data_6092 ####################### # 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 RIL (reversion induced LIM) ; _BMRB_accession_number 6092 _BMRB_flat_file_name bmr6092.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 T1_relaxation 1 T2_relaxation 1 heteronucl_NOE 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 498 "13C chemical shifts" 278 "15N chemical shifts" 105 "T1 relaxation values" 82 "T2 relaxation values" 82 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-08-11 update BMRB ; corrected sequence numbering in T1, T2, and heteronuclear NOE save frames updated T1 and T2 units from s to s-1 ; stop_ loop_ _Related_BMRB_accession_number _Relationship 5131 'Second PDZ domain of PTP-BL' 6060 'PDZ2 from PTP-BL (complex with APC)' 6091 'PDZ2 from PTP-BL (complex with NTR)' 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 'RIL C-terminus' $RIL 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 6091 '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_RIL _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C-terminus from RIL' _Abbreviation_common RIL _Molecular_mass 1301.55 _Mol_thiol_state 'not present' _Details 'At the N-terminal, non-interacting end there is a biotin tag.' _Residue_count 12 _Mol_residue_sequence VAVYPNAKVELV loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 201 VAL 2 202 ALA 3 203 VAL 4 204 TYR 5 205 PRO 6 206 ASN 7 207 ALA 8 208 LYS 9 209 VAL 10 2010 GLU 11 2011 LEU 12 2012 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' $RIL 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 $RIL '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PDZ2 1 mM 1 1 '[U-15N; U-13C]' $RIL 3.55 mM 3.55 3.55 . 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_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_ ####################### # 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 . . . 1.0 $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_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 59.034 0.05 1 2 . 9 LYS HA H 4.356 0.02 1 3 . 9 LYS H H 7.880 0.02 1 4 . 9 LYS N N 119.546 0.05 1 5 . 10 PRO CA C 64.682 0.05 1 6 . 10 PRO CB C 31.890 0.05 1 7 . 10 PRO CD C 50.142 0.05 1 8 . 10 PRO CG C 28.102 0.05 1 9 . 10 PRO HA H 3.975 0.02 1 10 . 10 PRO HB2 H 2.180 0.02 2 11 . 10 PRO HB3 H 1.845 0.02 2 12 . 10 PRO HD2 H 3.798 0.02 2 13 . 10 PRO HD3 H 3.554 0.02 2 14 . 10 PRO HG2 H 2.167 0.02 2 15 . 10 PRO HG3 H 1.996 0.02 2 16 . 11 GLY CA C 45.183 0.05 1 17 . 11 GLY HA2 H 4.376 0.02 2 18 . 11 GLY HA3 H 3.769 0.02 2 19 . 11 GLY H H 8.829 0.02 1 20 . 11 GLY N N 113.131 0.05 1 21 . 12 ASP CB C 41.596 0.05 1 22 . 12 ASP HA H 4.819 0.02 1 23 . 12 ASP HB2 H 3.013 0.02 2 24 . 12 ASP HB3 H 2.812 0.02 2 25 . 12 ASP H H 8.466 0.02 1 26 . 12 ASP N N 121.708 0.05 1 27 . 13 THR CA C 60.588 0.05 1 28 . 13 THR CB C 71.0754 0.05 1 29 . 13 THR CG2 C 21.980 0.05 1 30 . 13 THR HA H 5.671 0.02 1 31 . 13 THR HB H 4.140 0.02 1 32 . 13 THR HG2 H 1.145 0.02 1 33 . 13 THR H H 8.367 0.02 1 34 . 13 THR N N 112.773 0.05 1 35 . 14 PHE CA C 56.245 0.05 1 36 . 14 PHE CB C 40.505 0.05 1 37 . 14 PHE HA H 4.982 0.02 1 38 . 14 PHE HB2 H 3.170 0.02 2 39 . 14 PHE HB3 H 3.017 0.02 2 40 . 14 PHE HD1 H 6.832 0.02 1 41 . 14 PHE HD2 H 6.832 0.02 1 42 . 14 PHE HE1 H 6.872 0.02 1 43 . 14 PHE HE2 H 6.872 0.02 1 44 . 14 PHE H H 9.272 0.02 1 45 . 14 PHE N N 119.881 0.05 1 46 . 15 GLU CA C 54.178 0.05 1 47 . 15 GLU CB C 33.354 0.05 1 48 . 15 GLU CG C 37.382 0.05 1 49 . 15 GLU HA H 5.265 0.02 1 50 . 15 GLU HB2 H 1.876 0.02 1 51 . 15 GLU HB3 H 1.876 0.02 1 52 . 15 GLU HG2 H 2.190 0.02 2 53 . 15 GLU HG3 H 2.144 0.02 2 54 . 15 GLU H H 8.567 0.02 1 55 . 15 GLU N N 119.514 0.05 1 56 . 16 VAL CA C 60.840 0.05 1 57 . 16 VAL CB C 36.738 0.05 1 58 . 16 VAL CG1 C 22.454 0.05 1 59 . 16 VAL CG2 C 21.675 0.05 1 60 . 16 VAL HA H 4.171 0.02 1 61 . 16 VAL HB H 1.695 0.02 1 62 . 16 VAL HG1 H 0.789 0.02 1 63 . 16 VAL HG2 H 0.847 0.02 1 64 . 16 VAL H H 8.562 0.02 1 65 . 16 VAL N N 119.523 0.05 1 66 . 17 GLU CA C 54.858 0.05 1 67 . 17 GLU CB C 30.924 0.05 1 68 . 17 GLU CG C 37.179 0.05 1 69 . 17 GLU HA H 5.008 0.02 1 70 . 17 GLU HB2 H 1.846 0.02 1 71 . 17 GLU HB3 H 1.846 0.02 1 72 . 17 GLU HG2 H 1.833 0.02 1 73 . 17 GLU HG3 H 1.833 0.02 1 74 . 17 GLU H H 7.808 0.02 1 75 . 17 GLU N N 126.254 0.05 1 76 . 18 LEU CA C 53.350 0.05 1 77 . 18 LEU CB C 46.037 0.05 1 78 . 18 LEU CD1 C 25.172 0.05 1 79 . 18 LEU CG C 26.532 0.05 1 80 . 18 LEU HA H 4.659 0.02 1 81 . 18 LEU HB2 H 1.360 0.02 2 82 . 18 LEU HB3 H 1.296 0.02 2 83 . 18 LEU HD1 H 0.766 0.02 1 84 . 18 LEU HD2 H 0.766 0.02 1 85 . 18 LEU HG H 1.394 0.02 1 86 . 18 LEU H H 8.818 0.02 1 87 . 18 LEU N N 126.259 0.05 1 88 . 19 ALA CA C 49.953 0.05 1 89 . 19 ALA CB C 19.425 0.05 1 90 . 19 ALA HA H 5.134 0.02 1 91 . 19 ALA HB H 1.319 0.02 1 92 . 19 ALA H H 8.447 0.02 1 93 . 19 ALA N N 126.342 0.05 1 94 . 20 LYS CA C 57.674 0.05 1 95 . 20 LYS CB C 34.503 0.05 1 96 . 20 LYS CD C 30.095 0.05 1 97 . 20 LYS CE C 42.379 0.05 1 98 . 20 LYS CG C 27.339 0.05 1 99 . 20 LYS HA H 3.854 0.02 1 100 . 20 LYS HB2 H 1.400 0.02 1 101 . 20 LYS HB3 H 1.400 0.02 1 102 . 20 LYS HD2 H 1.469 0.02 2 103 . 20 LYS HD3 H 1.230 0.02 2 104 . 20 LYS HE2 H 2.856 0.02 2 105 . 20 LYS HE3 H 2.780 0.02 2 106 . 20 LYS HG2 H 0.803 0.02 1 107 . 20 LYS HG3 H 0.803 0.02 1 108 . 20 LYS H H 8.501 0.02 1 109 . 20 LYS N N 120.629 0.05 1 110 . 21 THR CA C 61.141 0.05 1 111 . 21 THR CB C 70.495 0.05 1 112 . 21 THR CG2 C 21.939 0.05 1 113 . 21 THR HA H 4.514 0.02 1 114 . 21 THR HB H 4.174 0.02 1 115 . 21 THR HG2 H 1.207 0.02 1 116 . 21 THR H H 8.099 0.02 1 117 . 21 THR N N 113.955 0.05 1 118 . 22 ASP CA C 55.363 0.05 1 119 . 22 ASP CB C 39.879 0.05 1 120 . 22 ASP HA H 4.318 0.02 1 121 . 22 ASP HB2 H 2.930 0.02 2 122 . 22 ASP HB3 H 2.656 0.02 2 123 . 22 ASP H H 9.346 0.02 1 124 . 22 ASP N N 125.685 0.05 1 125 . 23 GLY CA C 45.831 0.05 1 126 . 23 GLY HA2 H 4.170 0.02 2 127 . 23 GLY HA3 H 3.635 0.02 2 128 . 23 GLY H H 8.699 0.02 1 129 . 23 GLY N N 102.748 0.05 1 130 . 24 SER CA C 56.703 0.05 1 131 . 24 SER CB C 65.937 0.05 1 132 . 24 SER HA H 5.005 0.02 1 133 . 24 SER HB2 H 3.901 0.02 2 134 . 24 SER HB3 H 3.798 0.02 2 135 . 24 SER H H 7.991 0.02 1 136 . 24 SER N N 114.455 0.05 1 137 . 25 LEU CA C 56.379 0.05 1 138 . 25 LEU CB C 42.855 0.05 1 139 . 25 LEU CD1 C 23.491 0.05 1 140 . 25 LEU CG C 25.782 0.05 1 141 . 25 LEU HA H 4.242 0.02 1 142 . 25 LEU HB2 H 1.879 0.02 2 143 . 25 LEU HB3 H 1.302 0.02 2 144 . 25 LEU HD1 H 0.689 0.02 1 145 . 25 LEU HD2 H 0.689 0.02 1 146 . 25 LEU HG H 0.818 0.02 1 147 . 26 GLY CA C 46.584 0.05 1 148 . 26 GLY HA2 H 4.245 0.02 2 149 . 26 GLY HA3 H 3.832 0.02 2 150 . 26 GLY H H 9.163 0.02 1 151 . 26 GLY N N 106.798 0.05 1 152 . 27 ILE CA C 59.617 0.05 1 153 . 27 ILE CB C 42.543 0.05 1 154 . 27 ILE CD1 C 12.732 0.05 1 155 . 27 ILE CG1 C 26.161 0.05 1 156 . 27 ILE CG2 C 18.880 0.05 1 157 . 27 ILE HA H 4.994 0.02 1 158 . 27 ILE HB H 1.648 0.02 1 159 . 27 ILE HD1 H 0.495 0.02 1 160 . 27 ILE HG12 H 1.366 0.02 1 161 . 27 ILE HG2 H 0.724 0.02 1 162 . 27 ILE H H 7.774 0.02 1 163 . 27 ILE N N 116.245 0.05 1 164 . 28 SER CA C 56.035 0.05 1 165 . 28 SER CB C 65.243 0.05 1 166 . 28 SER HA H 5.366 0.02 1 167 . 28 SER HB2 H 3.742 0.02 1 168 . 28 SER HB3 H 3.742 0.02 1 169 . 28 SER H H 8.555 0.02 1 170 . 28 SER N N 118.090 0.05 1 171 . 29 VAL CA C 59.113 0.05 1 172 . 29 VAL CB C 35.628 0.05 1 173 . 29 VAL CG1 C 17.820 0.05 1 174 . 29 VAL CG2 C 21.543 0.05 1 175 . 29 VAL HA H 5.537 0.02 1 176 . 29 VAL HB H 2.057 0.02 1 177 . 29 VAL HG1 H 0.655 0.02 1 178 . 29 VAL HG2 H 0.617 0.02 1 179 . 29 VAL H H 9.234 0.02 1 180 . 29 VAL N N 116.897 0.05 1 181 . 30 THR CA C 59.617 0.05 1 182 . 30 THR CB C 71.300 0.05 1 183 . 30 THR CG2 C 18.903 0.05 1 184 . 30 THR HA H 4.941 0.02 1 185 . 30 THR HB H 3.930 0.02 1 186 . 30 THR HG2 H 1.122 0.02 1 187 . 30 THR H H 9.158 0.02 1 188 . 30 THR N N 116.439 0.05 1 189 . 31 GLY CA C 44.447 0.05 1 190 . 31 GLY HA2 H 5.356 0.02 2 191 . 31 GLY HA3 H 4.113 0.02 2 192 . 31 GLY H H 8.386 0.02 1 193 . 31 GLY N N 111.755 0.05 1 194 . 32 GLY CA C 43.763 0.05 1 195 . 32 GLY HA2 H 4.569 0.02 2 196 . 32 GLY HA3 H 3.748 0.02 2 197 . 32 GLY H H 7.433 0.02 1 198 . 32 GLY N N 107.002 0.05 1 199 . 33 VAL CA C 64.084 0.05 1 200 . 33 VAL CB C 31.843 0.05 1 201 . 33 VAL CG1 C 19.821 0.05 1 202 . 33 VAL CG2 C 21.370 0.05 1 203 . 33 VAL HA H 4.151 0.02 1 204 . 33 VAL HB H 2.116 0.02 1 205 . 33 VAL HG1 H 0.876 0.02 1 206 . 33 VAL HG2 H 0.934 0.02 1 207 . 33 VAL H H 8.184 0.02 1 208 . 33 VAL N N 116.859 0.05 1 209 . 34 ASN CA C 53.519 0.05 1 210 . 34 ASN CB C 37.712 0.05 1 211 . 34 ASN HA H 4.783 0.02 1 212 . 34 ASN HB2 H 3.088 0.02 2 213 . 34 ASN HB3 H 2.855 0.02 2 214 . 34 ASN HD21 H 7.748 0.02 2 215 . 34 ASN HD22 H 7.228 0.02 2 216 . 34 ASN H H 8.879 0.02 1 217 . 34 ASN N N 117.708 0.05 1 218 . 34 ASN ND2 N 115.242 0.05 1 219 . 35 THR HA H 4.468 0.02 1 220 . 35 THR HG2 H 1.084 0.02 1 221 . 35 THR H H 7.813 0.02 1 222 . 35 THR N N 111.266 0.05 1 223 . 36 SER CA C 58.437 0.05 1 224 . 36 SER CB C 63.653 0.05 1 225 . 36 SER HA H 4.536 0.02 1 226 . 36 SER HB2 H 4.016 0.02 2 227 . 36 SER HB3 H 3.891 0.02 2 228 . 36 SER H H 8.457 0.02 1 229 . 36 SER N N 112.912 0.05 1 230 . 37 VAL CA C 62.142 0.05 1 231 . 37 VAL CB C 32.499 0.05 1 232 . 37 VAL CG1 C 20.563 0.05 1 233 . 37 VAL CG2 C 21.343 0.05 1 234 . 37 VAL HA H 4.076 0.02 1 235 . 37 VAL HB H 2.138 0.02 1 236 . 37 VAL HG1 H 1.072 0.02 1 237 . 37 VAL HG2 H 0.968 0.02 1 238 . 37 VAL H H 7.560 0.02 1 239 . 37 VAL N N 118.139 0.05 1 240 . 38 ARG CA C 58.078 0.05 1 241 . 38 ARG CB C 29.758 0.05 1 242 . 38 ARG CD C 43.255 0.05 1 243 . 38 ARG CG C 26.779 0.05 1 244 . 38 ARG HA H 3.997 0.02 1 245 . 38 ARG HB2 H 1.652 0.02 2 246 . 38 ARG HB3 H 1.551 0.02 2 247 . 38 ARG HG2 H 1.345 0.02 1 248 . 38 ARG HG3 H 1.345 0.02 1 249 . 38 ARG H H 8.475 0.02 1 250 . 38 ARG N N 124.879 0.05 1 251 . 39 HIS CA C 61.513 0.05 1 252 . 39 HIS CB C 29.530 0.05 1 253 . 39 HIS CD2 C 120.047 0.05 1 254 . 39 HIS CE1 C 138.167 0.05 1 255 . 39 HIS HA H 3.867 0.02 1 256 . 39 HIS HB2 H 3.317 0.02 2 257 . 39 HIS HB3 H 3.026 0.02 2 258 . 39 HIS HD2 H 7.058 0.02 1 259 . 39 HIS HE1 H 8.022 0.02 1 260 . 39 HIS ND1 N 212.502 0.05 1 261 . 39 HIS NE2 N 179.85 0.05 1 262 . 40 GLY CA C 46.674 0.05 1 263 . 40 GLY HA2 H 3.912 0.02 2 264 . 40 GLY HA3 H 3.766 0.02 2 265 . 40 GLY H H 8.480 0.02 1 266 . 40 GLY N N 109.371 0.05 1 267 . 41 GLY CA C 44.661 0.05 1 268 . 41 GLY HA2 H 3.933 0.02 2 269 . 41 GLY HA3 H 3.369 0.02 2 270 . 41 GLY H H 7.787 0.02 1 271 . 41 GLY N N 105.070 0.05 1 272 . 42 ILE CA C 57.196 0.05 1 273 . 42 ILE CB C 35.811 0.05 1 274 . 42 ILE CD1 C 9.347 0.05 1 275 . 42 ILE CG1 C 26.105 0.05 1 276 . 42 ILE CG2 C 16.560 0.05 1 277 . 42 ILE HA H 4.743 0.02 1 278 . 42 ILE HB H 2.089 0.02 1 279 . 42 ILE HD1 H 0.516 0.02 1 280 . 42 ILE HG12 H 1.728 0.02 2 281 . 42 ILE HG13 H 1.101 0.02 2 282 . 42 ILE HG2 H 0.566 0.02 1 283 . 42 ILE H H 8.374 0.02 1 284 . 42 ILE N N 119.727 0.05 1 285 . 43 TYR CA C 56.230 0.05 1 286 . 43 TYR CB C 42.586 0.05 1 287 . 43 TYR HA H 5.286 0.02 1 288 . 43 TYR HB2 H 2.666 0.02 2 289 . 43 TYR HB3 H 2.444 0.02 2 290 . 43 TYR HD1 H 6.944 0.02 1 291 . 43 TYR HD2 H 6.944 0.02 1 292 . 43 TYR HE1 H 6.944 0.02 1 293 . 43 TYR HE2 H 6.944 0.02 1 294 . 43 TYR H H 8.913 0.02 1 295 . 43 TYR N N 123.239 0.05 1 296 . 44 VAL CA C 63.799 0.05 1 297 . 44 VAL CB C 31.650 0.05 1 298 . 44 VAL CG1 C 21.896 0.05 1 299 . 44 VAL CG2 C 21.896 0.05 1 300 . 44 VAL HA H 3.914 0.02 1 301 . 44 VAL HB H 2.287 0.02 1 302 . 44 VAL HG1 H 0.702 0.02 1 303 . 44 VAL HG2 H 0.704 0.02 1 304 . 44 VAL H H 9.133 0.02 1 305 . 44 VAL N N 120.468 0.05 1 306 . 45 LYS CA C 56.703 0.05 1 307 . 45 LYS CB C 33.612 0.05 1 308 . 45 LYS CD C 29.298 0.05 1 309 . 45 LYS CE C 42.197 0.05 1 310 . 45 LYS CG C 24.869 0.05 1 311 . 45 LYS HA H 4.327 0.02 1 312 . 45 LYS HB2 H 1.783 0.02 2 313 . 45 LYS HB3 H 1.423 0.02 2 314 . 45 LYS HD2 H 1.681 0.02 2 315 . 45 LYS HD3 H 1.539 0.02 2 316 . 45 LYS HE2 H 2.929 0.02 1 317 . 45 LYS HE3 H 2.929 0.02 1 318 . 45 LYS HG2 H 1.335 0.02 1 319 . 45 LYS HG3 H 1.335 0.02 1 320 . 45 LYS H H 9.527 0.02 1 321 . 45 LYS N N 134.677 0.05 1 322 . 46 ALA CA C 51.542 0.05 1 323 . 46 ALA CB C 22.248 0.05 1 324 . 46 ALA HA H 4.491 0.02 1 325 . 46 ALA HB H 1.277 0.02 1 326 . 46 ALA H H 7.525 0.02 1 327 . 46 ALA N N 117.354 0.05 1 328 . 47 ILE CA C 58.081 0.05 1 329 . 47 ILE CB C 36.919 0.05 1 330 . 47 ILE CD1 C 11.644 0.05 1 331 . 47 ILE CG1 C 25.964 0.05 1 332 . 47 ILE CG2 C 17.850 0.05 1 333 . 47 ILE HA H 4.365 0.02 1 334 . 47 ILE HB H 2.006 0.02 1 335 . 47 ILE HD1 H 0.504 0.02 1 336 . 47 ILE HG12 H 1.411 0.02 2 337 . 47 ILE HG13 H 1.269 0.02 2 338 . 47 ILE HG2 H 0.786 0.02 1 339 . 47 ILE H H 8.573 0.02 1 340 . 47 ILE N N 120.573 0.05 1 341 . 48 ILE CA C 57.674 0.05 1 342 . 48 ILE CB C 37.323 0.05 1 343 . 48 ILE CD1 C 9.937 0.05 1 344 . 48 ILE CG1 C 27.258 0.05 1 345 . 48 ILE CG2 C 16.370 0.05 1 346 . 48 ILE HA H 4.221 0.02 1 347 . 48 ILE HB H 1.700 0.02 1 348 . 48 ILE HD1 H 0.648 0.02 1 349 . 48 ILE HG12 H 1.318 0.02 2 350 . 48 ILE HG13 H 1.148 0.02 2 351 . 48 ILE HG2 H 0.934 0.02 1 352 . 48 ILE H H 7.783 0.02 1 353 . 48 ILE N N 129.270 0.05 1 354 . 49 PRO CA C 64.334 0.05 1 355 . 49 PRO CB C 31.940 0.05 1 356 . 49 PRO CD C 51.852 0.05 1 357 . 49 PRO CG C 27.822 0.05 1 358 . 49 PRO HA H 4.494 0.02 1 359 . 49 PRO HB2 H 2.398 0.02 2 360 . 49 PRO HB3 H 1.844 0.02 2 361 . 49 PRO HD2 H 4.114 0.02 2 362 . 49 PRO HD3 H 3.611 0.02 2 363 . 49 PRO HG2 H 2.130 0.02 2 364 . 49 PRO HG3 H 2.007 0.02 2 365 . 50 LYS CA C 58.063 0.05 1 366 . 50 LYS CB C 29.391 0.05 1 367 . 50 LYS CE C 42.158 0.05 1 368 . 50 LYS CG C 25.494 0.05 1 369 . 50 LYS HA H 3.857 0.02 1 370 . 50 LYS HB2 H 2.148 0.02 2 371 . 50 LYS HB3 H 2.018 0.02 2 372 . 50 LYS HE2 H 2.998 0.02 1 373 . 50 LYS HE3 H 2.998 0.02 1 374 . 50 LYS HG2 H 1.372 0.02 1 375 . 50 LYS HG3 H 1.372 0.02 1 376 . 50 LYS H H 9.351 0.02 1 377 . 50 LYS N N 117.595 0.05 1 378 . 51 GLY CA C 44.856 0.05 1 379 . 51 GLY HA2 H 4.248 0.02 2 380 . 51 GLY HA3 H 3.869 0.02 2 381 . 51 GLY H H 7.763 0.02 1 382 . 51 GLY N N 106.276 0.05 1 383 . 52 ALA CA C 55.338 0.05 1 384 . 52 ALA CB C 18.480 0.05 1 385 . 52 ALA HA H 4.050 0.02 1 386 . 52 ALA HB H 1.637 0.02 1 387 . 52 ALA H H 8.883 0.02 1 388 . 52 ALA N N 121.705 0.05 1 389 . 53 ALA CA C 55.036 0.05 1 390 . 53 ALA CB C 18.593 0.05 1 391 . 53 ALA HA H 4.057 0.02 1 392 . 53 ALA HB H 1.277 0.02 1 393 . 53 ALA H H 8.017 0.02 1 394 . 53 ALA N N 119.459 0.05 1 395 . 54 GLU CA C 59.860 0.05 1 396 . 54 GLU CB C 29.725 0.05 1 397 . 54 GLU CG C 37.564 0.05 1 398 . 54 GLU HA H 3.789 0.02 1 399 . 54 GLU HB2 H 2.119 0.02 2 400 . 54 GLU HB3 H 2.006 0.02 2 401 . 54 GLU HG2 H 2.127 0.02 1 402 . 54 GLU HG3 H 2.127 0.02 1 403 . 54 GLU H H 9.318 0.02 1 404 . 54 GLU N N 124.402 0.05 1 405 . 55 SER CA C 61.200 0.05 1 406 . 55 SER CB C 62.945 0.05 1 407 . 55 SER HA H 4.128 0.02 1 408 . 55 SER HB2 H 3.967 0.02 2 409 . 55 SER HB3 H 3.924 0.02 2 410 . 55 SER H H 7.973 0.02 1 411 . 55 SER N N 113.419 0.05 1 412 . 56 ASP CA C 57.480 0.05 1 413 . 56 ASP CB C 44.427 0.05 1 414 . 56 ASP HA H 4.418 0.02 1 415 . 56 ASP HB2 H 2.680 0.02 2 416 . 56 ASP HB3 H 2.593 0.02 2 417 . 56 ASP H H 7.662 0.02 1 418 . 56 ASP N N 120.122 0.05 1 419 . 57 GLY CA C 46.409 0.05 1 420 . 57 GLY HA2 H 4.103 0.02 2 421 . 57 GLY HA3 H 3.882 0.02 2 422 . 57 GLY H H 7.409 0.02 1 423 . 57 GLY N N 102.818 0.05 1 424 . 58 ARG CA C 57.871 0.05 1 425 . 58 ARG CB C 33.019 0.05 1 426 . 58 ARG CD C 43.752 0.05 1 427 . 58 ARG CG C 27.542 0.05 1 428 . 58 ARG HA H 4.249 0.02 1 429 . 58 ARG HB2 H 2.028 0.02 2 430 . 58 ARG HB3 H 1.715 0.02 2 431 . 58 ARG HD2 H 3.166 0.02 2 432 . 58 ARG HD3 H 3.193 0.02 2 433 . 58 ARG HE H 8.718 0.02 1 434 . 58 ARG HG2 H 1.610 0.02 1 435 . 58 ARG HG3 H 1.610 0.02 1 436 . 58 ARG H H 7.983 0.02 1 437 . 58 ARG N N 117.582 0.05 1 438 . 58 ARG NE N 116.772 0.05 1 439 . 59 ILE CA C 61.559 0.05 1 440 . 59 ILE CB C 39.431 0.05 1 441 . 59 ILE CD1 C 14.670 0.05 1 442 . 59 ILE CG1 C 28.384 0.05 1 443 . 59 ILE CG2 C 18.400 0.05 1 444 . 59 ILE HA H 4.213 0.02 1 445 . 59 ILE HB H 1.429 0.02 1 446 . 59 ILE HD1 H 0.746 0.02 1 447 . 59 ILE HG12 H 1.792 0.02 2 448 . 59 ILE HG13 H 0.878 0.02 2 449 . 59 ILE HG2 H 0.853 0.02 1 450 . 59 ILE H H 8.340 0.02 1 451 . 59 ILE N N 119.915 0.05 1 452 . 60 HIS CA C 54.761 0.05 1 453 . 60 HIS CB C 33.429 0.05 1 454 . 60 HIS CD2 C 119.489 0.05 1 455 . 60 HIS CE1 C 136.263 0.05 1 456 . 60 HIS HA H 4.761 0.02 1 457 . 60 HIS HB2 H 3.278 0.02 2 458 . 60 HIS HB3 H 2.947 0.02 2 459 . 60 HIS HD2 H 7.226 0.02 1 460 . 60 HIS HE1 H 8.148 0.02 1 461 . 60 HIS H H 9.146 0.02 1 462 . 60 HIS N N 124.058 0.05 1 463 . 60 HIS ND1 N 197.326 0.05 1 464 . 60 HIS NE2 N 174.301 0.05 1 465 . 61 LYS CA C 58.257 0.05 1 466 . 61 LYS CB C 32.416 0.05 1 467 . 61 LYS CD C 29.840 0.05 1 468 . 61 LYS CE C 41.991 0.05 1 469 . 61 LYS CG C 24.511 0.05 1 470 . 61 LYS HA H 3.643 0.02 1 471 . 61 LYS HB2 H 1.731 0.02 2 472 . 61 LYS HB3 H 1.670 0.02 2 473 . 61 LYS HD2 H 1.764 0.02 1 474 . 61 LYS HD3 H 1.764 0.02 1 475 . 61 LYS HE2 H 3.055 0.02 1 476 . 61 LYS HE3 H 3.055 0.02 1 477 . 61 LYS HG2 H 1.493 0.02 2 478 . 61 LYS HG3 H 1.310 0.02 2 479 . 61 LYS H H 8.630 0.02 1 480 . 61 LYS N N 120.696 0.05 1 481 . 62 GLY CA C 44.913 0.05 1 482 . 62 GLY HA2 H 4.594 0.02 2 483 . 62 GLY HA3 H 3.638 0.02 2 484 . 62 GLY H H 9.179 0.02 1 485 . 62 GLY N N 114.421 0.05 1 486 . 63 ASP CA C 55.810 0.05 1 487 . 63 ASP CB C 40.966 0.05 1 488 . 63 ASP HA H 4.921 0.02 1 489 . 63 ASP HB2 H 2.730 0.02 2 490 . 63 ASP HB3 H 2.627 0.02 2 491 . 63 ASP H H 7.983 0.02 1 492 . 63 ASP N N 121.667 0.05 1 493 . 64 ARG CA C 53.612 0.05 1 494 . 64 ARG CB C 33.979 0.05 1 495 . 64 ARG CD C 44.273 0.05 1 496 . 64 ARG CG C 27.375 0.05 1 497 . 64 ARG HA H 4.701 0.02 1 498 . 64 ARG HB2 H 1.660 0.02 1 499 . 64 ARG HB3 H 1.660 0.02 1 500 . 64 ARG HD2 H 3.019 0.02 2 501 . 64 ARG HD3 H 2.845 0.02 2 502 . 64 ARG HE H 7.447 0.02 1 503 . 64 ARG HG2 H 0.875 0.02 2 504 . 64 ARG HG3 H 0.665 0.02 2 505 . 64 ARG H H 8.952 0.02 1 506 . 64 ARG N N 122.742 0.05 1 507 . 65 VAL CA C 62.324 0.05 1 508 . 65 VAL CB C 31.022 0.05 1 509 . 65 VAL CG1 C 22.685 0.05 1 510 . 65 VAL CG2 C 19.954 0.05 1 511 . 65 VAL HA H 3.883 0.02 1 512 . 65 VAL HB H 1.745 0.02 1 513 . 65 VAL HG1 H 0.603 0.02 1 514 . 65 VAL HG2 H 0.542 0.02 1 515 . 65 VAL H H 8.906 0.02 1 516 . 65 VAL N N 126.212 0.05 1 517 . 66 LEU CA C 56.106 0.05 1 518 . 66 LEU CB C 42.781 0.05 1 519 . 66 LEU CD1 C 25.822 0.05 1 520 . 66 LEU CD2 C 21.904 0.05 1 521 . 66 LEU HA H 4.368 0.02 1 522 . 66 LEU HB2 H 1.409 0.02 1 523 . 66 LEU HB3 H 1.409 0.02 1 524 . 66 LEU HD1 H 0.721 0.02 1 525 . 66 LEU HD2 H 0.647 0.02 2 526 . 66 LEU H H 9.182 0.02 1 527 . 66 LEU N N 127.046 0.05 1 528 . 67 ALA CA C 52.204 0.05 1 529 . 67 ALA CB C 22.225 0.05 1 530 . 67 ALA HA H 4.993 0.02 1 531 . 67 ALA HB H 1.107 0.02 1 532 . 67 ALA H H 7.800 0.02 1 533 . 67 ALA N N 118.994 0.05 1 534 . 68 VAL CA C 60.484 0.05 1 535 . 68 VAL CB C 34.116 0.05 1 536 . 68 VAL CG1 C 20.935 0.05 1 537 . 68 VAL CG2 C 20.741 0.05 1 538 . 68 VAL HA H 4.508 0.02 1 539 . 68 VAL HB H 1.749 0.02 1 540 . 68 VAL HG1 H 0.658 0.02 1 541 . 68 VAL HG2 H 0.710 0.02 1 542 . 68 VAL H H 8.342 0.02 1 543 . 68 VAL N N 119.867 0.05 1 544 . 69 ASN CA C 54.178 0.05 1 545 . 69 ASN CB C 36.966 0.05 1 546 . 69 ASN HA H 4.543 0.02 1 547 . 69 ASN HB2 H 3.172 0.02 2 548 . 69 ASN HB3 H 3.037 0.02 2 549 . 69 ASN HD21 H 7.861 0.02 2 550 . 69 ASN HD22 H 7.334 0.02 2 551 . 69 ASN H H 10.357 0.02 1 552 . 69 ASN N N 128.795 0.05 1 553 . 69 ASN ND2 N 113.073 0.05 1 554 . 70 GLY CA C 45.244 0.05 1 555 . 70 GLY HA2 H 4.078 0.02 2 556 . 70 GLY HA3 H 3.509 0.02 2 557 . 70 GLY H H 9.042 0.02 1 558 . 70 GLY N N 103.301 0.05 1 559 . 71 VAL CA C 62.130 0.05 1 560 . 71 VAL CB C 31.850 0.05 1 561 . 71 VAL CG1 C 21.120 0.05 1 562 . 71 VAL CG2 C 20.772 0.05 1 563 . 71 VAL HA H 3.977 0.02 1 564 . 71 VAL HB H 2.209 0.02 1 565 . 71 VAL HG1 H 0.924 0.02 1 566 . 71 VAL HG2 H 0.897 0.02 1 567 . 71 VAL H H 8.046 0.02 1 568 . 71 VAL N N 123.736 0.05 1 569 . 72 SER CA C 58.257 0.05 1 570 . 72 SER CB C 63.837 0.05 1 571 . 72 SER HA H 4.357 0.02 1 572 . 72 SER HB2 H 4.054 0.02 2 573 . 72 SER HB3 H 3.831 0.02 2 574 . 72 SER H H 8.665 0.02 1 575 . 72 SER N N 121.074 0.05 1 576 . 73 LEU CA C 54.048 0.05 1 577 . 73 LEU CB C 41.044 0.05 1 578 . 73 LEU CD1 C 25.673 0.05 1 579 . 73 LEU CD2 C 22.614 0.05 1 580 . 73 LEU CG C 27.025 0.05 1 581 . 73 LEU HA H 4.451 0.02 1 582 . 73 LEU HB2 H 1.678 0.02 2 583 . 73 LEU HB3 H 1.460 0.02 2 584 . 73 LEU HD1 H 0.647 0.02 1 585 . 73 LEU HD2 H 0.710 0.02 2 586 . 73 LEU HG H 1.444 0.02 1 587 . 73 LEU H H 8.250 0.02 1 588 . 73 LEU N N 125.095 0.05 1 589 . 74 GLU CA C 58.646 0.05 1 590 . 74 GLU CB C 35.855 0.05 1 591 . 74 GLU CG C 29.085 0.05 1 592 . 74 GLU HA H 4.040 0.02 1 593 . 74 GLU HB2 H 2.187 0.02 1 594 . 74 GLU HB3 H 2.187 0.02 1 595 . 74 GLU HG2 H 1.937 0.02 2 596 . 74 GLU HG3 H 1.894 0.02 2 597 . 74 GLU H H 8.289 0.02 1 598 . 74 GLU N N 123.394 0.05 1 599 . 75 GLY CA C 45.511 0.05 1 600 . 75 GLY HA2 H 4.146 0.02 2 601 . 75 GLY HA3 H 3.674 0.02 2 602 . 75 GLY H H 8.989 0.02 1 603 . 75 GLY N N 115.458 0.05 1 604 . 76 ALA CA C 52.582 0.05 1 605 . 76 ALA CB C 19.546 0.05 1 606 . 76 ALA HA H 4.493 0.02 1 607 . 76 ALA HB H 1.403 0.02 1 608 . 76 ALA H H 7.849 0.02 1 609 . 76 ALA N N 122.246 0.05 1 610 . 77 THR CA C 60.976 0.05 1 611 . 77 THR CG2 C 22.064 0.05 1 612 . 77 THR HA H 4.470 0.02 1 613 . 77 THR HG2 H 1.314 0.02 1 614 . 77 THR H H 8.260 0.02 1 615 . 77 THR N N 111.811 0.05 1 616 . 78 HIS CA C 61.938 0.05 1 617 . 78 HIS CB C 30.250 0.05 1 618 . 78 HIS CD2 C 119.174 0.05 1 619 . 78 HIS CE1 C 136.993 0.05 1 620 . 78 HIS HA H 3.998 0.02 1 621 . 78 HIS HB2 H 3.624 0.02 2 622 . 78 HIS HB3 H 3.169 0.02 2 623 . 78 HIS HD2 H 6.852 0.02 1 624 . 78 HIS HE1 H 7.738 0.02 1 625 . 78 HIS H H 9.126 0.02 1 626 . 78 HIS N N 121.616 0.05 1 627 . 78 HIS ND1 N 166.077 0.05 1 628 . 78 HIS NE2 N 183.987 0.05 1 629 . 79 LYS CA C 59.688 0.05 1 630 . 79 LYS CB C 33.024 0.05 1 631 . 79 LYS CD C 28.929 0.05 1 632 . 79 LYS CE C 41.942 0.05 1 633 . 79 LYS CG C 24.854 0.05 1 634 . 79 LYS HA H 3.864 0.02 1 635 . 79 LYS HB2 H 1.953 0.02 2 636 . 79 LYS HB3 H 1.703 0.02 2 637 . 79 LYS HD2 H 1.700 0.02 1 638 . 79 LYS HD3 H 1.700 0.02 1 639 . 79 LYS HE2 H 2.996 0.02 1 640 . 79 LYS HE3 H 2.996 0.02 1 641 . 79 LYS HG2 H 1.487 0.02 2 642 . 79 LYS HG3 H 1.364 0.02 2 643 . 79 LYS H H 8.565 0.02 1 644 . 79 LYS N N 116.688 0.05 1 645 . 80 GLN CA C 58.282 0.05 1 646 . 80 GLN CB C 28.739 0.05 1 647 . 80 GLN CG C 34.043 0.05 1 648 . 80 GLN HA H 4.026 0.02 1 649 . 80 GLN HB2 H 2.242 0.02 2 650 . 80 GLN HB3 H 1.989 0.02 2 651 . 80 GLN HE21 H 7.468 0.02 2 652 . 80 GLN HE22 H 6.797 0.02 2 653 . 80 GLN HG2 H 2.382 0.02 1 654 . 80 GLN HG3 H 2.382 0.02 1 655 . 80 GLN H H 7.624 0.02 1 656 . 80 GLN N N 117.424 0.05 1 657 . 80 GLN NE2 N 111.146 0.05 1 658 . 81 ALA CA C 55.441 0.05 1 659 . 81 ALA CB C 19.157 0.05 1 660 . 81 ALA HA H 3.838 0.02 1 661 . 81 ALA HB H 1.349 0.02 1 662 . 81 ALA H H 8.553 0.02 1 663 . 81 ALA N N 123.442 0.05 1 664 . 82 VAL CA C 67.360 0.05 1 665 . 82 VAL CB C 31.438 0.05 1 666 . 82 VAL CG1 C 22.631 0.05 1 667 . 82 VAL CG2 C 21.001 0.05 1 668 . 82 VAL HA H 3.287 0.02 1 669 . 82 VAL HB H 1.929 0.02 1 670 . 82 VAL HG1 H 0.540 0.02 1 671 . 82 VAL HG2 H 0.737 0.02 1 672 . 82 VAL H H 8.253 0.02 1 673 . 82 VAL N N 117.556 0.05 1 674 . 83 GLU CA C 59.617 0.05 1 675 . 83 GLU CB C 29.123 0.05 1 676 . 83 GLU CG C 36.504 0.05 1 677 . 83 GLU HA H 3.928 0.02 1 678 . 83 GLU HB2 H 2.087 0.02 2 679 . 83 GLU HB3 H 2.007 0.02 2 680 . 83 GLU HG2 H 2.387 0.02 2 681 . 83 GLU HG3 H 2.260 0.02 2 682 . 83 GLU H H 8.130 0.02 1 683 . 83 GLU N N 119.560 0.05 1 684 . 84 THR CA C 67.000 0.05 1 685 . 84 THR CB C 68.340 0.05 1 686 . 84 THR CG2 C 21.174 0.05 1 687 . 84 THR HA H 3.889 0.02 1 688 . 84 THR HB H 4.221 0.02 1 689 . 84 THR HG2 H 1.060 0.02 1 690 . 84 THR H H 8.156 0.02 1 691 . 84 THR N N 116.754 0.05 1 692 . 85 LEU CA C 58.451 0.05 1 693 . 85 LEU CB C 42.273 0.05 1 694 . 85 LEU CD1 C 25.568 0.05 1 695 . 85 LEU CD2 C 24.698 0.05 1 696 . 85 LEU CG C 28.159 0.05 1 697 . 85 LEU HA H 3.822 0.02 1 698 . 85 LEU HB2 H 1.995 0.02 2 699 . 85 LEU HB3 H 1.272 0.02 2 700 . 85 LEU HD1 H 0.698 0.02 1 701 . 85 LEU HD2 H 0.677 0.02 2 702 . 85 LEU HG H 1.550 0.02 1 703 . 85 LEU H H 7.984 0.02 1 704 . 85 LEU N N 119.993 0.05 1 705 . 86 ARG CA C 58.840 0.05 1 706 . 86 ARG CB C 30.804 0.05 1 707 . 86 ARG CD C 43.725 0.05 1 708 . 86 ARG CG C 28.135 0.05 1 709 . 86 ARG HA H 4.256 0.02 1 710 . 86 ARG HB2 H 1.893 0.02 1 711 . 86 ARG HB3 H 1.893 0.02 1 712 . 86 ARG HD2 H 3.159 0.02 1 713 . 86 ARG HD3 H 3.159 0.02 1 714 . 86 ARG HE H 7.024 0.02 1 715 . 86 ARG HG2 H 1.891 0.02 2 716 . 86 ARG HG3 H 1.683 0.02 2 717 . 86 ARG H H 8.400 0.02 1 718 . 86 ARG N N 119.804 0.05 1 719 . 86 ARG NE N 123.939 0.05 1 720 . 87 ASN CA C 52.807 0.05 1 721 . 87 ASN CB C 37.078 0.05 1 722 . 87 ASN HA H 4.966 0.02 1 723 . 87 ASN HB2 H 2.977 0.02 2 724 . 87 ASN HB3 H 2.771 0.02 2 725 . 87 ASN HD21 H 7.624 0.02 2 726 . 87 ASN HD22 H 6.885 0.02 2 727 . 87 ASN H H 7.872 0.02 1 728 . 87 ASN N N 120.280 0.05 1 729 . 87 ASN ND2 N 112.350 0.05 1 730 . 88 THR CA C 59.811 0.05 1 731 . 88 THR CB C 72.629 0.05 1 732 . 88 THR CG2 C 22.549 0.05 1 733 . 88 THR HA H 4.432 0.02 1 734 . 88 THR HB H 4.289 0.02 1 735 . 88 THR HG2 H 1.246 0.02 1 736 . 88 THR H H 7.597 0.02 1 737 . 88 THR N N 109.844 0.05 1 738 . 89 GLY CA C 44.145 0.05 1 739 . 89 GLY HA2 H 4.374 0.02 2 740 . 89 GLY HA3 H 3.753 0.02 2 741 . 89 GLY H H 8.424 0.02 1 742 . 89 GLY N N 109.552 0.05 1 743 . 90 GLN CA C 58.456 0.05 1 744 . 90 GLN CB C 29.034 0.05 1 745 . 90 GLN CG C 33.922 0.05 1 746 . 90 GLN HA H 3.980 0.02 1 747 . 90 GLN HE21 H 7.422 0.02 2 748 . 90 GLN HE22 H 6.912 0.02 2 749 . 90 GLN HB2 H 2.075 0.02 1 750 . 90 GLN HB3 H 2.075 0.02 1 751 . 90 GLN HG2 H 2.448 0.02 1 752 . 90 GLN HG3 H 2.448 0.02 1 753 . 90 GLN H H 8.161 0.02 1 754 . 90 GLN N N 117.464 0.05 1 755 . 90 GLN NE2 N 112.109 0.05 1 756 . 91 VAL CA C 61.365 0.05 1 757 . 91 VAL CB C 33.221 0.05 1 758 . 91 VAL CG1 C 21.233 0.05 1 759 . 91 VAL CG2 C 21.370 0.05 1 760 . 91 VAL HA H 4.652 0.02 1 761 . 91 VAL HB H 1.830 0.02 1 762 . 91 VAL HG1 H 0.862 0.02 1 763 . 91 VAL HG2 H 0.688 0.02 1 764 . 91 VAL H H 7.712 0.02 1 765 . 91 VAL N N 115.959 0.05 1 766 . 92 VAL CA C 60.976 0.05 1 767 . 92 VAL CB C 35.102 0.05 1 768 . 92 VAL CG1 C 22.751 0.05 1 769 . 92 VAL CG2 C 22.478 0.05 1 770 . 92 VAL HA H 4.461 0.02 1 771 . 92 VAL HB H 1.859 0.02 1 772 . 92 VAL HG1 H 0.920 0.02 1 773 . 92 VAL HG2 H 0.858 0.02 1 774 . 92 VAL H H 9.022 0.02 1 775 . 92 VAL N N 128.360 0.05 1 776 . 93 HIS CA C 55.753 0.05 1 777 . 93 HIS CB C 31.193 0.05 1 778 . 93 HIS HA H 5.031 0.02 1 779 . 93 HIS HB2 H 3.150 0.02 1 780 . 93 HIS HB3 H 3.150 0.02 1 781 . 93 HIS HD2 H 7.024 0.02 2 782 . 93 HIS H H 8.759 0.02 1 783 . 93 HIS N N 126.136 0.05 1 784 . 93 HIS ND1 N 215.820 0.05 1 785 . 93 HIS CE1 C 137.379 0.05 1 786 . 93 HIS HE1 H 7.888 0.02 1 787 . 93 HIS NE2 N 173.660 0.02 1 788 . 93 HIS CD2 C 118.478 0.02 1 789 . 94 LEU CA C 53.584 0.05 1 790 . 94 LEU CB C 45.454 0.05 1 791 . 94 LEU CD1 C 25.130 0.05 1 792 . 94 LEU CD2 C 25.130 0.05 1 793 . 94 LEU CG C 25.987 0.05 1 794 . 94 LEU HA H 5.002 0.02 1 795 . 94 LEU HB2 H 1.626 0.02 2 796 . 94 LEU HB3 H 1.044 0.02 2 797 . 94 LEU HD1 H 0.716 0.02 1 798 . 94 LEU HD2 H 0.716 0.02 1 799 . 94 LEU HG H 0.647 0.02 1 800 . 94 LEU H H 9.014 0.02 1 801 . 94 LEU N N 126.717 0.05 1 802 . 95 LEU CA C 53.885 0.05 1 803 . 95 LEU CB C 44.805 0.05 1 804 . 95 LEU CD1 C 25.553 0.05 1 805 . 95 LEU CD2 C 23.308 0.05 1 806 . 95 LEU CG C 27.693 0.05 1 807 . 95 LEU HA H 4.782 0.02 1 808 . 95 LEU HB2 H 1.742 0.02 2 809 . 95 LEU HB3 H 1.298 0.02 2 810 . 95 LEU HD1 H 0.800 0.02 1 811 . 95 LEU HD2 H 0.847 0.02 2 812 . 95 LEU HG H 1.319 0.02 1 813 . 95 LEU H H 7.983 0.02 1 814 . 95 LEU N N 123.978 0.05 1 815 . 96 LEU CA C 53.984 0.05 1 816 . 96 LEU CB C 45.793 0.05 1 817 . 96 LEU CD1 C 27.199 0.05 1 818 . 96 LEU CD2 C 27.399 0.05 1 819 . 96 LEU CG C 28.152 0.05 1 820 . 96 LEU HA H 5.287 0.02 1 821 . 96 LEU HB2 H 1.022 0.02 2 822 . 96 LEU HB3 H 0.190 0.02 2 823 . 96 LEU HD1 H 0.645 0.02 1 824 . 96 LEU HD2 H 0.442 0.02 2 825 . 96 LEU HG H 1.198 0.02 1 826 . 96 LEU H H 8.898 0.02 1 827 . 96 LEU N N 127.568 0.05 1 828 . 97 GLU CA C 54.067 0.05 1 829 . 97 GLU CB C 34.173 0.05 1 830 . 97 GLU HA H 4.968 0.02 1 831 . 97 GLU HB2 H 2.003 0.02 2 832 . 97 GLU HB3 H 1.836 0.02 2 833 . 97 GLU H H 8.927 0.02 1 834 . 97 GLU N N 119.076 0.05 1 835 . 98 LYS CA C 55.882 0.05 1 836 . 98 LYS CB C 32.037 0.05 1 837 . 98 LYS CD C 28.735 0.05 1 838 . 98 LYS CE C 41.791 0.05 1 839 . 98 LYS CG C 23.528 0.05 1 840 . 98 LYS HA H 4.430 0.02 1 841 . 98 LYS HB2 H 2.152 0.02 2 842 . 98 LYS HB3 H 1.613 0.02 2 843 . 98 LYS HD2 H 1.883 0.02 2 844 . 98 LYS HD3 H 1.435 0.02 2 845 . 98 LYS HE2 H 2.735 0.02 1 846 . 98 LYS HE3 H 2.735 0.02 1 847 . 98 LYS HG2 H 1.629 0.02 2 848 . 98 LYS HG3 H 1.257 0.02 2 849 . 98 LYS H H 9.136 0.02 1 850 . 98 LYS N N 128.386 0.05 1 851 . 99 GLY CA C 45.478 0.05 1 852 . 99 GLY HA2 H 4.316 0.02 2 853 . 99 GLY HA3 H 3.852 0.02 2 854 . 99 GLY H H 9.596 0.02 1 855 . 99 GLY N N 117.346 0.05 1 856 . 100 GLN CA C 55.538 0.05 1 857 . 100 GLN CB C 30.056 0.05 1 858 . 100 GLN CG C 33.827 0.05 1 859 . 100 GLN HA H 4.311 0.02 1 860 . 100 GLN HB2 H 2.095 0.02 2 861 . 100 GLN HB3 H 1.900 0.02 2 862 . 100 GLN HE21 H 7.640 0.02 2 863 . 100 GLN HE22 H 6.835 0.02 2 864 . 100 GLN HG2 H 2.360 0.02 1 865 . 100 GLN HG3 H 2.360 0.02 1 866 . 100 GLN H H 8.169 0.02 1 867 . 100 GLN N N 122.697 0.05 1 868 . 100 GLN NE2 N 112.591 0.05 1 869 . 101 VAL H H 8.162 0.02 1 870 . 101 VAL N N 117.473 0.05 1 871 . 102 PRO CA C 62.918 0.05 1 872 . 102 PRO CB C 32.199 0.05 1 873 . 102 PRO CD C 49.711 0.05 1 874 . 102 PRO CG C 32.231 0.05 1 875 . 102 PRO HA H 4.401 0.02 1 876 . 102 PRO HB2 H 2.071 0.02 1 877 . 102 PRO HB3 H 2.071 0.02 1 878 . 102 PRO HD2 H 3.520 0.02 2 879 . 102 PRO HD3 H 3.386 0.02 2 880 . 102 PRO HG2 H 1.487 0.02 1 881 . 102 PRO HG3 H 1.487 0.02 1 stop_ save_ save_T1_values _Saveframe_category T1_relaxation _Details . loop_ _Sample_label $sample_1 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 11 GLY N 1.63599 0.0817996 2 12 ASP N 1.66667 0.0833333 3 14 PHE N 1.54979 0.0774893 4 17 GLU N 1.46039 0.0730194 5 18 LEU N 1.52683 0.0763417 6 19 ALA N 1.49813 0.0749064 7 20 LYS N 1.54464 0.077232 8 21 THR N 1.49421 0.0747105 9 22 ASP N 1.47743 0.0738716 10 23 GLY N 1.53421 0.0767106 11 24 SER N 1.55703 0.0778513 12 26 GLY N 1.53022 0.0765111 13 27 ILE N 1.63119 0.0815594 14 28 SER N 1.55533 0.0777665 15 29 VAL N 1.58065 0.0790326 16 30 THR N 1.54 0.0770001 17 31 GLY N 1.53681 0.0768403 18 32 GLY N 1.53799 0.0768994 19 33 VAL N 1.60668 0.0803342 20 34 ASN N 1.66583 0.0832917 21 35 THR N 1.58178 0.0790889 22 36 SER N 1.44791 0.0723956 23 37 VAL N 1.61956 0.0809782 24 38 ARG N 1.64487 0.0822436 25 40 GLY N 1.72801 0.0864006 26 41 GLY N 1.68762 0.0843811 27 43 TYR N 1.48865 0.0744325 28 44 VAL N 1.5024 0.0751202 29 45 LYS N 1.67687 0.0838434 30 46 ALA N 1.54083 0.0770416 31 47 ILE N 1.51538 0.0757691 32 48 ILE N 1.66085 0.0830427 33 50 LYS N 1.50161 0.0750807 34 51 GLY N 1.61564 0.080782 35 52 ALA N 1.54119 0.0770594 36 53 ALA N 1.5273 0.076365 37 54 GLU N 1.58529 0.0792644 38 55 SER N 1.52975 0.0764877 39 56 ASP N 1.55606 0.0778028 40 57 GLY N 1.53775 0.0768876 41 58 ARG N 1.58642 0.079321 42 60 HIS N 1.63706 0.0818532 43 61 LYS N 1.57332 0.0786658 44 62 GLY N 1.57134 0.0785669 45 63 ASP N 1.66806 0.0834028 46 64 ARG N 1.5528 0.0776398 47 65 VAL N 1.51976 0.0759878 48 66 LEU N 1.54763 0.0773814 49 67 ALA N 1.57159 0.0785793 50 69 ASN N 1.61799 0.0808996 51 70 GLY N 1.65385 0.0826925 52 71 VAL N 1.56961 0.0784806 53 72 SER N 1.57072 0.0785361 54 73 LEU N 1.523 0.0761499 55 74 GLU N 1.5348 0.0767401 56 75 GLY N 1.56605 0.0783024 57 76 ALA N 1.53268 0.0766342 58 77 THR N 1.60979 0.0804894 59 78 HIS N 1.61538 0.0807689 60 79 LYS N 1.55087 0.0775434 61 80 GLN N 1.58881 0.0794407 62 81 ALA N 1.59872 0.0799361 63 82 VAL N 1.54895 0.0774473 64 83 GLU N 1.61773 0.0808865 65 84 THR N 1.53929 0.0769645 66 85 LEU N 1.54955 0.0774773 67 86 ARG N 1.54048 0.0770238 68 87 ASN N 1.49802 0.0749008 69 88 THR N 1.21573 0.0607866 70 89 GLY N 1.54214 0.0771069 71 90 GLN N 1.558 0.0778998 72 91 VAL N 1.55075 0.0775374 73 92 VAL N 1.5921 0.0796052 74 93 HIS N 1.57754 0.0788768 75 94 LEU N 1.51458 0.0757289 76 95 LEU N 1.49779 0.0748895 77 96 LEU N 1.53421 0.0767106 78 97 GLU N 1.48082 0.0740412 79 98 LYS N 1.59502 0.0797512 80 99 GLY N 1.60436 0.0802182 81 100 GLN N 1.44415 0.0722074 82 101 VAL N 1.558 0.0778998 stop_ save_ save_T2_Values _Saveframe_category T2_relaxation _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Spectrometer_frequency_1H 600 _T2_coherence_type . _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 11 GLY N 10.7735 0.538674 . . 2 12 ASP N 9.29999 0.464999 . . 3 14 PHE N 11.3514 0.567568 . . 4 17 GLU N 9.32636 0.466318 . . 5 18 LEU N 9.85659 0.492829 . . 6 19 ALA N 9.24283 0.462141 . . 7 20 LYS N 8.8308 0.44154 . . 8 21 THR N 8.88968 0.444484 . . 9 22 ASP N 10.657 0.532849 . . 10 23 GLY N 10.7411 0.537056 . . 11 24 SER N 10.382 0.519101 . . 12 26 GLY N 13.2088 0.66044 . . 13 27 ILE N 12.729 0.63645 . . 14 28 SER N 11.5357 0.576786 . . 15 29 VAL N 10.8228 0.541141 . . 16 31 GLY N 10.12 0.506002 . . 17 32 GLY N 14.0246 0.701229 . . 18 33 VAL N 10.5432 0.527158 . . 19 34 ASN N 21.9374 1.09687 . . 20 35 THR N 15.3405 0.767025 . . 21 36 SER N 9.9555 0.497775 . . 22 37 VAL N 14.668 0.733398 . . 23 38 ARG N 14.8067 0.740337 . . 24 39 HIS N 11.5062 0.575309 . . 25 40 GLY N 9.88963 0.494482 . . 26 41 GLY N 21.1743 1.05872 . . 27 43 TYR N 10.6737 0.533685 . . 28 44 VAL N 10.2407 0.512033 . . 29 45 LYS N 11.0633 0.553165 . . 30 46 ALA N 8.71126 0.435563 . . 31 47 ILE N 9.09902 0.454951 . . 32 48 ILE N 10.2909 0.514547 . . 33 50 LYS N 9.29549 0.464775 . . 34 51 GLY N 10.0173 0.500865 . . 35 52 ALA N 11.1352 0.556761 . . 36 53 ALA N 10.0324 0.501621 . . 37 54 GLU N 10.5389 0.526945 . . 38 55 SER N 10.1852 0.509261 . . 39 56 ASP N 10.5717 0.528585 . . 40 57 GLY N 10.8236 0.541181 . . 41 58 ARG N 9.01502 0.450751 . . 42 60 HIS N 9.57845 0.478923 . . 43 61 LYS N 8.8563 0.442815 . . 44 62 GLY N 10.1032 0.50516 . . 45 63 ASP N 10.2496 0.51248 . . 46 64 ARG N 11.2211 0.561055 . . 47 65 VAL N 10.863 0.543151 . . 48 66 LEU N 10.8976 0.54488 . . 49 67 ALA N 9.64385 0.482193 . . 50 69 ASN N 10.2416 0.51208 . . 51 70 GLY N 10.498 0.524899 . . 52 71 VAL N 9.68129 0.484065 . . 53 72 SER N 9.79537 0.489769 . . 54 73 LEU N 10.2884 0.514422 . . 55 74 GLU N 10.5258 0.526289 . . 56 75 GLY N 10.4433 0.522165 . . 57 76 ALA N 10.7612 0.53806 . . 58 77 THR N 9.93049 0.496524 . . 59 78 HIS N 10.7171 0.535855 . . 60 79 LYS N 10.2161 0.510806 . . 61 80 GLN N 10.1998 0.509989 . . 62 81 ALA N 11.0385 0.551927 . . 63 82 VAL N 10.4131 0.520654 . . 64 83 GLU N 12.4411 0.622056 . . 65 84 THR N 10.2213 0.511067 . . 66 85 LEU N 10.2585 0.512926 . . 67 86 ARG N 13.1738 0.658688 . . 68 87 ASN N 9.56974 0.478487 . . 69 88 THR N 6.97175 0.348588 . . 70 89 GLY N 9.27412 0.463706 . . 71 90 GLN N 9.3335 0.466675 . . 72 91 VAL N 8.87871 0.443935 . . 73 92 VAL N 9.79595 0.489798 . . 74 93 HIS N 10.0807 0.504036 . . 75 94 LEU N 10.3223 0.516117 . . 76 95 LEU N 10.4491 0.522453 . . 77 96 LEU N 11.2697 0.563487 . . 78 97 GLU N 10.1977 0.509884 . . 79 98 LYS N 11.1981 0.559904 . . 80 99 GLY N 12.1215 0.606074 . . 81 100 GLN N 8.5042 0.42521 . . 82 101 VAL N 3.79377 0.189689 . . stop_ save_ save_heteronuclear_NOE _Saveframe_category heteronuclear_NOE _Details . loop_ _Sample_label $sample_1 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 11 GLY 0.84140 0.04207 12 ASP 0.72620 0.03631 14 PHE 0.76110 0.038055 17 GLU 0.69860 0.03493 18 LEU 0.849050 0.0424525 19 ALA 0.703450 0.0351725 21 THR 0.680650 0.0340325 22 ASP 0.80340 0.04017 23 GLY 0.74570 0.037285 24 SER 0.74380 0.03719 26 GLY 0.705250 0.0352625 27 ILE 0.802050 0.0401025 28 SER 0.7720 0.0386 29 VAL 0.72910 0.036455 30 THR 0.7930 0.03965 31 GLY 0.72190 0.036095 32 GLY 0.75960 0.03798 33 VAL 0.724250 0.0362125 34 ASN 0.788350 0.0394175 35 THR 0.742550 0.0371275 36 SER 0.836750 0.0418375 37 VAL 0.682450 0.0341225 38 ARG 0.689650 0.0344825 39 HIS 0.81040 0.04052 40 GLY 0.72940 0.03647 41 GLY 0.741450 0.0370725 43 TYR 0.751750 0.0375875 44 VAL 0.79790 0.039895 45 LYS 0.781150 0.0390575 46 ALA 0.74370 0.037185 47 ILE 0.708650 0.0354325 48 ILE 0.81680 0.04084 50 LYS 0.78180 0.03909 51 GLY 0.761650 0.0380825 52 ALA 0.786550 0.0393275 53 ALA 0.71540 0.03577 54 GLU 0.74220 0.03711 55 SER 0.758350 0.0379175 56 ASP 0.843750 0.0421875 57 GLY 0.7840 0.0392 58 ARG 0.75790 0.037895 60 HIS 0.80520 0.04026 61 LYS 0.8040 0.0402 62 GLY 0.818050 0.0409025 63 ASP 0.788550 0.0394275 64 ARG 0.80220 0.04011 65 VAL 0.81510 0.040755 66 LEU 0.770550 0.0385275 67 ALA 0.797250 0.0398625 69 ASN 0.835550 0.0417775 70 GLY 0.792950 0.0396475 71 VAL 0.77580 0.03879 72 SER 0.77490 0.038745 73 LEU 0.775950 0.0387975 74 GLU 0.72380 0.03619 75 GLY 0.7260 0.0363 76 ALA 0.78890 0.039445 77 THR 0.77270 0.038635 78 HIS 0.819250 0.0409625 79 LYS 0.79820 0.03991 80 GLN 0.771150 0.0385575 81 ALA 0.745350 0.0372675 82 VAL 0.82430 0.041215 83 GLU 0.526950 0.0263475 84 THR 0.772250 0.0386125 85 LEU 0.75340 0.03767 86 ARG 0.704450 0.0352225 87 ASN 0.71530 0.035765 88 THR 0.55790 0.027895 89 GLY 0.774750 0.0387375 90 GLN 0.757650 0.0378825 91 VAL 0.72980 0.03649 92 VAL 0.77190 0.038595 93 HIS 0.768050 0.0384025 94 LEU 0.763250 0.0381625 95 LEU 0.79580 0.03979 96 LEU 0.78350 0.039175 97 GLU 0.76230 0.038115 98 LYS 0.74910 0.037455 99 GLY 0.707950 0.0353975 100 GLN 0.519850 0.0259925 101 VAL 0.131950 0.0065975 stop_ save_