data_4882 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H NMR Study on the Binding of Pin1 Trp-trp domain with Phosphothreonine Peptides ; _BMRB_accession_number 4882 _BMRB_flat_file_name bmr4882.str _Entry_type original _Submission_date 2000-10-25 _Accession_date 2000-10-25 _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 Wintjens Rene . . 2 Wieruszeski Jean-Michel . . 3 Drobecq Herve . . 4 Rousselot-Pailley Pierre . . 5 Lippens Guy . . 6 Landrieu Isabelle . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 242 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-11 original author . stop_ _Original_release_date 2001-07-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title '1H NMR Study on the Binding of Pin1 Trp-trp domain with Phosphothreonine Peptides' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21326075 _PubMed_ID 11313338 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wintjens Rene . . 2 Wieruszeski Jean-Michel . . 3 Drobecq Herve . . 4 Rousselot-Pailley Pierre . . 5 Buee L. . . 6 Lippens Guy . . 7 Landrieu Isabelle . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 276 _Journal_issue 27 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 25150 _Page_last 25156 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_WW_domain _Saveframe_category molecular_system _Mol_system_name 'Pin1 WW domain' _Abbreviation_common 'WW domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'WW domain' $WW_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_WW_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Pin1 WW domain' _Abbreviation_common 'WW domain' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 39 _Mol_residue_sequence ; KLPPGWEKRMSRSSGRVYYF NHITNASQWERPSGNSSSG ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 LEU 3 PRO 4 PRO 5 GLY 6 TRP 7 GLU 8 LYS 9 ARG 10 MET 11 SER 12 ARG 13 SER 14 SER 15 GLY 16 ARG 17 VAL 18 TYR 19 TYR 20 PHE 21 ASN 22 HIS 23 ILE 24 THR 25 ASN 26 ALA 27 SER 28 GLN 29 TRP 30 GLU 31 ARG 32 PRO 33 SER 34 GLY 35 ASN 36 SER 37 SER 38 SER 39 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 87.18 36 100.00 100.00 7.70e-16 BMRB 16088 Pin1_WW 87.18 36 100.00 100.00 7.70e-16 BMRB 17545 "first domain of human PIN1" 92.31 36 100.00 100.00 3.89e-17 BMRB 19258 entity 87.18 43 100.00 100.00 4.74e-16 BMRB 19259 Pin1 87.18 43 97.06 97.06 1.42e-15 BMRB 5248 Pin1_WW_Domain 87.18 39 100.00 100.00 4.35e-16 BMRB 5305 Pin1 100.00 183 100.00 100.00 1.14e-18 PDB 1F8A "Structural Basis For The Phosphoserine-proline Recognition By Group Iv Ww Domains" 100.00 167 100.00 100.00 7.94e-19 PDB 1I6C "Solution Structure Of Pin1 Ww Domain" 100.00 39 100.00 100.00 7.73e-19 PDB 1I8G "Solution Structure Of Pin1 Ww Domain Complexed With Cdc25 Phosphothreonine Peptide" 100.00 39 100.00 100.00 7.73e-19 PDB 1I8H "Solution Structure Of Pin1 Ww Domain Complexed With Human Tau Phosphothreonine Peptide" 100.00 39 100.00 100.00 7.73e-19 PDB 1NMV "Solution Structure Of Human Pin1" 100.00 163 100.00 100.00 6.93e-19 PDB 1PIN "Pin1 Peptidyl-prolyl Cis-trans Isomerase From Homo Sapiens" 100.00 163 100.00 100.00 6.93e-19 PDB 2ITK "Human Pin1 Bound To D-Peptide" 100.00 167 97.44 97.44 6.83e-18 PDB 2KCF "The Nmr Solution Structure Of The Isolated Apo Pin1 Ww Domain" 87.18 36 100.00 100.00 7.70e-16 PDB 2LB3 "Structure Of The Ww Domain Of Pin1 In Complex With A Human Phosphorylated Smad3 Derived Peptide" 92.31 36 100.00 100.00 3.89e-17 PDB 2M8I "Structure Of Pin1 Ww Domain" 87.18 43 100.00 100.00 4.74e-16 PDB 2M8J "Structure Of Pin1 Ww Domain Phospho-mimic S16e" 87.18 43 97.06 97.06 1.42e-15 PDB 2Q5A "Human Pin1 Bound To L-Peptide" 100.00 167 97.44 97.44 6.83e-18 PDB 2XP3 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2XP4 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2XP5 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2XP6 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.28e-18 PDB 2XP7 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2XP8 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2XP9 "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2XPA "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2XPB "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 2ZQS "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 100.00 163 100.00 100.00 6.37e-19 PDB 2ZQT "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 100.00 163 100.00 100.00 6.44e-19 PDB 2ZQU "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 100.00 163 97.44 97.44 1.51e-17 PDB 2ZQV "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 100.00 163 97.44 97.44 1.15e-17 PDB 2ZR4 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 100.00 163 97.44 100.00 1.32e-18 PDB 2ZR5 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 100.00 163 100.00 100.00 6.78e-19 PDB 2ZR6 "Crystal Structure Of A Mutant Pin1 Peptidyl-Prolyl Cis-Trans Isomerase" 100.00 163 97.44 97.44 5.98e-18 PDB 3KAB "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 100.00 167 97.44 97.44 6.83e-18 PDB 3KAD "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 100.00 167 97.44 97.44 6.28e-18 PDB 3KAF "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 100.00 167 97.44 97.44 6.28e-18 PDB 3KAG "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 100.00 167 97.44 97.44 6.83e-18 PDB 3KAH "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 100.00 167 97.44 97.44 6.83e-18 PDB 3KAI "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 100.00 167 97.44 97.44 6.83e-18 PDB 3KCE "Structure-Guided Design Of Alpha-Amino Acid-Derived Pin1 Inhibitors" 100.00 167 97.44 97.44 6.83e-18 PDB 3NTP "Human Pin1 Complexed With Reduced Amide Inhibitor" 100.00 167 97.44 97.44 6.83e-18 PDB 3ODK "Discovery Of Cell-Active Phenyl-Imidazole Pin1 Inhibitors By Structure-Guided Fragment Evolution" 100.00 167 97.44 97.44 6.83e-18 PDB 3OOB "Structural And Functional Insights Of Directly Targeting Pin1 By Epigallocatechin-3-Gallate" 100.00 163 97.44 97.44 5.98e-18 PDB 3TC5 "Selective Targeting Of Disease-Relevant Protein Binding Domains By O- Phosphorylated Natural Product Derivatives" 100.00 166 97.44 97.44 6.44e-18 PDB 3TCZ "Human Pin1 Bound To Cis Peptidomimetic Inhibitor" 100.00 158 97.44 97.44 6.41e-18 PDB 3TDB "Human Pin1 Bound To Trans Peptidomimetic Inhibitor" 100.00 158 97.44 97.44 6.41e-18 PDB 3WH0 "Structure Of Pin1 Complex With 18-crown-6" 100.00 163 97.44 97.44 5.98e-18 PDB 4GWT "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Dl-malic Acid" 87.18 36 100.00 100.00 7.70e-16 PDB 4GWV "Structure Of Racemic Pin1 Ww Domain Cocrystallized With Tri-ammonium Citrate" 87.18 36 100.00 100.00 7.70e-16 DBJ BAA87037 "PIN1 [Mus sp.]" 82.05 165 100.00 100.00 1.43e-14 DBJ BAA87038 "PIN1 [Mus sp.]" 82.05 165 100.00 100.00 1.43e-14 DBJ BAB22270 "unnamed protein product [Mus musculus]" 82.05 165 100.00 100.00 1.43e-14 DBJ BAB22743 "unnamed protein product [Mus musculus]" 82.05 165 100.00 100.00 1.43e-14 DBJ BAC35631 "unnamed protein product [Mus musculus]" 82.05 165 100.00 100.00 1.43e-14 EMBL CAG28582 "UBL5 [Homo sapiens]" 100.00 163 100.00 100.00 6.93e-19 GB AAC50492 "Pin1 [Homo sapiens]" 100.00 163 100.00 100.00 6.93e-19 GB AAH02899 "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Homo sapiens]" 100.00 163 100.00 100.00 6.93e-19 GB AAH38254 "Protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Mus musculus]" 82.05 165 100.00 100.00 1.43e-14 GB AAI12584 "Peptidylprolyl cis/trans isomerase, NIMA-interacting 1 [Bos taurus]" 94.87 163 100.00 100.00 1.22e-17 GB AAV38138 "protein (peptidyl-prolyl cis/trans isomerase) NIMA-interacting 1 [Homo sapiens]" 100.00 163 100.00 100.00 6.93e-19 PRF 2209428A "peptidyl-Pro isomerase" 100.00 163 100.00 100.00 6.93e-19 REF NP_001029804 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" 94.87 163 100.00 100.00 1.22e-17 REF NP_001231300 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Sus scrofa]" 100.00 163 97.44 97.44 2.81e-18 REF NP_001270625 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Macaca fascicularis]" 100.00 163 97.44 97.44 4.85e-18 REF NP_006212 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Homo sapiens]" 100.00 163 100.00 100.00 6.93e-19 REF NP_075860 "peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Mus musculus]" 82.05 165 100.00 100.00 1.43e-14 SP Q13526 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 100.00 163 100.00 100.00 6.93e-19 SP Q4R383 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 100.00 163 97.44 97.44 4.85e-18 SP Q5BIN5 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 94.87 163 100.00 100.00 1.22e-17 SP Q9QUR7 "RecName: Full=Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; AltName: Full=Peptidyl-prolyl cis-trans isomerase Pin1; S" 82.05 165 100.00 100.00 1.43e-14 TPG DAA28013 "TPA: peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Bos taurus]" 94.87 163 100.00 100.00 1.22e-17 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $WW_domain 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 $WW_domain 'chemical synthesis' . . . . . 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 $WW_domain 1.0 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H_TOCY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCY' _Sample_label . save_ save_1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H TOCY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pD 6.4 0.1 n/a temperature 285 1 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 TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal . 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H TOCY' '1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'WW domain' _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 LYS HA H 4.18 0.02 1 2 . 1 LYS HB2 H 1.99 0.02 1 3 . 1 LYS HB3 H 1.99 0.02 1 4 . 1 LYS HG2 H 1.54 0.02 1 5 . 1 LYS HG3 H 1.61 0.02 1 6 . 1 LYS HD2 H 1.80 0.02 1 7 . 1 LYS HD3 H 1.80 0.02 1 8 . 1 LYS HE2 H 3.10 0.02 1 9 . 1 LYS HE3 H 3.10 0.02 1 10 . 2 LEU H H 8.86 0.02 1 11 . 2 LEU HA H 4.67 0.02 1 12 . 2 LEU HB2 H 1.89 0.02 1 13 . 2 LEU HB3 H 1.49 0.02 1 14 . 2 LEU HG H 2.00 0.02 1 15 . 2 LEU HD1 H 1.13 0.02 1 16 . 2 LEU HD2 H 0.86 0.02 1 17 . 3 PRO HA H 4.66 0.02 1 18 . 3 PRO HB2 H 2.67 0.02 1 19 . 3 PRO HB3 H 2.67 0.02 1 20 . 3 PRO HG2 H 1.86 0.02 1 21 . 3 PRO HG3 H 1.72 0.02 1 22 . 3 PRO HD2 H 3.75 0.02 1 23 . 3 PRO HD3 H 3.09 0.02 1 24 . 4 PRO HA H 4.42 0.02 1 25 . 4 PRO HB2 H 2.39 0.02 1 26 . 4 PRO HB3 H 1.91 0.02 1 27 . 4 PRO HG2 H 2.10 0.02 1 28 . 4 PRO HG3 H 2.20 0.02 1 29 . 4 PRO HD2 H 3.71 0.02 1 30 . 4 PRO HD3 H 3.99 0.02 1 31 . 5 GLY H H 8.83 0.02 1 32 . 5 GLY HA2 H 4.09 0.02 1 33 . 5 GLY HA3 H 3.23 0.02 1 34 . 6 TRP H H 7.44 0.02 1 35 . 6 TRP HA H 5.24 0.02 1 36 . 6 TRP HB2 H 3.00 0.02 1 37 . 6 TRP HB3 H 3.28 0.02 1 38 . 6 TRP HD1 H 7.01 0.02 1 39 . 6 TRP HE1 H 10.57 0.02 1 40 . 6 TRP HE3 H 7.42 0.02 1 41 . 6 TRP HZ2 H 7.47 0.02 1 42 . 6 TRP HZ3 H 7.03 0.02 1 43 . 6 TRP HH2 H 7.05 0.02 1 44 . 7 GLU H H 9.83 0.02 1 45 . 7 GLU HA H 4.91 0.02 1 46 . 7 GLU HB2 H 2.28 0.02 1 47 . 7 GLU HB3 H 2.37 0.02 1 48 . 7 GLU HG2 H 2.62 0.02 1 49 . 7 GLU HG3 H 2.62 0.02 1 50 . 8 LYS H H 8.98 0.02 1 51 . 8 LYS HA H 4.45 0.02 1 52 . 8 LYS HB2 H 1.83 0.02 1 53 . 8 LYS HB3 H 1.83 0.02 1 54 . 8 LYS HG2 H 1.13 0.02 1 55 . 8 LYS HG3 H 1.13 0.02 1 56 . 8 LYS HD2 H 1.69 0.02 1 57 . 8 LYS HD3 H 1.69 0.02 1 58 . 8 LYS HE2 H 3.01 0.02 1 59 . 8 LYS HE3 H 3.01 0.02 1 60 . 9 ARG H H 8.90 0.02 1 61 . 9 ARG HA H 4.45 0.02 1 62 . 9 ARG HB2 H 0.10 0.02 1 63 . 9 ARG HB3 H 0.10 0.02 1 64 . 9 ARG HG2 H 1.29 0.02 1 65 . 9 ARG HG3 H 1.47 0.02 1 66 . 9 ARG HD2 H 2.98 0.02 1 67 . 9 ARG HD3 H 2.69 0.02 1 68 . 9 ARG HE H 7.02 0.02 1 69 . 10 MET H H 8.28 0.02 1 70 . 10 MET HA H 5.00 0.02 1 71 . 10 MET HB2 H 2.33 0.02 1 72 . 10 MET HB3 H 2.33 0.02 1 73 . 10 MET HG2 H 2.49 0.02 1 74 . 10 MET HG3 H 2.49 0.02 1 75 . 10 MET HE H 1.92 0.02 1 76 . 11 SER H H 9.12 0.02 1 77 . 11 SER HA H 4.78 0.02 1 78 . 11 SER HB2 H 4.33 0.02 1 79 . 11 SER HB3 H 4.22 0.02 1 80 . 12 ARG H H 9.27 0.02 1 81 . 12 ARG HA H 4.20 0.02 1 82 . 12 ARG HB2 H 1.85 0.02 1 83 . 12 ARG HB3 H 1.78 0.02 1 84 . 12 ARG HG2 H 1.98 0.02 1 85 . 12 ARG HG3 H 1.98 0.02 1 86 . 12 ARG HD2 H 3.27 0.02 1 87 . 12 ARG HD3 H 3.27 0.02 1 88 . 12 ARG HE H 7.30 0.02 1 89 . 13 SER H H 8.48 0.02 1 90 . 13 SER HA H 4.43 0.02 1 91 . 13 SER HB2 H 3.98 0.02 1 92 . 13 SER HB3 H 3.98 0.02 1 93 . 14 SER H H 7.95 0.02 1 94 . 14 SER HA H 4.62 0.02 1 95 . 14 SER HB2 H 3.32 0.02 1 96 . 14 SER HB3 H 3.27 0.02 1 97 . 15 GLY H H 8.19 0.02 1 98 . 15 GLY HA2 H 3.99 0.02 1 99 . 15 GLY HA3 H 4.16 0.02 1 100 . 16 ARG H H 7.75 0.02 1 101 . 16 ARG HA H 4.50 0.02 1 102 . 16 ARG HB2 H 2.00 0.02 1 103 . 16 ARG HB3 H 1.78 0.02 2 104 . 16 ARG HG2 H 1.78 0.02 2 105 . 16 ARG HG3 H 1.73 0.02 1 106 . 16 ARG HD2 H 2.88 0.02 1 107 . 16 ARG HD3 H 2.53 0.02 1 108 . 16 ARG HE H 6.80 0.02 1 109 . 17 VAL H H 8.64 0.02 1 110 . 17 VAL HA H 4.73 0.02 1 111 . 17 VAL HB H 2.04 0.02 1 112 . 17 VAL HG1 H 1.08 0.02 1 113 . 17 VAL HG2 H 0.84 0.02 1 114 . 18 TYR H H 8.74 0.02 1 115 . 18 TYR HA H 4.96 0.02 1 116 . 18 TYR HB2 H 2.98 0.02 1 117 . 18 TYR HB3 H 2.56 0.02 1 118 . 18 TYR HD1 H 6.93 0.02 1 119 . 18 TYR HD2 H 6.93 0.02 1 120 . 18 TYR HE1 H 6.46 0.02 1 121 . 18 TYR HE2 H 6.46 0.02 1 122 . 19 TYR H H 9.06 0.02 1 123 . 19 TYR HA H 5.33 0.02 1 124 . 19 TYR HB2 H 2.98 0.02 1 125 . 19 TYR HB3 H 2.71 0.02 1 126 . 19 TYR HD1 H 6.88 0.02 1 127 . 19 TYR HD2 H 6.88 0.02 1 128 . 19 TYR HE1 H 6.80 0.02 1 129 . 19 TYR HE2 H 6.80 0.02 1 130 . 20 PHE H H 9.43 0.02 1 131 . 20 PHE HA H 5.70 0.02 1 132 . 20 PHE HB2 H 2.97 0.02 1 133 . 20 PHE HB3 H 2.57 0.02 1 134 . 20 PHE HD1 H 7.01 0.02 1 135 . 20 PHE HD2 H 7.01 0.02 1 136 . 20 PHE HE1 H 7.06 0.02 1 137 . 20 PHE HE2 H 7.06 0.02 1 138 . 20 PHE HZ H 7.37 0.02 1 139 . 21 ASN H H 8.23 0.02 1 140 . 21 ASN HA H 4.39 0.02 1 141 . 21 ASN HB2 H -0.64 0.02 1 142 . 21 ASN HB3 H 2.05 0.02 1 143 . 21 ASN HD21 H 6.70 0.02 1 144 . 21 ASN HD22 H 4.23 0.02 1 145 . 22 HIS H H 8.23 0.02 1 146 . 22 HIS HA H 4.24 0.02 1 147 . 22 HIS HB2 H 3.23 0.02 1 148 . 22 HIS HB3 H 3.55 0.02 1 149 . 22 HIS HD2 H 7.04 0.02 1 150 . 22 HIS HE1 H 7.71 0.02 1 151 . 23 ILE H H 8.35 0.02 1 152 . 23 ILE HA H 3.92 0.02 1 153 . 23 ILE HB H 2.04 0.02 1 154 . 23 ILE HG12 H 1.00 0.02 1 155 . 23 ILE HG13 H 1.27 0.02 1 156 . 23 ILE HG2 H 0.79 0.02 4 157 . 23 ILE HD1 H 0.79 0.02 4 158 . 24 THR H H 7.35 0.02 1 159 . 24 THR HA H 4.29 0.02 1 160 . 24 THR HB H 4.14 0.02 1 161 . 24 THR HG2 H 0.98 0.02 1 162 . 25 ASN H H 8.10 0.02 1 163 . 25 ASN HA H 4.16 0.02 1 164 . 25 ASN HB2 H 3.17 0.02 1 165 . 25 ASN HB3 H 2.96 0.02 1 166 . 25 ASN HD21 H 7.52 0.02 1 167 . 25 ASN HD22 H 6.90 0.02 1 168 . 26 ALA H H 7.16 0.02 1 169 . 26 ALA HA H 4.48 0.02 1 170 . 26 ALA HB H 1.29 0.02 1 171 . 27 SER H H 8.37 0.02 1 172 . 27 SER HA H 6.05 0.02 1 173 . 27 SER HB2 H 3.77 0.02 1 174 . 27 SER HB3 H 3.85 0.02 1 175 . 28 GLN H H 9.41 0.02 1 176 . 28 GLN HA H 4.89 0.02 1 177 . 28 GLN HB2 H 2.56 0.02 1 178 . 28 GLN HB3 H 2.56 0.02 1 179 . 28 GLN HG2 H 2.65 0.02 1 180 . 28 GLN HG3 H 2.65 0.02 1 181 . 28 GLN HE21 H 6.75 0.02 1 182 . 28 GLN HE22 H 7.51 0.02 1 183 . 29 TRP H H 8.54 0.02 1 184 . 29 TRP HA H 5.00 0.02 1 185 . 29 TRP HB2 H 3.25 0.02 1 186 . 29 TRP HB3 H 3.67 0.02 1 187 . 29 TRP HD1 H 7.51 0.02 1 188 . 29 TRP HE1 H 10.16 0.02 1 189 . 29 TRP HE3 H 8.20 0.02 1 190 . 29 TRP HZ2 H 7.41 0.02 1 191 . 29 TRP HZ3 H 6.94 0.02 1 192 . 29 TRP HH2 H 7.15 0.02 1 193 . 30 GLU H H 8.14 0.02 1 194 . 30 GLU HA H 4.45 0.02 1 195 . 30 GLU HB2 H 1.93 0.02 1 196 . 30 GLU HB3 H 1.93 0.02 1 197 . 30 GLU HG2 H 2.27 0.02 1 198 . 30 GLU HG3 H 2.37 0.02 1 199 . 31 ARG H H 8.60 0.02 1 200 . 31 ARG HA H 2.68 0.02 1 201 . 31 ARG HB2 H 1.43 0.02 1 202 . 31 ARG HB3 H 1.43 0.02 1 203 . 31 ARG HG2 H 1.01 0.02 1 204 . 31 ARG HG3 H 1.24 0.02 1 205 . 31 ARG HD2 H 3.10 0.02 1 206 . 31 ARG HD3 H 3.10 0.02 1 207 . 31 ARG HE H 7.22 0.02 1 208 . 32 PRO HA H 3.95 0.02 1 209 . 32 PRO HB2 H 0.03 0.02 1 210 . 32 PRO HB3 H 0.62 0.02 1 211 . 32 PRO HG2 H 0.79 0.02 1 212 . 32 PRO HG3 H 0.87 0.02 1 213 . 32 PRO HD2 H 2.34 0.02 1 214 . 32 PRO HD3 H 2.56 0.02 1 215 . 33 SER H H 8.26 0.02 1 216 . 33 SER HA H 4.37 0.02 1 217 . 33 SER HB2 H 3.77 0.02 1 218 . 33 SER HB3 H 3.85 0.02 1 219 . 34 GLY H H 8.55 0.02 1 220 . 34 GLY HA2 H 4.01 0.02 1 221 . 34 GLY HA3 H 4.01 0.02 1 222 . 35 ASN H H 8.50 0.02 1 223 . 35 ASN HA H 4.84 0.02 1 224 . 35 ASN HB2 H 2.92 0.02 1 225 . 35 ASN HB3 H 2.83 0.02 1 226 . 35 ASN HD21 H 7.56 0.02 1 227 . 35 ASN HD22 H 7.23 0.02 1 228 . 36 SER H H 8.53 0.02 1 229 . 36 SER HA H 4.53 0.02 1 230 . 36 SER HB2 H 3.94 0.02 1 231 . 36 SER HB3 H 3.94 0.02 1 232 . 37 SER H H 8.47 0.02 1 233 . 37 SER HA H 4.53 0.02 1 234 . 37 SER HB2 H 3.98 0.02 1 235 . 37 SER HB3 H 3.98 0.02 1 236 . 38 SER H H 8.58 0.02 1 237 . 38 SER HA H 4.56 0.02 1 238 . 38 SER HB2 H 3.97 0.02 1 239 . 38 SER HB3 H 3.97 0.02 1 240 . 39 GLY H H 8.86 0.02 1 241 . 39 GLY HA2 H 4.98 0.02 1 242 . 39 GLY HA3 H 4.98 0.02 1 stop_ save_