5 PRO HB3 H 1.91 . 1 21 . 6 THR H H 8.11 . 1 22 . 6 THR N N 113.5 . 1 23 . 6 THR CA C 61.9 . 1 24 . 6 THR HA H 4.26 . 1 25 . 6 THR C C 174.3 . 1 26 . 6 THR CB C 70 . 1 27 . 6 THR HB H 4.18 . 1 28 . 7 ASP H H 8.28 . 1 29 . 7 ASP N N 122.4 . 1 30 . 7 ASP CA C 54.3 . 1 31 . 7 ASP HA H 4.6 . 1 32 . 7 ASP C C 176.1 . 1 33 . 7 ASP CB C 41.1 . 1 34 . 7 ASP HB2 H 2.59 . 2 35 . 7 ASP HB3 H 2.69 . 2 36 . 8 VAL H H 7.94 . 1 37 . 8 VAL N N 119.7 . 1 38 . 8 VAL CA C 62.3 . 1 39 . 8 VAL HA H 4.11 . 1 40 . 8 VAL C C 176.2 . 1 41 . 8 VAL CB C 32.9 . 1 42 . 8 VAL HB H 2.07 . 1 43 . 9 SER H H 8.37 . 1 44 . 9 SER N N 119.4 . 1 45 . 9 SER CA C 58.5 . 1 46 . 9 SER HA H 4.42 . 1 47 . 9 SER C C 174.7 . 1 48 . 9 SER CB C 63.8 . 1 49 . 9 SER HB2 H 3.82 . 1 50 . 9 SER HB3 H 3.82 . 1 51 . 10 LEU H H 8.22 . 1 52 . 10 LEU N N 124.4 . 1 53 . 10 LEU CA C 55.6 . 1 54 . 10 LEU HA H 4.3 . 1 55 . 10 LEU C C 177.9 . 1 56 . 10 LEU CB C 42.4 . 1 57 . 10 LEU HB2 H 1.59 . 1 58 . 10 LEU HB3 H 1.59 . 1 59 . 11 GLY H H 8.28 . 1 60 . 11 GLY N N 109.1 . 1 61 . 11 GLY CA C 45.6 . 1 62 . 11 GLY HA2 H 3.92 . 1 63 . 11 GLY HA3 H 3.92 . 1 64 . 11 GLY C C 174.1 . 1 65 . 12 ASP H H 8.13 . 1 66 . 12 ASP N N 120.4 . 1 67 . 12 ASP CA C 54.4 . 1 68 . 12 ASP HA H 4.57 . 1 69 . 12 ASP C C 176.3 . 1 70 . 12 ASP CB C 41.2 . 1 71 . 12 ASP HB2 H 2.61 . 1 72 . 12 ASP HB3 H 2.61 . 1 73 . 13 GLU H H 8.31 . 1 74 . 13 GLU N N 120.4 . 1 75 . 13 GLU CA C 56.8 . 1 76 . 13 GLU HA H 4.18 . 1 77 . 13 GLU C C 176.1 . 1 78 . 13 GLU CB C 30 . 1 79 . 13 GLU HB2 H 1.89 . 2 80 . 13 GLU HB3 H 1.98 . 2 81 . 14 LEU H H 8.05 . 1 82 . 14 LEU N N 121.9 . 1 83 . 14 LEU CA C 55.2 . 1 84 . 14 LEU HA H 4.22 . 1 85 . 14 LEU C C 176.9 . 1 86 . 14 LEU CB C 42.5 . 1 87 . 14 LEU HB2 H 1.42 . 2 88 . 14 LEU HB3 H 1.53 . 2 89 . 15 HIS H H 8.39 . 1 90 . 15 HIS N N 119.5 . 1 91 . 15 HIS CA C 55.1 . 1 92 . 15 HIS HA H 4.68 . 1 93 . 15 HIS C C 174.2 . 1 94 . 15 HIS CB C 28.8 . 1 95 . 15 HIS HB2 H 3.11 . 2 96 . 15 HIS HB3 H 3.22 . 2 97 . 16 LEU H H 8.29 . 1 98 . 16 LEU N N 123.7 . 1 99 . 16 LEU CA C 55.1 . 1 100 . 16 LEU HA H 4.33 . 1 101 . 16 LEU C C 177 . 1 102 . 16 LEU CB C 42.5 . 1 103 . 16 LEU HB2 H 1.53 . 1 104 . 16 LEU HB3 H 1.53 . 1 105 . 17 ASP H H 8.42 . 1 106 . 17 ASP N N 121 . 1 107 . 17 ASP CA C 54.5 . 1 108 . 17 ASP HA H 4.56 . 1 109 . 17 ASP C C 176.6 . 1 110 . 17 ASP CB C 41.3 . 1 111 . 17 ASP HB2 H 2.6 . 2 112 . 17 ASP HB3 H 2.68 . 2 113 . 18 GLY H H 8.28 . 1 114 . 18 GLY N N 109.2 . 1 115 . 18 GLY CA C 45.7 . 1 116 . 18 GLY HA2 H 3.92 . 1 117 . 18 GLY HA3 H 3.92 . 1 118 . 18 GLY C C 174.4 . 1 119 . 19 GLU H H 8.19 . 1 120 . 19 GLU N N 120.3 . 1 121 . 19 GLU CA C 56.7 . 1 122 . 19 GLU HA H 4.25 . 1 123 . 19 GLU C C 176.2 . 1 124 . 19 GLU CB C 30.2 . 1 125 . 19 GLU HB2 H 1.9 . 2 126 . 19 GLU HB3 H 2.03 . 2 127 . 20 ASP H H 8.37 . 1 128 . 20 ASP N N 121.1 . 1 129 . 20 ASP CA C 54.5 . 1 130 . 20 ASP HA H 4.56 . 1 131 . 20 ASP C C 176.4 . 1 132 . 20 ASP CB C 41 . 1 133 . 20 ASP HB2 H 2.58 . 2 134 . 20 ASP HB3 H 2.69 . 2 135 . 21 VAL H H 7.9 . 1 136 . 21 VAL N N 120.2 . 1 137 . 21 VAL CA C 62.7 . 1 138 . 21 VAL HA H 4.01 . 1 139 . 21 VAL C C 176.1 . 1 140 . 21 VAL CB C 32.7 . 1 141 . 21 VAL HB H 2.05 . 1 142 . 22 ALA H H 8.21 . 1 143 . 22 ALA N N 126.4 . 1 144 . 22 ALA CA C 53 . 1 145 . 22 ALA HA H 4.23 . 1 146 . 22 ALA C C 178 . 1 147 . 22 ALA CB C 19.1 . 1 148 . 22 ALA HB H 1.34 . 1 149 . 23 MET H H 8.08 . 1 150 . 23 MET N N 119 . 1 151 . 23 MET CA C 55.6 . 1 152 . 23 MET HA H 4.34 . 1 153 . 23 MET C C 176 . 1 154 . 23 MET CB C 33 . 1 155 . 23 MET HB2 H 1.97 . 1 156 . 23 MET HB3 H 1.97 . 1 157 . 24 ALA H H 8.08 . 1 158 . 24 ALA N N 124.5 . 1 159 . 24 ALA CA C 52.8 . 1 160 . 24 ALA HA H 4.2 . 1 161 . 24 ALA C C 177.5 . 1 162 . 24 ALA CB C 19.3 . 1 163 . 24 ALA HB H 1.29 . 1 164 . 25 HIS H H 8.32 . 1 165 . 25 HIS N N 117.3 . 1 166 . 25 HIS CA C 55.2 . 1 167 . 25 HIS HA H 4.63 . 1 168 . 25 HIS C C 174.3 . 1 169 . 25 HIS CB C 29.2 . 1 170 . 25 HIS HB2 H 3.12 . 2 171 . 25 HIS HB3 H 3.24 . 2 172 . 26 ALA H H 8.24 . 1 173 . 26 ALA N N 125.2 . 1 174 . 26 ALA CA C 52.9 . 1 175 . 26 ALA HA H 4.25 . 1 176 . 26 ALA C C 177.3 . 1 177 . 26 ALA CB C 19.5 . 1 178 . 26 ALA HB H 1.34 . 1 179 . 27 ASP H H 8.31 . 1 180 . 27 ASP N N 119.5 . 1 181 . 27 ASP CA C 54.4 . 1 182 . 27 ASP HA H 4.52 . 1 183 . 27 ASP C C 175.8 . 1 184 . 27 ASP CB C 41.2 . 1 185 . 27 ASP HB2 H 2.59 . 2 186 . 27 ASP HB3 H 2.67 . 2 187 . 28 ALA H H 8.07 . 1 188 . 28 ALA N N 123.8 . 1 189 . 28 ALA CA C 52.6 . 1 190 . 28 ALA HA H 4.27 . 1 191 . 28 ALA C C 177.5 . 1 192 . 28 ALA CB C 19.5 . 1 193 . 28 ALA HB H 1.33 . 1 194 . 29 LEU H H 8.09 . 1 195 . 29 LEU N N 120.8 . 1 196 . 29 LEU CA C 55.3 . 1 197 . 29 LEU HA H 4.27 . 1 198 . 29 LEU C C 177.2 . 1 199 . 29 LEU CB C 42.3 . 1 200 . 29 LEU HB2 H 1.56 . 1 201 . 29 LEU HB3 H 1.56 . 1 202 . 30 ASP H H 8.15 . 1 203 . 30 ASP N N 120.3 . 1 204 . 30 ASP CA C 54.3 . 1 205 . 30 ASP HA H 4.51 . 1 206 . 30 ASP C C 175.7 . 1 207 . 30 ASP CB C 41.1 . 1 208 . 30 ASP HB2 H 2.56 . 1 209 . 30 ASP HB3 H 2.56 . 1 210 . 31 ASP H H 8.07 . 1 211 . 31 ASP N N 119.8 . 1 212 . 31 ASP CA C 54.3 . 1 213 . 31 ASP HA H 4.51 . 1 214 . 31 ASP C C 175.8 . 1 215 . 31 ASP CB C 40.8 . 1 216 . 31 ASP HB2 H 2.51 . 2 217 . 31 ASP HB3 H 2.58 . 2 218 . 32 PHE H H 7.96 . 1 219 . 32 PHE N N 120.1 . 1 220 . 32 PHE CA C 58 . 1 221 . 32 PHE HA H 4.49 . 1 222 . 32 PHE C C 175.4 . 1 223 . 32 PHE CB C 39.8 . 1 224 . 32 PHE HB2 H 2.99 . 2 225 . 32 PHE HB3 H 3.08 . 2 226 . 33 ASP H H 8.14 . 1 227 . 33 ASP N N 121.5 . 1 228 . 33 ASP CA C 54.2 . 1 229 . 33 ASP HA H 4.54 . 1 230 . 33 ASP C C 176.1 . 1 231 . 33 ASP CB C 40.9 . 1 232 . 33 ASP HB2 H 2.56 . 2 233 . 33 ASP HB3 H 2.68 . 2 234 . 34 LEU H H 8.02 . 1 235 . 34 LEU N N 122.5 . 1 236 . 34 LEU CA C 56 . 1 237 . 34 LEU HA H 4.14 . 1 238 . 34 LEU C C 177.6 . 1 239 . 34 LEU CB C 42.3 . 1 240 . 34 LEU HB2 H 1.56 . 2 241 . 34 LEU HB3 H 1.61 . 2 242 . 35 ASP H H 8.26 . 1 243 . 35 ASP N N 119.9 . 1 244 . 35 ASP CA C 54.9 . 1 245 . 35 ASP HA H 4.51 . 1 246 . 35 ASP C C 176.4 . 1 247 . 35 ASP CB C 40.6 . 1 248 . 35 ASP HB2 H 2.64 . 1 249 . 35 ASP HB3 H 2.64 . 1 250 . 36 MET H H 7.98 . 1 251 . 36 MET N N 119.4 . 1 252 . 36 MET CA C 55.8 . 1 253 . 36 MET HA H 4.38 . 1 254 . 36 MET C C 176.4 . 1 255 . 36 MET CB C 32.7 . 1 256 . 36 MET HB2 H 1.95 . 2 257 . 36 MET HB3 H 2.06 . 2 258 . 37 LEU H H 7.99 . 1 259 . 37 LEU N N 121.8 . 1 260 . 37 LEU CA C 55.6 . 1 261 . 37 LEU HA H 4.29 . 1 262 . 37 LEU C C 177.9 . 1 263 . 37 LEU CB C 42.4 . 1 264 . 37 LEU HB2 H 1.55 . 2 265 . 37 LEU HB3 H 1.67 . 2 266 . 38 GLY H H 8.24 . 1 267 . 38 GLY N N 109.3 . 1 268 . 38 GLY CA C 45.5 . 1 269 . 38 GLY HA2 H 3.92 . 1 270 . 38 GLY HA3 H 3.92 . 1 271 . 38 GLY C C 174 . 1 272 . 39 ASP H H 8.21 . 1 273 . 39 ASP N N 120.4 . 1 274 . 39 ASP CA C 54.3 . 1 275 . 39 ASP HA H 4.59 . 1 276 . 39 ASP C C 176.8 . 1 277 . 39 ASP CB C 41.2 . 1 278 . 39 ASP HB2 H 2.65 . 1 279 . 39 ASP HB3 H 2.65 . 1 280 . 40 GLY H H 8.35 . 1 281 . 40 GLY N N 109.4 . 1 282 . 40 GLY CA C 45.7 . 1 283 . 40 GLY HA2 H 3.91 . 1 284 . 40 GLY HA3 H 3.91 . 1 285 . 40 GLY C C 174 . 1 286 . 41 ASP H H 8.16 . 1 287 . 41 ASP N N 120.2 . 1 288 . 41 ASP CA C 54.2 . 1 289 . 41 ASP HA H 4.63 . 1 290 . 41 ASP C C 175.9 . 1 291 . 41 ASP CB C 41.3 . 1 292 . 41 ASP HB2 H 2.58 . 2 293 . 41 ASP HB3 H 2.65 . 2 294 . 42 SER H H 8.12 . 1 295 . 42 SER N N 116.6 . 1 296 . 42 SER CA C 56.4 . 1 297 . 42 SER HA H 4.68 . 1 298 . 42 SER C C 172.7 . 1 299 . 42 SER CB C 63.5 . 1 300 . 42 SER HB2 H 3.78 . 1 301 . 42 SER HB3 H 3.78 . 1 302 . 43 PRO CA C 63.4 . 1 303 . 43 PRO HA H 4.36 . 1 304 . 43 PRO C C 177.1 . 1 305 . 43 PRO CB C 32.3 . 1 306 . 43 PRO HB2 H 1.87 . 1 307 . 43 PRO HB3 H 1.87 . 1 308 . 44 GLY H H 8.12 . 1 309 . 44 GLY N N 108.8 . 1 310 . 44 GLY CA C 44.6 . 1 311 . 44 GLY HA2 H 4.04 . 1 312 . 44 GLY HA3 H 4.04 . 1 313 . 44 GLY C C 171.9 . 1 314 . 45 PRO CA C 63.6 . 1 315 . 45 PRO HA H 4.37 . 1 316 . 45 PRO C C 177.6 . 1 317 . 45 PRO CB C 32.2 . 1 318 . 46 GLY H H 8.44 . 1 319 . 46 GLY N N 109.2 . 1 320 . 46 GLY CA C 45.3 . 1 321 . 46 GLY HA2 H 3.84 . 1 322 . 46 GLY HA3 H 3.84 . 1 323 . 46 GLY C C 173.7 . 1 324 . 47 PHE H H 7.91 . 1 325 . 47 PHE N N 120.2 . 1 326 . 47 PHE CA C 57.8 . 1 327 . 47 PHE HA H 4.61 . 1 328 . 47 PHE C C 175.2 . 1 329 . 47 PHE CB C 40.1 . 1 330 . 47 PHE HB2 H 3 . 1 331 . 47 PHE HB3 H 3 . 1 332 . 48 THR H H 8.06 . 1 333 . 48 THR N N 119.9 . 1 334 . 48 THR CA C 59.3 . 1 335 . 48 THR HA H 4.51 . 1 336 . 48 THR C C 172.1 . 1 337 . 48 THR CB C 70.1 . 1 338 . 48 THR HB H 3.98 . 1 339 . 49 PRO CA C 63.1 . 1 340 . 49 PRO HA H 4.26 . 1 341 . 49 PRO C C 176.6 . 1 342 . 49 PRO CB C 32.2 . 1 343 . 49 PRO HB2 H 1.82 . 1 344 . 49 PRO HB3 H 1.82 . 1 345 . 50 HIS H H 8.51 . 1 346 . 50 HIS N N 118.6 . 1 347 . 50 HIS CA C 55.5 . 1 348 . 50 HIS HA H 4.61 . 1 349 . 50 HIS C C 174.3 . 1 350 . 50 HIS CB C 29.3 . 1 351 . 50 HIS HB2 H 3.13 . 2 352 . 50 HIS HB3 H 3.2 . 2 353 . 51 ASP H H 8.33 . 1 354 . 51 ASP N N 121.4 . 1 355 . 51 ASP CA C 54.5 . 1 356 . 51 ASP HA H 4.57 . 1 357 . 51 ASP C C 175.9 . 1 358 . 51 ASP CB C 41.3 . 1 359 . 51 ASP HB2 H 2.6 . 1 360 . 51 ASP HB3 H 2.6 . 1 361 . 52 SER H H 8.19 . 1 362 . 52 SER N N 115.9 . 1 363 . 52 SER CA C 58.3 . 1 364 . 52 SER HA H 4.39 . 1 365 . 52 SER C C 173.8 . 1 366 . 52 SER CB C 64.1 . 1 367 . 52 SER HB2 H 3.81 . 1 368 . 52 SER HB3 H 3.81 . 1 369 . 53 ALA H H 8.18 . 1 370 . 53 ALA N N 126.6 . 1 371 . 53 ALA CA C 50.8 . 1 372 . 53 ALA HA H 4.5 . 1 373 . 53 ALA C C 175.5 . 1 374 . 53 ALA CB C 18.6 . 1 375 . 53 ALA HB H 1.25 . 1 376 . 54 PRO CA C 63.3 . 1 377 . 54 PRO HA H 4.32 . 1 378 . 54 PRO C C 176.6 . 1 379 . 54 PRO CB C 31.9 . 1 380 . 55 TYR H H 8.03 . 1 381 . 55 TYR N N 119.6 . 1 382 . 55 TYR CA C 58 . 1 383 . 55 TYR HA H 4.47 . 1 384 . 55 TYR C C 176.4 . 1 385 . 55 TYR CB C 38.7 . 1 386 . 55 TYR HB2 H 2.97 . 1 387 . 55 TYR HB3 H 2.97 . 1 388 . 56 GLY H H 8.16 . 1 389 . 56 GLY N N 110.8 . 1 390 . 56 GLY CA C 45.4 . 1 391 . 56 GLY HA2 H 3.81 . 1 392 . 56 GLY HA3 H 3.81 . 1 393 . 56 GLY C C 173.7 . 1 394 . 57 ALA H H 7.94 . 1 395 . 57 ALA N N 123.6 . 1 396 . 57 ALA CA C 52.5 . 1 397 . 57 ALA HA H 4.25 . 1 398 . 57 ALA C C 177.6 . 1 399 . 57 ALA CB C 19.5 . 1 400 . 57 ALA HB H 1.31 . 1 401 . 58 LEU H H 8.09 . 1 402 . 58 LEU N N 120.7 . 1 403 . 58 LEU CA C 55.2 . 1 404 . 58 LEU HA H 4.27 . 1 405 . 58 LEU C C 177.1 . 1 406 . 58 LEU CB C 42.6 . 1 407 . 58 LEU HB2 H 1.57 . 1 408 . 58 LEU HB3 H 1.57 . 1 409 . 59 ASP H H 8.28 . 1 410 . 59 ASP N N 120.9 . 1 411 . 59 ASP CA C 54.2 . 1 412 . 59 ASP HA H 4.61 . 1 413 . 59 ASP C C 176.3 . 1 414 . 59 ASP CB C 41 . 1 415 . 59 ASP HB2 H 2.59 . 2 416 . 59 ASP HB3 H 2.71 . 2 417 . 60 THR H H 7.91 . 1 418 . 60 THR N N 113.8 . 1 419 . 60 THR CA C 62.1 . 1 420 . 60 THR HA H 4.25 . 1 421 . 60 THR C C 174.5 . 1 422 . 60 THR CB C 69.7 . 1 423 . 60 THR HB H 4.19 . 1 424 . 61 ALA H H 8.18 . 1 425 . 61 ALA N N 125.6 . 1 426 . 61 ALA CA C 53 . 1 427 . 61 ALA HA H 4.22 . 1 428 . 61 ALA C C 177.5 . 1 429 . 61 ALA CB C 19.4 . 1 430 . 61 ALA HB H 1.29 . 1 431 . 62 ASP H H 8.07 . 1 432 . 62 ASP N N 118.7 . 1 433 . 62 ASP CA C 54.5 . 1 434 . 62 ASP HA H 4.51 . 1 435 . 62 ASP C C 176 . 1 436 . 62 ASP CB C 41 . 1 437 . 62 ASP HB2 H 2.53 . 2 438 . 62 ASP HB3 H 2.62 . 2 439 . 63 PHE H H 7.92 . 1 440 . 63 PHE N N 120.1 . 1 441 . 63 PHE CA C 58.2 . 1 442 . 63 PHE HA H 4.49 . 1 443 . 63 PHE C C 175.8 . 1 444 . 63 PHE CB C 39.6 . 1 445 . 63 PHE HB2 H 2.99 . 1 446 . 63 PHE HB3 H 2.99 . 1 447 . 64 GLU H H 8.11 . 1 448 . 64 GLU N N 121.4 . 1 449 . 64 GLU CA C 56.8 . 1 450 . 64 GLU HA H 4.12 . 1 451 . 64 GLU C C 176.2 . 1 452 . 64 GLU CB C 29.8 . 1 453 . 64 GLU HB2 H 1.83 . 1 454 . 64 GLU HB3 H 1.83 . 1 455 . 65 PHE H H 7.98 . 1 456 . 65 PHE N N 120.4 . 1 457 . 65 PHE CA C 58.5 . 1 458 . 65 PHE HA H 4.48 . 1 459 . 65 PHE C C 176 . 1 460 . 65 PHE CB C 39.6 . 1 461 . 65 PHE HB2 H 3 . 2 462 . 65 PHE HB3 H 3.12 . 2 463 . 66 GLU H H 8.19 . 1 464 . 66 GLU N N 121 . 1 465 . 66 GLU CA C 57.1 . 1 466 . 66 GLU HA H 4.12 . 1 467 . 66 GLU C C 176.5 . 1 468 . 66 GLU CB C 29.9 . 1 469 . 66 GLU HB2 H 1.91 . 1 470 . 66 GLU HB3 H 1.91 . 1 471 . 67 GLN H H 8.11 . 1 472 . 67 GLN N N 120.1 . 1 473 . 67 GLN CA C 56.3 . 1 474 . 67 GLN HA H 4.13 . 1 475 . 67 GLN C C 175.9 . 1 476 . 67 GLN CB C 29.3 . 1 477 . 67 GLN HB2 H 1.95 . 1 478 . 67 GLN HB3 H 1.95 . 1 479 . 68 MET H H 8.04 . 1 480 . 68 MET N N 120.3 . 1 481 . 68 MET CA C 56 . 1 482 . 68 MET HA H 4.3 . 1 483 . 68 MET C C 175.9 . 1 484 . 68 MET CB C 33.1 . 1 485 . 68 MET HB2 H 1.82 . 1 486 . 68 MET HB3 H 1.82 . 1 487 . 69 PHE H H 8.09 . 1 488 . 69 PHE N N 120.5 . 1 489 . 69 PHE CA C 57.8 . 1 490 . 69 PHE HA H 4.64 . 1 491 . 69 PHE C C 175.9 . 1 492 . 69 PHE CB C 39.5 . 1 493 . 69 PHE HB2 H 2.91 . 2 494 . 69 PHE HB3 H 3.13 . 2 495 . 70 THR H H 7.97 . 1 496 . 70 THR N N 115.1 . 1 497 . 70 THR CA C 62.2 . 1 498 . 70 THR HA H 4.25 . 1 499 . 70 THR C C 174.3 . 1 500 . 70 THR CB C 69.9 . 1 501 . 70 THR HB H 4.16 . 1 502 . 71 ASP H H 8.22 . 1 503 . 71 ASP N N 122.5 . 1 504 . 71 ASP CA C 54.5 . 1 505 . 71 ASP HA H 4.53 . 1 506 . 71 ASP C C 176 . 1 507 . 71 ASP CB C 41.1 . 1 508 . 71 ASP HB2 H 2.65 . 1 509 . 71 ASP HB3 H 2.65 . 1 510 . 72 ALA H H 8.06 . 1 511 . 72 ALA N N 123.7 . 1 512 . 72 ALA CA C 52.8 . 1 513 . 72 ALA HA H 4.25 . 1 514 . 72 ALA C C 177.7 . 1 515 . 72 ALA CB C 19.4 . 1 516 . 72 ALA HB H 1.34 . 1 517 . 73 LEU H H 8.02 . 1 518 . 73 LEU N N 120.3 . 1 519 . 73 LEU CA C 55.4 . 1 520 . 73 LEU HA H 4.26 . 1 521 . 73 LEU C C 178 . 1 522 . 73 LEU CB C 42.6 . 1 523 . 73 LEU HB2 H 1.55 . 2 524 . 73 LEU HB3 H 1.63 . 2 525 . 74 GLY H H 8.26 . 1 526 . 74 GLY N N 109.3 . 1 527 . 74 GLY CA C 45.6 . 1 528 . 74 GLY HA2 H 3.89 . 1 529 . 74 GLY HA3 H 3.89 . 1 530 . 74 GLY C C 174.2 . 1 531 . 75 ILE H H 7.83 . 1 532 . 75 ILE N N 119.4 . 1 533 . 75 ILE CA C 61.3 . 1 534 . 75 ILE HA H 4.1 . 1 535 . 75 ILE C C 176 . 1 536 . 75 ILE CB C 39 . 1 537 . 75 ILE HB H 1.81 . 1 538 . 76 ASP H H 8.36 . 1 539 . 76 ASP N N 123.5 . 1 540 . 76 ASP CA C 54.4 . 1 541 . 76 ASP HA H 4.55 . 1 542 . 76 ASP C C 176 . 1 543 . 76 ASP CB C 41 . 1 544 . 76 ASP HB2 H 2.59 . 2 545 . 76 ASP HB3 H 2.65 . 2 546 . 77 GLU H H 8.14 . 1 547 . 77 GLU N N 120.9 . 1 548 . 77 GLU CA C 56.6 . 1 549 . 77 GLU HA H 4.18 . 1 550 . 77 GLU C C 176 . 1 551 . 77 GLU CB C 30.1 . 1 552 . 77 GLU HB2 H 1.8 . 2 553 . 77 GLU HB3 H 1.85 . 2 554 . 78 TYR H H 8.16 . 1 555 . 78 TYR N N 120.6 . 1 556 . 78 TYR CA C 58.1 . 1 557 . 78 TYR HA H 4.54 . 1 558 . 78 TYR C C 176.4 . 1 559 . 78 TYR CB C 38.8 . 1 560 . 78 TYR HB2 H 2.89 . 2 561 . 78 TYR HB3 H 3.06 . 2 562 . 79 GLY H H 8.2 . 1 563 . 79 GLY N N 111.3 . 1 564 . 79 GLY CA C 45.5 . 1 565 . 79 GLY HA2 H 3.88 . 1 566 . 79 GLY HA3 H 3.88 . 1 567 . 79 GLY C C 173.7 . 1 568 . 80 GLY H H 7.56 . 1 569 . 80 GLY N N 114.8 . 1 570 . 80 GLY CA C 46.1 . 1 571 . 80 GLY HA2 H 3.7 . 1 572 . 80 GLY HA3 H 3.7 . 1 573 . 80 GLY C C 179 . 1 stop_ save_