data_16088 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Apo Pin1 WW Domain ; _BMRB_accession_number 16088 _BMRB_flat_file_name bmr16088.str _Entry_type new _Submission_date 2008-12-23 _Accession_date 2008-12-23 _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 Jennifer A. . 2 Liu Kai . . 3 Kelly Jeffery W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 184 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-02 update BMRB 'edit assembly name' 2009-03-06 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11786999 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kowalski Jennifer A. . 2 Liu Kai . . 3 Kelly Jeffery W. . stop_ _Journal_abbreviation Biopolymers _Journal_volume 63 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 111 _Page_last 121 _Year 2002 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Pin1_WW _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Pin1_WW $Pin1_WW stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Pin1_WW _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Pin1_WW _Molecular_mass 4174.678 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 36 _Mol_residue_sequence ; GSKLPPGWEKRMSRSSGRVY YFNHITNASQWERPSG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 LYS 4 LEU 5 PRO 6 PRO 7 GLY 8 TRP 9 GLU 10 LYS 11 ARG 12 MET 13 SER 14 ARG 15 SER 16 SER 17 GLY 18 ARG 19 VAL 20 TYR 21 TYR 22 PHE 23 ASN 24 HIS 25 ILE 26 THR 27 ASN 28 ALA 29 SER 30 GLN 31 TRP 32 GLU 33 ARG 34 PRO 35 SER 36 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-04 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 16070 Pin1_WW 100.00 36 100.00 100.00 6.79e-17 BMRB 17545 "first domain of human PIN1" 94.44 36 100.00 100.00 1.16e-15 BMRB 19258 entity 94.44 43 100.00 100.00 7.85e-16 BMRB 19259 Pin1 94.44 43 97.06 97.06 2.54e-15 BMRB 25569 Pin1 91.67 33 100.00 100.00 6.38e-15 PDB 1F8A "Structural Basis For The Phosphoserine-proline Recognition By Group Iv Ww Domains" 94.44 167 100.00 100.00 1.22e-15 PDB 1I6C "Solution Structure Of Pin1 Ww Domain" 94.44 39 100.00 100.00 1.02e-15 PDB 1I8G "Solution Structure Of Pin1 Ww Domain Complexed With Cdc25 Phosphothreonine Peptide" 94.44 39 100.00 100.00 1.02e-15 PDB 1I8H "Solution Structure Of Pin1 Ww Domain Complexed With Human Tau Phosphothreonine Peptide" 94.44 39 100.00 100.00 1.02e-15 PDB 1NMV "Solution Structure Of Human Pin1" 94.44 163 100.00 100.00 1.01e-15 PDB 1PIN "Pin1 Peptidyl-prolyl Cis-trans Isomerase From Homo Sapiens" 94.44 163 100.00 100.00 1.01e-15 PDB 2ITK "Human Pin1 Bound To D-Peptide" 94.44 167 97.06 97.06 1.01e-14 PDB 2KCF "The Nmr Solution Structure Of The Isolated Apo Pin1 Ww Domain" 100.00 36 100.00 100.00 6.79e-17 PDB 2LB3 "Structure Of The Ww Domain Of Pin1 In Complex With A Human Phosphorylated Smad3 Derived Peptide" 94.44 36 100.00 100.00 1.16e-15 PDB 2M8I "Structure Of Pin1 Ww Domain" 94.44 43 100.00 100.00 7.85e-16 PDB 2M8J "Structure Of Pin1 Ww Domain Phospho-mimic S16e" 94.44 43 97.06 97.06 2.54e-15 PDB 2Q5A "Human Pin1 Bound To L-Peptide" 94.44 167 97.06 97.06 1.01e-14 PDB 2XP3 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2XP4 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2XP5 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2XP6 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 9.81e-15 PDB 2XP7 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2XP8 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2XP9 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2XPA "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2XPB "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 2ZQS "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 94.44 163 100.00 100.00 9.57e-16 PDB 2ZQT "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 94.44 163 100.00 100.00 1.05e-15 PDB 2ZQU "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 94.44 163 97.06 97.06 2.36e-14 PDB 2ZQV "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 94.44 163 97.06 97.06 1.59e-14 PDB 2ZR4 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 94.44 163 97.06 100.00 2.29e-15 PDB 2ZR5 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 94.44 163 100.00 100.00 1.06e-15 PDB 2ZR6 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 94.44 163 97.06 97.06 9.19e-15 PDB 3KAB "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 94.44 167 97.06 97.06 1.01e-14 PDB 3KAD "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 94.44 167 97.06 97.06 9.81e-15 PDB 3KAF "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 94.44 167 97.06 97.06 9.81e-15 PDB 3KAG "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 94.44 167 97.06 97.06 1.01e-14 PDB 3KAH "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 94.44 167 97.06 97.06 1.01e-14 PDB 3KAI "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 94.44 167 97.06 97.06 1.01e-14 PDB 3KCE "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 94.44 167 97.06 97.06 1.01e-14 PDB 3NTP "Human Pin1 Complexed With Reduced Amide Inhibitor" 94.44 167 97.06 97.06 1.01e-14 PDB 3ODK "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 94.44 167 97.06 97.06 1.01e-14 PDB 3OOB "Structural And Functional Insights Of Directly Targeting Pin1 By Epigallocatechin-3-Gallate" 94.44 163 97.06 97.06 9.19e-15 PDB 3TC5 "Selective Targeting Of Disease-Relevant Protein Binding Domains By O- Phosphorylated Natural Product Derivatives" 94.44 166 97.06 97.06 9.48e-15 PDB 3TCZ "Human Pin1 Bound To Cis Peptidomimetic Inhibitor" 94.44 158 97.06 97.06 1.00e-14 PDB 3TDB "Human Pin1 Bound To Trans Peptidomimetic Inhibitor" 94.44 158 97.06 97.06 1.00e-14 PDB 3WH0 "Structure Of Pin1 Complex With 18-crown-6" 94.44 163 97.06 97.06 9.19e-15 PDB 4GWT "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Dl-malic Acid" 100.00 36 100.00 100.00 6.79e-17 PDB 4GWV "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Tri-ammonium Citrate" 100.00 36 100.00 100.00 6.79e-17 PDB 4QIB "Oxidation-mediated Inhibition Of The Peptidyl-prolyl Isomerase Pin1" 91.67 159 96.97 96.97 4.46e-14 PDB 4U84 "Human Pin1 With S-hydroxyl-cysteine 113" 94.44 181 97.06 97.06 1.34e-14 PDB 4U85 "Human Pin1 With Cysteine Sulfinic Acid 113" 94.44 181 97.06 97.06 1.34e-14 PDB 4U86 "Human Pin1 With Cysteine Sulfonic Acid 113" 94.44 181 97.06 97.06 1.34e-14 DBJ BAA87037 "PIN1 [Mus sp.]" 88.89 165 100.00 100.00 2.42e-14 DBJ BAA87038 "PIN1 [Mus sp.]" 88.89 165 100.00 100.00 2.42e-14 DBJ BAB22270 "unnamed protein product [Mus musculus]" 88.89 165 100.00 100.00 2.42e-14 DBJ BAB22743 "unnamed protein product [Mus musculus]" 88.89 165 100.00 100.00 2.42e-14 DBJ BAC35631 "unnamed protein product [Mus musculus]" 88.89 165 100.00 100.00 2.42e-14 EMBL CAG28582 "UBL5 [Homo sapiens]" 94.44 163 100.00 100.00 1.01e-15 GB AAC50492 "Pin1 [Homo sapiens]" 94.44 163 100.00 100.00 1.01e-15 GB AAH02899 "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens]" 94.44 163 100.00 100.00 1.01e-15 GB AAH38254 "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Mus musculus]" 88.89 165 100.00 100.00 2.42e-14 GB AAH59553 "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Danio rerio]" 94.44 159 97.06 97.06 9.25e-15 GB AAI12584 "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Bos taurus]" 94.44 163 100.00 100.00 1.01e-15 PRF 2209428A "peptidyl-Pro isomerase" 94.44 163 100.00 100.00 1.01e-15 REF NP_001029804 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" 94.44 163 100.00 100.00 1.01e-15 REF NP_001231300 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Sus scrofa]" 94.44 163 100.00 100.00 1.07e-15 REF NP_001270625 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca fascicularis]" 94.44 163 97.06 97.06 7.40e-15 REF NP_006212 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Homo sapiens]" 94.44 163 100.00 100.00 1.01e-15 REF NP_075860 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Mus musculus]" 88.89 165 100.00 100.00 2.42e-14 SP Q13526 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 94.44 163 100.00 100.00 1.01e-15 SP Q4R383 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 94.44 163 97.06 97.06 7.40e-15 SP Q5BIN5 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 94.44 163 100.00 100.00 1.01e-15 SP Q9QUR7 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 88.89 165 100.00 100.00 2.42e-14 TPG DAA28013 "TPA: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" 94.44 163 100.00 100.00 1.01e-15 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Pin1_WW 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 $Pin1_WW 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'pH 6.2' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Pin1_WW . mM 1.0 1.2 'natural abundance' 'potassium phosphate' 50 mM . . 'natural abundance' 'sodium azide' 0.02 %v/v . . 'natural abundance' DSS trace % . . 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'pH 6.2' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Pin1_WW . mM 1.0 1.2 'natural abundance' 'potassium phosphate' 50 mM . . 'natural abundance' 'sodium azide' 0.02 %v/v . . 'natural abundance' DSS trace % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_PROSA _Saveframe_category software _Name PROSA _Version . loop_ _Vendor _Address _Electronic_address Guntert . . stop_ loop_ _Task processing stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_GARANT _Saveframe_category software _Name GARANT _Version . loop_ _Vendor _Address _Electronic_address 'Bartels, Guntert, Billeter and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_AMBER _Saveframe_category software _Name AMBER _Version OPAL loop_ _Vendor _Address _Electronic_address 'Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_DYANA _Saveframe_category software _Name DYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Braun and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_DQF-COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_DQF-COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D DQF-COSY' _Sample_label $sample_2 save_ save_2D_1H-1H_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 278 . K pH 6.2 . pH pressure 1.0 . atm 'ionic strength' 0 . M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $GARANT stop_ loop_ _Experiment_label '2D DQF-COSY' '2D 1H-1H TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name Pin1_WW _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 4 LEU H H 8.811 0.060 . 2 4 4 LEU HA H 4.574 0.043 . 3 4 4 LEU HD1 H 0.825 0.004 1 4 4 4 LEU HD2 H 1.110 0.005 1 5 4 4 LEU HG H 1.452 0.010 . 6 5 5 PRO HA H 4.891 0.006 . 7 5 5 PRO HB2 H 2.039 0.006 . 8 5 5 PRO HB3 H 2.647 0.003 . 9 5 5 PRO HD2 H 3.057 0.012 . 10 5 5 PRO HD3 H 3.726 0.014 . 11 5 5 PRO HG2 H 1.682 0.006 . 12 5 5 PRO HG3 H 1.818 0.004 . 13 6 6 PRO HA H 4.392 0.007 . 14 6 6 PRO HB2 H 1.901 0.005 . 15 6 6 PRO HB3 H 2.370 0.006 . 16 6 6 PRO HD2 H 3.676 0.010 . 17 6 6 PRO HD3 H 3.962 0.005 . 18 6 6 PRO HG2 H 2.090 0.010 . 19 6 6 PRO HG3 H 2.192 0.008 . 20 7 7 GLY H H 8.900 0.007 . 21 7 7 GLY HA2 H 3.288 0.010 . 22 7 7 GLY HA3 H 4.070 0.009 . 23 8 8 TRP H H 7.411 0.011 . 24 8 8 TRP HA H 5.274 0.009 . 25 8 8 TRP HB2 H 3.286 0.006 . 26 8 8 TRP HB3 H 2.996 0.010 . 27 8 8 TRP HD1 H 6.993 0.007 . 28 8 8 TRP HE1 H 10.714 0.005 . 29 8 8 TRP HE3 H 7.408 0.008 . 30 8 8 TRP HH2 H 7.037 0.010 . 31 8 8 TRP HZ2 H 7.469 0.009 . 32 8 8 TRP HZ3 H 6.981 0.009 . 33 9 9 GLU H H 9.849 0.003 . 34 9 9 GLU HA H 4.875 0.009 . 35 9 9 GLU HG2 H 2.352 0.007 . 36 9 9 GLU HG3 H 2.574 0.004 . 37 10 10 LYS H H 9.066 0.009 . 38 10 10 LYS HA H 4.413 0.023 . 39 11 11 ARG H H 8.953 0.007 . 40 11 11 ARG HA H 4.464 0.002 . 41 11 11 ARG HB2 H 0.110 0.006 . 42 11 11 ARG HB3 H 1.319 0.004 . 43 11 11 ARG HD2 H 2.665 0.009 . 44 11 11 ARG HD3 H 2.913 0.005 . 45 11 11 ARG HE H 7.017 0.008 . 46 11 11 ARG HG2 H 1.267 0.003 . 47 11 11 ARG HG3 H 1.413 0.013 . 48 11 11 ARG HH11 H 6.233 0.006 . 49 11 11 ARG HH12 H 6.233 0.006 . 50 11 11 ARG HH21 H 6.367 0.007 . 51 11 11 ARG HH22 H 6.367 0.007 . 52 12 12 MET H H 8.342 0.004 . 53 12 12 MET HA H 4.993 0.005 . 54 12 12 MET HG2 H 2.277 0.007 . 55 12 12 MET HG3 H 2.458 0.007 . 56 13 13 SER H H 9.131 0.005 . 57 13 13 SER HA H 4.887 0.002 . 58 13 13 SER HB2 H 4.310 0.011 . 59 13 13 SER HB3 H 4.228 0.009 . 60 14 14 ARG H H 10.000 0.040 . 61 14 14 ARG HA H 4.162 0.009 . 62 14 14 ARG HE H 7.765 0.029 . 63 15 15 SER H H 8.784 0.012 . 64 15 15 SER HA H 4.374 0.013 . 65 15 15 SER HB3 H 3.939 0.005 . 66 16 16 SER H H 8.333 0.005 . 67 16 16 SER HA H 4.312 0.005 . 68 16 16 SER HB2 H 3.753 0.012 . 69 16 16 SER HB3 H 3.823 0.007 . 70 17 17 GLY H H 8.146 0.015 . 71 17 17 GLY HA2 H 4.152 0.007 . 72 17 17 GLY HA3 H 3.978 0.009 . 73 18 18 ARG H H 7.743 0.003 . 74 18 18 ARG HA H 4.486 0.010 . 75 18 18 ARG HB2 H 1.774 0.005 . 76 18 18 ARG HB3 H 2.007 0.008 . 77 18 18 ARG HD2 H 2.511 0.010 . 78 18 18 ARG HD3 H 2.853 0.009 . 79 18 18 ARG HE H 6.816 0.010 . 80 18 18 ARG HH11 H 6.007 0.004 . 81 18 18 ARG HH12 H 6.007 0.004 . 82 18 18 ARG HH21 H 6.127 0.004 . 83 18 18 ARG HH22 H 6.127 0.004 . 84 19 19 VAL H H 8.681 0.006 . 85 19 19 VAL HA H 4.708 0.007 . 86 19 19 VAL HB H 2.026 0.003 . 87 19 19 VAL HG1 H 0.841 0.006 1 88 19 19 VAL HG2 H 1.089 0.008 1 89 20 20 TYR H H 8.761 0.008 . 90 20 20 TYR HA H 4.936 0.006 . 91 20 20 TYR HB2 H 2.569 0.004 . 92 20 20 TYR HB3 H 3.013 0.014 . 93 20 20 TYR HD1 H 6.924 0.006 . 94 20 20 TYR HD2 H 8.199 0.002 . 95 20 20 TYR HE1 H 6.468 0.004 . 96 20 20 TYR HE2 H 6.939 0.011 . 97 21 21 TYR H H 9.100 0.006 . 98 21 21 TYR HA H 5.302 0.007 . 99 21 21 TYR HB2 H 2.921 0.007 . 100 21 21 TYR HB3 H 2.678 0.012 . 101 21 21 TYR HD1 H 6.853 0.007 . 102 21 21 TYR HE1 H 6.790 0.006 . 103 21 21 TYR HE2 H 7.529 0.000 . 104 22 22 PHE H H 9.451 0.009 . 105 22 22 PHE HA H 5.687 0.009 . 106 22 22 PHE HB2 H 2.593 0.009 . 107 22 22 PHE HB3 H 2.955 0.005 . 108 22 22 PHE HZ H 7.340 0.009 . 109 23 23 ASN H H 8.267 0.009 . 110 23 23 ASN HA H 4.392 0.006 . 111 23 23 ASN HB2 H 2.026 0.009 . 112 23 23 ASN HB3 H -0.682 0.010 . 113 23 23 ASN HD21 H 6.668 0.004 . 114 23 23 ASN HD22 H 4.223 0.002 . 115 24 24 HIS H H 8.238 0.004 . 116 24 24 HIS HA H 4.174 0.014 . 117 24 24 HIS HB2 H 3.415 0.020 . 118 24 24 HIS HB3 H 3.158 0.009 . 119 24 24 HIS HD1 H 7.168 0.011 . 120 24 24 HIS HD2 H 7.129 0.056 . 121 24 24 HIS HE1 H 8.299 0.038 . 122 25 25 ILE H H 8.415 0.007 . 123 25 25 ILE HA H 3.864 0.009 . 124 25 25 ILE HB H 2.029 0.006 . 125 25 25 ILE HD1 H 0.753 0.007 1 126 25 25 ILE HG12 H 1.286 0.004 . 127 25 25 ILE HG13 H 0.988 0.010 . 128 25 25 ILE HG2 H 0.790 0.006 1 129 26 26 THR H H 7.372 0.005 . 130 26 26 THR HA H 4.117 0.007 . 131 26 26 THR HB H 4.261 0.008 . 132 26 26 THR HG2 H 0.959 0.004 1 133 27 27 ASN H H 8.111 0.007 . 134 27 27 ASN HA H 4.157 0.007 . 135 27 27 ASN HB2 H 2.943 0.007 . 136 27 27 ASN HB3 H 3.161 0.009 . 137 27 27 ASN HD21 H 6.947 0.000 . 138 27 27 ASN HD22 H 7.583 0.000 . 139 28 28 ALA H H 7.173 0.006 . 140 28 28 ALA HA H 4.460 0.009 . 141 28 28 ALA HB H 1.267 0.005 1 142 29 29 SER H H 8.440 0.006 . 143 29 29 SER HA H 6.071 0.004 . 144 29 29 SER HB2 H 3.742 0.003 . 145 29 29 SER HB3 H 3.838 0.009 . 146 30 30 GLN H H 9.428 0.006 . 147 30 30 GLN HA H 4.865 0.011 . 148 30 30 GLN HB2 H 2.234 0.006 . 149 30 30 GLN HB3 H 2.536 0.011 . 150 30 30 GLN HE21 H 6.788 0.001 . 151 30 30 GLN HE22 H 7.517 0.000 . 152 31 31 TRP H H 8.494 0.014 . 153 31 31 TRP HA H 5.002 0.007 . 154 31 31 TRP HB2 H 3.217 0.006 . 155 31 31 TRP HB3 H 3.642 0.007 . 156 31 31 TRP HD1 H 7.504 0.005 . 157 31 31 TRP HE1 H 10.211 0.004 . 158 31 31 TRP HE3 H 8.198 0.004 . 159 31 31 TRP HH2 H 7.114 0.006 . 160 31 31 TRP HZ2 H 7.399 0.004 . 161 31 31 TRP HZ3 H 6.938 0.007 . 162 32 32 GLU H H 8.156 0.005 . 163 32 32 GLU HA H 4.422 0.013 . 164 32 32 GLU HG2 H 2.272 0.008 . 165 32 32 GLU HG3 H 2.349 0.014 . 166 33 33 ARG H H 8.677 0.003 . 167 33 33 ARG HA H 2.627 0.009 . 168 33 33 ARG HE H 7.465 0.021 . 169 33 33 ARG HG2 H 0.914 0.018 . 170 33 33 ARG HG3 H 1.224 0.008 . 171 34 34 PRO HA H 3.938 0.009 . 172 34 34 PRO HB2 H 0.789 0.008 . 173 34 34 PRO HB3 H 0.897 0.014 . 174 34 34 PRO HD2 H 2.515 0.009 . 175 34 34 PRO HD3 H 2.300 0.010 . 176 34 34 PRO HG2 H -0.070 0.003 . 177 34 34 PRO HG3 H 0.567 0.045 . 178 35 35 SER H H 8.070 0.005 . 179 35 35 SER HA H 4.711 0.005 . 180 35 35 SER HB2 H 3.894 0.016 . 181 35 35 SER HB3 H 4.019 0.007 . 182 36 36 GLY H H 8.059 0.009 . 183 36 36 GLY HA2 H 3.830 0.016 . 184 36 36 GLY HA3 H 3.745 0.007 . stop_ save_