data_6093 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF THE HYALURONAN BINDING DOMAIN OF HUMAN CD44 ; _BMRB_accession_number 6093 _BMRB_flat_file_name bmr6093.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 Teriete Peter . . 2 Banerji Suneale . . 3 Blundell Charles D. . 4 Kahmann Jan D. . 5 Pickford Andrew R. . 6 Wright Alan . . 7 Campbell Iain D. . 8 Jackson David G. . 9 Day Anthony J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 683 "13C chemical shifts" 435 "15N chemical shifts" 164 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-03-15 original BMRB . stop_ _Original_release_date 2004-02-05 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the regulatory hyaluronan binding domain in the inflamatory leukocyte homing receptor CD44 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14992719 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Teriete Peter . . 2 Banerji Suneale . . 3 Noble Martin . . 4 Blundell Charles D. . 5 Wright Alan J. . 6 Pickford Andrew R. . 7 Lowe Edward . . 8 Mahoney David J. . 9 Tammi Marku I. . 10 Kahmann Jan D. . 11 Campbell Iain D. . 12 Day Anthony J. . 13 Jackson David G. . stop_ _Journal_abbreviation 'Mol. Cell' _Journal_volume 13 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 483 _Page_last 496 _Year 2004 _Details . loop_ _Keyword 'CARBOHYDRATE-BINDING DOMAIN' 'CELL ADHESION' GLYCOPROTEIN 'HYALURONAN-BINDING DOMAIN' 'LINK MODULE' stop_ save_ ################################## # Molecular system description # ################################## save_system_CD44 _Saveframe_category molecular_system _Mol_system_name 'CD44 antigen' _Abbreviation_common CD44 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CD44 antigen' $CD44 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CD44 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CD44 _Abbreviation_common CD44 _Molecular_mass 17580.36 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 159 _Mol_residue_sequence ; AQIDLNITCRFAGVFHVEKN GRYSISRTEAADLCKAFNST LPTMAQMEKALSIGFETCRY GFIEGHVVIPRIHPNSICAA NNTGVYILTSNTSQYDTYCF NASAPPEEDCTSVTDLPNAF DGPITITIVNRDGTRYVQKG EYRTNPEDIYPSNPTDDDV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 20 ALA 2 21 GLN 3 22 ILE 4 23 ASP 5 24 LEU 6 25 ASN 7 26 ILE 8 27 THR 9 28 CYS 10 29 ARG 11 30 PHE 12 31 ALA 13 32 GLY 14 33 VAL 15 34 PHE 16 35 HIS 17 36 VAL 18 37 GLU 19 38 LYS 20 39 ASN 21 40 GLY 22 41 ARG 23 42 TYR 24 43 SER 25 44 ILE 26 45 SER 27 46 ARG 28 47 THR 29 48 GLU 30 49 ALA 31 50 ALA 32 51 ASP 33 52 LEU 34 53 CYS 35 54 LYS 36 55 ALA 37 56 PHE 38 57 ASN 39 58 SER 40 59 THR 41 60 LEU 42 61 PRO 43 62 THR 44 63 MET 45 64 ALA 46 65 GLN 47 66 MET 48 67 GLU 49 68 LYS 50 69 ALA 51 70 LEU 52 71 SER 53 72 ILE 54 73 GLY 55 74 PHE 56 75 GLU 57 76 THR 58 77 CYS 59 78 ARG 60 79 TYR 61 80 GLY 62 81 PHE 63 82 ILE 64 83 GLU 65 84 GLY 66 85 HIS 67 86 VAL 68 87 VAL 69 88 ILE 70 89 PRO 71 90 ARG 72 91 ILE 73 92 HIS 74 93 PRO 75 94 ASN 76 95 SER 77 96 ILE 78 97 CYS 79 98 ALA 80 99 ALA 81 100 ASN 82 101 ASN 83 102 THR 84 103 GLY 85 104 VAL 86 105 TYR 87 106 ILE 88 107 LEU 89 108 THR 90 109 SER 91 110 ASN 92 111 THR 93 112 SER 94 113 GLN 95 114 TYR 96 115 ASP 97 116 THR 98 117 TYR 99 118 CYS 100 119 PHE 101 120 ASN 102 121 ALA 103 122 SER 104 123 ALA 105 124 PRO 106 125 PRO 107 126 GLU 108 127 GLU 109 128 ASP 110 129 CYS 111 130 THR 112 131 SER 113 132 VAL 114 133 THR 115 134 ASP 116 135 LEU 117 136 PRO 118 137 ASN 119 138 ALA 120 139 PHE 121 140 ASP 122 141 GLY 123 142 PRO 124 143 ILE 125 144 THR 126 145 ILE 127 146 THR 128 147 ILE 129 148 VAL 130 149 ASN 131 150 ARG 132 151 ASP 133 152 GLY 134 153 THR 135 154 ARG 136 155 TYR 137 156 VAL 138 157 GLN 139 158 LYS 140 159 GLY 141 160 GLU 142 161 TYR 143 162 ARG 144 163 THR 145 164 ASN 146 165 PRO 147 166 GLU 148 167 ASP 149 168 ILE 150 169 TYR 151 170 PRO 152 171 SER 153 172 ASN 154 173 PRO 155 174 THR 156 175 ASP 157 176 ASP 158 177 ASP 159 178 VAL 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 BMRB 5903 'CD44 hyaluronan-binding domain' 100.00 160 100.00 100.00 2.15e-89 PDB 1POZ 'Solution Structure Of The Hyaluronan Binding Domain Of Human Cd44' 100.00 159 100.00 100.00 2.71e-89 PDB 1UUH 'Hyaluronan Binding Domain Of Human Cd44' 100.00 159 98.74 98.74 1.22e-87 PDB 2I83 'Hyaluronan-Binding Domain Of Cd44 In Its Ligand-Bound Form' 100.00 160 100.00 100.00 2.15e-89 DBJ BAF83113 'unnamed protein product [Homo sapiens]' 100.00 361 99.37 99.37 1.73e-90 DBJ BAG10625 'CD44 antigen precursor [synthetic construct]' 100.00 361 100.00 100.00 6.35e-91 EMBL CAA38951 'CD44E (epithelial form) [Homo sapiens]' 100.00 493 99.37 99.37 6.19e-91 EMBL CAA40133 'CD44R1 [Homo sapiens]' 100.00 493 100.00 100.00 7.69e-92 EMBL CAA47271 'epican [Homo sapiens]' 100.00 699 100.00 100.00 1.88e-92 EMBL CAB61878 'transmembrane glycoprotein [Homo sapiens]' 100.00 742 99.37 99.37 5.46e-92 EMBL CAC10345 'CD44 molecule (Indian blood group) [Homo sapiens]' 97.48 676 100.00 100.00 4.15e-90 GenBank AAA35674 'CDw44 antigen precursor' 100.00 361 99.37 99.37 3.26e-90 GenBank AAA36138 'Hermes antigen gp90 homing receptor precursor' 100.00 293 100.00 100.00 1.50e-90 GenBank AAA51950 'cell adhesion molecule' 100.00 361 99.37 99.37 3.51e-90 GenBank AAA82949 'cell surface glycoprotein CD44' 100.00 361 99.37 100.00 1.23e-90 GenBank AAA92921 CD44i 70.44 514 100.00 100.00 1.28e-62 REF NP_000601 'CD44 antigen isoform 1 precursor [Homo sapiens]' 100.00 742 100.00 100.00 9.62e-93 REF NP_001001389 'CD44 antigen isoform 2 precursor [Homo sapiens]' 100.00 699 100.00 100.00 2.14e-92 REF NP_001001390 'CD44 antigen isoform 3 precursor [Homo sapiens]' 100.00 493 100.00 100.00 8.42e-92 REF NP_001001391 'CD44 antigen isoform 4 precursor [Homo sapiens]' 100.00 361 100.00 100.00 6.35e-91 REF XP_001151270 'PREDICTED: CD44 antigen isoform 2 [Pan troglodytes]' 100.00 294 99.37 99.37 1.67e-89 SWISS-PROT P16070 ; CD44 antigen precursor (Phagocytic glycoprotein I) (PGP-1) (HUTCH-I) (Extracellular matrix receptor-III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (Hermes antigen) (Hyaluronate receptor) (Heparan sulfate proteoglycan) (Epican) (CDw44) ; 100.00 742 100.00 100.00 1.06e-92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CD44 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $CD44 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CD44 1 mM '[U-13C; U-15N]' D2O 5 % . H2O 95 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CD44 1 mM [U-15N] D2O 5 % . H2O 95 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CD44 1 mM [U-15N] D2O 100 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CD44 1 mM . D2O 5 % . H2O 95 % . stop_ save_ ############################ # Computer software used # ############################ save_CNS _Saveframe_category software _Name CNS _Version 1.1 loop_ _Task 'structure solution' stop_ _Details 'Brunger, A.T.' save_ save_FELIX _Saveframe_category software _Name FELIX _Version 2.3 loop_ _Task processing stop_ _Details 'MSI, San Diego' save_ save_SOPHIE _Saveframe_category software _Name SOPHIE _Version 1.0 loop_ _Task refinement 'structure solution' stop_ _Details 'Pickford, A.R.' save_ save_Sparky _Saveframe_category software _Name Sparky _Version 2.0 loop_ _Task 'data analysis' stop_ _Details 'Goddard, T.D.' save_ save_XEasy _Saveframe_category software _Name XEasy _Version 3.13 loop_ _Task 'data analysis' stop_ _Details 'Xia, T' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model Omega _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model Omega _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer GE _Model Omega _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-separated_NOESY _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_HMQC-J_4 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-J _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label . save_ save_CC(CO)NH_7 _Saveframe_category NMR_applied_experiment _Experiment_name CC(CO)NH _Sample_label . save_ save_NH-Exchange_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name 'NH-Exchange HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 5 . mM pH 6.5 0.15 n/a pressure 1 . atm temperature 298 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio water C 13 protons ppm 4.75 external indirect . . . 0.251449530 water H 1 protons ppm 4.75 external indirect cylindrical external parallel 1 water N 15 protons ppm 4.75 external indirect . . . 0.101329118 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 3D_15N-separated_NOESY '2D NOESY' '2D TOCSY' HMQC-J CBCA(CO)NH HCCH-TOCSY CC(CO)NH 'NH-Exchange HSQC' stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'CD44 antigen' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA CA C 52.295 0.05 1 2 . 1 ALA HA H 4.169 0.02 1 3 . 1 ALA CB C 20.287 0.05 1 4 . 1 ALA HB H 1.781 0.02 1 5 . 2 GLN H H 8.262 0.02 1 6 . 2 GLN N N 122.252 0.05 1 7 . 2 GLN CA C 54.771 0.05 1 8 . 2 GLN HA H 5.3 0.02 1 9 . 2 GLN CB C 31.971 0.05 1 10 . 2 GLN HB2 H 2.092 0.02 1 11 . 2 GLN HB3 H 2.297 0.02 1 12 . 2 GLN HG2 H 2.978 0.02 1 13 . 2 GLN HG3 H 3.289 0.02 1 14 . 2 GLN NE2 N 109.621 0.05 1 15 . 2 GLN HE21 H 6.627 0.02 1 16 . 2 GLN HE22 H 7.768 0.02 1 17 . 3 ILE H H 8.592 0.02 1 18 . 3 ILE N N 123.892 0.05 1 19 . 3 ILE CA C 61.728 0.05 1 20 . 3 ILE HA H 4.508 0.02 1 21 . 3 ILE CB C 42.568 0.05 1 22 . 3 ILE HB H 1.555 0.02 1 23 . 3 ILE CG2 C 17.694 0.05 1 24 . 3 ILE CG1 C 28.675 0.05 1 25 . 3 ILE HG12 H 1.072 0.02 1 26 . 3 ILE CD1 C 13.850 0.05 1 27 . 3 ILE HG2 H 0.992 0.02 1 28 . 4 ASP H H 8.702 0.02 1 29 . 4 ASP N N 128.224 0.05 1 30 . 4 ASP CA C 52.820 0.05 1 31 . 4 ASP HA H 5.397 0.02 1 32 . 4 ASP CB C 42.359 0.05 1 33 . 4 ASP HB2 H 2.468 0.02 1 34 . 4 ASP HB3 H 2.693 0.02 1 35 . 5 LEU H H 9.409 0.02 1 36 . 5 LEU N N 123.345 0.05 1 37 . 5 LEU CA C 52.789 0.05 1 38 . 5 LEU HA H 5.140 0.02 1 39 . 5 LEU CB C 43.771 0.05 1 40 . 5 LEU HB2 H 1.024 0.02 1 41 . 5 LEU HB3 H 2.124 0.02 1 42 . 5 LEU CG C 26.492 0.05 1 43 . 5 LEU CD1 C 27.037 0.05 1 44 . 5 LEU HD1 H 0.687 0.02 1 45 . 5 LEU CD2 C 23.183 0.05 1 46 . 5 LEU HG H 1.596 0.02 1 47 . 6 ASN H H 8.921 0.02 1 48 . 6 ASN N N 123.252 0.05 1 49 . 6 ASN CA C 52.898 0.05 1 50 . 6 ASN HA H 5.457 0.02 1 51 . 6 ASN CB C 45.669 0.05 1 52 . 6 ASN HB2 H 2.644 0.02 1 53 . 6 ASN HB3 H 2.738 0.02 1 54 . 6 ASN ND2 N 111.586 0.05 1 55 . 6 ASN HD21 H 6.827 0.02 1 56 . 6 ASN HD22 H 7.528 0.02 1 57 . 7 ILE H H 8.287 0.02 1 58 . 7 ILE N N 120.216 0.05 1 59 . 7 ILE CA C 59.336 0.05 1 60 . 7 ILE HA H 5.860 0.02 1 61 . 7 ILE CB C 41.892 0.05 1 62 . 7 ILE HB H 1.950 0.02 1 63 . 7 ILE CG2 C 18.783 0.05 1 64 . 7 ILE CG1 C 26.483 0.05 1 65 . 7 ILE HG12 H 1.071 0.02 1 66 . 7 ILE HG13 H 1.550 0.02 1 67 . 7 ILE CD1 C 14.407 0.05 1 68 . 7 ILE HD1 H 0.585 0.02 1 69 . 7 ILE HG2 H 1.050 0.02 1 70 . 8 THR H H 7.945 0.02 1 71 . 8 THR N N 111.682 0.05 1 72 . 8 THR CA C 61.667 0.05 1 73 . 8 THR HA H 4.721 0.02 1 74 . 8 THR CB C 73.862 0.05 1 75 . 8 THR HB H 5.464 0.02 1 76 . 8 THR CG2 C 23.728 0.05 1 77 . 8 THR HG2 H 1.900 0.02 1 78 . 9 CYS H H 8.863 0.02 1 79 . 9 CYS N N 114.253 0.05 1 80 . 9 CYS CA C 59.374 0.05 1 81 . 9 CYS HA H 4.706 0.02 1 82 . 9 CYS CB C 45.671 0.05 1 83 . 9 CYS HB2 H 2.397 0.02 1 84 . 9 CYS HB3 H 3.519 0.02 1 85 . 10 ARG H H 8.483 0.02 1 86 . 10 ARG N N 120.927 0.05 1 87 . 10 ARG CA C 55.471 0.05 1 88 . 10 ARG HA H 5.078 0.02 1 89 . 10 ARG CB C 30.835 0.05 1 90 . 10 ARG HB2 H 1.855 0.02 1 91 . 10 ARG HB3 H 1.96 0.02 1 92 . 10 ARG CG C 28.549 0.05 1 93 . 10 ARG HG2 H 1.47 0.02 1 94 . 10 ARG HG3 H 1.676 0.02 1 95 . 10 ARG CD C 42.277 0.05 1 96 . 10 ARG HD3 H 2.988 0.02 1 97 . 11 PHE H H 9.738 0.02 1 98 . 11 PHE N N 123.336 0.05 1 99 . 11 PHE CA C 52.901 0.05 1 100 . 11 PHE HA H 4.372 0.02 1 101 . 11 PHE CB C 48.533 0.05 1 102 . 11 PHE HZ H 7.470 0.02 1 103 . 12 ALA H H 8.009 0.02 1 104 . 12 ALA N N 127.779 0.05 1 105 . 12 ALA CA C 53.309 0.05 1 106 . 12 ALA HA H 4.242 0.02 1 107 . 12 ALA CB C 16.712 0.05 1 108 . 12 ALA HB H 1.344 0.02 1 109 . 13 GLY H H 8.807 0.02 1 110 . 13 GLY N N 116.017 0.05 1 111 . 13 GLY CA C 46.774 0.05 1 112 . 13 GLY HA3 H 4.351 0.02 1 113 . 13 GLY HA2 H 3.249 0.02 1 114 . 14 VAL H H 7.870 0.02 1 115 . 14 VAL N N 122.600 0.05 1 116 . 14 VAL CA C 62.105 0.05 1 117 . 14 VAL HA H 5.287 0.02 1 118 . 14 VAL CB C 32.240 0.05 1 119 . 14 VAL HB H 1.963 0.02 1 120 . 14 VAL CG1 C 23.174 0.05 1 121 . 14 VAL HG1 H 0.793 0.02 1 122 . 14 VAL CG2 C 23.750 0.05 1 123 . 14 VAL HG2 H 1.041 0.02 1 124 . 15 PHE H H 9.121 0.02 1 125 . 15 PHE N N 120.433 0.05 1 126 . 15 PHE CA C 54.546 0.05 1 127 . 15 PHE HA H 5.094 0.02 1 128 . 15 PHE CB C 41.901 0.05 1 129 . 15 PHE HZ H 6.859 0.02 1 130 . 16 HIS H H 8.850 0.02 1 131 . 16 HIS N N 121.928 0.05 1 132 . 16 HIS CA C 55.039 0.05 1 133 . 16 HIS HA H 5.059 0.02 1 134 . 16 HIS CB C 35.167 0.05 1 135 . 16 HIS HB2 H 3.488 0.02 1 136 . 16 HIS HB3 H 3.59 0.02 1 137 . 16 HIS HD2 H 6.025 0.02 1 138 . 16 HIS HE1 H 7.639 0.02 1 139 . 16 HIS HE2 H 7.553 0.02 1 140 . 17 VAL H H 8.320 0.02 1 141 . 17 VAL N N 125.727 0.05 1 142 . 17 VAL CA C 61.083 0.05 1 143 . 17 VAL HA H 4.400 0.02 1 144 . 17 VAL CB C 34.110 0.05 1 145 . 17 VAL HB H 1.734 0.02 1 146 . 17 VAL CG1 C 22.620 0.05 1 147 . 17 VAL HG1 H 0.539 0.02 1 148 . 17 VAL CG2 C 23.185 0.05 1 149 . 17 VAL HG2 H 0.752 0.02 1 150 . 18 GLU H H 8.040 0.02 1 151 . 18 GLU N N 125.61 0.05 1 152 . 18 GLU CA C 53.941 0.05 1 153 . 18 GLU HA H 4.441 0.02 1 154 . 18 GLU CB C 33.75 0.05 1 155 . 18 GLU HB3 H 1.867 0.02 1 156 . 19 LYS H H 9.858 0.02 1 157 . 19 LYS N N 133.94 0.05 1 158 . 19 LYS CA C 54.903 0.05 1 159 . 19 LYS HA H 5.286 0.02 1 160 . 19 LYS CB C 35.220 0.05 1 161 . 19 LYS HB2 H 2.098 0.02 1 162 . 19 LYS HB3 H 2.308 0.02 1 163 . 20 ASN H H 9.680 0.02 1 164 . 20 ASN N N 122.266 0.05 1 165 . 20 ASN CA C 54.429 0.05 1 166 . 20 ASN HA H 4.607 0.02 1 167 . 20 ASN CB C 37.477 0.05 1 168 . 20 ASN HB2 H 2.777 0.02 1 169 . 20 ASN HB3 H 3.263 0.02 1 170 . 20 ASN ND2 N 112.432 0.05 1 171 . 20 ASN HD21 H 6.830 0.02 1 172 . 20 ASN HD22 H 7.562 0.02 1 173 . 21 GLY H H 8.835 0.02 1 174 . 21 GLY N N 104.757 0.05 1 175 . 21 GLY CA C 46.810 0.05 1 176 . 21 GLY HA3 H 3.843 0.02 1 177 . 21 GLY HA2 H 3.778 0.02 1 178 . 22 ARG H H 7.897 0.02 1 179 . 22 ARG N N 116.106 0.05 1 180 . 22 ARG CA C 54.655 0.05 1 181 . 22 ARG HA H 4.539 0.02 1 182 . 23 TYR H H 7.694 0.02 1 183 . 23 TYR N N 119.729 0.05 1 184 . 23 TYR CA C 58.627 0.05 1 185 . 23 TYR HA H 5.036 0.02 1 186 . 23 TYR CB C 36.539 0.05 1 187 . 23 TYR HB2 H 3.033 0.02 1 188 . 23 TYR HB3 H 3.314 0.02 1 189 . 24 SER H H 7.967 0.02 1 190 . 24 SER N N 118.551 0.05 1 191 . 24 SER CA C 58.690 0.05 1 192 . 24 SER HA H 4.584 0.02 1 193 . 24 SER CB C 64.253 0.05 1 194 . 25 ILE H H 9.286 0.02 1 195 . 25 ILE N N 125.607 0.05 1 196 . 25 ILE CA C 62.088 0.05 1 197 . 25 ILE HA H 4.485 0.02 1 198 . 25 ILE CB C 39.06 0.05 1 199 . 25 ILE HB H 2.319 0.02 1 200 . 25 ILE CG2 C 18.246 0.05 1 201 . 25 ILE HG12 H 1.558 0.02 1 202 . 25 ILE HG13 H 1.766 0.02 1 203 . 25 ILE CD1 C 15.004 0.05 1 204 . 25 ILE HD1 H 0.850 0.02 1 205 . 25 ILE HG2 H 1.111 0.02 1 206 . 26 SER H H 8.094 0.02 1 207 . 26 SER N N 123.339 0.05 1 208 . 26 SER CA C 57.202 0.05 1 209 . 26 SER HA H 5.211 0.02 1 210 . 26 SER CB C 65.964 0.05 1 211 . 26 SER HB2 H 4.161 0.02 1 212 . 26 SER HB3 H 4.455 0.02 1 213 . 27 ARG H H 8.946 0.02 1 214 . 27 ARG N N 121.073 0.05 1 215 . 27 ARG CA C 59.946 0.05 1 216 . 27 ARG HA H 2.51 0.02 1 217 . 27 ARG CB C 30.04 0.05 1 218 . 27 ARG CG C 27.078 0.05 1 219 . 27 ARG HG2 H 1.374 0.02 1 220 . 27 ARG HG3 H 1.45 0.02 1 221 . 27 ARG CD C 42.997 0.05 1 222 . 27 ARG HD2 H 3.157 0.02 1 223 . 27 ARG HD3 H 3.231 0.02 1 224 . 28 THR H H 7.689 0.02 1 225 . 28 THR N N 107.287 0.05 1 226 . 28 THR CA C 58.985 0.05 1 227 . 28 THR HA H 4.040 0.02 1 228 . 28 THR CB C 67.433 0.05 1 229 . 28 THR HB H 4.302 0.02 1 230 . 28 THR CG2 C 22.792 0.05 1 231 . 28 THR HG2 H 1.207 0.02 1 232 . 29 GLU H H 8.027 0.02 1 233 . 29 GLU N N 126.588 0.05 1 234 . 29 GLU CA C 59.947 0.05 1 235 . 29 GLU HA H 4.017 0.02 1 236 . 29 GLU CB C 29.265 0.05 1 237 . 29 GLU CG C 37.606 0.05 1 238 . 29 GLU HG2 H 2.157 0.02 1 239 . 29 GLU HG3 H 2.553 0.02 1 240 . 30 ALA H H 8.733 0.02 1 241 . 30 ALA N N 123.427 0.05 1 242 . 30 ALA CA C 56.226 0.05 1 243 . 30 ALA HA H 3.803 0.02 1 244 . 30 ALA CB C 17.819 0.05 1 245 . 30 ALA HB H 1.664 0.02 1 246 . 31 ALA H H 6.976 0.02 1 247 . 31 ALA N N 116.292 0.05 1 248 . 31 ALA CA C 54.767 0.05 1 249 . 31 ALA HA H 3.902 0.02 1 250 . 31 ALA CB C 18.558 0.05 1 251 . 31 ALA HB H 1.523 0.02 1 252 . 32 ASP H H 7.259 0.02 1 253 . 32 ASP N N 119.988 0.05 1 254 . 32 ASP CA C 57.558 0.05 1 255 . 32 ASP HA H 4.654 0.02 1 256 . 32 ASP CB C 40.718 0.05 1 257 . 32 ASP HB2 H 2.962 0.02 1 258 . 32 ASP HB3 H 3.632 0.02 1 259 . 33 LEU H H 9.470 0.02 1 260 . 33 LEU N N 126.592 0.05 1 261 . 33 LEU CA C 57.985 0.05 1 262 . 33 LEU HA H 3.678 0.02 1 263 . 33 LEU CB C 41.892 0.05 1 264 . 33 LEU HB2 H 1.674 0.02 1 265 . 33 LEU HB3 H 1.882 0.02 1 266 . 33 LEU CG C 27.589 0.05 1 267 . 33 LEU CD1 C 22.644 0.05 1 268 . 33 LEU HD1 H 0.330 0.02 1 269 . 33 LEU CD2 C 26.482 0.05 1 270 . 33 LEU HD2 H 0.697 0.02 1 271 . 33 LEU HG H 1.348 0.02 1 272 . 34 CYS H H 8.598 0.02 1 273 . 34 CYS N N 114.627 0.05 1 274 . 34 CYS CA C 56.810 0.05 1 275 . 34 CYS HA H 4.624 0.02 1 276 . 34 CYS CB C 33.131 0.05 1 277 . 34 CYS HB2 H 2.437 0.02 1 278 . 34 CYS HB3 H 2.463 0.02 1 279 . 35 LYS H H 8.130 0.02 1 280 . 35 LYS N N 122.578 0.05 1 281 . 35 LYS CA C 60.493 0.05 1 282 . 35 LYS HA H 4.447 0.02 1 283 . 35 LYS CB C 32.41 0.05 1 284 . 35 LYS CG C 25.380 0.05 1 285 . 35 LYS HG2 H 1.675 0.02 1 286 . 35 LYS HG3 H 1.743 0.02 1 287 . 35 LYS CD C 29.777 0.05 1 288 . 35 LYS HD3 H 1.950 0.02 1 289 . 35 LYS CE C 42.599 0.05 1 290 . 36 ALA H H 8.111 0.02 1 291 . 36 ALA N N 125.271 0.05 1 292 . 36 ALA CA C 55.712 0.05 1 293 . 36 ALA HA H 3.925 0.02 1 294 . 36 ALA CB C 18.073 0.05 1 295 . 36 ALA HB H 1.315 0.02 1 296 . 37 PHE H H 7.603 0.02 1 297 . 37 PHE N N 114.800 0.05 1 298 . 37 PHE CA C 59.666 0.05 1 299 . 37 PHE HA H 4.552 0.02 1 300 . 37 PHE CB C 39.926 0.05 1 301 . 37 PHE HB2 H 3.158 0.02 1 302 . 37 PHE HB3 H 3.880 0.02 1 303 . 37 PHE HZ H 6.957 0.02 1 304 . 38 ASN H H 8.954 0.02 1 305 . 38 ASN N N 122.773 0.05 1 306 . 38 ASN CA C 54.834 0.05 1 307 . 38 ASN HA H 4.622 0.02 1 308 . 38 ASN CB C 37.516 0.05 1 309 . 38 ASN HB2 H 2.451 0.02 1 310 . 38 ASN HB3 H 3.462 0.02 1 311 . 38 ASN ND2 N 111.416 0.05 1 312 . 38 ASN HD21 H 6.907 0.02 1 313 . 38 ASN HD22 H 7.623 0.02 1 314 . 39 SER H H 8.163 0.02 1 315 . 39 SER N N 111.674 0.05 1 316 . 39 SER CA C 58.884 0.05 1 317 . 39 SER HA H 5.229 0.02 1 318 . 39 SER CB C 67.557 0.05 1 319 . 39 SER HB2 H 3.763 0.02 1 320 . 39 SER HB3 H 3.86 0.02 1 321 . 40 THR H H 9.005 0.02 1 322 . 40 THR N N 112.095 0.05 1 323 . 40 THR CA C 59.454 0.05 1 324 . 40 THR HA H 4.903 0.02 1 325 . 40 THR CB C 71.959 0.05 1 326 . 40 THR HB H 4.470 0.02 1 327 . 40 THR CG2 C 23.180 0.05 1 328 . 40 THR HG2 H 1.309 0.02 1 329 . 41 LEU H H 8.996 0.02 1 330 . 41 LEU N N 124.419 0.05 1 331 . 41 LEU CA C 54.415 0.05 1 332 . 41 LEU HA H 5.007 0.02 1 333 . 41 LEU CB C 41.860 0.05 1 334 . 41 LEU HB2 H 1.193 0.02 1 335 . 41 LEU HB3 H 1.889 0.02 1 336 . 41 LEU CG C 28.549 0.05 1 337 . 41 LEU CD1 C 26.483 0.05 1 338 . 41 LEU HD1 H 0.900 0.02 1 339 . 41 LEU CD2 C 24.831 0.05 1 340 . 41 LEU HD2 H 0.991 0.02 1 341 . 41 LEU HG H 1.697 0.02 1 342 . 42 PRO CA C 58.480 0.05 1 343 . 42 PRO HA H 5.360 0.02 1 344 . 42 PRO CB C 33.254 0.05 1 345 . 43 THR H H 8.392 0.02 1 346 . 43 THR N N 111.219 0.05 1 347 . 43 THR CA C 60.390 0.05 1 348 . 43 THR HA H 4.625 0.02 1 349 . 43 THR CB C 71.452 0.05 1 350 . 43 THR HB H 4.652 0.02 1 351 . 43 THR CG2 C 22.084 0.05 1 352 . 43 THR HG2 H 1.173 0.02 1 353 . 44 MET H H 8.907 0.02 1 354 . 44 MET N N 120.970 0.05 1 355 . 44 MET CA C 57.798 0.05 1 356 . 44 MET HA H 4.146 0.02 1 357 . 44 MET CB C 30.342 0.05 1 358 . 44 MET HB2 H 1.988 0.02 1 359 . 44 MET HB3 H 2.092 0.02 1 360 . 44 MET CG C 32.294 0.05 1 361 . 44 MET HG2 H 2.113 0.02 1 362 . 44 MET HG3 H 2.487 0.02 1 363 . 45 ALA H H 8.304 0.02 1 364 . 45 ALA N N 120.387 0.05 1 365 . 45 ALA CA C 55.1 0.05 1 366 . 45 ALA HA H 4.168 0.02 1 367 . 45 ALA CB C 18.266 0.05 1 368 . 45 ALA HB H 1.310 0.02 1 369 . 46 GLN H H 7.621 0.02 1 370 . 46 GLN N N 119.118 0.05 1 371 . 46 GLN CA C 58.774 0.05 1 372 . 46 GLN HA H 3.823 0.02 1 373 . 46 GLN CB C 27.072 0.05 1 374 . 46 GLN CG C 33.621 0.05 1 375 . 46 GLN NE2 N 109.388 0.05 1 376 . 46 GLN HE21 H 5.581 0.02 1 377 . 46 GLN HE22 H 6.676 0.02 1 378 . 47 MET H H 8.052 0.02 1 379 . 47 MET N N 119.549 0.05 1 380 . 47 MET CA C 56.507 0.05 1 381 . 47 MET HA H 4.506 0.02 1 382 . 47 MET CB C 31.095 0.05 1 383 . 47 MET HB2 H 1.992 0.02 1 384 . 47 MET HB3 H 2.135 0.02 1 385 . 47 MET CG C 33.491 0.05 1 386 . 47 MET HG2 H 2.33 0.02 1 387 . 47 MET HG3 H 2.500 0.02 1 388 . 48 GLU H H 8.735 0.02 1 389 . 48 GLU N N 120.078 0.05 1 390 . 48 GLU CA C 59.957 0.05 1 391 . 48 GLU HA H 3.808 0.02 1 392 . 48 GLU CB C 29.59 0.05 1 393 . 48 GLU HB2 H 2.023 0.02 1 394 . 48 GLU HB3 H 2.135 0.02 1 395 . 48 GLU CG C 37.450 0.05 1 396 . 48 GLU HG2 H 2.149 0.02 1 397 . 48 GLU HG3 H 2.429 0.02 1 398 . 49 LYS H H 7.865 0.02 1 399 . 49 LYS N N 121.182 0.05 1 400 . 49 LYS CA C 58.565 0.05 1 401 . 49 LYS HA H 4.201 0.02 1 402 . 49 LYS CB C 31.112 0.05 1 403 . 49 LYS HB2 H 1.926 0.02 1 404 . 49 LYS HB3 H 2.110 0.02 1 405 . 49 LYS CG C 24.834 0.05 1 406 . 49 LYS HG2 H 1.312 0.02 1 407 . 49 LYS HG3 H 1.556 0.02 1 408 . 49 LYS CD C 28.680 0.05 1 409 . 49 LYS HD2 H 1.721 0.02 1 410 . 49 LYS HD3 H 1.821 0.02 1 411 . 49 LYS CE C 42.385 0.05 1 412 . 49 LYS HE2 H 2.913 0.02 1 413 . 49 LYS HE3 H 3.006 0.02 1 414 . 50 ALA H H 7.748 0.02 1 415 . 50 ALA N N 123.551 0.05 1 416 . 50 ALA CA C 55.629 0.05 1 417 . 50 ALA HA H 3.896 0.02 1 418 . 50 ALA CB C 18.166 0.05 1 419 . 50 ALA HB H 1.461 0.02 1 420 . 51 LEU H H 8.532 0.02 1 421 . 51 LEU N N 121.613 0.05 1 422 . 51 LEU CA C 58.403 0.05 1 423 . 51 LEU HA H 4.544 0.02 1 424 . 51 LEU CB C 43.161 0.05 1 425 . 51 LEU HB2 H 1.572 0.02 1 426 . 51 LEU HB3 H 1.858 0.02 1 427 . 51 LEU CG C 27.057 0.05 1 428 . 51 LEU CD1 C 26.488 0.05 1 429 . 51 LEU HD1 H 0.749 0.02 1 430 . 51 LEU CD2 C 26.511 0.05 1 431 . 51 LEU HG H 1.578 0.02 1 432 . 52 SER H H 7.847 0.02 1 433 . 52 SER N N 114.542 0.05 1 434 . 52 SER CA C 61.641 0.05 1 435 . 52 SER HA H 4.3 0.02 1 436 . 52 SER CB C 63.195 0.05 1 437 . 53 ILE H H 7.368 0.02 1 438 . 53 ILE N N 114.796 0.05 1 439 . 53 ILE CA C 60.464 0.05 1 440 . 53 ILE HA H 4.816 0.02 1 441 . 53 ILE CB C 38.469 0.05 1 442 . 53 ILE HB H 2.428 0.02 1 443 . 53 ILE CG2 C 18.288 0.05 1 444 . 53 ILE CG1 C 28.073 0.05 1 445 . 53 ILE HG12 H 1.541 0.02 1 446 . 53 ILE HG13 H 1.759 0.02 1 447 . 53 ILE CD1 C 15.523 0.05 1 448 . 53 ILE HG2 H 1.088 0.02 1 449 . 54 GLY H H 7.692 0.02 1 450 . 54 GLY N N 106.803 0.05 1 451 . 54 GLY CA C 45.514 0.05 1 452 . 54 GLY HA3 H 4.685 0.02 1 453 . 54 GLY HA2 H 3.545 0.02 1 454 . 55 PHE H H 7.833 0.02 1 455 . 55 PHE N N 124.317 0.05 1 456 . 55 PHE CA C 57.672 0.05 1 457 . 55 PHE HA H 3.476 0.02 1 458 . 55 PHE CB C 40.308 0.05 1 459 . 55 PHE HB2 H 2.170 0.02 1 460 . 55 PHE HB3 H 2.25 0.02 1 461 . 55 PHE HZ H 7.354 0.02 1 462 . 56 GLU H H 6.811 0.02 1 463 . 56 GLU N N 119.283 0.05 1 464 . 56 GLU CA C 54.353 0.05 1 465 . 56 GLU HA H 4.184 0.02 1 466 . 56 GLU CB C 32.951 0.05 1 467 . 56 GLU HB2 H 1.730 0.02 1 468 . 56 GLU HB3 H 2.048 0.02 1 469 . 56 GLU CG C 35.251 0.05 1 470 . 57 THR H H 7.880 0.02 1 471 . 57 THR N N 110.357 0.05 1 472 . 57 THR CA C 59.251 0.05 1 473 . 57 THR HA H 4.462 0.02 1 474 . 57 THR CB C 69.594 0.05 1 475 . 57 THR HB H 3.942 0.02 1 476 . 57 THR CG2 C 21.603 0.05 1 477 . 57 THR HG2 H 0.634 0.02 1 478 . 58 CYS H H 8.874 0.02 1 479 . 58 CYS N N 119.876 0.05 1 480 . 58 CYS CA C 56.055 0.05 1 481 . 58 CYS HA H 4.900 0.02 1 482 . 58 CYS CB C 47.79 0.05 1 483 . 58 CYS HB2 H 2.588 0.02 1 484 . 58 CYS HB3 H 3.363 0.02 1 485 . 59 ARG H H 7.847 0.02 1 486 . 59 ARG N N 119.264 0.05 1 487 . 59 ARG CA C 53.128 0.05 1 488 . 59 ARG HA H 4.828 0.02 1 489 . 59 ARG CB C 33.833 0.05 1 490 . 59 ARG HB3 H 2.351 0.02 1 491 . 60 TYR H H 8.327 0.02 1 492 . 60 TYR N N 123.042 0.05 1 493 . 60 TYR CA C 56.528 0.05 1 494 . 60 TYR HA H 4.682 0.02 1 495 . 60 TYR CB C 40.280 0.05 1 496 . 60 TYR HB2 H 2.224 0.02 1 497 . 60 TYR HB3 H 2.376 0.02 1 498 . 61 GLY H H 9.129 0.02 1 499 . 61 GLY N N 105.610 0.05 1 500 . 61 GLY CA C 45.086 0.05 1 501 . 61 GLY HA3 H 4.444 0.02 1 502 . 61 GLY HA2 H 3.28 0.02 1 503 . 62 PHE H H 7.795 0.02 1 504 . 62 PHE N N 120.428 0.05 1 505 . 62 PHE CA C 61.63 0.05 1 506 . 62 PHE HA H 4.842 0.02 1 507 . 62 PHE CB C 40.626 0.05 1 508 . 62 PHE HZ H 7.710 0.02 1 509 . 63 ILE H H 8.715 0.02 1 510 . 63 ILE N N 110.808 0.05 1 511 . 63 ILE CA C 60.700 0.05 1 512 . 63 ILE HA H 4.61 0.02 1 513 . 63 ILE CB C 40.007 0.05 1 514 . 63 ILE HB H 2.564 0.02 1 515 . 63 ILE CG2 C 20.603 0.05 1 516 . 63 ILE CG1 C 27.054 0.05 1 517 . 63 ILE HG12 H 0.972 0.02 1 518 . 63 ILE HG13 H 1.324 0.02 1 519 . 63 ILE CD1 C 14.948 0.05 1 520 . 63 ILE HD1 H 0.713 0.02 1 521 . 63 ILE HG2 H 1.000 0.02 1 522 . 64 GLU H H 9.127 0.02 1 523 . 64 GLU N N 122.651 0.05 1 524 . 64 GLU CA C 58.933 0.05 1 525 . 64 GLU HA H 4.158 0.02 1 526 . 64 GLU CB C 29.694 0.05 1 527 . 64 GLU HB2 H 1.991 0.02 1 528 . 64 GLU HB3 H 2.100 0.02 1 529 . 64 GLU CG C 35.958 0.05 1 530 . 65 GLY H H 8.533 0.02 1 531 . 65 GLY N N 116.735 0.05 1 532 . 65 GLY CA C 46.222 0.05 1 533 . 65 GLY HA3 H 3.949 0.02 1 534 . 65 GLY HA2 H 3.637 0.02 1 535 . 66 HIS H H 7.058 0.02 1 536 . 66 HIS N N 114.484 0.05 1 537 . 66 HIS CA C 55.434 0.05 1 538 . 66 HIS HA H 4.976 0.02 1 539 . 66 HIS CB C 34.362 0.05 1 540 . 67 VAL H H 8.793 0.02 1 541 . 67 VAL N N 123.023 0.05 1 542 . 67 VAL CA C 63.114 0.05 1 543 . 67 VAL HA H 4.22 0.02 1 544 . 67 VAL CB C 32.638 0.05 1 545 . 67 VAL HB H 1.536 0.02 1 546 . 67 VAL CG1 C 21.583 0.05 1 547 . 67 VAL HG1 H -0.279 0.02 1 548 . 67 VAL CG2 C 22.701 0.05 1 549 . 67 VAL HG2 H 0.426 0.02 1 550 . 68 VAL H H 8.615 0.02 1 551 . 68 VAL N N 115.134 0.05 1 552 . 68 VAL CA C 57.797 0.05 1 553 . 68 VAL HA H 5.996 0.02 1 554 . 68 VAL CB C 37.441 0.05 1 555 . 68 VAL HB H 1.857 0.02 1 556 . 68 VAL CG1 C 19.505 0.05 1 557 . 68 VAL HG1 H 0.511 0.02 1 558 . 68 VAL CG2 C 22.132 0.05 1 559 . 68 VAL HG2 H 0.637 0.02 1 560 . 69 ILE H H 8.437 0.02 1 561 . 69 ILE N N 116.809 0.05 1 562 . 69 ILE CA C 57.832 0.05 1 563 . 69 ILE HA H 4.696 0.02 1 564 . 69 ILE CB C 42.414 0.05 1 565 . 69 ILE HB H 1.299 0.02 1 566 . 69 ILE CG2 C 18.798 0.05 1 567 . 69 ILE CG1 C 27.074 0.05 1 568 . 69 ILE HG12 H 1.262 0.02 1 569 . 69 ILE HG13 H 1.302 0.02 1 570 . 69 ILE CD1 C 13.896 0.05 1 571 . 69 ILE HD1 H 0.009 0.02 1 572 . 70 PRO CA C 56.844 0.05 1 573 . 70 PRO CB C 29.818 0.05 1 574 . 71 ARG H H 8.052 0.02 1 575 . 71 ARG N N 120.863 0.05 1 576 . 71 ARG CA C 52.825 0.05 1 577 . 71 ARG CB C 30.756 0.05 1 578 . 71 ARG HD2 H 2.602 0.02 1 579 . 71 ARG HD3 H 3.808 0.02 1 580 . 72 ILE H H 8.399 0.02 1 581 . 72 ILE N N 120.827 0.05 1 582 . 72 ILE CA C 60.978 0.05 1 583 . 72 ILE HA H 4.405 0.02 1 584 . 72 ILE CB C 39.334 0.05 1 585 . 72 ILE HB H 1.347 0.02 1 586 . 72 ILE CG2 C 17.739 0.05 1 587 . 72 ILE CG1 C 28.169 0.05 1 588 . 72 ILE HG12 H 0.705 0.02 1 589 . 72 ILE HG13 H 1.665 0.02 1 590 . 72 ILE CD1 C 13.837 0.05 1 591 . 72 ILE HD1 H 0.693 0.02 1 592 . 72 ILE HG2 H 0.467 0.02 1 593 . 73 HIS H H 8.203 0.02 1 594 . 73 HIS N N 125.176 0.05 1 595 . 73 HIS CA C 55.589 0.05 1 596 . 73 HIS HB3 H 2.632 0.02 1 597 . 73 HIS HE1 H 7.354 0.02 1 598 . 74 PRO CA C 63.731 0.05 1 599 . 74 PRO CB C 31.158 0.05 1 600 . 74 PRO CG C 29.186 0.05 1 601 . 74 PRO HD2 H 4.032 0.02 2 602 . 75 ASN H H 9.063 0.02 1 603 . 75 ASN N N 124.747 0.05 1 604 . 75 ASN CA C 53.675 0.05 1 605 . 75 ASN HA H 4.747 0.02 1 606 . 75 ASN CB C 42.492 0.05 1 607 . 75 ASN HB2 H 2.308 0.02 1 608 . 75 ASN HB3 H 2.605 0.02 1 609 . 75 ASN ND2 N 112.54 0.05 1 610 . 75 ASN HD21 H 7.094 0.02 1 611 . 75 ASN HD22 H 7.084 0.02 1 612 . 76 SER H H 8.138 0.02 1 613 . 76 SER N N 112.421 0.05 1 614 . 76 SER CA C 62.029 0.05 1 615 . 76 SER HA H 4.107 0.02 1 616 . 76 SER CB C 63.572 0.05 1 617 . 77 ILE H H 7.817 0.02 1 618 . 77 ILE N N 115.502 0.05 1 619 . 77 ILE CA C 61.672 0.05 1 620 . 77 ILE HA H 4.419 0.02 1 621 . 77 ILE CB C 38.373 0.05 1 622 . 77 ILE HB H 2.077 0.02 1 623 . 77 ILE CG2 C 18.271 0.05 1 624 . 77 ILE CG1 C 27.564 0.05 1 625 . 77 ILE HG12 H 1.202 0.02 1 626 . 77 ILE HG13 H 1.436 0.02 1 627 . 77 ILE CD1 C 13.849 0.05 1 628 . 77 ILE HG2 H 0.916 0.02 1 629 . 78 CYS H H 7.491 0.02 1 630 . 78 CYS N N 118.898 0.05 1 631 . 78 CYS CA C 53.913 0.05 1 632 . 78 CYS HA H 4.683 0.02 1 633 . 78 CYS CB C 43.100 0.05 1 634 . 78 CYS HB2 H 2.629 0.02 1 635 . 78 CYS HB3 H 2.720 0.02 1 636 . 79 ALA H H 8.981 0.02 1 637 . 79 ALA N N 124.224 0.05 1 638 . 79 ALA CA C 53.022 0.05 1 639 . 79 ALA HA H 3.626 0.02 1 640 . 79 ALA CB C 17.700 0.05 1 641 . 79 ALA HB H 0.985 0.02 1 642 . 80 ALA H H 8.146 0.02 1 643 . 80 ALA N N 119.298 0.05 1 644 . 80 ALA CA C 53.388 0.05 1 645 . 80 ALA HA H 3.962 0.02 1 646 . 80 ALA CB C 17.117 0.05 1 647 . 80 ALA HB H 1.154 0.02 1 648 . 81 ASN H H 7.360 0.02 1 649 . 81 ASN N N 109.93 0.05 1 650 . 81 ASN CA C 55.431 0.05 1 651 . 81 ASN HA H 4.053 0.02 1 652 . 81 ASN CB C 39.07 0.05 1 653 . 81 ASN HB2 H 2.764 0.02 1 654 . 81 ASN HB3 H 2.946 0.02 1 655 . 81 ASN ND2 N 109.615 0.05 1 656 . 81 ASN HD21 H 6.390 0.02 1 657 . 81 ASN HD22 H 7.139 0.02 1 658 . 82 ASN H H 7.710 0.02 1 659 . 82 ASN N N 117.146 0.05 1 660 . 82 ASN CA C 54.582 0.05 1 661 . 82 ASN HA H 4.507 0.02 1 662 . 82 ASN CB C 36.419 0.05 1 663 . 82 ASN ND2 N 113.608 0.05 1 664 . 82 ASN HD21 H 6.723 0.02 1 665 . 82 ASN HD22 H 8.113 0.02 1 666 . 83 THR H H 8.232 0.02 1 667 . 83 THR N N 107.665 0.05 1 668 . 83 THR CA C 60.445 0.05 1 669 . 83 THR HA H 4.501 0.02 1 670 . 83 THR CB C 71.893 0.05 1 671 . 83 THR HB H 4.083 0.02 1 672 . 83 THR CG2 C 22.112 0.05 1 673 . 83 THR HG2 H 0.776 0.02 1 674 . 84 GLY H H 8.934 0.02 1 675 . 84 GLY N N 108.872 0.05 1 676 . 84 GLY CA C 44.588 0.05 1 677 . 84 GLY HA3 H 4.354 0.02 1 678 . 84 GLY HA2 H 3.619 0.02 1 679 . 85 VAL H H 8.653 0.02 1 680 . 85 VAL N N 121.207 0.05 1 681 . 85 VAL CA C 63.033 0.05 1 682 . 85 VAL HA H 3.94 0.02 1 683 . 85 VAL CB C 29.558 0.05 1 684 . 85 VAL HB H 2.093 0.02 1 685 . 85 VAL CG1 C 22.701 0.05 1 686 . 85 VAL HG1 H 0.536 0.02 1 687 . 85 VAL CG2 C 22.152 0.05 1 688 . 85 VAL HG2 H 0.745 0.02 1 689 . 86 TYR H H 8.172 0.02 1 690 . 86 TYR N N 130.242 0.05 1 691 . 86 TYR CA C 58.743 0.05 1 692 . 86 TYR HA H 4.323 0.02 1 693 . 86 TYR CB C 38.591 0.05 1 694 . 86 TYR HB2 H 2.515 0.02 1 695 . 86 TYR HB3 H 2.972 0.02 1 696 . 87 ILE H H 7.333 0.02 1 697 . 87 ILE N N 127.132 0.05 1 698 . 87 ILE CA C 61.032 0.05 1 699 . 87 ILE HA H 4.052 0.02 1 700 . 87 ILE CB C 39.574 0.05 1 701 . 87 ILE HB H 1.327 0.02 1 702 . 87 ILE CG2 C 18.249 0.05 1 703 . 87 ILE CG1 C 28.172 0.05 1 704 . 87 ILE HG12 H 0.337 0.02 1 705 . 87 ILE HG13 H 1.454 0.02 1 706 . 87 ILE CD1 C 13.326 0.05 1 707 . 87 ILE HD1 H 0.429 0.02 1 708 . 87 ILE HG2 H 0.715 0.02 1 709 . 88 LEU H H 8.383 0.02 1 710 . 88 LEU N N 129.179 0.05 1 711 . 88 LEU CA C 53.881 0.05 1 712 . 88 LEU HA H 4.227 0.02 1 713 . 88 LEU CB C 43.178 0.05 1 714 . 88 LEU HB2 H 0.977 0.02 1 715 . 88 LEU HB3 H 1.280 0.02 1 716 . 88 LEU CG C 27.074 0.05 1 717 . 88 LEU CD1 C 24.877 0.05 1 718 . 88 LEU HD1 H -0.118 0.02 1 719 . 88 LEU CD2 C 22.681 0.05 1 720 . 88 LEU HD2 H 0.618 0.02 1 721 . 88 LEU HG H 0.795 0.02 1 722 . 89 THR H H 8.367 0.02 1 723 . 89 THR N N 121.330 0.05 1 724 . 89 THR CA C 64.545 0.05 1 725 . 89 THR HA H 4.257 0.02 1 726 . 89 THR CB C 65.913 0.05 1 727 . 89 THR HB H 4.187 0.02 1 728 . 89 THR CG2 C 22.095 0.05 1 729 . 89 THR HG2 H 1.154 0.02 1 730 . 90 SER H H 7.794 0.02 1 731 . 90 SER N N 118.588 0.05 1 732 . 90 SER CA C 57.369 0.05 1 733 . 90 SER HA H 4.535 0.02 1 734 . 90 SER CB C 63.806 0.05 1 735 . 90 SER HB2 H 3.738 0.02 1 736 . 90 SER HB3 H 3.824 0.02 1 737 . 91 ASN H H 9.537 0.02 1 738 . 91 ASN N N 125.745 0.05 1 739 . 91 ASN CA C 53.058 0.05 1 740 . 91 ASN CB C 39.695 0.05 1 741 . 91 ASN ND2 N 111.765 0.05 1 742 . 91 ASN HD21 H 6.845 0.02 1 743 . 91 ASN HD22 H 7.471 0.02 1 744 . 92 THR N N 113.298 0.05 1 745 . 92 THR CA C 62.996 0.05 1 746 . 92 THR HA H 4.377 0.02 1 747 . 92 THR CB C 69.146 0.05 1 748 . 92 THR HB H 4.162 0.02 1 749 . 92 THR CG2 C 22.073 0.05 1 750 . 92 THR HG2 H 1.154 0.02 1 751 . 93 SER H H 8.046 0.02 1 752 . 93 SER N N 116.424 0.05 1 753 . 93 SER CA C 58.711 0.05 1 754 . 93 SER HA H 4.488 0.02 1 755 . 93 SER CB C 64.408 0.05 1 756 . 94 GLN H H 7.197 0.02 1 757 . 94 GLN N N 118.677 0.05 1 758 . 94 GLN CA C 54.969 0.05 1 759 . 94 GLN HA H 4.819 0.02 1 760 . 94 GLN CB C 32.271 0.05 1 761 . 94 GLN HB2 H 1.672 0.02 1 762 . 94 GLN HB3 H 1.918 0.02 1 763 . 94 GLN CG C 33.630 0.05 1 764 . 94 GLN HG2 H 1.936 0.02 1 765 . 94 GLN HG3 H 2.260 0.02 1 766 . 94 GLN NE2 N 110.144 0.05 1 767 . 94 GLN HE21 H 6.635 0.02 1 768 . 94 GLN HE22 H 7.201 0.02 1 769 . 95 TYR H H 8.598 0.02 1 770 . 95 TYR N N 119.497 0.05 1 771 . 95 TYR CA C 58.175 0.05 1 772 . 95 TYR HA H 4.677 0.02 1 773 . 95 TYR CB C 41.272 0.05 1 774 . 95 TYR HB2 H 2.089 0.02 1 775 . 95 TYR HB3 H 2.837 0.02 1 776 . 96 ASP H H 7.747 0.02 1 777 . 96 ASP N N 120.12 0.05 1 778 . 96 ASP CA C 54.775 0.05 1 779 . 96 ASP HA H 5.584 0.02 1 780 . 96 ASP CB C 40.708 0.05 1 781 . 96 ASP HB2 H 2.943 0.02 1 782 . 96 ASP HB3 H 3.616 0.02 1 783 . 97 THR H H 7.997 0.02 1 784 . 97 THR N N 111.118 0.05 1 785 . 97 THR CA C 62.717 0.05 1 786 . 97 THR HA H 5.129 0.02 1 787 . 97 THR CB C 71.585 0.05 1 788 . 97 THR HB H 3.942 0.02 1 789 . 97 THR CG2 C 20.988 0.05 1 790 . 97 THR HG2 H 0.998 0.02 1 791 . 98 TYR H H 8.542 0.02 1 792 . 98 TYR N N 123.345 0.05 1 793 . 98 TYR CA C 57.081 0.05 1 794 . 98 TYR HA H 5.532 0.02 1 795 . 98 TYR CB C 41.507 0.05 1 796 . 98 TYR HB2 H 2.921 0.02 1 797 . 98 TYR HB3 H 3.001 0.02 1 798 . 99 CYS H H 8.459 0.02 1 799 . 99 CYS N N 113.77 0.05 1 800 . 99 CYS CA C 51.803 0.05 1 801 . 99 CYS HA H 5.357 0.02 1 802 . 99 CYS CB C 42.299 0.05 1 803 . 99 CYS HB2 H 0.61 0.02 1 804 . 99 CYS HB3 H 2.467 0.02 1 805 . 100 PHE H H 9.879 0.02 1 806 . 100 PHE N N 120.619 0.05 1 807 . 100 PHE CA C 56.596 0.05 1 808 . 100 PHE HA H 5.313 0.02 1 809 . 100 PHE CB C 41.800 0.05 1 810 . 100 PHE HB2 H 2.528 0.02 1 811 . 100 PHE HB3 H 2.86 0.02 1 812 . 100 PHE HZ H 7.293 0.02 1 813 . 101 ASN H H 8.998 0.02 1 814 . 101 ASN N N 128.612 0.05 1 815 . 101 ASN CA C 51.796 0.05 1 816 . 101 ASN HA H 4.791 0.02 1 817 . 101 ASN CB C 40.539 0.05 1 818 . 101 ASN HB2 H 2.614 0.02 1 819 . 101 ASN HB3 H 2.77 0.02 1 820 . 101 ASN ND2 N 111.615 0.05 1 821 . 101 ASN HD21 H 7.04 0.02 1 822 . 101 ASN HD22 H 7.136 0.02 1 823 . 102 ALA H H 8.675 0.02 1 824 . 102 ALA N N 127.732 0.05 1 825 . 102 ALA CA C 54.055 0.05 1 826 . 102 ALA HA H 3.887 0.02 1 827 . 102 ALA CB C 18.789 0.05 1 828 . 102 ALA HB H 1.522 0.02 1 829 . 103 SER H H 8.103 0.02 1 830 . 103 SER N N 112.153 0.05 1 831 . 103 SER CA C 58.817 0.05 1 832 . 103 SER HA H 4.446 0.02 1 833 . 103 SER CB C 63.885 0.05 1 834 . 104 ALA H H 6.834 0.02 1 835 . 104 ALA N N 125.548 0.05 1 836 . 104 ALA CA C 50.716 0.05 1 837 . 104 ALA HA H 4.380 0.02 1 838 . 104 ALA CB C 18.288 0.05 1 839 . 104 ALA HB H 1.393 0.02 1 840 . 106 PRO CA C 64.288 0.05 1 841 . 106 PRO HA H 4.439 0.02 1 842 . 106 PRO CB C 31.425 0.05 1 843 . 106 PRO CG C 28.290 0.05 1 844 . 106 PRO CD C 50.090 0.05 1 845 . 106 PRO HD2 H 3.703 0.02 1 846 . 107 GLU H H 7.753 0.02 1 847 . 107 GLU N N 116.101 0.05 1 848 . 107 GLU CA C 55.167 0.05 1 849 . 107 GLU HA H 4.553 0.02 1 850 . 107 GLU CB C 30.389 0.05 1 851 . 107 GLU HB2 H 1.952 0.02 1 852 . 107 GLU HB3 H 2.208 0.02 1 853 . 107 GLU CG C 35.879 0.05 1 854 . 108 GLU H H 8.218 0.02 1 855 . 108 GLU N N 123.445 0.05 1 856 . 108 GLU CA C 56.569 0.05 1 857 . 108 GLU HA H 4.339 0.02 1 858 . 108 GLU CB C 30.314 0.05 1 859 . 108 GLU HB2 H 1.570 0.02 1 860 . 108 GLU CG C 36.349 0.05 1 861 . 108 GLU HG2 H 0.981 0.02 1 862 . 108 GLU HG3 H 1.740 0.02 1 863 . 109 ASP H H 9.385 0.02 1 864 . 109 ASP N N 127.344 0.05 1 865 . 109 ASP CA C 53.245 0.05 1 866 . 109 ASP HA H 4.890 0.02 1 867 . 109 ASP CB C 43.501 0.05 1 868 . 109 ASP HB2 H 2.404 0.02 1 869 . 109 ASP HB3 H 2.781 0.02 1 870 . 110 CYS H H 9.267 0.02 1 871 . 110 CYS N N 124.215 0.05 1 872 . 110 CYS CA C 53.253 0.05 1 873 . 110 CYS HA H 4.927 0.02 1 874 . 110 CYS CB C 41.100 0.05 1 875 . 111 THR H H 8.121 0.02 1 876 . 111 THR N N 119.108 0.05 1 877 . 111 THR CA C 64.766 0.05 1 878 . 111 THR HA H 3.939 0.02 1 879 . 111 THR CB C 69.395 0.05 1 880 . 111 THR HB H 3.952 0.02 1 881 . 111 THR CG2 C 21.642 0.05 1 882 . 111 THR HG2 H 1.263 0.02 1 883 . 112 SER H H 8.642 0.02 1 884 . 112 SER N N 122.15 0.05 1 885 . 112 SER CA C 60.404 0.05 1 886 . 112 SER HA H 3.924 0.02 1 887 . 112 SER CB C 63.216 0.05 1 888 . 112 SER HB2 H 3.634 0.02 1 889 . 112 SER HB3 H 3.737 0.02 1 890 . 113 VAL H H 8.789 0.02 1 891 . 113 VAL N N 128.322 0.05 1 892 . 113 VAL CA C 62.862 0.05 1 893 . 113 VAL HA H 3.978 0.02 1 894 . 113 VAL CB C 32.217 0.05 1 895 . 113 VAL HB H 1.998 0.02 1 896 . 113 VAL CG1 C 21.411 0.05 1 897 . 113 VAL HG1 H 0.693 0.02 1 898 . 113 VAL CG2 C 22.093 0.05 1 899 . 113 VAL HG2 H 1.022 0.02 1 900 . 114 THR H H 8.007 0.02 1 901 . 114 THR N N 113.83 0.05 1 902 . 114 THR CA C 60.996 0.05 1 903 . 114 THR HA H 3.47 0.02 1 904 . 114 THR CB C 69.812 0.05 1 905 . 114 THR HB H 3.735 0.02 1 906 . 114 THR CG2 C 20.445 0.05 1 907 . 114 THR HG2 H 0.323 0.02 1 908 . 115 ASP H H 7.321 0.02 1 909 . 115 ASP N N 116.956 0.05 1 910 . 115 ASP CA C 53.275 0.05 1 911 . 115 ASP HA H 4.280 0.02 1 912 . 115 ASP CB C 42.223 0.05 1 913 . 115 ASP HB2 H 2.411 0.02 1 914 . 115 ASP HB3 H 2.673 0.02 1 915 . 116 LEU H H 8.793 0.02 1 916 . 116 LEU N N 119.271 0.05 1 917 . 116 LEU CA C 51.687 0.05 1 918 . 116 LEU HA H 4.459 0.02 1 919 . 116 LEU CB C 41.350 0.05 1 920 . 116 LEU HB2 H 1.015 0.02 1 921 . 116 LEU HB3 H 1.283 0.02 1 922 . 116 LEU CG C 26.564 0.05 1 923 . 116 LEU CD1 C 24.289 0.05 1 924 . 116 LEU HD1 H -0.177 0.02 1 925 . 116 LEU CD2 C 25.350 0.05 1 926 . 116 LEU HD2 H 0.144 0.02 1 927 . 116 LEU HG H 0.823 0.02 1 928 . 117 PRO CA C 64.778 0.05 1 929 . 117 PRO HA H 4.237 0.02 1 930 . 117 PRO CB C 32.374 0.05 1 931 . 117 PRO HB2 H 1.804 0.02 1 932 . 117 PRO HB3 H 2.380 0.02 1 933 . 117 PRO CG C 29.743 0.05 1 934 . 117 PRO CD C 51.749 0.05 1 935 . 117 PRO HD2 H 3.912 0.02 2 936 . 118 ASN H H 8.104 0.02 1 937 . 118 ASN N N 113.095 0.05 1 938 . 118 ASN CA C 51.552 0.05 1 939 . 118 ASN HA H 5.278 0.02 1 940 . 118 ASN CB C 44 0.05 1 941 . 118 ASN HB2 H 2.834 0.02 1 942 . 118 ASN HB3 H 3.174 0.02 1 943 . 118 ASN ND2 N 110.475 0.05 1 944 . 118 ASN HD21 H 6.826 0.02 1 945 . 118 ASN HD22 H 7.226 0.02 1 946 . 119 ALA H H 7.117 0.02 1 947 . 119 ALA N N 122.049 0.05 1 948 . 119 ALA CA C 52.899 0.05 1 949 . 119 ALA HA H 4.186 0.02 1 950 . 119 ALA CB C 18.798 0.05 1 951 . 119 ALA HB H 1.255 0.02 1 952 . 120 PHE H H 8.091 0.02 1 953 . 120 PHE N N 119.019 0.05 1 954 . 120 PHE CA C 54.356 0.05 1 955 . 120 PHE HA H 5.160 0.02 1 956 . 120 PHE CB C 40.144 0.05 1 957 . 120 PHE HB2 H 3.093 0.02 1 958 . 120 PHE HB3 H 3.339 0.02 1 959 . 120 PHE HZ H 6.889 0.02 1 960 . 121 ASP H H 8.423 0.02 1 961 . 121 ASP N N 118.579 0.05 1 962 . 121 ASP CA C 55.917 0.05 1 963 . 121 ASP HA H 4.689 0.02 1 964 . 121 ASP CB C 41.82 0.05 1 965 . 122 GLY H H 7.873 0.02 1 966 . 122 GLY N N 108.636 0.05 1 967 . 122 GLY CA C 45.718 0.05 1 968 . 122 GLY HA3 H 4.142 0.02 1 969 . 122 GLY HA2 H 3.963 0.02 1 970 . 123 PRO CA C 63.646 0.05 1 971 . 123 PRO CB C 32.389 0.05 1 972 . 123 PRO HD2 H 3.563 0.02 2 973 . 124 ILE H H 8.142 0.02 1 974 . 124 ILE N N 124.751 0.05 1 975 . 124 ILE CA C 60.072 0.05 1 976 . 124 ILE HA H 4.029 0.02 1 977 . 124 ILE CB C 36.242 0.05 1 978 . 124 ILE HB H 2.382 0.02 1 979 . 124 ILE CG2 C 18.288 0.05 1 980 . 124 ILE CG1 C 27.603 0.05 1 981 . 124 ILE HG12 H 1.339 0.02 1 982 . 124 ILE HG13 H 1.573 0.02 1 983 . 124 ILE CD1 C 10.621 0.05 1 984 . 124 ILE HD1 H 0.625 0.02 1 985 . 124 ILE HG2 H 0.750 0.02 1 986 . 125 THR H H 8.262 0.02 1 987 . 125 THR N N 122.388 0.05 1 988 . 125 THR CA C 64.032 0.05 1 989 . 125 THR HA H 4.371 0.02 1 990 . 125 THR CB C 69.04 0.05 1 991 . 125 THR HB H 4.146 0.02 1 992 . 125 THR CG2 C 22.093 0.05 1 993 . 125 THR HG2 H 1.050 0.02 1 994 . 126 ILE H H 9.377 0.02 1 995 . 126 ILE N N 120.043 0.05 1 996 . 126 ILE CA C 60.512 0.05 1 997 . 126 ILE HA H 5.046 0.02 1 998 . 126 ILE CB C 39.738 0.05 1 999 . 126 ILE HB H 1.679 0.02 1 1000 . 126 ILE CG2 C 17.739 0.05 1 1001 . 126 ILE CG1 C 28.133 0.05 1 1002 . 126 ILE HG12 H 0.684 0.02 1 1003 . 126 ILE HG13 H 1.674 0.02 1 1004 . 126 ILE CD1 C 13.837 0.05 1 1005 . 126 ILE HD1 H 0.530 0.02 1 1006 . 126 ILE HG2 H 0.682 0.02 1 1007 . 127 THR H H 9.093 0.02 1 1008 . 127 THR N N 123.136 0.05 1 1009 . 127 THR CA C 61.414 0.05 1 1010 . 127 THR HA H 5.296 0.02 1 1011 . 127 THR CB C 69.979 0.05 1 1012 . 127 THR HB H 4.151 0.02 1 1013 . 127 THR CG2 C 21.563 0.05 1 1014 . 127 THR HG2 H 1.000 0.02 1 1015 . 128 ILE H H 9.396 0.02 1 1016 . 128 ILE N N 127.343 0.05 1 1017 . 128 ILE CA C 61.080 0.05 1 1018 . 128 ILE HA H 4.546 0.02 1 1019 . 128 ILE CB C 40.519 0.05 1 1020 . 128 ILE HB H 1.838 0.02 1 1021 . 128 ILE CG2 C 18.776 0.05 1 1022 . 128 ILE CG1 C 28.669 0.05 1 1023 . 128 ILE HG12 H 0.896 0.02 1 1024 . 128 ILE HG13 H 1.481 0.02 1 1025 . 128 ILE CD1 C 14.414 0.05 1 1026 . 128 ILE HD1 H 0.614 0.02 1 1027 . 128 ILE HG2 H 0.879 0.02 1 1028 . 129 VAL H H 9.157 0.02 1 1029 . 129 VAL N N 127.473 0.05 1 1030 . 129 VAL CA C 62.034 0.05 1 1031 . 129 VAL HA H 4.536 0.02 1 1032 . 129 VAL CB C 32.315 0.05 1 1033 . 129 VAL HB H 2.209 0.02 1 1034 . 129 VAL CG1 C 21.014 0.05 1 1035 . 129 VAL CG2 C 21.603 0.05 1 1036 . 129 VAL HG2 H 0.876 0.02 1 1037 . 129 VAL HG1 H 0.841 0.02 1 1038 . 130 ASN H H 8.499 0.02 1 1039 . 130 ASN N N 123.903 0.05 1 1040 . 130 ASN CA C 53.880 0.05 1 1041 . 130 ASN HA H 4.929 0.02 1 1042 . 130 ASN CB C 42.335 0.05 1 1043 . 130 ASN HB2 H 2.931 0.02 1 1044 . 130 ASN HB3 H 3.267 0.02 1 1045 . 130 ASN ND2 N 114.323 0.05 1 1046 . 130 ASN HD21 H 6.979 0.02 1 1047 . 130 ASN HD22 H 8.048 0.02 1 1048 . 131 ARG H H 9.282 0.02 1 1049 . 131 ARG N N 123.306 0.05 1 1050 . 131 ARG CA C 58.516 0.05 1 1051 . 131 ARG HA H 4.250 0.02 1 1052 . 131 ARG CB C 29.827 0.05 1 1053 . 131 ARG HB3 H 2.126 0.02 1 1054 . 131 ARG CG C 26.479 0.05 1 1055 . 131 ARG CD C 44.050 0.05 1 1056 . 131 ARG HD2 H 3.394 0.02 1 1057 . 131 ARG HD3 H 3.431 0.02 1 1058 . 132 ASP H H 7.936 0.02 1 1059 . 132 ASP N N 116.529 0.05 1 1060 . 132 ASP CA C 53.876 0.05 1 1061 . 132 ASP HA H 4.492 0.02 1 1062 . 132 ASP CB C 39.766 0.05 1 1063 . 132 ASP HB2 H 2.688 0.02 1 1064 . 132 ASP HB3 H 3.097 0.02 1 1065 . 133 GLY H H 8.210 0.02 1 1066 . 133 GLY N N 108.680 0.05 1 1067 . 133 GLY CA C 45.104 0.05 1 1068 . 133 GLY HA3 H 4.364 0.02 1 1069 . 133 GLY HA2 H 3.62 0.02 1 1070 . 134 THR H H 8.286 0.02 1 1071 . 134 THR N N 116.092 0.05 1 1072 . 134 THR CA C 63.681 0.05 1 1073 . 134 THR HA H 4.076 0.02 1 1074 . 134 THR CB C 69.890 0.05 1 1075 . 134 THR HB H 4.086 0.02 1 1076 . 134 THR CG2 C 22.642 0.05 1 1077 . 134 THR HG2 H 1.149 0.02 1 1078 . 135 ARG H H 8.094 0.02 1 1079 . 135 ARG N N 124.208 0.05 1 1080 . 135 ARG CA C 54.513 0.05 1 1081 . 135 ARG HA H 5.594 0.02 1 1082 . 135 ARG CB C 33.843 0.05 1 1083 . 135 ARG CG C 28.133 0.05 1 1084 . 135 ARG HG2 H 1.408 0.02 1 1085 . 135 ARG HG3 H 1.687 0.02 1 1086 . 135 ARG CD C 43.556 0.05 1 1087 . 135 ARG HD2 H 3.057 0.02 1 1088 . 135 ARG HD3 H 3.222 0.02 1 1089 . 136 TYR H H 8.793 0.02 1 1090 . 136 TYR N N 123.122 0.05 1 1091 . 136 TYR CA C 57.759 0.05 1 1092 . 136 TYR HA H 4.705 0.02 1 1093 . 136 TYR CB C 42.501 0.05 1 1094 . 136 TYR HB2 H 2.546 0.02 1 1095 . 136 TYR HB3 H 3.174 0.02 1 1096 . 137 VAL H H 8.481 0.02 1 1097 . 137 VAL N N 122.583 0.05 1 1098 . 137 VAL CA C 61.251 0.05 1 1099 . 137 VAL HA H 5.103 0.02 1 1100 . 137 VAL CB C 34.622 0.05 1 1101 . 137 VAL HB H 1.854 0.02 1 1102 . 137 VAL CG1 C 21.566 0.05 1 1103 . 137 VAL CG2 C 21.585 0.05 1 1104 . 137 VAL HG1 H 0.855 0.02 1 1105 . 138 GLN H H 9.440 0.02 1 1106 . 138 GLN N N 127.841 0.05 1 1107 . 138 GLN CA C 54.562 0.05 1 1108 . 138 GLN HA H 4.679 0.02 1 1109 . 138 GLN CB C 33.404 0.05 1 1110 . 138 GLN CG C 33.567 0.05 1 1111 . 138 GLN HG2 H 1.98 0.02 1 1112 . 138 GLN HG3 H 2.12 0.02 1 1113 . 138 GLN NE2 N 109.683 0.05 1 1114 . 138 GLN HE21 H 6.669 0.02 1 1115 . 138 GLN HE22 H 7.548 0.02 1 1116 . 139 LYS H H 8.566 0.02 1 1117 . 139 LYS N N 124.205 0.05 1 1118 . 139 LYS CA C 54.218 0.05 1 1119 . 139 LYS HA H 5.528 0.02 1 1120 . 139 LYS CB C 33.555 0.05 1 1121 . 139 LYS HB2 H 1.721 0.02 1 1122 . 139 LYS HB3 H 1.826 0.02 1 1123 . 139 LYS CG C 24.799 0.05 1 1124 . 139 LYS HG2 H 1.383 0.02 1 1125 . 139 LYS HG3 H 1.488 0.02 1 1126 . 139 LYS CD C 29.270 0.05 1 1127 . 139 LYS HD2 H 1.646 0.02 1 1128 . 139 LYS CE C 41.842 0.05 1 1129 . 140 GLY H H 9.069 0.02 1 1130 . 140 GLY N N 114.808 0.05 1 1131 . 140 GLY CA C 46.891 0.05 1 1132 . 140 GLY HA3 H 4.191 0.02 1 1133 . 140 GLY HA2 H 3.965 0.02 1 1134 . 141 GLU H H 7.952 0.02 1 1135 . 141 GLU N N 118.705 0.05 1 1136 . 141 GLU CA C 54.948 0.05 1 1137 . 141 GLU HA H 3.980 0.02 1 1138 . 141 GLU CB C 32.719 0.05 1 1139 . 141 GLU HB2 H 2.228 0.02 1 1140 . 141 GLU HB3 H 2.338 0.02 1 1141 . 142 TYR H H 8.698 0.02 1 1142 . 142 TYR N N 116.996 0.05 1 1143 . 142 TYR CA C 57.273 0.05 1 1144 . 142 TYR HA H 4.383 0.02 1 1145 . 142 TYR CB C 41.685 0.05 1 1146 . 142 TYR HB2 H 2.122 0.02 1 1147 . 142 TYR HB3 H 3.076 0.02 1 1148 . 143 ARG H H 8.894 0.02 1 1149 . 143 ARG N N 127.829 0.05 1 1150 . 143 ARG CA C 57.764 0.05 1 1151 . 143 ARG HA H 4.096 0.02 1 1152 . 143 ARG CB C 30.750 0.05 1 1153 . 144 THR H H 8.751 0.02 1 1154 . 144 THR N N 111.356 0.05 1 1155 . 144 THR CA C 61.856 0.05 1 1156 . 144 THR HA H 4.411 0.02 1 1157 . 144 THR CB C 70.759 0.05 1 1158 . 144 THR HB H 4.312 0.02 1 1159 . 144 THR CG2 C 22.073 0.05 1 1160 . 144 THR HG2 H 1.234 0.02 1 1161 . 145 ASN H H 8.745 0.02 1 1162 . 145 ASN N N 124.857 0.05 1 1163 . 145 ASN CA C 50.078 0.05 1 1164 . 145 ASN HA H 5.229 0.02 1 1165 . 145 ASN CB C 44.441 0.05 1 1166 . 145 ASN HB2 H 2.814 0.02 1 1167 . 145 ASN HB3 H 3.484 0.02 1 1168 . 145 ASN ND2 N 112.624 0.05 1 1169 . 145 ASN HD21 H 7.261 0.02 1 1170 . 145 ASN HD22 H 7.441 0.02 1 1171 . 146 PRO CA C 65.518 0.05 1 1172 . 146 PRO HA H 4.163 0.02 1 1173 . 146 PRO CB C 32.412 0.05 1 1174 . 146 PRO HB2 H 2.148 0.02 1 1175 . 146 PRO HB3 H 2.485 0.02 1 1176 . 146 PRO CG C 27.603 0.05 1 1177 . 146 PRO CD C 51.749 0.05 1 1178 . 146 PRO HD2 H 3.447 0.02 2 1179 . 147 GLU H H 7.888 0.02 1 1180 . 147 GLU N N 115.24 0.05 1 1181 . 147 GLU CA C 58.241 0.05 1 1182 . 147 GLU HA H 4.080 0.02 1 1183 . 147 GLU CB C 29.632 0.05 1 1184 . 147 GLU HB2 H 1.841 0.02 1 1185 . 147 GLU HB3 H 2.056 0.02 1 1186 . 147 GLU CG C 36.918 0.05 1 1187 . 147 GLU HG2 H 2.303 0.02 1 1188 . 147 GLU HG3 H 2.391 0.02 1 1189 . 148 ASP H H 7.758 0.02 1 1190 . 148 ASP N N 115.073 0.05 1 1191 . 148 ASP CA C 55.111 0.05 1 1192 . 148 ASP HA H 4.687 0.02 1 1193 . 148 ASP CB C 41.231 0.05 1 1194 . 148 ASP HB2 H 2.593 0.02 1 1195 . 148 ASP HB3 H 2.743 0.02 1 1196 . 149 ILE H H 7.073 0.02 1 1197 . 149 ILE N N 120.422 0.05 1 1198 . 149 ILE CA C 63.752 0.05 1 1199 . 149 ILE HA H 3.537 0.02 1 1200 . 149 ILE CB C 39.449 0.05 1 1201 . 149 ILE HB H 1.323 0.02 1 1202 . 149 ILE CG2 C 17.190 0.05 1 1203 . 149 ILE CG1 C 28.701 0.05 1 1204 . 149 ILE CD1 C 12.719 0.05 1 1205 . 149 ILE HD1 H 0.534 0.02 1 1206 . 149 ILE HG13 H 0.3 0.02 1 1207 . 149 ILE HG12 H 0.346 0.02 1 1208 . 150 TYR H H 7.850 0.02 1 1209 . 150 TYR N N 119.983 0.05 1 1210 . 150 TYR CA C 55.012 0.05 1 1211 . 150 TYR HA H 4.902 0.02 1 1212 . 150 TYR CB C 38.075 0.05 1 1213 . 150 TYR HB2 H 2.868 0.02 1 1214 . 150 TYR HB3 H 3.027 0.02 1 1215 . 151 PRO CA C 63.264 0.05 1 1216 . 151 PRO HA H 4.545 0.02 1 1217 . 151 PRO CB C 32.424 0.05 1 1218 . 151 PRO HB2 H 2.018 0.02 1 1219 . 151 PRO HB3 H 2.34 0.02 1 1220 . 151 PRO CG C 27.583 0.05 1 1221 . 151 PRO CD C 50.671 0.05 1 1222 . 152 SER H H 8.692 0.02 1 1223 . 152 SER N N 117.294 0.05 1 1224 . 152 SER CA C 58.98 0.05 1 1225 . 152 SER HA H 4.426 0.02 1 1226 . 152 SER CB C 63.887 0.05 1 1227 . 153 ASN H H 8.403 0.02 1 1228 . 153 ASN N N 120.770 0.05 1 1229 . 153 ASN CA C 51.611 0.05 1 1230 . 153 ASN HA H 5.066 0.02 1 1231 . 153 ASN CB C 39.089 0.05 1 1232 . 153 ASN HB2 H 2.670 0.02 1 1233 . 153 ASN HB3 H 2.836 0.02 1 1234 . 153 ASN ND2 N 113.530 0.05 1 1235 . 153 ASN HD21 H 6.903 0.02 1 1236 . 153 ASN HD22 H 7.625 0.02 1 1237 . 154 PRO CA C 63.722 0.05 1 1238 . 154 PRO HA H 4.528 0.02 1 1239 . 154 PRO CB C 32.443 0.05 1 1240 . 154 PRO HB2 H 2.032 0.02 1 1241 . 154 PRO HB3 H 2.319 0.02 1 1242 . 154 PRO CG C 27.564 0.05 1 1243 . 154 PRO CD C 50.676 0.05 1 1244 . 154 PRO HD2 H 3.744 0.02 2 1245 . 155 THR H H 8.278 0.02 1 1246 . 155 THR N N 113.448 0.05 1 1247 . 155 THR CA C 61.706 0.05 1 1248 . 155 THR HA H 4.423 0.02 1 1249 . 155 THR CB C 70.258 0.05 1 1250 . 155 THR HB H 4.313 0.02 1 1251 . 155 THR CG2 C 21.859 0.05 1 1252 . 155 THR HG2 H 1.214 0.02 1 1253 . 156 ASP H H 8.273 0.02 1 1254 . 156 ASP N N 122.244 0.05 1 1255 . 156 ASP CA C 54.668 0.05 1 1256 . 156 ASP HA H 4.651 0.02 1 1257 . 156 ASP CB C 41.263 0.05 1 1258 . 156 ASP HB2 H 2.591 0.02 1 1259 . 156 ASP HB3 H 2.719 0.02 1 1260 . 157 ASP H H 8.210 0.02 1 1261 . 157 ASP N N 120.057 0.05 1 1262 . 157 ASP CA C 54.626 0.05 1 1263 . 157 ASP HA H 4.623 0.02 1 1264 . 157 ASP CB C 41.423 0.05 1 1265 . 157 ASP HB2 H 2.595 0.02 1 1266 . 157 ASP HB3 H 2.736 0.02 1 1267 . 158 ASP H H 8.272 0.02 1 1268 . 158 ASP N N 121.267 0.05 1 1269 . 158 ASP CA C 54.59 0.05 1 1270 . 158 ASP HA H 4.65 0.02 1 1271 . 158 ASP CB C 41.207 0.05 1 1272 . 158 ASP HB2 H 2.617 0.02 1 1273 . 158 ASP HB3 H 2.736 0.02 1 1274 . 159 VAL H H 7.555 0.02 1 1275 . 159 VAL N N 123.538 0.05 1 1276 . 159 VAL CA C 63.842 0.05 1 1277 . 159 VAL HA H 4.033 0.02 1 1278 . 159 VAL CB C 33.584 0.05 1 1279 . 159 VAL HB H 2.114 0.02 1 1280 . 159 VAL CG1 C 20.485 0.05 1 1281 . 159 VAL CG2 C 22.001 0.05 1 1282 . 159 VAL HG2 H 0.903 0.02 1 stop_ save_