data_6916 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR structure of the C-terminal domain (dimer) of HPV45 oncoprotein E7 ; _BMRB_accession_number 6916 _BMRB_flat_file_name bmr6916.str _Entry_type original _Submission_date 2005-12-05 _Accession_date 2005-12-21 _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 Ohlenschlager O. . . 2 Gorlach M. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 316 "13C chemical shifts" 241 "15N chemical shifts" 56 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-05-02 original author 'original release' 2006-08-25 update author 'changed the system to dimer, etc.' 2007-11-15 update BMRB 'complete entry citation' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16636661 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ohlenschlager O. . . 2 Seiboth T. . . 3 Zengerling H. . . 4 Briese L. . . 5 Marchanka A. . . 6 Ramachandran R. . . 7 Baum M. . . 8 Korbas M. . . 9 Meyer-Klaucke W. . . 10 Durst M. . . 11 Gorlach M. . . stop_ _Journal_abbreviation Oncogene _Journal_volume 25 _Journal_issue 44 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5953 _Page_last 5959 _Year 2006 _Details . loop_ _Keyword E7 HPV ONCOPROTEIN 'ZINC BINDING' stop_ save_ ################################## # Molecular system description # ################################## save_system_1 _Saveframe_category molecular_system _Mol_system_name 'Protein E7' _Abbreviation_common 'Protein E7' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Protein E7, chain 1' $Protein-E7 'Protein E7, chain 2' $Protein-E7 'ZINC ION, 1' $ZN 'ZINC ION, 2' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state homodimer _System_paramagnetic no _System_thiol_state 'other bound and free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Protein-E7 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Protein E7' _Abbreviation_common 'Protein E7' _Molecular_mass . _Mol_thiol_state 'other bound and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; GSHMAEPQRHKILCVCCKCD GRIELTVESSAEDLRTLQQL FLSTLSFVCPWCATNQ ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 ALA 6 GLU 7 PRO 8 GLN 9 ARG 10 HIS 11 LYS 12 ILE 13 LEU 14 CYS 15 VAL 16 CYS 17 CYS 18 LYS 19 CYS 20 ASP 21 GLY 22 ARG 23 ILE 24 GLU 25 LEU 26 THR 27 VAL 28 GLU 29 SER 30 SER 31 ALA 32 GLU 33 ASP 34 LEU 35 ARG 36 THR 37 LEU 38 GLN 39 GLN 40 LEU 41 PHE 42 LEU 43 SER 44 THR 45 LEU 46 SER 47 PHE 48 VAL 49 CYS 50 PRO 51 TRP 52 CYS 53 ALA 54 THR 55 ASN 56 GLN stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 SWISS-PROT P21736 'Protein E7' 92.86 106 100.00 100.00 8.79e-23 GenBank ABP99833 'E7 [Human papillomavirus type 45]' 92.86 106 98.08 100.00 1.86e-22 GenBank ABP99825 'E7 [Human papillomavirus type 45]' 92.86 106 98.08 100.00 1.86e-22 GenBank ABP99817 'E7 [Human papillomavirus type 45]' 92.86 106 98.08 100.00 1.86e-22 GenBank ABP99809 'E7 [Human papillomavirus type 45]' 92.86 106 100.00 100.00 8.79e-23 GenBank AAA46974 E7 92.86 106 100.00 100.00 7.14e-23 EMBL CAB44707 'E7 protein [Homo sapiens]' 92.86 106 98.08 100.00 1.86e-22 EMBL CAA73661 'oncoprotein E7 [Human papillomavirus type 45]' 92.86 106 98.08 100.00 1.86e-22 EMBL CAA52574 'early protein [Human papillomavirus type 45]' 92.86 106 100.00 100.00 8.79e-23 PDB 2F8B 'Nmr Structure Of The C-Terminal Domain (Dimer) Of Hpv45 Oncoprotein E7' 100.00 56 100.00 100.00 3.72e-25 PDB 2EWL 'Solution Structure Of The C-Terminal Domain (Monomer) Of The Hpv45 Oncoprotein E7' 100.00 56 100.00 100.00 3.72e-25 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Fri Jun 10 14:23:33 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Protein-E7 'Human papillomavirus' 10566 Viruses . . . 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 $Protein-E7 'recombinant technology' 'E. coli' Escherichia coli . . 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 $Protein-E7 1 mM [U-15N] d-TRIS 20 mM . NaCl 100 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Protein-E7 1 mM '[U-13C; U-15N]' d-TRIS 20 mM . NaCl 100 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version '6.1 rev. C' loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.9 loop_ _Task 'data analysis' stop_ _Details 'Xia and Bartels' save_ save_CYANA _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Task 'structure solution' stop_ _Details 'Guntert et al' save_ save_OPAL _Saveframe_category software _Name OPAL _Version 2.6 loop_ _Task refinement stop_ _Details 'Luginbuhl et al' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 120 . mM pH 7.4 . pH pressure 1 . atm temperature 298 . 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 _Correction_value_citation_label DIOXANE C 13 'methylene carbons' ppm 67.80 external direct . . . 1.0 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 external direct . . . 1.0 $entry_citation $entry_citation NH4Cl N 15 nitrogen ppm 24.93 external direct . . . 1.0 $entry_citation $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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Protein E7, chain 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY CA C 43.883 0.400 1 2 . 1 GLY HA2 H 3.813 0.020 1 3 . 1 GLY HA3 H 3.813 0.020 1 4 . 3 HIS CA C 56.510 0.400 1 5 . 3 HIS CB C 30.809 0.400 1 6 . 3 HIS HB2 H 3.075 0.020 2 7 . 3 HIS HB3 H 3.125 0.020 2 8 . 3 HIS CD2 C 120.6 0.400 1 9 . 3 HIS CE1 C 139.2 0.400 1 10 . 3 HIS HD2 H 7.003 0.020 1 11 . 3 HIS HE1 H 7.826 0.020 1 12 . 3 HIS C C 174.500 0.400 1 13 . 4 MET N N 121.896 0.400 1 14 . 4 MET H H 8.273 0.020 1 15 . 4 MET CA C 55.495 0.400 1 16 . 4 MET HA H 4.420 0.020 1 17 . 4 MET CB C 32.951 0.400 1 18 . 4 MET HB2 H 1.932 0.020 2 19 . 4 MET HB3 H 2.053 0.020 2 20 . 4 MET CG C 31.870 0.400 1 21 . 4 MET HG2 H 2.417 0.020 2 22 . 4 MET HG3 H 2.488 0.020 2 23 . 4 MET HE H 2.081 0.020 1 24 . 4 MET CE C 16.935 0.400 1 25 . 4 MET C C 174.600 0.400 1 26 . 5 ALA N N 125.274 0.400 1 27 . 5 ALA H H 8.345 0.020 1 28 . 5 ALA CA C 52.197 0.400 1 29 . 5 ALA HA H 4.355 0.020 1 30 . 5 ALA HB H 1.401 0.020 1 31 . 5 ALA CB C 19.541 0.400 1 32 . 5 ALA C C 176.200 0.400 1 33 . 6 GLU N N 121.197 0.400 1 34 . 6 GLU H H 8.280 0.020 1 35 . 6 GLU CA C 54.421 0.400 1 36 . 6 GLU HA H 4.535 0.020 1 37 . 6 GLU CB C 29.580 0.400 1 38 . 6 GLU HB2 H 1.890 0.020 2 39 . 6 GLU HB3 H 2.018 0.020 2 40 . 6 GLU CG C 36.016 0.400 1 41 . 6 GLU HG2 H 2.277 0.020 2 42 . 6 GLU HG3 H 2.290 0.020 2 43 . 7 PRO CD C 50.700 0.400 1 44 . 7 PRO CA C 63.157 0.400 1 45 . 7 PRO HA H 4.176 0.020 1 46 . 7 PRO CB C 32.317 0.400 1 47 . 7 PRO HB2 H 1.790 0.020 2 48 . 7 PRO HB3 H 2.042 0.020 2 49 . 7 PRO CG C 27.740 0.400 1 50 . 7 PRO HG2 H 1.924 0.020 2 51 . 7 PRO HG3 H 2.090 0.020 2 52 . 7 PRO HD2 H 3.658 0.020 2 53 . 7 PRO HD3 H 3.840 0.020 2 54 . 7 PRO C C 174.900 0.400 1 55 . 8 GLN N N 120.084 0.400 1 56 . 8 GLN H H 8.009 0.020 1 57 . 8 GLN CA C 54.186 0.400 1 58 . 8 GLN HA H 4.461 0.020 1 59 . 8 GLN CB C 31.710 0.400 1 60 . 8 GLN HB2 H 1.886 0.020 2 61 . 8 GLN HB3 H 1.971 0.020 2 62 . 8 GLN CG C 33.812 0.400 1 63 . 8 GLN HG2 H 2.303 0.020 2 64 . 8 GLN HG3 H 2.328 0.020 2 65 . 8 GLN CD C 179.800 0.400 1 66 . 8 GLN NE2 N 112.668 0.400 1 67 . 8 GLN HE21 H 7.471 0.020 2 68 . 8 GLN HE22 H 6.862 0.020 2 69 . 8 GLN C C 172.800 0.400 1 70 . 9 ARG N N 121.218 0.400 1 71 . 9 ARG H H 8.169 0.020 1 72 . 9 ARG CA C 54.983 0.400 1 73 . 9 ARG HA H 4.998 0.020 1 74 . 9 ARG CB C 31.278 0.400 1 75 . 9 ARG HB2 H 1.615 0.020 2 76 . 9 ARG HB3 H 1.693 0.020 2 77 . 9 ARG CG C 27.038 0.400 1 78 . 9 ARG HG2 H 1.426 0.020 2 79 . 9 ARG HG3 H 1.526 0.020 2 80 . 9 ARG CD C 43.147 0.400 1 81 . 9 ARG HD2 H 3.020 0.020 2 82 . 9 ARG HD3 H 3.063 0.020 2 83 . 9 ARG C C 174.400 0.400 1 84 . 10 HIS N N 125.259 0.400 1 85 . 10 HIS H H 9.321 0.020 1 86 . 10 HIS CA C 55.159 0.400 1 87 . 10 HIS HA H 4.789 0.020 1 88 . 10 HIS CB C 34.695 0.400 1 89 . 10 HIS HB2 H 2.550 0.020 2 90 . 10 HIS HB3 H 2.828 0.020 2 91 . 10 HIS CD2 C 121.2 0.400 1 92 . 10 HIS CE1 C 138.5 0.400 1 93 . 10 HIS HD2 H 6.745 0.020 1 94 . 10 HIS HE1 H 7.668 0.020 1 95 . 10 HIS C C 172.600 0.400 1 96 . 11 LYS N N 122.385 0.400 1 97 . 11 LYS H H 8.458 0.020 1 98 . 11 LYS CA C 54.832 0.400 1 99 . 11 LYS HA H 5.119 0.020 1 100 . 11 LYS CB C 33.752 0.400 1 101 . 11 LYS HB2 H 1.601 0.020 2 102 . 11 LYS HB3 H 1.657 0.020 2 103 . 11 LYS CG C 24.588 0.400 1 104 . 11 LYS HG2 H 1.279 0.020 2 105 . 11 LYS HG3 H 1.338 0.020 2 106 . 11 LYS CD C 29.035 0.400 1 107 . 11 LYS HD2 H 1.539 0.020 2 108 . 11 LYS HD3 H 1.604 0.020 2 109 . 11 LYS CE C 41.906 0.400 1 110 . 11 LYS HE2 H 2.839 0.020 2 111 . 11 LYS HE3 H 2.857 0.020 2 112 . 11 LYS C C 175.200 0.400 1 113 . 12 ILE N N 125.503 0.400 1 114 . 12 ILE H H 9.238 0.020 1 115 . 12 ILE CA C 59.707 0.400 1 116 . 12 ILE HA H 4.279 0.020 1 117 . 12 ILE CB C 40.350 0.400 1 118 . 12 ILE HB H 1.739 0.020 1 119 . 12 ILE HG2 H 0.743 0.020 1 120 . 12 ILE CG2 C 17.532 0.400 1 121 . 12 ILE CG1 C 26.970 0.400 1 122 . 12 ILE HG12 H 1.062 0.020 2 123 . 12 ILE HG13 H 1.348 0.020 2 124 . 12 ILE HD1 H 0.722 0.020 1 125 . 12 ILE CD1 C 13.501 0.400 1 126 . 12 ILE C C 172.900 0.400 1 127 . 13 LEU N N 127.889 0.400 1 128 . 13 LEU H H 8.474 0.020 1 129 . 13 LEU CA C 53.590 0.400 1 130 . 13 LEU HA H 4.950 0.020 1 131 . 13 LEU CB C 42.219 0.400 1 132 . 13 LEU HB2 H 1.497 0.020 2 133 . 13 LEU HB3 H 1.598 0.020 2 134 . 13 LEU CG C 27.368 0.400 1 135 . 13 LEU HG H 1.521 0.020 1 136 . 13 LEU HD1 H 0.817 0.020 2 137 . 13 LEU HD2 H 0.849 0.020 2 138 . 13 LEU CD1 C 24.287 0.400 1 139 . 13 LEU CD2 C 24.444 0.400 1 140 . 13 LEU C C 175.400 0.400 1 141 . 14 CYS N N 123.040 0.400 1 142 . 14 CYS H H 9.028 0.020 1 143 . 14 CYS CA C 56.607 0.400 1 144 . 14 CYS HA H 4.652 0.020 1 145 . 14 CYS CB C 30.011 0.400 1 146 . 14 CYS HB2 H 2.591 0.020 2 147 . 14 CYS HB3 H 2.636 0.020 2 148 . 14 CYS C C 171.900 0.400 1 149 . 15 VAL N N 119.221 0.400 1 150 . 15 VAL H H 8.232 0.020 1 151 . 15 VAL CA C 60.226 0.400 1 152 . 15 VAL HA H 4.758 0.020 1 153 . 15 VAL CB C 34.475 0.400 1 154 . 15 VAL HB H 1.831 0.020 1 155 . 15 VAL HG1 H 0.822 0.020 2 156 . 15 VAL HG2 H 0.791 0.020 2 157 . 15 VAL CG1 C 21.377 0.400 1 158 . 15 VAL CG2 C 20.328 0.400 1 159 . 15 VAL C C 175.000 0.400 1 160 . 16 CYS N N 129.482 0.400 1 161 . 16 CYS H H 9.473 0.020 1 162 . 16 CYS CA C 59.707 0.400 1 163 . 16 CYS HA H 4.611 0.020 1 164 . 16 CYS CB C 30.899 0.400 1 165 . 16 CYS HB2 H 2.703 0.020 2 166 . 16 CYS HB3 H 3.426 0.020 2 167 . 16 CYS C C 176.800 0.400 1 168 . 17 CYS N N 126.526 0.400 1 169 . 17 CYS H H 8.513 0.020 1 170 . 17 CYS CA C 59.187 0.400 1 171 . 17 CYS HA H 4.689 0.020 1 172 . 17 CYS CB C 27.665 0.400 1 173 . 17 CYS HB2 H 3.175 0.020 2 174 . 17 CYS HB3 H 3.268 0.020 2 175 . 17 CYS C C 173.400 0.400 1 176 . 18 LYS N N 124.570 0.400 1 177 . 18 LYS H H 9.445 0.020 1 178 . 18 LYS CA C 56.168 0.400 1 179 . 18 LYS HA H 4.714 0.020 1 180 . 18 LYS CB C 32.618 0.400 1 181 . 18 LYS HB2 H 2.066 0.020 2 182 . 18 LYS HB3 H 2.547 0.020 2 183 . 18 LYS CG C 24.684 0.400 1 184 . 18 LYS HG2 H 1.450 0.020 2 185 . 18 LYS HG3 H 1.605 0.020 2 186 . 18 LYS CD C 27.385 0.400 1 187 . 18 LYS HD2 H 0.911 0.020 2 188 . 18 LYS HD3 H 1.475 0.020 2 189 . 18 LYS CE C 42.064 0.400 1 190 . 18 LYS HE2 H 2.825 0.020 2 191 . 18 LYS HE3 H 2.887 0.020 2 192 . 18 LYS C C 176.600 0.400 1 193 . 19 CYS N N 117.766 0.400 1 194 . 19 CYS H H 8.174 0.020 1 195 . 19 CYS CA C 58.868 0.400 1 196 . 19 CYS HA H 4.988 0.020 1 197 . 19 CYS CB C 33.145 0.400 1 198 . 19 CYS HB2 H 2.635 0.020 2 199 . 19 CYS HB3 H 3.246 0.020 2 200 . 19 CYS C C 175.400 0.400 1 201 . 20 ASP N N 120.042 0.400 1 202 . 20 ASP H H 8.065 0.020 1 203 . 20 ASP CA C 56.662 0.400 1 204 . 20 ASP HA H 4.559 0.020 1 205 . 20 ASP CB C 40.700 0.400 1 206 . 20 ASP HB2 H 2.854 0.020 2 207 . 20 ASP HB3 H 2.963 0.020 2 208 . 20 ASP C C 174.300 0.400 1 209 . 21 GLY N N 112.757 0.400 1 210 . 21 GLY H H 9.386 0.020 1 211 . 21 GLY CA C 44.302 0.400 1 212 . 21 GLY HA2 H 4.005 0.020 2 213 . 21 GLY HA3 H 3.854 0.020 2 214 . 21 GLY C C 172.000 0.400 1 215 . 22 ARG N N 121.309 0.400 1 216 . 22 ARG H H 8.390 0.020 1 217 . 22 ARG CA C 56.613 0.400 1 218 . 22 ARG HA H 4.525 0.020 1 219 . 22 ARG CB C 31.222 0.400 1 220 . 22 ARG HB2 H 1.714 0.020 2 221 . 22 ARG HB3 H 1.819 0.020 2 222 . 22 ARG CG C 27.678 0.400 1 223 . 22 ARG HG2 H 1.552 0.020 2 224 . 22 ARG HG3 H 1.678 0.020 2 225 . 22 ARG CD C 43.413 0.400 1 226 . 22 ARG HD2 H 3.165 0.020 2 227 . 22 ARG HD3 H 3.202 0.020 2 228 . 22 ARG C C 175.400 0.400 1 229 . 23 ILE N N 126.519 0.400 1 230 . 23 ILE H H 8.754 0.020 1 231 . 23 ILE CA C 60.664 0.400 1 232 . 23 ILE HA H 4.144 0.020 1 233 . 23 ILE CB C 41.145 0.400 1 234 . 23 ILE HB H 1.614 0.020 1 235 . 23 ILE HG2 H 0.638 0.020 1 236 . 23 ILE CG2 C 16.993 0.400 1 237 . 23 ILE CG1 C 27.140 0.400 1 238 . 23 ILE HG12 H 1.430 0.020 2 239 . 23 ILE HG13 H 1.535 0.020 2 240 . 23 ILE HD1 H 0.708 0.020 1 241 . 23 ILE CD1 C 14.163 0.400 1 242 . 23 ILE C C 172.800 0.400 1 243 . 24 GLU N N 126.359 0.400 1 244 . 24 GLU H H 8.558 0.020 1 245 . 24 GLU CA C 54.904 0.400 1 246 . 24 GLU HA H 4.929 0.020 1 247 . 24 GLU CB C 31.475 0.400 1 248 . 24 GLU HB2 H 1.808 0.020 2 249 . 24 GLU HB3 H 1.840 0.020 2 250 . 24 GLU CG C 36.911 0.400 1 251 . 24 GLU HG2 H 1.911 0.020 2 252 . 24 GLU HG3 H 2.059 0.020 2 253 . 24 GLU C C 174.500 0.400 1 254 . 25 LEU N N 127.902 0.400 1 255 . 25 LEU H H 9.059 0.020 1 256 . 25 LEU CA C 53.523 0.400 1 257 . 25 LEU HA H 4.678 0.020 1 258 . 25 LEU CB C 44.723 0.400 1 259 . 25 LEU HB2 H 1.406 0.020 2 260 . 25 LEU HB3 H 1.565 0.020 2 261 . 25 LEU CG C 26.680 0.400 1 262 . 25 LEU HG H 1.313 0.020 1 263 . 25 LEU HD1 H 0.386 0.020 2 264 . 25 LEU HD2 H 0.615 0.020 2 265 . 25 LEU CD1 C 25.193 0.400 1 266 . 25 LEU CD2 C 23.190 0.400 1 267 . 25 LEU C C 174.300 0.400 1 268 . 26 THR N N 120.390 0.400 1 269 . 26 THR H H 8.820 0.020 1 270 . 26 THR CA C 62.695 0.400 1 271 . 26 THR HA H 5.004 0.020 1 272 . 26 THR CB C 69.248 0.400 1 273 . 26 THR HB H 3.907 0.020 1 274 . 26 THR HG2 H 0.994 0.020 1 275 . 26 THR CG2 C 21.607 0.400 1 276 . 26 THR C C 171.900 0.400 1 277 . 27 VAL N N 118.400 0.400 1 278 . 27 VAL H H 8.740 0.020 1 279 . 27 VAL CA C 57.794 0.400 1 280 . 27 VAL HA H 5.123 0.020 1 281 . 27 VAL CB C 35.544 0.400 1 282 . 27 VAL HB H 1.932 0.020 1 283 . 27 VAL HG1 H 0.305 0.020 2 284 . 27 VAL HG2 H 0.574 0.020 2 285 . 27 VAL CG1 C 21.268 0.400 1 286 . 27 VAL CG2 C 18.971 0.400 1 287 . 27 VAL C C 174.000 0.400 1 288 . 28 GLU N N 120.613 0.400 1 289 . 28 GLU H H 8.884 0.020 1 290 . 28 GLU CA C 55.336 0.400 1 291 . 28 GLU HA H 5.234 0.020 1 292 . 28 GLU CB C 31.840 0.400 1 293 . 28 GLU HB2 H 1.691 0.020 2 294 . 28 GLU HB3 H 1.717 0.020 2 295 . 28 GLU CG C 37.324 0.400 1 296 . 28 GLU HG2 H 1.863 0.020 2 297 . 28 GLU HG3 H 2.035 0.020 2 298 . 28 GLU C C 174.500 0.400 1 299 . 29 SER N N 113.641 0.400 1 300 . 29 SER H H 8.563 0.020 1 301 . 29 SER CA C 58.583 0.400 1 302 . 29 SER HA H 4.899 0.020 1 303 . 29 SER CB C 67.032 0.400 1 304 . 29 SER HB2 H 3.612 0.020 2 305 . 29 SER HB3 H 3.893 0.020 2 306 . 29 SER C C 174.000 0.400 1 307 . 30 SER N N 119.450 0.400 1 308 . 30 SER H H 9.979 0.020 1 309 . 30 SER CA C 57.610 0.400 1 310 . 30 SER HA H 4.676 0.020 1 311 . 30 SER CB C 64.945 0.400 1 312 . 30 SER HB2 H 4.075 0.020 2 313 . 30 SER HB3 H 4.438 0.020 2 314 . 31 ALA CA C 55.470 0.400 1 315 . 31 ALA HA H 3.922 0.020 1 316 . 31 ALA HB H 1.460 0.020 1 317 . 31 ALA CB C 18.038 0.400 1 318 . 31 ALA C C 179.500 0.400 1 319 . 32 GLU N N 118.734 0.400 1 320 . 32 GLU H H 8.867 0.020 1 321 . 32 GLU CA C 59.943 0.400 1 322 . 32 GLU HA H 3.918 0.020 1 323 . 32 GLU CB C 29.067 0.400 1 324 . 32 GLU HB2 H 1.890 0.020 2 325 . 32 GLU HB3 H 1.996 0.020 2 326 . 32 GLU CG C 36.586 0.400 1 327 . 32 GLU HG2 H 2.227 0.020 2 328 . 32 GLU HG3 H 2.368 0.020 2 329 . 32 GLU C C 177.500 0.400 1 330 . 33 ASP N N 120.077 0.400 1 331 . 33 ASP H H 7.623 0.020 1 332 . 33 ASP CA C 56.956 0.400 1 333 . 33 ASP HA H 4.396 0.020 1 334 . 33 ASP CB C 39.684 0.400 1 335 . 33 ASP HB2 H 2.387 0.020 2 336 . 33 ASP HB3 H 2.575 0.020 2 337 . 33 ASP C C 176.600 0.400 1 338 . 34 LEU N N 121.509 0.400 1 339 . 34 LEU H H 7.582 0.020 1 340 . 34 LEU CA C 57.484 0.400 1 341 . 34 LEU HA H 3.804 0.020 1 342 . 34 LEU CB C 40.752 0.400 1 343 . 34 LEU HB2 H 1.054 0.020 2 344 . 34 LEU HB3 H 1.577 0.020 2 345 . 34 LEU CG C 26.238 0.400 1 346 . 34 LEU HG H 1.185 0.020 1 347 . 34 LEU HD1 H 0.136 0.020 2 348 . 34 LEU HD2 H 0.515 0.020 2 349 . 34 LEU CD1 C 23.975 0.400 1 350 . 34 LEU CD2 C 22.527 0.400 1 351 . 34 LEU C C 177.400 0.400 1 352 . 35 ARG N N 118.852 0.400 1 353 . 35 ARG H H 7.649 0.020 1 354 . 35 ARG CA C 59.427 0.400 1 355 . 35 ARG HA H 4.051 0.020 1 356 . 35 ARG CB C 29.456 0.400 1 357 . 35 ARG HB2 H 1.894 0.020 2 358 . 35 ARG HB3 H 1.931 0.020 2 359 . 35 ARG CG C 27.631 0.400 1 360 . 35 ARG HG2 H 1.551 0.020 2 361 . 35 ARG HG3 H 1.744 0.020 2 362 . 35 ARG CD C 43.487 0.400 1 363 . 35 ARG HD2 H 3.165 0.020 2 364 . 35 ARG HD3 H 3.201 0.020 2 365 . 35 ARG C C 178.400 0.400 1 366 . 36 THR N N 117.321 0.400 1 367 . 36 THR H H 7.915 0.020 1 368 . 36 THR CA C 66.522 0.400 1 369 . 36 THR HA H 3.809 0.020 1 370 . 36 THR CB C 67.483 0.400 1 371 . 36 THR HB H 4.234 0.020 1 372 . 36 THR HG2 H 1.120 0.020 1 373 . 36 THR CG2 C 22.819 0.400 1 374 . 36 THR C C 175.000 0.400 1 375 . 37 LEU N N 122.991 0.400 1 376 . 37 LEU H H 7.963 0.020 1 377 . 37 LEU CA C 58.602 0.400 1 378 . 37 LEU HA H 3.687 0.020 1 379 . 37 LEU CB C 41.374 0.400 1 380 . 37 LEU HB2 H 1.273 0.020 2 381 . 37 LEU HB3 H 2.080 0.020 2 382 . 37 LEU CG C 26.574 0.400 1 383 . 37 LEU HG H 1.357 0.020 1 384 . 37 LEU HD1 H 0.676 0.020 2 385 . 37 LEU HD2 H 0.793 0.020 2 386 . 37 LEU CD1 C 23.538 0.400 1 387 . 37 LEU CD2 C 26.180 0.400 1 388 . 37 LEU C C 176.600 0.400 1 389 . 38 GLN N N 115.312 0.400 1 390 . 38 GLN H H 8.494 0.020 1 391 . 38 GLN CA C 59.134 0.400 1 392 . 38 GLN HA H 3.958 0.020 1 393 . 38 GLN CB C 28.181 0.400 1 394 . 38 GLN HB2 H 1.996 0.020 2 395 . 38 GLN HB3 H 2.308 0.020 2 396 . 38 GLN CG C 34.176 0.400 1 397 . 38 GLN HG2 H 2.498 0.020 2 398 . 38 GLN HG3 H 2.514 0.020 2 399 . 38 GLN CD C 178.700 0.400 1 400 . 38 GLN NE2 N 109.979 0.400 1 401 . 38 GLN HE21 H 7.068 0.020 2 402 . 38 GLN HE22 H 6.764 0.020 2 403 . 38 GLN C C 179.000 0.400 1 404 . 39 GLN N N 118.434 0.400 1 405 . 39 GLN H H 8.109 0.020 1 406 . 39 GLN CA C 58.515 0.400 1 407 . 39 GLN HA H 4.014 0.020 1 408 . 39 GLN CB C 27.931 0.400 1 409 . 39 GLN HB2 H 2.181 0.020 2 410 . 39 GLN HB3 H 2.320 0.020 2 411 . 39 GLN CG C 34.120 0.400 1 412 . 39 GLN HG2 H 2.442 0.020 2 413 . 39 GLN HG3 H 2.458 0.020 2 414 . 39 GLN CD C 179.200 0.400 1 415 . 39 GLN NE2 N 111.808 0.400 1 416 . 39 GLN HE21 H 7.402 0.020 2 417 . 39 GLN HE22 H 6.831 0.020 2 418 . 39 GLN C C 178.700 0.400 1 419 . 40 LEU N N 121.455 0.400 1 420 . 40 LEU H H 8.043 0.020 1 421 . 40 LEU CA C 58.063 0.400 1 422 . 40 LEU HA H 4.096 0.020 1 423 . 40 LEU CB C 41.457 0.400 1 424 . 40 LEU HB2 H 1.183 0.020 2 425 . 40 LEU HB3 H 2.123 0.020 2 426 . 40 LEU CG C 25.970 0.400 1 427 . 40 LEU HG H 2.004 0.020 1 428 . 40 LEU HD1 H 0.835 0.020 2 429 . 40 LEU HD2 H 0.729 0.020 2 430 . 40 LEU CD1 C 22.409 0.400 1 431 . 40 LEU CD2 C 25.706 0.400 1 432 . 40 LEU C C 179.800 0.400 1 433 . 41 PHE N N 118.212 0.400 1 434 . 41 PHE H H 7.587 0.020 1 435 . 41 PHE CA C 59.086 0.400 1 436 . 41 PHE HA H 5.136 0.020 1 437 . 41 PHE CB C 38.506 0.400 1 438 . 41 PHE HB2 H 3.179 0.020 2 439 . 41 PHE HB3 H 3.412 0.020 2 440 . 41 PHE CZ C 129.4 0.400 1 441 . 41 PHE HZ H 6.998 0.020 1 442 . 41 PHE CE2 C 131.1 0.400 1 443 . 41 PHE HE2 H 7.162 0.020 1 444 . 41 PHE CD2 C 132.5 0.400 1 445 . 41 PHE HD2 H 7.489 0.020 1 446 . 41 PHE C C 177.000 0.400 1 447 . 42 LEU N N 117.286 0.400 1 448 . 42 LEU H H 7.369 0.020 1 449 . 42 LEU CA C 55.202 0.400 1 450 . 42 LEU HA H 4.443 0.020 1 451 . 42 LEU CB C 41.759 0.400 1 452 . 42 LEU HB2 H 1.763 0.020 2 453 . 42 LEU HB3 H 1.877 0.020 2 454 . 42 LEU CG C 26.945 0.400 1 455 . 42 LEU HG H 1.822 0.020 1 456 . 42 LEU HD1 H 0.922 0.020 2 457 . 42 LEU HD2 H 0.946 0.020 2 458 . 42 LEU CD1 C 22.536 0.400 1 459 . 42 LEU CD2 C 25.413 0.400 1 460 . 42 LEU C C 175.700 0.400 1 461 . 43 SER N N 116.284 0.400 1 462 . 43 SER H H 7.518 0.020 1 463 . 43 SER CA C 56.903 0.400 1 464 . 43 SER HA H 4.760 0.020 1 465 . 43 SER CB C 61.307 0.400 1 466 . 43 SER HB2 H 3.860 0.020 2 467 . 43 SER HB3 H 4.238 0.020 2 468 . 43 SER C C 173.800 0.400 1 469 . 44 THR N N 108.861 0.400 1 470 . 44 THR H H 7.754 0.020 1 471 . 44 THR CA C 61.929 0.400 1 472 . 44 THR HA H 4.752 0.020 1 473 . 44 THR CB C 71.385 0.400 1 474 . 44 THR HB H 4.467 0.020 1 475 . 44 THR HG2 H 1.220 0.020 1 476 . 44 THR CG2 C 21.679 0.400 1 477 . 44 THR C C 173.300 0.400 1 478 . 45 LEU N N 123.520 0.400 1 479 . 45 LEU H H 7.669 0.020 1 480 . 45 LEU CA C 56.595 0.400 1 481 . 45 LEU HA H 4.627 0.020 1 482 . 45 LEU CB C 43.508 0.400 1 483 . 45 LEU HB2 H 1.001 0.020 2 484 . 45 LEU HB3 H 1.429 0.020 2 485 . 45 LEU CG C 27.589 0.400 1 486 . 45 LEU HG H 1.179 0.020 1 487 . 45 LEU HD1 H 0.652 0.020 2 488 . 45 LEU HD2 H 0.444 0.020 2 489 . 45 LEU CD1 C 24.199 0.400 1 490 . 45 LEU CD2 C 27.044 0.400 1 491 . 45 LEU C C 174.700 0.400 1 492 . 46 SER N N 121.418 0.400 1 493 . 46 SER H H 8.913 0.020 1 494 . 46 SER CA C 57.509 0.400 1 495 . 46 SER HA H 4.968 0.020 1 496 . 46 SER CB C 66.664 0.400 1 497 . 46 SER HB2 H 3.867 0.020 2 498 . 46 SER HB3 H 4.071 0.020 2 499 . 46 SER C C 171.400 0.400 1 500 . 47 PHE N N 123.011 0.400 1 501 . 47 PHE H H 9.643 0.020 1 502 . 47 PHE CA C 58.071 0.400 1 503 . 47 PHE HA H 4.922 0.020 1 504 . 47 PHE CB C 41.890 0.400 1 505 . 47 PHE HB2 H 2.923 0.020 2 506 . 47 PHE HB3 H 2.974 0.020 2 507 . 47 PHE CZ C 128.5 0.400 1 508 . 47 PHE HZ H 7.021 0.020 1 509 . 47 PHE CE2 C 131.7 0.400 1 510 . 47 PHE HE2 H 7.112 0.020 1 511 . 47 PHE CD2 C 132.4 0.400 1 512 . 47 PHE HD2 H 7.293 0.020 1 513 . 47 PHE C C 172.900 0.400 1 514 . 48 VAL N N 121.919 0.400 1 515 . 48 VAL H H 8.010 0.020 1 516 . 48 VAL CA C 60.266 0.400 1 517 . 48 VAL HA H 4.906 0.020 1 518 . 48 VAL CB C 33.426 0.400 1 519 . 48 VAL HB H 1.542 0.020 1 520 . 48 VAL HG1 H 0.660 0.020 2 521 . 48 VAL HG2 H 0.881 0.020 2 522 . 48 VAL CG1 C 21.394 0.400 1 523 . 48 VAL CG2 C 21.784 0.400 1 524 . 48 VAL C C 174.700 0.400 1 525 . 49 CYS N N 131.911 0.400 1 526 . 49 CYS H H 10.027 0.020 1 527 . 49 CYS CA C 58.121 0.400 1 528 . 49 CYS HA H 4.601 0.020 1 529 . 49 CYS CB C 28.521 0.400 1 530 . 49 CYS HB2 H 2.806 0.020 2 531 . 49 CYS HB3 H 3.640 0.020 2 532 . 50 PRO CD C 50.176 0.400 1 533 . 50 PRO CA C 65.590 0.400 1 534 . 50 PRO HA H 4.236 0.020 1 535 . 50 PRO CB C 31.883 0.400 1 536 . 50 PRO HB2 H 1.644 0.020 2 537 . 50 PRO HB3 H 2.296 0.020 2 538 . 50 PRO CG C 28.051 0.400 1 539 . 50 PRO HG2 H 2.009 0.020 2 540 . 50 PRO HG3 H 2.040 0.020 2 541 . 50 PRO HD2 H 3.831 0.020 1 542 . 50 PRO HD3 H 3.831 0.020 1 543 . 50 PRO C C 177.900 0.400 1 544 . 51 TRP N N 119.137 0.400 1 545 . 51 TRP H H 7.960 0.020 1 546 . 51 TRP CA C 61.243 0.400 1 547 . 51 TRP HA H 4.335 0.020 1 548 . 51 TRP CB C 29.301 0.400 1 549 . 51 TRP HB2 H 3.402 0.020 2 550 . 51 TRP HB3 H 3.444 0.020 2 551 . 51 TRP CD1 C 128.2 0.400 1 552 . 51 TRP CE3 C 122.7 0.400 1 553 . 51 TRP NE1 N 129.516 0.400 1 554 . 51 TRP HD1 H 7.421 0.020 1 555 . 51 TRP HE3 H 7.937 0.020 1 556 . 51 TRP CZ3 C 122.5 0.400 1 557 . 51 TRP CZ2 C 115.3 0.400 1 558 . 51 TRP HE1 H 10.130 0.020 1 559 . 51 TRP HZ3 H 7.140 0.020 1 560 . 51 TRP CH2 C 125.4 0.400 1 561 . 51 TRP HZ2 H 7.452 0.020 1 562 . 51 TRP HH2 H 7.209 0.020 1 563 . 51 TRP C C 178.100 0.400 1 564 . 52 CYS N N 124.654 0.400 1 565 . 52 CYS H H 8.770 0.020 1 566 . 52 CYS CA C 63.890 0.400 1 567 . 52 CYS HA H 3.821 0.020 1 568 . 52 CYS CB C 29.479 0.400 1 569 . 52 CYS HB2 H 2.687 0.020 2 570 . 52 CYS HB3 H 2.988 0.020 2 571 . 52 CYS C C 176.800 0.400 1 572 . 53 ALA N N 120.453 0.400 1 573 . 53 ALA H H 8.532 0.020 1 574 . 53 ALA CA C 53.943 0.400 1 575 . 53 ALA HA H 3.904 0.020 1 576 . 53 ALA HB H 1.328 0.020 1 577 . 53 ALA CB C 18.561 0.400 1 578 . 53 ALA C C 177.500 0.400 1 579 . 54 THR N N 109.349 0.400 1 580 . 54 THR H H 7.310 0.020 1 581 . 54 THR CA C 62.706 0.400 1 582 . 54 THR HA H 4.201 0.020 1 583 . 54 THR CB C 69.821 0.400 1 584 . 54 THR HB H 4.138 0.020 1 585 . 54 THR HG2 H 1.154 0.020 1 586 . 54 THR CG2 C 21.412 0.400 1 587 . 54 THR C C 173.400 0.400 1 588 . 55 ASN N N 120.258 0.400 1 589 . 55 ASN H H 7.774 0.020 1 590 . 55 ASN CA C 53.750 0.400 1 591 . 55 ASN HA H 4.601 0.020 1 592 . 55 ASN CB C 39.434 0.400 1 593 . 55 ASN HB2 H 2.123 0.020 2 594 . 55 ASN HB3 H 2.484 0.020 2 595 . 55 ASN CG C 176.000 0.400 1 596 . 55 ASN ND2 N 113.815 0.400 1 597 . 55 ASN HD21 H 6.955 0.020 2 598 . 55 ASN HD22 H 6.520 0.020 2 599 . 55 ASN C C 173.000 0.400 1 600 . 56 GLN N N 125.448 0.400 1 601 . 56 GLN H H 7.984 0.020 1 602 . 56 GLN CA C 57.232 0.400 1 603 . 56 GLN HA H 4.146 0.020 1 604 . 56 GLN CB C 30.493 0.400 1 605 . 56 GLN HB2 H 1.856 0.020 2 606 . 56 GLN HB3 H 2.091 0.020 2 607 . 56 GLN CG C 34.375 0.400 1 608 . 56 GLN HG2 H 2.248 0.020 2 609 . 56 GLN HG3 H 2.265 0.020 2 610 . 56 GLN CD C 180.200 0.400 1 611 . 56 GLN NE2 N 112.595 0.400 1 612 . 56 GLN HE21 H 7.542 0.020 2 613 . 56 GLN HE22 H 6.778 0.020 2 stop_ save_