data_6259 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N chemical shift assignments for GatB (backbone + side chains) ; _BMRB_accession_number 6259 _BMRB_flat_file_name bmr6259.str _Entry_type original _Submission_date 2004-07-02 _Accession_date 2004-07-06 _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 VOLPON Laurent . . 2 YOUNG Chris R. . 3 GEHRING Kalle . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 480 "13C chemical shifts" 412 "15N chemical shifts" 99 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-10-02 original author . stop_ _Original_release_date 2006-10-02 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR structure of the enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system and its interaction with GatA. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16963640 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Volpon Laurent . . 2 Young Chris R. . 3 Matte A. S. . 4 Gehring Kalle . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 15 _Journal_issue 10 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2435 _Page_last 2441 _Year 2006 _Details . loop_ _Keyword 'phosphotransferase system' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'GatB monomer' _Abbreviation_common GatB _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GatB monomer' $GatB stop_ _System_molecular_weight 12462.3 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_GatB _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common GatB _Abbreviation_common GatB _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 113 _Mol_residue_sequence ; MGSSHHHHHHHHENLYFQGS KRKIIVACGGAVATSTMAAE EIKELCQSHNIPVELIQCRV NEIETYMDGVHLICTTARVD RSFGDIPLVHGMPFVSGVGI EALQNKILTILQG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 SER 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 HIS 12 HIS 13 GLU 14 ASN 15 LEU 16 TYR 17 PHE 18 GLN 19 GLY 20 SER 21 LYS 22 ARG 23 LYS 24 ILE 25 ILE 26 VAL 27 ALA 28 CYS 29 GLY 30 GLY 31 ALA 32 VAL 33 ALA 34 THR 35 SER 36 THR 37 MET 38 ALA 39 ALA 40 GLU 41 GLU 42 ILE 43 LYS 44 GLU 45 LEU 46 CYS 47 GLN 48 SER 49 HIS 50 ASN 51 ILE 52 PRO 53 VAL 54 GLU 55 LEU 56 ILE 57 GLN 58 CYS 59 ARG 60 VAL 61 ASN 62 GLU 63 ILE 64 GLU 65 THR 66 TYR 67 MET 68 ASP 69 GLY 70 VAL 71 HIS 72 LEU 73 ILE 74 CYS 75 THR 76 THR 77 ALA 78 ARG 79 VAL 80 ASP 81 ARG 82 SER 83 PHE 84 GLY 85 ASP 86 ILE 87 PRO 88 LEU 89 VAL 90 HIS 91 GLY 92 MET 93 PRO 94 PHE 95 VAL 96 SER 97 GLY 98 VAL 99 GLY 100 ILE 101 GLU 102 ALA 103 LEU 104 GLN 105 ASN 106 LYS 107 ILE 108 LEU 109 THR 110 ILE 111 LEU 112 GLN 113 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 PDB 1TVM "Nmr Structure Of Enzyme Gatb Of The Galactitol-Specific Phosphoenolpyruvate-Dependent Phosphotransferase System" 100.00 113 100.00 100.00 4.40e-76 DBJ BAB36319 "galactitol-specific enzyme IIB of phosphotransferase system [Escherichia coli O157:H7 str. Sakai]" 82.30 94 100.00 100.00 3.75e-60 DBJ BAG77886 "PTS system galactitol-specific IIB component [Escherichia coli SE11]" 69.91 89 100.00 100.00 9.23e-50 DBJ BAH46969 "galactitol-specific enzyme IIB component of PTS [Escherichia coli O55:H7]" 82.30 94 98.92 100.00 1.08e-59 DBJ BAI31343 "galactitol-specific enzyme IIB component of PTS [Escherichia coli O103:H2 str. 12009]" 82.30 94 98.92 98.92 7.12e-59 DBJ BAI55515 "PTS system galactitol-specific IIB component [Escherichia coli SE15]" 82.30 94 97.85 100.00 5.85e-59 EMBL CAA56229 "gatB [Escherichia coli]" 82.30 94 100.00 100.00 3.75e-60 EMBL CAR03521 "galactitol-specific enzyme IIB component of PTS [Escherichia coli S88]" 82.30 94 97.85 100.00 6.67e-59 EMBL CAR13613 "galactitol-specific enzyme IIB component of PTS [Escherichia coli UMN026]" 82.30 94 98.92 100.00 1.08e-59 EMBL CAR17061 "galactitol-specific enzyme IIB component of PTS [Escherichia coli IAI39]" 82.30 94 98.92 100.00 1.76e-59 EMBL CAS09786 "galactitol-specific enzyme IIB component of PTS [Escherichia coli O127:H6 str. E2348/69]" 82.30 94 98.92 98.92 2.22e-59 GB AAG57150 "galactitol-specific enzyme IIB of phosphotransferase system [Escherichia coli O157:H7 str. EDL933]" 82.30 94 100.00 100.00 3.75e-60 GB AAN43688 "galactitol-specific enzyme IIB of phosphotransferase system [Shigella flexneri 2a str. 301]" 82.30 94 100.00 100.00 3.75e-60 GB AAN81074 "PTS system, galactitol-specific IIB component [Escherichia coli CFT073]" 82.30 94 100.00 100.00 3.75e-60 GB AAP17514 "galactitol-specific enzyme IIB of phosphotransferase system [Shigella flexneri 2a str. 2457T]" 82.30 94 100.00 100.00 3.75e-60 GB ABB62344 "galactitol-specific enzyme IIB of phosphotransferase system [Shigella dysenteriae Sd197]" 72.57 86 98.78 100.00 1.74e-51 PRF 2113201D "carbohydrate phosphotransferase II" 82.30 94 100.00 100.00 3.75e-60 REF NP_288595 "PTS system galactitol-specific transporter subunit IIB [Escherichia coli O157:H7 str. EDL933]" 82.30 94 100.00 100.00 3.75e-60 REF NP_310923 "PTS system galactitol-specific transporter subunit IIB [Escherichia coli O157:H7 str. Sakai]" 82.30 94 100.00 100.00 3.75e-60 REF NP_707981 "PTS system galactitol-specific transporter subunit IIB [Shigella flexneri 2a str. 301]" 82.30 94 100.00 100.00 3.75e-60 REF NP_754506 "PTS system galactitol-specific transporter subunit IIB [Escherichia coli CFT073]" 82.30 94 100.00 100.00 3.75e-60 REF NP_837705 "galactitol-specific PTS system component IIB [Shigella flexneri 2a str. 2457T]" 82.30 94 100.00 100.00 3.75e-60 SP P0A435 "RecName: Full=Galactitol-specific phosphotransferase enzyme IIB component; AltName: Full=EIIB-Gat; AltName: Full=PTS system gal" 82.30 94 100.00 100.00 3.75e-60 SP P0A436 "RecName: Full=Galactitol-specific phosphotransferase enzyme IIB component; AltName: Full=EIIB-Gat; AltName: Full=PTS system gal" 82.30 94 100.00 100.00 3.75e-60 SP P0A437 "RecName: Full=Galactitol-specific phosphotransferase enzyme IIB component; AltName: Full=EIIB-Gat; AltName: Full=PTS system gal" 82.30 94 100.00 100.00 3.75e-60 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GatB 'Escherichia coli' 562 Bacteria . Escherichia coli 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 $GatB 'recombinant technology' 'E. coli' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; Uniformly isotope-labeled protein was obtained by growing E. coli bacteria at 37????C in M9 minimal medium containing 0.5 g of 15N-NH4Cl and/or 2 g of 13C6-Glucose (Cambridge Isotope Laboratory) per liter of media and 100 mg/ml of ampicilin. The culture was then induced with 1 mM IPTG at 30??C for 4 hours. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $GatB 1.0 mM '[U-13C; U-15N]' KCl 75 mM . NaCl 75 mM . stop_ save_ ############################ # Computer software used # ############################ save_Sparky _Saveframe_category software _Name Sparky _Version 3.106 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_(HCCH)_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '(HCCH) TOCSY' _Sample_label $sample_1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_2D_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '(HCCH) TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.1 pH temperature 298 0.1 K pressure 1 . atm 'ionic strength' 0.15 0.01 M 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 water H 1 protons ppm 4.772925 external indirect . . . . $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.00 external indirect . . . 0.101329118 $citation_1 $citation_1 DSS C 13 'methyl protons' ppm 0.00 external indirect . . . 0.251449530 $citation_1 $citation_1 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_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GatB monomer' _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 MET CA C 55.07 0.1 1 2 . 1 MET HA H 4.543 0.02 1 3 . 1 MET C C 174.619 0.1 1 4 . 1 MET CB C 29.05 0.1 1 5 . 1 MET HB2 H 2.696 0.02 1 6 . 1 MET HB3 H 2.638 0.02 1 7 . 2 GLY H H 7.877 0.02 1 8 . 2 GLY N N 108.5 0.1 1 9 . 2 GLY CA C 44.22 0.1 1 10 . 3 SER CA C 57.73 0.1 1 11 . 3 SER HA H 4.49 0.02 1 12 . 3 SER CB C 63.28 0.1 1 13 . 3 SER HB2 H 3.815 0.02 2 14 . 12 HIS CA C 55.24 0.1 1 15 . 12 HIS HA H 4.543 0.02 1 16 . 12 HIS C C 174.124 0.1 1 17 . 12 HIS CB C 29.21 0.1 1 18 . 12 HIS HB2 H 3.039 0.02 1 19 . 12 HIS HB3 H 2.96 0.02 1 20 . 13 GLU H H 8.456 0.02 1 21 . 13 GLU N N 120.2 0.1 1 22 . 13 GLU CA C 56.19 0.1 1 23 . 13 GLU HA H 4.195 0.02 1 24 . 13 GLU C C 175.281 0.1 1 25 . 13 GLU CB C 29.7 0.1 1 26 . 13 GLU HB2 H 1.962 0.02 1 27 . 13 GLU HB3 H 1.851 0.02 1 28 . 13 GLU CG C 35.53 0.1 1 29 . 13 GLU HG2 H 2.157 0.02 2 30 . 14 ASN H H 8.471 0.02 1 31 . 14 ASN N N 117.8 0.1 1 32 . 14 ASN CA C 52.66 0.1 1 33 . 14 ASN HA H 4.622 0.02 1 34 . 14 ASN C C 174 0.1 1 35 . 14 ASN CB C 38.14 0.1 1 36 . 14 ASN HB2 H 2.749 0.02 1 37 . 14 ASN HB3 H 2.69 0.02 1 38 . 15 LEU H H 8.05 0.02 1 39 . 15 LEU N N 120.5 0.1 1 40 . 15 LEU CA C 54.54 0.1 1 41 . 15 LEU HA H 4.2 0.02 1 42 . 15 LEU C C 176.245 0.1 1 43 . 15 LEU CB C 41.68 0.1 1 44 . 15 LEU HB2 H 1.424 0.02 1 45 . 15 LEU HB3 H 1.302 0.02 1 46 . 15 LEU CG C 26.29 0.1 1 47 . 15 LEU CD1 C 24.3 0.1 1 48 . 15 LEU HD1 H 0.762 0.02 2 49 . 15 LEU CD2 C 22.66 0.1 1 50 . 15 LEU HD2 H 0.764 0.02 2 51 . 15 LEU HG H 1.413 0.02 1 52 . 16 TYR H H 7.972 0.02 1 53 . 16 TYR N N 118.1 0.1 1 54 . 16 TYR CA C 57.2 0.1 1 55 . 16 TYR HA H 4.48 0.02 1 56 . 16 TYR C C 174.757 0.1 1 57 . 16 TYR CB C 38.18 0.1 1 58 . 16 TYR HB2 H 2.807 0.02 2 59 . 16 TYR HD1 H 6.875 0.02 3 60 . 16 TYR HE1 H 6.627 0.02 3 61 . 17 PHE H H 8.001 0.02 1 62 . 17 PHE N N 119.9 0.1 1 63 . 17 PHE CA C 57.42 0.1 1 64 . 17 PHE HA H 4.543 0.02 1 65 . 17 PHE C C 174.923 0.1 1 66 . 17 PHE CB C 38.97 0.1 1 67 . 17 PHE HB2 H 3.049 0.02 1 68 . 17 PHE HB3 H 3.007 0.02 1 69 . 17 PHE HD1 H 7.084 0.02 3 70 . 17 PHE HE1 H 7.08 0.02 3 71 . 18 GLN H H 8.224 0.02 1 72 . 18 GLN N N 120.8 0.1 1 73 . 18 GLN CA C 55.56 0.1 1 74 . 18 GLN HA H 4.216 0.02 1 75 . 18 GLN C C 175.419 0.1 1 76 . 18 GLN CB C 28.4 0.1 1 77 . 18 GLN HB2 H 2.141 0.02 2 78 . 18 GLN CG C 33.02 0.1 1 79 . 18 GLN HG2 H 2.252 0.02 2 80 . 19 GLY H H 7.772 0.02 1 81 . 19 GLY N N 107.4 0.1 1 82 . 19 GLY CA C 44.52 0.1 1 83 . 19 GLY HA2 H 4.021 0.02 1 84 . 19 GLY HA3 H 3.878 0.02 1 85 . 19 GLY C C 173.01 0.1 1 86 . 20 SER H H 8.008 0.02 1 87 . 20 SER N N 113.5 0.1 1 88 . 20 SER CA C 57.52 0.1 1 89 . 20 SER HA H 4.411 0.02 1 90 . 20 SER C C 173.407 0.1 1 91 . 20 SER CB C 63.52 0.1 1 92 . 20 SER HB2 H 3.841 0.02 2 93 . 21 LYS H H 8.141 0.02 1 94 . 21 LYS N N 120.2 0.1 1 95 . 21 LYS CA C 56.44 0.1 1 96 . 21 LYS HA H 4.079 0.02 1 97 . 21 LYS C C 176.273 0.1 1 98 . 21 LYS CB C 32.24 0.1 1 99 . 21 LYS HB2 H 1.624 0.02 2 100 . 21 LYS CG C 24.22 0.1 1 101 . 21 LYS HG2 H 1.244 0.02 2 102 . 21 LYS CD C 28.84 0.1 1 103 . 21 LYS HD2 H 1.55 0.02 2 104 . 21 LYS CE C 41.26 0.1 1 105 . 21 LYS HE2 H 2.844 0.02 2 106 . 22 ARG H H 8.374 0.02 1 107 . 22 ARG N N 122.3 0.1 1 108 . 22 ARG CA C 52.85 0.1 1 109 . 22 ARG HA H 4.665 0.02 1 110 . 22 ARG C C 173.903 0.1 1 111 . 22 ARG CB C 31.51 0.1 1 112 . 22 ARG HB2 H 1.724 0.02 1 113 . 22 ARG HB3 H 1.355 0.02 1 114 . 22 ARG CG C 26.54 0.1 1 115 . 22 ARG HG2 H 1.587 0.02 1 116 . 22 ARG HG3 H 1.302 0.02 1 117 . 22 ARG CD C 41.64 0.1 1 118 . 22 ARG HD2 H 2.574 0.02 1 119 . 22 ARG HD3 H 2.474 0.02 1 120 . 23 LYS H H 11.22 0.02 1 121 . 23 LYS N N 126.6 0.1 1 122 . 23 LYS CA C 55.2 0.1 1 123 . 23 LYS HA H 5.256 0.02 1 124 . 23 LYS C C 174.867 0.1 1 125 . 23 LYS CB C 34.32 0.1 1 126 . 23 LYS HB2 H 1.909 0.02 1 127 . 23 LYS HB3 H 1.777 0.02 1 128 . 23 LYS CG C 25.14 0.1 1 129 . 23 LYS HG2 H 1.403 0.02 1 130 . 23 LYS HG3 H 1.144 0.02 1 131 . 23 LYS CD C 29.07 0.1 1 132 . 23 LYS HD2 H 1.582 0.02 1 133 . 23 LYS HD3 H 1.484 0.02 1 134 . 23 LYS CE C 41.45 0.1 1 135 . 23 LYS HE2 H 2.78 0.02 2 136 . 24 ILE H H 8.687 0.02 1 137 . 24 ILE N N 123.7 0.1 1 138 . 24 ILE CA C 58.7 0.1 1 139 . 24 ILE HA H 4.981 0.02 1 140 . 24 ILE C C 174.316 0.1 1 141 . 24 ILE CB C 42.42 0.1 1 142 . 24 ILE HB H 1.524 0.02 1 143 . 24 ILE CG2 C 15.81 0.1 1 144 . 24 ILE HG2 H 0.653 0.02 1 145 . 24 ILE CG1 C 26.19 0.1 1 146 . 24 ILE HG12 H 1.418 0.02 1 147 . 24 ILE HG13 H 0.912 0.02 1 148 . 24 ILE CD1 C 14.95 0.1 1 149 . 24 ILE HD1 H 0.637 0.02 1 150 . 25 ILE H H 8.204 0.02 1 151 . 25 ILE N N 123.4 0.1 1 152 . 25 ILE CA C 59.1 0.1 1 153 . 25 ILE HA H 4.86 0.02 1 154 . 25 ILE C C 174.427 0.1 1 155 . 25 ILE CB C 40.33 0.1 1 156 . 25 ILE HB H 1.461 0.02 1 157 . 25 ILE CG2 C 18.01 0.1 1 158 . 25 ILE HG2 H 0.706 0.02 1 159 . 25 ILE CG1 C 27.76 0.1 1 160 . 25 ILE HG12 H 1.566 0.02 1 161 . 25 ILE CD1 C 14.38 0.1 1 162 . 25 ILE HD1 H 0.674 0.02 1 163 . 26 VAL H H 9.005 0.02 1 164 . 26 VAL N N 126.7 0.1 1 165 . 26 VAL CA C 60.54 0.1 1 166 . 26 VAL HA H 4.876 0.02 1 167 . 26 VAL C C 173.6 0.1 1 168 . 26 VAL CB C 31.9 0.1 1 169 . 26 VAL HB H 1.798 0.02 1 170 . 26 VAL CG1 C 21.07 0.1 1 171 . 26 VAL HG1 H 0.827 0.02 2 172 . 26 VAL CG2 C 21.64 0.1 1 173 . 26 VAL HG2 H 0.685 0.02 2 174 . 27 ALA H H 8.692 0.02 1 175 . 27 ALA N N 127.8 0.1 1 176 . 27 ALA CA C 48.59 0.1 1 177 . 27 ALA HA H 5.53 0.02 1 178 . 27 ALA C C 175.363 0.1 1 179 . 27 ALA CB C 21.54 0.1 1 180 . 27 ALA HB H 0.964 0.02 1 181 . 28 CYS H H 8.601 0.02 1 182 . 28 CYS N N 118.8 0.1 1 183 . 28 CYS CA C 56.19 0.1 1 184 . 28 CYS HA H 4.907 0.02 1 185 . 28 CYS C C 174.124 0.1 1 186 . 28 CYS CB C 30.68 0.1 1 187 . 28 CYS HB2 H 2.923 0.02 1 188 . 28 CYS HB3 H 2.743 0.02 1 189 . 29 GLY H H 8.365 0.02 1 190 . 29 GLY N N 110.8 0.1 1 191 . 30 GLY H H 8.517 0.02 1 192 . 30 GLY N N 109 0.1 1 193 . 30 GLY CA C 44.37 0.1 1 194 . 30 GLY HA2 H 3.941 0.02 2 195 . 30 GLY C C 172.994 0.1 1 196 . 31 ALA H H 8.171 0.02 1 197 . 31 ALA N N 123.5 0.1 1 198 . 31 ALA CA C 51.25 0.1 1 199 . 31 ALA HA H 4.469 0.02 1 200 . 31 ALA C C 177.38 0.1 1 201 . 31 ALA CB C 17.65 0.1 1 202 . 31 ALA HB H 1.429 0.02 1 203 . 32 VAL H H 8.056 0.02 1 204 . 32 VAL N N 120 0.1 1 205 . 32 VAL CA C 63.495 0.1 1 206 . 32 VAL C C 176.548 0.1 1 207 . 32 VAL CB C 31.503 0.1 1 208 . 33 ALA H H 8.564 0.02 1 209 . 33 ALA N N 122.4 0.1 1 210 . 33 ALA CA C 53.83 0.1 1 211 . 33 ALA HA H 4.2 0.02 1 212 . 33 ALA C C 178.78 0.1 1 213 . 33 ALA CB C 18.01 0.1 1 214 . 33 ALA HB H 1.408 0.02 1 215 . 34 THR H H 7.629 0.02 1 216 . 34 THR N N 108.8 0.1 1 217 . 34 THR CA C 63.2 0.1 1 218 . 34 THR HA H 4.195 0.02 1 219 . 34 THR C C 175.487 0.1 1 220 . 34 THR CB C 68.7 0.1 1 221 . 34 THR HB H 4.316 0.02 1 222 . 34 THR CG2 C 21.52 0.1 1 223 . 34 THR HG2 H 1.297 0.02 1 224 . 35 SER H H 7.88 0.02 1 225 . 35 SER N N 115.5 0.1 1 226 . 35 SER CA C 59.61 0.1 1 227 . 35 SER HA H 4.2 0.02 1 228 . 35 SER C C 175.088 0.1 1 229 . 35 SER CB C 62.41 0.1 1 230 . 35 SER HB2 H 3.905 0.02 1 231 . 35 SER HB3 H 3.82 0.02 1 232 . 36 THR H H 8.031 0.02 1 233 . 36 THR N N 115.9 0.1 1 234 . 36 THR CA C 64.93 0.1 1 235 . 36 THR HA H 3.941 0.02 1 236 . 36 THR C C 174.923 0.1 1 237 . 36 THR CB C 68.51 0.1 1 238 . 36 THR HB H 4.2 0.02 1 239 . 36 THR CG2 C 21.24 0.1 1 240 . 36 THR HG2 H 1.207 0.02 1 241 . 37 MET H H 7.816 0.02 1 242 . 37 MET N N 118.8 0.1 1 243 . 37 MET CA C 58.34 0.1 1 244 . 37 MET HA H 4.121 0.02 1 245 . 37 MET C C 177.347 0.1 1 246 . 37 MET CB C 31.73 0.1 1 247 . 37 MET HB2 H 2.046 0.02 2 248 . 37 MET CG C 31.61 0.1 1 249 . 37 MET HG2 H 2.648 0.02 1 250 . 37 MET HG3 H 2.495 0.02 1 251 . 38 ALA H H 7.915 0.02 1 252 . 38 ALA N N 118 0.1 1 253 . 38 ALA CA C 54.23 0.1 1 254 . 38 ALA HA H 3.493 0.02 1 255 . 38 ALA C C 177.595 0.1 1 256 . 38 ALA CB C 17.14 0.1 1 257 . 38 ALA HB H 1.26 0.02 1 258 . 39 ALA H H 8.116 0.02 1 259 . 39 ALA N N 116.3 0.1 1 260 . 39 ALA CA C 54.99 0.1 1 261 . 39 ALA HA H 3.709 0.02 1 262 . 39 ALA C C 178.422 0.1 1 263 . 39 ALA CB C 17.48 0.1 1 264 . 39 ALA HB H 1.308 0.02 1 265 . 40 GLU H H 8.023 0.02 1 266 . 40 GLU N N 115.2 0.1 1 267 . 40 GLU CA C 58.66 0.1 1 268 . 40 GLU HA H 3.841 0.02 1 269 . 40 GLU C C 179.056 0.1 1 270 . 40 GLU CB C 28.01 0.1 1 271 . 40 GLU CG C 35.56 0.1 1 272 . 40 GLU HG2 H 2.332 0.02 1 273 . 40 GLU HG3 H 2.289 0.02 1 274 . 41 GLU H H 7.794 0.02 1 275 . 41 GLU N N 116.9 0.1 1 276 . 41 GLU CA C 58.07 0.1 1 277 . 41 GLU HA H 3.894 0.02 1 278 . 41 GLU C C 179.772 0.1 1 279 . 41 GLU CB C 27.93 0.1 1 280 . 41 GLU HB2 H 1.482 0.02 1 281 . 41 GLU HB3 H 1.049 0.02 1 282 . 42 ILE H H 8.043 0.02 1 283 . 42 ILE N N 119.5 0.1 1 284 . 42 ILE CA C 65.27 0.1 1 285 . 42 ILE HA H 3.456 0.02 1 286 . 42 ILE C C 176.934 0.1 1 287 . 42 ILE CB C 36.97 0.1 1 288 . 42 ILE HB H 1.682 0.02 1 289 . 42 ILE CG2 C 18.01 0.1 1 290 . 42 ILE HG2 H 0.706 0.02 1 291 . 42 ILE CG1 C 30.28 0.1 1 292 . 42 ILE HG12 H 1.746 0.02 2 293 . 42 ILE CD1 C 12.82 0.1 1 294 . 42 ILE HD1 H 0.706 0.02 1 295 . 43 LYS H H 8.36 0.02 1 296 . 43 LYS N N 119.7 0.1 1 297 . 43 LYS CA C 60.29 0.1 1 298 . 43 LYS HA H 3.646 0.02 1 299 . 43 LYS C C 178.256 0.1 1 300 . 43 LYS CB C 31.42 0.1 1 301 . 43 LYS HB2 H 1.856 0.02 1 302 . 43 LYS HB3 H 1.809 0.02 1 303 . 43 LYS CG C 24.68 0.1 1 304 . 43 LYS HG2 H 1.466 0.02 1 305 . 43 LYS HG3 H 1.255 0.02 1 306 . 43 LYS CD C 28.8 0.1 1 307 . 43 LYS HD2 H 1.593 0.02 2 308 . 43 LYS CE C 41.24 0.1 1 309 . 43 LYS HE2 H 2.817 0.02 2 310 . 44 GLU H H 7.95 0.02 1 311 . 44 GLU N N 117.5 0.1 1 312 . 44 GLU CA C 58.75 0.1 1 313 . 44 GLU HA H 4.047 0.02 1 314 . 44 GLU C C 178.394 0.1 1 315 . 44 GLU CB C 28.38 0.1 1 316 . 44 GLU HB2 H 2.052 0.02 2 317 . 44 GLU CG C 35.11 0.1 1 318 . 44 GLU HG2 H 2.284 0.02 2 319 . 45 LEU H H 7.986 0.02 1 320 . 45 LEU N N 120.7 0.1 1 321 . 45 LEU CA C 57.52 0.1 1 322 . 45 LEU HA H 4.195 0.02 1 323 . 45 LEU C C 178.67 0.1 1 324 . 45 LEU CB C 42.12 0.1 1 325 . 45 LEU HB2 H 2.041 0.02 1 326 . 45 LEU HB3 H 1.698 0.02 1 327 . 45 LEU CD1 C 23.39 0.1 1 328 . 45 LEU HD1 H 0.901 0.02 2 329 . 45 LEU CD2 C 25.61 0.1 1 330 . 45 LEU HD2 H 0.905 0.02 2 331 . 46 CYS H H 8.265 0.02 1 332 . 46 CYS N N 114.8 0.1 1 333 . 46 CYS CA C 64.72 0.1 1 334 . 46 CYS HA H 3.91 0.02 1 335 . 46 CYS C C 176.851 0.1 1 336 . 46 CYS CB C 25.42 0.1 1 337 . 46 CYS HB2 H 3.313 0.02 1 338 . 46 CYS HB3 H 2.838 0.02 1 339 . 47 GLN H H 8.655 0.02 1 340 . 47 GLN N N 119.6 0.1 1 341 . 47 GLN CA C 58.75 0.1 1 342 . 47 GLN HA H 4.079 0.02 1 343 . 47 GLN C C 179.744 0.1 1 344 . 47 GLN CB C 27.27 0.1 1 345 . 47 GLN CG C 33.42 0.1 1 346 . 47 GLN HG2 H 2.442 0.02 1 347 . 47 GLN HG3 H 2.395 0.02 1 348 . 48 SER H H 8.359 0.02 1 349 . 48 SER N N 113.1 0.1 1 350 . 48 SER CA C 60.5 0.1 1 351 . 48 SER HA H 4.153 0.02 1 352 . 48 SER C C 174.316 0.1 1 353 . 48 SER CB C 62.56 0.1 1 354 . 48 SER HB2 H 3.968 0.02 1 355 . 48 SER HB3 H 3.899 0.02 1 356 . 49 HIS H H 7.262 0.02 1 357 . 49 HIS N N 115.2 0.1 1 358 . 49 HIS CA C 55.6 0.1 1 359 . 49 HIS HA H 4.533 0.02 1 360 . 49 HIS C C 171.947 0.1 1 361 . 49 HIS CB C 28.38 0.1 1 362 . 49 HIS HB2 H 2.543 0.02 2 363 . 50 ASN H H 7.755 0.02 1 364 . 50 ASN N N 114.3 0.1 1 365 . 50 ASN CA C 53.64 0.1 1 366 . 50 ASN HA H 4.227 0.02 1 367 . 50 ASN C C 172.925 0.1 1 368 . 50 ASN CB C 36.59 0.1 1 369 . 50 ASN HB2 H 3.028 0.02 2 370 . 51 ILE H H 8.23 0.02 1 371 . 51 ILE N N 117.9 0.1 1 372 . 51 ILE CA C 57.73 0.1 1 373 . 51 ILE HA H 4.306 0.02 1 374 . 51 ILE CB C 39.55 0.1 1 375 . 51 ILE HB H 1.471 0.02 1 376 . 51 ILE CG2 C 16 0.1 1 377 . 51 ILE HG2 H 0.579 0.02 1 378 . 51 ILE CG1 C 26.2 0.1 1 379 . 51 ILE HG12 H 1.508 0.02 1 380 . 51 ILE HG13 H 0.769 0.02 1 381 . 51 ILE CD1 C 13.64 0.1 1 382 . 51 ILE HD1 H 0.664 0.02 1 383 . 52 PRO CA C 61.87 0.1 1 384 . 52 PRO HA H 4.411 0.02 1 385 . 52 PRO C C 175.749 0.1 1 386 . 52 PRO CB C 30.95 0.1 1 387 . 52 PRO HB2 H 2.157 0.02 1 388 . 52 PRO HB3 H 1.693 0.02 1 389 . 52 PRO CG C 26.65 0.1 1 390 . 52 PRO HG2 H 1.973 0.02 1 391 . 52 PRO HG3 H 1.841 0.02 1 392 . 52 PRO CD C 50.4 0.1 1 393 . 52 PRO HD2 H 3.862 0.02 1 394 . 52 PRO HD3 H 3.514 0.02 1 395 . 53 VAL H H 8.208 0.02 1 396 . 53 VAL N N 117.2 0.1 1 397 . 53 VAL CA C 58.2 0.1 1 398 . 53 VAL HA H 5.419 0.02 1 399 . 53 VAL C C 173.297 0.1 1 400 . 53 VAL CB C 36.1 0.1 1 401 . 53 VAL HB H 1.809 0.02 1 402 . 53 VAL CG1 C 20.14 0.1 1 403 . 53 VAL HG1 H 0.843 0.02 2 404 . 53 VAL CG2 C 20.25 0.1 1 405 . 53 VAL HG2 H 0.748 0.02 2 406 . 54 GLU H H 8.774 0.02 1 407 . 54 GLU N N 125.3 0.1 1 408 . 54 GLU CA C 54.42 0.1 1 409 . 54 GLU HA H 4.469 0.02 1 410 . 54 GLU C C 172.746 0.1 1 411 . 54 GLU CB C 31.7 0.1 1 412 . 54 GLU CG C 35.12 0.1 1 413 . 54 GLU HG2 H 2.126 0.02 1 414 . 54 GLU HG3 H 1.946 0.02 1 415 . 55 LEU H H 8.624 0.02 1 416 . 55 LEU N N 125.9 0.1 1 417 . 55 LEU CA C 53.17 0.1 1 418 . 55 LEU HA H 5.092 0.02 1 419 . 55 LEU C C 175.556 0.1 1 420 . 55 LEU CB C 43.23 0.1 1 421 . 55 LEU HB2 H 1.445 0.02 2 422 . 55 LEU CG C 27.64 0.1 1 423 . 55 LEU CD1 C 25.53 0.1 1 424 . 55 LEU HD1 H 0.695 0.02 2 425 . 55 LEU CD2 C 24.89 0.1 1 426 . 55 LEU HD2 H 0.753 0.02 2 427 . 55 LEU HG H 1.424 0.02 1 428 . 56 ILE H H 9.051 0.02 1 429 . 56 ILE N N 126.4 0.1 1 430 . 56 ILE CA C 59.38 0.1 1 431 . 56 ILE HA H 4.068 0.02 1 432 . 56 ILE C C 173.572 0.1 1 433 . 56 ILE CB C 39.64 0.1 1 434 . 56 ILE HB H 1.54 0.02 1 435 . 56 ILE CG2 C 16.13 0.1 1 436 . 56 ILE HG2 H 0.236 0.02 1 437 . 56 ILE CG1 C 27.02 0.1 1 438 . 56 ILE HG12 H 1.26 0.02 1 439 . 56 ILE HG13 H 0.975 0.02 1 440 . 56 ILE CD1 C 13.51 0.1 1 441 . 56 ILE HD1 H 0.7 0.02 1 442 . 57 GLN H H 8.437 0.02 1 443 . 57 GLN N N 124.6 0.1 1 444 . 57 GLN CA C 53.81 0.1 1 445 . 57 GLN HA H 5.314 0.02 1 446 . 57 GLN C C 173.958 0.1 1 447 . 57 GLN CB C 29.83 0.1 1 448 . 57 GLN HB2 H 1.746 0.02 2 449 . 57 GLN CG C 34.33 0.1 1 450 . 57 GLN HG2 H 2.041 0.02 1 451 . 57 GLN HG3 H 1.909 0.02 1 452 . 58 CYS H H 8.306 0.02 1 453 . 58 CYS N N 117.2 0.1 1 454 . 58 CYS CA C 55.07 0.1 1 455 . 58 CYS HA H 4.929 0.02 1 456 . 58 CYS C C 171.947 0.1 1 457 . 58 CYS CB C 30.66 0.1 1 458 . 58 CYS HB2 H 3.424 0.02 1 459 . 58 CYS HB3 H 2.089 0.02 1 460 . 59 ARG H H 9.021 0.02 1 461 . 59 ARG N N 117.1 0.1 1 462 . 59 ARG CA C 54.65 0.1 1 463 . 59 ARG HA H 5.066 0.02 1 464 . 59 ARG C C 179.331 0.1 1 465 . 59 ARG CB C 30.96 0.1 1 466 . 59 ARG HB2 H 2.157 0.02 1 467 . 59 ARG HB3 H 1.688 0.02 1 468 . 59 ARG CG C 27.44 0.1 1 469 . 59 ARG HG2 H 1.746 0.02 1 470 . 59 ARG HG3 H 1.677 0.02 1 471 . 59 ARG CD C 42.66 0.1 1 472 . 59 ARG HD2 H 3.187 0.02 2 473 . 60 VAL H H 8.339 0.02 1 474 . 60 VAL N N 119.3 0.1 1 475 . 60 VAL CA C 65.57 0.1 1 476 . 60 VAL HA H 3.54 0.02 1 477 . 60 VAL C C 176.59 0.1 1 478 . 60 VAL CB C 31.12 0.1 1 479 . 60 VAL HB H 2.073 0.02 1 480 . 60 VAL CG1 C 21.13 0.1 1 481 . 60 VAL HG1 H 0.917 0.02 2 482 . 60 VAL CG2 C 21.1 0.1 1 483 . 60 VAL HG2 H 0.91 0.02 2 484 . 61 ASN H H 8.333 0.02 1 485 . 61 ASN N N 112.9 0.1 1 486 . 61 ASN CA C 53.85 0.1 1 487 . 61 ASN HA H 4.274 0.02 1 488 . 61 ASN C C 174.895 0.1 1 489 . 61 ASN CB C 36.56 0.1 1 490 . 61 ASN HB2 H 3.034 0.02 1 491 . 61 ASN HB3 H 2.775 0.02 1 492 . 62 GLU H H 7.802 0.02 1 493 . 62 GLU N N 115.4 0.1 1 494 . 62 GLU CA C 55.02 0.1 1 495 . 62 GLU C C 176.08 0.1 1 496 . 62 GLU CB C 31.235 0.1 1 497 . 63 ILE H H 7.105 0.02 1 498 . 63 ILE N N 118.5 0.1 1 499 . 63 ILE CA C 66.38 0.1 1 500 . 63 ILE HA H 3.382 0.02 1 501 . 63 ILE C C 176.686 0.1 1 502 . 63 ILE CB C 37.73 0.1 1 503 . 63 ILE HB H 1.423 0.02 1 504 . 63 ILE CG2 C 17.17 0.1 1 505 . 63 ILE HG2 H 0.171 0.02 1 506 . 63 ILE CG1 C 29.87 0.1 1 507 . 63 ILE HG12 H 1.804 0.02 1 508 . 63 ILE HG13 H 0.373 0.02 1 509 . 63 ILE CD1 C 13.66 0.1 1 510 . 63 ILE HD1 H 0.547 0.02 1 511 . 64 GLU H H 9.157 0.02 1 512 . 64 GLU N N 113.8 0.1 1 513 . 64 GLU CA C 59.74 0.1 1 514 . 64 GLU HA H 4.073 0.02 1 515 . 64 GLU C C 177.76 0.1 1 516 . 64 GLU CB C 27.81 0.1 1 517 . 64 GLU HB2 H 2.004 0.02 2 518 . 65 THR H H 7.563 0.02 1 519 . 65 THR N N 112.6 0.1 1 520 . 65 THR CA C 64.32 0.1 1 521 . 65 THR HA H 3.783 0.02 1 522 . 65 THR C C 174.399 0.1 1 523 . 65 THR CB C 68.34 0.1 1 524 . 65 THR HB H 3.894 0.02 1 525 . 65 THR CG2 C 20.75 0.1 1 526 . 65 THR HG2 H 0.606 0.02 1 527 . 66 TYR H H 7.369 0.02 1 528 . 66 TYR N N 116.7 0.1 1 529 . 66 TYR CA C 57.86 0.1 1 530 . 66 TYR HA H 4.654 0.02 1 531 . 66 TYR C C 175.529 0.1 1 532 . 66 TYR CB C 40.07 0.1 1 533 . 66 TYR HB2 H 3.282 0.02 1 534 . 66 TYR HB3 H 2.337 0.02 1 535 . 66 TYR HD1 H 7.047 0.02 3 536 . 66 TYR HE1 H 6.577 0.02 3 537 . 67 MET H H 6.972 0.02 1 538 . 67 MET N N 113.7 0.1 1 539 . 67 MET CA C 57.71 0.1 1 540 . 67 MET HA H 3.868 0.02 1 541 . 67 MET C C 174.768 0.1 1 542 . 67 MET CB C 32.1 0.1 1 543 . 67 MET HB2 H 1.994 0.02 1 544 . 67 MET HB3 H 1.851 0.02 1 545 . 67 MET CG C 30.56 0.1 1 546 . 67 MET HG2 H 2.648 0.02 1 547 . 67 MET HG3 H 2.347 0.02 1 548 . 68 ASP H H 8.04 0.02 1 549 . 68 ASP N N 120 0.1 1 550 . 68 ASP CA C 55.56 0.1 1 551 . 68 ASP HA H 4.316 0.02 1 552 . 68 ASP C C 176.603 0.1 1 553 . 68 ASP CB C 40.14 0.1 1 554 . 68 ASP HB2 H 2.500 0.02 2 555 . 69 GLY H H 8.564 0.02 1 556 . 69 GLY N N 112.1 0.1 1 557 . 69 GLY CA C 45.26 0.1 1 558 . 69 GLY HA2 H 3.862 0.02 1 559 . 69 GLY HA3 H 3.577 0.02 1 560 . 69 GLY C C 173.38 0.1 1 561 . 70 VAL H H 7.214 0.02 1 562 . 70 VAL N N 116.5 0.1 1 563 . 70 VAL CA C 62.61 0.1 1 564 . 70 VAL HA H 3.656 0.02 1 565 . 70 VAL C C 174.482 0.1 1 566 . 70 VAL CB C 31.44 0.1 1 567 . 70 VAL HB H 1.962 0.02 1 568 . 70 VAL CG1 C 22.19 0.1 1 569 . 70 VAL HG1 H 0.848 0.02 2 570 . 70 VAL CG2 C 23.29 0.1 1 571 . 70 VAL HG2 H 0.832 0.02 2 572 . 71 HIS H H 9.061 0.02 1 573 . 71 HIS N N 120.7 0.1 1 574 . 71 HIS CA C 58.91 0.1 1 575 . 71 HIS HA H 4.411 0.02 1 576 . 71 HIS C C 174.44 0.1 1 577 . 71 HIS CB C 32.73 0.1 1 578 . 71 HIS HB2 H 2.675 0.02 2 579 . 72 LEU H H 7.144 0.02 1 580 . 72 LEU N N 114.9 0.1 1 581 . 72 LEU CA C 54.42 0.1 1 582 . 72 LEU HA H 4.575 0.02 1 583 . 72 LEU C C 172.36 0.1 1 584 . 72 LEU CB C 44.92 0.1 1 585 . 72 LEU HB2 H 1.614 0.02 1 586 . 72 LEU HB3 H 1.524 0.02 1 587 . 72 LEU CG C 26.69 0.1 1 588 . 72 LEU CD1 C 24.34 0.1 1 589 . 72 LEU HD1 H 0.890 0.02 2 590 . 72 LEU CD2 C 22.89 0.1 1 591 . 72 LEU HD2 H 0.822 0.02 2 592 . 72 LEU HG H 1.366 0.02 1 593 . 73 ILE H H 8.645 0.02 1 594 . 73 ILE N N 123.6 0.1 1 595 . 73 ILE CA C 59.23 0.1 1 596 . 73 ILE HA H 4.585 0.02 1 597 . 73 ILE C C 172.829 0.1 1 598 . 73 ILE CB C 40.21 0.1 1 599 . 73 ILE HB H 1.498 0.02 1 600 . 73 ILE CG2 C 16.89 0.1 1 601 . 73 ILE HG2 H 0.468 0.02 1 602 . 73 ILE CG1 C 27.61 0.1 1 603 . 73 ILE HG12 H 1.445 0.02 1 604 . 73 ILE HG13 H 0.553 0.02 1 605 . 73 ILE CD1 C 14.44 0.1 1 606 . 73 ILE HD1 H 0.384 0.02 1 607 . 74 CYS H H 9.472 0.02 1 608 . 74 CYS N N 125.9 0.1 1 609 . 74 CYS CA C 55.07 0.1 1 610 . 74 CYS HA H 5.567 0.02 1 611 . 74 CYS C C 173.214 0.1 1 612 . 74 CYS CB C 27.64 0.1 1 613 . 74 CYS HB2 H 2.717 0.02 1 614 . 74 CYS HB3 H 2.205 0.02 1 615 . 75 THR H H 8.64 0.02 1 616 . 75 THR N N 117.5 0.1 1 617 . 75 THR CA C 58.26 0.1 1 618 . 75 THR HA H 5.504 0.02 1 619 . 75 THR C C 174.427 0.1 1 620 . 75 THR CB C 69.92 0.1 1 621 . 75 THR HB H 4.195 0.02 1 622 . 75 THR CG2 C 20.56 0.1 1 623 . 75 THR HG2 H 1.186 0.02 1 624 . 76 THR H H 8.542 0.02 1 625 . 76 THR N N 112.6 0.1 1 626 . 76 THR CA C 61.51 0.1 1 627 . 76 THR HA H 4.295 0.02 1 628 . 76 THR C C 172.277 0.1 1 629 . 76 THR CB C 67.41 0.1 1 630 . 76 THR HB H 4.543 0.02 1 631 . 76 THR CG2 C 21.01 0.1 1 632 . 76 THR HG2 H 0.964 0.02 1 633 . 77 ALA H H 7.799 0.02 1 634 . 77 ALA N N 122 0.1 1 635 . 77 ALA CA C 49.9 0.1 1 636 . 77 ALA C C 175.501 0.1 1 637 . 77 ALA CB C 21.58 0.1 1 638 . 77 ALA HB H 1.334 0.02 1 639 . 78 ARG H H 8.426 0.02 1 640 . 78 ARG N N 119.5 0.1 1 641 . 78 ARG CA C 56.57 0.1 1 642 . 78 ARG HA H 4.015 0.02 1 643 . 78 ARG C C 175.253 0.1 1 644 . 78 ARG CB C 29.28 0.1 1 645 . 78 ARG HB2 H 1.698 0.02 1 646 . 78 ARG HB3 H 1.645 0.02 1 647 . 78 ARG CG C 26.65 0.1 1 648 . 78 ARG HG2 H 1.624 0.02 1 649 . 78 ARG HG3 H 1.529 0.02 1 650 . 78 ARG CD C 42.64 0.1 1 651 . 78 ARG HD2 H 3.107 0.02 2 652 . 79 VAL H H 8.298 0.02 1 653 . 79 VAL N N 120.6 0.1 1 654 . 79 VAL CA C 60.37 0.1 1 655 . 79 VAL HA H 4.395 0.02 1 656 . 79 VAL C C 174.372 0.1 1 657 . 79 VAL CB C 34.06 0.1 1 658 . 79 VAL HB H 2.168 0.02 1 659 . 79 VAL CG1 C 21.16 0.1 1 660 . 79 VAL HG1 H 1.049 0.02 2 661 . 79 VAL CG2 C 20.5 0.1 1 662 . 79 VAL HG2 H 1.054 0.02 2 663 . 80 ASP H H 8.52 0.02 1 664 . 80 ASP N N 122.9 0.1 1 665 . 80 ASP CA C 53.4 0.1 1 666 . 80 ASP HA H 4.512 0.02 1 667 . 80 ASP C C 174.399 0.1 1 668 . 80 ASP CB C 40.47 0.1 1 669 . 80 ASP HB2 H 2.675 0.02 1 670 . 80 ASP HB3 H 2.569 0.02 1 671 . 81 ARG H H 7.098 0.02 1 672 . 81 ARG N N 114.7 0.1 1 673 . 81 ARG CA C 53.88 0.1 1 674 . 81 ARG C C 172.691 0.1 1 675 . 81 ARG CB C 30.89 0.1 1 676 . 82 SER H H 7.882 0.02 1 677 . 82 SER N N 111.2 0.1 1 678 . 82 SER CA C 56.09 0.1 1 679 . 82 SER HA H 4.427 0.02 1 680 . 82 SER C C 172.994 0.1 1 681 . 82 SER CB C 64.34 0.1 1 682 . 82 SER HB2 H 3.783 0.02 1 683 . 82 SER HB3 H 3.72 0.02 1 684 . 83 PHE H H 8.746 0.02 1 685 . 83 PHE N N 121.4 0.1 1 686 . 83 PHE CA C 56.06 0.1 1 687 . 83 PHE HA H 4.607 0.02 1 688 . 83 PHE C C 174.675 0.1 1 689 . 83 PHE CB C 38.73 0.1 1 690 . 83 PHE HB2 H 3.102 0.02 1 691 . 83 PHE HB3 H 2.606 0.02 1 692 . 83 PHE HD1 H 6.979 0.02 3 693 . 83 PHE HE1 H 6.984 0.02 3 694 . 83 PHE HZ H 6.900 0.02 1 695 . 84 GLY H H 8.241 0.02 1 696 . 84 GLY N N 107.9 0.1 1 697 . 84 GLY CA C 46.35 0.1 1 698 . 84 GLY HA2 H 3.862 0.02 1 699 . 84 GLY HA3 H 3.641 0.02 1 700 . 84 GLY C C 174.316 0.1 1 701 . 85 ASP H H 8.71 0.02 1 702 . 85 ASP N N 124.2 0.1 1 703 . 85 ASP CA C 53.3 0.1 1 704 . 85 ASP HA H 4.644 0.02 1 705 . 85 ASP C C 175.404 0.1 1 706 . 85 ASP CB C 40.1 0.1 1 707 . 85 ASP HB2 H 2.796 0.02 1 708 . 85 ASP HB3 H 2.585 0.02 1 709 . 86 ILE H H 7.746 0.02 1 710 . 86 ILE N N 122.1 0.1 1 711 . 86 ILE CA C 59.27 0.1 1 712 . 86 ILE HA H 4.147 0.02 1 713 . 86 ILE C C 176 0.1 1 714 . 86 ILE CB C 38.71 0.1 1 715 . 86 ILE HB H 1.904 0.02 1 716 . 86 ILE CG2 C 16.62 0.1 1 717 . 86 ILE HG2 H 0.748 0.02 1 718 . 86 ILE CG1 C 27.24 0.1 1 719 . 86 ILE HG12 H 1.719 0.02 1 720 . 86 ILE HG13 H 1.102 0.02 1 721 . 86 ILE CD1 C 13.53 0.1 1 722 . 86 ILE HD1 H 0.896 0.02 1 723 . 87 PRO CA C 63.16 0.1 1 724 . 87 PRO HA H 4.295 0.02 1 725 . 87 PRO C C 173.297 0.1 1 726 . 87 PRO CB C 32.12 0.1 1 727 . 87 PRO HB2 H 2.268 0.02 1 728 . 87 PRO HB3 H 1.851 0.02 1 729 . 87 PRO CD C 50.54 0.1 1 730 . 87 PRO HD2 H 4.079 0.02 1 731 . 87 PRO HD3 H 3.762 0.02 1 732 . 88 LEU H H 7.929 0.02 1 733 . 88 LEU N N 122.8 0.1 1 734 . 88 LEU CA C 52.92 0.1 1 735 . 88 LEU HA H 5.499 0.02 1 736 . 88 LEU C C 176.493 0.1 1 737 . 88 LEU CB C 44.9 0.1 1 738 . 88 LEU HB2 H 1.714 0.02 1 739 . 88 LEU HB3 H 1.524 0.02 1 740 . 88 LEU CG C 27.28 0.1 1 741 . 88 LEU CD1 C 25.53 0.1 1 742 . 88 LEU HD1 H 0.954 0.02 2 743 . 88 LEU CD2 C 24.93 0.1 1 744 . 88 LEU HD2 H 0.848 0.02 2 745 . 88 LEU HG H 1.439 0.02 1 746 . 89 VAL H H 9.066 0.02 1 747 . 89 VAL N N 117.2 0.1 1 748 . 89 VAL CA C 57.84 0.1 1 749 . 89 VAL HA H 4.659 0.02 1 750 . 89 VAL C C 173.242 0.1 1 751 . 89 VAL CB C 34.12 0.1 1 752 . 89 VAL HB H 2.025 0.02 1 753 . 89 VAL CG1 C 18.43 0.1 1 754 . 89 VAL HG1 H 0.774 0.02 2 755 . 89 VAL CG2 C 20.88 0.1 1 756 . 89 VAL HG2 H 0.754 0.02 2 757 . 90 HIS H H 8.612 0.02 1 758 . 90 HIS N N 121.7 0.1 1 759 . 90 HIS CA C 54.63 0.1 1 760 . 90 HIS HA H 5.14 0.02 1 761 . 90 HIS C C 176.052 0.1 1 762 . 90 HIS CB C 30.67 0.1 1 763 . 90 HIS HB2 H 3.218 0.02 1 764 . 90 HIS HB3 H 3.007 0.02 1 765 . 91 GLY H H 8.943 0.02 1 766 . 91 GLY N N 107.9 0.1 1 767 . 91 GLY CA C 44.83 0.1 1 768 . 91 GLY HA2 H 4.026 0.02 1 769 . 91 GLY HA3 H 3.208 0.02 1 770 . 91 GLY C C 173.269 0.1 1 771 . 92 MET H H 7.83 0.02 1 772 . 92 MET N N 119.1 0.1 1 773 . 92 MET CA C 59.272 0.1 1 774 . 92 MET C C 177.5 0.1 1 775 . 92 MET CB C 28.176 0.1 1 776 . 93 PRO CA C 65.52 0.1 1 777 . 93 PRO HA H 4.395 0.02 1 778 . 93 PRO C C 177.017 0.1 1 779 . 93 PRO CB C 30.32 0.1 1 780 . 93 PRO HB2 H 1.999 0.02 2 781 . 93 PRO CG C 27.7 0.1 1 782 . 93 PRO HG2 H 1.841 0.02 2 783 . 93 PRO CD C 50.1 0.1 1 784 . 93 PRO HD2 H 3.583 0.02 1 785 . 93 PRO HD3 H 3.229 0.02 1 786 . 94 PHE H H 7.334 0.02 1 787 . 94 PHE N N 108.8 0.1 1 788 . 94 PHE CA C 58.43 0.1 1 789 . 94 PHE HA H 4.406 0.02 1 790 . 94 PHE C C 175.474 0.1 1 791 . 94 PHE CB C 37.5 0.1 1 792 . 94 PHE HD1 H 7.130 0.02 3 793 . 94 PHE HE1 H 7.073 0.02 3 794 . 94 PHE HZ H 6.725 0.02 1 795 . 95 VAL H H 7.857 0.02 1 796 . 95 VAL N N 115.2 0.1 1 797 . 95 VAL CA C 63.14 0.1 1 798 . 95 VAL HA H 4.047 0.02 1 799 . 95 VAL C C 176.879 0.1 1 800 . 95 VAL CB C 32.28 0.1 1 801 . 95 VAL HB H 2.342 0.02 1 802 . 95 VAL CG1 C 20.52 0.1 1 803 . 95 VAL HG1 H 0.959 0.02 1 804 . 95 VAL CG2 C 20.52 0.1 1 805 . 95 VAL HG2 H 0.96 0.02 1 806 . 96 SER H H 8.385 0.02 1 807 . 96 SER N N 112.7 0.1 1 808 . 96 SER CA C 58.47 0.1 1 809 . 96 SER HA H 4.332 0.02 1 810 . 96 SER C C 175.694 0.1 1 811 . 96 SER CB C 63.84 0.1 1 812 . 96 SER HB2 H 3.978 0.02 1 813 . 96 SER HB3 H 3.81 0.02 1 814 . 97 GLY H H 8.216 0.02 1 815 . 97 GLY N N 109.5 0.1 1 816 . 97 GLY CA C 45.19 0.1 1 817 . 97 GLY HA2 H 4.227 0.02 1 818 . 97 GLY HA3 H 3.672 0.02 1 819 . 97 GLY C C 173.242 0.1 1 820 . 98 VAL H H 7.923 0.02 1 821 . 98 VAL N N 120.9 0.1 1 822 . 98 VAL CA C 62.08 0.1 1 823 . 98 VAL HA H 4.053 0.02 1 824 . 98 VAL C C 175.914 0.1 1 825 . 98 VAL CB C 31.54 0.1 1 826 . 98 VAL HB H 2.046 0.02 1 827 . 98 VAL CG1 C 19.97 0.1 1 828 . 98 VAL HG1 H 0.891 0.02 2 829 . 98 VAL CG2 C 20.48 0.1 1 830 . 98 VAL HG2 H 0.912 0.02 2 831 . 99 GLY H H 9.006 0.02 1 832 . 99 GLY N N 113.9 0.1 1 833 . 99 GLY CA C 44.83 0.1 1 834 . 99 GLY HA2 H 3.915 0.02 2 835 . 99 GLY C C 175.859 0.1 1 836 . 100 ILE H H 7.517 0.02 1 837 . 100 ILE N N 118.4 0.1 1 838 . 100 ILE CA C 63.83 0.1 1 839 . 100 ILE HA H 3.366 0.02 1 840 . 100 ILE C C 175.419 0.1 1 841 . 100 ILE CB C 37.22 0.1 1 842 . 100 ILE HB H 1.587 0.02 1 843 . 100 ILE CG2 C 16.45 0.1 1 844 . 100 ILE HG2 H 0.864 0.02 1 845 . 100 ILE CG1 C 29.31 0.1 1 846 . 100 ILE HG12 H 1.16 0.02 1 847 . 100 ILE HG13 H 0.854 0.02 1 848 . 100 ILE CD1 C 13.53 0.1 1 849 . 100 ILE HD1 H 0.896 0.02 1 850 . 101 GLU H H 8.716 0.02 1 851 . 101 GLU N N 121.1 0.1 1 852 . 101 GLU CA C 59.57 0.1 1 853 . 101 GLU HA H 4.073 0.02 1 854 . 101 GLU C C 178.27 0.1 1 855 . 101 GLU CB C 27.68 0.1 1 856 . 101 GLU HB2 H 1.988 0.02 2 857 . 101 GLU CG C 36.13 0.1 1 858 . 101 GLU HG2 H 2.279 0.02 2 859 . 102 ALA H H 7.952 0.02 1 860 . 102 ALA N N 118.9 0.1 1 861 . 102 ALA CA C 54.02 0.1 1 862 . 102 ALA HA H 4.116 0.02 1 863 . 102 ALA C C 180.089 0.1 1 864 . 102 ALA CB C 17.29 0.1 1 865 . 102 ALA HB H 1.366 0.02 1 866 . 103 LEU H H 7.277 0.02 1 867 . 103 LEU N N 118.7 0.1 1 868 . 103 LEU CA C 57.01 0.1 1 869 . 103 LEU HA H 4.174 0.02 1 870 . 103 LEU C C 177.761 0.1 1 871 . 103 LEU CB C 40.23 0.1 1 872 . 103 LEU HB2 H 1.635 0.02 1 873 . 103 LEU HB3 H 1.318 0.02 1 874 . 103 LEU CG C 26.45 0.1 1 875 . 103 LEU CD1 C 25.84 0.1 1 876 . 103 LEU HD1 H 0.078 0.02 2 877 . 103 LEU CD2 C 21.83 0.1 1 878 . 103 LEU HD2 H 0.838 0.02 2 879 . 103 LEU HG H 1.139 0.02 1 880 . 104 GLN H H 8.662 0.02 1 881 . 104 GLN N N 116.2 0.1 1 882 . 104 GLN CA C 59.15 0.1 1 883 . 104 GLN HA H 3.678 0.02 1 884 . 104 GLN C C 177.127 0.1 1 885 . 104 GLN CB C 27.42 0.1 1 886 . 104 GLN HB2 H 2.469 0.02 1 887 . 104 GLN HB3 H 1.82 0.02 1 888 . 104 GLN CG C 34.11 0.1 1 889 . 104 GLN HG2 H 2.77 0.02 1 890 . 104 GLN HG3 H 2.136 0.02 1 891 . 105 ASN H H 7.974 0.02 1 892 . 105 ASN N N 113.5 0.1 1 893 . 105 ASN CA C 55.75 0.1 1 894 . 105 ASN HA H 4.343 0.02 1 895 . 105 ASN C C 177.237 0.1 1 896 . 105 ASN CB C 37.67 0.1 1 897 . 105 ASN HB2 H 2.785 0.02 1 898 . 105 ASN HB3 H 2.759 0.02 1 899 . 106 LYS H H 7.995 0.02 1 900 . 106 LYS N N 121.2 0.1 1 901 . 106 LYS CA C 58.94 0.1 1 902 . 106 LYS HA H 4.042 0.02 1 903 . 106 LYS C C 177.953 0.1 1 904 . 106 LYS CB C 31.75 0.1 1 905 . 106 LYS HB2 H 1.999 0.02 2 906 . 106 LYS CG C 24.07 0.1 1 907 . 106 LYS HG2 H 1.476 0.02 1 908 . 106 LYS HG3 H 1.387 0.02 1 909 . 106 LYS CD C 28.65 0.1 1 910 . 106 LYS HD2 H 1.693 0.02 2 911 . 106 LYS CE C 41.35 0.1 1 912 . 106 LYS HE2 H 2.912 0.02 2 913 . 107 ILE H H 8.332 0.02 1 914 . 107 ILE N N 116.5 0.1 1 915 . 107 ILE CA C 65.82 0.1 1 916 . 107 ILE HA H 3.387 0.02 1 917 . 107 ILE C C 176.686 0.1 1 918 . 107 ILE CB C 37.18 0.1 1 919 . 107 ILE HB H 1.846 0.02 1 920 . 107 ILE CG2 C 16.22 0.1 1 921 . 107 ILE HG2 H 0.653 0.02 1 922 . 107 ILE CG1 C 29.14 0.1 1 923 . 107 ILE HG12 H 1.893 0.02 1 924 . 107 ILE CD1 C 13.32 0.1 1 925 . 107 ILE HD1 H 0.843 0.02 1 926 . 108 LEU H H 8.186 0.02 1 927 . 108 LEU N N 116.7 0.1 1 928 . 108 LEU CA C 57.88 0.1 1 929 . 108 LEU HA H 3.693 0.02 1 930 . 108 LEU C C 178.119 0.1 1 931 . 108 LEU CB C 40.59 0.1 1 932 . 108 LEU HB2 H 1.73 0.02 1 933 . 108 LEU HB3 H 1.297 0.02 1 934 . 108 LEU CG C 25.67 0.1 1 935 . 108 LEU CD1 C 23.86 0.1 1 936 . 108 LEU HD1 H 0.315 0.02 2 937 . 108 LEU CD2 C 21.66 0.1 1 938 . 108 LEU HD2 H 0.273 0.02 2 939 . 108 LEU HG H 1.529 0.02 1 940 . 109 THR H H 7.948 0.02 1 941 . 109 THR N N 112.7 0.1 1 942 . 109 THR CA C 66.01 0.1 1 943 . 109 THR HA H 3.899 0.02 1 944 . 109 THR C C 176.658 0.1 1 945 . 109 THR CB C 68.25 0.1 1 946 . 109 THR HB H 4.285 0.02 1 947 . 109 THR CG2 C 20.84 0.1 1 948 . 109 THR HG2 H 1.218 0.02 1 949 . 110 ILE H H 7.839 0.02 1 950 . 110 ILE N N 120.6 0.1 1 951 . 110 ILE CA C 64.34 0.1 1 952 . 110 ILE HA H 3.72 0.02 1 953 . 110 ILE C C 178.036 0.1 1 954 . 110 ILE CB C 37.95 0.1 1 955 . 110 ILE HB H 1.846 0.02 1 956 . 110 ILE CG2 C 17.33 0.1 1 957 . 110 ILE HG2 H 0.954 0.02 1 958 . 110 ILE CG1 C 28.69 0.1 1 959 . 110 ILE HG12 H 1.798 0.02 1 960 . 110 ILE HG13 H 1.086 0.02 1 961 . 110 ILE CD1 C 13.87 0.1 1 962 . 110 ILE HD1 H 0.727 0.02 1 963 . 111 LEU H H 8.193 0.02 1 964 . 111 LEU N N 114.5 0.1 1 965 . 111 LEU CA C 55.9 0.1 1 966 . 111 LEU HA H 4.052 0.02 1 967 . 111 LEU C C 177.099 0.1 1 968 . 111 LEU CB C 41.85 0.1 1 969 . 111 LEU HB2 H 1.756 0.02 1 970 . 111 LEU HB3 H 1.265 0.02 1 971 . 111 LEU CG C 25.23 0.1 1 972 . 111 LEU CD1 C 27.02 0.1 1 973 . 111 LEU HD1 H 0.611 0.02 1 974 . 111 LEU CD2 C 20.75 0.1 1 975 . 111 LEU HD2 H 0.611 0.02 1 976 . 111 LEU HG H 1.962 0.02 1 977 . 112 GLN H H 8.038 0.02 1 978 . 112 GLN N N 115.1 0.1 1 979 . 112 GLN CA C 56.27 0.1 1 980 . 112 GLN HA H 4.285 0.02 1 981 . 112 GLN C C 175.171 0.1 1 982 . 112 GLN CB C 28.52 0.1 1 983 . 112 GLN HB2 H 2.089 0.02 2 984 . 112 GLN CG C 34.06 0.1 1 985 . 112 GLN HG2 H 2.427 0.02 1 986 . 112 GLN HG3 H 2.273 0.02 1 987 . 113 GLY H H 7.525 0.02 1 988 . 113 GLY N N 112.2 0.1 1 989 . 113 GLY CA C 45.82 0.1 1 990 . 113 GLY HA2 H 3.81 0.02 1 991 . 113 GLY HA3 H 3.709 0.02 1 stop_ save_