data_4333 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The Three-dimensional Solution Structure and Dynamic Properties of the Human FADD Death Domain ; _BMRB_accession_number 4333 _BMRB_flat_file_name bmr4333.str _Entry_type original _Submission_date 1999-04-16 _Accession_date 1999-04-16 _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 Berglund Helena . . 2 Olerenshaw Dionne . . 3 Sankar A. . . 4 Federwisch M. . . 5 McDonald Neil Q. . 6 Driscoll Paul C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 591 "13C chemical shifts" 330 "15N chemical shifts" 116 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-12-15 original author . stop_ _Original_release_date 2000-12-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Three-dimensional Solution Structure and Dynamic Properties of the Human FADD Death Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20422733 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Berglund Helena . . 2 Olerenshaw Dionne . . 3 Sankar A. . . 4 Federwisch M. . . 5 McDonald Neil Q. . 6 Driscoll Paul C. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of Molecular Biology' _Journal_volume 302 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 171 _Page_last 188 _Year 2000 _Details . save_ ################################## # Molecular system description # ################################## save_system_FADD_dd _Saveframe_category molecular_system _Mol_system_name 'FADD death domain' _Abbreviation_common 'FADD dd' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'FADD death domain' $FADD_dd stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FADD_dd _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'FADD death domain' _Abbreviation_common 'FADD dd' _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; GSHMGEEDLCAAFNVICDNV GKDWRRLARQLKVSDTKIDS IEDRYPRNLTERVRESLRIW KNTEKENATVAHLVGALRSC QMNLVADLVQEVQQARDLQN RSGA ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 GLY 6 GLU 7 GLU 8 ASP 9 LEU 10 CYS 11 ALA 12 ALA 13 PHE 14 ASN 15 VAL 16 ILE 17 CYS 18 ASP 19 ASN 20 VAL 21 GLY 22 LYS 23 ASP 24 TRP 25 ARG 26 ARG 27 LEU 28 ALA 29 ARG 30 GLN 31 LEU 32 LYS 33 VAL 34 SER 35 ASP 36 THR 37 LYS 38 ILE 39 ASP 40 SER 41 ILE 42 GLU 43 ASP 44 ARG 45 TYR 46 PRO 47 ARG 48 ASN 49 LEU 50 THR 51 GLU 52 ARG 53 VAL 54 ARG 55 GLU 56 SER 57 LEU 58 ARG 59 ILE 60 TRP 61 LYS 62 ASN 63 THR 64 GLU 65 LYS 66 GLU 67 ASN 68 ALA 69 THR 70 VAL 71 ALA 72 HIS 73 LEU 74 VAL 75 GLY 76 ALA 77 LEU 78 ARG 79 SER 80 CYS 81 GLN 82 MET 83 ASN 84 LEU 85 VAL 86 ALA 87 ASP 88 LEU 89 VAL 90 GLN 91 GLU 92 VAL 93 GLN 94 GLN 95 ALA 96 ARG 97 ASP 98 LEU 99 GLN 100 ASN 101 ARG 102 SER 103 GLY 104 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-06-02 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 PDB 1E3Y "Death Domain From Human FaddMORT1" 100.00 104 100.00 100.00 5.65e-69 PDB 1E41 "Death Domain From Human FaddMORT1" 100.00 104 100.00 100.00 5.65e-69 PDB 2GF5 "Structure Of Intact Fadd (Mort1)" 99.04 191 97.09 98.06 6.66e-65 PDB 3EZQ "Crystal Structure Of The FasFADD DEATH DOMAIN COMPLEX" 96.15 122 100.00 100.00 1.58e-65 PDB 3OQ9 "Structure Of The FasFADD DEATH DOMAIN ASSEMBLY" 88.46 100 100.00 100.00 2.52e-59 DBJ BAF83694 "unnamed protein product [Homo sapiens]" 100.00 208 97.12 98.08 1.63e-65 DBJ BAJ17951 "Fas (TNFRSF6)-associated via death domain [synthetic construct]" 100.00 208 97.12 98.08 1.63e-65 EMBL CAA59197 "mediator of receptor induced toxicity [Homo sapiens]" 100.00 208 97.12 98.08 1.51e-65 EMBL CAG33019 "FADD [Homo sapiens]" 100.00 208 97.12 98.08 1.63e-65 GB AAA86517 "FADD [Homo sapiens]" 100.00 208 97.12 98.08 1.63e-65 GB AAB58483 "FADD protein [Homo sapiens]" 100.00 149 97.12 98.08 5.73e-66 GB AAH00334 "Fas (TNFRSF6)-associated via death domain [Homo sapiens]" 100.00 208 97.12 98.08 1.63e-65 GB AAP35573 "Fas (TNFRSF6)-associated via death domain [Homo sapiens]" 100.00 208 97.12 98.08 1.63e-65 GB AAP36297 "Homo sapiens Fas (TNFRSF6)-associated via death domain [synthetic construct]" 100.00 209 97.12 98.08 1.77e-65 REF NP_003815 "FAS-associated death domain protein [Homo sapiens]" 100.00 208 97.12 98.08 1.63e-65 REF XP_002821454 "PREDICTED: FAS-associated death domain protein [Pongo abelii]" 93.27 208 97.94 100.00 1.75e-60 REF XP_008952492 "PREDICTED: FAS-associated death domain protein, partial [Pan paniscus]" 96.15 136 99.00 100.00 9.16e-65 REF XP_011798139 "PREDICTED: FAS-associated death domain protein [Colobus angolensis palliatus]" 93.27 212 96.91 97.94 3.11e-59 REF XP_508611 "PREDICTED: FAS-associated death domain protein [Pan troglodytes]" 96.15 208 99.00 100.00 2.14e-64 SP Q13158 "RecName: Full=FAS-associated death domain protein; AltName: Full=FAS-associating death domain-containing protein; AltName: Full" 100.00 208 97.12 98.08 1.63e-65 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FADD_dd 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 $FADD_dd 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_15N_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $FADD_dd 1.5 mM 0.6 2.4 [U-15N] 'potassium phosphate buffer' 50 mM . . . NaCl 150 mM . . . DTT 10 mM . . . azide 0.01 % . . . stop_ save_ save_15N13C_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FADD_dd 1.5 mM '[U-13C; U-15N]' 'potassium phosphate buffer' 50 mM . NaCl 150 mM . DTT 10 mM . azide 0.01 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.2 0.1 na temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $15N_sample $15N13C_sample stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'FADD death domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 5 GLY H H 8.536 0.01 1 2 . 5 GLY HA2 H 3.95 0.01 1 3 . 5 GLY HA3 H 3.95 0.01 1 4 . 5 GLY CA C 46.318 0.1 1 5 . 5 GLY N N 110.523 0.1 1 6 . 6 GLU H H 8.195 0.01 1 7 . 6 GLU HA H 4.174 0.01 1 8 . 6 GLU HB2 H 2.026 0.01 2 9 . 6 GLU HB3 H 1.984 0.01 2 10 . 6 GLU CA C 57.935 0.1 1 11 . 6 GLU CB C 29.812 0.1 1 12 . 6 GLU CG C 36.357 0.1 1 13 . 6 GLU N N 121.467 0.1 1 14 . 7 GLU H H 8.513 0.01 1 15 . 7 GLU HA H 4.048 0.01 1 16 . 7 GLU HB2 H 1.994 0.01 1 17 . 7 GLU HB3 H 1.994 0.01 1 18 . 7 GLU HG2 H 2.289 0.01 1 19 . 7 GLU HG3 H 2.289 0.01 1 20 . 7 GLU CA C 58.922 0.1 1 21 . 7 GLU CB C 29.709 0.1 1 22 . 7 GLU CG C 36.801 0.1 1 23 . 7 GLU N N 121.427 0.1 1 24 . 8 ASP H H 8.465 0.01 1 25 . 8 ASP HA H 4.352 0.01 1 26 . 8 ASP HB2 H 2.868 0.01 2 27 . 8 ASP HB3 H 2.701 0.01 2 28 . 8 ASP CA C 56.582 0.1 1 29 . 8 ASP CB C 40.323 0.1 1 30 . 8 ASP N N 122.407 0.1 1 31 . 9 LEU H H 7.997 0.01 1 32 . 9 LEU HA H 3.753 0.01 1 33 . 9 LEU HB2 H 1.422 0.01 2 34 . 9 LEU HB3 H 1.12 0.01 2 35 . 9 LEU HG H 1.231 0.01 1 36 . 9 LEU HD1 H 0.829 0.01 1 37 . 9 LEU HD2 H 0.764 0.01 1 38 . 9 LEU CA C 57.31 0.1 1 39 . 9 LEU CB C 41.735 0.1 1 40 . 9 LEU CG C 26.634 0.1 1 41 . 9 LEU CD1 C 25.118 0.1 1 42 . 9 LEU CD2 C 24.462 0.1 1 43 . 9 LEU N N 122.753 0.1 1 44 . 10 CYS H H 7.856 0.01 1 45 . 10 CYS HA H 3.704 0.01 1 46 . 10 CYS HB2 H 2.909 0.01 1 47 . 10 CYS HB3 H 2.909 0.01 1 48 . 10 CYS CA C 63.237 0.1 1 49 . 10 CYS CB C 26.537 0.1 1 50 . 10 CYS N N 117.174 0.1 1 51 . 11 ALA H H 7.82 0.1 1 52 . 11 ALA HA H 4.137 0.01 1 53 . 11 ALA HB H 1.408 0.01 1 54 . 11 ALA CA C 55.307 0.1 1 55 . 11 ALA CB C 17.794 0.1 1 56 . 11 ALA N N 121.958 0.1 1 57 . 12 ALA H H 7.831 0.01 1 58 . 12 ALA HA H 4.14 0.01 1 59 . 12 ALA HB H 1.497 0.01 1 60 . 12 ALA CA C 55.278 0.1 1 61 . 12 ALA CB C 19.157 0.1 1 62 . 12 ALA N N 121.714 0.1 1 63 . 13 PHE H H 9.016 0.01 1 64 . 13 PHE HA H 4.315 0.01 1 65 . 13 PHE HB2 H 3.612 0.01 2 66 . 13 PHE HB3 H 3.023 0.01 2 67 . 13 PHE HD1 H 7.108 0.01 1 68 . 13 PHE HD2 H 7.108 0.01 1 69 . 13 PHE HE1 H 7.352 0.01 1 70 . 13 PHE HE2 H 7.352 0.01 1 71 . 13 PHE CA C 57.945 0.1 1 72 . 13 PHE CB C 36.708 0.1 1 73 . 13 PHE CD1 C 131.7 0.5 1 74 . 13 PHE CD2 C 131.7 0.5 1 75 . 13 PHE CE1 C 132.9 0.5 1 76 . 13 PHE CE2 C 132.9 0.5 1 77 . 13 PHE N N 117.567 0.1 1 78 . 14 ASN H H 8.033 0.01 1 79 . 14 ASN HA H 4.37 0.01 1 80 . 14 ASN HB2 H 2.943 0.01 1 81 . 14 ASN HB3 H 2.943 0.01 1 82 . 14 ASN HD21 H 7.583 0.01 2 83 . 14 ASN HD22 H 6.804 0.01 2 84 . 14 ASN CA C 56.676 0.1 1 85 . 14 ASN CB C 37.579 0.1 1 86 . 14 ASN N N 119.194 0.1 1 87 . 14 ASN ND2 N 112.57 0.1 1 88 . 15 VAL H H 7.504 0.01 1 89 . 15 VAL HA H 3.778 0.01 1 90 . 15 VAL HB H 2.226 0.01 1 91 . 15 VAL HG1 H 0.823 0.01 1 92 . 15 VAL HG2 H 1.072 0.01 1 93 . 15 VAL CA C 66.126 0.1 1 94 . 15 VAL CB C 32.018 0.1 1 95 . 15 VAL CG1 C 23.124 0.1 1 96 . 15 VAL CG2 C 22.926 0.1 1 97 . 15 VAL N N 119.587 0.1 1 98 . 16 ILE H H 8.136 0.01 1 99 . 16 ILE HA H 3.369 0.01 1 100 . 16 ILE HB H 1.87 0.01 1 101 . 16 ILE HG12 H 1.852 0.01 2 102 . 16 ILE HG13 H 0.637 0.01 2 103 . 16 ILE HG2 H 0.713 0.01 1 104 . 16 ILE HD1 H 0.791 0.01 1 105 . 16 ILE CA C 66.614 0.1 1 106 . 16 ILE CB C 37.878 0.1 1 107 . 16 ILE CG1 C 29.912 0.1 1 108 . 16 ILE CG2 C 18.2 0.1 1 109 . 16 ILE CD1 C 15.991 0.1 1 110 . 16 ILE N N 121.602 0.1 1 111 . 17 CYS H H 8.586 0.01 1 112 . 17 CYS HA H 3.971 0.01 1 113 . 17 CYS HB2 H 3.042 0.01 2 114 . 17 CYS HB3 H 2.717 0.01 2 115 . 17 CYS CA C 64.409 0.1 1 116 . 17 CYS CB C 27.143 0.1 1 117 . 17 CYS N N 117.287 0.1 1 118 . 18 ASP H H 7.632 0.01 1 119 . 18 ASP HA H 4.592 0.01 1 120 . 18 ASP HB2 H 2.612 0.01 1 121 . 18 ASP HB3 H 2.612 0.01 1 122 . 18 ASP CA C 55.831 0.1 1 123 . 18 ASP CB C 41.618 0.1 1 124 . 18 ASP N N 116.65 0.1 1 125 . 19 ASN H H 7.419 0.01 1 126 . 19 ASN HA H 4.936 0.01 1 127 . 19 ASN HB2 H 2.594 0.01 2 128 . 19 ASN HB3 H 2.4 0.01 2 129 . 19 ASN HD21 H 8.368 0.01 2 130 . 19 ASN HD22 H 7.462 0.01 2 131 . 19 ASN CA C 55.077 0.1 1 132 . 19 ASN CB C 43.914 0.1 1 133 . 19 ASN N N 115.07 0.1 1 134 . 19 ASN ND2 N 118.584 0.1 1 135 . 20 VAL H H 8.04 0.01 1 136 . 20 VAL HA H 4.065 0.01 1 137 . 20 VAL HB H 2.052 0.01 1 138 . 20 VAL HG1 H 0.877 0.01 1 139 . 20 VAL HG2 H 1.018 0.01 1 140 . 20 VAL CA C 63.881 0.1 1 141 . 20 VAL CB C 32.539 0.1 1 142 . 20 VAL CG1 C 21.495 0.1 1 143 . 20 VAL CG2 C 23.728 0.1 1 144 . 20 VAL N N 121.456 0.1 1 145 . 21 GLY H H 8.551 0.01 1 146 . 21 GLY HA2 H 4.023 0.01 2 147 . 21 GLY HA3 H 3.753 0.01 2 148 . 21 GLY CA C 46.455 0.1 1 149 . 21 GLY N N 113.607 0.1 1 150 . 22 LYS H H 8.844 0.01 1 151 . 22 LYS HA H 4.226 0.01 1 152 . 22 LYS HB2 H 1.938 0.01 1 153 . 22 LYS HB3 H 1.938 0.01 1 154 . 22 LYS HG2 H 1.512 0.01 1 155 . 22 LYS HG3 H 1.512 0.01 1 156 . 22 LYS HD2 H 1.722 0.01 1 157 . 22 LYS HD3 H 1.722 0.01 1 158 . 22 LYS HE2 H 3.03 0.01 1 159 . 22 LYS HE3 H 3.03 0.01 1 160 . 22 LYS CA C 59.249 0.1 1 161 . 22 LYS CB C 32.513 0.1 1 162 . 22 LYS CG C 24.716 0.1 1 163 . 22 LYS CD C 29.455 0.1 1 164 . 22 LYS CE C 42.315 0.1 1 165 . 22 LYS N N 124.951 0.1 1 166 . 23 ASP H H 8.421 0.01 1 167 . 23 ASP HA H 4.919 0.01 1 168 . 23 ASP HB2 H 2.953 0.01 2 169 . 23 ASP HB3 H 2.611 0.01 2 170 . 23 ASP CA C 54.49 0.1 1 171 . 23 ASP CB C 40.29 0.1 1 172 . 23 ASP N N 119.331 0.1 1 173 . 24 TRP H H 7.968 0.01 1 174 . 24 TRP HA H 3.903 0.01 1 175 . 24 TRP HB2 H 3.373 0.01 2 176 . 24 TRP HB3 H 3.305 0.01 2 177 . 24 TRP HD1 H 7.509 0.01 1 178 . 24 TRP HE1 H 10.79 0.01 1 179 . 24 TRP HE3 H 7.214 0.01 1 180 . 24 TRP HZ2 H 7.549 0.01 1 181 . 24 TRP HZ3 H 6.827 0.01 1 182 . 24 TRP HH2 H 7.378 0.01 1 183 . 24 TRP CA C 60.439 0.1 1 184 . 24 TRP CB C 27.891 0.1 1 185 . 24 TRP CD1 C 128.1 0.5 1 186 . 24 TRP CE3 C 120.8 0.5 1 187 . 24 TRP CZ2 C 114.95 0.5 1 188 . 24 TRP CZ3 C 122.7 0.5 1 189 . 24 TRP N N 119.895 0.1 1 190 . 24 TRP NE1 N 130.2 0.1 1 191 . 25 ARG H H 7.068 0.01 1 192 . 25 ARG HA H 2.703 0.01 1 193 . 25 ARG HB2 H 1.159 0.01 2 194 . 25 ARG HB3 H 0.819 0.01 2 195 . 25 ARG HG2 H 0.387 0.01 2 196 . 25 ARG HG3 H 0.263 0.01 2 197 . 25 ARG HD2 H 2.857 0.01 1 198 . 25 ARG HD3 H 2.857 0.01 1 199 . 25 ARG HE H 7.095 0.01 1 200 . 25 ARG CA C 60.121 0.1 1 201 . 25 ARG CB C 29.626 0.1 1 202 . 25 ARG CG C 28.055 0.1 1 203 . 25 ARG CD C 43.056 0.1 1 204 . 25 ARG N N 123.086 0.1 1 205 . 26 ARG H H 7.347 0.01 1 206 . 26 ARG HA H 3.825 0.01 1 207 . 26 ARG HB2 H 1.833 0.01 2 208 . 26 ARG HB3 H 1.769 0.01 2 209 . 26 ARG HG2 H 1.665 0.01 2 210 . 26 ARG HG3 H 1.572 0.01 2 211 . 26 ARG HD2 H 3.218 0.01 1 212 . 26 ARG HD3 H 3.218 0.01 1 213 . 26 ARG CA C 59.167 0.1 1 214 . 26 ARG CB C 30.388 0.1 1 215 . 26 ARG CG C 27.674 0.1 1 216 . 26 ARG CD C 43.854 0.1 1 217 . 26 ARG N N 118.654 0.1 1 218 . 27 LEU H H 6.986 0.01 1 219 . 27 LEU HA H 4.256 0.01 1 220 . 27 LEU HB2 H 1.891 0.01 2 221 . 27 LEU HB3 H 1.262 0.01 2 222 . 27 LEU HG H 1.283 0.01 1 223 . 27 LEU HD1 H 0.635 0.01 1 224 . 27 LEU HD2 H 0.744 0.01 1 225 . 27 LEU CA C 57.467 0.1 1 226 . 27 LEU CB C 41.042 0.1 1 227 . 27 LEU CG C 27.409 0.1 1 228 . 27 LEU CD1 C 22.465 0.1 1 229 . 27 LEU CD2 C 26.594 0.1 1 230 . 27 LEU N N 119.902 0.1 1 231 . 28 ALA H H 8.151 0.01 1 232 . 28 ALA HA H 3.714 0.01 1 233 . 28 ALA HB H 1.334 0.01 1 234 . 28 ALA CA C 56.21 0.1 1 235 . 28 ALA CB C 17.372 0.1 1 236 . 28 ALA N N 121.168 0.1 1 237 . 29 ARG H H 8.021 0.01 1 238 . 29 ARG HA H 4.038 0.01 1 239 . 29 ARG HB2 H 1.709 0.01 1 240 . 29 ARG HB3 H 1.709 0.01 1 241 . 29 ARG HG2 H 1.723 0.01 2 242 . 29 ARG HG3 H 1.506 0.01 2 243 . 29 ARG HD2 H 3.082 0.01 1 244 . 29 ARG HD3 H 3.082 0.01 1 245 . 29 ARG HE H 7.502 0.01 1 246 . 29 ARG CA C 59.458 0.1 1 247 . 29 ARG CB C 30.234 0.1 1 248 . 29 ARG CG C 28.127 0.1 1 249 . 29 ARG CD C 43.36 0.1 1 250 . 29 ARG N N 115.621 0.1 1 251 . 29 ARG NE N 86.361 0.1 1 252 . 30 GLN H H 7.651 0.01 1 253 . 30 GLN HA H 3.873 0.01 1 254 . 30 GLN HB2 H 2.16 0.01 2 255 . 30 GLN HB3 H 2.055 0.01 2 256 . 30 GLN HG2 H 2.685 0.01 2 257 . 30 GLN HG3 H 2.266 0.01 2 258 . 30 GLN HE21 H 7.558 0.01 2 259 . 30 GLN HE22 H 6.918 0.01 2 260 . 30 GLN CA C 57.947 0.1 1 261 . 30 GLN CB C 28.105 0.1 1 262 . 30 GLN CG C 33.431 0.1 1 263 . 30 GLN N N 123.614 0.1 1 264 . 30 GLN NE2 N 114.109 0.1 1 265 . 31 LEU H H 7.81 0.01 1 266 . 31 LEU HA H 4.088 0.01 1 267 . 31 LEU HB2 H 1.708 0.01 1 268 . 31 LEU HB3 H 1.708 0.01 1 269 . 31 LEU HG H 1.449 0.01 1 270 . 31 LEU HD1 H 0.125 0.01 1 271 . 31 LEU HD2 H -0.371 0.01 1 272 . 31 LEU CA C 54.843 0.1 1 273 . 31 LEU CB C 40.075 0.1 1 274 . 31 LEU CG C 25.41 0.1 1 275 . 31 LEU CD1 C 25.46 0.1 1 276 . 31 LEU CD2 C 19.477 0.1 1 277 . 31 LEU N N 118.234 0.1 1 278 . 32 LYS H H 7.677 0.01 1 279 . 32 LYS HA H 3.715 0.01 1 280 . 32 LYS HB2 H 2.338 0.01 2 281 . 32 LYS HB3 H 1.971 0.01 2 282 . 32 LYS HG2 H 1.372 0.01 2 283 . 32 LYS HG3 H 1.327 0.01 2 284 . 32 LYS HD2 H 1.701 0.01 1 285 . 32 LYS HD3 H 1.701 0.01 1 286 . 32 LYS HE2 H 3.029 0.01 1 287 . 32 LYS HE3 H 3.029 0.01 1 288 . 32 LYS CA C 57.504 0.1 1 289 . 32 LYS CB C 28.335 0.1 1 290 . 32 LYS CG C 25.147 0.1 1 291 . 32 LYS CD C 29.25 0.1 1 292 . 32 LYS CE C 42.621 0.1 1 293 . 32 LYS N N 110.786 0.1 1 294 . 33 VAL H H 7.946 0.01 1 295 . 33 VAL HA H 3.833 0.01 1 296 . 33 VAL HB H 1.718 0.01 1 297 . 33 VAL HG1 H 1.049 0.01 1 298 . 33 VAL HG2 H 1.007 0.01 1 299 . 33 VAL CA C 63.643 0.1 1 300 . 33 VAL CB C 31.305 0.1 1 301 . 33 VAL CG1 C 23.031 0.1 1 302 . 33 VAL CG2 C 21.731 0.1 1 303 . 33 VAL N N 123.31 0.1 1 304 . 34 SER H H 8.448 0.01 1 305 . 34 SER HA H 4.231 0.01 1 306 . 34 SER HB2 H 4.037 0.01 1 307 . 34 SER HB3 H 4.037 0.01 1 308 . 34 SER CA C 58.411 0.1 1 309 . 34 SER CB C 64.724 0.1 1 310 . 34 SER N N 124.052 0.1 1 311 . 35 ASP H H 8.772 0.01 1 312 . 35 ASP HA H 4.273 0.01 1 313 . 35 ASP HB2 H 2.701 0.01 2 314 . 35 ASP HB3 H 2.588 0.01 2 315 . 35 ASP CA C 58.307 0.1 1 316 . 35 ASP CB C 40.21 0.1 1 317 . 35 ASP N N 122.953 0.1 1 318 . 36 THR H H 8.02 0.01 1 319 . 36 THR HA H 4.091 0.01 1 320 . 36 THR HB H 4.049 0.01 1 321 . 36 THR HG2 H 1.247 0.01 1 322 . 36 THR CA C 65.485 0.1 1 323 . 36 THR CB C 68.98 0.1 1 324 . 36 THR CG2 C 21.998 0.1 1 325 . 36 THR N N 112.408 0.1 1 326 . 37 LYS H H 7.586 0.01 1 327 . 37 LYS HA H 4.164 0.01 1 328 . 37 LYS HB2 H 2.054 0.01 2 329 . 37 LYS HB3 H 1.774 0.01 2 330 . 37 LYS HG2 H 1.467 0.01 1 331 . 37 LYS HG3 H 1.467 0.01 1 332 . 37 LYS HD2 H 1.741 0.01 1 333 . 37 LYS HD3 H 1.741 0.01 1 334 . 37 LYS HE2 H 2.968 0.01 1 335 . 37 LYS HE3 H 2.968 0.01 1 336 . 37 LYS CA C 58.663 0.1 1 337 . 37 LYS CB C 31.88 0.1 1 338 . 37 LYS CG C 25.806 0.1 1 339 . 37 LYS CD C 28.837 0.1 1 340 . 37 LYS CE C 42.101 0.1 1 341 . 37 LYS N N 124.519 0.1 1 342 . 38 ILE H H 8.719 0.01 1 343 . 38 ILE HA H 3.598 0.01 1 344 . 38 ILE HB H 1.918 0.01 1 345 . 38 ILE HG12 H 1.818 0.01 2 346 . 38 ILE HG13 H 0.475 0.01 2 347 . 38 ILE HG2 H 0.74 0.01 1 348 . 38 ILE HD1 H 0.621 0.01 1 349 . 38 ILE CA C 67.348 0.1 1 350 . 38 ILE CB C 38.003 0.1 1 351 . 38 ILE CG1 C 30.359 0.1 1 352 . 38 ILE CG2 C 18.244 0.1 1 353 . 38 ILE CD1 C 14.684 0.1 1 354 . 38 ILE N N 123.252 0.1 1 355 . 39 ASP H H 8.076 0.01 1 356 . 39 ASP HA H 4.416 0.01 1 357 . 39 ASP HB2 H 2.729 0.01 1 358 . 39 ASP HB3 H 2.729 0.01 1 359 . 39 ASP CA C 57.827 0.1 1 360 . 39 ASP CB C 39.897 0.1 1 361 . 39 ASP N N 119.918 0.1 1 362 . 40 SER H H 7.693 0.01 1 363 . 40 SER HA H 4.313 0.01 1 364 . 40 SER HB2 H 4.051 0.01 1 365 . 40 SER HB3 H 4.051 0.01 1 366 . 40 SER CA C 61.492 0.1 1 367 . 40 SER CB C 63.143 0.1 1 368 . 40 SER N N 115.827 0.1 1 369 . 41 ILE H H 8.422 0.01 1 370 . 41 ILE HA H 3.581 0.01 1 371 . 41 ILE HB H 2.36 0.01 1 372 . 41 ILE HG12 H 0.921 0.01 2 373 . 41 ILE HG13 H 2.083 0.01 2 374 . 41 ILE HG2 H 0.906 0.01 1 375 . 41 ILE HD1 H 0.9 0.01 1 376 . 41 ILE CA C 66.395 0.1 1 377 . 41 ILE CB C 38.275 0.1 1 378 . 41 ILE CG1 C 29.768 0.1 1 379 . 41 ILE CG2 C 19.713 0.1 1 380 . 41 ILE CD1 C 14.133 0.1 1 381 . 41 ILE N N 125.278 0.1 1 382 . 42 GLU H H 8.063 0.01 1 383 . 42 GLU HA H 3.554 0.01 1 384 . 42 GLU HB2 H 2.357 0.01 2 385 . 42 GLU HB3 H 2.291 0.01 2 386 . 42 GLU HG2 H 2.341 0.01 1 387 . 42 GLU HG3 H 2.341 0.01 1 388 . 42 GLU CA C 60.314 0.1 1 389 . 42 GLU CB C 29.57 0.1 1 390 . 42 GLU CG C 36.809 0.1 1 391 . 42 GLU N N 120.111 0.1 1 392 . 43 ASP H H 7.644 0.01 1 393 . 43 ASP HA H 4.276 0.01 1 394 . 43 ASP HB2 H 2.694 0.01 2 395 . 43 ASP HB3 H 2.61 0.01 2 396 . 43 ASP CA C 56.64 0.1 1 397 . 43 ASP CB C 41.77 0.1 1 398 . 43 ASP N N 116.635 0.1 1 399 . 44 ARG H H 7.722 0.01 1 400 . 44 ARG HA H 3.804 0.01 1 401 . 44 ARG HB2 H 1.57 0.01 2 402 . 44 ARG HB3 H 1.267 0.01 2 403 . 44 ARG HG2 H 1.167 0.01 2 404 . 44 ARG HG3 H 0.97 0.01 2 405 . 44 ARG HD2 H 2.944 0.01 2 406 . 44 ARG HD3 H 2.915 0.01 2 407 . 44 ARG CA C 57.827 0.1 1 408 . 44 ARG CB C 31.063 0.1 1 409 . 44 ARG CG C 27.401 0.1 1 410 . 44 ARG CD C 43.637 0.1 1 411 . 44 ARG N N 118.47 0.1 1 412 . 45 TYR H H 7.269 0.01 1 413 . 45 TYR HA H 5.187 0.01 1 414 . 45 TYR HB2 H 3.11 0.01 2 415 . 45 TYR HB3 H 2.554 0.01 2 416 . 45 TYR HD1 H 7.083 0.01 1 417 . 45 TYR HD2 H 7.083 0.01 1 418 . 45 TYR HE1 H 6.595 0.01 1 419 . 45 TYR HE2 H 6.595 0.01 1 420 . 45 TYR CA C 54.689 0.1 1 421 . 45 TYR CB C 38.843 0.1 1 422 . 45 TYR CD1 C 134.4 0.5 1 423 . 45 TYR CD2 C 134.4 0.5 1 424 . 45 TYR CE1 C 117.2 0.5 1 425 . 45 TYR CE2 C 117.2 0.5 1 426 . 45 TYR N N 115.893 0.1 1 427 . 46 PRO HA H 4.398 0.01 1 428 . 46 PRO HB2 H 2.405 0.01 2 429 . 46 PRO HB3 H 1.908 0.01 2 430 . 46 PRO HG2 H 2.04 0.01 2 431 . 46 PRO HG3 H 1.886 0.01 2 432 . 46 PRO HD2 H 3.645 0.01 2 433 . 46 PRO HD3 H 3.374 0.01 2 434 . 46 PRO CA C 65.222 0.1 1 435 . 46 PRO CB C 32.418 0.1 1 436 . 46 PRO CG C 27.525 0.1 1 437 . 46 PRO CD C 50.718 0.1 1 438 . 47 ARG H H 8.48 0.01 1 439 . 47 ARG HA H 4.505 0.01 1 440 . 47 ARG HB2 H 2.013 0.01 2 441 . 47 ARG HB3 H 1.735 0.01 2 442 . 47 ARG HG2 H 1.541 0.01 1 443 . 47 ARG HG3 H 1.541 0.01 1 444 . 47 ARG HD2 H 3.221 0.01 2 445 . 47 ARG HD3 H 3.178 0.01 2 446 . 47 ARG CA C 55.754 0.1 1 447 . 47 ARG CB C 31.56 0.1 1 448 . 47 ARG CG C 27.683 0.1 1 449 . 47 ARG CD C 42.992 0.1 1 450 . 47 ARG N N 116.16 0.1 1 451 . 48 ASN H H 7.133 0.01 1 452 . 48 ASN HA H 4.793 0.01 1 453 . 48 ASN HB2 H 2.887 0.01 2 454 . 48 ASN HB3 H 2.592 0.01 2 455 . 48 ASN HD21 H 6.961 0.01 2 456 . 48 ASN HD22 H 7.639 0.01 2 457 . 48 ASN CA C 52.724 0.1 1 458 . 48 ASN CB C 39.62 0.1 1 459 . 48 ASN N N 118.48 0.1 1 460 . 48 ASN ND2 N 113.246 0.1 1 461 . 49 LEU H H 8.485 0.01 1 462 . 49 LEU HA H 3.477 0.01 1 463 . 49 LEU HB2 H 1.652 0.01 2 464 . 49 LEU HB3 H 1.444 0.01 2 465 . 49 LEU HG H 1.522 0.01 1 466 . 49 LEU HD1 H 0.805 0.01 1 467 . 49 LEU HD2 H 0.708 0.01 1 468 . 49 LEU CA C 58.426 0.1 1 469 . 49 LEU CB C 41.784 0.1 1 470 . 49 LEU CG C 27.467 0.1 1 471 . 49 LEU CD1 C 24.703 0.1 1 472 . 49 LEU CD2 C 23.905 0.1 1 473 . 49 LEU N N 125.275 0.1 1 474 . 50 THR H H 7.889 0.01 1 475 . 50 THR HA H 3.837 0.01 1 476 . 50 THR HB H 4.078 0.01 1 477 . 50 THR HG2 H 1.209 0.01 1 478 . 50 THR CA C 66.454 0.1 1 479 . 50 THR CB C 68.698 0.1 1 480 . 50 THR CG2 C 22.062 0.1 1 481 . 50 THR N N 114.139 0.1 1 482 . 51 GLU H H 7.246 0.01 1 483 . 51 GLU HA H 3.738 0.01 1 484 . 51 GLU HB2 H 1.148 0.01 2 485 . 51 GLU HB3 H 0.833 0.01 2 486 . 51 GLU HG2 H 1.933 0.01 2 487 . 51 GLU HG3 H 1.859 0.01 2 488 . 51 GLU CA C 57.955 0.1 1 489 . 51 GLU CB C 28.727 0.1 1 490 . 51 GLU CG C 36.063 0.1 1 491 . 51 GLU N N 119.235 0.1 1 492 . 52 ARG H H 6.93 0.01 1 493 . 52 ARG HA H 3.438 0.01 1 494 . 52 ARG HB2 H 1.171 0.01 2 495 . 52 ARG HB3 H 0.258 0.01 2 496 . 52 ARG HG2 H 1.853 0.01 2 497 . 52 ARG HG3 H 1.095 0.01 2 498 . 52 ARG HD2 H 2.212 0.01 2 499 . 52 ARG HD3 H 1.931 0.01 2 500 . 52 ARG HE H 6.557 0.01 1 501 . 52 ARG CA C 58.967 0.1 1 502 . 52 ARG CB C 28.532 0.1 1 503 . 52 ARG CG C 27.215 0.1 1 504 . 52 ARG CD C 43.645 0.1 1 505 . 52 ARG N N 117.625 0.1 1 506 . 52 ARG NE N 82.665 0.1 1 507 . 53 VAL H H 7.315 0.01 1 508 . 53 VAL HA H 3.453 0.01 1 509 . 53 VAL HB H 2.236 0.01 1 510 . 53 VAL HG1 H 0.837 0.01 1 511 . 53 VAL HG2 H 1 0.01 2 512 . 53 VAL CA C 66.234 0.1 1 513 . 53 VAL CB C 31.434 0.1 1 514 . 53 VAL CG1 C 22.931 0.1 1 515 . 53 VAL CG2 C 22.834 0.1 1 516 . 53 VAL N N 120.023 0.1 1 517 . 54 ARG H H 8.165 0.01 1 518 . 54 ARG HA H 3.373 0.01 1 519 . 54 ARG HB2 H 1.907 0.01 2 520 . 54 ARG HB3 H 1.682 0.01 2 521 . 54 ARG HG2 H 1.517 0.01 1 522 . 54 ARG HG3 H 1.517 0.01 1 523 . 54 ARG HD2 H 3.227 0.01 2 524 . 54 ARG HD3 H 3.088 0.01 2 525 . 54 ARG CA C 60.431 0.1 1 526 . 54 ARG CB C 30.042 0.1 1 527 . 54 ARG CG C 27.966 0.1 1 528 . 54 ARG CD C 42.835 0.1 1 529 . 54 ARG N N 121.102 0.1 1 530 . 55 GLU H H 8.142 0.01 1 531 . 55 GLU HA H 4.335 0.01 1 532 . 55 GLU HB2 H 2.123 0.01 2 533 . 55 GLU HB3 H 1.872 0.01 2 534 . 55 GLU HG2 H 2.396 0.01 2 535 . 55 GLU HG3 H 2.327 0.01 2 536 . 55 GLU CA C 58.602 0.1 1 537 . 55 GLU CB C 28.946 0.1 1 538 . 55 GLU CG C 35.446 0.1 1 539 . 55 GLU N N 118.932 0.1 1 540 . 56 SER H H 7.81 0.01 1 541 . 56 SER HA H 4.027 0.01 1 542 . 56 SER HB2 H 4.119 0.01 2 543 . 56 SER HB3 H 3.76 0.01 2 544 . 56 SER CA C 63.162 0.1 1 545 . 56 SER CB C 63.205 0.1 1 546 . 56 SER N N 116.526 0.1 1 547 . 57 LEU H H 7.559 0.01 1 548 . 57 LEU HA H 3.832 0.01 1 549 . 57 LEU HB2 H 1.175 0.01 2 550 . 57 LEU HB3 H -0.035 0.01 2 551 . 57 LEU HG H 1.494 0.01 1 552 . 57 LEU HD1 H 0.337 0.01 1 553 . 57 LEU HD2 H 0.318 0.01 1 554 . 57 LEU CA C 57.584 0.1 1 555 . 57 LEU CB C 39.676 0.1 1 556 . 57 LEU CG C 25.727 0.1 1 557 . 57 LEU CD1 C 26.513 0.1 1 558 . 57 LEU CD2 C 22.041 0.1 1 559 . 57 LEU N N 121.436 0.1 1 560 . 58 ARG H H 8.031 0.01 1 561 . 58 ARG HA H 3.953 0.01 1 562 . 58 ARG HB2 H 1.976 0.01 1 563 . 58 ARG HB3 H 1.976 0.01 1 564 . 58 ARG HG2 H 1.79 0.01 2 565 . 58 ARG HG3 H 1.545 0.01 2 566 . 58 ARG HD2 H 3.279 0.01 2 567 . 58 ARG HD3 H 3.172 0.01 2 568 . 58 ARG CA C 60.349 0.1 1 569 . 58 ARG CB C 30.714 0.1 1 570 . 58 ARG CG C 28.221 0.1 1 571 . 58 ARG CD C 43.533 0.1 1 572 . 58 ARG N N 120.709 0.1 1 573 . 59 ILE H H 8.317 0.1 1 574 . 59 ILE HA H 3.737 0.01 1 575 . 59 ILE HB H 1.973 0.01 1 576 . 59 ILE HG12 H 1.835 0.01 2 577 . 59 ILE HG13 H 1.207 0.01 2 578 . 59 ILE HG2 H 0.998 0.01 1 579 . 59 ILE HD1 H 0.916 0.01 1 580 . 59 ILE CA C 65.33 0.1 1 581 . 59 ILE CB C 37.984 0.1 1 582 . 59 ILE CG1 C 29.218 0.1 1 583 . 59 ILE CG2 C 18.014 0.1 1 584 . 59 ILE CD1 C 14.795 0.1 1 585 . 59 ILE N N 120.826 0.1 1 586 . 60 TRP H H 8.226 0.01 1 587 . 60 TRP HA H 4.478 0.01 1 588 . 60 TRP HB2 H 3.639 0.01 2 589 . 60 TRP HB3 H 3.184 0.01 2 590 . 60 TRP HD1 H 7.677 0.01 1 591 . 60 TRP HE1 H 10.219 0.01 1 592 . 60 TRP HE3 H 7.921 0.01 1 593 . 60 TRP HZ2 H 7.243 0.01 1 594 . 60 TRP HZ3 H 7.111 0.01 1 595 . 60 TRP HH2 H 7.331 0.01 1 596 . 60 TRP CA C 61.749 0.1 1 597 . 60 TRP CB C 28.166 0.1 1 598 . 60 TRP CD1 C 129.8 0.5 1 599 . 60 TRP CZ2 C 114 0.5 1 600 . 60 TRP CZ3 C 120.9 0.5 1 601 . 60 TRP N N 124.685 0.1 1 602 . 60 TRP NE1 N 131.8 0.1 1 603 . 61 LYS HA H 3.205 0.01 1 604 . 61 LYS HB2 H 2.161 0.01 2 605 . 61 LYS HB3 H 2.114 0.01 2 606 . 61 LYS HG2 H 1.423 0.01 2 607 . 61 LYS HG3 H 1.337 0.01 2 608 . 61 LYS HD2 H 1.732 0.01 1 609 . 61 LYS HD3 H 1.732 0.01 1 610 . 61 LYS HE2 H 2.941 0.01 1 611 . 61 LYS HE3 H 2.941 0.01 1 612 . 61 LYS CA C 59.474 0.1 1 613 . 61 LYS CB C 32.807 0.1 1 614 . 61 LYS CG C 20.175 0.1 1 615 . 61 LYS CE C 42.319 0.1 1 616 . 61 LYS N N 120.967 0.1 1 617 . 62 ASN H H 8.331 0.01 1 618 . 62 ASN HA H 4.409 0.01 1 619 . 62 ASN HB2 H 2.904 0.01 2 620 . 62 ASN HB3 H 2.819 0.01 2 621 . 62 ASN HD21 H 7.59 0.01 2 622 . 62 ASN HD22 H 6.906 0.01 2 623 . 62 ASN CA C 55.37 0.1 1 624 . 62 ASN CB C 38.736 0.1 1 625 . 62 ASN N N 117.432 0.1 1 626 . 62 ASN ND2 N 112.497 0.1 1 627 . 63 THR H H 8.091 0.01 1 628 . 63 THR HA H 4.008 0.01 1 629 . 63 THR HB H 4.267 0.01 1 630 . 63 THR HG2 H 1.224 0.01 1 631 . 63 THR CA C 65.865 0.1 1 632 . 63 THR CB C 69.432 0.1 1 633 . 63 THR CG2 C 21.22 0.1 1 634 . 63 THR N N 116.3 0.1 1 635 . 64 GLU H H 8.356 0.01 1 636 . 64 GLU HA H 3.954 0.01 1 637 . 64 GLU HB2 H 1.374 0.01 2 638 . 64 GLU HB3 H 0.857 0.01 2 639 . 64 GLU HG2 H 1.876 0.01 2 640 . 64 GLU HG3 H 1.725 0.01 2 641 . 64 GLU CA C 57.041 0.1 1 642 . 64 GLU CB C 29.874 0.1 1 643 . 64 GLU CG C 35.887 0.1 1 644 . 64 GLU N N 119.545 0.1 1 645 . 65 LYS H H 7.894 0.01 1 646 . 65 LYS HA H 3.718 0.01 1 647 . 65 LYS HB2 H 1.939 0.01 2 648 . 65 LYS HB3 H 1.751 0.01 2 649 . 65 LYS HG2 H 1.285 0.01 1 650 . 65 LYS HG3 H 1.285 0.01 1 651 . 65 LYS HD2 H 1.721 0.01 2 652 . 65 LYS HD3 H 1.629 0.01 2 653 . 65 LYS HE2 H 3.028 0.01 1 654 . 65 LYS HE3 H 3.028 0.01 1 655 . 65 LYS CA C 58.611 0.1 1 656 . 65 LYS CB C 30.278 0.1 1 657 . 65 LYS CG C 25.318 0.1 1 658 . 65 LYS CD C 29.129 0.1 1 659 . 65 LYS CE C 42.849 0.1 1 660 . 65 LYS N N 118.595 0.1 1 661 . 66 GLU H H 9.323 0.01 1 662 . 66 GLU HA H 4.104 0.01 1 663 . 66 GLU HB2 H 2.053 0.01 2 664 . 66 GLU HB3 H 1.994 0.01 2 665 . 66 GLU HG2 H 2.312 0.01 2 666 . 66 GLU HG3 H 2.229 0.01 2 667 . 66 GLU CA C 59.114 0.1 1 668 . 66 GLU CB C 28.369 0.1 1 669 . 66 GLU CG C 36.146 0.1 1 670 . 66 GLU N N 125.167 0.1 1 671 . 67 ASN H H 8.115 0.01 1 672 . 67 ASN HA H 4.799 0.01 1 673 . 67 ASN HB2 H 2.902 0.01 2 674 . 67 ASN HB3 H 2.699 0.01 2 675 . 67 ASN HD21 H 7.855 0.01 2 676 . 67 ASN HD22 H 6.933 0.01 2 677 . 67 ASN CA C 53.426 0.1 1 678 . 67 ASN CB C 38.893 0.1 1 679 . 67 ASN N N 116.3 0.1 1 680 . 67 ASN ND2 N 115.443 0.1 1 681 . 68 ALA H H 7.792 0.01 1 682 . 68 ALA HA H 4.015 0.01 1 683 . 68 ALA HB H 0.613 0.01 1 684 . 68 ALA CA C 51.705 0.1 1 685 . 68 ALA CB C 16.593 0.1 1 686 . 68 ALA N N 127.75 0.1 1 687 . 69 THR H H 7.212 0.01 1 688 . 69 THR HA H 4.83 0.01 1 689 . 69 THR HB H 4.629 0.01 1 690 . 69 THR HG2 H 1.134 0.01 1 691 . 69 THR CA C 58.696 0.1 1 692 . 69 THR CB C 72.026 0.1 1 693 . 69 THR CG2 C 21.761 0.1 1 694 . 69 THR N N 112.596 0.1 1 695 . 70 VAL H H 9.107 0.01 1 696 . 70 VAL HA H 3.484 0.01 1 697 . 70 VAL HB H 1.993 0.01 1 698 . 70 VAL HG1 H 0.798 0.01 1 699 . 70 VAL HG2 H 0.934 0.01 1 700 . 70 VAL CA C 67.913 0.1 1 701 . 70 VAL CB C 31.316 0.1 1 702 . 70 VAL CG1 C 21.831 0.1 1 703 . 70 VAL CG2 C 24.099 0.1 1 704 . 70 VAL N N 123.435 0.1 1 705 . 71 ALA H H 8.623 0.01 1 706 . 71 ALA HA H 4.046 0.01 1 707 . 71 ALA HB H 1.322 0.01 1 708 . 71 ALA CA C 55.698 0.1 1 709 . 71 ALA CB C 18.109 0.1 1 710 . 71 ALA N N 121.191 0.1 1 711 . 72 HIS H H 8.03 0.01 1 712 . 72 HIS HA H 4.587 0.01 1 713 . 72 HIS HB2 H 3.592 0.01 2 714 . 72 HIS HB3 H 3.525 0.01 2 715 . 72 HIS HD2 H 7.251 0.01 2 716 . 72 HIS HE1 H 8.28 0.1 1 717 . 72 HIS CA C 58.573 0.1 1 718 . 72 HIS CB C 30.017 0.1 1 719 . 72 HIS CD2 C 124.6 0.5 1 720 . 72 HIS CE1 C 138 0.5 1 721 . 72 HIS N N 117.683 0.1 1 722 . 73 LEU H H 8.288 0.01 1 723 . 73 LEU HA H 3.728 0.01 1 724 . 73 LEU HB2 H 1.937 0.01 2 725 . 73 LEU HB3 H 1.75 0.01 2 726 . 73 LEU HG H 1.464 0.01 1 727 . 73 LEU HD1 H 0.42 0.01 1 728 . 73 LEU HD2 H 0.464 0.01 1 729 . 73 LEU CA C 57.991 0.1 1 730 . 73 LEU CB C 42.388 0.1 1 731 . 73 LEU CG C 26.51 0.1 1 732 . 73 LEU CD1 C 23.07 0.1 1 733 . 73 LEU CD2 C 24.885 0.1 1 734 . 73 LEU N N 124.888 0.1 1 735 . 74 VAL H H 8.783 0.01 1 736 . 74 VAL HA H 3.389 0.01 1 737 . 74 VAL HB H 2.147 0.01 1 738 . 74 VAL HG1 H 0.905 0.01 1 739 . 74 VAL HG2 H 1.008 0.01 1 740 . 74 VAL CA C 67.787 0.1 1 741 . 74 VAL CB C 31.986 0.1 1 742 . 74 VAL CG1 C 21.615 0.1 1 743 . 74 VAL CG2 C 23.823 0.1 1 744 . 74 VAL N N 119.76 0.1 1 745 . 75 GLY H H 7.935 0.01 1 746 . 75 GLY HA2 H 3.918 0.01 2 747 . 75 GLY HA3 H 3.767 0.01 2 748 . 75 GLY CA C 47.407 0.1 1 749 . 75 GLY N N 105.664 0.1 1 750 . 76 ALA H H 7.97 0.01 1 751 . 76 ALA HA H 4.064 0.01 1 752 . 76 ALA HB H 1.236 0.01 1 753 . 76 ALA CA C 55.347 0.1 1 754 . 76 ALA CB C 18.427 0.1 1 755 . 76 ALA N N 126.201 0.1 1 756 . 77 LEU H H 8.113 0.01 1 757 . 77 LEU HA H 3.766 0.01 1 758 . 77 LEU HB2 H 2.01 0.01 2 759 . 77 LEU HB3 H 1.372 0.01 2 760 . 77 LEU HG H 1.634 0.01 1 761 . 77 LEU HD1 H 0.653 0.01 1 762 . 77 LEU HD2 H 0.791 0.01 1 763 . 77 LEU CA C 58.234 0.1 1 764 . 77 LEU CB C 42.485 0.1 1 765 . 77 LEU CG C 27.039 0.1 1 766 . 77 LEU CD1 C 26.306 0.1 1 767 . 77 LEU CD2 C 24.938 0.1 1 768 . 77 LEU N N 118.885 0.1 1 769 . 78 ARG H H 8.38 0.01 1 770 . 78 ARG HA H 3.685 0.01 1 771 . 78 ARG HB2 H 1.841 0.01 2 772 . 78 ARG HB3 H 1.417 0.01 2 773 . 78 ARG HG2 H 1.882 0.01 2 774 . 78 ARG HG3 H 1.71 0.01 2 775 . 78 ARG HD2 H 3.155 0.01 2 776 . 78 ARG HD3 H 3.026 0.01 2 777 . 78 ARG HE H 7.161 0.01 1 778 . 78 ARG CA C 60.801 0.1 1 779 . 78 ARG CB C 29.242 0.1 1 780 . 78 ARG CG C 28.656 0.1 1 781 . 78 ARG CD C 42.83 0.1 1 782 . 78 ARG N N 118.108 0.1 1 783 . 78 ARG NE N 85.624 0.1 1 784 . 79 SER H H 8.31 0.01 1 785 . 79 SER HA H 4.251 0.01 1 786 . 79 SER HB2 H 3.981 0.01 2 787 . 79 SER HB3 H 3.847 0.01 2 788 . 79 SER CA C 62.293 0.1 1 789 . 79 SER CB C 63.47 0.1 1 790 . 79 SER N N 117.883 0.1 1 791 . 80 CYS H H 7.368 0.01 1 792 . 80 CYS HA H 4.799 0.01 1 793 . 80 CYS HB2 H 2.904 0.01 2 794 . 80 CYS HB3 H 2.803 0.01 2 795 . 80 CYS CA C 57.574 0.1 1 796 . 80 CYS CB C 27.335 0.1 1 797 . 80 CYS N N 115.261 0.1 1 798 . 81 GLN H H 7.832 0.01 1 799 . 81 GLN HA H 3.748 0.01 1 800 . 81 GLN HB2 H 2.36 0.01 1 801 . 81 GLN HB3 H 2.36 0.01 1 802 . 81 GLN HG2 H 2.284 0.01 1 803 . 81 GLN HG3 H 2.284 0.01 1 804 . 81 GLN HE21 H 7.485 0.01 2 805 . 81 GLN CA C 57.911 0.1 1 806 . 81 GLN CB C 25.207 0.1 1 807 . 81 GLN CG C 34.547 0.1 1 808 . 81 GLN N N 113.24 0.1 1 809 . 81 GLN NE2 N 113.233 0.1 1 810 . 82 MET H H 8.347 0.01 1 811 . 82 MET HA H 4.839 0.01 1 812 . 82 MET HB2 H 1.873 0.01 2 813 . 82 MET HB3 H 1.809 0.01 2 814 . 82 MET HG2 H 2.522 0.01 1 815 . 82 MET HG3 H 2.522 0.01 1 816 . 82 MET HE H 1.997 0.01 1 817 . 82 MET CA C 54.859 0.1 1 818 . 82 MET CB C 30.261 0.1 1 819 . 82 MET CG C 33.495 0.1 1 820 . 82 MET CE C 18.788 0.1 1 821 . 82 MET N N 122.313 0.1 1 822 . 83 ASN H H 7.452 0.01 1 823 . 83 ASN HA H 4.015 0.01 1 824 . 83 ASN HB2 H 2.768 0.01 2 825 . 83 ASN HB3 H 2.623 0.01 2 826 . 83 ASN HD21 H 7.744 0.01 2 827 . 83 ASN HD22 H 7.094 0.01 2 828 . 83 ASN CA C 57.608 0.1 1 829 . 83 ASN CB C 38.857 0.1 1 830 . 83 ASN N N 117.828 0.1 1 831 . 83 ASN ND2 N 114.322 0.1 1 832 . 84 LEU H H 8.289 0.01 1 833 . 84 LEU HA H 4.175 0.01 1 834 . 84 LEU HB2 H 1.733 0.01 2 835 . 84 LEU HB3 H 1.655 0.01 2 836 . 84 LEU HG H 1.602 0.01 1 837 . 84 LEU HD1 H 0.921 0.01 1 838 . 84 LEU HD2 H 0.859 0.01 1 839 . 84 LEU CA C 58.55 0.1 1 840 . 84 LEU CB C 41.165 0.1 1 841 . 84 LEU CG C 27.552 0.1 1 842 . 84 LEU CD1 C 24.748 0.1 1 843 . 84 LEU CD2 C 24.23 0.1 1 844 . 84 LEU N N 120.803 0.1 1 845 . 85 VAL H H 7.314 0.01 1 846 . 85 VAL HA H 3.414 0.01 1 847 . 85 VAL HB H 1.953 0.01 1 848 . 85 VAL HG1 H 0.836 0.01 1 849 . 85 VAL HG2 H 0.904 0.01 1 850 . 85 VAL CA C 66.287 0.1 1 851 . 85 VAL CB C 31.688 0.1 1 852 . 85 VAL CG1 C 23.85 0.1 1 853 . 85 VAL CG2 C 23.593 0.1 1 854 . 85 VAL N N 117.737 0.1 1 855 . 86 ALA H H 8 0.01 1 856 . 86 ALA HA H 3.776 0.01 1 857 . 86 ALA HB H 1.436 0.01 1 858 . 86 ALA CA C 55.975 0.1 1 859 . 86 ALA CB C 18.388 0.1 1 860 . 86 ALA N N 121.824 0.1 1 861 . 87 ASP H H 8.219 0.01 1 862 . 87 ASP HA H 4.229 0.01 1 863 . 87 ASP HB2 H 2.909 0.01 2 864 . 87 ASP HB3 H 2.619 0.01 2 865 . 87 ASP CA C 57.646 0.1 1 866 . 87 ASP CB C 39.64 0.1 1 867 . 87 ASP N N 118.221 0.1 1 868 . 88 LEU H H 7.771 0.01 1 869 . 88 LEU HA H 4.104 0.01 1 870 . 88 LEU HB2 H 1.894 0.01 2 871 . 88 LEU HB3 H 1.399 0.01 2 872 . 88 LEU HG H 1.847 0.01 1 873 . 88 LEU HD1 H 0.754 0.01 1 874 . 88 LEU HD2 H 0.811 0.01 1 875 . 88 LEU CA C 58.075 0.1 1 876 . 88 LEU CB C 42.443 0.1 1 877 . 88 LEU CG C 27.571 0.1 1 878 . 88 LEU CD1 C 25.471 0.1 1 879 . 88 LEU CD2 C 22.702 0.1 1 880 . 88 LEU N N 121.683 0.1 1 881 . 89 VAL H H 8.386 0.01 1 882 . 89 VAL HA H 3.461 0.01 1 883 . 89 VAL HB H 2.135 0.01 1 884 . 89 VAL HG1 H 0.789 0.01 1 885 . 89 VAL HG2 H 0.922 0.01 1 886 . 89 VAL CA C 66.759 0.1 1 887 . 89 VAL CB C 31.446 0.1 1 888 . 89 VAL CG1 C 23.153 0.1 1 889 . 89 VAL CG2 C 24.01 0.1 1 890 . 89 VAL N N 121.001 0.1 1 891 . 90 GLN H H 8.415 0.01 1 892 . 90 GLN HA H 3.958 0.01 1 893 . 90 GLN HB2 H 2.202 0.01 2 894 . 90 GLN HB3 H 2.107 0.01 2 895 . 90 GLN HG2 H 2.414 0.01 2 896 . 90 GLN HG3 H 2.31 0.01 2 897 . 90 GLN HE21 H 7.478 0.01 2 898 . 90 GLN HE22 H 6.799 0.01 2 899 . 90 GLN CA C 59.322 0.1 1 900 . 90 GLN CB C 28.931 0.1 1 901 . 90 GLN CG C 34.872 0.1 1 902 . 90 GLN N N 119.168 0.1 1 903 . 90 GLN NE2 N 112.025 0.1 1 904 . 91 GLU H H 8.03 0.01 1 905 . 91 GLU HA H 4.028 0.01 1 906 . 91 GLU HB2 H 2.133 0.01 1 907 . 91 GLU HB3 H 2.133 0.01 1 908 . 91 GLU HG2 H 2.405 0.01 2 909 . 91 GLU HG3 H 2.235 0.01 2 910 . 91 GLU CA C 59.439 0.1 1 911 . 91 GLU CB C 29.769 0.1 1 912 . 91 GLU CG C 36.412 0.1 1 913 . 91 GLU N N 120.131 0.1 1 914 . 92 VAL H H 7.855 0.01 1 915 . 92 VAL HA H 3.823 0.01 1 916 . 92 VAL HB H 2.271 0.01 1 917 . 92 VAL HG1 H 0.906 0.01 2 918 . 92 VAL HG2 H 1.022 0.01 2 919 . 92 VAL CA C 65.819 0.1 1 920 . 92 VAL CB C 31.715 0.1 1 921 . 92 VAL CG1 C 21.365 0.1 2 922 . 92 VAL CG2 C 22.856 0.1 2 923 . 92 VAL N N 120.634 0.1 1 924 . 93 GLN H H 7.99 0.01 1 925 . 93 GLN HA H 3.961 0.01 1 926 . 93 GLN HB2 H 2.107 0.01 1 927 . 93 GLN HB3 H 2.107 0.01 1 928 . 93 GLN HG2 H 2.321 0.01 1 929 . 93 GLN HG3 H 2.321 0.01 1 930 . 93 GLN HE21 H 7.46 0.01 2 931 . 93 GLN HE22 H 6.665 0.01 2 932 . 93 GLN CA C 58.055 0.1 1 933 . 93 GLN CB C 28.427 0.1 1 934 . 93 GLN CG C 33.575 0.1 1 935 . 93 GLN N N 120.678 0.1 1 936 . 93 GLN NE2 N 112.565 0.1 1 937 . 94 GLN H H 8.326 0.01 1 938 . 94 GLN HA H 4.146 0.01 1 939 . 94 GLN HB2 H 2.106 0.01 1 940 . 94 GLN HB3 H 2.106 0.01 1 941 . 94 GLN HG2 H 2.476 0.01 2 942 . 94 GLN HG3 H 2.404 0.01 2 943 . 94 GLN CA C 58.187 0.1 1 944 . 94 GLN CB C 28.906 0.1 1 945 . 94 GLN CG C 34.342 0.1 1 946 . 94 GLN N N 119.115 0.1 1 947 . 95 ALA H H 7.843 0.01 1 948 . 95 ALA HA H 4.167 0.01 1 949 . 95 ALA HB H 1.462 0.01 1 950 . 95 ALA CA C 54.501 0.1 1 951 . 95 ALA CB C 18.302 0.1 1 952 . 95 ALA N N 122.579 0.1 1 953 . 96 ARG H H 8.02 0.01 1 954 . 96 ARG HA H 4.035 0.01 1 955 . 96 ARG HB2 H 1.906 0.01 2 956 . 96 ARG HB3 H 1.804 0.01 2 957 . 96 ARG HG2 H 1.733 0.01 2 958 . 96 ARG HG3 H 1.595 0.01 2 959 . 96 ARG HD2 H 3.168 0.01 2 960 . 96 ARG HD3 H 3.098 0.01 2 961 . 96 ARG HE H 7.672 0.01 1 962 . 96 ARG CA C 58.428 0.1 1 963 . 96 ARG CB C 30.128 0.1 1 964 . 96 ARG CG C 27.528 0.1 1 965 . 96 ARG N N 120.222 0.1 1 966 . 96 ARG NE N 83.642 0.1 1 967 . 97 ASP H H 8.375 0.01 1 968 . 97 ASP HA H 4.47 0.01 1 969 . 97 ASP HB2 H 2.694 0.01 1 970 . 97 ASP HB3 H 2.694 0.01 1 971 . 97 ASP CA C 56.29 0.1 1 972 . 97 ASP CB C 40.784 0.1 1 973 . 97 ASP N N 120.87 0.1 1 974 . 98 LEU H H 7.852 0.01 1 975 . 98 LEU HA H 4.156 0.01 1 976 . 98 LEU HB2 H 1.731 0.01 2 977 . 98 LEU HB3 H 1.613 0.01 2 978 . 98 LEU HG H 1.683 0.01 1 979 . 98 LEU HD1 H 0.888 0.01 1 980 . 98 LEU HD2 H 0.841 0.01 1 981 . 98 LEU CA C 56.762 0.1 1 982 . 98 LEU CB C 42.169 0.1 1 983 . 98 LEU CG C 27.026 0.1 1 984 . 98 LEU CD1 C 24.898 0.1 1 985 . 98 LEU CD2 C 23.598 0.1 1 986 . 98 LEU N N 120.884 0.1 1 987 . 99 GLN H H 7.906 0.01 1 988 . 99 GLN HA H 4.156 0.01 1 989 . 99 GLN HB2 H 2.098 0.01 1 990 . 99 GLN HB3 H 2.098 0.01 1 991 . 99 GLN HG2 H 2.393 0.01 1 992 . 99 GLN HG3 H 2.393 0.01 1 993 . 99 GLN CA C 57.148 0.1 1 994 . 99 GLN CB C 28.919 0.1 1 995 . 99 GLN CG C 34.024 0.1 1 996 . 99 GLN N N 119.075 0.1 1 997 . 100 ASN H H 8.184 0.01 1 998 . 100 ASN HA H 4.665 0.01 1 999 . 100 ASN HB2 H 2.864 0.01 2 1000 . 100 ASN HB3 H 2.785 0.01 2 1001 . 100 ASN HD21 H 6.91 0.01 2 1002 . 100 ASN HD22 H 7.71 0.01 2 1003 . 100 ASN CA C 53.911 0.1 1 1004 . 100 ASN CB C 38.894 0.1 1 1005 . 100 ASN N N 118.47 0.1 1 1006 . 100 ASN ND2 N 113.523 0.1 1 1007 . 101 ARG H H 8.041 0.01 1 1008 . 101 ARG HA H 4.351 0.01 1 1009 . 101 ARG HB2 H 1.906 0.01 2 1010 . 101 ARG HB3 H 1.791 0.01 2 1011 . 101 ARG HG2 H 1.639 0.01 1 1012 . 101 ARG HG3 H 1.639 0.01 1 1013 . 101 ARG HD2 H 3.163 0.01 1 1014 . 101 ARG HD3 H 3.163 0.01 1 1015 . 101 ARG CA C 56.548 0.1 1 1016 . 101 ARG CB C 30.764 0.1 1 1017 . 101 ARG CG C 27.262 0.1 1 1018 . 101 ARG CD C 43.568 0.1 1 1019 . 101 ARG N N 121.224 0.1 1 1020 . 102 SER H H 8.248 0.01 1 1021 . 102 SER HA H 4.426 0.01 1 1022 . 102 SER HB2 H 3.881 0.01 1 1023 . 102 SER HB3 H 3.881 0.01 1 1024 . 102 SER CA C 58.899 0.1 1 1025 . 102 SER CB C 63.947 0.1 1 1026 . 102 SER N N 116.881 0.1 1 1027 . 103 GLY H H 8.321 0.01 1 1028 . 103 GLY HA2 H 3.918 0.01 1 1029 . 103 GLY HA3 H 3.918 0.01 1 1030 . 103 GLY CA C 45.444 0.1 1 1031 . 103 GLY N N 111.883 0.1 1 1032 . 104 ALA H H 7.789 0.01 1 1033 . 104 ALA HA H 4.109 0.01 1 1034 . 104 ALA HB H 1.289 0.01 1 1035 . 104 ALA CA C 53.841 0.1 1 1036 . 104 ALA CB C 20.228 0.1 1 1037 . 104 ALA N N 129.703 0.1 1 stop_ save_