data_4778 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1HN, 15N and 13C shifts for GMPPNP-loaded Cdc42 from Candida albicans ; _BMRB_accession_number 4778 _BMRB_flat_file_name bmr4778.str _Entry_type original _Submission_date 2000-07-07 _Accession_date 2000-07-07 _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 Osborne Michael J . 2 Stevens Willem K . 3 Ping Xu . . 4 Ni Feng . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 140 "13C chemical shifts" 253 "15N chemical shifts" 140 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-13 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4770 'GDP-loaded Cdc42' stop_ _Original_release_date 2004-02-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Efficient expression of isotopically labeled peptides for high resolution NMR studies: application to the Cdc42/Rac binding domains of virulent kinases in Candida albicans ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12815258 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Osborne Michael J . 2 Su Z. . . 3 Sridaran V. . . 4 Ni Feng . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 26 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 317 _Page_last 326 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_Cdc42 _Saveframe_category molecular_system _Mol_system_name 'Cell Division Control Protein 42 from Candida albicans' _Abbreviation_common Cdc42 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Cdc42 $Cdc42 GNP $GNP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'involved in hyphal transformation' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Cdc42 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cell division control protein 42' _Abbreviation_common Cdc42 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 181 _Mol_residue_sequence ; GSHMQTIKCVVVGDGAVGKT CLLISYTTSKFPADYVPTVF DNYAVTVMIGDEPFTLGLFD TAGQEDYDRLRPLSYPSTDV FLVCFSVISPASFENVKEKW FPEVHHHCPGVPIIIVGTQT DLRNDDVILQRLHRQKLSPI TQEQGEKLAKELRAVKYVEC SALTQRGLKTVFDEAIVAAL E ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -3 GLY 2 -2 SER 3 -1 HIS 4 1 MET 5 2 GLN 6 3 THR 7 4 ILE 8 5 LYS 9 6 CYS 10 7 VAL 11 8 VAL 12 9 VAL 13 10 GLY 14 11 ASP 15 12 GLY 16 13 ALA 17 14 VAL 18 15 GLY 19 16 LYS 20 17 THR 21 18 CYS 22 19 LEU 23 20 LEU 24 21 ILE 25 22 SER 26 23 TYR 27 24 THR 28 25 THR 29 26 SER 30 27 LYS 31 28 PHE 32 29 PRO 33 30 ALA 34 31 ASP 35 32 TYR 36 33 VAL 37 34 PRO 38 35 THR 39 36 VAL 40 37 PHE 41 38 ASP 42 39 ASN 43 40 TYR 44 41 ALA 45 42 VAL 46 43 THR 47 44 VAL 48 45 MET 49 46 ILE 50 47 GLY 51 48 ASP 52 49 GLU 53 50 PRO 54 51 PHE 55 52 THR 56 53 LEU 57 54 GLY 58 55 LEU 59 56 PHE 60 57 ASP 61 58 THR 62 59 ALA 63 60 GLY 64 61 GLN 65 62 GLU 66 63 ASP 67 64 TYR 68 65 ASP 69 66 ARG 70 67 LEU 71 68 ARG 72 69 PRO 73 70 LEU 74 71 SER 75 72 TYR 76 73 PRO 77 74 SER 78 75 THR 79 76 ASP 80 77 VAL 81 78 PHE 82 79 LEU 83 80 VAL 84 81 CYS 85 82 PHE 86 83 SER 87 84 VAL 88 85 ILE 89 86 SER 90 87 PRO 91 88 ALA 92 89 SER 93 90 PHE 94 91 GLU 95 92 ASN 96 93 VAL 97 94 LYS 98 95 GLU 99 96 LYS 100 97 TRP 101 98 PHE 102 99 PRO 103 100 GLU 104 101 VAL 105 102 HIS 106 103 HIS 107 104 HIS 108 105 CYS 109 106 PRO 110 107 GLY 111 108 VAL 112 109 PRO 113 110 ILE 114 111 ILE 115 112 ILE 116 113 VAL 117 114 GLY 118 115 THR 119 116 GLN 120 117 THR 121 118 ASP 122 119 LEU 123 120 ARG 124 121 ASN 125 122 ASP 126 123 ASP 127 124 VAL 128 125 ILE 129 126 LEU 130 127 GLN 131 128 ARG 132 129 LEU 133 130 HIS 134 131 ARG 135 132 GLN 136 133 LYS 137 134 LEU 138 135 SER 139 136 PRO 140 137 ILE 141 138 THR 142 139 GLN 143 140 GLU 144 141 GLN 145 142 GLY 146 143 GLU 147 144 LYS 148 145 LEU 149 146 ALA 150 147 LYS 151 148 GLU 152 149 LEU 153 150 ARG 154 151 ALA 155 152 VAL 156 153 LYS 157 154 TYR 158 155 VAL 159 156 GLU 160 157 CYS 161 158 SER 162 159 ALA 163 160 LEU 164 161 THR 165 162 GLN 166 163 ARG 167 164 GLY 168 165 LEU 169 166 LYS 170 167 THR 171 168 VAL 172 169 PHE 173 170 ASP 174 171 GLU 175 172 ALA 176 173 ILE 177 174 VAL 178 175 ALA 179 176 ALA 180 177 LEU 181 178 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-09-14 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4770 Cdc42 100.00 181 100.00 100.00 3.23e-130 EMBL CAX45095 "Cell division control protein CDC42 homologue, putative [Candida dubliniensis CD36]" 98.34 191 100.00 100.00 2.16e-127 EMBL CCE43086 "hypothetical protein CPAR2_207290 [Candida parapsilosis]" 98.34 191 97.19 98.31 2.67e-123 EMBL CCG21049 "Cdc42 Rho-type GTPase [Candida orthopsilosis Co 90-125]" 98.34 191 97.19 98.31 2.67e-123 GB AAB69764 "cell division control protein 42 homolog [Candida albicans]" 98.34 191 100.00 100.00 2.16e-127 GB EAK92670 "likely rho family Ras-like GTPase [Candida albicans SC5314]" 98.34 191 100.00 100.00 2.16e-127 GB EAK92699 "likely rho family Ras-like GTPase [Candida albicans SC5314]" 98.34 191 100.00 100.00 2.16e-127 GB EDK42478 "cell division control protein 42 [Lodderomyces elongisporus NRRL YB-4239]" 98.34 191 97.19 98.31 8.76e-124 GB EEQ42372 "cell division control protein 42 [Candida albicans WO-1]" 98.34 191 100.00 100.00 2.16e-127 REF XP_001528136 "cell division control protein 42 [Lodderomyces elongisporus NRRL YB-4239]" 98.34 191 97.19 98.31 8.76e-124 REF XP_002417442 "Cell division control protein CDC42 homologue, putative; cell polarity effector, putative; rho family Ras-like GTPase, putative" 98.34 191 100.00 100.00 2.16e-127 REF XP_002548861 "cell division control protein 42 [Candida tropicalis MYA-3404]" 98.34 191 98.88 100.00 3.59e-126 REF XP_003866489 "Cdc42 Rho-type GTPase [Candida orthopsilosis Co 90-125]" 98.34 191 97.19 98.31 2.67e-123 REF XP_007376934 "cell division control protein 42 [Spathaspora passalidarum NRRL Y-27907]" 98.34 191 97.75 98.31 2.14e-124 SP C4YDI6 "RecName: Full=Cell division control protein 42 homolog; Flags: Precursor [Candida albicans WO-1]" 98.34 191 100.00 100.00 2.16e-127 SP P0CY33 "RecName: Full=Cell division control protein 42 homolog; Flags: Precursor [Candida albicans SC5314]" 98.34 191 100.00 100.00 2.16e-127 stop_ save_ ############# # Ligands # ############# save_GNP _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "5p-guanosyl-imido-triphosphate (PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER)" _Abbreviation_common GMPPNP _BMRB_code GNP _PDB_code GNP _Molecular_mass 522.196 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1' C1' C . 0 . ? C2 C2 C . 0 . ? C2' C2' C . 0 . ? C3' C3' C . 0 . ? C4 C4 C . 0 . ? C4' C4' C . 0 . ? C5 C5 C . 0 . ? C5' C5' C . 0 . ? C6 C6 C . 0 . ? C8 C8 C . 0 . ? H1' H1' H . 0 . ? H2' H2' H . 0 . ? H3' H3' H . 0 . ? H4' H4' H . 0 . ? H5'1 H5'1 H . 0 . ? H5'2 H5'2 H . 0 . ? H8 H8 H . 0 . ? HN1 HN1 H . 0 . ? HN21 HN21 H . 0 . ? HN22 HN22 H . 0 . ? HNB3 HNB3 H . 0 . ? HO2' HO2' H . 0 . ? HO3' HO3' H . 0 . ? HOA2 HOA2 H . 0 . ? HOB2 HOB2 H . 0 . ? HOG2 HOG2 H . 0 . ? HOG3 HOG3 H . 0 . ? N1 N1 N . 0 . ? N2 N2 N . 0 . ? N3 N3 N . 0 . ? N3B N3B N . 0 . ? N7 N7 N . 0 . ? N9 N9 N . 0 . ? O1A O1A O . 0 . ? O1B O1B O . 0 . ? O1G O1G O . 0 . ? O2' O2' O . 0 . ? O2A O2A O . 0 . ? O2B O2B O . 0 . ? O2G O2G O . 0 . ? O3' O3' O . 0 . ? O3A O3A O . 0 . ? O3G O3G O . 0 . ? O4' O4' O . 0 . ? O5' O5' O . 0 . ? O6 O6 O . 0 . ? PA PA P . 0 . ? PB PB P . 0 . ? PG PG P . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name DOUB PG O1G ? ? SING PG O2G ? ? SING PG O3G ? ? SING PG N3B ? ? SING O2G HOG2 ? ? SING O3G HOG3 ? ? SING N3B PB ? ? SING N3B HNB3 ? ? DOUB PB O1B ? ? SING PB O2B ? ? SING PB O3A ? ? SING O2B HOB2 ? ? SING O3A PA ? ? DOUB PA O1A ? ? SING PA O2A ? ? SING PA O5' ? ? SING O2A HOA2 ? ? SING O5' C5' ? ? SING C5' C4' ? ? SING C5' H5'2 ? ? SING C5' H5'1 ? ? SING C4' O4' ? ? SING C4' C3' ? ? SING C4' H4' ? ? SING O4' C1' ? ? SING C3' O3' ? ? SING C3' C2' ? ? SING C3' H3' ? ? SING O3' HO3' ? ? SING C2' O2' ? ? SING C2' C1' ? ? SING C2' H2' ? ? SING O2' HO2' ? ? SING C1' N9 ? ? SING C1' H1' ? ? SING N9 C8 ? ? SING N9 C4 ? ? DOUB C8 N7 ? ? SING C8 H8 ? ? SING N7 C5 ? ? SING C5 C6 ? ? DOUB C5 C4 ? ? DOUB C6 O6 ? ? SING C6 N1 ? ? SING N1 C2 ? ? SING N1 HN1 ? ? SING C2 N2 ? ? DOUB C2 N3 ? ? SING N2 HN21 ? ? SING N2 HN22 ? ? SING N3 C4 ? ? 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 $Cdc42 Yeast 5476 Eukaryota Fungi Candida albicans 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 $Cdc42 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) . 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 $Cdc42 0.7 mM '[U-15N; U-13C]' $GNP 7 mM . 'sodium phosphate' 50 mM . 'magnesium chloride' 2 mM . 'sodium chloride' 50 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _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_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.8 0.2 n/a temperature 298 0.2 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 . . . . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Cdc42 _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 . 4 MET CA C 55.22 0.20 1 2 . 5 GLN CA C 56.15 0.20 1 3 . 5 GLN CB C 28.86 0.20 1 4 . 5 GLN H H 8.48 0.04 1 5 . 5 GLN N N 126.73 0.15 1 6 . 6 THR CA C 61.26 0.20 1 7 . 6 THR CB C 70.52 0.20 1 8 . 6 THR H H 8.18 0.04 1 9 . 6 THR N N 121.34 0.15 1 10 . 7 ILE CA C 59.61 0.20 1 11 . 7 ILE CB C 40.23 0.20 1 12 . 7 ILE H H 8.99 0.04 1 13 . 7 ILE N N 131.61 0.15 1 14 . 8 LYS CA C 55.94 0.20 1 15 . 8 LYS H H 10.57 0.04 1 16 . 8 LYS N N 136.05 0.15 1 17 . 9 CYS CA C 55.76 0.20 1 18 . 9 CYS CB C 28.61 0.20 1 19 . 9 CYS H H 9.39 0.04 1 20 . 9 CYS N N 135.77 0.15 1 21 . 10 VAL CA C 60.44 0.20 1 22 . 10 VAL H H 7.47 0.04 1 23 . 10 VAL N N 133.56 0.15 1 24 . 11 VAL CA C 60.88 0.20 1 25 . 11 VAL H H 8.29 0.04 1 26 . 11 VAL N N 131.35 0.15 1 27 . 12 VAL CA C 58.09 0.20 1 28 . 12 VAL H H 8.83 0.04 1 29 . 12 VAL N N 121.71 0.15 1 30 . 13 GLY CA C 43.03 0.20 1 31 . 13 GLY H H 6.62 0.04 1 32 . 13 GLY N N 111.92 0.15 1 33 . 14 ASP CA C 55.73 0.20 1 34 . 14 ASP CB C 40.69 0.20 1 35 . 14 ASP H H 8.26 0.04 1 36 . 14 ASP N N 123.12 0.15 1 37 . 15 GLY CA C 46.54 0.20 1 38 . 15 GLY H H 8.62 0.04 1 39 . 15 GLY N N 109.92 0.15 1 40 . 16 ALA CA C 53.10 0.20 1 41 . 16 ALA H H 9.40 0.04 1 42 . 16 ALA N N 127.82 0.15 1 43 . 17 VAL CA C 61.86 0.20 1 44 . 18 GLY CA C 44.79 0.20 1 45 . 18 GLY H H 8.38 0.04 1 46 . 18 GLY N N 113.33 0.15 1 47 . 19 LYS CA C 60.54 0.20 1 48 . 19 LYS H H 9.48 0.04 1 49 . 19 LYS N N 130.60 0.15 1 50 . 20 THR CA C 66.82 0.20 1 51 . 20 THR H H 9.21 0.04 1 52 . 20 THR N N 123.55 0.15 1 53 . 21 CYS CA C 65.49 0.20 1 54 . 21 CYS H H 9.26 0.04 1 55 . 21 CYS N N 123.68 0.15 1 56 . 22 LEU CA C 59.28 0.20 1 57 . 22 LEU CB C 41.02 0.20 1 58 . 22 LEU H H 8.15 0.04 1 59 . 22 LEU N N 126.82 0.15 1 60 . 23 LEU CA C 57.56 0.20 1 61 . 23 LEU H H 7.40 0.04 1 62 . 23 LEU N N 122.83 0.15 1 63 . 24 ILE CA C 65.56 0.20 1 64 . 24 ILE H H 8.73 0.04 1 65 . 24 ILE N N 126.05 0.15 1 66 . 25 SER CA C 61.38 0.20 1 67 . 25 SER H H 8.81 0.04 1 68 . 25 SER N N 123.71 0.15 1 69 . 26 TYR CA C 60.47 0.20 1 70 . 26 TYR CB C 39.81 0.20 1 71 . 26 TYR H H 7.95 0.04 1 72 . 26 TYR N N 122.60 0.15 1 73 . 27 THR CA C 60.50 0.20 1 74 . 27 THR CB C 68.93 0.20 1 75 . 27 THR H H 7.83 0.04 1 76 . 27 THR N N 111.86 0.15 1 77 . 28 THR CA C 62.03 0.20 1 78 . 28 THR CB C 72.02 0.20 1 79 . 28 THR H H 8.12 0.04 1 80 . 28 THR N N 114.81 0.15 1 81 . 29 SER CA C 60.51 0.20 1 82 . 29 SER CB C 62.31 0.20 1 83 . 29 SER H H 7.43 0.04 1 84 . 29 SER N N 118.97 0.15 1 85 . 30 LYS CA C 54.55 0.20 1 86 . 30 LYS CB C 34.41 0.20 1 87 . 30 LYS H H 7.79 0.04 1 88 . 30 LYS N N 125.28 0.15 1 89 . 31 PHE CA C 55.25 0.20 1 90 . 31 PHE H H 8.48 0.04 1 91 . 31 PHE N N 130.49 0.15 1 92 . 32 PRO CA C 61.93 0.20 1 93 . 33 ALA CA C 52.66 0.20 1 94 . 33 ALA CB C 19.36 0.20 1 95 . 33 ALA H H 7.90 0.04 1 96 . 33 ALA N N 130.56 0.15 1 97 . 34 ASP CA C 54.55 0.20 1 98 . 34 ASP CB C 41.13 0.20 1 99 . 34 ASP H H 8.13 0.04 1 100 . 34 ASP N N 120.54 0.15 1 101 . 35 TYR CA C 57.84 0.20 1 102 . 35 TYR H H 7.81 0.04 1 103 . 35 TYR N N 124.62 0.15 1 104 . 39 VAL H H 5.71 0.04 1 105 . 39 VAL N N 109.67 0.15 1 106 . 44 ALA CA C 50.68 0.20 1 107 . 45 VAL CA C 59.41 0.20 1 108 . 45 VAL CB C 35.08 0.20 1 109 . 45 VAL H H 8.72 0.04 1 110 . 45 VAL N N 123.14 0.15 1 111 . 46 THR CA C 62.32 0.20 1 112 . 46 THR H H 8.59 0.04 1 113 . 46 THR N N 126.12 0.15 1 114 . 47 VAL CA C 60.14 0.20 1 115 . 47 VAL CB C 34.38 0.20 1 116 . 47 VAL H H 9.37 0.04 1 117 . 47 VAL N N 131.62 0.15 1 118 . 48 MET CA C 53.03 0.20 1 119 . 48 MET CB C 30.98 0.20 1 120 . 48 MET H H 8.45 0.04 1 121 . 48 MET N N 127.15 0.15 1 122 . 49 ILE CA C 59.78 0.20 1 123 . 49 ILE CB C 36.06 0.20 1 124 . 49 ILE H H 8.88 0.04 1 125 . 49 ILE N N 131.11 0.15 1 126 . 50 GLY CA C 47.10 0.20 1 127 . 50 GLY H H 8.95 0.04 1 128 . 50 GLY N N 123.90 0.15 1 129 . 51 ASP CA C 54.14 0.20 1 130 . 51 ASP CB C 40.53 0.20 1 131 . 51 ASP H H 8.71 0.04 1 132 . 51 ASP N N 127.37 0.15 1 133 . 52 GLU CA C 52.86 0.20 1 134 . 52 GLU H H 7.90 0.04 1 135 . 52 GLU N N 126.19 0.15 1 136 . 53 PRO CA C 61.86 0.20 1 137 . 53 PRO CB C 31.98 0.20 1 138 . 54 PHE CA C 56.72 0.20 1 139 . 54 PHE CB C 42.39 0.20 1 140 . 54 PHE H H 9.23 0.04 1 141 . 54 PHE N N 126.60 0.15 1 142 . 55 THR CA C 62.30 0.20 1 143 . 55 THR CB C 69.35 0.20 1 144 . 55 THR H H 8.80 0.04 1 145 . 55 THR N N 122.32 0.15 1 146 . 56 LEU CA C 53.36 0.20 1 147 . 56 LEU H H 9.46 0.04 1 148 . 56 LEU N N 135.82 0.15 1 149 . 57 GLY CA C 44.93 0.20 1 150 . 57 GLY H H 9.68 0.04 1 151 . 57 GLY N N 120.65 0.15 1 152 . 58 LEU CA C 53.59 0.20 1 153 . 58 LEU H H 8.65 0.04 1 154 . 58 LEU N N 130.21 0.15 1 155 . 64 GLN CA C 60.21 0.20 1 156 . 65 GLU CA C 58.12 0.20 1 157 . 65 GLU H H 9.08 0.04 1 158 . 65 GLU N N 126.97 0.15 1 159 . 66 ASP CA C 55.63 0.20 1 160 . 66 ASP CB C 39.31 0.20 1 161 . 66 ASP H H 8.58 0.04 1 162 . 66 ASP N N 122.59 0.15 1 163 . 67 TYR CA C 57.92 0.20 1 164 . 67 TYR H H 7.89 0.04 1 165 . 67 TYR N N 121.39 0.15 1 166 . 72 PRO CA C 63.40 0.20 1 167 . 72 PRO CB C 29.61 0.20 1 168 . 73 LEU CA C 56.90 0.20 1 169 . 73 LEU CB C 40.16 0.20 1 170 . 73 LEU H H 7.46 0.04 1 171 . 73 LEU N N 123.33 0.15 1 172 . 74 SER CA C 60.33 0.20 1 173 . 74 SER CB C 63.69 0.20 1 174 . 74 SER H H 7.94 0.04 1 175 . 74 SER N N 117.11 0.15 1 176 . 75 TYR CA C 55.89 0.20 1 177 . 75 TYR H H 7.22 0.04 1 178 . 75 TYR N N 124.87 0.15 1 179 . 76 PRO CA C 65.91 0.20 1 180 . 77 SER CA C 58.98 0.20 1 181 . 77 SER CB C 60.79 0.20 1 182 . 77 SER H H 9.03 0.04 1 183 . 77 SER N N 118.47 0.15 1 184 . 78 THR CA C 66.57 0.20 1 185 . 78 THR CB C 67.76 0.20 1 186 . 78 THR H H 7.39 0.04 1 187 . 78 THR N N 122.52 0.15 1 188 . 79 ASP CA C 55.85 0.20 1 189 . 79 ASP CB C 43.92 0.20 1 190 . 79 ASP H H 8.75 0.04 1 191 . 79 ASP N N 127.70 0.15 1 192 . 80 VAL CA C 60.39 0.20 1 193 . 80 VAL CB C 31.70 0.20 1 194 . 80 VAL H H 7.49 0.04 1 195 . 80 VAL N N 120.94 0.15 1 196 . 81 PHE CA C 56.61 0.20 1 197 . 81 PHE CB C 42.91 0.20 1 198 . 81 PHE H H 8.38 0.04 1 199 . 81 PHE N N 127.87 0.15 1 200 . 82 LEU CA C 52.79 0.20 1 201 . 82 LEU CB C 40.88 0.20 1 202 . 82 LEU H H 8.78 0.04 1 203 . 82 LEU N N 124.07 0.15 1 204 . 83 VAL CA C 60.65 0.20 1 205 . 83 VAL CB C 31.33 0.20 1 206 . 83 VAL H H 8.75 0.04 1 207 . 83 VAL N N 128.59 0.15 1 208 . 84 CYS CA C 57.13 0.20 1 209 . 84 CYS CB C 30.13 0.20 1 210 . 84 CYS H H 8.95 0.04 1 211 . 84 CYS N N 128.87 0.15 1 212 . 85 PHE CA C 56.43 0.20 1 213 . 85 PHE H H 8.97 0.04 1 214 . 85 PHE N N 122.98 0.15 1 215 . 86 SER CA C 55.09 0.20 1 216 . 86 SER H H 8.09 0.04 1 217 . 86 SER N N 117.90 0.15 1 218 . 87 VAL CA C 63.68 0.20 1 219 . 87 VAL H H 8.70 0.04 1 220 . 87 VAL N N 125.69 0.15 1 221 . 88 ILE CA C 58.92 0.20 1 222 . 88 ILE CB C 36.33 0.20 1 223 . 88 ILE H H 7.44 0.04 1 224 . 88 ILE N N 112.03 0.15 1 225 . 89 SER CA C 53.04 0.20 1 226 . 89 SER H H 7.99 0.04 1 227 . 89 SER N N 116.27 0.15 1 228 . 90 PRO CA C 65.22 0.20 1 229 . 90 PRO CB C 31.20 0.20 1 230 . 91 ALA CA C 55.26 0.20 1 231 . 91 ALA CB C 17.70 0.20 1 232 . 91 ALA H H 8.99 0.04 1 233 . 91 ALA N N 125.09 0.15 1 234 . 92 SER CA C 61.16 0.20 1 235 . 92 SER CB C 63.91 0.20 1 236 . 92 SER H H 8.13 0.04 1 237 . 92 SER N N 120.54 0.15 1 238 . 93 PHE CA C 59.65 0.20 1 239 . 93 PHE CB C 38.65 0.20 1 240 . 93 PHE H H 7.43 0.04 1 241 . 93 PHE N N 130.55 0.15 1 242 . 94 GLU CA C 58.71 0.20 1 243 . 94 GLU CB C 28.38 0.20 1 244 . 94 GLU H H 8.21 0.04 1 245 . 94 GLU N N 124.91 0.15 1 246 . 95 ASN CA C 54.43 0.20 1 247 . 95 ASN CB C 37.66 0.20 1 248 . 95 ASN H H 7.95 0.04 1 249 . 95 ASN N N 119.51 0.15 1 250 . 96 VAL CA C 68.60 0.20 1 251 . 96 VAL CB C 30.53 0.20 1 252 . 96 VAL H H 7.93 0.04 1 253 . 96 VAL N N 129.72 0.15 1 254 . 97 LYS CA C 58.44 0.20 1 255 . 97 LYS CB C 32.90 0.20 1 256 . 97 LYS H H 6.74 0.04 1 257 . 97 LYS N N 120.15 0.15 1 258 . 98 GLU CA C 57.72 0.20 1 259 . 98 GLU CB C 30.20 0.20 1 260 . 98 GLU H H 7.77 0.04 1 261 . 98 GLU N N 117.54 0.15 1 262 . 99 LYS CA C 57.19 0.20 1 263 . 99 LYS H H 8.20 0.04 1 264 . 99 LYS N N 120.84 0.15 1 265 . 102 PRO CA C 65.87 0.20 1 266 . 103 GLU CA C 60.55 0.20 1 267 . 103 GLU H H 7.55 0.04 1 268 . 103 GLU N N 122.56 0.15 1 269 . 104 VAL CA C 66.27 0.20 1 270 . 104 VAL H H 8.35 0.04 1 271 . 104 VAL N N 121.92 0.15 1 272 . 105 HIS CA C 57.18 0.20 1 273 . 105 HIS H H 8.45 0.04 1 274 . 105 HIS N N 120.82 0.15 1 275 . 109 PRO CA C 63.83 0.20 1 276 . 109 PRO CB C 30.64 0.20 1 277 . 110 GLY CA C 45.31 0.20 1 278 . 110 GLY H H 8.70 0.04 1 279 . 110 GLY N N 115.12 0.15 1 280 . 111 VAL CA C 60.62 0.20 1 281 . 111 VAL H H 7.28 0.04 1 282 . 111 VAL N N 128.30 0.15 1 283 . 112 PRO CA C 63.38 0.20 1 284 . 112 PRO CB C 32.92 0.20 1 285 . 113 ILE CA C 59.58 0.20 1 286 . 113 ILE H H 8.02 0.04 1 287 . 113 ILE N N 123.41 0.15 1 288 . 114 ILE CA C 59.47 0.20 1 289 . 114 ILE H H 8.80 0.04 1 290 . 114 ILE N N 131.44 0.15 1 291 . 115 ILE CA C 60.15 0.20 1 292 . 115 ILE CB C 37.98 0.20 1 293 . 115 ILE H H 8.21 0.04 1 294 . 115 ILE N N 130.84 0.15 1 295 . 116 VAL CA C 59.01 0.20 1 296 . 116 VAL CB C 33.30 0.20 1 297 . 116 VAL H H 8.94 0.04 1 298 . 116 VAL N N 133.04 0.15 1 299 . 117 GLY CA C 44.09 0.20 1 300 . 117 GLY H H 8.70 0.04 1 301 . 117 GLY N N 119.79 0.15 1 302 . 118 THR CA C 59.45 0.20 1 303 . 118 THR CB C 70.05 0.20 1 304 . 118 THR H H 9.29 0.04 1 305 . 118 THR N N 121.08 0.15 1 306 . 119 GLN CA C 55.78 0.20 1 307 . 119 GLN CB C 24.31 0.20 1 308 . 119 GLN H H 9.43 0.04 1 309 . 119 GLN N N 113.44 0.15 1 310 . 120 THR CA C 64.77 0.20 1 311 . 120 THR CB C 67.92 0.20 1 312 . 120 THR H H 8.05 0.04 1 313 . 120 THR N N 109.95 0.15 1 314 . 121 ASP CA C 55.12 0.20 1 315 . 121 ASP CB C 40.02 0.20 1 316 . 121 ASP H H 8.58 0.04 1 317 . 121 ASP N N 123.48 0.15 1 318 . 122 LEU CA C 55.06 0.20 1 319 . 122 LEU CB C 42.02 0.20 1 320 . 122 LEU H H 7.81 0.04 1 321 . 122 LEU N N 122.73 0.15 1 322 . 123 ARG CA C 60.21 0.20 1 323 . 123 ARG H H 7.22 0.04 1 324 . 123 ARG N N 120.32 0.15 1 325 . 124 ASN CA C 51.57 0.20 1 326 . 124 ASN CB C 38.85 0.20 1 327 . 124 ASN H H 7.23 0.04 1 328 . 124 ASN N N 115.68 0.15 1 329 . 125 ASP CA C 53.32 0.20 1 330 . 125 ASP CB C 43.11 0.20 1 331 . 125 ASP H H 7.24 0.04 1 332 . 125 ASP N N 126.66 0.15 1 333 . 126 ASP CA C 58.22 0.20 1 334 . 126 ASP CB C 41.17 0.20 1 335 . 126 ASP H H 8.73 0.04 1 336 . 126 ASP N N 130.88 0.15 1 337 . 127 VAL CA C 66.33 0.20 1 338 . 127 VAL CB C 30.44 0.20 1 339 . 127 VAL H H 7.97 0.04 1 340 . 127 VAL N N 125.13 0.15 1 341 . 128 ILE CA C 63.14 0.20 1 342 . 128 ILE CB C 35.83 0.20 1 343 . 128 ILE H H 8.10 0.04 1 344 . 128 ILE N N 127.53 0.15 1 345 . 129 LEU CA C 58.22 0.20 1 346 . 129 LEU CB C 40.86 0.20 1 347 . 129 LEU H H 8.72 0.04 1 348 . 129 LEU N N 124.09 0.15 1 349 . 130 GLN CA C 58.90 0.20 1 350 . 130 GLN H H 8.11 0.04 1 351 . 130 GLN N N 122.66 0.15 1 352 . 131 ARG CA C 59.38 0.20 1 353 . 131 ARG CB C 29.50 0.20 1 354 . 132 LEU CA C 57.87 0.20 1 355 . 132 LEU CB C 40.63 0.20 1 356 . 132 LEU H H 8.49 0.04 1 357 . 132 LEU N N 124.10 0.15 1 358 . 133 HIS CA C 59.06 0.20 1 359 . 133 HIS CB C 29.38 0.20 1 360 . 133 HIS H H 8.87 0.04 1 361 . 133 HIS N N 124.64 0.15 1 362 . 134 ARG CA C 59.06 0.20 1 363 . 135 GLN CA C 54.88 0.20 1 364 . 135 GLN CB C 29.43 0.20 1 365 . 135 GLN H H 7.44 0.04 1 366 . 135 GLN N N 121.26 0.15 1 367 . 136 LYS CA C 57.15 0.20 1 368 . 136 LYS CB C 27.91 0.20 1 369 . 136 LYS H H 8.02 0.04 1 370 . 136 LYS N N 119.22 0.15 1 371 . 137 LEU CA C 52.69 0.20 1 372 . 137 LEU CB C 46.25 0.20 1 373 . 137 LEU H H 8.05 0.04 1 374 . 137 LEU N N 122.75 0.15 1 375 . 138 SER CA C 56.34 0.20 1 376 . 138 SER H H 7.74 0.04 1 377 . 138 SER N N 118.00 0.15 1 378 . 139 PRO CA C 62.72 0.20 1 379 . 139 PRO CB C 32.10 0.20 1 380 . 140 ILE CA C 58.49 0.20 1 381 . 140 ILE H H 9.19 0.04 1 382 . 140 ILE N N 128.08 0.15 1 383 . 141 THR CA C 60.17 0.20 1 384 . 141 THR H H 8.31 0.04 1 385 . 141 THR N N 123.38 0.15 1 386 . 142 GLN CA C 58.78 0.20 1 387 . 142 GLN H H 9.06 0.04 1 388 . 142 GLN N N 126.64 0.15 1 389 . 144 GLN CA C 59.04 0.20 1 390 . 145 GLY CA C 46.61 0.20 1 391 . 145 GLY H H 7.86 0.04 1 392 . 145 GLY N N 113.98 0.15 1 393 . 146 GLU CA C 59.50 0.20 1 394 . 146 GLU CB C 28.96 0.20 1 395 . 146 GLU H H 8.19 0.04 1 396 . 146 GLU N N 125.47 0.15 1 397 . 147 LYS CA C 59.56 0.20 1 398 . 147 LYS CB C 31.62 0.20 1 399 . 147 LYS H H 8.05 0.04 1 400 . 147 LYS N N 125.17 0.15 1 401 . 148 LEU CA C 57.41 0.20 1 402 . 148 LEU CB C 40.51 0.20 1 403 . 148 LEU H H 7.84 0.04 1 404 . 148 LEU N N 126.34 0.15 1 405 . 149 ALA CA C 55.05 0.20 1 406 . 149 ALA CB C 17.83 0.20 1 407 . 149 ALA H H 8.15 0.04 1 408 . 149 ALA N N 123.12 0.15 1 409 . 150 LYS CA C 58.77 0.20 1 410 . 150 LYS CB C 31.73 0.20 1 411 . 150 LYS H H 7.65 0.04 1 412 . 150 LYS N N 121.54 0.15 1 413 . 151 GLU CA C 59.16 0.20 1 414 . 151 GLU CB C 29.43 0.20 1 415 . 151 GLU H H 8.23 0.04 1 416 . 151 GLU N N 126.12 0.15 1 417 . 152 LEU CA C 53.84 0.20 1 418 . 152 LEU CB C 40.37 0.20 1 419 . 152 LEU H H 8.04 0.04 1 420 . 152 LEU N N 119.32 0.15 1 421 . 153 ARG CA C 57.15 0.20 1 422 . 153 ARG CB C 25.60 0.20 1 423 . 153 ARG H H 7.67 0.04 1 424 . 153 ARG N N 119.29 0.15 1 425 . 154 ALA CA C 51.33 0.20 1 426 . 154 ALA CB C 19.39 0.20 1 427 . 154 ALA H H 8.53 0.04 1 428 . 154 ALA N N 124.83 0.15 1 429 . 155 VAL CA C 65.79 0.20 1 430 . 155 VAL CB C 31.66 0.20 1 431 . 155 VAL H H 9.11 0.04 1 432 . 155 VAL N N 125.06 0.15 1 433 . 156 LYS CA C 54.85 0.20 1 434 . 156 LYS CB C 34.99 0.20 1 435 . 156 LYS H H 7.08 0.04 1 436 . 156 LYS N N 114.70 0.15 1 437 . 157 TYR CA C 55.95 0.20 1 438 . 157 TYR CB C 40.73 0.20 1 439 . 157 TYR H H 8.57 0.04 1 440 . 157 TYR N N 126.23 0.15 1 441 . 158 VAL CA C 58.53 0.20 1 442 . 158 VAL CB C 34.38 0.20 1 443 . 158 VAL H H 8.26 0.04 1 444 . 158 VAL N N 126.99 0.15 1 445 . 159 GLU CA C 53.43 0.20 1 446 . 159 GLU CB C 31.08 0.20 1 447 . 159 GLU H H 7.90 0.04 1 448 . 159 GLU N N 118.97 0.15 1 449 . 160 CYS CA C 55.69 0.20 1 450 . 160 CYS CB C 31.25 0.20 1 451 . 160 CYS H H 8.86 0.04 1 452 . 160 CYS N N 117.56 0.15 1 453 . 161 SER CA C 55.78 0.20 1 454 . 161 SER CB C 64.74 0.20 1 455 . 161 SER H H 7.82 0.04 1 456 . 161 SER N N 114.22 0.15 1 457 . 162 ALA CA C 54.38 0.20 1 458 . 162 ALA CB C 18.84 0.20 1 459 . 162 ALA H H 9.25 0.04 1 460 . 162 ALA N N 137.04 0.15 1 461 . 163 LEU CA C 57.29 0.20 1 462 . 163 LEU CB C 42.82 0.20 1 463 . 163 LEU H H 7.32 0.04 1 464 . 163 LEU N N 122.86 0.15 1 465 . 164 THR CA C 61.45 0.20 1 466 . 164 THR CB C 69.39 0.20 1 467 . 164 THR H H 7.99 0.04 1 468 . 164 THR N N 111.33 0.15 1 469 . 165 GLN CA C 58.43 0.20 1 470 . 165 GLN CB C 25.12 0.20 1 471 . 165 GLN H H 7.50 0.04 1 472 . 165 GLN N N 118.29 0.15 1 473 . 166 ARG CA C 57.71 0.20 1 474 . 166 ARG H H 7.89 0.04 1 475 . 166 ARG N N 128.54 0.15 1 476 . 167 GLY CA C 46.09 0.20 1 477 . 167 GLY H H 9.16 0.04 1 478 . 167 GLY N N 120.67 0.15 1 479 . 168 LEU CA C 58.43 0.20 1 480 . 168 LEU CB C 42.85 0.20 1 481 . 168 LEU H H 7.39 0.04 1 482 . 168 LEU N N 125.47 0.15 1 483 . 169 LYS CA C 60.04 0.20 1 484 . 169 LYS CB C 31.41 0.20 1 485 . 169 LYS H H 8.48 0.04 1 486 . 169 LYS N N 121.32 0.15 1 487 . 170 THR CA C 65.91 0.20 1 488 . 170 THR CB C 68.89 0.20 1 489 . 170 THR H H 7.64 0.04 1 490 . 170 THR N N 118.78 0.15 1 491 . 171 VAL CA C 67.10 0.20 1 492 . 171 VAL CB C 31.13 0.20 1 493 . 171 VAL H H 7.26 0.04 1 494 . 171 VAL N N 124.27 0.15 1 495 . 172 PHE CA C 61.68 0.20 1 496 . 172 PHE CB C 38.99 0.20 1 497 . 172 PHE H H 6.33 0.04 1 498 . 172 PHE N N 118.75 0.15 1 499 . 173 ASP CA C 57.53 0.20 1 500 . 173 ASP CB C 39.60 0.20 1 501 . 173 ASP H H 8.14 0.04 1 502 . 173 ASP N N 126.07 0.15 1 503 . 174 GLU CA C 57.72 0.20 1 504 . 174 GLU CB C 26.93 0.20 1 505 . 174 GLU H H 8.16 0.04 1 506 . 174 GLU N N 121.34 0.15 1 507 . 175 ALA CA C 55.20 0.20 1 508 . 175 ALA CB C 16.99 0.20 1 509 . 175 ALA H H 7.75 0.04 1 510 . 175 ALA N N 128.02 0.15 1 511 . 176 ILE CA C 65.49 0.20 1 512 . 176 ILE CB C 36.88 0.20 1 513 . 176 ILE H H 7.68 0.04 1 514 . 176 ILE N N 120.76 0.15 1 515 . 177 VAL CA C 66.21 0.20 1 516 . 177 VAL CB C 31.03 0.20 1 517 . 177 VAL H H 7.33 0.04 1 518 . 177 VAL N N 120.91 0.15 1 519 . 178 ALA CA C 53.87 0.20 1 520 . 178 ALA CB C 18.36 0.20 1 521 . 178 ALA H H 8.01 0.04 1 522 . 178 ALA N N 124.36 0.15 1 523 . 179 ALA CA C 53.44 0.20 1 524 . 179 ALA CB C 19.39 0.20 1 525 . 179 ALA H H 7.78 0.04 1 526 . 179 ALA N N 122.37 0.15 1 527 . 180 LEU CA C 54.75 0.20 1 528 . 180 LEU CB C 42.36 0.20 1 529 . 180 LEU H H 7.33 0.04 1 530 . 180 LEU N N 120.92 0.15 1 531 . 181 GLU CA C 58.87 0.20 1 532 . 181 GLU H H 7.37 0.04 1 533 . 181 GLU N N 129.82 0.15 1 stop_ save_