data_4939 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structures of Two CCHC Zinc Fingers from the FOG Family Protein U-shaped that Mediate Protein-Protein Interactions ; _BMRB_accession_number 4939 _BMRB_flat_file_name bmr4939.str _Entry_type original _Submission_date 2001-01-13 _Accession_date 2001-01-14 _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 Kowalski K. . . 2 Mackay J. P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 186 "15N chemical shifts" 34 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-01-23 original author . stop_ _Original_release_date 2001-01-23 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structures of Two CCHC Zinc Fingers from the FOG Family Protein U-shaped that Mediate Protein-Protein Interactions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liew C. K. . 2 Kowalski K. . . 3 Fox A. H. . 4 Newton A. . . 5 Sharpe B. K. . 6 Crossley M. . . 7 Mackay J. P. . stop_ _Journal_abbreviation Structure _Journal_volume 8 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1157 _Page_last 1166 _Year 2000 _Details . loop_ _Keyword zinc-finger beta-hairpin alpha-helix stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Liew, C.K., Kowalski, K., Fox, A.H., Newton, A., Sharpe, B.K., Crossley, M., and Mackay, J.P. Solution Structures of Two CCHC Zinc Fingers from the FOG Family Protein U-shaped that Mediate Protein-Protein Interactions. Structure, 8, 1157-1166 (2000). ; _Citation_title 'Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11080638 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Liew C.K. K. . 2 Kowalski K. . . 3 Fox A.H. H. . 4 Newton A. . . 5 Sharpe B.K. K. . 6 Crossley M. . . 7 Mackay J.P. P. . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 8 _Journal_issue 11 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1157 _Page_last 1166 _Year 2000 _Details ; BACKGROUND: Zinc finger domains have traditionally been regarded as sequence-specific DNA binding motifs. However, recent evidence indicates that many zinc fingers mediate specific protein-protein interactions. For instance, several zinc fingers from FOG family proteins have been shown to interact with the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to determine the first structures of two FOG family zinc fingers that are involved in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers resemble classical TFIIIA-like zinc fingers, with the exception of an unusual extended portion of the polypeptide backbone prior to the fourth zinc ligand. [15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of USH-F1, and comparison with other FOG family proteins indicates that the recognition mechanism is conserved across species. The surface of FOG-type fingers that interacts with GATA-1 overlaps substantially with the surface through which classical fingers typically recognize DNA. This suggests that these fingers could not contact both GATA and DNA simultaneously. In addition, results from NMR, gel filtration, and sedimentation equilibrium experiments suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results demonstrate unequivocally that zinc fingers comprising the classical betabetaalpha fold are capable of mediating specific contacts between proteins. The existence of this alternative function has implications for the prediction of protein function from sequence data and for the evolution of protein function. ; save_ ################################## # Molecular system description # ################################## save_system_U-shaped _Saveframe_category molecular_system _Mol_system_name 'ninth zinc-finger domain of the u-shaped transcription factor' _Abbreviation_common U-shaped _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'U-shaped transcriptional cofactor' $U-shaped 'ZINC ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'transcription factor' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_U-shaped _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'U-shaped transcriptional cofactor' _Abbreviation_common Ush _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; GSAAEVMKKYCSTCDISFNY VKTYLAHKQFYCKNKP ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 ALA 4 ALA 5 GLU 6 VAL 7 MET 8 LYS 9 LYS 10 TYR 11 CYS 12 SER 13 THR 14 CYS 15 ASP 16 ILE 17 SER 18 PHE 19 ASN 20 TYR 21 VAL 22 LYS 23 THR 24 TYR 25 LEU 26 ALA 27 HIS 28 LYS 29 GLN 30 PHE 31 TYR 32 CYS 33 LYS 34 ASN 35 LYS 36 PRO stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value REF XP_002077649 'GD23030 [Drosophila simulans]' 88.89 675 100.00 100.00 1.23e-11 GenBank EDX03234 'GD23030 [Drosophila simulans]' 88.89 675 100.00 100.00 1.23e-11 PDB 1FU9 'Solution Structure Of The Ninth Zinc-Finger Domain Of The U- Shaped Transcription Factor' 100.00 36 100.00 100.00 8.80e-13 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Jul 20 13:11:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $U-shaped 'fruit fly' 7227 Eukaryota Metazoa Drosophila melanogaster 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 $U-shaped 'recombinant technology' Bacteria Escherichia coli . PGEX-2T 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 $U-shaped 0.4 mM . ZnSO4 0.6 mM . TCEP 0.6 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $U-shaped 0.2 mM [U-15N] ZnSO4 0.3 mM . TCEP 0.3 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.1 loop_ _Task 'data processing' stop_ _Details Bruker save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' stop_ _Details 'Bartels et al' save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details 'Guntert et al' save_ save_CNS _Saveframe_category software _Name CNS _Version 0.5 loop_ _Task refinement stop_ _Details 'Brunger et al' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_HNHA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HNHB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHB _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 n/a temperature 293 1 K 'ionic strength' 0.6 . mM pressure 1 . atm stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 n/a temperature 293 1 K 'ionic strength' 0.3 . mM pressure 1 . atm 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 'liquid ammonia' N 15 nitrogen ppm 0.0 external indirect . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'U-shaped transcriptional cofactor' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 SER HA H 4.536 0.020 1 2 . 2 SER HB2 H 3.930 0.020 2 3 . 2 SER N N 114.4 0.2 1 4 . 3 ALA H H 8.632 0.003 1 5 . 3 ALA HA H 4.321 0.006 1 6 . 3 ALA HB H 1.434 0.006 1 7 . 3 ALA N N 124.8 0.2 1 8 . 4 ALA H H 8.290 0.002 1 9 . 4 ALA HA H 4.260 0.005 1 10 . 4 ALA HB H 1.403 0.001 1 11 . 4 ALA N N 120.8 0.2 1 12 . 5 GLU H H 8.250 0.001 1 13 . 5 GLU HA H 4.282 0.003 1 14 . 5 GLU HB2 H 2.111 0.004 2 15 . 5 GLU HB3 H 2.033 0.006 2 16 . 5 GLU HG2 H 2.364 0.002 2 17 . 5 GLU HG3 H 2.327 0.005 2 18 . 5 GLU N N 118.2 0.2 1 19 . 6 VAL H H 8.087 0.001 1 20 . 6 VAL HA H 4.027 0.004 1 21 . 6 VAL HB H 2.122 0.007 1 22 . 6 VAL HG1 H 0.995 0.007 2 23 . 6 VAL HG2 H 0.953 0.002 2 24 . 6 VAL N N 119.1 0.2 1 25 . 7 MET H H 8.212 0.002 1 26 . 7 MET HA H 4.441 0.002 1 27 . 7 MET HB2 H 2.055 0.002 2 28 . 7 MET HG2 H 2.620 0.002 2 29 . 7 MET HG3 H 2.528 0.003 2 30 . 7 MET N N 121.2 0.2 1 31 . 8 LYS H H 7.987 0.002 1 32 . 8 LYS HA H 4.192 0.005 1 33 . 8 LYS HB2 H 1.751 0.014 2 34 . 8 LYS HG2 H 1.447 0.020 2 35 . 8 LYS HG3 H 1.355 0.002 2 36 . 8 LYS HD2 H 1.702 0.020 2 37 . 8 LYS HE2 H 2.988 0.002 2 38 . 8 LYS N N 120.1 0.2 1 39 . 9 LYS H H 8.247 0.003 1 40 . 9 LYS HA H 4.112 0.002 1 41 . 9 LYS HB2 H 1.631 0.003 2 42 . 9 LYS HG2 H 1.175 0.001 2 43 . 9 LYS HD2 H 1.521 0.023 2 44 . 9 LYS HD3 H 1.367 0.017 2 45 . 9 LYS HE2 H 2.853 0.002 2 46 . 9 LYS N N 119.8 0.2 1 47 . 10 TYR H H 7.577 0.002 1 48 . 10 TYR HA H 5.289 0.005 1 49 . 10 TYR HB2 H 3.011 0.001 2 50 . 10 TYR HB3 H 2.627 0.004 2 51 . 10 TYR HE1 H 6.621 0.003 3 52 . 10 TYR HD1 H 6.937 0.004 3 53 . 10 TYR N N 119.6 0.2 1 54 . 11 CYS H H 8.790 0.005 1 55 . 11 CYS HA H 4.920 0.003 1 56 . 11 CYS HB2 H 3.027 0.007 2 57 . 11 CYS HB3 H 2.900 0.002 2 58 . 11 CYS N N 126.2 0.2 1 59 . 12 SER H H 9.047 0.002 1 60 . 12 SER HB2 H 4.158 0.001 2 61 . 12 SER HB3 H 4.038 0.003 2 62 . 12 SER N N 122.8 0.2 1 63 . 13 THR H H 8.279 0.001 1 64 . 13 THR HA H 4.133 0.004 1 65 . 13 THR HB H 4.096 0.006 1 66 . 13 THR HG2 H 1.299 0.003 1 67 . 13 THR N N 117.3 0.2 1 68 . 14 CYS H H 8.506 0.004 1 69 . 14 CYS HA H 4.178 0.008 1 70 . 14 CYS HB2 H 3.182 0.003 2 71 . 14 CYS HB3 H 2.568 0.004 2 72 . 14 CYS N N 121.0 0.2 1 73 . 15 ASP H H 8.083 0.002 1 74 . 15 ASP HA H 4.166 0.006 1 75 . 15 ASP HB2 H 3.278 0.006 2 76 . 15 ASP HB3 H 2.453 0.001 2 77 . 15 ASP N N 117.5 0.2 1 78 . 16 ILE H H 6.838 0.004 1 79 . 16 ILE HA H 4.227 0.002 1 80 . 16 ILE HB H 1.010 0.004 1 81 . 16 ILE HG2 H 0.196 0.129 1 82 . 16 ILE HG12 H 0.710 0.004 2 83 . 16 ILE HD1 H 1.215 0.005 1 84 . 16 ILE N N 113.7 0.2 1 85 . 17 SER H H 8.309 0.003 1 86 . 17 SER HA H 5.050 0.002 1 87 . 17 SER HB2 H 3.776 0.003 2 88 . 17 SER HB3 H 3.727 0.005 2 89 . 17 SER N N 118.4 0.2 1 90 . 18 PHE H H 8.617 0.002 1 91 . 18 PHE HA H 4.680 0.003 1 92 . 18 PHE HB2 H 2.707 0.003 2 93 . 18 PHE HB3 H 3.305 0.180 2 94 . 18 PHE HZ H 6.132 0.003 1 95 . 18 PHE HD1 H 7.233 0.002 3 96 . 18 PHE HE1 H 7.036 0.002 3 97 . 18 PHE N N 118.7 0.2 1 98 . 19 ASN H H 8.976 0.001 1 99 . 19 ASN HA H 4.553 0.005 1 100 . 19 ASN HB2 H 2.458 0.005 2 101 . 19 ASN HD21 H 7.380 0.020 2 102 . 19 ASN HD22 H 6.994 0.001 2 103 . 19 ASN N N 117.3 0.2 1 104 . 20 TYR H H 7.488 0.003 1 105 . 20 TYR HA H 5.142 0.002 1 106 . 20 TYR HB2 H 2.998 0.002 2 107 . 20 TYR HB3 H 3.534 0.003 2 108 . 20 TYR HE1 H 6.933 0.004 3 109 . 20 TYR HD1 H 7.321 0.002 3 110 . 20 TYR N N 113.0 0.2 1 111 . 21 VAL H H 9.215 0.002 1 112 . 21 VAL HA H 3.822 0.004 1 113 . 21 VAL HB H 2.192 0.001 1 114 . 21 VAL HG1 H 1.170 0.002 2 115 . 21 VAL HG2 H 1.101 0.003 2 116 . 21 VAL N N 124.0 0.2 1 117 . 22 LYS H H 8.748 0.002 1 118 . 22 LYS HA H 4.081 0.003 1 119 . 22 LYS HB2 H 1.952 0.007 2 120 . 22 LYS HB3 H 1.821 0.001 2 121 . 22 LYS HG2 H 1.453 0.001 2 122 . 22 LYS HD2 H 1.692 0.006 2 123 . 22 LYS HD3 H 1.552 0.005 2 124 . 22 LYS HE2 H 2.943 0.001 2 125 . 22 LYS N N 116.1 0.2 1 126 . 23 THR H H 7.192 0.003 1 127 . 23 THR HA H 4.198 0.004 1 128 . 23 THR HB H 4.534 0.001 1 129 . 23 THR HG2 H 1.617 0.006 1 130 . 23 THR N N 111.9 0.2 1 131 . 24 TYR H H 7.480 0.003 1 132 . 24 TYR HA H 2.889 0.004 1 133 . 24 TYR HB2 H 3.182 0.005 2 134 . 24 TYR HB3 H 2.710 0.003 2 135 . 24 TYR HE1 H 6.724 0.003 3 136 . 24 TYR HD1 H 6.878 0.003 3 137 . 24 TYR N N 123.4 0.2 1 138 . 25 LEU H H 8.743 0.001 1 139 . 25 LEU HA H 3.644 0.005 1 140 . 25 LEU HB2 H 1.825 0.002 2 141 . 25 LEU HB3 H 1.420 0.005 2 142 . 25 LEU HG H 1.933 0.005 1 143 . 25 LEU HD1 H 0.904 0.010 2 144 . 25 LEU N N 117.7 0.2 1 145 . 26 ALA H H 7.718 0.002 1 146 . 26 ALA HA H 4.208 0.002 1 147 . 26 ALA HB H 1.690 0.003 1 148 . 26 ALA N N 120.1 0.2 1 149 . 27 HIS H H 7.891 0.004 1 150 . 27 HIS HA H 4.387 0.003 1 151 . 27 HIS HB2 H 3.346 0.002 2 152 . 27 HIS HB3 H 3.039 0.002 2 153 . 27 HIS HD2 H 6.577 0.001 1 154 . 27 HIS HE1 H 8.335 0.001 1 155 . 27 HIS N N 116.1 0.2 1 156 . 28 LYS H H 7.982 0.004 1 157 . 28 LYS HA H 3.702 0.004 1 158 . 28 LYS HB2 H 1.595 0.003 2 159 . 28 LYS HG2 H 1.168 0.001 2 160 . 28 LYS HG3 H 1.067 0.006 2 161 . 28 LYS HD2 H 1.725 0.001 2 162 . 28 LYS HE2 H 3.150 0.020 2 163 . 28 LYS HE3 H 2.990 0.002 2 164 . 28 LYS N N 114.9 0.2 1 165 . 29 GLN H H 7.610 0.003 1 166 . 29 GLN HA H 3.730 0.004 1 167 . 29 GLN HB2 H 1.053 0.001 2 168 . 29 GLN HB3 H 1.381 0.002 2 169 . 29 GLN HG2 H 1.780 0.002 2 170 . 29 GLN HG3 H 1.547 0.003 2 171 . 29 GLN HE21 H 7.029 0.002 2 172 . 29 GLN HE22 H 6.679 0.020 2 173 . 29 GLN N N 114.9 0.2 1 174 . 30 PHE H H 7.683 0.003 1 175 . 30 PHE HA H 4.669 0.001 1 176 . 30 PHE HB2 H 2.436 0.003 2 177 . 30 PHE HB3 H 1.879 0.002 2 178 . 30 PHE HZ H 7.221 0.009 1 179 . 30 PHE HD1 H 7.165 0.001 3 180 . 30 PHE HE1 H 7.276 0.001 3 181 . 30 PHE N N 110.5 0.2 1 182 . 31 TYR H H 7.835 0.003 1 183 . 31 TYR HA H 5.003 0.002 1 184 . 31 TYR HB2 H 3.549 0.002 2 185 . 31 TYR HB3 H 2.668 0.002 2 186 . 31 TYR HE1 H 6.851 0.003 3 187 . 31 TYR HD1 H 7.228 0.003 3 188 . 31 TYR N N 114.9 0.2 1 189 . 32 CYS H H 7.761 0.001 1 190 . 32 CYS HA H 3.770 0.005 1 191 . 32 CYS HB2 H 2.059 0.003 2 192 . 32 CYS HB3 H 2.549 0.001 2 193 . 32 CYS N N 122.4 0.2 1 194 . 33 LYS H H 7.795 0.002 1 195 . 33 LYS HA H 4.227 0.005 1 196 . 33 LYS HB2 H 1.871 0.003 2 197 . 33 LYS HG2 H 1.553 0.005 2 198 . 33 LYS HG3 H 1.474 0.001 2 199 . 33 LYS HD2 H 1.703 0.005 2 200 . 33 LYS HE2 H 3.043 0.005 2 201 . 33 LYS N N 124.8 0.2 1 202 . 34 ASN H H 8.442 0.001 1 203 . 34 ASN HA H 4.746 0.001 1 204 . 34 ASN HB2 H 2.846 0.004 2 205 . 34 ASN HB3 H 2.722 0.004 2 206 . 34 ASN HD21 H 7.550 0.001 2 207 . 34 ASN HD22 H 6.942 0.001 2 208 . 34 ASN N N 117.7 0.2 1 209 . 35 LYS H H 8.093 0.001 1 210 . 35 LYS HA H 4.574 0.002 1 211 . 35 LYS HB2 H 1.805 0.004 2 212 . 35 LYS HB3 H 1.731 0.002 2 213 . 35 LYS HG2 H 1.431 0.003 2 214 . 35 LYS N N 121.7 0.2 1 215 . 36 PRO HA H 4.229 0.003 1 216 . 36 PRO HB2 H 2.211 0.006 2 217 . 36 PRO HG2 H 1.957 0.004 2 218 . 36 PRO HG3 H 1.875 0.004 2 219 . 36 PRO HD2 H 3.733 0.002 2 220 . 36 PRO HD3 H 3.625 0.020 2 stop_ save_