data_6060 ####################### # 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 APC (adenomatous polyposis coli) ; _BMRB_accession_number 6060 _BMRB_flat_file_name bmr6060.str _Entry_type original _Submission_date 2004-01-06 _Accession_date 2004-01-06 _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 W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 T1_relaxation 1 T2_relaxation 1 heteronucl_NOE 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 508 "13C chemical shifts" 286 "15N chemical shifts" 92 "T1 relaxation values" 78 "T2 relaxation values" 78 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-08-11 update BMRB ; updated T1 and T2 units from s to s-1 and added the spectrometer frequency to the heteronuclear NOE save frame ; stop_ loop_ _Related_BMRB_accession_number _Relationship 5131 'Second PDZ domain of PTP-BL' 6091 'PDZ2 from PTP-BL (complex with NTR)' 6092 'PDZ2 from PTP-BL (complex with RIL)' stop_ 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 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_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_author_seq_code _Residue_label 1 1 MET 2 2 HIS 3 3 HIS 4 4 HIS 5 5 HIS 6 6 HIS 7 7 HIS 8 8 MET 9 9 LYS 10 10 PRO 11 11 GLY 12 12 ASP 13 13 THR 14 14 PHE 15 15 GLU 16 16 VAL 17 17 GLU 18 18 LEU 19 19 ALA 20 20 LYS 21 21 THR 22 22 ASP 23 23 GLY 24 24 SER 25 25 LEU 26 26 GLY 27 27 ILE 28 28 SER 29 29 VAL 30 30 THR 31 31 GLY 32 32 GLY 33 33 VAL 34 34 ASN 35 35 THR 36 36 SER 37 37 VAL 38 38 ARG 39 39 HIS 40 40 GLY 41 41 GLY 42 42 ILE 43 43 TYR 44 44 VAL 45 45 LYS 46 46 ALA 47 47 ILE 48 48 ILE 49 49 PRO 50 50 LYS 51 51 GLY 52 52 ALA 53 53 ALA 54 54 GLU 55 55 SER 56 56 ASP 57 57 GLY 58 58 ARG 59 59 ILE 60 60 HIS 61 61 LYS 62 62 GLY 63 63 ASP 64 64 ARG 65 65 VAL 66 66 LEU 67 67 ALA 68 68 VAL 69 69 ASN 70 70 GLY 71 71 VAL 72 72 SER 73 73 LEU 74 74 GLU 75 75 GLY 76 76 ALA 77 77 THR 78 78 HIS 79 79 LYS 80 80 GLN 81 81 ALA 82 82 VAL 83 83 GLU 84 84 THR 85 85 LEU 86 86 ARG 87 87 ASN 88 88 THR 89 89 GLY 90 90 GLN 91 91 VAL 92 92 VAL 93 93 HIS 94 94 LEU 95 95 LEU 96 96 LEU 97 97 GLU 98 98 LYS 99 99 GLY 100 100 GLN 101 101 VAL 102 102 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 6091 '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_APC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C-terminus from APC' _Abbreviation_common APC _Molecular_mass 1333.51 _Mol_thiol_state 'not present' _Details . _Residue_count 12 _Mol_residue_sequence KRHSGSYLVTSV loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 201 LYS 2 202 ARG 3 203 HIS 4 204 SER 5 205 GLY 6 206 SER 7 207 TYR 8 208 LEU 9 209 VAL 10 210 THR 11 211 SER 12 212 VAL stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2005-06-09 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' $APC mouse 10090 Eukaryota Metazoa Mus musculus . 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 $APC 'chemical synthesis' . . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PDZ2 1.0 mM '[U-2H; U-13C; U-15N]' $APC 3 mM [U-2H] 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_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_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 $sample_one save_ save_3D_HAHB(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HAHB(CO)NH' _Sample_label $sample_one save_ save_3D_CCH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CCH' _Sample_label $sample_one save_ save_3D_13C_NOESY_HSQC_(aliphatic)_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C NOESY HSQC (aliphatic)' _Sample_label $sample_one save_ save_3D_15N_NOESY_HSQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N NOESY HSQC' _Sample_label $sample_one 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one 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 53.876 0.05 1 2 . 9 LYS CB C 31.541 0.05 1 3 . 9 LYS CD C 28.822 0.05 1 4 . 9 LYS CE C 41.835 0.05 1 5 . 9 LYS CG C 24.549 0.05 1 6 . 9 LYS HA H 4.543 0.05 1 7 . 9 LYS HB2 H 1.766 0.05 2 8 . 9 LYS HB3 H 1.707 0.05 2 9 . 9 LYS HD2 H 1.706 0.05 1 10 . 9 LYS HD3 H 1.706 0.05 1 11 . 9 LYS HE2 H 3.022 0.05 1 12 . 9 LYS HE3 H 3.022 0.05 1 13 . 9 LYS HG2 H 1.497 0.05 1 14 . 9 LYS HG3 H 1.497 0.05 1 15 . 9 LYS H H 7.921 0.05 1 16 . 9 LYS N N 119.592 0.05 1 17 . 10 PRO CA C 64.526 0.05 1 18 . 10 PRO CB C 31.795 0.05 1 19 . 10 PRO CD C 50.213 0.05 1 20 . 10 PRO CG C 28.092 0.05 1 21 . 10 PRO HA H 3.996 0.05 1 22 . 10 PRO HB2 H 2.182 0.05 2 23 . 10 PRO HB3 H 1.857 0.05 2 24 . 10 PRO HD2 H 3.810 0.05 2 25 . 10 PRO HD3 H 3.567 0.05 2 26 . 10 PRO HG2 H 2.173 0.05 2 27 . 10 PRO HG3 H 1.992 0.05 2 28 . 11 GLY CA C 45.236 0.05 1 29 . 11 GLY HA2 H 4.380 0.05 2 30 . 11 GLY HA3 H 3.789 0.05 2 31 . 11 GLY H H 8.880 0.05 1 32 . 11 GLY N N 113.024 0.05 1 33 . 12 ASP CA C 54.742 0.05 1 34 . 12 ASP CB C 41.672 0.05 1 35 . 12 ASP HA H 4.840 0.05 1 36 . 12 ASP HB2 H 3.029 0.05 2 37 . 12 ASP HB3 H 2.843 0.05 2 38 . 12 ASP H H 8.503 0.05 1 39 . 12 ASP N N 121.877 0.05 1 40 . 13 THR CA C 60.406 0.05 1 41 . 13 THR CB C 70.971 0.05 1 42 . 13 THR CG2 C 21.960 0.05 1 43 . 13 THR HA H 5.700 0.05 1 44 . 13 THR HB H 4.157 0.05 1 45 . 13 THR HG2 H 1.151 0.05 1 46 . 13 THR H H 8.373 0.05 1 47 . 13 THR N N 112.301 0.05 1 48 . 14 PHE CA C 56.130 0.05 1 49 . 14 PHE CB C 40.561 0.05 1 50 . 14 PHE HA H 4.993 0.05 1 51 . 14 PHE HB2 H 3.185 0.05 2 52 . 14 PHE HB3 H 3.033 0.05 2 53 . 14 PHE HD1 H 6.957 0.05 1 54 . 14 PHE HD2 H 6.957 0.05 1 55 . 14 PHE HE1 H 6.842 0.05 1 56 . 14 PHE HE2 H 6.842 0.05 1 57 . 14 PHE H H 9.308 0.05 1 58 . 14 PHE N N 119.626 0.05 1 59 . 15 GLU CA C 54.179 0.05 1 60 . 15 GLU CB C 33.317 0.05 1 61 . 15 GLU CG C 37.331 0.05 1 62 . 15 GLU HA H 5.284 0.05 1 63 . 15 GLU HB2 H 1.879 0.05 1 64 . 15 GLU HB3 H 1.879 0.05 1 65 . 15 GLU HG2 H 2.207 0.05 2 66 . 15 GLU HG3 H 2.145 0.05 2 67 . 15 GLU H H 8.605 0.05 1 68 . 15 GLU N N 119.592 0.05 1 69 . 16 VAL CA C 60.995 0.05 1 70 . 16 VAL CB C 36.842 0.05 1 71 . 16 VAL CG1 C 22.634 0.05 1 72 . 16 VAL CG2 C 21.683 0.05 1 73 . 16 VAL HA H 4.153 0.05 1 74 . 16 VAL HB H 1.694 0.05 1 75 . 16 VAL HG1 H 0.797 0.05 1 76 . 16 VAL HG2 H 0.852 0.05 1 77 . 16 VAL H H 8.607 0.05 1 78 . 16 VAL N N 119.592 0.05 1 79 . 17 GLU CA C 54.789 0.05 1 80 . 17 GLU CB C 30.763 0.05 1 81 . 17 GLU CG C 37.013 0.05 1 82 . 17 GLU HA H 5.016 0.05 1 83 . 17 GLU HB2 H 1.822 0.05 1 84 . 17 GLU HB3 H 1.822 0.05 1 85 . 17 GLU HG2 H 1.851 0.05 1 86 . 17 GLU HG3 H 1.851 0.05 1 87 . 17 GLU H H 7.756 0.05 1 88 . 17 GLU N N 126.180 0.05 1 89 . 18 LEU CA C 53.231 0.05 1 90 . 18 LEU CB C 45.846 0.05 1 91 . 18 LEU CD1 C 25.195 0.05 1 92 . 18 LEU CG C 26.708 0.05 1 93 . 18 LEU HA H 4.663 0.05 1 94 . 18 LEU HB2 H 1.382 0.05 2 95 . 18 LEU HB3 H 1.284 0.05 2 96 . 18 LEU HD1 H 0.762 0.05 1 97 . 18 LEU HD2 H 0.762 0.05 1 98 . 18 LEU HG H 1.383 0.05 1 99 . 18 LEU H H 8.853 0.05 1 100 . 18 LEU N N 126.180 0.05 1 101 . 19 ALA CA C 49.930 0.05 1 102 . 19 ALA CB C 19.190 0.05 1 103 . 19 ALA HA H 5.117 0.05 1 104 . 19 ALA HB H 1.320 0.05 1 105 . 19 ALA H H 8.528 0.05 1 106 . 19 ALA N N 126.446 0.05 1 107 . 20 LYS CA C 57.855 0.05 1 108 . 20 LYS CB C 34.441 0.05 1 109 . 20 LYS CD C 30.084 0.05 1 110 . 20 LYS CE C 42.405 0.05 1 111 . 20 LYS CG C 27.105 0.05 1 112 . 20 LYS HA H 3.900 0.05 1 113 . 20 LYS HB2 H 1.697 0.05 2 114 . 20 LYS HB3 H 1.427 0.05 2 115 . 20 LYS HD2 H 1.470 0.05 2 116 . 20 LYS HD3 H 1.266 0.05 2 117 . 20 LYS HE2 H 2.849 0.05 2 118 . 20 LYS HE3 H 2.745 0.05 2 119 . 20 LYS HG2 H 1.425 0.05 2 120 . 20 LYS HG3 H 0.815 0.05 2 121 . 20 LYS H H 8.565 0.05 1 122 . 20 LYS N N 120.735 0.05 1 123 . 21 THR CA C 61.257 0.05 1 124 . 21 THR CB C 70.512 0.05 1 125 . 21 THR CG2 C 22.056 0.05 1 126 . 21 THR HA H 4.524 0.05 1 127 . 21 THR HB H 4.183 0.05 1 128 . 21 THR HG2 H 1.212 0.05 1 129 . 21 THR H H 8.175 0.05 1 130 . 21 THR N N 114.167 0.05 1 131 . 22 ASP CA C 55.336 0.05 1 132 . 22 ASP CB C 40.004 0.05 1 133 . 22 ASP HA H 4.347 0.05 1 134 . 22 ASP HB2 H 2.923 0.05 2 135 . 22 ASP HB3 H 2.665 0.05 2 136 . 22 ASP H H 9.364 0.05 1 137 . 22 ASP N N 125.875 0.05 1 138 . 23 GLY CA C 45.867 0.05 1 139 . 23 GLY HA2 H 4.194 0.05 2 140 . 23 GLY HA3 H 3.644 0.05 2 141 . 23 GLY H H 8.697 0.05 1 142 . 24 SER CA C 57.431 0.05 1 143 . 24 SER CB C 66.132 0.05 1 144 . 24 SER HA H 5.015 0.05 1 145 . 24 SER HB2 H 3.927 0.05 2 146 . 24 SER HB3 H 3.873 0.05 2 147 . 24 SER H H 8.082 0.05 1 148 . 24 SER N N 115.386 0.05 1 149 . 25 LEU CA C 56.555 0.05 1 150 . 25 LEU CB C 42.965 0.05 1 151 . 25 LEU CD1 C 25.924 0.05 1 152 . 25 LEU CD2 C 23.934 0.05 1 153 . 25 LEU CG C 27.159 0.05 1 154 . 25 LEU HA H 4.239 0.05 1 155 . 25 LEU HB2 H 1.818 0.05 2 156 . 25 LEU HB3 H 1.269 0.05 2 157 . 25 LEU HD1 H 0.822 0.05 1 158 . 25 LEU HD2 H 0.709 0.05 2 159 . 25 LEU HG H 1.708 0.05 1 160 . 26 GLY CA C 46.422 0.05 1 161 . 26 GLY HA2 H 4.300 0.05 2 162 . 26 GLY HA3 H 3.921 0.05 2 163 . 26 GLY H H 9.435 0.05 1 164 . 26 GLY N N 107.290 0.05 1 165 . 27 ILE CA C 59.579 0.05 1 166 . 27 ILE CB C 42.426 0.05 1 167 . 27 ILE CD1 C 12.506 0.05 1 168 . 27 ILE CG1 C 26.001 0.05 1 169 . 27 ILE CG2 C 19.009 0.05 1 170 . 27 ILE HA H 4.981 0.05 1 171 . 27 ILE HB H 1.627 0.05 1 172 . 27 ILE HD1 H 0.480 0.05 1 173 . 27 ILE HG12 H 1.383 0.05 2 174 . 27 ILE HG13 H 0.633 0.05 2 175 . 27 ILE HG2 H 0.730 0.05 1 176 . 27 ILE H H 7.821 0.05 1 177 . 27 ILE N N 116.157 0.05 1 178 . 28 SER CA C 56.310 0.05 1 179 . 28 SER CB C 64.107 0.05 1 180 . 28 SER HA H 5.519 0.05 1 181 . 28 SER HB2 H 3.704 0.05 2 182 . 28 SER HB3 H 3.593 0.05 2 183 . 28 SER H H 8.802 0.05 1 184 . 28 SER N N 118.470 0.05 1 185 . 29 VAL CA C 58.643 0.05 1 186 . 29 VAL CB C 35.197 0.05 1 187 . 29 VAL CG1 C 21.619 0.05 1 188 . 29 VAL CG2 C 17.148 0.05 1 189 . 29 VAL HA H 5.541 0.05 1 190 . 29 VAL HB H 2.033 0.05 1 191 . 29 VAL HG1 H 0.622 0.05 1 192 . 29 VAL HG2 H 0.663 0.05 1 193 . 29 VAL H H 9.353 0.05 1 194 . 29 VAL N N 118.084 0.05 1 195 . 30 THR CA C 58.737 0.05 1 196 . 30 THR CB C 72.150 0.05 1 197 . 30 THR CG2 C 19.319 0.05 1 198 . 30 THR HA H 5.474 0.05 1 199 . 30 THR HB H 3.981 0.05 1 200 . 30 THR HG2 H 1.197 0.05 1 201 . 30 THR H H 9.287 0.05 1 202 . 30 THR N N 115.880 0.05 1 203 . 31 GLY CA C 44.774 0.05 1 204 . 31 GLY HA2 H 5.822 0.05 2 205 . 31 GLY HA3 H 4.155 0.05 2 206 . 31 GLY H H 8.105 0.05 1 207 . 31 GLY N N 110.374 0.05 1 208 . 32 GLY CA C 43.293 0.05 1 209 . 32 GLY HA2 H 4.694 0.05 2 210 . 32 GLY HA3 H 3.724 0.05 2 211 . 32 GLY H H 6.963 0.05 1 212 . 32 GLY N N 105.747 0.05 1 213 . 33 VAL CA C 64.776 0.05 1 214 . 33 VAL CB C 31.698 0.05 1 215 . 33 VAL CG1 C 21.554 0.05 1 216 . 33 VAL CG2 C 19.485 0.05 1 217 . 33 VAL HA H 4.159 0.05 1 218 . 33 VAL HB H 2.184 0.05 1 219 . 33 VAL HG1 H 0.982 0.05 1 220 . 33 VAL HG2 H 0.982 0.05 1 221 . 33 VAL H H 8.546 0.05 1 222 . 33 VAL N N 116.928 0.05 1 223 . 34 ASN CA C 53.231 0.05 1 224 . 34 ASN CB C 36.779 0.05 1 225 . 34 ASN HA H 4.830 0.05 1 226 . 34 ASN HB2 H 3.195 0.05 2 227 . 34 ASN HB3 H 2.795 0.05 2 228 . 34 ASN HD21 H 7.914 0.05 2 229 . 34 ASN HD22 H 7.325 0.05 2 230 . 34 ASN H H 9.203 0.05 1 231 . 34 ASN N N 116.157 0.05 1 232 . 35 THR H H 7.729 0.05 1 233 . 36 SER CA C 58.056 0.05 1 234 . 36 SER CB C 63.546 0.05 1 235 . 36 SER HA H 4.614 0.05 1 236 . 36 SER HB2 H 4.019 0.05 2 237 . 36 SER HB3 H 3.911 0.05 2 238 . 36 SER H H 8.406 0.05 1 239 . 36 SER N N 113.072 0.05 1 240 . 37 VAL CA C 62.338 0.05 1 241 . 37 VAL CB C 32.467 0.05 1 242 . 37 VAL CG1 C 21.043 0.05 1 243 . 37 VAL CG2 C 21.452 0.05 1 244 . 37 VAL HA H 4.073 0.05 1 245 . 37 VAL HB H 2.183 0.05 1 246 . 37 VAL HG1 H 1.151 0.05 1 247 . 37 VAL HG2 H 1.034 0.05 1 248 . 37 VAL H H 7.579 0.05 1 249 . 37 VAL N N 118.450 0.05 1 250 . 38 ARG CA C 58.410 0.05 1 251 . 38 ARG CB C 29.589 0.05 1 252 . 38 ARG CD C 43.203 0.05 1 253 . 38 ARG CG C 26.621 0.05 1 254 . 38 ARG HA H 3.958 0.05 1 255 . 38 ARG HB2 H 1.641 0.05 2 256 . 38 ARG HB3 H 1.518 0.05 2 257 . 38 ARG HD2 H 3.022 0.05 1 258 . 38 ARG HD3 H 3.022 0.05 1 259 . 38 ARG HG2 H 1.331 0.05 2 260 . 38 ARG HG3 H 1.035 0.05 2 261 . 38 ARG H H 8.598 0.05 1 262 . 38 ARG N N 125.795 0.05 1 263 . 39 HIS CA C 57.040 0.05 1 264 . 39 HIS CB C 28.924 0.05 1 265 . 39 HIS HA H 4.580 0.05 1 266 . 39 HIS HB2 H 3.429 0.05 2 267 . 39 HIS HB3 H 3.323 0.05 2 268 . 39 HIS HD2 H 7.028 0.05 2 269 . 39 HIS ND1 N 209.317 0.05 1 270 . 39 HIS CE1 C 138.33 0.05 1 271 . 39 HIS HE1 H 8.040 0.05 1 272 . 39 HIS NE2 N 179.292 0.05 1 273 . 39 HIS CD2 C 120.025 0.05 1 274 . 40 GLY CA C 46.883 0.05 1 275 . 40 GLY HA2 H 3.895 0.05 2 276 . 40 GLY HA3 H 3.692 0.05 2 277 . 40 GLY H H 8.566 0.05 1 278 . 40 GLY N N 109.217 0.05 1 279 . 41 GLY CA C 44.598 0.05 1 280 . 41 GLY HA2 H 3.947 0.05 2 281 . 41 GLY HA3 H 3.245 0.05 2 282 . 41 GLY H H 7.756 0.05 1 283 . 41 GLY N N 104.591 0.05 1 284 . 42 ILE CB C 35.601 0.05 1 285 . 42 ILE CD1 C 9.0315 0.05 1 286 . 42 ILE CG1 C 26.080 0.05 1 287 . 42 ILE CG2 C 16.314 0.05 1 288 . 42 ILE HA H 4.792 0.05 1 289 . 42 ILE HB H 2.111 0.05 1 290 . 42 ILE HD1 H 0.471 0.05 1 291 . 42 ILE HG12 H 1.725 0.05 2 292 . 42 ILE HG13 H 1.063 0.05 2 293 . 42 ILE HG2 H 0.526 0.05 1 294 . 42 ILE H H 8.398 0.05 1 295 . 42 ILE N N 118.855 0.05 1 296 . 43 TYR CA C 56.024 0.05 1 297 . 43 TYR CB C 42.508 0.05 1 298 . 43 TYR HA H 5.306 0.05 1 299 . 43 TYR HB2 H 2.684 0.05 2 300 . 43 TYR HB3 H 2.474 0.05 2 301 . 43 TYR HD1 H 6.930 0.05 1 302 . 43 TYR HD2 H 6.930 0.05 1 303 . 43 TYR HE1 H 6.886 0.05 1 304 . 43 TYR HE2 H 6.886 0.05 1 305 . 43 TYR H H 8.988 0.05 1 306 . 43 TYR N N 123.096 0.05 1 307 . 44 VAL CA C 63.787 0.05 1 308 . 44 VAL CB C 31.464 0.05 1 309 . 44 VAL CG1 C 21.946 0.05 1 310 . 44 VAL CG2 C 20.840 0.05 1 311 . 44 VAL HA H 3.928 0.05 1 312 . 44 VAL HB H 2.314 0.05 1 313 . 44 VAL HG1 H 0.691 0.05 1 314 . 44 VAL HG2 H 0.719 0.05 1 315 . 44 VAL H H 9.222 0.05 1 316 . 44 VAL N N 120.449 0.05 1 317 . 45 LYS CA C 56.281 0.05 1 318 . 45 LYS CB C 33.834 0.05 1 319 . 45 LYS CD C 28.822 0.05 1 320 . 45 LYS CE C 42.612 0.05 1 321 . 45 LYS CG C 24.743 0.05 1 322 . 45 LYS HA H 4.415 0.05 1 323 . 45 LYS HB2 H 1.760 0.05 2 324 . 45 LYS HB3 H 1.473 0.05 2 325 . 45 LYS HD2 H 1.749 0.05 2 326 . 45 LYS HD3 H 1.536 0.05 2 327 . 45 LYS HE2 H 2.946 0.05 1 328 . 45 LYS HE3 H 2.946 0.05 1 329 . 45 LYS HG2 H 1.465 0.05 2 330 . 45 LYS HG3 H 1.386 0.05 2 331 . 45 LYS H H 9.617 0.05 1 332 . 45 LYS N N 134.727 0.05 1 333 . 46 ALA CA C 51.454 0.05 1 334 . 46 ALA CB C 22.339 0.05 1 335 . 46 ALA HA H 4.519 0.05 1 336 . 46 ALA HB H 1.295 0.05 1 337 . 46 ALA H H 7.677 0.05 1 338 . 46 ALA N N 117.308 0.05 1 339 . 47 ILE CA C 58.239 0.05 1 340 . 47 ILE CB C 36.693 0.05 1 341 . 47 ILE CD1 C 11.372 0.05 1 342 . 47 ILE CG1 C 26.059 0.05 1 343 . 47 ILE CG2 C 17.807 0.05 1 344 . 47 ILE HA H 4.318 0.05 1 345 . 47 ILE HB H 2.040 0.05 1 346 . 47 ILE HD1 H 0.494 0.05 1 347 . 47 ILE HG12 H 1.416 0.05 2 348 . 47 ILE HG13 H 1.306 0.05 2 349 . 47 ILE HG2 H 0.803 0.05 1 350 . 47 ILE H H 8.730 0.05 1 351 . 47 ILE N N 121.020 0.05 1 352 . 48 ILE CA C 58.817 0.05 1 353 . 48 ILE CB C 37.857 0.05 1 354 . 48 ILE CD1 C 11.022 0.05 1 355 . 48 ILE CG1 C 27.623 0.05 1 356 . 48 ILE CG2 C 16.048 0.05 1 357 . 48 ILE HA H 4.180 0.05 1 358 . 48 ILE HB H 1.594 0.05 1 359 . 48 ILE HD1 H 0.716 0.05 1 360 . 48 ILE HG12 H 1.365 0.05 2 361 . 48 ILE HG13 H 1.092 0.05 2 362 . 48 ILE HG2 H 0.941 0.05 1 363 . 48 ILE H H 7.755 0.05 1 364 . 48 ILE N N 129.587 0.05 1 365 . 49 PRO CA C 64.245 0.05 1 366 . 49 PRO CB C 31.944 0.05 1 367 . 49 PRO CD C 51.784 0.05 1 368 . 49 PRO CG C 27.888 0.05 1 369 . 49 PRO HA H 4.500 0.05 1 370 . 49 PRO HB2 H 2.404 0.05 2 371 . 49 PRO HB3 H 1.846 0.05 2 372 . 49 PRO HD2 H 4.129 0.05 2 373 . 49 PRO HD3 H 3.616 0.05 2 374 . 49 PRO HG2 H 2.136 0.05 2 375 . 49 PRO HG3 H 2.009 0.05 2 376 . 50 LYS CA C 57.970 0.05 1 377 . 50 LYS CB C 29.302 0.05 1 378 . 50 LYS CG C 25.514 0.05 1 379 . 50 LYS HA H 3.867 0.05 1 380 . 50 LYS HB2 H 2.162 0.05 2 381 . 50 LYS HB3 H 2.024 0.05 2 382 . 50 LYS HG2 H 1.377 0.05 1 383 . 50 LYS HG3 H 1.377 0.05 1 384 . 50 LYS H H 9.366 0.05 1 385 . 50 LYS N N 117.879 0.05 1 386 . 51 GLY CA C 44.921 0.05 1 387 . 51 GLY HA2 H 4.270 0.05 2 388 . 51 GLY HA3 H 3.883 0.05 2 389 . 51 GLY H H 7.745 0.05 1 390 . 51 GLY N N 106.171 0.05 1 391 . 52 ALA CA C 55.262 0.05 1 392 . 52 ALA CB C 18.438 0.05 1 393 . 52 ALA HA H 4.057 0.05 1 394 . 52 ALA H H 8.910 0.05 1 395 . 52 ALA N N 121.939 0.05 1 396 . 53 ALA CA C 54.942 0.05 1 397 . 53 ALA CB C 18.502 0.05 1 398 . 53 ALA HA H 4.064 0.05 1 399 . 53 ALA HB H 1.276 0.05 1 400 . 53 ALA H H 8.143 0.05 1 401 . 53 ALA N N 119.592 0.05 1 402 . 54 GLU CA C 60.034 0.05 1 403 . 54 GLU CB C 29.686 0.05 1 404 . 54 GLU CG C 37.555 0.05 1 405 . 54 GLU HA H 3.791 0.05 1 406 . 54 GLU HB2 H 2.122 0.05 2 407 . 54 GLU HB3 H 2.011 0.05 2 408 . 54 GLU HG2 H 2.123 0.05 1 409 . 54 GLU HG3 H 2.123 0.05 1 410 . 54 GLU H H 9.470 0.05 1 411 . 54 GLU N N 124.447 0.05 1 412 . 55 SER CA C 61.256 0.05 1 413 . 55 SER CB C 62.853 0.05 1 414 . 55 SER HA H 4.140 0.05 1 415 . 55 SER HB2 H 3.983 0.05 2 416 . 55 SER HB3 H 3.939 0.05 2 417 . 55 SER H H 7.954 0.05 1 418 . 55 SER N N 113.310 0.05 1 419 . 56 ASP CA C 57.339 0.05 1 420 . 56 ASP CB C 44.360 0.05 1 421 . 56 ASP HA H 4.424 0.05 1 422 . 56 ASP HB2 H 2.687 0.05 2 423 . 56 ASP HB3 H 2.583 0.05 2 424 . 56 ASP H H 7.751 0.05 1 425 . 56 ASP N N 120.164 0.05 1 426 . 57 GLY CA C 46.486 0.05 1 427 . 57 GLY HA2 H 4.099 0.05 2 428 . 57 GLY HA3 H 3.892 0.05 2 429 . 57 GLY H H 7.503 0.05 1 430 . 57 GLY N N 102.744 0.05 1 431 . 58 ARG CA C 58.071 0.05 1 432 . 58 ARG CB C 33.105 0.05 1 433 . 58 ARG CD C 44.165 0.05 1 434 . 58 ARG CG C 27.454 0.05 1 435 . 58 ARG HA H 4.264 0.05 1 436 . 58 ARG HB2 H 2.056 0.05 2 437 . 58 ARG HB3 H 1.731 0.05 2 438 . 58 ARG HD2 H 3.235 0.05 2 439 . 58 ARG HD3 H 3.084 0.05 2 440 . 58 ARG HG2 H 1.617 0.05 1 441 . 58 ARG HG3 H 1.617 0.05 1 442 . 58 ARG H H 8.034 0.05 1 443 . 58 ARG N N 117.593 0.05 1 444 . 59 ILE CA C 61.716 0.05 1 445 . 59 ILE CB C 39.229 0.05 1 446 . 59 ILE CD1 C 14.612 0.05 1 447 . 59 ILE CG1 C 28.369 0.05 1 448 . 59 ILE CG2 C 18.423 0.05 1 449 . 59 ILE HA H 4.189 0.05 1 450 . 59 ILE HB H 1.440 0.05 1 451 . 59 ILE HD1 H 0.741 0.05 1 452 . 59 ILE HG12 H 1.802 0.05 2 453 . 59 ILE HG13 H 0.881 0.05 2 454 . 59 ILE HG2 H 0.862 0.05 1 455 . 59 ILE H H 8.401 0.05 1 456 . 59 ILE N N 119.878 0.05 1 457 . 60 HIS CB C 33.068 0.05 1 458 . 60 HIS HA H 4.792 0.05 1 459 . 60 HIS HB2 H 3.306 0.05 2 460 . 60 HIS HB3 H 2.990 0.05 2 461 . 60 HIS H H 9.201 0.05 1 462 . 60 HIS N N 123.876 0.05 1 463 . 60 HIS ND1 N 191.156 0.05 1 464 . 60 HIS CE1 C 136.049 0.05 1 465 . 60 HIS HE1 H 8.182 0.05 1 466 . 60 HIS NE2 N 174.477 0.05 1 467 . 60 HIS CD2 C 119.583 0.05 1 468 . 60 HIS HD2 H 7.214 0.05 1 469 . 61 LYS CA C 58.434 0.05 1 470 . 61 LYS CB C 32.398 0.05 1 471 . 61 LYS CD C 29.923 0.05 1 472 . 61 LYS CE C 41.983 0.05 1 473 . 61 LYS CG C 24.534 0.05 1 474 . 61 LYS HA H 3.667 0.05 1 475 . 61 LYS HB2 H 1.744 0.05 2 476 . 61 LYS HB3 H 1.686 0.05 2 477 . 61 LYS HD2 H 1.775 0.05 1 478 . 61 LYS HD3 H 1.775 0.05 1 479 . 61 LYS HE2 H 3.072 0.05 1 480 . 61 LYS HE3 H 3.072 0.05 1 481 . 61 LYS HG2 H 1.505 0.05 2 482 . 61 LYS HG3 H 1.305 0.05 2 483 . 61 LYS H H 8.677 0.05 1 484 . 61 LYS N N 120.783 0.05 1 485 . 62 GLY CA C 44.895 0.05 1 486 . 62 GLY HA2 H 4.630 0.05 2 487 . 62 GLY HA3 H 3.656 0.05 2 488 . 62 GLY H H 9.302 0.05 1 489 . 62 GLY N N 114.229 0.05 1 490 . 63 ASP CA C 55.837 0.05 1 491 . 63 ASP CB C 41.221 0.05 1 492 . 63 ASP HA H 4.906 0.05 1 493 . 63 ASP HB2 H 2.739 0.05 2 494 . 63 ASP HB3 H 2.626 0.05 2 495 . 63 ASP H H 7.996 0.05 1 496 . 64 ARG CB C 33.985 0.05 1 497 . 64 ARG CD C 44.335 0.05 1 498 . 64 ARG CG C 27.411 0.05 1 499 . 64 ARG HA H 4.750 0.05 1 500 . 64 ARG HB2 H 1.813 0.05 2 501 . 64 ARG HB3 H 1.689 0.05 2 502 . 64 ARG HD2 H 3.009 0.05 2 503 . 64 ARG HD3 H 2.820 0.05 2 504 . 64 ARG HE H 7.515 0.05 1 505 . 64 ARG HG2 H 0.927 0.05 2 506 . 64 ARG HG3 H 0.823 0.05 2 507 . 64 ARG H H 9.009 0.05 1 508 . 64 ARG N N 122.710 0.05 1 509 . 65 VAL CA C 62.372 0.05 1 510 . 65 VAL CB C 31.142 0.05 1 511 . 65 VAL CG1 C 22.665 0.05 1 512 . 65 VAL CG2 C 19.946 0.05 1 513 . 65 VAL HA H 3.889 0.05 1 514 . 65 VAL HB H 1.748 0.05 1 515 . 65 VAL HG1 H 0.607 0.05 1 516 . 65 VAL HG2 H 0.539 0.05 1 517 . 65 VAL H H 8.977 0.05 1 518 . 65 VAL N N 126.446 0.05 1 519 . 66 LEU CA C 56.024 0.05 1 520 . 66 LEU CB C 42.927 0.05 1 521 . 66 LEU CD1 C 25.852 0.05 1 522 . 66 LEU CD2 C 21.636 0.05 1 523 . 66 LEU CG C 27.074 0.05 1 524 . 66 LEU HA H 4.490 0.05 1 525 . 66 LEU HB2 H 1.412 0.05 1 526 . 66 LEU HB3 H 1.412 0.05 1 527 . 66 LEU HD1 H 0.732 0.05 1 528 . 66 LEU HD2 H 0.691 0.05 2 529 . 66 LEU HG H 1.418 0.05 1 530 . 66 LEU H H 9.240 0.05 1 531 . 66 LEU N N 127.017 0.05 1 532 . 67 ALA CA C 52.215 0.05 1 533 . 67 ALA CB C 22.213 0.05 1 534 . 67 ALA HA H 5.005 0.05 1 535 . 67 ALA HB H 1.108 0.05 1 536 . 67 ALA H H 7.835 0.05 1 537 . 67 ALA N N 119.021 0.05 1 538 . 68 VAL CA C 60.363 0.05 1 539 . 68 VAL CB C 34.093 0.05 1 540 . 68 VAL CG1 C 20.700 0.05 1 541 . 68 VAL CG2 C 20.808 0.05 1 542 . 68 VAL HA H 4.501 0.05 1 543 . 68 VAL HB H 1.764 0.05 1 544 . 68 VAL HG1 H 0.721 0.05 1 545 . 68 VAL HG2 H 0.645 0.05 1 546 . 68 VAL H H 8.412 0.05 1 547 . 68 VAL N N 119.878 0.05 1 548 . 69 ASN CA C 54.207 0.05 1 549 . 69 ASN CB C 36.979 0.05 1 550 . 69 ASN HA H 4.538 0.05 1 551 . 69 ASN HB2 H 3.178 0.05 2 552 . 69 ASN HB3 H 3.065 0.05 2 553 . 69 ASN HD21 H 7.873 0.05 2 554 . 69 ASN HD22 H 7.313 0.05 2 555 . 69 ASN H H 10.386 0.05 1 556 . 69 ASN N N 128.730 0.05 1 557 . 70 GLY CA C 45.204 0.05 1 558 . 70 GLY HA2 H 4.086 0.05 2 559 . 70 GLY HA3 H 3.508 0.05 2 560 . 70 GLY H H 9.055 0.05 1 561 . 70 GLY N N 103.601 0.05 1 562 . 71 VAL CA C 62.291 0.05 1 563 . 71 VAL CB C 31.805 0.05 1 564 . 71 VAL CG1 C 21.123 0.05 1 565 . 71 VAL CG2 C 20.873 0.05 1 566 . 71 VAL HA H 3.975 0.05 1 567 . 71 VAL HB H 2.219 0.05 1 568 . 71 VAL HG1 H 0.931 0.05 1 569 . 71 VAL HG2 H 0.908 0.05 1 570 . 71 VAL H H 8.124 0.05 1 571 . 71 VAL N N 123.876 0.05 1 572 . 72 SER CA C 58.388 0.05 1 573 . 72 SER CB C 63.671 0.05 1 574 . 72 SER HA H 4.364 0.05 1 575 . 72 SER HB2 H 4.059 0.05 2 576 . 72 SER HB3 H 3.833 0.05 2 577 . 72 SER H H 8.686 0.05 1 578 . 72 SER N N 121.020 0.05 1 579 . 73 LEU CA C 53.993 0.05 1 580 . 73 LEU CB C 40.981 0.05 1 581 . 73 LEU CD1 C 25.631 0.05 1 582 . 73 LEU CD2 C 22.730 0.05 1 583 . 73 LEU HA H 4.435 0.05 1 584 . 73 LEU HB2 H 1.661 0.05 2 585 . 73 LEU HB3 H 1.493 0.05 2 586 . 73 LEU HD1 H 0.633 0.05 1 587 . 73 LEU HD2 H 0.717 0.05 2 588 . 73 LEU H H 8.201 0.05 1 589 . 73 LEU N N 124.638 0.05 1 590 . 74 GLU CA C 58.448 0.05 1 591 . 74 GLU CB C 29.159 0.05 1 592 . 74 GLU CG C 35.748 0.05 1 593 . 74 GLU HA H 4.028 0.05 1 594 . 74 GLU HB2 H 1.942 0.05 2 595 . 74 GLU HB3 H 1.869 0.05 2 596 . 74 GLU HG2 H 2.191 0.05 1 597 . 74 GLU HG3 H 2.191 0.05 1 598 . 74 GLU H H 8.300 0.05 1 599 . 74 GLU N N 123.096 0.05 1 600 . 75 GLY CA C 45.460 0.05 1 601 . 75 GLY HA2 H 4.186 0.05 2 602 . 75 GLY HA3 H 3.647 0.05 2 603 . 75 GLY H H 9.112 0.05 1 604 . 75 GLY N N 115.309 0.05 1 605 . 76 ALA CA C 52.723 0.05 1 606 . 76 ALA CB C 19.459 0.05 1 607 . 76 ALA HA H 4.499 0.05 1 608 . 76 ALA HB H 1.426 0.05 1 609 . 76 ALA H H 7.954 0.05 1 610 . 76 ALA N N 122.162 0.05 1 611 . 77 THR CA C 61.317 0.05 1 612 . 77 THR CB C 71.514 0.05 1 613 . 77 THR CG2 C 22.152 0.05 1 614 . 77 THR HA H 4.437 0.05 1 615 . 77 THR HB H 4.631 0.05 1 616 . 77 THR HG2 H 1.322 0.05 1 617 . 77 THR H H 8.361 0.05 1 618 . 77 THR N N 112.295 0.05 1 619 . 78 HIS CA C 62.180 0.05 1 620 . 78 HIS CB C 29.178 0.05 1 621 . 78 HIS HA H 3.947 0.05 1 622 . 78 HIS HB2 H 3.496 0.05 2 623 . 78 HIS HB3 H 3.246 0.05 2 624 . 78 HIS HD2 H 6.652 0.05 2 625 . 78 HIS H H 9.199 0.05 1 626 . 78 HIS N N 121.591 0.05 1 627 . 78 HIS CE1 C 138.848 0.05 1 628 . 78 HIS HE1 H 7.336 0.05 1 629 . 78 HIS NE2 N 169.555 0.05 1 630 . 78 HIS CD2 C 117.416 0.05 1 631 . 79 LYS CA C 59.562 0.05 1 632 . 79 LYS CB C 33.009 0.05 1 633 . 79 LYS CD C 29.599 0.05 1 634 . 79 LYS CE C 42.176 0.05 1 635 . 79 LYS CG C 24.935 0.05 1 636 . 79 LYS HA H 3.922 0.05 1 637 . 79 LYS HB2 H 1.975 0.05 2 638 . 79 LYS HB3 H 1.714 0.05 2 639 . 79 LYS HD2 H 1.731 0.05 2 640 . 79 LYS HD3 H 1.668 0.05 2 641 . 79 LYS HE2 H 3.005 0.05 1 642 . 79 LYS HE3 H 3.005 0.05 1 643 . 79 LYS HG2 H 1.505 0.05 2 644 . 79 LYS HG3 H 1.378 0.05 2 645 . 79 LYS H H 8.707 0.05 1 646 . 79 LYS N N 115.771 0.05 1 647 . 80 GLN CA C 58.513 0.05 1 648 . 80 GLN CB C 28.656 0.05 1 649 . 80 GLN CG C 34.064 0.05 1 650 . 80 GLN HA H 4.034 0.05 1 651 . 80 GLN HB2 H 2.235 0.05 2 652 . 80 GLN HB3 H 1.992 0.05 2 653 . 80 GLN HE21 H 7.489 0.05 2 654 . 80 GLN HE22 H 6.814 0.05 2 655 . 80 GLN HG2 H 2.398 0.05 1 656 . 80 GLN HG3 H 2.398 0.05 1 657 . 80 GLN H H 7.664 0.05 1 658 . 80 GLN N N 117.593 0.05 1 659 . 81 ALA CA C 55.332 0.05 1 660 . 81 ALA CB C 18.957 0.05 1 661 . 81 ALA HA H 3.840 0.05 1 662 . 81 ALA HB H 1.314 0.05 1 663 . 81 ALA H H 8.528 0.05 1 664 . 81 ALA N N 123.096 0.05 1 665 . 82 VAL CA C 67.451 0.05 1 666 . 82 VAL CB C 31.647 0.05 1 667 . 82 VAL CG1 C 23.345 0.05 1 668 . 82 VAL CG2 C 21.556 0.05 1 669 . 82 VAL HA H 3.224 0.05 1 670 . 82 VAL HB H 2.044 0.05 1 671 . 82 VAL HG1 H 0.553 0.05 1 672 . 82 VAL HG2 H 0.797 0.05 1 673 . 82 VAL H H 8.363 0.05 1 674 . 82 VAL N N 118.084 0.05 1 675 . 83 GLU CA C 59.839 0.05 1 676 . 83 GLU CB C 29.016 0.05 1 677 . 83 GLU CG C 36.711 0.05 1 678 . 83 GLU HA H 3.920 0.05 1 679 . 83 GLU HB2 H 2.106 0.05 2 680 . 83 GLU HB3 H 2.015 0.05 2 681 . 83 GLU HG2 H 2.418 0.05 2 682 . 83 GLU HG3 H 2.280 0.05 2 683 . 83 GLU H H 8.379 0.05 1 684 . 83 GLU N N 119.241 0.05 1 685 . 84 THR CA C 66.821 0.05 1 686 . 84 THR CB C 68.248 0.05 1 687 . 84 THR CG2 C 21.480 0.05 1 688 . 84 THR HA H 3.894 0.05 1 689 . 84 THR HB H 4.214 0.05 1 690 . 84 THR HG2 H 1.061 0.05 1 691 . 84 THR H H 8.045 0.05 1 692 . 84 THR N N 116.157 0.05 1 693 . 85 LEU CA C 58.545 0.05 1 694 . 85 LEU CB C 42.514 0.05 1 695 . 85 LEU CD1 C 25.687 0.05 1 696 . 85 LEU CD2 C 24.937 0.05 1 697 . 85 LEU CG C 28.146 0.05 1 698 . 85 LEU HA H 3.812 0.05 1 699 . 85 LEU HB2 H 2.043 0.05 2 700 . 85 LEU HB3 H 1.184 0.05 2 701 . 85 LEU HD1 H 0.666 0.05 1 702 . 85 LEU HD2 H 0.668 0.05 2 703 . 85 LEU HG H 1.542 0.05 1 704 . 85 LEU H H 8.074 0.05 1 705 . 85 LEU N N 119.878 0.05 1 706 . 86 ARG CA C 58.697 0.05 1 707 . 86 ARG CB C 31.164 0.05 1 708 . 86 ARG CD C 43.817 0.05 1 709 . 86 ARG CG C 28.198 0.05 1 710 . 86 ARG HA H 4.264 0.05 1 711 . 86 ARG HB2 H 1.869 0.05 1 712 . 86 ARG HB3 H 1.869 0.05 1 713 . 86 ARG HD2 H 3.133 0.05 1 714 . 86 ARG HD3 H 3.133 0.05 1 715 . 86 ARG HE H 7.177 0.05 1 716 . 86 ARG HG2 H 1.891 0.05 2 717 . 86 ARG HG3 H 1.696 0.05 2 718 . 86 ARG H H 8.589 0.05 1 719 . 86 ARG N N 118.470 0.05 1 720 . 86 ARG NE N 121.692 0.05 1 721 . 87 ASN CA C 52.723 0.05 1 722 . 87 ASN CB C 36.737 0.05 1 723 . 87 ASN HA H 4.987 0.05 1 724 . 87 ASN HB2 H 2.967 0.05 2 725 . 87 ASN HB3 H 2.818 0.05 2 726 . 87 ASN HD22 H 6.878 0.05 2 727 . 87 ASN H H 7.986 0.05 1 728 . 87 ASN N N 120.783 0.05 1 729 . 88 THR CA C 59.916 0.05 1 730 . 88 THR CB C 72.7157 0.05 1 731 . 88 THR CG2 C 22.519 0.05 1 732 . 88 THR HA H 4.466 0.05 1 733 . 88 THR HB H 4.292 0.05 1 734 . 88 THR HG2 H 1.211 0.05 1 735 . 88 THR H H 7.727 0.05 1 736 . 88 THR N N 109.883 0.05 1 737 . 89 GLY CA C 44.090 0.05 1 738 . 89 GLY HA2 H 4.365 0.05 2 739 . 89 GLY HA3 H 3.785 0.05 2 740 . 89 GLY H H 8.483 0.05 1 741 . 89 GLY N N 109.603 0.05 1 742 . 90 GLN CA C 58.521 0.05 1 743 . 90 GLN CB C 29.034 0.05 1 744 . 90 GLN CG C 33.866 0.05 1 745 . 90 GLN HA H 3.987 0.05 1 746 . 90 GLN HB2 H 2.080 0.05 1 747 . 90 GLN HB3 H 2.080 0.05 1 748 . 90 GLN HE21 H 7.435 0.05 2 749 . 90 GLN HE22 H 6.919 0.05 2 750 . 90 GLN HG2 H 2.457 0.05 1 751 . 90 GLN HG3 H 2.457 0.05 1 752 . 90 GLN H H 8.233 0.05 1 753 . 90 GLN N N 117.699 0.05 1 754 . 91 VAL CA C 61.273 0.05 1 755 . 91 VAL CB C 33.122 0.05 1 756 . 91 VAL CG1 C 21.243 0.05 1 757 . 91 VAL CG2 C 21.247 0.05 1 758 . 91 VAL HA H 4.668 0.05 1 759 . 91 VAL HB H 1.837 0.05 1 760 . 91 VAL HG1 H 0.864 0.05 1 761 . 91 VAL HG2 H 0.684 0.05 1 762 . 91 VAL H H 7.759 0.05 1 763 . 91 VAL N N 116.166 0.05 1 764 . 92 VAL CA C 61.012 0.05 1 765 . 92 VAL CB C 34.948 0.05 1 766 . 92 VAL CG1 C 22.801 0.05 1 767 . 92 VAL CG2 C 22.421 0.05 1 768 . 92 VAL HA H 4.433 0.05 1 769 . 92 VAL HB H 1.859 0.05 1 770 . 92 VAL HG1 H 0.924 0.05 1 771 . 92 VAL HG2 H 0.867 0.05 2 772 . 92 VAL H H 9.071 0.05 1 773 . 92 VAL N N 128.445 0.05 1 774 . 93 HIS CA C 55.643 0.05 1 775 . 93 HIS CB C 30.873 0.05 1 776 . 93 HIS HA H 5.030 0.05 1 777 . 93 HIS HB2 H 3.203 0.05 2 778 . 93 HIS HB3 H 3.159 0.05 2 779 . 93 HIS HD1 H 0.003 0.05 1 780 . 93 HIS HD2 H 7.058 0.05 2 781 . 93 HIS H H 8.843 0.05 1 782 . 93 HIS N N 126.160 0.05 1 783 . 93 HIS ND1 N 211.448 0.05 1 784 . 93 HIS CE1 C 137.275 0.05 1 785 . 93 HIS HE1 H 7.921 0.05 1 786 . 93 HIS NE2 N 173.883 0.05 1 787 . 93 HIS CD2 C 118.478 0.05 1 788 . 94 LEU CA C 53.485 0.05 1 789 . 94 LEU CB C 45.306 0.05 1 790 . 94 LEU CD1 C 25.184 0.05 1 791 . 94 LEU CD2 C 25.184 0.05 1 792 . 94 LEU CG C 26.061 0.05 1 793 . 94 LEU HA H 5.007 0.05 1 794 . 94 LEU HB2 H 1.642 0.05 2 795 . 94 LEU HB3 H 1.041 0.05 2 796 . 94 LEU HD1 H 0.717 0.05 1 797 . 94 LEU HD2 H 0.717 0.05 1 798 . 94 LEU HG H 0.636 0.05 1 799 . 94 LEU H H 9.080 0.05 1 800 . 94 LEU N N 126.731 0.05 1 801 . 95 LEU CA C 53.875 0.05 1 802 . 95 LEU CB C 44.651 0.05 1 803 . 95 LEU CD1 C 25.663 0.05 1 804 . 95 LEU CD2 C 23.282 0.05 1 805 . 95 LEU CG C 27.730 0.05 1 806 . 95 LEU HA H 4.770 0.05 1 807 . 95 LEU HB2 H 1.744 0.05 2 808 . 95 LEU HB3 H 1.319 0.05 2 809 . 95 LEU HD1 H 0.802 0.05 1 810 . 95 LEU HD2 H 0.856 0.05 2 811 . 95 LEU HG H 1.323 0.05 1 812 . 95 LEU H H 8.065 0.05 1 813 . 95 LEU N N 124.161 0.05 1 814 . 96 LEU CA C 53.993 0.05 1 815 . 96 LEU CB C 45.591 0.05 1 816 . 96 LEU CD1 C 27.331 0.05 1 817 . 96 LEU CD2 C 27.391 0.05 1 818 . 96 LEU CG C 28.181 0.05 1 819 . 96 LEU HA H 5.303 0.05 1 820 . 96 LEU HB2 H 1.034 0.05 2 821 . 96 LEU HB3 H 0.203 0.05 2 822 . 96 LEU HD1 H 0.651 0.05 1 823 . 96 LEU HD2 H 0.447 0.05 2 824 . 96 LEU HG H 1.203 0.05 1 825 . 96 LEU H H 8.951 0.05 1 826 . 96 LEU N N 127.588 0.05 1 827 . 97 GLU CA C 53.993 0.05 1 828 . 97 GLU CB C 36.863 0.05 1 829 . 97 GLU CG C 34.055 0.05 1 830 . 97 GLU HA H 4.952 0.05 1 831 . 97 GLU HB2 H 2.010 0.05 1 832 . 97 GLU HB3 H 2.010 0.05 1 833 . 97 GLU HG2 H 2.006 0.05 2 834 . 97 GLU HG3 H 1.852 0.05 2 835 . 97 GLU H H 8.995 0.05 1 836 . 97 GLU N N 119.241 0.05 1 837 . 98 LYS CA C 56.278 0.05 1 838 . 98 LYS CB C 32.228 0.05 1 839 . 98 LYS CD C 28.847 0.05 1 840 . 98 LYS CE C 41.957 0.05 1 841 . 98 LYS CG C 23.776 0.05 1 842 . 98 LYS HA H 4.441 0.05 1 843 . 98 LYS HB2 H 2.277 0.05 2 844 . 98 LYS HB3 H 1.628 0.05 2 845 . 98 LYS HD2 H 1.838 0.05 2 846 . 98 LYS HD3 H 1.392 0.05 2 847 . 98 LYS HE2 H 2.729 0.05 1 848 . 98 LYS HE3 H 2.729 0.05 1 849 . 98 LYS HG2 H 1.631 0.05 2 850 . 98 LYS HG3 H 1.262 0.05 2 851 . 98 LYS H H 9.176 0.05 1 852 . 98 LYS N N 128.445 0.05 1 853 . 99 GLY CA C 45.501 0.05 1 854 . 99 GLY HA2 H 4.316 0.05 2 855 . 99 GLY HA3 H 3.845 0.05 2 856 . 99 GLY H H 9.561 0.05 1 857 . 100 GLN CA C 55.584 0.05 1 858 . 100 GLN CB C 30.070 0.05 1 859 . 100 GLN CG C 33.675 0.05 1 860 . 100 GLN HA H 4.321 0.05 1 861 . 100 GLN HB2 H 2.113 0.05 2 862 . 100 GLN HB3 H 1.918 0.05 2 863 . 100 GLN HG2 H 2.378 0.05 1 864 . 100 GLN HG3 H 2.378 0.05 1 865 . 100 GLN H H 8.243 0.05 1 866 . 100 GLN N N 117.593 0.05 1 867 . 101 VAL CA C 60.010 0.05 1 868 . 101 VAL CB C 32.546 0.05 1 869 . 101 VAL CG1 C 21.220 0.05 1 870 . 101 VAL CG2 C 20.493 0.05 1 871 . 101 VAL HA H 4.376 0.05 1 872 . 101 VAL HB H 2.092 0.05 1 873 . 101 VAL HG1 H 0.967 0.05 1 874 . 101 VAL HG2 H 0.925 0.05 1 875 . 101 VAL H H 8.179 0.05 1 876 . 102 PRO CA C 62.737 0.05 1 877 . 102 PRO CB C 32.546 0.05 1 878 . 102 PRO CD C 50.746 0.05 1 879 . 102 PRO CG C 27.268 0.05 1 880 . 102 PRO HA H 4.410 0.05 1 881 . 102 PRO HB2 H 2.093 0.05 1 882 . 102 PRO HB3 H 2.093 0.05 1 883 . 102 PRO HD2 H 3.810 0.05 2 884 . 102 PRO HD3 H 3.631 0.05 2 885 . 102 PRO HG2 H 1.967 0.05 2 886 . 102 PRO HG3 H 1.879 0.05 2 stop_ save_ save_T1_values _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 600 _T1_coherence_type Nz _T1_value_units s-1 _Mol_system_component_name 'PDZ2 from PTP-BL' _Text_data_format . _Text_data . loop_ _T1_ID _Residue_seq_code _Residue_label _Atom_name _T1_value _T1_value_error 1 9 LYS N 1.50716 0.075358 2 11 GLY N 1.71248 0.085624 3 12 ASP N 1.74034 0.087017 4 13 THR N 1.64704 0.082352 5 14 PHE N 1.61005 0.0805025 6 17 GLU N 1.50886 0.075443 7 19 ALA N 1.57146 0.078573 8 20 LYS N 1.62668 0.081334 9 21 THR N 1.54202 0.077101 10 22 ASP N 1.59821 0.0799105 11 23 GLY N 1.63465 0.0817325 12 24 SER N 1.62787 0.0813935 13 26 GLY N 1.61134 0.080567 14 27 ILE N 1.73958 0.086979 15 28 SER N 1.62232 0.081116 16 29 VAL N 1.67645 0.0838225 17 30 THR N 1.62483 0.0812415 18 31 GLY N 1.62986 0.081493 19 32 GLY N 1.53539 0.0767695 20 33 VAL N 1.71659 0.0858295 21 34 ASN N 1.82216 0.091108 22 36 SER N 1.69794 0.084897 23 37 VAL N 1.71116 0.085558 24 38 ARG N 1.73717 0.0868585 25 40 GLY N 1.83993 0.0919965 26 41 GLY N 1.74034 0.087017 27 42 ILE N 1.64055 0.0820275 28 43 TYR N 1.58743 0.0793715 29 44 VAL N 1.60167 0.0800835 30 45 LYS N 1.77132 0.088566 31 46 ALA N 1.63733 0.0818665 32 47 ILE N 1.59147 0.0795735 33 48 ILE N 1.73145 0.0865725 34 50 LYS N 1.56482 0.078241 35 51 GLY N 1.69434 0.084717 36 52 ALA N 1.63908 0.081954 37 53 ALA N 1.58366 0.079183 38 54 GLU N 1.66667 0.0833335 39 55 SER N 1.57766 0.078883 40 56 ASP N 1.61447 0.0807235 41 57 GLY N 1.58945 0.0794725 42 58 ARG N 1.6488 0.08244 43 60 HIS N 1.68039 0.0840195 44 62 GLY N 1.65604 0.082802 45 63 ASP N 1.75562 0.087781 46 64 ARG N 1.6276 0.08138 47 65 VAL N 1.58818 0.079409 48 66 LEU N 1.62364 0.081182 49 67 ALA N 1.63239 0.0816195 50 69 ASN N 1.716 0.0858 51 70 GLY N 1.73551 0.0867755 52 71 VAL N 1.66667 0.0833335 53 73 LEU N 1.58453 0.0792265 54 74 GLU N 1.61355 0.0806775 55 75 GLY N 1.66694 0.083347 56 76 ALA N 1.61381 0.0806905 57 77 THR N 1.6621 0.083105 58 78 HIS N 1.67392 0.083696 59 79 LYS N 1.60449 0.0802245 60 80 GLN N 1.6965 0.084825 61 81 ALA N 1.6889 0.084445 62 82 VAL N 1.62206 0.081103 63 83 GLU N 1.66168 0.083084 64 84 THR N 1.63425 0.0817125 65 85 LEU N 1.6292 0.08146 66 86 ARG N 1.60295 0.0801475 67 87 ASN N 1.58945 0.0794725 68 88 THR N 1.32793 0.0663965 69 89 GLY N 1.60888 0.080444 70 91 VAL N 1.62127 0.0810635 71 92 VAL N 1.66403 0.0832015 72 94 LEU N 1.5794 0.07897 73 95 LEU N 1.56104 0.078052 74 96 LEU N 1.61186 0.080593 75 97 GLU N 1.52882 0.076441 76 98 LYS N 1.68677 0.0843385 77 99 GLY N 1.71895 0.0859475 78 101 VAL N 1.61095 0.0805475 stop_ save_ save_T2_Values _Saveframe_category T2_relaxation _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 600 _T2_coherence_type Nx _T2_value_units s-1 _Mol_system_component_name 'PDZ2 from PTP-BL' _Text_data_format . _Text_data . loop_ _T2_ID _Residue_seq_code _Residue_label _Atom_name _T2_value _T2_value_error _Rex_value _Rex_error 1 9 LYS N 4.17745 0.208873 . . 2 11 GLY N 9.90542 0.495271 . . 3 12 ASP N 9.35933 0.467967 . . 4 13 THR N 9.76669 0.488335 . . 5 14 PHE N 11.2178 0.56089 . . 6 17 GLU N 9.31217 0.465609 . . 7 19 ALA N 9.22332 0.461166 . . 8 20 LYS N 8.92819 0.44641 . . 9 21 THR N 9.00544 0.450272 . . 10 22 ASP N 10.6218 0.53109 . . 11 23 GLY N 10.8539 0.542695 . . 12 24 SER N 10.3766 0.51883 . . 13 26 GLY N 11.1244 0.55622 . . 14 27 ILE N 10.6800 0.534 . . 15 28 SER N 10.0410 0.50205 . . 16 29 VAL N 10.3345 0.516725 . . 17 30 THR N 10.7101 0.535505 . . 18 31 GLY N 25.4426 1.27213 . . 19 32 GLY N 11.6051 0.580255 . . 20 33 VAL N 12.8045 0.640225 . . 21 34 ASN N 14.3556 0.71778 . . 22 36 SER N 12.5928 0.62964 . . 23 37 VAL N 17.4124 0.87062 . . 24 38 ARG N 14.8675 0.743375 . . 25 40 GLY N 10.1771 0.508855 . . 26 41 GLY N 16.2605 0.813025 . . 27 42 ILE N 11.7526 0.58763 . . 28 43 TYR N 10.2997 0.514985 . . 29 44 VAL N 10.1252 0.50626 . . 30 45 LYS N 11.1784 0.55892 . . 31 46 ALA N 8.90570 0.445285 . . 32 47 ILE N 9.10788 0.455394 . . 33 48 ILE N 10.0031 0.500155 . . 34 50 LYS N 9.39018 0.469509 . . 35 51 GLY N 10.0336 0.50168 . . 36 52 ALA N 10.6663 0.533315 . . 37 53 ALA N 9.90043 0.495022 . . 38 54 GLU N 11.0044 0.55022 . . 39 55 SER N 10.1437 0.507185 . . 40 56 ASP N 10.7541 0.537705 . . 41 57 GLY N 10.8653 0.543265 . . 42 58 ARG N 9.32190 0.466095 . . 43 60 HIS N 9.50135 0.475068 . . 44 62 GLY N 9.89381 0.494691 . . 45 63 ASP N 9.89021 0.494511 . . 46 64 ARG N 10.9855 0.549275 . . 47 65 VAL N 10.9791 0.548955 . . 48 66 LEU N 10.7709 0.538545 . . 49 67 ALA N 9.65816 0.482908 . . 50 69 ASN N 10.2553 0.512765 . . 51 70 GLY N 10.5743 0.528715 . . 52 71 VAL N 9.79414 0.489707 . . 53 73 LEU N 10.1103 0.505515 . . 54 74 GLU N 10.2212 0.51106 . . 55 75 GLY N 9.22395 0.461198 . . 56 76 ALA N 10.8695 0.543475 . . 57 77 THR N 12.3129 0.615645 . . 58 78 HIS N 10.6767 0.533835 . . 59 79 LYS N 10.8500 0.5425 . . 60 80 GLN N 10.3858 0.51929 . . 61 81 ALA N 10.6550 0.53275 . . 62 82 VAL N 10.3565 0.517825 . . 63 83 GLU N 10.5949 0.529745 . . 64 84 THR N 10.6785 0.533925 . . 65 85 LEU N 9.98472 0.499236 . . 66 86 ARG N 11.8994 0.59497 . . 67 87 ASN N 9.71121 0.485561 . . 68 88 THR N 7.49152 0.374576 . . 69 89 GLY N 9.26388 0.463194 . . 70 91 VAL N 8.68374 0.434187 . . 71 92 VAL N 9.65097 0.482548 . . 72 94 LEU N 10.4056 0.52028 . . 73 95 LEU N 10.1906 0.50953 . . 74 96 LEU N 11.0508 0.55254 . . 75 97 GLU N 10.2274 0.51137 . . 76 98 LYS N 10.9696 0.54848 . . 77 99 GLY N 10.8343 0.541715 . . 78 101 VAL N 3.82442 0.191221 . . stop_ save_ save_heteronuclear_NOE _Saveframe_category heteronuclear_NOE _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 600 _Mol_system_component_name 'PDZ2 from PTP-BL' _Atom_one_atom_name H _Atom_two_atom_name N _Heteronuclear_NOE_value_type . _NOE_reference_value . _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 9 LYS 0.11425 0.0057125 11 GLY 0.8264 0.04132 12 ASP 0.7169 0.035845 13 THR 0.8013 0.040065 14 PHE 0.8305 0.041525 17 GLU 0.81145 0.0405725 19 ALA 0.7287 0.036435 20 LYS 0.6787 0.033935 21 THR 0.6536 0.03268 22 ASP 0.7315 0.036575 23 GLY 0.7746 0.03873 24 SER 0.7249 0.036245 26 GLY 0.6965 0.034825 27 ILE 0.82855 0.0414275 28 SER 0.7756 0.03878 29 VAL 0.8434 0.04217 30 THR 0.8371 0.041855 31 GLY 0.5922 0.02961 32 GLY 0.7716 0.03858 33 VAL 0.7796 0.03898 34 ASN 0.6975 0.034875 35 THR 0.7901 0.039505 36 SER 0.74475 0.0372375 37 VAL 0.6897 0.034485 38 ARG 0.8203 0.041015 40 GLY 0.7514 0.03757 41 GLY 0.7049 0.035245 42 ILE 0.807 0.04035 43 TYR 0.8446 0.04223 44 VAL 0.8153 0.040765 45 LYS 0.7534 0.03767 46 ALA 0.716 0.0358 47 ILE 0.7609 0.038045 48 ILE 0.7707 0.038535 50 LYS 0.7501 0.037505 51 GLY 0.7698 0.03849 52 ALA 0.7582 0.03791 53 ALA 0.7658 0.03829 54 GLU 0.7867 0.039335 55 SER 0.8032 0.04016 56 ASP 0.7247 0.036235 57 GLY 0.8019 0.040095 58 ARG 0.7841 0.039205 60 HIS 0.735 0.03675 61 LYS 0.77545 0.0387725 62 GLY 0.8167 0.040835 63 ASP 0.7954 0.03977 64 ARG 0.8258 0.04129 65 VAL 0.8087 0.040435 66 LEU 0.7537 0.037685 67 ALA 0.775 0.03875 69 ASN 0.7594 0.03797 70 GLY 0.77795 0.0388975 71 VAL 0.7811 0.039055 72 SER 0.7484 0.03742 73 LEU 0.8234 0.04117 74 GLU 0.7435 0.037175 75 GLY 0.7618 0.03809 76 ALA 0.7341 0.036705 77 THR 0.8018 0.04009 78 HIS 0.8617 0.043085 79 LYS 0.8399 0.041995 80 GLN 0.7868 0.03934 81 ALA 0.8318 0.04159 82 VAL 0.7842 0.03921 83 GLU 0.8492 0.04246 84 THR 0.8161 0.040805 85 LEU 0.8242 0.04121 86 ARG 0.77715 0.0388575 87 ASN 0.7283 0.036415 88 THR 0.6465 0.032325 89 GLY 0.8049 0.040245 91 VAL 0.7602 0.03801 92 VAL 0.7693 0.038465 94 LEU 0.8334 0.04167 95 LEU 0.8084 0.04042 96 LEU 0.8357 0.041785 97 GLU 0.8024 0.04012 98 LYS 0.7562 0.03781 99 GLY 0.7856 0.03928 101 VAL 0.1843 0.009215 stop_ save_