data_6091 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for a complex of PDZ2 from PTP-BL with the C-terminus of p75 (NTR) ; _BMRB_accession_number 6091 _BMRB_flat_file_name bmr6091.str _Entry_type original _Submission_date 2004-02-04 _Accession_date 2004-02-04 _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 Walma Tine . . 2 Vuister Geerten . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 415 "13C chemical shifts" 93 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-05-20 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 5131 'Second PDZ domain of PTP-BL' 6060 'PDZ2 from PTP-BL (complex with APC)' 6092 'PDZ2 from PTP-BL (complex with RIL)' stop_ _Original_release_date 2005-05-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14725761 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Walma Tine . . 2 Aelen J. . . 3 Nabuurs S. B. . 4 Oostendorp M. . . 5 'van den Berk' L. . . 6 Hendriks W. . . 7 Vuister Geerten W. . stop_ _Journal_abbreviation Structure _Journal_volume 12 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11 _Page_last 20 _Year 2004 _Details . save_ ################################## # Molecular system description # ################################## save_system_PDZ2 _Saveframe_category molecular_system _Mol_system_name 'PDZ2 from PTP-BL' _Abbreviation_common PDZ2 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PDZ2 from PTP-BL' $PDZ2 'p75 (NTR) C-terminus' $NTR stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PDZ2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Second PDZ domain from PTP-BL' _Abbreviation_common PDZ2 _Molecular_mass 9752.07 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 102 _Mol_residue_sequence ; MHHHHHHMKPGDTFEVELAK TDGSLGISVTGGVNTSVRHG GIYVKAIIPKGAAESDGRIH KGDRVLAVNGVSLEGATHKQ AVETLRNTGQVVHLLLEKGQ VP ; loop_ _Residue_seq_code _Residue_label 1 MET 2 HIS 3 HIS 4 HIS 5 HIS 6 HIS 7 HIS 8 MET 9 LYS 10 PRO 11 GLY 12 ASP 13 THR 14 PHE 15 GLU 16 VAL 17 GLU 18 LEU 19 ALA 20 LYS 21 THR 22 ASP 23 GLY 24 SER 25 LEU 26 GLY 27 ILE 28 SER 29 VAL 30 THR 31 GLY 32 GLY 33 VAL 34 ASN 35 THR 36 SER 37 VAL 38 ARG 39 HIS 40 GLY 41 GLY 42 ILE 43 TYR 44 VAL 45 LYS 46 ALA 47 ILE 48 ILE 49 PRO 50 LYS 51 GLY 52 ALA 53 ALA 54 GLU 55 SER 56 ASP 57 GLY 58 ARG 59 ILE 60 HIS 61 LYS 62 GLY 63 ASP 64 ARG 65 VAL 66 LEU 67 ALA 68 VAL 69 ASN 70 GLY 71 VAL 72 SER 73 LEU 74 GLU 75 GLY 76 ALA 77 THR 78 HIS 79 LYS 80 GLN 81 ALA 82 VAL 83 GLU 84 THR 85 LEU 86 ARG 87 ASN 88 THR 89 GLY 90 GLN 91 VAL 92 VAL 93 HIS 94 LEU 95 LEU 96 LEU 97 GLU 98 LYS 99 GLY 100 GLN 101 VAL 102 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 GenBank AAC42056 'tyrosine phosphatase' 92.16 126 98.94 98.94 1.91e-45 GenBank AAC42055 'tyrosine phosphatase' 92.16 117 98.94 98.94 5.03e-45 PDB 1VJ6 'Pdz2 From Ptp-Bl In Complex With The C-Terminal Ligand From The Apc Protein' 100.00 102 100.00 100.00 6.35e-51 PDB 1GM1 'Second Pdz Domain (Pdz2) Of Ptp-Bl' 91.18 94 100.00 100.00 3.18e-45 BMRB 6092 'Second PDZ domain from PTP-BL' 100.00 102 100.00 100.00 6.35e-51 BMRB 6060 'Second PDZ domain from PTP-BL' 100.00 102 100.00 100.00 6.35e-51 BMRB 5131 'Protein Tyrosine Phosphatase-BAS Like' 100.00 102 100.00 100.00 6.35e-51 stop_ save_ save_NTR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C-terminus from NTR' _Abbreviation_common NTR _Molecular_mass 877.90 _Mol_thiol_state 'not present' _Details . _Residue_count 9 _Mol_residue_sequence SESTATSPV loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 201 SER 2 202 GLU 3 203 SER 4 204 THR 5 205 ALA 6 206 THR 7 207 SER 8 208 PRO 9 209 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $PDZ2 Mouse 10090 Eukaryota Metazoa Mus musculus 'protein tyrosine phosphatase,non-receptor type 13' $NTR Mouse 10090 Eukaryota Metazoa Mus musculus 'protein tyrosine phosphatase,non-receptor type 13' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $PDZ2 'recombinant technology' 'E. coli' . . 'BL 21' DE3 plasmid pET28a $NTR '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 $PDZ2 1 mM '[U-13C; U-15N]' $NTR 3 mM . K2HPO4/KH2PO4 50 mM . KCl 50 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task 'spectral processing' stop_ _Details 'Delaglio 1995, J Biomol NMR 6 277-293.' save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'peak integration' assignment stop_ _Details 'Bartels et al,1995, J Biomol NMR 5, 1-10.' save_ save_XPLOR _Saveframe_category software _Name XPLOR _Version 3.851 loop_ _Task 'simulated annealing' 'restrained MD refinement in water' stop_ _Details 'Brunger, AT. (1996) Yale University.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label . save_ save_3D_15N_NOESY_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N NOESY HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N NOESY HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 pH temperature 298 1 K 'ionic strength' 0.1 . M 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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 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 $conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PDZ2 from PTP-BL' _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 . 9 LYS CA C 59.262 0.05 1 2 . 9 LYS HA H 4.605 0.02 1 3 . 9 LYS HB2 H 1.757 0.02 1 4 . 9 LYS HB3 H 1.757 0.02 1 5 . 9 LYS HE2 H 3.062 0.02 1 6 . 9 LYS HE3 H 3.062 0.02 1 7 . 9 LYS HG2 H 1.539 0.02 1 8 . 9 LYS HG3 H 1.539 0.02 1 9 . 9 LYS H H 8.790 0.02 1 10 . 9 LYS N N 123.431 0.05 1 11 . 10 PRO CA C 64.830 0.05 1 12 . 10 PRO HA H 4.021 0.02 1 13 . 10 PRO HB2 H 2.283 0.02 2 14 . 10 PRO HB3 H 1.885 0.02 2 15 . 11 GLY CA C 45.486 0.05 1 16 . 11 GLY HA2 H 4.414 0.02 2 17 . 11 GLY HA3 H 3.826 0.02 2 18 . 11 GLY H H 8.895 0.02 1 19 . 11 GLY N N 113.128 0.05 1 20 . 12 ASP CA C 54.931 0.05 1 21 . 12 ASP HA H 4.885 0.02 1 22 . 12 ASP HB2 H 3.063 0.02 2 23 . 12 ASP HB3 H 2.881 0.02 2 24 . 12 ASP H H 8.520 0.02 1 25 . 12 ASP N N 121.689 0.05 1 26 . 13 THR CA C 60.815 0.05 1 27 . 13 THR HA H 5.744 0.02 1 28 . 13 THR HB H 4.195 0.02 1 29 . 13 THR HG2 H 1.187 0.02 1 30 . 13 THR H H 8.396 0.02 1 31 . 13 THR N N 112.442 0.05 1 32 . 14 PHE CA C 56.416 0.05 1 33 . 14 PHE HA H 5.031 0.02 1 34 . 14 PHE HB2 H 3.222 0.02 2 35 . 14 PHE HB3 H 3.072 0.02 2 36 . 14 PHE HD1 H 7.074 0.02 1 37 . 14 PHE HD2 H 7.074 0.02 1 38 . 14 PHE HE1 H 6.910 0.02 1 39 . 14 PHE HE2 H 6.910 0.02 1 40 . 14 PHE H H 9.335 0.02 1 41 . 14 PHE N N 119.750 0.05 1 42 . 15 GLU CA C 54.472 0.05 1 43 . 15 GLU HA H 5.316 0.02 1 44 . 15 GLU HB2 H 1.914 0.02 1 45 . 15 GLU HB3 H 1.914 0.02 1 46 . 15 GLU HG2 H 2.227 0.02 1 47 . 15 GLU HG3 H 2.227 0.02 1 48 . 15 GLU H H 8.621 0.02 1 49 . 15 GLU N N 119.589 0.05 1 50 . 16 VAL CA C 61.189 0.05 1 51 . 16 VAL HA H 4.200 0.02 1 52 . 16 VAL HB H 1.717 0.02 1 53 . 16 VAL HG1 H 0.854 0.02 1 54 . 16 VAL HG2 H 0.854 0.02 1 55 . 16 VAL H H 8.620 0.02 1 56 . 16 VAL N N 119.656 0.05 1 57 . 17 GLU CA C 55.149 0.05 1 58 . 17 GLU HA H 5.040 0.02 1 59 . 17 GLU HB2 H 1.854 0.02 1 60 . 17 GLU HB3 H 1.854 0.02 1 61 . 17 GLU H H 7.828 0.02 1 62 . 17 GLU N N 126.209 0.05 1 63 . 18 LEU CA C 53.597 0.05 1 64 . 18 LEU HA H 4.705 0.02 1 65 . 18 LEU HB2 H 1.367 0.02 1 66 . 18 LEU HB3 H 1.367 0.02 1 67 . 18 LEU HD1 H 0.798 0.02 1 68 . 18 LEU HD2 H 0.798 0.02 1 69 . 18 LEU H H 8.858 0.02 1 70 . 18 LEU N N 125.974 0.05 1 71 . 19 ALA CA C 50.270 0.05 1 72 . 19 ALA HA H 5.153 0.02 1 73 . 19 ALA HB H 1.366 0.02 1 74 . 19 ALA H H 8.514 0.02 1 75 . 19 ALA N N 126.582 0.05 1 76 . 20 LYS CA C 58.141 0.05 1 77 . 20 LYS HA H 3.950 0.02 1 78 . 20 LYS HB2 H 1.718 0.02 2 79 . 20 LYS HB3 H 1.466 0.02 2 80 . 20 LYS HE2 H 2.840 0.02 1 81 . 20 LYS HE3 H 2.840 0.02 1 82 . 20 LYS HG3 H 0.884 0.02 2 83 . 20 LYS H H 8.590 0.02 1 84 . 20 LYS N N 120.769 0.05 1 85 . 21 THR CA C 61.613 0.05 1 86 . 21 THR HA H 4.565 0.02 1 87 . 21 THR HB H 4.237 0.02 1 88 . 21 THR HG2 H 1.265 0.02 1 89 . 21 THR H H 8.163 0.02 1 90 . 21 THR N N 114.080 0.05 1 91 . 22 ASP CA C 55.563 0.05 1 92 . 22 ASP HA H 4.366 0.02 1 93 . 22 ASP HB2 H 2.947 0.02 2 94 . 22 ASP HB3 H 2.706 0.02 2 95 . 22 ASP H H 9.383 0.02 1 96 . 22 ASP N N 125.500 0.05 1 97 . 23 GLY CA C 46.253 0.05 1 98 . 23 GLY HA2 H 4.248 0.02 2 99 . 23 GLY HA3 H 3.675 0.02 2 100 . 23 GLY H H 8.755 0.02 1 101 . 23 GLY N N 103.015 0.05 1 102 . 24 SER CA C 57.431 0.05 1 103 . 24 SER HA H 5.058 0.02 1 104 . 24 SER HB2 H 3.922 0.02 1 105 . 24 SER HB3 H 3.922 0.02 1 106 . 24 SER H H 8.090 0.02 1 107 . 24 SER N N 114.904 0.05 1 108 . 25 LEU CA C 56.413 0.05 1 109 . 25 LEU HB2 H 1.860 0.02 2 110 . 25 LEU HB3 H 1.378 0.02 2 111 . 25 LEU HD1 H 0.883 0.02 1 112 . 26 GLY CA C 46.776 0.05 1 113 . 26 GLY HA2 H 4.330 0.02 2 114 . 26 GLY HA3 H 3.948 0.02 2 115 . 26 GLY H H 9.277 0.02 1 116 . 26 GLY N N 107.290 0.05 1 117 . 27 ILE CA C 59.887 0.05 1 118 . 27 ILE HA H 5.020 0.02 1 119 . 27 ILE HB H 1.660 0.02 1 120 . 27 ILE HD1 H 0.533 0.02 1 121 . 27 ILE HG13 H 0.720 0.02 2 122 . 27 ILE HG2 H 0.725 0.02 1 123 . 27 ILE H H 7.817 0.02 1 124 . 27 ILE N N 116.728 0.05 1 125 . 28 SER CA C 56.679 0.05 1 126 . 28 SER HA H 5.564 0.02 1 127 . 28 SER HB2 H 3.682 0.02 1 128 . 28 SER H H 8.679 0.02 1 129 . 28 SER N N 118.306 0.05 1 130 . 29 VAL CA C 59.079 0.05 1 131 . 29 VAL HA H 5.575 0.02 1 132 . 29 VAL HB H 2.067 0.02 1 133 . 29 VAL HG1 H 0.732 0.02 1 134 . 29 VAL H H 9.185 0.02 1 135 . 29 VAL N N 118.038 0.05 1 136 . 30 THR CA C 59.314 0.05 1 137 . 30 THR HA H 5.566 0.02 1 138 . 30 THR HB H 3.993 0.02 1 139 . 30 THR HG2 H 1.226 0.02 1 140 . 30 THR H H 9.407 0.02 1 141 . 30 THR N N 115.648 0.05 1 142 . 31 GLY CA C 45.141 0.05 1 143 . 31 GLY HA2 H 5.833 0.02 2 144 . 31 GLY HA3 H 4.179 0.02 2 145 . 31 GLY H H 8.278 0.02 1 146 . 31 GLY N N 111.244 0.05 1 147 . 32 GLY CA C 43.697 0.05 1 148 . 32 GLY HA3 H 3.765 0.02 2 149 . 32 GLY H H 7.043 0.02 1 150 . 32 GLY N N 106.055 0.05 1 151 . 33 VAL CA C 64.928 0.05 1 152 . 33 VAL HA H 4.182 0.02 1 153 . 33 VAL HB H 2.237 0.02 1 154 . 33 VAL HG1 H 1.013 0.02 1 155 . 33 VAL HG2 H 0.973 0.02 1 156 . 33 VAL H H 8.509 0.02 1 157 . 33 VAL N N 117.164 0.05 1 158 . 34 ASN CA C 53.551 0.05 1 159 . 34 ASN HB2 H 3.235 0.02 2 160 . 34 ASN HB3 H 2.839 0.02 2 161 . 34 ASN HD21 H 7.921 0.02 2 162 . 34 ASN HD22 H 7.425 0.02 2 163 . 34 ASN H H 9.113 0.02 1 164 . 34 ASN N N 116.813 0.05 1 165 . 34 ASN ND2 N 116.207 0.05 1 166 . 35 THR CA C 61.504 0.05 1 167 . 35 THR H H 7.778 0.02 1 168 . 35 THR N N 110.898 0.05 1 169 . 36 SER CA C 58.540 0.05 1 170 . 36 SER H H 8.527 0.02 1 171 . 36 SER N N 113.072 0.05 1 172 . 37 VAL CA C 62.476 0.05 1 173 . 37 VAL HA H 4.106 0.02 1 174 . 37 VAL HB H 2.223 0.02 1 175 . 37 VAL HG2 H 1.082 0.02 1 176 . 37 VAL H H 7.629 0.02 1 177 . 37 VAL N N 118.418 0.05 1 178 . 38 ARG CA C 58.537 0.05 1 179 . 38 ARG HB2 H 1.672 0.02 1 180 . 38 ARG HB3 H 1.672 0.02 1 181 . 38 ARG H H 8.593 0.02 1 182 . 38 ARG N N 125.624 0.05 1 183 . 39 HIS CA C 57.323 0.05 1 184 . 39 HIS HA H 4.614 0.02 1 185 . 40 GLY CA C 47.209 0.05 1 186 . 40 GLY HA2 H 3.932 0.02 2 187 . 40 GLY HA3 H 3.742 0.02 2 188 . 40 GLY H H 8.577 0.02 1 189 . 40 GLY N N 109.217 0.05 1 190 . 41 GLY CA C 44.974 0.05 1 191 . 41 GLY HA2 H 3.977 0.02 2 192 . 41 GLY HA3 H 3.293 0.02 2 193 . 41 GLY H H 7.769 0.02 1 194 . 41 GLY N N 104.738 0.05 1 195 . 42 ILE CA C 57.387 0.05 1 196 . 42 ILE HB H 2.151 0.02 1 197 . 42 ILE HG12 H 1.778 0.02 2 198 . 42 ILE HG13 H 1.104 0.02 2 199 . 42 ILE HG2 H 0.578 0.02 1 200 . 42 ILE H H 8.394 0.02 1 201 . 42 ILE N N 118.844 0.05 1 202 . 43 TYR CA C 56.369 0.05 1 203 . 43 TYR HA H 5.339 0.02 1 204 . 43 TYR HB2 H 2.720 0.02 2 205 . 43 TYR HB3 H 2.513 0.02 2 206 . 43 TYR HD1 H 7.078 0.02 1 207 . 43 TYR HD2 H 7.078 0.02 1 208 . 43 TYR HE1 H 6.898 0.02 1 209 . 43 TYR HE2 H 6.898 0.02 1 210 . 43 TYR H H 9.142 0.02 1 211 . 43 TYR N N 122.904 0.05 1 212 . 44 VAL CA C 64.246 0.05 1 213 . 44 VAL HA H 3.959 0.02 1 214 . 44 VAL HB H 2.345 0.02 1 215 . 44 VAL HG1 H 0.747 0.02 1 216 . 44 VAL H H 9.262 0.02 1 217 . 44 VAL N N 120.763 0.05 1 218 . 45 LYS CA C 56.856 0.05 1 219 . 45 LYS HA H 4.464 0.02 1 220 . 45 LYS HG2 H 0.722 0.02 1 221 . 45 LYS H H 9.577 0.02 1 222 . 45 LYS N N 134.725 0.05 1 223 . 46 ALA CA C 51.767 0.05 1 224 . 46 ALA HA H 4.551 0.02 1 225 . 46 ALA HB H 1.361 0.02 1 226 . 46 ALA H H 7.666 0.02 1 227 . 46 ALA N N 116.792 0.05 1 228 . 47 ILE CA C 58.537 0.05 1 229 . 47 ILE HA H 4.368 0.02 1 230 . 47 ILE HB H 2.079 0.02 1 231 . 47 ILE HD1 H 0.555 0.02 1 232 . 47 ILE HG12 H 1.384 0.02 2 233 . 47 ILE HG13 H 1.319 0.02 2 234 . 47 ILE HG2 H 0.842 0.02 1 235 . 47 ILE H H 8.728 0.02 1 236 . 47 ILE N N 121.411 0.05 1 237 . 48 ILE CA C 59.201 0.05 1 238 . 48 ILE HB H 1.624 0.02 1 239 . 48 ILE HD1 H 0.805 0.02 1 240 . 48 ILE HG12 H 1.389 0.02 2 241 . 48 ILE HG13 H 1.135 0.02 2 242 . 48 ILE H H 7.824 0.02 1 243 . 48 ILE N N 129.818 0.05 1 244 . 49 PRO CA C 64.459 0.05 1 245 . 49 PRO HA H 4.549 0.02 1 246 . 49 PRO HB2 H 2.436 0.02 2 247 . 49 PRO HB3 H 1.899 0.02 2 248 . 50 LYS CA C 58.272 0.05 1 249 . 50 LYS HA H 3.907 0.02 1 250 . 50 LYS HB3 H 2.161 0.02 2 251 . 50 LYS HG2 H 1.426 0.02 1 252 . 50 LYS HG3 H 1.426 0.02 1 253 . 50 LYS H H 9.379 0.02 1 254 . 50 LYS N N 117.491 0.05 1 255 . 51 GLY CA C 45.203 0.05 1 256 . 51 GLY HA2 H 4.297 0.02 2 257 . 51 GLY HA3 H 3.914 0.02 2 258 . 51 GLY H H 7.774 0.02 1 259 . 51 GLY N N 106.176 0.05 1 260 . 52 ALA CA C 55.669 0.05 1 261 . 52 ALA HA H 4.090 0.02 1 262 . 52 ALA HB H 1.676 0.02 1 263 . 52 ALA H H 8.908 0.02 1 264 . 52 ALA N N 121.679 0.05 1 265 . 53 ALA CA C 55.389 0.05 1 266 . 53 ALA HA H 4.098 0.02 1 267 . 53 ALA HB H 1.315 0.02 1 268 . 53 ALA H H 8.120 0.02 1 269 . 53 ALA N N 119.592 0.05 1 270 . 54 GLU CA C 60.174 0.05 1 271 . 54 GLU HA H 3.830 0.02 1 272 . 54 GLU HB2 H 2.138 0.02 1 273 . 54 GLU HB3 H 2.138 0.02 1 274 . 54 GLU H H 9.440 0.02 1 275 . 54 GLU N N 124.478 0.05 1 276 . 55 SER CA C 61.546 0.05 1 277 . 55 SER HA H 4.213 0.02 1 278 . 55 SER HB2 H 4.090 0.02 2 279 . 55 SER HB3 H 3.998 0.02 2 280 . 55 SER H H 7.959 0.02 1 281 . 55 SER N N 113.416 0.05 1 282 . 56 ASP CA C 57.730 0.05 1 283 . 56 ASP HA H 4.455 0.02 1 284 . 56 ASP HB2 H 2.743 0.02 2 285 . 56 ASP HB3 H 2.620 0.02 2 286 . 56 ASP H H 7.747 0.02 1 287 . 56 ASP N N 120.270 0.05 1 288 . 57 GLY CA C 46.678 0.05 1 289 . 57 GLY HA2 H 4.137 0.02 2 290 . 57 GLY HA3 H 3.937 0.02 2 291 . 57 GLY H H 7.505 0.02 1 292 . 57 GLY N N 102.745 0.05 1 293 . 58 ARG CA C 58.354 0.05 1 294 . 58 ARG HA H 4.320 0.02 1 295 . 58 ARG HB2 H 2.095 0.02 2 296 . 58 ARG HD2 H 3.276 0.02 2 297 . 58 ARG HD3 H 3.115 0.02 2 298 . 58 ARG HE H 8.770 0.02 1 299 . 58 ARG HG2 H 1.675 0.02 1 300 . 58 ARG HG3 H 1.675 0.02 1 301 . 58 ARG H H 8.049 0.02 1 302 . 58 ARG N N 117.733 0.05 1 303 . 58 ARG NE N 123.177 0.05 1 304 . 59 ILE CA C 61.900 0.05 1 305 . 59 ILE HA H 4.252 0.02 1 306 . 59 ILE HB H 1.484 0.02 1 307 . 59 ILE HD1 H 0.775 0.02 1 308 . 59 ILE HG12 H 1.822 0.02 2 309 . 59 ILE HG2 H 0.889 0.02 1 310 . 59 ILE H H 8.392 0.02 1 311 . 59 ILE N N 120.104 0.05 1 312 . 60 HIS CA C 55.086 0.05 1 313 . 60 HIS HB2 H 3.340 0.02 2 314 . 60 HIS HB3 H 3.049 0.02 2 315 . 60 HIS H H 9.200 0.02 1 316 . 60 HIS N N 123.918 0.05 1 317 . 61 LYS CA C 58.670 0.05 1 318 . 61 LYS HA H 3.692 0.02 1 319 . 61 LYS HB2 H 1.717 0.02 1 320 . 61 LYS HB3 H 1.717 0.02 1 321 . 61 LYS HG2 H 1.532 0.02 2 322 . 61 LYS HG3 H 1.364 0.02 2 323 . 61 LYS H H 8.700 0.02 1 324 . 61 LYS N N 120.820 0.05 1 325 . 62 GLY CA C 45.234 0.05 1 326 . 62 GLY HA2 H 4.655 0.02 2 327 . 62 GLY HA3 H 3.701 0.02 2 328 . 62 GLY H H 9.296 0.02 1 329 . 62 GLY N N 114.508 0.05 1 330 . 63 ASP CA C 56.236 0.05 1 331 . 63 ASP HA H 4.931 0.02 1 332 . 63 ASP HB2 H 2.759 0.02 1 333 . 63 ASP HB3 H 2.759 0.02 1 334 . 63 ASP H H 8.053 0.02 1 335 . 63 ASP N N 121.722 0.05 1 336 . 64 ARG CA C 54.820 0.05 1 337 . 64 ARG HB2 H 1.793 0.02 1 338 . 64 ARG HB3 H 1.793 0.02 1 339 . 64 ARG HD2 H 3.056 0.02 2 340 . 64 ARG HD3 H 2.858 0.02 2 341 . 64 ARG HE H 7.546 0.02 1 342 . 64 ARG HG2 H 0.982 0.02 2 343 . 64 ARG H H 9.046 0.02 1 344 . 64 ARG N N 122.810 0.05 1 345 . 64 ARG NE N 121.318 0.05 1 346 . 65 VAL CA C 62.645 0.05 1 347 . 65 VAL HA H 3.921 0.02 1 348 . 65 VAL HB H 1.793 0.02 1 349 . 65 VAL HG1 H 0.691 0.02 1 350 . 65 VAL HG2 H 0.599 0.02 1 351 . 65 VAL H H 9.013 0.02 1 352 . 65 VAL N N 126.413 0.05 1 353 . 66 LEU CA C 56.280 0.05 1 354 . 66 LEU HA H 4.443 0.02 1 355 . 66 LEU HB2 H 1.441 0.02 1 356 . 66 LEU HB3 H 1.441 0.02 1 357 . 66 LEU H H 9.238 0.02 1 358 . 66 LEU N N 127.017 0.05 1 359 . 67 ALA CA C 52.475 0.05 1 360 . 67 ALA HA H 5.053 0.02 1 361 . 67 ALA HB H 1.136 0.02 1 362 . 67 ALA H H 7.848 0.02 1 363 . 67 ALA N N 118.890 0.05 1 364 . 68 VAL CA C 60.484 0.05 1 365 . 68 VAL HA H 4.555 0.02 1 366 . 68 VAL HB H 1.778 0.02 1 367 . 68 VAL HG1 H 0.739 0.02 1 368 . 68 VAL H H 8.445 0.02 1 369 . 68 VAL N N 119.903 0.05 1 370 . 69 ASN CA C 54.538 0.05 1 371 . 69 ASN HA H 4.484 0.02 1 372 . 69 ASN HB2 H 3.137 0.02 1 373 . 69 ASN HB3 H 3.137 0.02 1 374 . 69 ASN HD21 H 7.916 0.02 2 375 . 69 ASN HD22 H 7.354 0.02 2 376 . 69 ASN H H 11.063 0.02 1 377 . 69 ASN N N 128.831 0.05 1 378 . 69 ASN ND2 N 113.016 0.05 1 379 . 70 GLY CA C 45.487 0.05 1 380 . 70 GLY HA2 H 4.121 0.02 2 381 . 70 GLY HA3 H 3.547 0.02 2 382 . 70 GLY H H 9.079 0.02 1 383 . 70 GLY N N 103.217 0.05 1 384 . 71 VAL CA C 62.476 0.05 1 385 . 71 VAL HA H 4.036 0.02 1 386 . 71 VAL HB H 2.266 0.02 1 387 . 71 VAL HG1 H 0.959 0.02 1 388 . 71 VAL HG2 H 0.959 0.02 1 389 . 71 VAL H H 8.123 0.02 1 390 . 71 VAL N N 123.814 0.05 1 391 . 72 SER CA C 58.654 0.05 1 392 . 72 SER HA H 4.397 0.02 1 393 . 72 SER HB2 H 4.087 0.02 2 394 . 72 SER HB3 H 3.878 0.02 2 395 . 72 SER H H 8.717 0.02 1 396 . 72 SER N N 121.178 0.05 1 397 . 73 LEU CA C 54.293 0.05 1 398 . 73 LEU HB2 H 1.671 0.02 2 399 . 73 LEU HB3 H 1.502 0.02 2 400 . 73 LEU HG H 0.744 0.02 1 401 . 73 LEU H H 8.211 0.02 1 402 . 73 LEU N N 124.934 0.05 1 403 . 74 GLU CA C 58.758 0.05 1 404 . 74 GLU HA H 4.075 0.02 1 405 . 74 GLU HB2 H 1.946 0.02 1 406 . 74 GLU HB3 H 1.946 0.02 1 407 . 74 GLU HG2 H 2.221 0.02 1 408 . 74 GLU HG3 H 2.221 0.02 1 409 . 74 GLU H H 8.315 0.02 1 410 . 74 GLU N N 123.024 0.05 1 411 . 75 GLY CA C 45.704 0.05 1 412 . 75 GLY HA2 H 4.228 0.02 2 413 . 75 GLY HA3 H 3.677 0.02 2 414 . 75 GLY H H 9.112 0.02 1 415 . 75 GLY N N 115.570 0.05 1 416 . 76 ALA CA C 52.943 0.05 1 417 . 76 ALA HA H 4.526 0.02 1 418 . 76 ALA HB H 1.460 0.02 1 419 . 76 ALA H H 7.945 0.02 1 420 . 76 ALA N N 122.249 0.05 1 421 . 77 THR CA C 61.534 0.05 1 422 . 77 THR HB H 4.680 0.02 1 423 . 77 THR HG2 H 1.392 0.02 1 424 . 77 THR H H 8.349 0.02 1 425 . 77 THR N N 112.333 0.05 1 426 . 78 HIS CA C 62.424 0.05 1 427 . 78 HIS HA H 3.989 0.02 1 428 . 78 HIS HB2 H 3.547 0.02 2 429 . 78 HIS HB3 H 3.284 0.02 2 430 . 78 HIS H H 9.249 0.02 1 431 . 78 HIS N N 121.209 0.05 1 432 . 79 LYS CA C 59.931 0.05 1 433 . 79 LYS HA H 3.950 0.02 1 434 . 79 LYS HB2 H 2.012 0.02 2 435 . 79 LYS HB3 H 1.753 0.02 2 436 . 79 LYS H H 8.758 0.02 1 437 . 79 LYS N N 115.820 0.05 1 438 . 80 GLN CA C 58.692 0.05 1 439 . 80 GLN HA H 4.069 0.02 1 440 . 80 GLN HB2 H 2.279 0.02 2 441 . 80 GLN HB3 H 2.032 0.02 2 442 . 80 GLN HE21 H 7.518 0.02 2 443 . 80 GLN HE22 H 6.856 0.02 2 444 . 80 GLN HG2 H 2.434 0.02 1 445 . 80 GLN HG3 H 2.434 0.02 1 446 . 80 GLN H H 7.647 0.02 1 447 . 80 GLN N N 117.367 0.05 1 448 . 80 GLN NE2 N 111.039 0.05 1 449 . 81 ALA CA C 55.705 0.05 1 450 . 81 ALA HA H 3.876 0.02 1 451 . 81 ALA HB H 1.348 0.02 1 452 . 81 ALA H H 8.576 0.02 1 453 . 81 ALA N N 123.096 0.05 1 454 . 82 VAL CA C 67.598 0.05 1 455 . 82 VAL HA H 3.248 0.02 1 456 . 82 VAL HB H 2.069 0.02 1 457 . 82 VAL HG1 H 0.584 0.02 1 458 . 82 VAL HG2 H 0.828 0.02 1 459 . 82 VAL H H 8.336 0.02 1 460 . 82 VAL N N 117.946 0.05 1 461 . 83 GLU CA C 60.082 0.05 1 462 . 83 GLU HA H 3.969 0.02 1 463 . 83 GLU HB2 H 2.100 0.02 1 464 . 83 GLU HB3 H 2.100 0.02 1 465 . 83 GLU HG2 H 2.398 0.02 1 466 . 83 GLU HG3 H 2.398 0.02 1 467 . 83 GLU H H 8.392 0.02 1 468 . 83 GLU N N 119.154 0.05 1 469 . 84 THR CA C 67.210 0.05 1 470 . 84 THR HA H 3.924 0.02 1 471 . 84 THR HB H 4.259 0.02 1 472 . 84 THR HG2 H 1.104 0.02 1 473 . 84 THR H H 8.103 0.02 1 474 . 84 THR N N 116.541 0.05 1 475 . 85 LEU CA C 58.803 0.05 1 476 . 85 LEU HA H 3.885 0.02 1 477 . 85 LEU HB2 H 2.084 0.02 2 478 . 85 LEU HB3 H 1.236 0.02 2 479 . 85 LEU HD1 H 0.729 0.02 1 480 . 85 LEU HD2 H 0.729 0.02 1 481 . 85 LEU HG H 1.581 0.02 1 482 . 85 LEU H H 8.051 0.02 1 483 . 85 LEU N N 120.191 0.05 1 484 . 86 ARG CA C 59.020 0.05 1 485 . 86 ARG HA H 4.299 0.02 1 486 . 86 ARG HB2 H 1.900 0.02 1 487 . 86 ARG HB3 H 1.900 0.02 1 488 . 86 ARG HD2 H 3.172 0.02 1 489 . 86 ARG HD3 H 3.172 0.02 1 490 . 86 ARG H H 8.590 0.02 1 491 . 86 ARG N N 119.096 0.05 1 492 . 87 ASN CA C 53.050 0.05 1 493 . 87 ASN HA H 5.017 0.02 1 494 . 87 ASN HB2 H 2.990 0.02 2 495 . 87 ASN HB3 H 2.858 0.02 2 496 . 87 ASN HD21 H 7.693 0.02 2 497 . 87 ASN HD22 H 6.938 0.02 2 498 . 87 ASN H H 8.041 0.02 1 499 . 87 ASN N N 120.293 0.05 1 500 . 87 ASN ND2 N 112.331 0.05 1 501 . 88 THR CA C 60.219 0.05 1 502 . 88 THR HA H 4.504 0.02 1 503 . 88 THR HB H 4.289 0.02 1 504 . 88 THR HG2 H 1.244 0.02 1 505 . 88 THR H H 7.655 0.02 1 506 . 88 THR N N 110.095 0.05 1 507 . 89 GLY CA C 44.443 0.05 1 508 . 89 GLY HA2 H 4.406 0.02 2 509 . 89 GLY HA3 H 3.831 0.02 2 510 . 89 GLY H H 8.454 0.02 1 511 . 89 GLY N N 109.502 0.05 1 512 . 90 GLN CA C 58.811 0.05 1 513 . 90 GLN HA H 4.024 0.02 1 514 . 90 GLN HB2 H 2.117 0.02 1 515 . 90 GLN HB3 H 2.117 0.02 1 516 . 90 GLN HE21 H 7.483 0.02 2 517 . 90 GLN HE22 H 6.960 0.02 2 518 . 90 GLN HG2 H 2.495 0.02 1 519 . 90 GLN HG3 H 2.495 0.02 1 520 . 90 GLN H H 8.219 0.02 1 521 . 90 GLN N N 117.315 0.05 1 522 . 90 GLN NE2 N 112.068 0.05 1 523 . 91 VAL CA C 61.677 0.05 1 524 . 91 VAL HA H 4.720 0.02 1 525 . 91 VAL HB H 1.870 0.02 1 526 . 91 VAL HG1 H 0.905 0.02 1 527 . 91 VAL HG2 H 0.721 0.02 1 528 . 91 VAL H H 7.771 0.02 1 529 . 91 VAL N N 115.949 0.05 1 530 . 92 VAL CA C 61.403 0.05 1 531 . 92 VAL HA H 4.473 0.02 1 532 . 92 VAL HB H 1.869 0.02 1 533 . 92 VAL HG1 H 0.924 0.02 1 534 . 92 VAL HG2 H 0.735 0.02 1 535 . 92 VAL H H 9.060 0.02 1 536 . 92 VAL N N 128.151 0.05 1 537 . 93 HIS CA C 55.930 0.05 1 538 . 93 HIS HA H 5.055 0.02 1 539 . 93 HIS HB2 H 3.217 0.02 1 540 . 93 HIS HB3 H 3.217 0.02 1 541 . 93 HIS HD1 H 7.052 0.02 1 542 . 93 HIS H H 8.827 0.02 1 543 . 93 HIS N N 126.026 0.05 1 544 . 94 LEU CA C 53.758 0.05 1 545 . 94 LEU HA H 5.047 0.02 1 546 . 94 LEU HB2 H 1.655 0.02 2 547 . 94 LEU HB3 H 1.076 0.02 2 548 . 94 LEU HD1 H 0.733 0.02 1 549 . 94 LEU HD2 H 0.733 0.02 1 550 . 94 LEU HG H 0.721 0.02 1 551 . 94 LEU H H 9.084 0.02 1 552 . 94 LEU N N 126.740 0.05 1 553 . 95 LEU CA C 54.099 0.05 1 554 . 95 LEU HB2 H 1.778 0.02 2 555 . 95 LEU HB3 H 1.351 0.02 2 556 . 95 LEU HD1 H 0.832 0.02 1 557 . 95 LEU HD2 H 0.899 0.02 2 558 . 95 LEU H H 8.062 0.02 1 559 . 95 LEU N N 124.120 0.05 1 560 . 96 LEU CA C 54.353 0.05 1 561 . 96 LEU HA H 5.344 0.02 1 562 . 96 LEU HB2 H 1.068 0.02 2 563 . 96 LEU HB3 H 0.239 0.02 2 564 . 96 LEU HD1 H 0.715 0.02 1 565 . 96 LEU HD2 H 0.485 0.02 2 566 . 96 LEU H H 8.962 0.02 1 567 . 96 LEU N N 127.588 0.05 1 568 . 97 GLU CA C 54.343 0.05 1 569 . 97 GLU HA H 4.979 0.02 1 570 . 97 GLU HB2 H 2.054 0.02 1 571 . 97 GLU HB3 H 2.054 0.02 1 572 . 97 GLU H H 9.014 0.02 1 573 . 97 GLU N N 119.102 0.05 1 574 . 98 LYS CA C 56.453 0.05 1 575 . 98 LYS HA H 4.458 0.02 1 576 . 98 LYS HB2 H 2.319 0.02 2 577 . 98 LYS HD2 H 1.897 0.02 2 578 . 98 LYS HE2 H 2.750 0.02 1 579 . 98 LYS HE3 H 2.750 0.02 1 580 . 98 LYS HG2 H 1.674 0.02 2 581 . 98 LYS H H 9.193 0.02 1 582 . 98 LYS N N 128.373 0.05 1 583 . 99 GLY CA C 45.704 0.05 1 584 . 99 GLY HA2 H 4.375 0.02 2 585 . 99 GLY HA3 H 3.876 0.02 2 586 . 99 GLY H H 9.643 0.02 1 587 . 99 GLY N N 117.214 0.05 1 588 . 100 GLN CA C 55.794 0.05 1 589 . 100 GLN HA H 4.355 0.02 1 590 . 100 GLN HB2 H 2.135 0.02 2 591 . 100 GLN HB3 H 1.964 0.02 2 592 . 100 GLN HE21 H 7.694 0.02 2 593 . 100 GLN HE22 H 6.897 0.02 2 594 . 100 GLN HG2 H 2.416 0.02 1 595 . 100 GLN HG3 H 2.416 0.02 1 596 . 100 GLN H H 8.246 0.02 1 597 . 100 GLN N N 117.462 0.05 1 598 . 100 GLN NE2 N 112.873 0.05 1 599 . 101 VAL CA C 60.211 0.05 1 600 . 101 VAL HA H 4.366 0.02 1 601 . 101 VAL HB H 2.161 0.02 1 602 . 101 VAL HG1 H 0.966 0.02 1 603 . 101 VAL HG2 H 0.966 0.02 1 604 . 101 VAL H H 8.219 0.02 1 605 . 101 VAL N N 122.692 0.05 1 stop_ save_