data_5555 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the 2nd PHD domain from Mi2b ; _BMRB_accession_number 5555 _BMRB_flat_file_name bmr5555.str _Entry_type original _Submission_date 2002-10-10 _Accession_date 2002-10-10 _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 Kwan A. H.Y. . 2 Gell D. A. . 3 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" 321 "15N chemical shifts" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2009-08-05 update author 'Update chemical shifts' 2003-08-01 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 5556 'Mi2-beta and transcription factor WSTF' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Engineering a Protein Scaffold from a PHD Finger' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22728194 _PubMed_ID 12842043 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kwan A. H.Y. . 2 Gell D. A. . 3 Verger A. . . 4 Crossley M. . . 5 Matthews J. M. . 6 Mackay J. P. . stop_ _Journal_abbreviation Structure _Journal_name_full Structure _Journal_volume 11 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 803 _Page_last 813 _Year 2003 _Details . loop_ _Keyword PHD 'zinc finger' 'protein scaffold' stop_ save_ ################################## # Molecular system description # ################################## save_system_PHD _Saveframe_category molecular_system _Mol_system_name 'Chromodomain helicase-DNA-binding protein 4' _Abbreviation_common PHD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Mi2-beta $Mi2_beta 'ZINC ION 1' $ZN 'ZINC ION 2' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Mi2_beta _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common PHD _Abbreviation_common PHD _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; GPLGSDHHMEFCRVCKDGGE LLCCDTCPSSYHIHCLNPPL PEIPNGEWLCPRCTCPALKG K ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLY 2 2 PRO 3 3 LEU 4 4 GLY 5 5 SER 6 446 ASP 7 447 HIS 8 448 HIS 9 449 MET 10 450 GLU 11 451 PHE 12 452 CYS 13 453 ARG 14 454 VAL 15 455 CYS 16 456 LYS 17 457 ASP 18 458 GLY 19 459 GLY 20 460 GLU 21 461 LEU 22 462 LEU 23 463 CYS 24 464 CYS 25 465 ASP 26 466 THR 27 467 CYS 28 468 PRO 29 469 SER 30 470 SER 31 471 TYR 32 472 HIS 33 473 ILE 34 474 HIS 35 475 CYS 36 476 LEU 37 477 ASN 38 478 PRO 39 479 PRO 40 480 LEU 41 481 PRO 42 482 GLU 43 483 ILE 44 484 PRO 45 485 ASN 46 486 GLY 47 487 GLU 48 488 TRP 49 489 LEU 50 490 CYS 51 491 PRO 52 492 ARG 53 493 CYS 54 494 THR 55 495 CYS 56 496 PRO 57 497 ALA 58 498 LEU 59 499 LYS 60 500 GLY 61 501 LYS 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 PDB 1MM2 'Solution Structure Of The 2nd Phd Domain From Mi2b' 100.00 61 100.00 100.00 2.09e-27 DBJ BAE32198 'unnamed protein product [Mus musculus]' 93.44 895 98.25 98.25 8.84e-28 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 Mon Jul 25 12:24:02 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 $Mi2_beta Human 9606 Eukaryota Metazoa Homo sapiens 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 $Mi2_beta 'recombinant technology' E.coli Escherichia coli BL21(DE3) 'plasmid PGEX-6p' 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 $Mi2_beta 1 mM . DTT 1 mM . 'sodium phosphate buffer' 10 mM . NaCl 150 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Mi2_beta 0.2 mM [U-15N] DTT 1 mM . 'sodium phosphate buffer' 10 mM . NaCl 150 mM . H2O 95 % . D2O 5 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.5 loop_ _Task 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 refinement stop_ _Details 'Guntert et al' save_ save_ARIA _Saveframe_category software _Name ARIA _Version 1.1.2 loop_ _Task 'structure solution' stop_ _Details 'Linge 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_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ save_N15-HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name N15-HSQC _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 '2D TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name N15-HSQC _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 7.5 0.1 n/a temperature 298 0.1 K 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm . . . . . . $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Mi2-beta _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 GLY HA2 H 4.018 0.010 . 2 . 2 PRO HA H 4.495 0.010 . 3 . 2 PRO HB2 H 2.311 0.010 . 4 . 2 PRO HB3 H 1.972 0.001 . 5 . 2 PRO HG2 H 2.003 0.003 . 6 . 2 PRO HG3 H 1.952 0.004 . 7 . 2 PRO HD2 H 3.589 0.007 . 8 . 3 LEU N N 122.178 0.001 . 9 . 3 LEU H H 8.497 0.001 . 10 . 3 LEU HA H 4.365 0.002 . 11 . 3 LEU HB2 H 1.652 0.010 . 12 . 3 LEU HG H 1.606 0.002 . 13 . 3 LEU HD1 H 0.891 0.008 . 14 . 3 LEU HD2 H 0.852 0.007 . 15 . 4 GLY H H 8.444 0.001 . 16 . 4 GLY HA2 H 4.043 0.004 . 17 . 4 GLY HA3 H 3.981 0.001 . 18 . 5 SER H H 8.258 0.010 . 19 . 5 SER HA H 4.417 0.011 . 20 . 5 SER HB2 H 3.843 0.007 . 21 . 5 SER HB3 H 3.776 0.010 . 22 . 6 ASP H H 8.404 0.010 . 23 . 6 ASP HA H 4.586 0.001 . 24 . 6 ASP HB2 H 2.633 0.006 . 25 . 7 HIS H H 8.186 0.001 . 26 . 7 HIS HA H 4.672 0.004 . 27 . 7 HIS HB2 H 3.145 0.008 . 28 . 7 HIS HB3 H 3.080 0.009 . 29 . 7 HIS HD2 H 7.019 0.001 . 30 . 8 HIS H H 8.266 0.002 . 31 . 8 HIS HA H 4.721 0.003 . 32 . 8 HIS HB2 H 3.288 0.007 . 33 . 8 HIS HB3 H 2.913 0.009 . 34 . 8 HIS HD2 H 7.506 0.005 . 35 . 8 HIS HE1 H 8.603 0.008 . 36 . 9 MET N N 119.906 0.005 . 37 . 9 MET H H 8.750 0.005 . 38 . 9 MET HA H 4.178 0.005 . 39 . 9 MET HB2 H 1.872 0.009 . 40 . 9 MET HB3 H 1.688 0.012 . 41 . 9 MET HG2 H 2.644 0.005 . 42 . 10 GLU N N 122.157 0.001 . 43 . 10 GLU H H 8.895 0.001 . 44 . 10 GLU HA H 4.109 0.002 . 45 . 10 GLU HB2 H 1.827 0.008 . 46 . 10 GLU HG2 H 2.269 0.006 . 47 . 10 GLU HG3 H 2.136 0.008 . 48 . 11 PHE N N 115.044 0.005 . 49 . 11 PHE H H 6.744 0.005 . 50 . 11 PHE HA H 4.464 0.006 . 51 . 11 PHE HB2 H 2.707 0.009 . 52 . 11 PHE HB3 H 2.456 0.007 . 53 . 11 PHE HD2 H 6.921 0.007 . 54 . 11 PHE HE2 H 7.282 0.001 . 55 . 12 CYS N N 120.973 0.002 . 56 . 12 CYS H H 8.274 0.002 . 57 . 12 CYS HA H 3.886 0.009 . 58 . 12 CYS HB2 H 3.339 0.008 . 59 . 12 CYS HB3 H 1.824 0.013 . 60 . 12 CYS HG H 7.392 0.009 . 61 . 13 ARG N N 129.064 0.015 . 62 . 13 ARG H H 8.646 0.015 . 63 . 13 ARG HB2 H 1.985 0.007 . 64 . 13 ARG HB3 H 1.369 0.006 . 65 . 13 ARG HG2 H 1.699 0.009 . 66 . 13 ARG HG3 H 1.613 0.008 . 67 . 13 ARG HD2 H 3.287 0.005 . 68 . 13 ARG HD3 H 3.151 0.005 . 69 . 13 ARG HE H 8.640 0.002 . 70 . 14 VAL N N 120.597 0.002 . 71 . 14 VAL H H 8.869 0.002 . 72 . 14 VAL HA H 4.008 0.002 . 73 . 14 VAL HB H 2.298 0.008 . 74 . 14 VAL HG1 H 1.305 0.008 . 75 . 14 VAL HG2 H 1.125 0.006 . 76 . 15 CYS N N 117.929 0.005 . 77 . 15 CYS H H 8.097 0.005 . 78 . 15 CYS HA H 4.929 0.003 . 79 . 15 CYS HB2 H 3.397 0.005 . 80 . 15 CYS HB3 H 2.999 0.010 . 81 . 16 LYS N N 116.975 0.008 . 82 . 16 LYS H H 8.144 0.008 . 83 . 16 LYS HA H 4.175 0.003 . 84 . 16 LYS HB2 H 2.209 0.007 . 85 . 16 LYS HB3 H 1.811 0.010 . 86 . 16 LYS HG2 H 1.307 0.007 . 87 . 16 LYS HG3 H 1.197 0.009 . 88 . 16 LYS HD2 H 1.624 0.006 . 89 . 16 LYS HD3 H 1.485 0.007 . 90 . 16 LYS HE2 H 2.975 0.003 . 91 . 17 ASP N N 121.842 0.011 . 92 . 17 ASP H H 8.615 0.011 . 93 . 17 ASP HA H 5.306 0.004 . 94 . 17 ASP HB2 H 3.090 0.005 . 95 . 17 ASP HB3 H 2.985 0.012 . 96 . 18 GLY N N 107.978 0.003 . 97 . 18 GLY H H 8.576 0.003 . 98 . 18 GLY HA2 H 4.504 0.001 . 99 . 18 GLY HA3 H 3.905 0.003 . 100 . 19 GLY N N 110.712 0.003 . 101 . 19 GLY H H 8.625 0.003 . 102 . 19 GLY HA2 H 4.551 0.001 . 103 . 19 GLY HA3 H 3.671 0.007 . 104 . 20 GLU N N 125.080 0.001 . 105 . 20 GLU H H 8.769 0.001 . 106 . 20 GLU HA H 4.192 0.003 . 107 . 20 GLU HB2 H 2.086 0.006 . 108 . 20 GLU HB3 H 2.015 0.009 . 109 . 20 GLU HG2 H 2.247 0.010 . 110 . 20 GLU HG3 H 2.170 0.005 . 111 . 21 LEU N N 124.822 0.006 . 112 . 21 LEU H H 7.945 0.006 . 113 . 21 LEU HA H 4.354 0.003 . 114 . 21 LEU HB2 H 1.441 0.011 . 115 . 21 LEU HB3 H 0.906 0.007 . 116 . 21 LEU HG H 1.248 0.008 . 117 . 21 LEU HD1 H 0.411 0.008 . 118 . 21 LEU HD2 H 0.144 0.008 . 119 . 22 LEU N N 125.097 0.003 . 120 . 22 LEU H H 9.014 0.003 . 121 . 22 LEU HA H 4.339 0.007 . 122 . 22 LEU HB2 H 1.246 0.007 . 123 . 22 LEU HB3 H 0.785 0.007 . 124 . 22 LEU HG H 0.594 0.006 . 125 . 22 LEU HD1 H 0.377 0.010 . 126 . 22 LEU HD2 H 0.628 0.008 . 127 . 23 CYS N N 124.354 0.005 . 128 . 23 CYS H H 8.406 0.005 . 129 . 23 CYS HA H 4.867 0.003 . 130 . 23 CYS HB2 H 2.233 0.008 . 131 . 23 CYS HB3 H 1.559 0.008 . 132 . 24 CYS N N 126.581 0.006 . 133 . 24 CYS H H 8.615 0.006 . 134 . 24 CYS HA H 4.683 0.004 . 135 . 24 CYS HB2 H 3.875 0.005 . 136 . 24 CYS HB3 H 2.724 0.006 . 137 . 25 ASP N N 128.400 0.005 . 138 . 25 ASP H H 9.181 0.005 . 139 . 25 ASP HA H 4.889 0.002 . 140 . 25 ASP HB2 H 2.803 0.010 . 141 . 25 ASP HB3 H 2.736 0.006 . 142 . 26 THR N N 111.684 0.002 . 143 . 26 THR H H 9.690 0.002 . 144 . 26 THR HA H 4.659 0.004 . 145 . 26 THR HG2 H 1.056 0.008 . 146 . 27 CYS N N 126.954 0.008 . 147 . 27 CYS H H 8.247 0.008 . 148 . 27 CYS HA H 5.039 0.002 . 149 . 27 CYS HB2 H 3.271 0.010 . 150 . 27 CYS HB3 H 2.710 0.010 . 151 . 28 PRO HA H 4.354 0.005 . 152 . 28 PRO HB2 H 2.213 0.006 . 153 . 28 PRO HB3 H 1.916 0.009 . 154 . 28 PRO HG2 H 1.784 0.001 . 155 . 28 PRO HD2 H 3.732 0.006 . 156 . 28 PRO HD3 H 3.521 0.007 . 157 . 29 SER N N 119.235 0.001 . 158 . 29 SER H H 9.277 0.001 . 159 . 29 SER HA H 4.433 0.003 . 160 . 29 SER HB2 H 4.326 0.008 . 161 . 29 SER HB3 H 3.857 0.008 . 162 . 30 SER N N 117.497 0.007 . 163 . 30 SER H H 7.595 0.007 . 164 . 30 SER HA H 5.730 0.004 . 165 . 30 SER HB2 H 3.511 0.006 . 166 . 30 SER HB3 H 3.331 0.008 . 167 . 31 TYR N N 119.767 0.001 . 168 . 31 TYR H H 9.168 0.001 . 169 . 31 TYR HA H 5.536 0.002 . 170 . 31 TYR HB2 H 2.972 0.006 . 171 . 31 TYR HB3 H 2.420 0.009 . 172 . 31 TYR HD2 H 7.111 0.008 . 173 . 31 TYR HE2 H 6.882 0.010 . 174 . 32 HIS N N 119.600 0.004 . 175 . 32 HIS H H 8.654 0.004 . 176 . 32 HIS HA H 4.881 0.001 . 177 . 32 HIS HB2 H 3.321 0.005 . 178 . 32 HIS HB3 H 2.793 0.006 . 179 . 32 HIS HE1 H 7.464 0.007 . 180 . 32 HIS HD2 H 7.629 0.001 . 181 . 33 ILE N N 118.073 0.002 . 182 . 33 ILE H H 9.204 0.002 . 183 . 33 ILE HA H 3.886 0.002 . 184 . 33 ILE HB H 2.087 0.006 . 185 . 33 ILE HG2 H 0.784 0.008 . 186 . 33 ILE HG12 H 1.459 0.008 . 187 . 33 ILE HG13 H 1.287 0.008 . 188 . 33 ILE HD1 H 0.636 0.008 . 189 . 34 HIS N N 112.654 0.006 . 190 . 34 HIS H H 7.007 0.006 . 191 . 34 HIS HA H 4.821 0.010 . 192 . 34 HIS HB2 H 3.462 0.004 . 193 . 34 HIS HB3 H 3.121 0.005 . 194 . 34 HIS HD2 H 7.174 0.002 . 195 . 34 HIS HE1 H 7.630 0.010 . 196 . 35 CYS N N 121.387 0.007 . 197 . 35 CYS H H 7.363 0.007 . 198 . 35 CYS HA H 4.445 0.007 . 199 . 35 CYS HB2 H 3.279 0.007 . 200 . 35 CYS HB3 H 2.873 0.007 . 201 . 36 LEU N N 120.563 0.006 . 202 . 36 LEU H H 6.501 0.006 . 203 . 36 LEU HA H 4.183 0.002 . 204 . 36 LEU HB2 H 1.466 0.008 . 205 . 36 LEU HG H 1.731 0.009 . 206 . 36 LEU HD1 H 0.836 0.008 . 207 . 36 LEU HD2 H 0.550 0.009 . 208 . 37 ASN N N 116.876 0.001 . 209 . 37 ASN ND2 N 113.119 0.001 . 210 . 37 ASN H H 8.297 0.001 . 211 . 37 ASN HA H 4.996 0.002 . 212 . 37 ASN HB2 H 2.916 0.008 . 213 . 37 ASN HB3 H 2.620 0.010 . 214 . 37 ASN HD21 H 7.594 0.002 . 215 . 37 ASN HD22 H 6.915 0.007 . 216 . 38 PRO HA H 5.096 0.004 . 217 . 38 PRO HB2 H 2.445 0.006 . 218 . 38 PRO HB3 H 2.072 0.009 . 219 . 38 PRO HG2 H 2.121 0.002 . 220 . 38 PRO HG3 H 2.015 0.003 . 221 . 38 PRO HD2 H 3.801 0.006 . 222 . 38 PRO HD3 H 3.694 0.008 . 223 . 39 PRO HA H 4.434 0.002 . 224 . 39 PRO HB2 H 2.303 0.005 . 225 . 39 PRO HB3 H 1.858 0.002 . 226 . 39 PRO HG2 H 2.084 0.001 . 227 . 39 PRO HD2 H 3.791 0.006 . 228 . 39 PRO HD3 H 3.686 0.005 . 229 . 40 LEU N N 121.573 0.001 . 230 . 40 LEU H H 7.554 0.001 . 231 . 40 LEU HA H 4.835 0.003 . 232 . 40 LEU HB2 H 1.533 0.005 . 233 . 40 LEU HB3 H 1.450 0.009 . 234 . 40 LEU HG H 1.752 0.007 . 235 . 40 LEU HD1 H 0.924 0.008 . 236 . 40 LEU HD2 H 0.702 0.008 . 237 . 41 PRO HA H 4.407 0.004 . 238 . 41 PRO HB2 H 2.243 0.006 . 239 . 41 PRO HB3 H 1.839 0.002 . 240 . 41 PRO HG2 H 2.121 0.001 . 241 . 41 PRO HG3 H 1.536 0.006 . 242 . 41 PRO HD2 H 3.905 0.006 . 243 . 41 PRO HD3 H 3.788 0.010 . 244 . 42 GLU N N 113.213 0.005 . 245 . 42 GLU H H 6.981 0.005 . 246 . 42 GLU HA H 4.404 0.004 . 247 . 42 GLU HB2 H 1.830 0.008 . 248 . 42 GLU HG2 H 2.054 0.009 . 249 . 42 GLU HG3 H 2.013 0.006 . 250 . 43 ILE N N 124.243 0.002 . 251 . 43 ILE H H 8.657 0.002 . 252 . 43 ILE HA H 3.924 0.008 . 253 . 43 ILE HB H 1.776 0.007 . 254 . 43 ILE HG2 H 0.903 0.009 . 255 . 43 ILE HG12 H 1.589 0.005 . 256 . 43 ILE HG13 H 1.074 0.007 . 257 . 43 ILE HD1 H 0.779 0.005 . 258 . 44 PRO HA H 4.474 0.004 . 259 . 44 PRO HB2 H 2.325 0.009 . 260 . 44 PRO HB3 H 1.964 0.010 . 261 . 44 PRO HG2 H 1.837 0.008 . 262 . 44 PRO HG3 H 1.818 0.009 . 263 . 44 PRO HD2 H 3.674 0.004 . 264 . 44 PRO HD3 H 3.407 0.006 . 265 . 45 ASN N N 119.314 0.001 . 266 . 45 ASN ND2 N 112.216 0.001 . 267 . 45 ASN H H 8.533 0.001 . 268 . 45 ASN HA H 4.780 0.003 . 269 . 45 ASN HB2 H 2.772 0.004 . 270 . 45 ASN HD21 H 7.585 0.001 . 271 . 45 ASN HD22 H 6.877 0.010 . 272 . 46 GLY N N 110.254 0.007 . 273 . 46 GLY H H 8.090 0.007 . 274 . 46 GLY HA2 H 4.048 0.001 . 275 . 46 GLY HA3 H 3.984 0.002 . 276 . 47 GLU N N 121.768 0.005 . 277 . 47 GLU H H 8.373 0.005 . 278 . 47 GLU HA H 4.368 0.006 . 279 . 47 GLU HB2 H 1.984 0.006 . 280 . 47 GLU HB3 H 1.895 0.010 . 281 . 47 GLU HG2 H 2.233 0.007 . 282 . 48 TRP N N 126.773 0.004 . 283 . 48 TRP NE1 N 129.513 0.004 . 284 . 48 TRP H H 9.105 0.004 . 285 . 48 TRP HA H 4.535 0.004 . 286 . 48 TRP HB2 H 3.210 0.007 . 287 . 48 TRP HB3 H 2.962 0.009 . 288 . 48 TRP HD1 H 7.294 0.006 . 289 . 48 TRP HE3 H 7.286 0.008 . 290 . 48 TRP HE1 H 9.815 0.001 . 291 . 48 TRP HZ3 H 6.645 0.008 . 292 . 48 TRP HZ2 H 7.109 0.008 . 293 . 48 TRP HH2 H 6.511 0.008 . 294 . 49 LEU N N 127.291 0.008 . 295 . 49 LEU H H 6.847 0.008 . 296 . 49 LEU HA H 4.895 0.003 . 297 . 49 LEU HB2 H 1.178 0.009 . 298 . 49 LEU HB3 H 0.880 0.009 . 299 . 49 LEU HG H 1.582 0.008 . 300 . 49 LEU HD1 H 0.817 0.011 . 301 . 49 LEU HD2 H 0.742 0.009 . 302 . 50 CYS N N 126.871 0.005 . 303 . 50 CYS H H 9.087 0.005 . 304 . 50 CYS HA H 3.469 0.007 . 305 . 50 CYS HB2 H 3.321 0.009 . 306 . 50 CYS HB3 H 2.428 0.006 . 307 . 51 PRO HA H 4.184 0.005 . 308 . 51 PRO HB2 H 2.451 0.005 . 309 . 51 PRO HB3 H 1.951 0.002 . 310 . 51 PRO HG2 H 2.070 0.001 . 311 . 51 PRO HG3 H 1.919 0.014 . 312 . 51 PRO HD2 H 3.642 0.002 . 313 . 51 PRO HD3 H 3.510 0.009 . 314 . 52 ARG N N 118.138 0.002 . 315 . 52 ARG H H 8.363 0.002 . 316 . 52 ARG HA H 4.186 0.003 . 317 . 52 ARG HB2 H 2.402 0.012 . 318 . 52 ARG HB3 H 1.831 0.009 . 319 . 52 ARG HG2 H 1.922 0.014 . 320 . 52 ARG HG3 H 1.784 0.011 . 321 . 52 ARG HD2 H 3.342 0.008 . 322 . 52 ARG HD3 H 3.205 0.007 . 323 . 53 CYS N N 121.987 0.006 . 324 . 53 CYS H H 8.001 0.006 . 325 . 53 CYS HA H 4.020 0.006 . 326 . 53 CYS HB2 H 2.833 0.004 . 327 . 53 CYS HB3 H 2.627 0.006 . 328 . 54 THR N N 111.930 0.007 . 329 . 54 THR H H 7.649 0.007 . 330 . 54 THR HA H 4.005 0.003 . 331 . 54 THR HB H 4.050 0.003 . 332 . 54 THR HG2 H 1.004 0.007 . 333 . 55 CYS N N 122.698 0.001 . 334 . 55 CYS H H 7.666 0.001 . 335 . 55 CYS HA H 4.753 0.004 . 336 . 55 CYS HB2 H 2.912 0.007 . 337 . 56 PRO HA H 4.388 0.002 . 338 . 56 PRO HB2 H 2.301 0.004 . 339 . 56 PRO HB3 H 2.014 0.002 . 340 . 56 PRO HG2 H 1.965 0.010 . 341 . 56 PRO HG3 H 1.924 0.007 . 342 . 56 PRO HD2 H 3.745 0.007 . 343 . 57 ALA N N 123.105 0.010 . 344 . 57 ALA H H 8.259 0.010 . 345 . 57 ALA HA H 4.285 0.002 . 346 . 57 ALA HB H 1.386 0.006 . 347 . 58 LEU N N 120.576 0.001 . 348 . 58 LEU H H 8.045 0.001 . 349 . 58 LEU HA H 4.339 0.003 . 350 . 58 LEU HB2 H 1.684 0.008 . 351 . 58 LEU HB3 H 1.592 0.008 . 352 . 58 LEU HG H 1.614 0.011 . 353 . 58 LEU HD1 H 0.928 0.010 . 354 . 58 LEU HD2 H 0.869 0.009 . 355 . 59 LYS N N 121.843 0.010 . 356 . 59 LYS H H 8.094 0.010 . 357 . 59 LYS HA H 4.301 0.010 . 358 . 59 LYS HB2 H 1.857 0.007 . 359 . 59 LYS HB3 H 1.675 0.005 . 360 . 59 LYS HG2 H 1.399 0.010 . 361 . 59 LYS HD2 H 1.592 0.010 . 362 . 60 GLY N N 110.323 0.001 . 363 . 60 GLY H H 8.409 0.001 . 364 . 60 GLY HA2 H 3.960 0.003 . 365 . 61 LYS N N 126.105 0.007 . 366 . 61 LYS H H 7.794 0.007 . 367 . 61 LYS HA H 4.191 0.001 . 368 . 61 LYS HB2 H 1.838 0.013 . 369 . 61 LYS HB3 H 1.741 0.014 . 370 . 61 LYS HG2 H 1.389 0.010 . 371 . 61 LYS HD2 H 1.709 0.014 . stop_ save_