data_10011 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SOLUTION STRUCTURE OF THE SWIRM DOMAIN OF HUMAN LSD1 ; _BMRB_accession_number 10011 _BMRB_flat_file_name bmr10011.str _Entry_type original _Submission_date 2005-11-07 _Accession_date 2005-11-07 _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 Tochio N. . . 2 Umehara T. . . 3 Koshiba S. . . 4 Inoue M. . . 5 TANAKA A. . . 6 Kigawa T. . . 7 Yokoyama S. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 702 "13C chemical shifts" 525 "15N chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2006-11-14 original author . stop_ _Original_release_date 2006-11-14 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution structure of the SWIRM domain of human histone demethylase LSD1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 16531230 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tochio N. . . 2 Umehara T. . . 3 Koshiba S. . . 4 Inoue M. . . 5 Yabuki T. . . 6 Aoki M. . . 7 Seki E. . . 8 Watanabe S. . . 9 Tomo Y. . . 10 Hanada M. . . 11 Ikari M. . . 12 Sato M. . . 13 Terada T. . . 14 Nagase T. . . 15 Ohara O. . . 16 Shirouzu M. . . 17 Tanaka A. . . 18 Kigawa T. . . 19 Yokoyama S. . . stop_ _Journal_abbreviation Structure _Journal_volume 14 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 457 _Page_last 468 _Year 2006 _Details . loop_ _Keyword AOF2 'HISTONE MODULATION' KIAA0601 LSD1 'NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES' NPPSFA 'RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE' RSGI 'structural genomics' 'SWIRM DOMAIN' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'the SWIRM domain of human LSD1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SWIRM domain' $SWIRM_domain stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state 'protein monomer' _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SWIRM_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'SWIRM domain' _Molecular_mass 13710.63 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 124 _Mol_residue_sequence ; GSSGSSGEEPSGVEGAAFQS RLPHDRMTSQEAACFPDIIS GPQQTQKVFLFIRNRTLQLW LDNPKIQLTFEATLQQLEAP YNSDTVLVHRVHSYLERHGL INFGIYKRIKPLPTKKTGSG PSSG ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 SER 4 GLY 5 SER 6 SER 7 GLY 8 GLU 9 GLU 10 PRO 11 SER 12 GLY 13 VAL 14 GLU 15 GLY 16 ALA 17 ALA 18 PHE 19 GLN 20 SER 21 ARG 22 LEU 23 PRO 24 HIS 25 ASP 26 ARG 27 MET 28 THR 29 SER 30 GLN 31 GLU 32 ALA 33 ALA 34 CYS 35 PHE 36 PRO 37 ASP 38 ILE 39 ILE 40 SER 41 GLY 42 PRO 43 GLN 44 GLN 45 THR 46 GLN 47 LYS 48 VAL 49 PHE 50 LEU 51 PHE 52 ILE 53 ARG 54 ASN 55 ARG 56 THR 57 LEU 58 GLN 59 LEU 60 TRP 61 LEU 62 ASP 63 ASN 64 PRO 65 LYS 66 ILE 67 GLN 68 LEU 69 THR 70 PHE 71 GLU 72 ALA 73 THR 74 LEU 75 GLN 76 GLN 77 LEU 78 GLU 79 ALA 80 PRO 81 TYR 82 ASN 83 SER 84 ASP 85 THR 86 VAL 87 LEU 88 VAL 89 HIS 90 ARG 91 VAL 92 HIS 93 SER 94 TYR 95 LEU 96 GLU 97 ARG 98 HIS 99 GLY 100 LEU 101 ILE 102 ASN 103 PHE 104 GLY 105 ILE 106 TYR 107 LYS 108 ARG 109 ILE 110 LYS 111 PRO 112 LEU 113 PRO 114 THR 115 LYS 116 LYS 117 THR 118 GLY 119 SER 120 GLY 121 PRO 122 SER 123 SER 124 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-03-17 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 17171 SWIRM 81.45 102 99.01 99.01 8.31e-68 PDB 2COM "The Solution Structure Of The Swirm Domain Of Human Lsd1" 100.00 124 100.00 100.00 1.72e-85 PDB 2DW4 "Crystal Structure Of Human Lsd1 At 2.3 A Resolution" 87.10 660 100.00 100.00 1.12e-68 PDB 2EJR "Lsd1-Tranylcypromine Complex" 87.10 662 100.00 100.00 1.12e-68 PDB 2H94 "Crystal Structure And Mechanism Of Human Lysine-Specific Demethylase-1" 87.10 664 100.00 100.00 1.11e-68 PDB 2HKO "Crystal Structure Of Lsd1" 87.10 664 100.00 100.00 1.10e-68 PDB 2IW5 "Structural Basis For Corest-dependent Demethylation Of Nucleosomes By The Human Lsd1 Histone Demethylase" 87.90 666 100.00 100.00 1.11e-69 PDB 2L3D "The Solution Structure Of The Short Form Swirm Domain Of Lsd1" 81.45 102 99.01 99.01 8.31e-68 PDB 2UXN "Structural Basis Of Histone Demethylation By Lsd1 Revealed By Suicide Inactivation" 87.90 666 100.00 100.00 1.11e-69 PDB 2UXX "Human Lsd1 Histone Demethylase-corest In Complex With An Fad-tranylcypromine Adduct" 87.90 666 100.00 100.00 1.11e-69 PDB 2V1D "Structural Basis Of Lsd1-Corest Selectivity In Histone H3 Recognition" 91.94 730 98.25 98.25 8.46e-71 PDB 2X0L "Crystal Structure Of A Neuro-Specific Splicing Variant Of Human Histone Lysine Demethylase Lsd1" 91.94 734 98.25 98.25 9.42e-71 PDB 2XAF "Crystal Structure Of Lsd1-Corest In Complex With Para-Bromo- (+)-Cis-2-Phenylcyclopropyl-1-Amine" 91.94 852 98.25 98.25 1.70e-70 PDB 2XAG "Crystal Structure Of Lsd1-Corest In Complex With Para-Bromo- (-)-Trans-2-Phenylcyclopropyl-1-Amine" 91.94 852 98.25 98.25 1.70e-70 PDB 2XAH "Crystal Structure Of Lsd1-Corest In Complex With (+)- Trans-2-Phenylcyclopropyl-1-Amine" 91.94 852 98.25 98.25 1.70e-70 PDB 2XAJ "Crystal Structure Of Lsd1-Corest In Complex With (-)-Trans- 2-Phenylcyclopropyl-1-Amine" 91.94 852 98.25 98.25 1.70e-70 PDB 2XAQ "Crystal Structure Of Lsd1-Corest In Complex With A Tranylcypromine Derivative (Mc2584, 13b)" 91.94 852 98.25 98.25 1.70e-70 PDB 2XAS "Crystal Structure Of Lsd1-Corest In Complex With A Tranylcypromine Derivative (Mc2580, 14e)" 91.94 852 98.25 98.25 1.70e-70 PDB 2Y48 "Crystal Structure Of Lsd1-Corest In Complex With A N- Terminal Snail Peptide" 91.94 730 98.25 98.25 8.46e-71 PDB 2Z3Y "Crystal Structure Of Lysine-Specific Demethylase1" 87.10 662 100.00 100.00 1.12e-68 PDB 2Z5U "Crystal Structure Of Lysine-specific Histone Demethylase 1" 87.10 662 100.00 100.00 1.12e-68 PDB 3ABT "Crystal Structure Of Lsd1 In Complex With Trans-2- Pentafluorophenylcyclopropylamine" 87.10 662 100.00 100.00 1.12e-68 PDB 3ABU "Crystal Structure Of Lsd1 In Complex With A 2-Pcpa Derivative, S1201" 87.10 662 100.00 100.00 1.12e-68 PDB 4BAY "Phosphomimetic Mutant Of Lsd1-8a Splicing Variant In Complex With Corest" 87.90 686 100.00 100.00 1.93e-69 PDB 4KUM "Structure Of Lsd1-corest-tetrahydrofolate Complex" 87.90 666 100.00 100.00 1.11e-69 PDB 4UXN "Lsd1(kdm1a)-corest In Complex With Z-pro Derivative Of Mc2580" 91.94 852 98.25 98.25 1.70e-70 DBJ BAA25527 "KIAA0601 protein [Homo sapiens]" 91.94 886 98.25 98.25 2.85e-70 DBJ BAC97980 "mKIAA0601 protein [Mus musculus]" 91.94 879 97.37 97.37 1.14e-69 DBJ BAF83017 "unnamed protein product [Homo sapiens]" 91.94 730 98.25 98.25 1.11e-70 DBJ BAG09773 "amine oxidase (flavin containing) domain 2 [synthetic construct]" 91.94 852 98.25 98.25 1.70e-70 EMBL CAH90077 "hypothetical protein [Pongo abelii]" 91.94 688 98.25 98.25 6.96e-71 GB AAH16639 "AOF2 protein, partial [Homo sapiens]" 60.48 648 100.00 100.00 2.74e-43 GB AAH48134 "Amine oxidase (flavin containing) domain 2 [Homo sapiens]" 91.94 852 98.25 98.25 1.77e-70 GB AAI51757 "AOF2 protein [Bos taurus]" 91.94 363 98.25 98.25 4.78e-76 GB ABX10191 "amine oxidase (flavin containing) domain 2 isoform b [Sus scrofa]" 91.94 853 97.37 98.25 5.41e-70 GB AIC62107 "KDM1A, partial [synthetic construct]" 91.94 730 98.25 98.25 8.46e-71 REF NP_055828 "lysine-specific histone demethylase 1A isoform b [Homo sapiens]" 91.94 852 98.25 98.25 1.70e-70 REF NP_598633 "lysine-specific histone demethylase 1A [Mus musculus]" 91.94 853 97.37 97.37 8.43e-70 REF XP_002685763 "PREDICTED: lysine-specific histone demethylase 1A isoform X2 [Bos taurus]" 91.94 853 98.25 98.25 1.79e-70 REF XP_003271633 "PREDICTED: lysine-specific histone demethylase 1A [Nomascus leucogenys]" 91.94 730 98.25 98.25 8.73e-71 REF XP_003415419 "PREDICTED: lysine-specific histone demethylase 1A isoform X3 [Loxodonta africana]" 86.29 855 97.20 97.20 8.31e-65 SP O60341 "RecName: Full=Lysine-specific histone demethylase 1A; AltName: Full=BRAF35-HDAC complex protein BHC110; AltName: Full=Flavin-co" 91.94 852 98.25 98.25 1.70e-70 SP Q6ZQ88 "RecName: Full=Lysine-specific histone demethylase 1A; AltName: Full=BRAF35-HDAC complex protein BHC110; AltName: Full=Flavin-co" 91.94 853 97.37 97.37 8.43e-70 TPG DAA32188 "TPA: lysine (K)-specific demethylase 1A isoform 2 [Bos taurus]" 91.94 853 98.25 98.25 1.79e-70 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction $SWIRM_domain human 9606 Eukaryota Metazoa Homo sapiens no stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $SWIRM_domain 'cell free synthesis' . . . . plasmid P040401-21 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 $SWIRM_domain 1.2 mM '[U-13C, U-15N]' D-Tris 20 mM . NaCl 100 mM . d-DTT 1 mM . NaN3 0.02 % . D2O 10 % . H2O 90 % . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRPipe _Version 20031121 loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ save_software_3 _Saveframe_category software _Name NMRView _Version 5.0.4 loop_ _Task 'data analysis' stop_ _Details 'Johnson, B.A.' save_ save_software_4 _Saveframe_category software _Name Kujira _Version 0.8994 loop_ _Task 'data analysis' stop_ _Details 'Kobayashi, N.' save_ save_software_5 _Saveframe_category software _Name CYANA _Version 2.0.17 loop_ _Task refinement 'structure solution' stop_ _Details 'Guntert, P.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_13C-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_13C-separated_NOESY _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 3D_15N-separated_NOESY _Sample_label $sample_1 save_ save_3D_13C-separated_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D_15N-separated_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.12 0.001 M pH 7.0 0.05 pH pressure 1 0.03 atm temperature 296 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_reference_1 _Saveframe_category chemical_shift_reference _Details ; Chemical shift reference of 1H was based on the proton of water (4.784 ppm at 296 K) and then those of 15N and 13C were calculated based on their gyromagnetic ratios. ; 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_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label 3D_13C-separated_NOESY 3D_15N-separated_NOESY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $reference_1 _Mol_system_component_name 'SWIRM 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 4 4 GLY HA2 H 4.029 0.030 1 2 4 4 GLY HA3 H 4.029 0.030 1 3 4 4 GLY C C 174.317 0.300 1 4 4 4 GLY CA C 45.334 0.300 1 5 5 5 SER H H 8.271 0.030 1 6 5 5 SER HA H 4.514 0.030 1 7 5 5 SER HB2 H 3.889 0.030 1 8 5 5 SER HB3 H 3.889 0.030 1 9 5 5 SER C C 174.852 0.300 1 10 5 5 SER CA C 58.280 0.300 1 11 5 5 SER CB C 64.094 0.300 1 12 5 5 SER N N 115.800 0.300 1 13 6 6 SER H H 8.526 0.030 1 14 6 6 SER HA H 4.496 0.030 1 15 6 6 SER HB2 H 3.889 0.030 1 16 6 6 SER HB3 H 3.889 0.030 1 17 6 6 SER C C 175.045 0.300 1 18 6 6 SER CA C 58.647 0.300 1 19 6 6 SER CB C 64.041 0.300 1 20 6 6 SER N N 118.100 0.300 1 21 7 7 GLY H H 8.410 0.030 1 22 7 7 GLY HA2 H 3.994 0.030 1 23 7 7 GLY HA3 H 3.994 0.030 1 24 7 7 GLY C C 173.944 0.300 1 25 7 7 GLY CA C 45.291 0.300 1 26 7 7 GLY N N 110.810 0.300 1 27 8 8 GLU H H 8.212 0.030 1 28 8 8 GLU HA H 4.294 0.030 1 29 8 8 GLU HB2 H 2.016 0.030 2 30 8 8 GLU HB3 H 1.859 0.030 2 31 8 8 GLU HG2 H 2.208 0.030 1 32 8 8 GLU HG3 H 2.208 0.030 1 33 8 8 GLU C C 176.298 0.300 1 34 8 8 GLU CA C 56.123 0.300 1 35 8 8 GLU CB C 30.564 0.300 1 36 8 8 GLU CG C 36.284 0.300 1 37 8 8 GLU N N 120.287 0.300 1 38 9 9 GLU H H 8.467 0.030 1 39 9 9 GLU HA H 4.502 0.030 1 40 9 9 GLU HB2 H 1.984 0.030 2 41 9 9 GLU HB3 H 1.857 0.030 2 42 9 9 GLU HG2 H 2.257 0.030 1 43 9 9 GLU HG3 H 2.257 0.030 1 44 9 9 GLU C C 174.652 0.300 1 45 9 9 GLU CA C 54.376 0.300 1 46 9 9 GLU CB C 29.630 0.300 1 47 9 9 GLU CG C 35.944 0.300 1 48 9 9 GLU N N 123.546 0.300 1 49 10 10 PRO HA H 4.423 0.030 1 50 10 10 PRO HB2 H 2.242 0.030 2 51 10 10 PRO HB3 H 1.866 0.030 2 52 10 10 PRO HG2 H 1.939 0.030 1 53 10 10 PRO HG3 H 1.939 0.030 1 54 10 10 PRO HD2 H 3.762 0.030 2 55 10 10 PRO HD3 H 3.591 0.030 2 56 10 10 PRO C C 176.835 0.300 1 57 10 10 PRO CA C 63.189 0.300 1 58 10 10 PRO CB C 32.011 0.300 1 59 10 10 PRO CG C 27.290 0.300 1 60 10 10 PRO CD C 50.620 0.300 1 61 11 11 SER H H 8.518 0.030 1 62 11 11 SER HA H 4.464 0.030 1 63 11 11 SER HB2 H 3.905 0.030 2 64 11 11 SER HB3 H 3.849 0.030 2 65 11 11 SER C C 175.297 0.300 1 66 11 11 SER CA C 58.295 0.300 1 67 11 11 SER CB C 64.153 0.300 1 68 11 11 SER N N 116.375 0.300 1 69 12 12 GLY H H 8.479 0.030 1 70 12 12 GLY HA2 H 3.982 0.030 1 71 12 12 GLY HA3 H 3.982 0.030 1 72 12 12 GLY C C 174.621 0.300 1 73 12 12 GLY CA C 45.511 0.300 1 74 12 12 GLY N N 110.767 0.300 1 75 13 13 VAL H H 8.069 0.030 1 76 13 13 VAL HA H 4.015 0.030 1 77 13 13 VAL HB H 2.024 0.030 1 78 13 13 VAL HG1 H 0.871 0.030 1 79 13 13 VAL HG2 H 0.856 0.030 1 80 13 13 VAL C C 176.561 0.300 1 81 13 13 VAL CA C 62.842 0.300 1 82 13 13 VAL CB C 32.352 0.300 1 83 13 13 VAL CG1 C 20.353 0.300 1 84 13 13 VAL CG2 C 21.232 0.300 1 85 13 13 VAL N N 119.033 0.300 1 86 14 14 GLU H H 8.563 0.030 1 87 14 14 GLU HA H 4.130 0.030 1 88 14 14 GLU HB2 H 1.935 0.030 1 89 14 14 GLU HB3 H 1.935 0.030 1 90 14 14 GLU HG2 H 2.205 0.030 1 91 14 14 GLU HG3 H 2.205 0.030 1 92 14 14 GLU C C 177.531 0.300 1 93 14 14 GLU CA C 57.635 0.300 1 94 14 14 GLU CB C 29.738 0.300 1 95 14 14 GLU CG C 36.392 0.300 1 96 14 14 GLU N N 123.564 0.300 1 97 15 15 GLY H H 8.285 0.030 1 98 15 15 GLY HA2 H 3.889 0.030 1 99 15 15 GLY HA3 H 3.889 0.030 1 100 15 15 GLY C C 174.357 0.300 1 101 15 15 GLY CA C 45.701 0.300 1 102 15 15 GLY N N 109.581 0.300 1 103 16 16 ALA H H 7.965 0.030 1 104 16 16 ALA HA H 4.201 0.030 1 105 16 16 ALA HB H 1.345 0.030 1 106 16 16 ALA C C 178.219 0.300 1 107 16 16 ALA CA C 53.129 0.300 1 108 16 16 ALA CB C 19.101 0.300 1 109 16 16 ALA N N 123.852 0.300 1 110 17 17 ALA H H 8.004 0.030 1 111 17 17 ALA HA H 4.136 0.030 1 112 17 17 ALA HB H 1.299 0.030 1 113 17 17 ALA C C 178.138 0.300 1 114 17 17 ALA CA C 53.319 0.300 1 115 17 17 ALA CB C 18.410 0.300 1 116 17 17 ALA N N 122.122 0.300 1 117 18 18 PHE H H 8.007 0.030 1 118 18 18 PHE HA H 4.500 0.030 1 119 18 18 PHE HB2 H 3.149 0.030 2 120 18 18 PHE HB3 H 3.097 0.030 2 121 18 18 PHE HD1 H 7.228 0.030 1 122 18 18 PHE HD2 H 7.228 0.030 1 123 18 18 PHE HE1 H 7.314 0.030 1 124 18 18 PHE HE2 H 7.314 0.030 1 125 18 18 PHE C C 176.733 0.300 1 126 18 18 PHE CA C 58.690 0.300 1 127 18 18 PHE CB C 39.299 0.300 1 128 18 18 PHE CD1 C 131.765 0.300 1 129 18 18 PHE CD2 C 131.765 0.300 1 130 18 18 PHE CE1 C 131.641 0.300 1 131 18 18 PHE CE2 C 131.641 0.300 1 132 18 18 PHE N N 118.776 0.300 1 133 19 19 GLN H H 8.292 0.030 1 134 19 19 GLN HA H 4.229 0.030 1 135 19 19 GLN HB2 H 2.095 0.030 2 136 19 19 GLN HB3 H 2.002 0.030 2 137 19 19 GLN HG2 H 2.354 0.030 1 138 19 19 GLN HG3 H 2.354 0.030 1 139 19 19 GLN HE21 H 7.515 0.030 2 140 19 19 GLN HE22 H 6.887 0.030 2 141 19 19 GLN C C 175.925 0.300 1 142 19 19 GLN CA C 56.430 0.300 1 143 19 19 GLN CB C 29.431 0.300 1 144 19 19 GLN CG C 33.964 0.300 1 145 19 19 GLN N N 120.888 0.300 1 146 19 19 GLN NE2 N 112.157 0.300 1 147 20 20 SER H H 8.062 0.030 1 148 20 20 SER HA H 4.420 0.030 1 149 20 20 SER HB2 H 3.900 0.030 1 150 20 20 SER HB3 H 3.900 0.030 1 151 20 20 SER C C 173.723 0.300 1 152 20 20 SER CA C 58.482 0.300 1 153 20 20 SER CB C 63.763 0.300 1 154 20 20 SER N N 116.021 0.300 1 155 21 21 ARG H H 8.163 0.030 1 156 21 21 ARG HA H 4.258 0.030 1 157 21 21 ARG HB2 H 1.846 0.030 1 158 21 21 ARG HB3 H 1.846 0.030 1 159 21 21 ARG HG2 H 1.601 0.030 1 160 21 21 ARG HG3 H 1.601 0.030 1 161 21 21 ARG HD2 H 3.164 0.030 1 162 21 21 ARG HD3 H 3.164 0.030 1 163 21 21 ARG C C 175.753 0.300 1 164 21 21 ARG CA C 56.294 0.300 1 165 21 21 ARG CB C 30.061 0.300 1 166 21 21 ARG CG C 27.222 0.300 1 167 21 21 ARG CD C 43.273 0.300 1 168 21 21 ARG N N 120.623 0.300 1 169 22 22 LEU H H 8.196 0.030 1 170 22 22 LEU HA H 4.656 0.030 1 171 22 22 LEU HB2 H 1.435 0.030 2 172 22 22 LEU HB3 H 1.314 0.030 2 173 22 22 LEU HG H 1.632 0.030 1 174 22 22 LEU HD1 H 0.902 0.030 1 175 22 22 LEU HD2 H 0.873 0.030 1 176 22 22 LEU C C 174.502 0.300 1 177 22 22 LEU CA C 52.555 0.300 1 178 22 22 LEU CB C 41.855 0.300 1 179 22 22 LEU CG C 27.225 0.300 1 180 22 22 LEU CD1 C 24.114 0.300 1 181 22 22 LEU CD2 C 25.972 0.300 1 182 22 22 LEU N N 122.862 0.300 1 183 23 23 PRO HA H 4.546 0.030 1 184 23 23 PRO HB2 H 2.241 0.030 2 185 23 23 PRO HB3 H 2.047 0.030 2 186 23 23 PRO HG2 H 2.344 0.030 2 187 23 23 PRO HG3 H 1.911 0.030 2 188 23 23 PRO HD2 H 3.775 0.030 2 189 23 23 PRO HD3 H 3.467 0.030 2 190 23 23 PRO C C 178.396 0.300 1 191 23 23 PRO CA C 62.431 0.300 1 192 23 23 PRO CB C 31.721 0.300 1 193 23 23 PRO CG C 27.047 0.300 1 194 23 23 PRO CD C 50.371 0.300 1 195 24 24 HIS H H 8.760 0.030 1 196 24 24 HIS HA H 4.149 0.030 1 197 24 24 HIS HB2 H 3.136 0.030 2 198 24 24 HIS HB3 H 3.057 0.030 2 199 24 24 HIS HD2 H 7.005 0.030 1 200 24 24 HIS C C 175.864 0.300 1 201 24 24 HIS CA C 58.977 0.300 1 202 24 24 HIS CB C 30.835 0.300 1 203 24 24 HIS CD2 C 119.734 0.300 1 204 24 24 HIS N N 122.711 0.300 1 205 25 25 ASP H H 8.256 0.030 1 206 25 25 ASP HA H 4.478 0.030 1 207 25 25 ASP HB2 H 2.738 0.030 2 208 25 25 ASP HB3 H 2.098 0.030 2 209 25 25 ASP C C 175.065 0.300 1 210 25 25 ASP CA C 52.750 0.300 1 211 25 25 ASP CB C 40.860 0.300 1 212 25 25 ASP N N 114.074 0.300 1 213 26 26 ARG H H 7.156 0.030 1 214 26 26 ARG HA H 4.505 0.030 1 215 26 26 ARG HB2 H 1.733 0.030 2 216 26 26 ARG HB3 H 1.577 0.030 2 217 26 26 ARG HG2 H 1.502 0.030 2 218 26 26 ARG HG3 H 1.386 0.030 2 219 26 26 ARG HD2 H 3.121 0.030 1 220 26 26 ARG HD3 H 3.121 0.030 1 221 26 26 ARG C C 173.690 0.300 1 222 26 26 ARG CA C 54.770 0.300 1 223 26 26 ARG CB C 33.172 0.300 1 224 26 26 ARG CG C 26.052 0.300 1 225 26 26 ARG CD C 43.333 0.300 1 226 26 26 ARG N N 116.806 0.300 1 227 27 27 MET H H 8.466 0.030 1 228 27 27 MET HA H 4.539 0.030 1 229 27 27 MET HB2 H 2.020 0.030 2 230 27 27 MET HB3 H 1.602 0.030 2 231 27 27 MET HG2 H 2.413 0.030 2 232 27 27 MET HG3 H 2.257 0.030 2 233 27 27 MET HE H 0.869 0.030 1 234 27 27 MET C C 177.744 0.300 1 235 27 27 MET CA C 55.795 0.300 1 236 27 27 MET CB C 34.030 0.300 1 237 27 27 MET CG C 32.407 0.300 1 238 27 27 MET CE C 14.899 0.300 1 239 27 27 MET N N 119.491 0.300 1 240 28 28 THR H H 9.335 0.030 1 241 28 28 THR HA H 4.424 0.030 1 242 28 28 THR HB H 4.838 0.030 1 243 28 28 THR HG1 H 5.708 0.030 1 244 28 28 THR HG2 H 1.341 0.030 1 245 28 28 THR C C 175.621 0.300 1 246 28 28 THR CA C 60.549 0.300 1 247 28 28 THR CB C 71.345 0.300 1 248 28 28 THR CG2 C 22.677 0.300 1 249 28 28 THR N N 114.793 0.300 1 250 29 29 SER HA H 4.161 0.030 1 251 29 29 SER HB2 H 3.917 0.030 1 252 29 29 SER HB3 H 3.917 0.030 1 253 29 29 SER C C 177.613 0.300 1 254 29 29 SER CA C 61.788 0.300 1 255 29 29 SER CB C 62.086 0.300 1 256 30 30 GLN H H 8.356 0.030 1 257 30 30 GLN HA H 4.175 0.030 1 258 30 30 GLN HB2 H 2.139 0.030 2 259 30 30 GLN HB3 H 2.033 0.030 2 260 30 30 GLN HG2 H 2.417 0.030 2 261 30 30 GLN HG3 H 2.349 0.030 2 262 30 30 GLN HE21 H 7.424 0.030 2 263 30 30 GLN HE22 H 6.889 0.030 2 264 30 30 GLN C C 178.798 0.300 1 265 30 30 GLN CA C 59.161 0.300 1 266 30 30 GLN CB C 28.849 0.300 1 267 30 30 GLN CG C 34.514 0.300 1 268 30 30 GLN N N 122.982 0.300 1 269 30 30 GLN NE2 N 112.001 0.300 1 270 31 31 GLU H H 7.744 0.030 1 271 31 31 GLU HA H 3.493 0.030 1 272 31 31 GLU HB2 H 2.293 0.030 2 273 31 31 GLU HB3 H 1.402 0.030 2 274 31 31 GLU HG2 H 1.877 0.030 2 275 31 31 GLU HG3 H 2.490 0.030 2 276 31 31 GLU C C 178.643 0.300 1 277 31 31 GLU CA C 59.411 0.300 1 278 31 31 GLU CB C 29.237 0.300 1 279 31 31 GLU CG C 37.562 0.300 1 280 31 31 GLU N N 120.782 0.300 1 281 32 32 ALA H H 8.572 0.030 1 282 32 32 ALA HA H 3.593 0.030 1 283 32 32 ALA HB H 1.386 0.030 1 284 32 32 ALA C C 179.159 0.300 1 285 32 32 ALA CA C 55.169 0.300 1 286 32 32 ALA CB C 17.969 0.300 1 287 32 32 ALA N N 120.976 0.300 1 288 33 33 ALA H H 7.384 0.030 1 289 33 33 ALA HA H 4.063 0.030 1 290 33 33 ALA HB H 1.512 0.030 1 291 33 33 ALA C C 179.816 0.300 1 292 33 33 ALA CA C 54.200 0.300 1 293 33 33 ALA CB C 18.459 0.300 1 294 33 33 ALA N N 117.321 0.300 1 295 34 34 CYS H H 7.540 0.030 1 296 34 34 CYS HA H 4.208 0.030 1 297 34 34 CYS HB2 H 2.625 0.030 1 298 34 34 CYS HB3 H 2.625 0.030 1 299 34 34 CYS C C 173.689 0.300 1 300 34 34 CYS CA C 61.135 0.300 1 301 34 34 CYS CB C 28.641 0.300 1 302 34 34 CYS N N 114.470 0.300 1 303 35 35 PHE H H 8.037 0.030 1 304 35 35 PHE HA H 4.595 0.030 1 305 35 35 PHE HB2 H 2.592 0.030 2 306 35 35 PHE HB3 H 2.420 0.030 2 307 35 35 PHE HD1 H 7.185 0.030 1 308 35 35 PHE HD2 H 7.185 0.030 1 309 35 35 PHE HE1 H 6.838 0.030 1 310 35 35 PHE HE2 H 6.838 0.030 1 311 35 35 PHE HZ H 7.168 0.030 1 312 35 35 PHE C C 173.339 0.300 1 313 35 35 PHE CA C 55.384 0.300 1 314 35 35 PHE CB C 37.599 0.300 1 315 35 35 PHE CD1 C 132.978 0.300 1 316 35 35 PHE CD2 C 132.978 0.300 1 317 35 35 PHE CE1 C 130.365 0.300 1 318 35 35 PHE CE2 C 130.365 0.300 1 319 35 35 PHE CZ C 128.576 0.300 1 320 35 35 PHE N N 117.181 0.300 1 321 36 36 PRO HA H 4.382 0.030 1 322 36 36 PRO HB2 H 2.216 0.030 2 323 36 36 PRO HB3 H 2.006 0.030 2 324 36 36 PRO HG2 H 2.012 0.030 1 325 36 36 PRO HG3 H 2.012 0.030 1 326 36 36 PRO HD2 H 3.388 0.030 2 327 36 36 PRO HD3 H 3.263 0.030 2 328 36 36 PRO C C 178.130 0.300 1 329 36 36 PRO CA C 65.214 0.300 1 330 36 36 PRO CB C 30.974 0.300 1 331 36 36 PRO CG C 27.260 0.300 1 332 36 36 PRO CD C 50.474 0.300 1 333 37 37 ASP H H 9.773 0.030 1 334 37 37 ASP HA H 4.187 0.030 1 335 37 37 ASP HB2 H 2.718 0.030 2 336 37 37 ASP HB3 H 2.518 0.030 2 337 37 37 ASP C C 176.754 0.300 1 338 37 37 ASP CA C 54.743 0.300 1 339 37 37 ASP CB C 38.613 0.300 1 340 37 37 ASP N N 115.556 0.300 1 341 38 38 ILE H H 7.276 0.030 1 342 38 38 ILE HA H 3.930 0.030 1 343 38 38 ILE HB H 1.865 0.030 1 344 38 38 ILE HG12 H 1.530 0.030 2 345 38 38 ILE HG13 H 1.268 0.030 2 346 38 38 ILE HG2 H 0.539 0.030 1 347 38 38 ILE HD1 H 0.723 0.030 1 348 38 38 ILE C C 178.997 0.300 1 349 38 38 ILE CA C 60.772 0.300 1 350 38 38 ILE CB C 36.347 0.300 1 351 38 38 ILE CG1 C 27.457 0.300 1 352 38 38 ILE CG2 C 17.760 0.300 1 353 38 38 ILE CD1 C 10.408 0.300 1 354 38 38 ILE N N 119.418 0.300 1 355 39 39 ILE H H 7.367 0.030 1 356 39 39 ILE HA H 3.969 0.030 1 357 39 39 ILE HB H 1.687 0.030 1 358 39 39 ILE HG12 H 1.386 0.030 1 359 39 39 ILE HG13 H 1.386 0.030 1 360 39 39 ILE HG2 H 1.007 0.030 1 361 39 39 ILE HD1 H 0.829 0.030 1 362 39 39 ILE C C 175.318 0.300 1 363 39 39 ILE CA C 61.621 0.300 1 364 39 39 ILE CB C 37.908 0.300 1 365 39 39 ILE CG1 C 28.735 0.300 1 366 39 39 ILE CG2 C 18.428 0.300 1 367 39 39 ILE CD1 C 13.531 0.300 1 368 39 39 ILE N N 118.769 0.300 1 369 40 40 SER H H 7.129 0.030 1 370 40 40 SER HA H 4.503 0.030 1 371 40 40 SER HB2 H 3.987 0.030 2 372 40 40 SER HB3 H 3.883 0.030 2 373 40 40 SER C C 174.529 0.300 1 374 40 40 SER CA C 58.428 0.300 1 375 40 40 SER CB C 64.011 0.300 1 376 40 40 SER N N 112.170 0.300 1 377 41 41 GLY H H 7.183 0.030 1 378 41 41 GLY HA2 H 4.481 0.030 2 379 41 41 GLY HA3 H 3.858 0.030 2 380 41 41 GLY C C 171.117 0.300 1 381 41 41 GLY CA C 44.483 0.300 1 382 41 41 GLY N N 110.767 0.300 1 383 42 42 PRO HA H 4.540 0.030 1 384 42 42 PRO HB2 H 2.529 0.030 2 385 42 42 PRO HB3 H 2.079 0.030 2 386 42 42 PRO HG2 H 2.111 0.030 1 387 42 42 PRO HG3 H 2.111 0.030 1 388 42 42 PRO HD2 H 3.722 0.030 2 389 42 42 PRO HD3 H 3.652 0.030 2 390 42 42 PRO CA C 62.723 0.300 1 391 42 42 PRO CB C 32.739 0.300 1 392 42 42 PRO CG C 27.624 0.300 1 393 42 42 PRO CD C 49.707 0.300 1 394 43 43 GLN HA H 3.907 0.030 1 395 43 43 GLN HB2 H 2.153 0.030 1 396 43 43 GLN HB3 H 2.153 0.030 1 397 43 43 GLN HG2 H 2.500 0.030 2 398 43 43 GLN HG3 H 2.439 0.030 2 399 43 43 GLN HE21 H 7.612 0.030 2 400 43 43 GLN HE22 H 6.849 0.030 2 401 43 43 GLN C C 178.555 0.300 1 402 43 43 GLN CA C 59.543 0.300 1 403 43 43 GLN CB C 28.299 0.300 1 404 43 43 GLN CG C 34.106 0.300 1 405 43 43 GLN NE2 N 112.213 0.300 1 406 44 44 GLN H H 9.184 0.030 1 407 44 44 GLN HA H 4.082 0.030 1 408 44 44 GLN HB2 H 2.185 0.030 2 409 44 44 GLN HB3 H 2.011 0.030 2 410 44 44 GLN HG2 H 2.482 0.030 1 411 44 44 GLN HG3 H 2.482 0.030 1 412 44 44 GLN HE21 H 7.464 0.030 2 413 44 44 GLN HE22 H 6.903 0.030 2 414 44 44 GLN C C 178.007 0.300 1 415 44 44 GLN CA C 59.484 0.300 1 416 44 44 GLN CB C 27.730 0.300 1 417 44 44 GLN CG C 33.277 0.300 1 418 44 44 GLN N N 117.813 0.300 1 419 44 44 GLN NE2 N 111.525 0.300 1 420 45 45 THR H H 7.234 0.030 1 421 45 45 THR HA H 4.105 0.030 1 422 45 45 THR HB H 4.310 0.030 1 423 45 45 THR HG2 H 1.381 0.030 1 424 45 45 THR C C 176.410 0.300 1 425 45 45 THR CA C 65.709 0.300 1 426 45 45 THR CB C 68.260 0.300 1 427 45 45 THR CG2 C 23.046 0.300 1 428 45 45 THR N N 114.758 0.300 1 429 46 46 GLN H H 7.433 0.030 1 430 46 46 GLN HA H 3.822 0.030 1 431 46 46 GLN HB2 H 2.187 0.030 2 432 46 46 GLN HB3 H 2.087 0.030 2 433 46 46 GLN HG2 H 2.305 0.030 2 434 46 46 GLN HG3 H 2.190 0.030 2 435 46 46 GLN HE21 H 6.855 0.030 2 436 46 46 GLN HE22 H 6.638 0.030 2 437 46 46 GLN C C 177.815 0.300 1 438 46 46 GLN CA C 59.909 0.300 1 439 46 46 GLN CB C 27.440 0.300 1 440 46 46 GLN CG C 34.827 0.300 1 441 46 46 GLN N N 122.032 0.300 1 442 46 46 GLN NE2 N 111.546 0.300 1 443 47 47 LYS H H 8.040 0.030 1 444 47 47 LYS HA H 4.045 0.030 1 445 47 47 LYS HB2 H 2.080 0.030 2 446 47 47 LYS HB3 H 2.020 0.030 2 447 47 47 LYS HG2 H 1.674 0.030 2 448 47 47 LYS HG3 H 1.496 0.030 2 449 47 47 LYS HD2 H 1.717 0.030 1 450 47 47 LYS HD3 H 1.717 0.030 1 451 47 47 LYS HE2 H 3.001 0.030 1 452 47 47 LYS HE3 H 3.001 0.030 1 453 47 47 LYS C C 179.938 0.300 1 454 47 47 LYS CA C 59.845 0.300 1 455 47 47 LYS CB C 31.990 0.300 1 456 47 47 LYS CG C 25.560 0.300 1 457 47 47 LYS CD C 29.246 0.300 1 458 47 47 LYS CE C 42.173 0.300 1 459 47 47 LYS N N 117.633 0.300 1 460 48 48 VAL H H 7.778 0.030 1 461 48 48 VAL HA H 3.894 0.030 1 462 48 48 VAL HB H 2.406 0.030 1 463 48 48 VAL HG1 H 1.242 0.030 1 464 48 48 VAL HG2 H 1.190 0.030 1 465 48 48 VAL C C 177.035 0.300 1 466 48 48 VAL CA C 67.440 0.300 1 467 48 48 VAL CB C 31.797 0.300 1 468 48 48 VAL CG1 C 21.993 0.300 1 469 48 48 VAL CG2 C 22.761 0.300 1 470 48 48 VAL N N 121.839 0.300 1 471 49 49 PHE H H 8.202 0.030 1 472 49 49 PHE HA H 3.669 0.030 1 473 49 49 PHE HB2 H 3.397 0.030 2 474 49 49 PHE HB3 H 2.840 0.030 2 475 49 49 PHE HD1 H 6.551 0.030 1 476 49 49 PHE HD2 H 6.551 0.030 1 477 49 49 PHE HE1 H 5.996 0.030 1 478 49 49 PHE HE2 H 5.996 0.030 1 479 49 49 PHE HZ H 6.408 0.030 1 480 49 49 PHE C C 176.006 0.300 1 481 49 49 PHE CA C 62.743 0.300 1 482 49 49 PHE CB C 39.496 0.300 1 483 49 49 PHE CD1 C 131.184 0.300 1 484 49 49 PHE CD2 C 131.184 0.300 1 485 49 49 PHE CE1 C 131.121 0.300 1 486 49 49 PHE CE2 C 131.121 0.300 1 487 49 49 PHE CZ C 128.112 0.300 1 488 49 49 PHE N N 119.350 0.300 1 489 50 50 LEU H H 8.482 0.030 1 490 50 50 LEU HA H 3.624 0.030 1 491 50 50 LEU HB2 H 1.874 0.030 2 492 50 50 LEU HB3 H 1.276 0.030 2 493 50 50 LEU HG H 1.871 0.030 1 494 50 50 LEU HD1 H 0.669 0.030 1 495 50 50 LEU HD2 H 0.686 0.030 1 496 50 50 LEU C C 177.572 0.300 1 497 50 50 LEU CA C 57.766 0.300 1 498 50 50 LEU CB C 41.718 0.300 1 499 50 50 LEU CG C 26.970 0.300 1 500 50 50 LEU CD1 C 25.702 0.300 1 501 50 50 LEU CD2 C 22.130 0.300 1 502 50 50 LEU N N 118.532 0.300 1 503 51 51 PHE H H 8.112 0.030 1 504 51 51 PHE HA H 3.872 0.030 1 505 51 51 PHE HB2 H 2.825 0.030 1 506 51 51 PHE HB3 H 2.825 0.030 1 507 51 51 PHE HD1 H 6.517 0.030 1 508 51 51 PHE HD2 H 6.517 0.030 1 509 51 51 PHE HE1 H 7.064 0.030 1 510 51 51 PHE HE2 H 7.064 0.030 1 511 51 51 PHE HZ H 7.181 0.030 1 512 51 51 PHE C C 178.370 0.300 1 513 51 51 PHE CA C 62.170 0.300 1 514 51 51 PHE CB C 39.559 0.300 1 515 51 51 PHE CD1 C 131.493 0.300 1 516 51 51 PHE CD2 C 131.493 0.300 1 517 51 51 PHE CE1 C 130.594 0.300 1 518 51 51 PHE CE2 C 130.594 0.300 1 519 51 51 PHE CZ C 129.202 0.300 1 520 51 51 PHE N N 119.842 0.300 1 521 52 52 ILE H H 8.349 0.030 1 522 52 52 ILE HA H 3.338 0.030 1 523 52 52 ILE HB H 1.709 0.030 1 524 52 52 ILE HG12 H 2.262 0.030 2 525 52 52 ILE HG13 H 1.044 0.030 2 526 52 52 ILE HG2 H 0.840 0.030 1 527 52 52 ILE HD1 H 1.007 0.030 1 528 52 52 ILE C C 178.998 0.300 1 529 52 52 ILE CA C 65.994 0.300 1 530 52 52 ILE CB C 38.706 0.300 1 531 52 52 ILE CG1 C 29.327 0.300 1 532 52 52 ILE CG2 C 18.044 0.300 1 533 52 52 ILE CD1 C 15.676 0.300 1 534 52 52 ILE N N 118.124 0.300 1 535 53 53 ARG H H 8.856 0.030 1 536 53 53 ARG HA H 3.424 0.030 1 537 53 53 ARG HB2 H 1.347 0.030 2 538 53 53 ARG HB3 H 1.198 0.030 2 539 53 53 ARG HG2 H 1.666 0.030 2 540 53 53 ARG HG3 H 1.491 0.030 2 541 53 53 ARG HD2 H 2.740 0.030 2 542 53 53 ARG HD3 H 3.000 0.030 2 543 53 53 ARG HE H 9.568 0.030 1 544 53 53 ARG HH11 H 7.455 0.030 1 545 53 53 ARG HH12 H 7.455 0.030 1 546 53 53 ARG HH21 H 7.257 0.030 1 547 53 53 ARG HH22 H 7.257 0.030 1 548 53 53 ARG C C 176.642 0.300 1 549 53 53 ARG CA C 61.003 0.300 1 550 53 53 ARG CB C 30.198 0.300 1 551 53 53 ARG CG C 24.205 0.300 1 552 53 53 ARG CD C 45.852 0.300 1 553 53 53 ARG N N 123.564 0.300 1 554 53 53 ARG NE N 84.181 0.300 1 555 54 54 ASN H H 8.859 0.030 1 556 54 54 ASN HA H 4.292 0.030 1 557 54 54 ASN HB2 H 2.595 0.030 2 558 54 54 ASN HB3 H 2.546 0.030 2 559 54 54 ASN HD21 H 7.294 0.030 1 560 54 54 ASN HD22 H 7.294 0.030 1 561 54 54 ASN C C 178.088 0.300 1 562 54 54 ASN CA C 55.814 0.300 1 563 54 54 ASN CB C 37.275 0.300 1 564 54 54 ASN N N 117.736 0.300 1 565 54 54 ASN ND2 N 112.644 0.300 1 566 55 55 ARG H H 8.565 0.030 1 567 55 55 ARG HA H 3.915 0.030 1 568 55 55 ARG HB2 H 1.612 0.030 2 569 55 55 ARG HB3 H 1.315 0.030 2 570 55 55 ARG HG2 H 1.590 0.030 2 571 55 55 ARG HG3 H 1.315 0.030 2 572 55 55 ARG HD2 H 3.338 0.030 2 573 55 55 ARG HD3 H 2.960 0.030 2 574 55 55 ARG HE H 7.464 0.030 1 575 55 55 ARG C C 177.492 0.300 1 576 55 55 ARG CA C 57.503 0.300 1 577 55 55 ARG CB C 29.103 0.300 1 578 55 55 ARG CG C 26.638 0.300 1 579 55 55 ARG CD C 42.019 0.300 1 580 55 55 ARG N N 121.226 0.300 1 581 55 55 ARG NE N 84.996 0.300 1 582 56 56 THR H H 8.178 0.030 1 583 56 56 THR HA H 3.717 0.030 1 584 56 56 THR HB H 3.925 0.030 1 585 56 56 THR HG1 H 4.467 0.030 1 586 56 56 THR HG2 H 1.217 0.030 1 587 56 56 THR C C 175.854 0.300 1 588 56 56 THR CA C 68.526 0.300 1 589 56 56 THR CB C 67.855 0.300 1 590 56 56 THR CG2 C 22.804 0.300 1 591 56 56 THR N N 116.770 0.300 1 592 57 57 LEU H H 7.695 0.030 1 593 57 57 LEU HA H 3.988 0.030 1 594 57 57 LEU HB2 H 1.834 0.030 2 595 57 57 LEU HB3 H 1.517 0.030 2 596 57 57 LEU HG H 1.764 0.030 1 597 57 57 LEU HD1 H 0.921 0.030 1 598 57 57 LEU HD2 H 0.903 0.030 1 599 57 57 LEU C C 178.231 0.300 1 600 57 57 LEU CA C 58.310 0.300 1 601 57 57 LEU CB C 42.125 0.300 1 602 57 57 LEU CG C 27.088 0.300 1 603 57 57 LEU CD1 C 26.258 0.300 1 604 57 57 LEU CD2 C 24.819 0.300 1 605 57 57 LEU N N 118.679 0.300 1 606 58 58 GLN H H 7.928 0.030 1 607 58 58 GLN HA H 3.807 0.030 1 608 58 58 GLN HB2 H 2.273 0.030 2 609 58 58 GLN HB3 H 2.085 0.030 2 610 58 58 GLN HG2 H 2.399 0.030 2 611 58 58 GLN HG3 H 2.260 0.030 2 612 58 58 GLN HE21 H 7.775 0.030 2 613 58 58 GLN HE22 H 6.713 0.030 2 614 58 58 GLN C C 177.583 0.300 1 615 58 58 GLN CA C 59.087 0.300 1 616 58 58 GLN CB C 28.504 0.300 1 617 58 58 GLN CG C 33.391 0.300 1 618 58 58 GLN N N 118.676 0.300 1 619 58 58 GLN NE2 N 113.979 0.300 1 620 59 59 LEU H H 8.203 0.030 1 621 59 59 LEU HA H 4.014 0.030 1 622 59 59 LEU HB2 H 2.245 0.030 2 623 59 59 LEU HB3 H 1.392 0.030 2 624 59 59 LEU HG H 1.968 0.030 1 625 59 59 LEU HD1 H 0.910 0.030 1 626 59 59 LEU HD2 H 0.846 0.030 1 627 59 59 LEU C C 180.099 0.300 1 628 59 59 LEU CA C 57.825 0.300 1 629 59 59 LEU CB C 42.781 0.300 1 630 59 59 LEU CG C 26.762 0.300 1 631 59 59 LEU CD1 C 27.015 0.300 1 632 59 59 LEU CD2 C 22.556 0.300 1 633 59 59 LEU N N 118.796 0.300 1 634 60 60 TRP H H 7.659 0.030 1 635 60 60 TRP HA H 4.690 0.030 1 636 60 60 TRP HB2 H 3.450 0.030 2 637 60 60 TRP HB3 H 3.214 0.030 2 638 60 60 TRP HD1 H 7.152 0.030 1 639 60 60 TRP HE1 H 9.413 0.030 1 640 60 60 TRP HE3 H 7.838 0.030 1 641 60 60 TRP HZ2 H 6.660 0.030 1 642 60 60 TRP HZ3 H 7.220 0.030 1 643 60 60 TRP HH2 H 6.880 0.030 1 644 60 60 TRP C C 176.410 0.300 1 645 60 60 TRP CA C 58.911 0.300 1 646 60 60 TRP CB C 30.226 0.300 1 647 60 60 TRP CD1 C 128.796 0.300 1 648 60 60 TRP CE3 C 122.232 0.300 1 649 60 60 TRP CZ2 C 114.156 0.300 1 650 60 60 TRP CZ3 C 123.862 0.300 1 651 60 60 TRP CH2 C 125.532 0.300 1 652 60 60 TRP N N 120.464 0.300 1 653 60 60 TRP NE1 N 128.267 0.300 1 654 61 61 LEU H H 8.542 0.030 1 655 61 61 LEU HA H 3.487 0.030 1 656 61 61 LEU HB2 H 1.865 0.030 2 657 61 61 LEU HB3 H 1.359 0.030 2 658 61 61 LEU HG H 2.037 0.030 1 659 61 61 LEU HD1 H 0.897 0.030 1 660 61 61 LEU HD2 H 0.968 0.030 1 661 61 61 LEU C C 180.028 0.300 1 662 61 61 LEU CA C 57.107 0.300 1 663 61 61 LEU CB C 41.502 0.300 1 664 61 61 LEU CG C 26.844 0.300 1 665 61 61 LEU CD1 C 25.830 0.300 1 666 61 61 LEU CD2 C 22.696 0.300 1 667 61 61 LEU N N 116.806 0.300 1 668 62 62 ASP H H 8.138 0.030 1 669 62 62 ASP HA H 4.355 0.030 1 670 62 62 ASP HB2 H 2.759 0.030 2 671 62 62 ASP HB3 H 2.553 0.030 2 672 62 62 ASP C C 177.492 0.300 1 673 62 62 ASP CA C 56.079 0.300 1 674 62 62 ASP CB C 41.122 0.300 1 675 62 62 ASP N N 117.686 0.300 1 676 63 63 ASN H H 7.222 0.030 1 677 63 63 ASN HA H 4.700 0.030 1 678 63 63 ASN HB2 H 2.914 0.030 2 679 63 63 ASN HB3 H 2.649 0.030 2 680 63 63 ASN HD21 H 7.814 0.030 2 681 63 63 ASN HD22 H 6.683 0.030 2 682 63 63 ASN C C 171.420 0.300 1 683 63 63 ASN CA C 51.713 0.300 1 684 63 63 ASN CB C 38.302 0.300 1 685 63 63 ASN N N 113.126 0.300 1 686 63 63 ASN ND2 N 111.479 0.300 1 687 64 64 PRO HA H 2.856 0.030 1 688 64 64 PRO HB2 H 1.424 0.030 2 689 64 64 PRO HB3 H 0.764 0.030 2 690 64 64 PRO HG2 H 1.642 0.030 2 691 64 64 PRO HG3 H 1.393 0.030 2 692 64 64 PRO HD2 H 3.320 0.030 2 693 64 64 PRO HD3 H 3.267 0.030 2 694 64 64 PRO C C 175.389 0.300 1 695 64 64 PRO CA C 63.224 0.300 1 696 64 64 PRO CB C 30.123 0.300 1 697 64 64 PRO CG C 26.444 0.300 1 698 64 64 PRO CD C 48.581 0.300 1 699 65 65 LYS H H 7.077 0.030 1 700 65 65 LYS HA H 4.356 0.030 1 701 65 65 LYS HB2 H 1.959 0.030 2 702 65 65 LYS HB3 H 1.732 0.030 2 703 65 65 LYS HG2 H 1.339 0.030 2 704 65 65 LYS HG3 H 1.270 0.030 2 705 65 65 LYS HD2 H 1.624 0.030 1 706 65 65 LYS HD3 H 1.624 0.030 1 707 65 65 LYS HE2 H 2.955 0.030 1 708 65 65 LYS HE3 H 2.955 0.030 1 709 65 65 LYS C C 176.460 0.300 1 710 65 65 LYS CA C 55.724 0.300 1 711 65 65 LYS CB C 32.533 0.300 1 712 65 65 LYS CG C 25.097 0.300 1 713 65 65 LYS CD C 28.611 0.300 1 714 65 65 LYS CE C 42.094 0.300 1 715 65 65 LYS N N 114.557 0.300 1 716 66 66 ILE H H 7.315 0.030 1 717 66 66 ILE HA H 4.653 0.030 1 718 66 66 ILE HB H 1.808 0.030 1 719 66 66 ILE HG12 H 1.424 0.030 2 720 66 66 ILE HG13 H 1.100 0.030 2 721 66 66 ILE HG2 H 0.909 0.030 1 722 66 66 ILE HD1 H 0.855 0.030 1 723 66 66 ILE C C 173.311 0.300 1 724 66 66 ILE CA C 58.856 0.300 1 725 66 66 ILE CB C 41.837 0.300 1 726 66 66 ILE CG1 C 26.526 0.300 1 727 66 66 ILE CG2 C 17.246 0.300 1 728 66 66 ILE CD1 C 13.235 0.300 1 729 66 66 ILE N N 117.320 0.300 1 730 67 67 GLN H H 8.381 0.030 1 731 67 67 GLN HA H 3.877 0.030 1 732 67 67 GLN HB2 H 2.108 0.030 2 733 67 67 GLN HB3 H 2.042 0.030 2 734 67 67 GLN HG2 H 2.158 0.030 2 735 67 67 GLN HG3 H 1.966 0.030 2 736 67 67 GLN HE21 H 7.902 0.030 2 737 67 67 GLN HE22 H 6.871 0.030 2 738 67 67 GLN C C 175.257 0.300 1 739 67 67 GLN CA C 56.671 0.300 1 740 67 67 GLN CB C 29.399 0.300 1 741 67 67 GLN CG C 32.838 0.300 1 742 67 67 GLN N N 123.285 0.300 1 743 67 67 GLN NE2 N 111.848 0.300 1 744 68 68 LEU H H 10.349 0.030 1 745 68 68 LEU HA H 4.822 0.030 1 746 68 68 LEU HB2 H 2.142 0.030 2 747 68 68 LEU HB3 H 2.055 0.030 2 748 68 68 LEU HG H 1.401 0.030 1 749 68 68 LEU HD1 H 0.991 0.030 1 750 68 68 LEU HD2 H 1.162 0.030 1 751 68 68 LEU C C 177.896 0.300 1 752 68 68 LEU CA C 53.891 0.300 1 753 68 68 LEU CB C 41.457 0.300 1 754 68 68 LEU CG C 28.131 0.300 1 755 68 68 LEU CD1 C 23.059 0.300 1 756 68 68 LEU CD2 C 29.524 0.300 1 757 68 68 LEU N N 132.001 0.300 1 758 69 69 THR H H 8.418 0.030 1 759 69 69 THR HA H 4.654 0.030 1 760 69 69 THR HB H 4.779 0.030 1 761 69 69 THR HG1 H 5.730 0.030 1 762 69 69 THR HG2 H 1.281 0.030 1 763 69 69 THR C C 176.117 0.300 1 764 69 69 THR CA C 60.922 0.300 1 765 69 69 THR CB C 71.302 0.300 1 766 69 69 THR CG2 C 22.060 0.300 1 767 69 69 THR N N 121.163 0.300 1 768 70 70 PHE H H 9.211 0.030 1 769 70 70 PHE HA H 3.411 0.030 1 770 70 70 PHE HB2 H 2.779 0.030 2 771 70 70 PHE HB3 H 2.570 0.030 2 772 70 70 PHE HD1 H 6.872 0.030 1 773 70 70 PHE HD2 H 6.872 0.030 1 774 70 70 PHE HE1 H 7.245 0.030 1 775 70 70 PHE HE2 H 7.245 0.030 1 776 70 70 PHE C C 175.985 0.300 1 777 70 70 PHE CA C 60.071 0.300 1 778 70 70 PHE CB C 38.514 0.300 1 779 70 70 PHE CD1 C 131.350 0.300 1 780 70 70 PHE CD2 C 131.350 0.300 1 781 70 70 PHE CE1 C 130.785 0.300 1 782 70 70 PHE CE2 C 130.785 0.300 1 783 70 70 PHE N N 125.865 0.300 1 784 71 71 GLU H H 9.208 0.030 1 785 71 71 GLU HA H 3.189 0.030 1 786 71 71 GLU HB2 H 1.938 0.030 2 787 71 71 GLU HB3 H 1.752 0.030 2 788 71 71 GLU HG2 H 2.439 0.030 2 789 71 71 GLU HG3 H 2.119 0.030 2 790 71 71 GLU C C 178.866 0.300 1 791 71 71 GLU CA C 61.098 0.300 1 792 71 71 GLU CB C 28.348 0.300 1 793 71 71 GLU CG C 37.541 0.300 1 794 71 71 GLU N N 119.181 0.300 1 795 72 72 ALA H H 7.898 0.030 1 796 72 72 ALA HA H 4.006 0.030 1 797 72 72 ALA HB H 1.411 0.030 1 798 72 72 ALA C C 180.382 0.300 1 799 72 72 ALA CA C 54.640 0.300 1 800 72 72 ALA CB C 18.998 0.300 1 801 72 72 ALA N N 121.264 0.300 1 802 73 73 THR H H 7.558 0.030 1 803 73 73 THR HA H 3.553 0.030 1 804 73 73 THR HB H 4.193 0.030 1 805 73 73 THR HG1 H 3.768 0.030 1 806 73 73 THR HG2 H 1.110 0.030 1 807 73 73 THR C C 178.167 0.300 1 808 73 73 THR CA C 67.762 0.300 1 809 73 73 THR CB C 68.230 0.300 1 810 73 73 THR CG2 C 21.335 0.300 1 811 73 73 THR N N 116.877 0.300 1 812 74 74 LEU H H 7.912 0.030 1 813 74 74 LEU HA H 3.744 0.030 1 814 74 74 LEU HB2 H 1.430 0.030 2 815 74 74 LEU HB3 H 1.001 0.030 2 816 74 74 LEU HG H 1.412 0.030 1 817 74 74 LEU HD1 H 0.830 0.030 1 818 74 74 LEU HD2 H 0.829 0.030 1 819 74 74 LEU C C 179.290 0.300 1 820 74 74 LEU CA C 57.928 0.300 1 821 74 74 LEU CB C 41.846 0.300 1 822 74 74 LEU CG C 26.463 0.300 1 823 74 74 LEU CD1 C 24.445 0.300 1 824 74 74 LEU CD2 C 25.108 0.300 1 825 74 74 LEU N N 119.371 0.300 1 826 75 75 GLN H H 7.435 0.030 1 827 75 75 GLN HA H 3.985 0.030 1 828 75 75 GLN HB2 H 2.088 0.030 1 829 75 75 GLN HB3 H 2.088 0.030 1 830 75 75 GLN HG2 H 2.458 0.030 2 831 75 75 GLN HG3 H 2.396 0.030 2 832 75 75 GLN HE21 H 7.381 0.030 2 833 75 75 GLN HE22 H 6.733 0.030 2 834 75 75 GLN C C 176.986 0.300 1 835 75 75 GLN CA C 57.714 0.300 1 836 75 75 GLN CB C 28.882 0.300 1 837 75 75 GLN CG C 33.893 0.300 1 838 75 75 GLN N N 113.811 0.300 1 839 75 75 GLN NE2 N 111.477 0.300 1 840 76 76 GLN H H 7.330 0.030 1 841 76 76 GLN HA H 4.363 0.030 1 842 76 76 GLN HB2 H 2.405 0.030 2 843 76 76 GLN HB3 H 1.899 0.030 2 844 76 76 GLN HG2 H 2.500 0.030 2 845 76 76 GLN HG3 H 2.234 0.030 2 846 76 76 GLN HE21 H 7.262 0.030 2 847 76 76 GLN HE22 H 7.009 0.030 2 848 76 76 GLN C C 175.014 0.300 1 849 76 76 GLN CA C 55.609 0.300 1 850 76 76 GLN CB C 30.806 0.300 1 851 76 76 GLN CG C 35.011 0.300 1 852 76 76 GLN N N 115.600 0.300 1 853 76 76 GLN NE2 N 111.355 0.300 1 854 77 77 LEU H H 7.324 0.030 1 855 77 77 LEU HA H 4.528 0.030 1 856 77 77 LEU HB2 H 1.811 0.030 2 857 77 77 LEU HB3 H 1.350 0.030 2 858 77 77 LEU HG H 1.932 0.030 1 859 77 77 LEU HD1 H 0.922 0.030 1 860 77 77 LEU HD2 H 0.913 0.030 1 861 77 77 LEU C C 175.125 0.300 1 862 77 77 LEU CA C 54.332 0.300 1 863 77 77 LEU CB C 44.412 0.300 1 864 77 77 LEU CG C 26.366 0.300 1 865 77 77 LEU CD1 C 27.862 0.300 1 866 77 77 LEU CD2 C 25.147 0.300 1 867 77 77 LEU N N 122.126 0.300 1 868 78 78 GLU H H 9.126 0.030 1 869 78 78 GLU HA H 4.319 0.030 1 870 78 78 GLU HB2 H 2.178 0.030 2 871 78 78 GLU HB3 H 2.125 0.030 2 872 78 78 GLU HG2 H 2.456 0.030 2 873 78 78 GLU HG3 H 2.381 0.030 2 874 78 78 GLU C C 176.035 0.300 1 875 78 78 GLU CA C 55.419 0.300 1 876 78 78 GLU CB C 31.216 0.300 1 877 78 78 GLU CG C 36.653 0.300 1 878 78 78 GLU N N 122.965 0.300 1 879 79 79 ALA H H 8.481 0.030 1 880 79 79 ALA HA H 4.213 0.030 1 881 79 79 ALA HB H 1.307 0.030 1 882 79 79 ALA C C 176.894 0.300 1 883 79 79 ALA CA C 51.587 0.300 1 884 79 79 ALA CB C 17.298 0.300 1 885 79 79 ALA N N 124.312 0.300 1 886 80 80 PRO HA H 4.534 0.030 1 887 80 80 PRO HB2 H 2.131 0.030 2 888 80 80 PRO HB3 H 2.005 0.030 2 889 80 80 PRO HG2 H 1.601 0.030 2 890 80 80 PRO HG3 H 0.574 0.030 2 891 80 80 PRO HD2 H 3.130 0.030 2 892 80 80 PRO HD3 H 2.657 0.030 2 893 80 80 PRO C C 176.673 0.300 1 894 80 80 PRO CA C 63.711 0.300 1 895 80 80 PRO CB C 33.660 0.300 1 896 80 80 PRO CG C 23.441 0.300 1 897 80 80 PRO CD C 49.532 0.300 1 898 81 81 TYR H H 8.037 0.030 1 899 81 81 TYR HA H 4.086 0.030 1 900 81 81 TYR HB2 H 3.156 0.030 2 901 81 81 TYR HB3 H 3.007 0.030 2 902 81 81 TYR HD1 H 6.846 0.030 1 903 81 81 TYR HD2 H 6.846 0.030 1 904 81 81 TYR HE1 H 6.345 0.030 1 905 81 81 TYR HE2 H 6.345 0.030 1 906 81 81 TYR C C 174.408 0.300 1 907 81 81 TYR CA C 60.736 0.300 1 908 81 81 TYR CB C 37.430 0.300 1 909 81 81 TYR CD1 C 132.382 0.300 1 910 81 81 TYR CD2 C 132.382 0.300 1 911 81 81 TYR CE1 C 118.147 0.300 1 912 81 81 TYR CE2 C 118.147 0.300 1 913 81 81 TYR N N 127.096 0.300 1 914 82 82 ASN H H 7.646 0.030 1 915 82 82 ASN HA H 4.220 0.030 1 916 82 82 ASN HB2 H 3.072 0.030 2 917 82 82 ASN HB3 H 2.627 0.030 2 918 82 82 ASN HD21 H 7.673 0.030 2 919 82 82 ASN HD22 H 6.726 0.030 2 920 82 82 ASN C C 175.803 0.300 1 921 82 82 ASN CA C 51.939 0.300 1 922 82 82 ASN CB C 37.308 0.300 1 923 82 82 ASN N N 112.924 0.300 1 924 82 82 ASN ND2 N 110.764 0.300 1 925 83 83 SER H H 7.472 0.030 1 926 83 83 SER HA H 4.087 0.030 1 927 83 83 SER HB2 H 3.917 0.030 1 928 83 83 SER HB3 H 3.917 0.030 1 929 83 83 SER C C 174.519 0.300 1 930 83 83 SER CA C 61.165 0.300 1 931 83 83 SER CB C 63.760 0.300 1 932 83 83 SER N N 113.570 0.300 1 933 84 84 ASP H H 8.126 0.030 1 934 84 84 ASP HA H 5.026 0.030 1 935 84 84 ASP HB2 H 3.106 0.030 2 936 84 84 ASP HB3 H 2.477 0.030 2 937 84 84 ASP C C 176.864 0.300 1 938 84 84 ASP CA C 51.950 0.300 1 939 84 84 ASP CB C 40.105 0.300 1 940 84 84 ASP N N 121.551 0.300 1 941 85 85 THR H H 8.378 0.030 1 942 85 85 THR HA H 3.816 0.030 1 943 85 85 THR HB H 4.453 0.030 1 944 85 85 THR HG2 H 1.448 0.030 1 945 85 85 THR C C 176.682 0.300 1 946 85 85 THR CA C 65.981 0.300 1 947 85 85 THR CB C 68.224 0.300 1 948 85 85 THR CG2 C 22.888 0.300 1 949 85 85 THR N N 116.087 0.300 1 950 86 86 VAL H H 7.955 0.030 1 951 86 86 VAL HA H 3.774 0.030 1 952 86 86 VAL HB H 2.265 0.030 1 953 86 86 VAL HG1 H 1.052 0.030 1 954 86 86 VAL HG2 H 0.962 0.030 1 955 86 86 VAL C C 178.462 0.300 1 956 86 86 VAL CA C 66.259 0.300 1 957 86 86 VAL CB C 31.238 0.300 1 958 86 86 VAL CG1 C 22.692 0.300 2 959 86 86 VAL CG2 C 21.081 0.300 2 960 86 86 VAL N N 124.024 0.300 1 961 87 87 LEU H H 7.770 0.030 1 962 87 87 LEU HA H 4.232 0.030 1 963 87 87 LEU HB2 H 1.890 0.030 2 964 87 87 LEU HB3 H 1.653 0.030 2 965 87 87 LEU HG H 1.568 0.030 1 966 87 87 LEU HD1 H 1.147 0.030 1 967 87 87 LEU HD2 H 1.024 0.030 1 968 87 87 LEU C C 178.947 0.300 1 969 87 87 LEU CA C 58.324 0.300 1 970 87 87 LEU CB C 40.810 0.300 1 971 87 87 LEU CG C 27.469 0.300 1 972 87 87 LEU CD1 C 22.984 0.300 1 973 87 87 LEU CD2 C 26.415 0.300 1 974 87 87 LEU N N 122.270 0.300 1 975 88 88 VAL H H 7.880 0.030 1 976 88 88 VAL HA H 3.564 0.030 1 977 88 88 VAL HB H 2.369 0.030 1 978 88 88 VAL HG1 H 0.982 0.030 1 979 88 88 VAL HG2 H 1.134 0.030 1 980 88 88 VAL C C 177.380 0.300 1 981 88 88 VAL CA C 67.528 0.300 1 982 88 88 VAL CB C 31.395 0.300 1 983 88 88 VAL CG1 C 21.745 0.300 1 984 88 88 VAL CG2 C 22.896 0.300 1 985 88 88 VAL N N 115.800 0.300 1 986 89 89 HIS H H 8.413 0.030 1 987 89 89 HIS HA H 3.932 0.030 1 988 89 89 HIS HB2 H 3.214 0.030 2 989 89 89 HIS HB3 H 2.725 0.030 2 990 89 89 HIS HD2 H 6.079 0.030 1 991 89 89 HIS C C 178.562 0.300 1 992 89 89 HIS CA C 60.452 0.300 1 993 89 89 HIS CB C 29.950 0.300 1 994 89 89 HIS CD2 C 118.478 0.300 1 995 89 89 HIS N N 120.437 0.300 1 996 90 90 ARG H H 9.009 0.030 1 997 90 90 ARG HA H 4.175 0.030 1 998 90 90 ARG HB2 H 2.445 0.030 2 999 90 90 ARG HB3 H 2.296 0.030 2 1000 90 90 ARG HG2 H 2.345 0.030 2 1001 90 90 ARG HG3 H 1.772 0.030 2 1002 90 90 ARG HD2 H 3.380 0.030 2 1003 90 90 ARG HD3 H 3.132 0.030 2 1004 90 90 ARG C C 180.898 0.300 1 1005 90 90 ARG CA C 60.010 0.300 1 1006 90 90 ARG CB C 32.933 0.300 1 1007 90 90 ARG CG C 27.061 0.300 1 1008 90 90 ARG CD C 45.104 0.300 1 1009 90 90 ARG N N 119.919 0.300 1 1010 91 91 VAL H H 8.822 0.030 1 1011 91 91 VAL HA H 3.847 0.030 1 1012 91 91 VAL HB H 2.135 0.030 1 1013 91 91 VAL HG1 H 0.588 0.030 1 1014 91 91 VAL HG2 H 0.785 0.030 1 1015 91 91 VAL C C 176.662 0.300 1 1016 91 91 VAL CA C 67.930 0.300 1 1017 91 91 VAL CB C 31.648 0.300 1 1018 91 91 VAL CG1 C 21.098 0.300 1 1019 91 91 VAL CG2 C 23.276 0.300 1 1020 91 91 VAL N N 122.082 0.300 1 1021 92 92 HIS H H 8.863 0.030 1 1022 92 92 HIS HA H 3.779 0.030 1 1023 92 92 HIS HB2 H 3.278 0.030 1 1024 92 92 HIS HB3 H 3.278 0.030 1 1025 92 92 HIS HD2 H 6.837 0.030 1 1026 92 92 HIS HE1 H 7.602 0.030 1 1027 92 92 HIS C C 176.733 0.300 1 1028 92 92 HIS CA C 63.207 0.300 1 1029 92 92 HIS CB C 31.717 0.300 1 1030 92 92 HIS CD2 C 116.203 0.300 1 1031 92 92 HIS CE1 C 138.635 0.300 1 1032 92 92 HIS N N 121.514 0.300 1 1033 93 93 SER H H 8.770 0.030 1 1034 93 93 SER HA H 4.269 0.030 1 1035 93 93 SER HB2 H 3.996 0.030 2 1036 93 93 SER HB3 H 3.923 0.030 2 1037 93 93 SER C C 176.946 0.300 1 1038 93 93 SER CA C 61.671 0.300 1 1039 93 93 SER CB C 63.361 0.300 1 1040 93 93 SER N N 111.582 0.300 1 1041 94 94 TYR H H 8.151 0.030 1 1042 94 94 TYR HA H 4.433 0.030 1 1043 94 94 TYR HB2 H 3.644 0.030 1 1044 94 94 TYR HB3 H 3.644 0.030 1 1045 94 94 TYR HD1 H 7.190 0.030 1 1046 94 94 TYR HD2 H 7.190 0.030 1 1047 94 94 TYR HE1 H 6.553 0.030 1 1048 94 94 TYR HE2 H 6.553 0.030 1 1049 94 94 TYR C C 177.532 0.300 1 1050 94 94 TYR CA C 61.470 0.300 1 1051 94 94 TYR CB C 38.314 0.300 1 1052 94 94 TYR CD1 C 133.523 0.300 1 1053 94 94 TYR CD2 C 133.523 0.300 1 1054 94 94 TYR CE1 C 118.543 0.300 1 1055 94 94 TYR CE2 C 118.543 0.300 1 1056 94 94 TYR N N 123.509 0.300 1 1057 95 95 LEU H H 8.432 0.030 1 1058 95 95 LEU HA H 3.577 0.030 1 1059 95 95 LEU HB2 H 1.811 0.030 2 1060 95 95 LEU HB3 H 1.019 0.030 2 1061 95 95 LEU HG H 2.103 0.030 1 1062 95 95 LEU HD1 H 0.819 0.030 1 1063 95 95 LEU HD2 H 0.810 0.030 1 1064 95 95 LEU C C 179.136 0.300 1 1065 95 95 LEU CA C 57.781 0.300 1 1066 95 95 LEU CB C 41.683 0.300 1 1067 95 95 LEU CG C 26.655 0.300 1 1068 95 95 LEU CD1 C 27.259 0.300 1 1069 95 95 LEU CD2 C 23.823 0.300 1 1070 95 95 LEU N N 121.264 0.300 1 1071 96 96 GLU H H 8.198 0.030 1 1072 96 96 GLU HA H 3.819 0.030 1 1073 96 96 GLU HB2 H 1.918 0.030 2 1074 96 96 GLU HB3 H 1.778 0.030 2 1075 96 96 GLU HG2 H 2.027 0.030 1 1076 96 96 GLU HG3 H 2.027 0.030 1 1077 96 96 GLU C C 180.376 0.300 1 1078 96 96 GLU CA C 59.669 0.300 1 1079 96 96 GLU CB C 30.224 0.300 1 1080 96 96 GLU CG C 37.730 0.300 1 1081 96 96 GLU N N 119.299 0.300 1 1082 97 97 ARG H H 8.791 0.030 1 1083 97 97 ARG HA H 4.003 0.030 1 1084 97 97 ARG HB2 H 1.919 0.030 2 1085 97 97 ARG HB3 H 1.712 0.030 2 1086 97 97 ARG HG2 H 1.563 0.030 2 1087 97 97 ARG HG3 H 1.407 0.030 2 1088 97 97 ARG HD2 H 3.130 0.030 1 1089 97 97 ARG HD3 H 3.130 0.030 1 1090 97 97 ARG C C 177.926 0.300 1 1091 97 97 ARG CA C 58.911 0.300 1 1092 97 97 ARG CB C 29.754 0.300 1 1093 97 97 ARG CG C 27.578 0.300 1 1094 97 97 ARG CD C 43.369 0.300 1 1095 97 97 ARG N N 121.744 0.300 1 1096 98 98 HIS H H 7.533 0.030 1 1097 98 98 HIS HA H 4.380 0.030 1 1098 98 98 HIS HB2 H 3.309 0.030 2 1099 98 98 HIS HB3 H 2.362 0.030 2 1100 98 98 HIS HD2 H 6.808 0.030 1 1101 98 98 HIS HE1 H 7.806 0.030 1 1102 98 98 HIS C C 174.610 0.300 1 1103 98 98 HIS CA C 57.209 0.300 1 1104 98 98 HIS CB C 28.427 0.300 1 1105 98 98 HIS CD2 C 123.126 0.300 1 1106 98 98 HIS CE1 C 137.716 0.300 1 1107 98 98 HIS N N 113.955 0.300 1 1108 99 99 GLY H H 7.598 0.030 1 1109 99 99 GLY HA2 H 3.881 0.030 2 1110 99 99 GLY HA3 H 3.736 0.030 2 1111 99 99 GLY C C 173.549 0.300 1 1112 99 99 GLY CA C 46.553 0.300 1 1113 99 99 GLY N N 107.447 0.300 1 1114 100 100 LEU H H 8.129 0.030 1 1115 100 100 LEU HA H 4.162 0.030 1 1116 100 100 LEU HB2 H 1.578 0.030 2 1117 100 100 LEU HB3 H 1.446 0.030 2 1118 100 100 LEU HG H 1.446 0.030 1 1119 100 100 LEU HD1 H 0.866 0.030 1 1120 100 100 LEU HD2 H 0.852 0.030 1 1121 100 100 LEU C C 175.975 0.300 1 1122 100 100 LEU CA C 56.035 0.300 1 1123 100 100 LEU CB C 43.466 0.300 1 1124 100 100 LEU CG C 28.116 0.300 1 1125 100 100 LEU CD1 C 26.024 0.300 1 1126 100 100 LEU CD2 C 23.684 0.300 1 1127 100 100 LEU N N 117.796 0.300 1 1128 101 101 ILE H H 6.561 0.030 1 1129 101 101 ILE HA H 2.416 0.030 1 1130 101 101 ILE HB H 0.772 0.030 1 1131 101 101 ILE HG12 H 0.447 0.030 2 1132 101 101 ILE HG13 H 0.120 0.030 2 1133 101 101 ILE HG2 H 0.628 0.030 1 1134 101 101 ILE HD1 H 0.204 0.030 1 1135 101 101 ILE C C 173.114 0.300 1 1136 101 101 ILE CA C 57.855 0.300 1 1137 101 101 ILE CB C 41.992 0.300 1 1138 101 101 ILE CG1 C 24.121 0.300 1 1139 101 101 ILE CG2 C 17.727 0.300 1 1140 101 101 ILE CD1 C 13.334 0.300 1 1141 101 101 ILE N N 104.448 0.300 1 1142 102 102 ASN H H 3.636 0.030 1 1143 102 102 ASN HA H 3.318 0.030 1 1144 102 102 ASN HB2 H 2.601 0.030 2 1145 102 102 ASN HB3 H 2.544 0.030 2 1146 102 102 ASN HD21 H 8.169 0.030 2 1147 102 102 ASN HD22 H 7.473 0.030 2 1148 102 102 ASN C C 172.295 0.300 1 1149 102 102 ASN CA C 54.244 0.300 1 1150 102 102 ASN CB C 35.802 0.300 1 1151 102 102 ASN N N 111.982 0.300 1 1152 102 102 ASN ND2 N 110.639 0.300 1 1153 103 103 PHE H H 6.328 0.030 1 1154 103 103 PHE HA H 4.924 0.030 1 1155 103 103 PHE HB2 H 3.071 0.030 2 1156 103 103 PHE HB3 H 2.639 0.030 2 1157 103 103 PHE HD1 H 6.792 0.030 1 1158 103 103 PHE HD2 H 6.792 0.030 1 1159 103 103 PHE HE1 H 7.323 0.030 1 1160 103 103 PHE HE2 H 7.323 0.030 1 1161 103 103 PHE HZ H 7.485 0.030 1 1162 103 103 PHE C C 175.066 0.300 1 1163 103 103 PHE CA C 55.786 0.300 1 1164 103 103 PHE CB C 41.405 0.300 1 1165 103 103 PHE CD1 C 132.328 0.300 1 1166 103 103 PHE CD2 C 132.328 0.300 1 1167 103 103 PHE CE1 C 131.457 0.300 1 1168 103 103 PHE CE2 C 131.457 0.300 1 1169 103 103 PHE CZ C 129.882 0.300 1 1170 103 103 PHE N N 115.512 0.300 1 1171 104 104 GLY H H 8.743 0.030 1 1172 104 104 GLY HA2 H 4.058 0.030 2 1173 104 104 GLY HA3 H 3.744 0.030 2 1174 104 104 GLY C C 173.963 0.300 1 1175 104 104 GLY CA C 45.510 0.300 1 1176 104 104 GLY N N 110.732 0.300 1 1177 105 105 ILE H H 7.988 0.030 1 1178 105 105 ILE HA H 4.122 0.030 1 1179 105 105 ILE HB H 1.770 0.030 1 1180 105 105 ILE HG12 H 1.292 0.030 2 1181 105 105 ILE HG13 H 0.998 0.030 2 1182 105 105 ILE HG2 H 0.763 0.030 1 1183 105 105 ILE HD1 H 0.731 0.030 1 1184 105 105 ILE C C 175.217 0.300 1 1185 105 105 ILE CA C 60.721 0.300 1 1186 105 105 ILE CB C 38.051 0.300 1 1187 105 105 ILE CG1 C 26.777 0.300 1 1188 105 105 ILE CG2 C 17.603 0.300 1 1189 105 105 ILE CD1 C 12.372 0.300 1 1190 105 105 ILE N N 120.333 0.300 1 1191 106 106 TYR H H 7.806 0.030 1 1192 106 106 TYR HA H 4.609 0.030 1 1193 106 106 TYR HB2 H 3.078 0.030 2 1194 106 106 TYR HB3 H 2.629 0.030 2 1195 106 106 TYR HD1 H 6.861 0.030 1 1196 106 106 TYR HD2 H 6.861 0.030 1 1197 106 106 TYR HE1 H 6.535 0.030 1 1198 106 106 TYR HE2 H 6.535 0.030 1 1199 106 106 TYR C C 174.560 0.300 1 1200 106 106 TYR CA C 56.617 0.300 1 1201 106 106 TYR CB C 39.178 0.300 1 1202 106 106 TYR CD1 C 133.439 0.300 1 1203 106 106 TYR CD2 C 133.439 0.300 1 1204 106 106 TYR CE1 C 117.483 0.300 1 1205 106 106 TYR CE2 C 117.483 0.300 1 1206 106 106 TYR N N 122.724 0.300 1 1207 107 107 LYS H H 8.225 0.030 1 1208 107 107 LYS HA H 4.232 0.030 1 1209 107 107 LYS HB2 H 1.815 0.030 2 1210 107 107 LYS HB3 H 1.734 0.030 2 1211 107 107 LYS HG2 H 1.326 0.030 1 1212 107 107 LYS HG3 H 1.326 0.030 1 1213 107 107 LYS HD2 H 1.647 0.030 1 1214 107 107 LYS HD3 H 1.647 0.030 1 1215 107 107 LYS HE2 H 2.951 0.030 1 1216 107 107 LYS HE3 H 2.951 0.030 1 1217 107 107 LYS C C 175.732 0.300 1 1218 107 107 LYS CA C 56.034 0.300 1 1219 107 107 LYS CB C 33.322 0.300 1 1220 107 107 LYS CG C 24.676 0.300 1 1221 107 107 LYS CD C 29.190 0.300 1 1222 107 107 LYS CE C 42.082 0.300 1 1223 107 107 LYS N N 123.133 0.300 1 1224 108 108 ARG H H 8.439 0.030 1 1225 108 108 ARG HA H 4.373 0.030 1 1226 108 108 ARG HB2 H 1.836 0.030 2 1227 108 108 ARG HB3 H 1.710 0.030 2 1228 108 108 ARG HG2 H 1.607 0.030 1 1229 108 108 ARG HG3 H 1.607 0.030 1 1230 108 108 ARG HD2 H 3.150 0.030 1 1231 108 108 ARG HD3 H 3.150 0.030 1 1232 108 108 ARG C C 176.268 0.300 1 1233 108 108 ARG CA C 56.138 0.300 1 1234 108 108 ARG CB C 30.770 0.300 1 1235 108 108 ARG CG C 27.637 0.300 1 1236 108 108 ARG CD C 43.270 0.300 1 1237 108 108 ARG N N 124.715 0.300 1 1238 109 109 ILE H H 8.287 0.030 1 1239 109 109 ILE HA H 4.185 0.030 1 1240 109 109 ILE HB H 1.807 0.030 1 1241 109 109 ILE HG12 H 1.478 0.030 2 1242 109 109 ILE HG13 H 1.252 0.030 2 1243 109 109 ILE HG2 H 0.896 0.030 1 1244 109 109 ILE HD1 H 0.875 0.030 1 1245 109 109 ILE C C 175.915 0.300 1 1246 109 109 ILE CA C 60.819 0.300 1 1247 109 109 ILE CB C 38.758 0.300 1 1248 109 109 ILE CG1 C 27.294 0.300 1 1249 109 109 ILE CG2 C 17.558 0.300 1 1250 109 109 ILE CD1 C 12.541 0.300 1 1251 109 109 ILE N N 122.702 0.300 1 1252 110 110 LYS H H 8.337 0.030 1 1253 110 110 LYS HA H 4.639 0.030 1 1254 110 110 LYS HB2 H 1.827 0.030 2 1255 110 110 LYS HB3 H 1.718 0.030 2 1256 110 110 LYS HG2 H 1.484 0.030 2 1257 110 110 LYS HG3 H 1.440 0.030 2 1258 110 110 LYS HD2 H 1.708 0.030 1 1259 110 110 LYS HD3 H 1.708 0.030 1 1260 110 110 LYS HE2 H 3.012 0.030 1 1261 110 110 LYS HE3 H 3.012 0.030 1 1262 110 110 LYS C C 174.127 0.300 1 1263 110 110 LYS CA C 53.949 0.300 1 1264 110 110 LYS CB C 32.924 0.300 1 1265 110 110 LYS CG C 24.716 0.300 1 1266 110 110 LYS CD C 29.391 0.300 1 1267 110 110 LYS CE C 42.140 0.300 1 1268 110 110 LYS N N 126.296 0.300 1 1269 111 111 PRO HA H 4.416 0.030 1 1270 111 111 PRO HB2 H 2.271 0.030 2 1271 111 111 PRO HB3 H 1.862 0.030 2 1272 111 111 PRO HD2 H 3.841 0.030 2 1273 111 111 PRO HD3 H 3.641 0.030 2 1274 111 111 PRO C C 176.683 0.300 1 1275 111 111 PRO CA C 62.712 0.300 1 1276 111 111 PRO CB C 32.186 0.300 1 1277 111 111 PRO CG C 27.290 0.300 1 1278 111 111 PRO CD C 50.767 0.300 1 1279 112 112 LEU H H 8.385 0.030 1 1280 112 112 LEU HA H 4.554 0.030 1 1281 112 112 LEU HB2 H 1.581 0.030 2 1282 112 112 LEU HB3 H 1.551 0.030 2 1283 112 112 LEU HG H 1.720 0.030 1 1284 112 112 LEU HD1 H 0.942 0.030 1 1285 112 112 LEU HD2 H 0.928 0.030 1 1286 112 112 LEU C C 175.571 0.300 1 1287 112 112 LEU CA C 53.154 0.300 1 1288 112 112 LEU CB C 41.641 0.300 1 1289 112 112 LEU CG C 27.165 0.300 1 1290 112 112 LEU CD1 C 25.216 0.300 2 1291 112 112 LEU CD2 C 23.354 0.300 2 1292 112 112 LEU N N 123.983 0.300 1 1293 113 113 PRO HA H 4.480 0.030 1 1294 113 113 PRO HB2 H 2.293 0.030 2 1295 113 113 PRO HB3 H 1.902 0.030 2 1296 113 113 PRO HG2 H 2.026 0.030 1 1297 113 113 PRO HG3 H 2.026 0.030 1 1298 113 113 PRO HD2 H 3.850 0.030 2 1299 113 113 PRO HD3 H 3.646 0.030 2 1300 113 113 PRO C C 176.977 0.300 1 1301 113 113 PRO CA C 63.065 0.300 1 1302 113 113 PRO CB C 32.068 0.300 1 1303 113 113 PRO CG C 27.428 0.300 1 1304 113 113 PRO CD C 50.576 0.300 1 1305 114 114 THR H H 8.212 0.030 1 1306 114 114 THR HA H 4.276 0.030 1 1307 114 114 THR HB H 4.167 0.030 1 1308 114 114 THR HG2 H 1.208 0.030 1 1309 114 114 THR C C 174.469 0.300 1 1310 114 114 THR CA C 61.803 0.300 1 1311 114 114 THR CB C 69.995 0.300 1 1312 114 114 THR CG2 C 21.676 0.300 1 1313 114 114 THR N N 115.081 0.300 1 1314 115 115 LYS H H 8.330 0.030 1 1315 115 115 LYS C C 176.369 0.300 1 1316 115 115 LYS CA C 56.255 0.300 1 1317 115 115 LYS CB C 33.233 0.300 1 1318 115 115 LYS N N 124.255 0.300 1 1319 116 116 LYS HA H 4.373 0.030 1 1320 116 116 LYS HB2 H 1.794 0.030 1 1321 116 116 LYS HB3 H 1.794 0.030 1 1322 116 116 LYS HG2 H 1.419 0.030 1 1323 116 116 LYS HG3 H 1.419 0.030 1 1324 116 116 LYS HD2 H 1.662 0.030 1 1325 116 116 LYS HD3 H 1.662 0.030 1 1326 116 116 LYS HE2 H 2.980 0.030 1 1327 116 116 LYS HE3 H 2.980 0.030 1 1328 116 116 LYS C C 176.775 0.300 1 1329 116 116 LYS CA C 56.314 0.300 1 1330 116 116 LYS CB C 33.110 0.300 1 1331 116 116 LYS CG C 24.676 0.300 1 1332 116 116 LYS CD C 29.148 0.300 1 1333 116 116 LYS CE C 42.151 0.300 1 1334 117 117 THR H H 8.253 0.030 1 1335 117 117 THR HA H 4.349 0.030 1 1336 117 117 THR HB H 4.223 0.030 1 1337 117 117 THR HG2 H 1.204 0.030 1 1338 117 117 THR C C 175.015 0.300 1 1339 117 117 THR CA C 61.905 0.300 1 1340 117 117 THR CB C 69.888 0.300 1 1341 117 117 THR CG2 C 21.580 0.300 1 1342 117 117 THR N N 115.944 0.300 1 1343 118 118 GLY H H 8.465 0.030 1 1344 118 118 GLY C C 174.127 0.300 1 1345 118 118 GLY CA C 45.305 0.300 1 1346 118 118 GLY N N 111.486 0.300 1 stop_ save_