data_5665 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; ClpX Zinc Binding Domain ; _BMRB_accession_number 5665 _BMRB_flat_file_name bmr5665.str _Entry_type original _Submission_date 2003-01-21 _Accession_date 2003-01-21 _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 Donaldson Logan WF . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 264 "13C chemical shifts" 203 "15N chemical shifts" 47 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-03-15 original author . stop_ _Original_release_date 2004-03-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution structure of the dimeric zinc binding domain of the chaperone ClpX. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14525985 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Donaldson Logan W . 2 Wojtyra Urszula . . 3 Houry Walid A . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 278 _Journal_issue 49 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 48991 _Page_last 48996 _Year 2003 _Details . loop_ _Keyword 'ClpX chaperonin' 'zinc binding domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_ClpX_Zinc_Finger _Saveframe_category molecular_system _Mol_system_name 'Clpx Zinc Finger dimer' _Abbreviation_common 'Clpx ZBD' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ClpX Zinc Finger, monomer 1' $CLPX 'ClpX Zinc Finger, monomer 2' $CLPX stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state homodimer _System_paramagnetic no _System_thiol_state 'other bound, and free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'ClpX Zinc Finger, monomer 1' 1 'ClpX Zinc Finger, monomer 2' stop_ loop_ _Biological_function 'molecular chaperone' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CLPX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ClpX Zinc Finger' _Abbreviation_common 'Clpx ZBD' _Molecular_mass . _Mol_thiol_state 'other bound, and free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; TDKRKDGSGKLLYCSFCGKS QHEVRKLIAGPSVYICDECV DLCNDIIREEIKEVAPHR ; loop_ _Residue_seq_code _Residue_label 1 THR 2 ASP 3 LYS 4 ARG 5 LYS 6 ASP 7 GLY 8 SER 9 GLY 10 LYS 11 LEU 12 LEU 13 TYR 14 CYS 15 SER 16 PHE 17 CYS 18 GLY 19 LYS 20 SER 21 GLN 22 HIS 23 GLU 24 VAL 25 ARG 26 LYS 27 LEU 28 ILE 29 ALA 30 GLY 31 PRO 32 SER 33 VAL 34 TYR 35 ILE 36 CYS 37 ASP 38 GLU 39 CYS 40 VAL 41 ASP 42 LEU 43 CYS 44 ASN 45 ASP 46 ILE 47 ILE 48 ARG 49 GLU 50 GLU 51 ILE 52 LYS 53 GLU 54 VAL 55 ALA 56 PRO 57 HIS 58 ARG 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 PDB 1OVX "Nmr Structure Of The E. Coli Clpx Chaperone Zinc Binding Domain Dimer" 100.00 67 100.00 100.00 2.90e-33 PDB 2DS5 "Structure Of The Zbd In The Orthorhomibic Crystal From" 87.93 51 100.00 100.00 1.15e-27 PDB 2DS6 "Structure Of The Zbd In The Tetragonal Crystal Form" 87.93 51 100.00 100.00 1.15e-27 PDB 2DS7 "Structure Of The Zbd In The Hexagonal Crystal Form" 87.93 51 98.04 98.04 1.75e-26 PDB 2DS8 "Structure Of The Zbd-Xb Complex" 87.93 51 100.00 100.00 1.15e-27 DBJ BAA94669 "ATPase subunit [Salmonella enterica subsp. enterica serovar Typhimurium]" 100.00 423 100.00 100.00 1.82e-32 DBJ BAB33915 "ATP-dependent specificity component of clpP serine protease ClpX [Escherichia coli O157:H7 str. Sakai]" 100.00 424 100.00 100.00 1.96e-32 DBJ BAE73947 "ATP-dependent Clp protease ATP-binding subunit [Sodalis glossinidius str. 'morsitans']" 100.00 424 100.00 100.00 1.87e-32 DBJ BAE76218 "ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease [Escherichia coli str. K-12 substr. W3110]" 100.00 424 100.00 100.00 1.96e-32 DBJ BAG75988 "ATP-dependent Clp protease ATP-binding subunit [Escherichia coli SE11]" 100.00 424 100.00 100.00 1.96e-32 EMBL CAA80816 "ATP-binding protein [Escherichia coli]" 100.00 424 100.00 100.00 3.17e-32 EMBL CAD08908 "ATP-dependent clp protease ATP-binding subunit ClpX [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 423 100.00 100.00 1.51e-32 EMBL CAG74059 "ATP-dependent Clp protease ATP-binding subunit [Pectobacterium atrosepticum SCRI1043]" 100.00 424 100.00 100.00 2.55e-32 EMBL CAH20200 "specificity component of clpA-clpP ATP-dependent serine protease, chaperone [Yersinia pseudotuberculosis IP 32953]" 100.00 423 98.28 100.00 5.30e-32 EMBL CAL13168 "ATP-dependent Clp protease ATP-binding subunit ClpX [Yersinia enterocolitica subsp. enterocolitica 8081]" 100.00 423 100.00 100.00 1.78e-32 GB AAA16116 "ATP-dependent protease ATPase subunit [Escherichia coli]" 100.00 424 100.00 100.00 1.96e-32 GB AAB40194 "ATP-dependent Clp proteinase [Escherichia coli]" 100.00 424 100.00 100.00 1.96e-32 GB AAC45783 "ClpX [Yersinia enterocolitica]" 100.00 423 100.00 100.00 1.78e-32 GB AAC73541 "ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease [Escherichia coli str. K-12 substr. MG1655]" 100.00 424 100.00 100.00 1.96e-32 GB AAG54788 "ATP-dependent specificity component of clpP serine protease, chaperone [Escherichia coli O157:H7 str. EDL933]" 100.00 424 100.00 100.00 1.96e-32 PIR AD0558 "ATP-dependent clp protease ATP-binding chain ClpX [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 423 100.00 100.00 1.51e-32 REF NP_286180 "ATP-dependent protease ATP-binding subunit ClpX [Escherichia coli O157:H7 str. EDL933]" 100.00 424 100.00 100.00 1.96e-32 REF NP_308519 "ATP-dependent protease ATP-binding protein ClpX [Escherichia coli O157:H7 str. Sakai]" 100.00 424 100.00 100.00 1.96e-32 REF NP_414972 "ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease [Escherichia coli str. K-12 substr. MG1655]" 100.00 424 100.00 100.00 1.96e-32 REF NP_455046 "ATP-dependent CLP protease ATP-binding subunit ClpX [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 423 100.00 100.00 1.51e-32 REF NP_459445 "ATP-dependent protease ATP-binding subunit ClpX [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 423 100.00 100.00 1.71e-32 SP A1A8A7 "RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX [Escherichia coli APEC O1]" 100.00 424 100.00 100.00 1.96e-32 SP A1JNN1 "RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX [Yersinia enterocolitica subsp. enterocolitica 8081]" 100.00 423 100.00 100.00 1.78e-32 SP A4TPE2 "RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX [Yersinia pestis Pestoides F]" 100.00 423 98.28 100.00 5.41e-32 SP A4W7A9 "RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX [Enterobacter sp. 638]" 100.00 424 100.00 100.00 2.22e-32 SP A6T5I1 "RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]" 100.00 424 100.00 100.00 1.89e-32 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $CLPX 'E. coli' 562 Eubacteria . Escherichia coli 'ClpX Zinc Binding Domain' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $CLPX 'recombinant technology' 'E. coli' Escherichia coli 'BL21 Gold' plasmid pET28b 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 $CLPX 1.5 mM '[U-15N; U-13C]' 'sodium phosphate' 20 mM . 'sodium azide' 0.02 % . 'sodium chloride' 150 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_15N_HSQC-NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC-NOESY' _Sample_label . save_ save_13C_HSQC-NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC-NOESY' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_CBCACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_C(CC)-TOCSY-(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CC)-TOCSY-(CO)NH _Sample_label . save_ save_H(CC)-TOCSY-(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC)-TOCSY-(CO)NH _Sample_label . save_ save_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_13C_HSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _Sample_label . save_ save_15N_HSQC_10 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _Sample_label . save_ save_13C-filtered_NOESY_11 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-filtered NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC-NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name C(CC)-TOCSY-(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(CC)-TOCSY-(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_11 _Saveframe_category NMR_applied_experiment _Experiment_name '13C-filtered NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_standard_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.5 0.05 n/a temperature 303 0.5 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_PBX_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $standard_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'ClpX Zinc Finger, monomer 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 . 11 LEU N N 124.564 . 1 2 . 11 LEU CA C 54.598 . 1 3 . 11 LEU HA H 4.239 . 1 4 . 11 LEU CB C 42.900 . 1 5 . 11 LEU HB3 H 1.478 . 2 6 . 11 LEU HB2 H 1.461 . 2 7 . 11 LEU HG H 1.259 . 1 8 . 11 LEU CD1 C 26.860 . 1 9 . 11 LEU HD1 H 0.824 . 2 10 . 11 LEU CD2 C 24.429 . 1 11 . 11 LEU HD2 H 0.797 . 2 12 . 11 LEU C C 177.095 . 1 13 . 12 LEU N N 122.606 . 1 14 . 12 LEU H H 7.845 . 1 15 . 12 LEU CA C 53.114 . 1 16 . 12 LEU HA H 4.254 . 1 17 . 12 LEU CB C 43.576 . 1 18 . 12 LEU HB3 H 1.230 . 2 19 . 12 LEU HB2 H 1.431 . 2 20 . 12 LEU CG C 26.340 . 1 21 . 12 LEU HG H 1.053 . 1 22 . 12 LEU CD1 C 24.663 . 1 23 . 12 LEU HD1 H 0.626 . 2 24 . 12 LEU CD2 C 21.950 . 1 25 . 12 LEU HD2 H 0.560 . 2 26 . 12 LEU C C 174.901 . 1 27 . 13 TYR N N 116.340 . 1 28 . 13 TYR H H 7.576 . 1 29 . 13 TYR CA C 55.500 . 1 30 . 13 TYR HA H 4.873 . 1 31 . 13 TYR CB C 41.727 . 1 32 . 13 TYR HB3 H 2.411 . 2 33 . 13 TYR HB2 H 2.512 . 2 34 . 13 TYR CD1 C 131.450 . 1 35 . 13 TYR HD1 H 6.970 . 1 36 . 13 TYR CD2 C 131.450 . 1 37 . 13 TYR HD2 H 6.970 . 1 38 . 13 TYR CE1 C 116.870 . 1 39 . 13 TYR HE1 H 6.910 . 1 40 . 13 TYR CE2 C 116.870 . 1 41 . 13 TYR HE2 H 6.910 . 1 42 . 13 TYR C C 177.403 . 1 43 . 14 CYS N N 122.868 . 1 44 . 14 CYS H H 9.166 . 1 45 . 14 CYS CA C 61.103 . 1 46 . 14 CYS HA H 4.025 . 1 47 . 14 CYS CB C 31.357 . 1 48 . 14 CYS HB3 H 2.695 . 2 49 . 14 CYS HB2 H 3.483 . 2 50 . 14 CYS C C 180.732 . 1 51 . 15 SER N N 106.795 . 1 52 . 15 SER H H 9.607 . 1 53 . 15 SER CA C 61.547 . 1 54 . 15 SER HA H 4.427 . 1 55 . 15 SER CB C 62.986 . 1 56 . 15 SER HB3 H 4.067 . 1 57 . 15 SER HB2 H 4.067 . 1 58 . 15 SER C C 175.273 . 1 59 . 16 PHE N N 122.393 . 1 60 . 16 PHE H H 9.920 . 1 61 . 16 PHE CA C 61.121 . 1 62 . 16 PHE HA H 4.211 . 1 63 . 16 PHE CB C 41.318 . 1 64 . 16 PHE HB3 H 3.107 . 2 65 . 16 PHE HB2 H 3.925 . 2 66 . 16 PHE CD1 C 129.770 . 1 67 . 16 PHE CD2 C 129.770 . 1 68 . 16 PHE HD1 H 7.400 . 1 69 . 16 PHE HD2 H 7.400 . 1 70 . 16 PHE CE1 C 128.790 . 1 71 . 16 PHE CE2 C 128.790 . 1 72 . 16 PHE HE1 H 7.080 . 1 73 . 16 PHE HE2 H 7.080 . 1 74 . 16 PHE CZ C 126.960 . 1 75 . 16 PHE HZ H 7.000 . 1 76 . 16 PHE C C 179.064 . 1 77 . 17 CYS N N 118.657 . 1 78 . 17 CYS H H 8.689 . 1 79 . 17 CYS CA C 58.878 . 1 80 . 17 CYS HA H 4.997 . 1 81 . 17 CYS CB C 32.920 . 1 82 . 17 CYS HB3 H 2.665 . 2 83 . 17 CYS HB2 H 3.194 . 2 84 . 17 CYS C C 177.197 . 1 85 . 18 GLY N N 112.516 . 1 86 . 18 GLY H H 7.648 . 1 87 . 18 GLY CA C 46.407 . 1 88 . 18 GLY HA3 H 3.965 . 2 89 . 18 GLY HA2 H 4.229 . 2 90 . 18 GLY C C 176.783 . 1 91 . 19 LYS N N 123.321 . 1 92 . 19 LYS H H 8.758 . 1 93 . 19 LYS CA C 58.806 . 1 94 . 19 LYS HA H 4.337 . 1 95 . 19 LYS CB C 34.163 . 1 96 . 19 LYS HB3 H 1.754 . 2 97 . 19 LYS HB2 H 1.910 . 2 98 . 19 LYS CG C 27.708 . 1 99 . 19 LYS HG3 H 1.750 . 2 100 . 19 LYS HG2 H 1.597 . 2 101 . 19 LYS CD C 30.282 . 1 102 . 19 LYS HD3 H 1.393 . 1 103 . 19 LYS HD2 H 1.393 . 1 104 . 19 LYS CE C 42.152 . 1 105 . 19 LYS HE3 H 3.029 . 1 106 . 19 LYS HE2 H 3.029 . 1 107 . 19 LYS C C 178.696 . 1 108 . 20 SER N N 116.658 . 1 109 . 20 SER H H 9.117 . 1 110 . 20 SER CA C 57.273 . 1 111 . 20 SER HA H 4.504 . 1 112 . 20 SER CB C 66.155 . 1 113 . 20 SER HB3 H 3.683 . 2 114 . 20 SER HB2 H 3.909 . 2 115 . 20 SER C C 178.686 . 1 116 . 21 GLN N N 117.211 . 1 117 . 21 GLN H H 8.129 . 1 118 . 21 GLN CA C 57.833 . 1 119 . 21 GLN HA H 3.757 . 1 120 . 21 GLN CB C 29.021 . 1 121 . 21 GLN HB3 H 1.743 . 2 122 . 21 GLN HB2 H 1.873 . 2 123 . 21 GLN CG C 33.200 . 1 124 . 21 GLN HG3 H 1.743 . 2 125 . 21 GLN HG2 H 1.850 . 2 126 . 21 GLN NE2 N 110.740 . 1 127 . 21 GLN HE21 H 7.440 . 2 128 . 21 GLN HE22 H 6.730 . 2 129 . 21 GLN C C 177.839 . 1 130 . 22 HIS N N 115.527 . 1 131 . 22 HIS H H 7.547 . 1 132 . 22 HIS CA C 56.573 . 1 133 . 22 HIS HA H 4.793 . 1 134 . 22 HIS CB C 30.937 . 1 135 . 22 HIS HB3 H 2.850 . 2 136 . 22 HIS HB2 H 3.243 . 2 137 . 22 HIS C C 179.014 . 1 138 . 23 GLU N N 118.288 . 1 139 . 23 GLU H H 7.869 . 1 140 . 23 GLU CA C 56.321 . 1 141 . 23 GLU HA H 4.443 . 1 142 . 23 GLU CB C 32.409 . 1 143 . 23 GLU HB3 H 2.267 . 1 144 . 23 GLU HB2 H 2.267 . 1 145 . 23 GLU CG C 37.362 . 1 146 . 23 GLU HG3 H 2.240 . 2 147 . 23 GLU HG2 H 2.267 . 2 148 . 23 GLU C C 177.634 . 1 149 . 24 VAL N N 111.116 . 1 150 . 24 VAL H H 6.985 . 1 151 . 24 VAL CA C 58.835 . 1 152 . 24 VAL HA H 4.909 . 1 153 . 24 VAL CB C 33.620 . 1 154 . 24 VAL HB H 2.714 . 1 155 . 24 VAL CG2 C 17.349 . 1 156 . 24 VAL HG2 H 0.710 . 2 157 . 24 VAL CG1 C 22.762 . 1 158 . 24 VAL HG1 H 0.977 . 2 159 . 24 VAL C C 177.373 . 1 160 . 25 ARG N N 122.511 . 1 161 . 25 ARG H H 9.099 . 1 162 . 25 ARG CA C 58.393 . 1 163 . 25 ARG HA H 4.255 . 1 164 . 25 ARG CB C 30.688 . 1 165 . 25 ARG HB3 H 1.834 . 1 166 . 25 ARG HB2 H 1.834 . 1 167 . 25 ARG CG C 27.565 . 1 168 . 25 ARG HG3 H 1.632 . 1 169 . 25 ARG HG2 H 1.632 . 1 170 . 25 ARG CD C 43.425 . 1 171 . 25 ARG HD3 H 3.239 . 1 172 . 25 ARG HD2 H 3.239 . 1 173 . 25 ARG C C 180.401 . 1 174 . 26 LYS N N 119.925 . 1 175 . 26 LYS H H 8.538 . 1 176 . 26 LYS CA C 54.896 . 1 177 . 26 LYS HA H 4.503 . 1 178 . 26 LYS CB C 36.732 . 1 179 . 26 LYS HB3 H 1.648 . 1 180 . 26 LYS HB2 H 1.648 . 1 181 . 26 LYS CG C 28.721 . 1 182 . 26 LYS HG3 H 1.288 . 1 183 . 26 LYS HG2 H 1.288 . 1 184 . 26 LYS CD C 25.096 . 1 185 . 26 LYS HD3 H 1.648 . 1 186 . 26 LYS HD2 H 1.648 . 1 187 . 26 LYS CE C 42.076 . 1 188 . 26 LYS HE3 H 2.771 . 2 189 . 26 LYS HE2 H 2.869 . 2 190 . 26 LYS C C 175.124 . 1 191 . 27 LEU N N 124.916 . 1 192 . 27 LEU H H 8.459 . 1 193 . 27 LEU CA C 53.355 . 1 194 . 27 LEU HA H 4.815 . 1 195 . 27 LEU CB C 44.467 . 1 196 . 27 LEU HB3 H 1.180 . 2 197 . 27 LEU HB2 H 1.628 . 2 198 . 27 LEU CD1 C 25.094 . 1 199 . 27 LEU HD1 H 0.526 . 2 200 . 27 LEU CD2 C 25.145 . 1 201 . 27 LEU HD2 H 0.485 . 2 202 . 27 LEU C C 177.863 . 1 203 . 28 ILE N N 128.928 . 1 204 . 28 ILE H H 9.439 . 1 205 . 28 ILE CA C 61.459 . 1 206 . 28 ILE HA H 4.215 . 1 207 . 28 ILE CB C 38.190 . 1 208 . 28 ILE HB H 2.100 . 1 209 . 28 ILE CG1 C 29.045 . 2 210 . 28 ILE HG13 H 1.450 . 2 211 . 28 ILE HG12 H 1.156 . 2 212 . 28 ILE CD1 C 14.347 . 1 213 . 28 ILE HD1 H 0.813 . 1 214 . 28 ILE CG2 C 18.125 . 1 215 . 28 ILE HG2 H 0.997 . 1 216 . 28 ILE C C 177.360 . 1 217 . 29 ALA N N 129.946 . 1 218 . 29 ALA H H 8.607 . 1 219 . 29 ALA CA C 52.192 . 1 220 . 29 ALA HA H 4.776 . 1 221 . 29 ALA CB C 21.504 . 1 222 . 29 ALA HB H 1.538 . 1 223 . 29 ALA C C 180.423 . 1 224 . 30 GLY N N 113.524 . 1 225 . 30 GLY H H 8.337 . 1 226 . 30 GLY CA C 44.264 . 1 227 . 30 GLY HA3 H 4.570 . 2 228 . 30 GLY HA2 H 3.120 . 2 229 . 31 PRO CA C 63.622 . 1 230 . 31 PRO HA H 4.450 . 1 231 . 31 PRO CB C 29.423 . 1 232 . 31 PRO HB3 H 2.131 . 1 233 . 31 PRO HB2 H 2.131 . 1 234 . 31 PRO CG C 27.609 . 1 235 . 31 PRO HG3 H 1.985 . 1 236 . 31 PRO HG2 H 1.985 . 1 237 . 31 PRO CD C 49.203 . 1 238 . 31 PRO C C 177.465 . 1 239 . 32 SER N N 116.123 . 1 240 . 32 SER H H 8.154 . 1 241 . 32 SER CA C 58.806 . 1 242 . 32 SER CB C 62.489 . 1 243 . 32 SER HB3 H 4.180 . 1 244 . 32 SER HB2 H 4.180 . 1 245 . 32 SER C C 174.914 . 1 246 . 33 VAL N N 113.846 . 1 247 . 33 VAL H H 6.446 . 1 248 . 33 VAL CA C 59.238 . 1 249 . 33 VAL HA H 4.281 . 1 250 . 33 VAL CB C 34.814 . 1 251 . 33 VAL HB H 1.725 . 1 252 . 33 VAL CG2 C 18.361 . 1 253 . 33 VAL HG2 H 0.084 . 2 254 . 33 VAL CG1 C 19.962 . 1 255 . 33 VAL HG1 H 0.257 . 2 256 . 33 VAL C C 173.945 . 1 257 . 34 TYR N N 119.897 . 1 258 . 34 TYR H H 8.658 . 1 259 . 34 TYR CA C 57.072 . 1 260 . 34 TYR HA H 5.676 . 1 261 . 34 TYR CB C 43.726 . 1 262 . 34 TYR HB3 H 2.794 . 2 263 . 34 TYR HB2 H 3.269 . 2 264 . 34 TYR CD1 C 131.450 . 1 265 . 34 TYR CD2 C 131.450 . 1 266 . 34 TYR HD1 H 6.970 . 1 267 . 34 TYR HD2 H 6.970 . 1 268 . 34 TYR CE1 C 118.430 . 1 269 . 34 TYR CE2 C 118.430 . 1 270 . 34 TYR HE1 H 7.000 . 1 271 . 34 TYR HE2 H 7.000 . 1 272 . 34 TYR C C 177.936 . 1 273 . 35 ILE N N 121.429 . 1 274 . 35 ILE H H 9.391 . 1 275 . 35 ILE CA C 60.082 . 1 276 . 35 ILE HA H 6.133 . 1 277 . 35 ILE CB C 41.716 . 1 278 . 35 ILE HB H 1.838 . 1 279 . 35 ILE CG1 C 30.247 . 1 280 . 35 ILE HG12 H 1.530 . 1 281 . 35 ILE HG13 H 1.530 . 1 282 . 35 ILE CD1 C 13.003 . 1 283 . 35 ILE HD1 H -0.121 . 1 284 . 35 ILE CG2 C 15.453 . 1 285 . 35 ILE HG2 H 0.638 . 1 286 . 35 ILE C C 175.073 . 1 287 . 36 CYS N N 108.279 . 1 288 . 36 CYS H H 9.012 . 1 289 . 36 CYS CA C 56.877 . 1 290 . 36 CYS HA H 5.983 . 1 291 . 36 CYS CB C 34.608 . 1 292 . 36 CYS HB3 H 2.833 . 2 293 . 36 CYS HB2 H 3.480 . 2 294 . 36 CYS C C 177.940 . 1 295 . 37 ASP N N 116.087 . 1 296 . 37 ASP H H 8.993 . 1 297 . 37 ASP CA C 57.280 . 1 298 . 37 ASP HA H 4.641 . 1 299 . 37 ASP CB C 41.471 . 1 300 . 37 ASP HB3 H 2.430 . 2 301 . 37 ASP HB2 H 2.706 . 2 302 . 37 ASP C C 179.640 . 1 303 . 38 GLU N N 123.464 . 1 304 . 38 GLU H H 8.184 . 1 305 . 38 GLU CA C 59.234 . 1 306 . 38 GLU HA H 4.217 . 1 307 . 38 GLU CB C 28.836 . 1 308 . 38 GLU HB3 H 2.331 . 2 309 . 38 GLU HB2 H 2.525 . 2 310 . 38 GLU CG C 36.310 . 1 311 . 38 GLU HG3 H 2.094 . 1 312 . 38 GLU HG2 H 2.094 . 1 313 . 38 GLU C C 173.199 . 1 314 . 39 CYS N N 127.261 . 1 315 . 39 CYS H H 9.201 . 1 316 . 39 CYS CA C 65.571 . 1 317 . 39 CYS HA H 4.030 . 1 318 . 39 CYS CB C 27.364 . 1 319 . 39 CYS HB3 H 2.541 . 2 320 . 39 CYS HB2 H 3.043 . 2 321 . 39 CYS C C 181.040 . 1 322 . 40 VAL N N 123.028 . 1 323 . 40 VAL H H 8.533 . 1 324 . 40 VAL CA C 68.368 . 1 325 . 40 VAL HA H 3.204 . 1 326 . 40 VAL CB C 31.139 . 1 327 . 40 VAL HB H 1.963 . 1 328 . 40 VAL CG2 C 22.160 . 1 329 . 40 VAL HG2 H 0.725 . 2 330 . 40 VAL CG1 C 24.349 . 1 331 . 40 VAL HG1 H 0.768 . 2 332 . 40 VAL C C 179.536 . 1 333 . 41 ASP N N 119.752 . 1 334 . 41 ASP H H 7.465 . 1 335 . 41 ASP CA C 58.067 . 1 336 . 41 ASP HA H 4.483 . 1 337 . 41 ASP CB C 40.539 . 1 338 . 41 ASP HB3 H 2.758 . 2 339 . 41 ASP HB2 H 2.878 . 2 340 . 41 ASP C C 180.931 . 1 341 . 42 LEU N N 120.851 . 1 342 . 42 LEU H H 7.562 . 1 343 . 42 LEU CA C 58.175 . 1 344 . 42 LEU HA H 4.198 . 1 345 . 42 LEU CB C 41.622 . 1 346 . 42 LEU HB3 H 1.819 . 1 347 . 42 LEU HB2 H 1.819 . 1 348 . 42 LEU CD1 C 26.739 . 1 349 . 42 LEU HD1 H 0.978 . 2 350 . 42 LEU CD2 C 24.559 . 1 351 . 42 LEU HD2 H 0.930 . 2 352 . 42 LEU C C 175.305 . 1 353 . 43 CYS N N 117.822 . 1 354 . 43 CYS H H 8.311 . 1 355 . 43 CYS CA C 64.330 . 1 356 . 43 CYS HA H 3.916 . 1 357 . 43 CYS CB C 27.390 . 1 358 . 43 CYS HB3 H 2.281 . 2 359 . 43 CYS HB2 H 3.241 . 2 360 . 43 CYS C C 176.643 . 1 361 . 44 ASN N N 118.807 . 1 362 . 44 ASN H H 8.490 . 1 363 . 44 ASN CA C 56.397 . 1 364 . 44 ASN HA H 4.303 . 1 365 . 44 ASN CB C 38.264 . 1 366 . 44 ASN HB3 H 2.657 . 2 367 . 44 ASN HB2 H 3.032 . 2 368 . 44 ASN ND2 N 110.740 . 1 369 . 44 ASN HD21 H 7.520 . 2 370 . 44 ASN HD22 H 7.820 . 2 371 . 44 ASN C C 179.993 . 1 372 . 45 ASP N N 121.320 . 1 373 . 45 ASP H H 7.781 . 1 374 . 45 ASP CA C 57.680 . 1 375 . 45 ASP HA H 4.404 . 1 376 . 45 ASP CB C 40.444 . 1 377 . 45 ASP HB3 H 2.703 . 2 378 . 45 ASP HB2 H 2.956 . 2 379 . 45 ASP C C 180.747 . 1 380 . 46 ILE N N 121.342 . 1 381 . 46 ILE H H 7.893 . 1 382 . 46 ILE CA C 64.874 . 1 383 . 46 ILE HA H 3.773 . 1 384 . 46 ILE CB C 38.527 . 1 385 . 46 ILE HB H 1.954 . 1 386 . 46 ILE CG1 C 28.939 . 2 387 . 46 ILE HG13 H 1.110 . 1 388 . 46 ILE HG12 H 1.110 . 1 389 . 46 ILE CD1 C 13.809 . 1 390 . 46 ILE HD1 H 0.910 . 1 391 . 46 ILE CG2 C 17.442 . 2 392 . 46 ILE HG2 H 0.902 . 4 393 . 46 ILE C C 181.232 . 1 394 . 47 ILE N N 119.729 . 1 395 . 47 ILE H H 8.280 . 1 396 . 47 ILE CA C 64.917 . 1 397 . 47 ILE HA H 4.167 . 1 398 . 47 ILE CB C 38.140 . 1 399 . 47 ILE HB H 2.343 . 1 400 . 47 ILE CD1 C 13.507 . 1 401 . 47 ILE HD1 H 0.800 . 1 402 . 47 ILE CG2 C 17.443 . 1 403 . 47 ILE HG2 H 0.923 . 1 404 . 47 ILE C C 176.880 . 1 405 . 48 ARG N N 119.325 . 1 406 . 48 ARG H H 8.035 . 1 407 . 48 ARG CA C 58.522 . 1 408 . 48 ARG HA H 4.081 . 1 409 . 48 ARG CB C 30.330 . 1 410 . 48 ARG HB3 H 1.938 . 1 411 . 48 ARG HB2 H 1.938 . 1 412 . 48 ARG CG C 27.730 . 1 413 . 48 ARG HG3 H 1.480 . 2 414 . 48 ARG HG2 H 1.685 . 2 415 . 48 ARG CD C 43.384 . 1 416 . 48 ARG HD3 H 3.219 . 1 417 . 48 ARG HD2 H 3.219 . 1 418 . 48 ARG C C 179.760 . 1 419 . 49 GLU N N 117.933 . 1 420 . 49 GLU H H 7.711 . 1 421 . 49 GLU CA C 57.790 . 1 422 . 49 GLU HA H 4.162 . 1 423 . 49 GLU CB C 30.025 . 1 424 . 49 GLU HB3 H 2.103 . 1 425 . 49 GLU HB2 H 2.103 . 1 426 . 49 GLU CG C 36.170 . 1 427 . 49 GLU HG3 H 2.100 . 2 428 . 49 GLU HG2 H 2.347 . 2 429 . 49 GLU C C 179.871 . 1 430 . 50 GLU N N 118.928 . 1 431 . 50 GLU H H 8.025 . 1 432 . 50 GLU CA C 57.463 . 1 433 . 50 GLU HA H 4.288 . 1 434 . 50 GLU CB C 30.597 . 1 435 . 50 GLU HB3 H 2.365 . 1 436 . 50 GLU HB2 H 2.365 . 1 437 . 50 GLU CG C 36.400 . 1 438 . 50 GLU HG3 H 1.970 . 1 439 . 50 GLU HG2 H 1.970 . 1 440 . 50 GLU C C 179.285 . 1 441 . 51 ILE N N 120.127 . 1 442 . 51 ILE H H 8.030 . 1 443 . 51 ILE CA C 61.214 . 1 444 . 51 ILE HA H 4.190 . 1 445 . 51 ILE CB C 38.094 . 1 446 . 51 ILE HB H 1.990 . 1 447 . 51 ILE CG1 C 27.257 . 1 448 . 51 ILE HG12 H 1.480 . 1 449 . 51 ILE HG13 H 1.480 . 1 450 . 51 ILE CD1 C 13.003 . 1 451 . 51 ILE HD1 H 0.860 . 1 452 . 51 ILE CG2 C 17.426 . 1 453 . 51 ILE HG2 H 0.876 . 1 454 . 51 ILE C C 175.916 . 1 455 . 52 LYS N N 124.569 . 1 456 . 52 LYS H H 8.087 . 1 457 . 52 LYS CA C 56.365 . 1 458 . 52 LYS HA H 4.324 . 1 459 . 52 LYS CB C 33.019 . 1 460 . 52 LYS HB3 H 1.837 . 1 461 . 52 LYS HB2 H 1.837 . 1 462 . 52 LYS CG C 24.632 . 1 463 . 52 LYS HG3 H 1.437 . 1 464 . 52 LYS HG2 H 1.437 . 1 465 . 52 LYS CD C 29.006 . 1 466 . 52 LYS HD3 H 1.686 . 1 467 . 52 LYS HD2 H 1.686 . 1 468 . 52 LYS CE C 42.119 . 1 469 . 52 LYS HE3 H 3.003 . 1 470 . 52 LYS HE2 H 3.003 . 1 471 . 52 LYS C C 178.652 . 1 472 . 53 GLU N N 121.933 . 1 473 . 53 GLU H H 8.300 . 1 474 . 53 GLU CA C 56.433 . 1 475 . 53 GLU HA H 4.332 . 1 476 . 53 GLU CB C 30.494 . 1 477 . 53 GLU HB3 H 2.250 . 1 478 . 53 GLU HB2 H 2.250 . 1 479 . 53 GLU CG C 36.223 . 1 480 . 53 GLU HG3 H 1.965 . 1 481 . 53 GLU HG2 H 1.965 . 1 482 . 53 GLU C C 176.148 . 1 483 . 54 VAL N N 121.631 . 1 484 . 54 VAL H H 8.111 . 1 485 . 54 VAL CA C 61.957 . 1 486 . 54 VAL HA H 4.127 . 1 487 . 54 VAL CB C 32.950 . 1 488 . 54 VAL HB H 2.081 . 1 489 . 54 VAL CG2 C 20.818 . 1 490 . 54 VAL HG2 H 0.943 . 1 491 . 54 VAL CG1 C 20.818 . 1 492 . 54 VAL HG1 H 0.943 . 1 493 . 54 VAL C C 175.298 . 1 494 . 55 ALA N N 129.578 . 1 495 . 55 ALA H H 8.338 . 1 496 . 55 ALA CA C 50.421 . 1 497 . 55 ALA CB C 18.480 . 1 498 . 55 ALA HB H 1.350 . 1 499 . 56 PRO CA C 63.296 . 1 500 . 56 PRO HA H 4.422 . 1 501 . 56 PRO CB C 31.924 . 1 502 . 56 PRO HB3 H 2.262 . 1 503 . 56 PRO HB2 H 2.262 . 1 504 . 56 PRO CG C 27.164 . 1 505 . 56 PRO HG3 H 1.983 . 1 506 . 56 PRO HG2 H 1.983 . 1 507 . 56 PRO CD C 50.394 . 1 508 . 56 PRO C C 175.827 . 1 509 . 57 HIS N N 124.186 . 1 510 . 57 HIS H H 7.859 . 1 511 . 57 HIS CA C 57.233 . 1 512 . 57 HIS CB C 30.681 . 1 513 . 57 HIS HD2 H 3.653 . 2 514 . 57 HIS HD1 H 3.794 . 2 stop_ save_