data_4899 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; SMN Tudor Domain Structure and its Interaction with the Sm Proteins ; _BMRB_accession_number 4899 _BMRB_flat_file_name bmr4899.str _Entry_type original _Submission_date 2000-11-15 _Accession_date 2000-11-15 _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 Selenko Philipp . . 2 Sprangers Remco . . 3 Stier Gunter . . 4 Buehler Dirk . . 5 Fischer Utz . . 6 Sattler Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 313 "13C chemical shifts" 188 "15N chemical shifts" 61 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-05-03 original author . stop_ _Original_release_date 2001-05-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'SMN Tudor Domain Structure and its Interaction with the Sm Proteins' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20577270 _PubMed_ID 11135666 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Selenko Philipp . . 2 Sprangers Remco . . 3 Stier Gunter . . 4 Buehler Dirk . . 5 Fischer Utz . . 6 Sattler Michael . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_volume 8 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 27 _Page_last 31 _Year 2001 _Details . loop_ _Keyword SMA 'Sm interacting protein' SMN splicing stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code 96088118 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J Biomol NMR.' _Journal_name_full . _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full . _Citation_title ; The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. ; _Citation_status . _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bartels C. . . 2 Xia T.-H. . . 3 Billeter Martin . . 4 Guntert Peter . . 5 Wuthrich Kurt . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full . _Journal_volume 6 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1 _Page_last 10 _Year 1995 _Details . loop_ _Keyword software 'spectrum analysis' stop_ save_ save_ref_3 _Saveframe_category citation _Citation_full . _Citation_title ; Crystallography & NMR system: A new software suite for macromolecular structure determination. ; _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code 98437621 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brunger A. T. . 2 Adams P. D. . 3 Clore G. M. . 4 DeLano W. L. . 5 Gros P. . . 6 Grosse-Kunstleve R. W. . 7 Jiang J. S. . 8 Kuszewski J. . . 9 Nilges M. . . 10 Pannu N. S. . 11 Read R. J. . 12 Rice L. M. . 13 Simonson T. . . 14 Warren G. L. . stop_ _Journal_abbreviation 'Acta Crystallogr., Sect. D: Biol. Crystallogr.' _Journal_name_full . _Journal_volume 54 _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 905 _Page_last 921 _Year 1998 _Details . loop_ _Keyword 'Structure analysis' 'Structure calculation' stop_ save_ ################################## # Molecular system description # ################################## save_system_tudor _Saveframe_category molecular_system _Mol_system_name 'SMN tudor domain' _Abbreviation_common tudor _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label tudor $tudor stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'Involved in splicing' 'Mutations cause SMA' 'Sm protein interaction' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_tudor _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Survival of Motor Neurons protein' _Abbreviation_common SMN _Molecular_mass 10049.0 _Mol_thiol_state 'all free' _Details ; only residues 90 to 145 are folded. a n terminal H6-GST tag has been cleaved of with TEV construct contains residues 82 to 169 of the SMN protein ; ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; GAMKKNTAASLQQWKVGDKC SAIWSEDGCIYPATIASIDF KRETCVVVYTGYGNREEQNL SDLLSPICEVANNIEQNAQE NENESQVSTDE ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 MET 4 LYS 5 LYS 6 ASN 7 THR 8 ALA 9 ALA 10 SER 11 LEU 12 GLN 13 GLN 14 TRP 15 LYS 16 VAL 17 GLY 18 ASP 19 LYS 20 CYS 21 SER 22 ALA 23 ILE 24 TRP 25 SER 26 GLU 27 ASP 28 GLY 29 CYS 30 ILE 31 TYR 32 PRO 33 ALA 34 THR 35 ILE 36 ALA 37 SER 38 ILE 39 ASP 40 PHE 41 LYS 42 ARG 43 GLU 44 THR 45 CYS 46 VAL 47 VAL 48 VAL 49 TYR 50 THR 51 GLY 52 TYR 53 GLY 54 ASN 55 ARG 56 GLU 57 GLU 58 GLN 59 ASN 60 LEU 61 SER 62 ASP 63 LEU 64 LEU 65 SER 66 PRO 67 ILE 68 CYS 69 GLU 70 VAL 71 ALA 72 ASN 73 ASN 74 ILE 75 GLU 76 GLN 77 ASN 78 ALA 79 GLN 80 GLU 81 ASN 82 GLU 83 ASN 84 GLU 85 SER 86 GLN 87 VAL 88 SER 89 THR 90 ASP 91 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 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 18005 A 70.33 64 100.00 100.00 2.17e-39 BMRB 18007 A 70.33 64 100.00 100.00 2.17e-39 PDB 1G5V "Solution Structure Of The Tudor Domain Of The Human Smn Protein" 96.70 88 100.00 100.00 2.01e-56 PDB 1MHN "High Resolution Crystal Structure Of The Smn Tudor Domain" 64.84 59 100.00 100.00 6.60e-36 PDB 4A4E "Solution Structure Of Smn Tudor Domain In Complex With Symmetrically Dimethylated Arginine" 70.33 64 100.00 100.00 2.17e-39 PDB 4A4G "Solution Structure Of Smn Tudor Domain In Complex With Asymmetrically Dimethylated Arginine" 70.33 64 100.00 100.00 2.17e-39 PDB 4QQ6 "Crystal Structure Of Tudor Domain Of Smn1 In Complex With A Small Organic Molecule" 72.53 67 100.00 100.00 8.42e-41 DBJ BAF82358 "unnamed protein product [Homo sapiens]" 98.90 282 97.78 98.89 7.37e-56 DBJ BAJ21116 "survival of motor neuron 1, telomeric [synthetic construct]" 98.90 294 97.78 98.89 1.47e-55 EMBL CAH89989 "hypothetical protein [Pongo abelii]" 98.90 294 97.78 98.89 1.47e-55 GB AAA64505 "putative open reading frame; duplicate of the functional spinal muscular atrophy gene, cDNA clone BCD514, GenBank Accession Num" 98.90 293 97.78 98.89 1.48e-55 GB AAA66242 "survival motor neuron [Homo sapiens]" 98.90 294 97.78 98.89 1.47e-55 GB AAC50473 "survival motor neuron [Homo sapiens]" 98.90 294 97.78 98.89 1.47e-55 GB AAC52048 "survival motor neuron protein SMN [Homo sapiens]" 98.90 294 97.78 98.89 1.47e-55 GB AAC62262 "survival of motor neuron 1 product [Homo sapiens]" 98.90 294 97.78 98.89 1.47e-55 REF NP_000335 "survival motor neuron protein isoform d [Homo sapiens]" 98.90 294 97.78 98.89 1.47e-55 REF NP_001124942 "survival motor neuron protein [Pongo abelii]" 98.90 294 97.78 98.89 1.47e-55 REF NP_001284644 "survival motor neuron protein isoform a [Homo sapiens]" 98.90 282 97.78 98.89 7.37e-56 REF NP_059107 "survival motor neuron protein isoform d [Homo sapiens]" 98.90 294 97.78 98.89 1.47e-55 REF NP_075012 "survival motor neuron protein isoform b [Homo sapiens]" 98.90 262 97.78 98.89 1.89e-55 SP Q16637 "RecName: Full=Survival motor neuron protein; AltName: Full=Component of gems 1; AltName: Full=Gemin-1 [Homo sapiens]" 98.90 294 97.78 98.89 1.47e-55 SP Q5RE18 "RecName: Full=Survival motor neuron protein [Pongo abelii]" 98.90 294 97.78 98.89 1.47e-55 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $tudor 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_type _Vector_name $tudor 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET9d 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 $tudor 1.0 mM '[U-100% 15N]' 'sodium chloride' 20 mM . 'phosphate buffer' 30 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $tudor 1.0 mM '[U-100% 13C; U-100% 15N]' 'sodium chloride' 20 mM . 'phosphate buffer' 30 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $tudor 1.0 mM '[U-100% 13C; U-100% 15N]' 'sodium chloride' 20 mM . 'phosphate buffer' 30 mM . D2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name xwinnmr _Version 2.6 loop_ _Task 'recording experiments' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'processing spectra' stop_ _Details . _Citation_label $ref_1 save_ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Task 'chemical shift assignment' stop_ _Details . _Citation_label $ref_2 save_ save_CNS _Saveframe_category software _Name CNS _Version . loop_ _Task 'structure calculations' stop_ _Details . _Citation_label $ref_3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_CBCANH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_H(C)CH_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 'H(C)CH TOCSY' _Sample_label . save_ save_CCH_TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name 'CCH TOCSY' _Sample_label . save_ save_15N_edited_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '15N edited NOESY' _Sample_label . save_ save_13C_edited_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '13C edited NOESY' _Sample_label . save_ save_IPAP_(dipolar_couplings)_9 _Saveframe_category NMR_applied_experiment _Experiment_name 'IPAP (dipolar couplings)' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Cond_sample_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0 n/a pressure 1 . atm temperature 295 2 K stop_ save_ save_Cond_sample_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0 n/a pressure 1 . atm temperature 295 2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details 'Wishart, et al. (1995), J Biol NMR, 6, 135-140' 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 protons ppm 0.0 . indirect . . . 0.251449530 H2O H 1 protons ppm 4.81 internal direct . . . . DSS N 15 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; 78 must be added to every residue number in the chemical shift file to get the residue number in the protein ; loop_ _Sample_label $sample_1 $sample_2 stop_ _Sample_conditions_label $Cond_sample_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name tudor _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 . 12 GLN N N 116.636 0.02 1 2 . 12 GLN H H 8.047 0.02 1 3 . 12 GLN CA C 55.500 0.02 1 4 . 12 GLN HA H 4.164 0.02 1 5 . 12 GLN CB C 28.620 0.02 1 6 . 12 GLN HB2 H 1.957 0.02 1 7 . 12 GLN HB3 H 1.961 0.004 1 8 . 12 GLN CG C 32.585 0.02 1 9 . 12 GLN HG2 H 1.694 0.006 2 10 . 12 GLN NE2 N 109.698 0.02 1 11 . 12 GLN HE21 H 7.381 0.02 1 12 . 12 GLN HE22 H 6.803 0.02 1 13 . 13 GLN N N 119.051 0.02 1 14 . 13 GLN H H 8.201 0.02 1 15 . 13 GLN CA C 55.135 0.02 1 16 . 13 GLN HA H 4.299 0.02 1 17 . 13 GLN CB C 28.724 0.02 1 18 . 13 GLN HB2 H 2.125 0.007 1 19 . 13 GLN HB3 H 1.846 0.002 1 20 . 13 GLN CG C 33.105 0.02 1 21 . 13 GLN HG2 H 1.939 0.02 1 22 . 13 GLN HG3 H 1.950 0.02 1 23 . 13 GLN NE2 N 109.945 0.02 1 24 . 13 GLN HE21 H 7.614 0.02 1 25 . 13 GLN HE22 H 6.899 0.02 1 26 . 14 TRP N N 120.015 0.02 1 27 . 14 TRP H H 7.821 0.02 1 28 . 14 TRP CA C 56.510 0.02 1 29 . 14 TRP HA H 4.832 0.001 1 30 . 14 TRP CB C 31.890 0.02 1 31 . 14 TRP HB2 H 3.073 0.007 1 32 . 14 TRP HB3 H 2.857 0.02 1 33 . 14 TRP CD1 C 126.9198 0.02 1 34 . 14 TRP CE3 C 121.7428 0.02 1 35 . 14 TRP NE1 N 125.757 0.02 1 36 . 14 TRP HD1 H 7.259 0.003 1 37 . 14 TRP HE3 H 7.974 0.001 1 38 . 14 TRP CZ3 C 121.7428 0.02 3 39 . 14 TRP CZ2 C 113.9778 0.02 3 40 . 14 TRP HE1 H 10.158 0.02 1 41 . 14 TRP HZ3 H 7.305 0.007 1 42 . 14 TRP CH2 C 124.3318 0.02 1 43 . 14 TRP HZ2 H 7.101 0.02 1 44 . 14 TRP HH2 H 7.105 0.003 1 45 . 15 LYS N N 117.489 0.02 1 46 . 15 LYS H H 9.015 0.02 1 47 . 15 LYS CA C 54.015 0.02 1 48 . 15 LYS HA H 4.726 0.02 1 49 . 15 LYS CB C 35.360 0.02 1 50 . 15 LYS HB2 H 1.881 0.02 1 51 . 15 LYS HB3 H 1.806 0.02 1 52 . 15 LYS CG C 23.235 0.02 1 53 . 15 LYS HG2 H 1.411 0.02 1 54 . 15 LYS HG3 H 1.653 0.001 1 55 . 15 LYS CD C 28.726 0.02 1 56 . 15 LYS HD2 H 1.768 0.02 2 57 . 15 LYS CE C 41.490 0.02 1 58 . 15 LYS HE2 H 3.106 0.02 2 59 . 16 VAL N N 118.081 0.02 1 60 . 16 VAL H H 8.567 0.02 1 61 . 16 VAL CA C 65.800 0.02 1 62 . 16 VAL HA H 3.203 0.001 1 63 . 16 VAL CB C 30.881 0.02 1 64 . 16 VAL HB H 1.935 0.004 1 65 . 16 VAL HG1 H 1.017 0.002 1 66 . 16 VAL HG2 H 0.917 0.002 1 67 . 16 VAL CG1 C 23.383 0.02 1 68 . 16 VAL CG2 C 21.083 0.02 1 69 . 17 GLY N N 113.949 0.02 1 70 . 17 GLY H H 9.036 0.02 1 71 . 17 GLY CA C 44.149 0.02 1 72 . 17 GLY HA2 H 4.486 0.006 1 73 . 17 GLY HA3 H 3.598 0.007 1 74 . 18 ASP N N 118.309 0.02 1 75 . 18 ASP H H 8.146 0.02 1 76 . 18 ASP CA C 55.338 0.02 1 77 . 18 ASP HA H 4.709 0.006 1 78 . 18 ASP CB C 41.314 0.02 1 79 . 18 ASP HB2 H 3.287 0.02 1 80 . 18 ASP HB3 H 2.983 0.02 1 81 . 19 LYS N N 116.386 0.02 1 82 . 19 LYS H H 8.459 0.02 1 83 . 19 LYS CA C 55.590 0.02 1 84 . 19 LYS HA H 4.951 0.02 1 85 . 19 LYS CB C 32.659 0.02 1 86 . 19 LYS HB2 H 2.188 0.005 1 87 . 19 LYS HB3 H 1.850 0.02 1 88 . 19 LYS CG C 25.164 0.02 1 89 . 19 LYS HG2 H 1.791 0.02 1 90 . 19 LYS HG3 H 1.617 0.02 1 91 . 19 LYS CD C 28.801 0.02 1 92 . 19 LYS HD2 H 1.803 0.02 2 93 . 19 LYS CE C 41.935 0.02 1 94 . 19 LYS HE2 H 3.063 0.02 2 95 . 20 CYS N N 112.897 0.02 1 96 . 20 CYS H H 8.946 0.02 1 97 . 20 CYS CA C 55.664 0.02 1 98 . 20 CYS HA H 5.064 0.001 1 99 . 20 CYS CB C 31.769 0.02 1 100 . 20 CYS HB2 H 2.858 0.001 1 101 . 20 CYS HB3 H 2.854 0.001 1 102 . 21 SER N N 113.068 0.02 1 103 . 21 SER H H 8.594 0.02 1 104 . 21 SER CA C 58.484 0.02 1 105 . 21 SER HA H 5.254 0.003 1 106 . 21 SER CB C 64.868 0.02 1 107 . 21 SER HB2 H 3.694 0.006 1 108 . 21 SER HB3 H 3.561 0.002 1 109 . 22 ALA N N 120.873 0.02 1 110 . 22 ALA H H 9.035 0.02 1 111 . 22 ALA CA C 50.446 0.02 1 112 . 22 ALA HA H 4.866 0.001 1 113 . 22 ALA HB H 1.226 0.002 1 114 . 22 ALA CB C 21.897 0.02 1 115 . 23 ILE N N 118.748 0.02 1 116 . 23 ILE H H 8.993 0.02 1 117 . 23 ILE CA C 60.413 0.02 1 118 . 23 ILE HA H 4.436 0.02 1 119 . 23 ILE CB C 37.854 0.02 1 120 . 23 ILE HB H 1.841 0.02 1 121 . 23 ILE HG2 H 0.668 0.02 1 122 . 23 ILE CG2 C 17.150 0.02 1 123 . 23 ILE CG1 C 28.875 0.02 1 124 . 23 ILE HG12 H 1.566 0.002 2 125 . 23 ILE HD1 H 0.901 0.02 1 126 . 23 ILE CD1 C 13.355 0.02 1 127 . 24 TRP N N 129.869 0.02 1 128 . 24 TRP H H 9.101 0.02 1 129 . 24 TRP CA C 54.254 0.02 1 130 . 24 TRP HA H 5.398 0.02 1 131 . 24 TRP CB C 29.404 0.02 1 132 . 24 TRP HB2 H 3.787 0.006 1 133 . 24 TRP HB3 H 2.506 0.02 1 134 . 24 TRP CD1 C 124.8488 0.02 1 135 . 24 TRP CE3 C 121.2248 0.02 1 136 . 24 TRP NE1 N 125.098 0.02 1 137 . 24 TRP HD1 H 7.669 0.001 1 138 . 24 TRP HE3 H 7.378 0.02 1 139 . 24 TRP CZ3 C 121.2248 0.02 1 140 . 24 TRP CZ2 C 113.9778 0.02 1 141 . 24 TRP HE1 H 9.992 0.02 1 142 . 24 TRP HZ3 H 6.618 0.02 1 143 . 24 TRP CH2 C 124.3318 0.02 1 144 . 24 TRP HZ2 H 7.118 0.003 1 145 . 24 TRP HH2 H 6.851 0.003 1 146 . 25 SER N N 124.182 0.02 1 147 . 25 SER H H 9.552 0.02 1 148 . 25 SER CA C 61.106 0.02 1 149 . 25 SER HA H 3.977 0.007 1 150 . 25 SER CB C 61.933 0.02 1 151 . 25 SER HB2 H 3.781 0.006 1 152 . 25 SER HB3 H 3.781 0.006 1 153 . 26 GLU N N 115.353 0.02 1 154 . 26 GLU H H 5.460 0.02 1 155 . 26 GLU CA C 58.039 0.02 1 156 . 26 GLU HA H 3.614 0.02 1 157 . 26 GLU CB C 27.910 0.02 1 158 . 26 GLU HB2 H 0.390 0.02 1 159 . 26 GLU HB3 H -0.049 0.006 1 160 . 26 GLU CG C 35.405 0.02 1 161 . 26 GLU HG2 H 1.632 0.006 1 162 . 26 GLU HG3 H 1.546 0.006 1 163 . 27 ASP N N 109.745 0.02 1 164 . 27 ASP H H 6.583 0.02 1 165 . 27 ASP CA C 52.261 0.02 1 166 . 27 ASP HA H 4.701 0.02 1 167 . 27 ASP CB C 42.108 0.02 1 168 . 27 ASP HB2 H 3.086 0.02 1 169 . 27 ASP HB3 H 2.316 0.02 1 170 . 28 GLY N N 107.604 0.02 1 171 . 28 GLY H H 8.820 0.02 1 172 . 28 GLY CA C 46.231 0.02 1 173 . 28 GLY HA2 H 4.038 0.006 1 174 . 28 GLY HA3 H 3.659 0.007 1 175 . 29 CYS N N 117.698 0.02 1 176 . 29 CYS H H 8.779 0.02 1 177 . 29 CYS CA C 58.550 0.02 1 178 . 29 CYS HA H 4.598 0.007 1 179 . 29 CYS CB C 28.448 0.02 1 180 . 29 CYS HB2 H 3.262 0.02 1 181 . 29 CYS HB3 H 2.641 0.02 1 182 . 30 ILE N N 118.170 0.02 1 183 . 30 ILE H H 8.084 0.02 1 184 . 30 ILE CA C 61.327 0.02 1 185 . 30 ILE HA H 4.407 0.02 1 186 . 30 ILE CB C 38.759 0.02 1 187 . 30 ILE HB H 1.514 0.02 1 188 . 30 ILE HG2 H 0.789 0.001 1 189 . 30 ILE CG2 C 18.708 0.02 1 190 . 30 ILE CG1 C 29.073 0.02 1 191 . 30 ILE HG12 H 1.651 0.02 1 192 . 30 ILE HG13 H 0.794 0.02 1 193 . 30 ILE HD1 H 0.860 0.02 1 194 . 30 ILE CD1 C 13.614 0.02 1 195 . 31 TYR N N 123.821 0.02 1 196 . 31 TYR H H 9.324 0.02 1 197 . 31 TYR CA C 55.993 0.02 1 198 . 31 TYR HA H 5.072 0.004 1 199 . 31 TYR CB C 42.347 0.02 1 200 . 31 TYR HB2 H 3.344 0.001 1 201 . 31 TYR HB3 H 2.776 0.02 1 202 . 31 TYR CD1 C 133.1318 0.02 3 203 . 31 TYR HD1 H 7.142 0.003 3 204 . 31 TYR CE1 C 118.1188 0.02 3 205 . 31 TYR HE1 H 7.349 0.004 3 206 . 32 PRO CD C 50.840 0.02 1 207 . 32 PRO CA C 62.538 0.02 1 208 . 32 PRO HA H 4.976 0.001 1 209 . 32 PRO CB C 32.511 0.02 1 210 . 32 PRO HB2 H 2.599 0.02 1 211 . 32 PRO HB3 H 2.133 0.006 1 212 . 32 PRO CG C 27.242 0.02 1 213 . 32 PRO HG2 H 2.369 0.02 1 214 . 32 PRO HG3 H 2.208 0.001 1 215 . 32 PRO HD2 H 4.158 0.02 1 216 . 32 PRO HD3 H 4.009 0.006 1 217 . 33 ALA N N 122.141 0.02 1 218 . 33 ALA H H 8.968 0.02 1 219 . 33 ALA CA C 50.889 0.02 1 220 . 33 ALA HA H 5.218 0.003 1 221 . 33 ALA HB H 0.915 0.002 1 222 . 33 ALA CB C 23.161 0.02 1 223 . 34 THR N N 108.216 0.02 1 224 . 34 THR H H 8.044 0.02 1 225 . 34 THR CA C 59.949 0.02 1 226 . 34 THR HA H 5.208 0.001 1 227 . 34 THR CB C 71.598 0.02 1 228 . 34 THR HB H 3.682 0.02 1 229 . 34 THR HG2 H 1.104 0.001 1 230 . 34 THR CG2 C 21.528 0.02 1 231 . 35 ILE N N 119.503 0.02 1 232 . 35 ILE H H 8.306 0.02 1 233 . 35 ILE CA C 63.060 0.02 1 234 . 35 ILE HA H 3.945 0.001 1 235 . 35 ILE CB C 37.883 0.02 1 236 . 35 ILE HB H 1.929 0.02 1 237 . 35 ILE HG2 H 0.647 0.001 1 238 . 35 ILE CG2 C 18.783 0.02 1 239 . 35 ILE CG1 C 27.603 0.010 1 240 . 35 ILE HG12 H 1.621 0.001 1 241 . 35 ILE HG13 H 0.552 0.02 1 242 . 35 ILE HD1 H 0.609 0.005 1 243 . 35 ILE CD1 C 14.701 0.02 1 244 . 36 ALA N N 131.347 0.02 1 245 . 36 ALA H H 9.571 0.02 1 246 . 36 ALA CA C 53.024 0.02 1 247 . 36 ALA HA H 4.463 0.003 1 248 . 36 ALA HB H 1.277 0.002 1 249 . 36 ALA CB C 19.819 0.02 1 250 . 37 SER N N 107.079 0.02 1 251 . 37 SER H H 7.627 0.02 1 252 . 37 SER CA C 57.343 0.02 1 253 . 37 SER HA H 4.420 0.002 1 254 . 37 SER CB C 63.245 0.02 1 255 . 37 SER HB2 H 3.768 0.006 1 256 . 37 SER HB3 H 3.666 0.006 1 257 . 38 ILE N N 117.664 0.02 1 258 . 38 ILE H H 8.462 0.02 1 259 . 38 ILE CA C 61.244 0.02 1 260 . 38 ILE HA H 4.203 0.02 1 261 . 38 ILE CB C 42.678 0.02 1 262 . 38 ILE HB H 1.051 0.02 1 263 . 38 ILE HG2 H 0.083 0.003 1 264 . 38 ILE CG2 C 15.814 0.02 1 265 . 38 ILE CG1 C 29.097 0.02 1 266 . 38 ILE HG12 H 1.237 0.02 1 267 . 38 ILE HG13 H 0.507 0.02 1 268 . 38 ILE HD1 H 0.707 0.002 1 269 . 38 ILE CD1 C 14.033 0.02 1 270 . 39 ASP N N 124.375 0.02 1 271 . 39 ASP H H 8.703 0.02 1 272 . 39 ASP CA C 51.715 0.02 1 273 . 39 ASP HA H 4.791 0.02 1 274 . 39 ASP CB C 40.590 0.02 1 275 . 39 ASP HB2 H 3.192 0.02 1 276 . 39 ASP HB3 H 2.210 0.02 1 277 . 40 PHE N N 120.138 0.02 1 278 . 40 PHE H H 8.710 0.02 1 279 . 40 PHE CA C 61.687 0.02 1 280 . 40 PHE HA H 4.142 0.02 1 281 . 40 PHE CB C 38.678 0.02 1 282 . 40 PHE HB2 H 3.331 0.02 1 283 . 40 PHE HB3 H 2.977 0.02 1 284 . 40 PHE CD1 C 131.5788 0.02 3 285 . 40 PHE HD1 H 7.410 0.02 3 286 . 40 PHE CE1 C 131.5788 0.02 3 287 . 40 PHE HE1 H 7.487 0.02 3 288 . 40 PHE CZ C 130.5438 0.02 1 289 . 40 PHE HZ H 7.495 0.001 1 290 . 41 LYS N N 116.544 0.02 1 291 . 41 LYS H H 8.322 0.02 1 292 . 41 LYS CA C 58.484 0.02 1 293 . 41 LYS HA H 4.294 0.02 1 294 . 41 LYS CB C 31.695 0.02 1 295 . 41 LYS HB2 H 2.020 0.02 1 296 . 41 LYS HB3 H 2.022 0.002 1 297 . 41 LYS CG C 24.645 0.02 1 298 . 41 LYS HG2 H 1.578 0.02 1 299 . 41 LYS HG3 H 1.465 0.006 1 300 . 41 LYS CD C 28.726 0.02 1 301 . 41 LYS HD2 H 1.760 0.006 2 302 . 41 LYS CE C 41.497 0.02 1 303 . 41 LYS HE2 H 3.061 0.02 2 304 . 42 ARG N N 114.036 0.02 1 305 . 42 ARG H H 7.623 0.02 1 306 . 42 ARG CA C 56.183 0.02 1 307 . 42 ARG HA H 4.241 0.02 1 308 . 42 ARG CB C 30.878 0.02 1 309 . 42 ARG HB2 H 1.957 0.002 1 310 . 42 ARG HB3 H 1.469 0.003 1 311 . 42 ARG CG C 28.059 0.02 1 312 . 42 ARG HG2 H 1.694 0.001 1 313 . 42 ARG HG3 H 1.547 0.002 1 314 . 42 ARG CD C 42.974 0.02 1 315 . 42 ARG HD2 H 3.225 0.003 1 316 . 42 ARG HD3 H 3.167 0.02 1 317 . 43 GLU N N 112.530 0.02 1 318 . 43 GLU H H 8.161 0.02 1 319 . 43 GLU CA C 57.519 0.02 1 320 . 43 GLU HA H 3.754 0.006 1 321 . 43 GLU CB C 26.203 0.02 1 322 . 43 GLU HB2 H 2.501 0.006 1 323 . 43 GLU HB3 H 2.215 0.006 1 324 . 43 GLU CG C 36.592 0.02 1 325 . 43 GLU HG2 H 2.221 0.006 1 326 . 43 GLU HG3 H 1.561 0.006 1 327 . 44 THR N N 107.014 0.02 1 328 . 44 THR H H 7.991 0.02 1 329 . 44 THR CA C 58.945 0.02 1 330 . 44 THR HA H 5.135 0.02 1 331 . 44 THR CB C 72.502 0.02 1 332 . 44 THR HB H 4.180 0.02 1 333 . 44 THR HG2 H 1.107 0.006 1 334 . 44 THR CG2 C 21.009 0.02 1 335 . 45 CYS N N 111.585 0.02 1 336 . 45 CYS H H 9.450 0.02 1 337 . 45 CYS CA C 54.874 0.02 1 338 . 45 CYS HA H 5.186 0.001 1 339 . 45 CYS CB C 32.168 0.02 1 340 . 45 CYS HB2 H 3.123 0.005 1 341 . 45 CYS HB3 H 2.673 0.001 1 342 . 46 VAL N N 116.236 0.02 1 343 . 46 VAL H H 8.045 0.02 1 344 . 46 VAL CA C 61.605 0.02 1 345 . 46 VAL HA H 4.552 0.02 1 346 . 46 VAL CB C 32.520 0.02 1 347 . 46 VAL HB H 1.924 0.02 1 348 . 46 VAL HG1 H 0.711 0.003 1 349 . 46 VAL HG2 H 0.797 0.006 1 350 . 46 VAL CG1 C 20.789 0.02 1 351 . 46 VAL CG2 C 21.157 0.02 1 352 . 47 VAL N N 116.632 0.02 1 353 . 47 VAL H H 8.631 0.02 1 354 . 47 VAL CA C 57.742 0.02 1 355 . 47 VAL HA H 5.009 0.001 1 356 . 47 VAL CB C 33.546 0.02 1 357 . 47 VAL HB H 1.386 0.02 1 358 . 47 VAL HG1 H 0.473 0.02 1 359 . 47 VAL HG2 H 0.259 0.02 1 360 . 47 VAL CG1 C 22.716 0.02 1 361 . 47 VAL CG2 C 17.521 0.02 1 362 . 48 VAL N N 116.097 0.02 1 363 . 48 VAL H H 8.423 0.02 1 364 . 48 VAL CA C 59.236 0.02 1 365 . 48 VAL HA H 4.471 0.02 1 366 . 48 VAL CB C 33.126 0.02 1 367 . 48 VAL HB H 1.735 0.02 1 368 . 48 VAL HG1 H 0.723 0.02 1 369 . 48 VAL HG2 H 0.721 0.001 1 370 . 48 VAL CG1 C 20.085 0.02 1 371 . 48 VAL CG2 C 20.085 0.02 1 372 . 49 TYR N N 126.566 0.02 1 373 . 49 TYR H H 8.631 0.02 1 374 . 49 TYR CA C 59.367 0.02 1 375 . 49 TYR HA H 4.552 0.002 1 376 . 49 TYR CB C 37.210 0.02 1 377 . 49 TYR HB2 H 2.857 0.02 1 378 . 49 TYR HB3 H 2.549 0.02 1 379 . 49 TYR CD1 C 132.0968 0.02 1 380 . 49 TYR HD1 H 6.665 0.003 1 381 . 49 TYR CE1 C 117.0838 0.02 1 382 . 49 TYR HE1 H 6.478 0.001 1 383 . 50 THR N N 120.847 0.02 1 384 . 50 THR H H 8.630 0.02 1 385 . 50 THR CA C 64.681 0.02 1 386 . 50 THR HA H 3.885 0.02 1 387 . 50 THR CB C 68.935 0.02 1 388 . 50 THR HB H 3.956 0.002 1 389 . 50 THR HG2 H 1.264 0.002 1 390 . 50 THR CG2 C 22.156 0.02 1 391 . 51 GLY N N 111.779 0.02 1 392 . 51 GLY H H 9.222 0.02 1 393 . 51 GLY CA C 45.827 0.02 1 394 . 51 GLY HA2 H 4.001 0.02 1 395 . 51 GLY HA3 H 3.500 0.02 1 396 . 52 TYR N N 116.262 0.02 1 397 . 52 TYR H H 7.878 0.02 1 398 . 52 TYR CA C 58.632 0.02 1 399 . 52 TYR HA H 4.475 0.002 1 400 . 52 TYR CB C 39.487 0.02 1 401 . 52 TYR HB2 H 3.122 0.006 1 402 . 52 TYR HB3 H 2.536 0.02 1 403 . 52 TYR CD1 C 132.6148 0.02 3 404 . 52 TYR HD1 H 6.937 0.002 3 405 . 52 TYR CE1 C 118.1188 0.02 3 406 . 52 TYR HE1 H 6.822 0.003 3 407 . 53 GLY N N 102.991 0.02 1 408 . 53 GLY H H 8.186 0.02 1 409 . 53 GLY CA C 45.720 0.02 1 410 . 53 GLY HA2 H 4.073 0.02 1 411 . 53 GLY HA3 H 3.679 0.02 1 412 . 54 ASN N N 113.547 0.02 1 413 . 54 ASN H H 8.136 0.02 1 414 . 54 ASN CA C 53.080 0.02 1 415 . 54 ASN HA H 4.689 0.02 1 416 . 54 ASN CB C 37.429 0.02 1 417 . 54 ASN HB2 H 2.729 0.02 1 418 . 54 ASN HB3 H 2.621 0.002 1 419 . 54 ASN ND2 N 110.768 0.02 1 420 . 54 ASN HD21 H 7.588 0.02 1 421 . 54 ASN HD22 H 5.685 0.02 1 422 . 55 ARG N N 115.051 0.02 1 423 . 55 ARG H H 8.577 0.02 1 424 . 55 ARG CA C 53.769 0.02 1 425 . 55 ARG HA H 5.753 0.02 1 426 . 55 ARG CB C 33.946 0.02 1 427 . 55 ARG HB2 H 1.621 0.02 1 428 . 55 ARG HB3 H 1.620 0.001 1 429 . 55 ARG CG C 26.500 0.02 1 430 . 55 ARG HG2 H 1.565 0.001 2 431 . 55 ARG CD C 43.568 0.02 1 432 . 55 ARG HD2 H 3.172 0.006 1 433 . 55 ARG HD3 H 2.974 0.006 1 434 . 56 GLU N N 115.862 0.02 1 435 . 56 GLU H H 8.478 0.02 1 436 . 56 GLU CA C 55.595 0.02 1 437 . 56 GLU HA H 4.699 0.02 1 438 . 56 GLU CB C 33.743 0.02 1 439 . 56 GLU HB2 H 2.311 0.001 1 440 . 56 GLU HB3 H 2.313 0.002 1 441 . 56 GLU CG C 35.099 0.02 1 442 . 56 GLU HG2 H 2.552 0.02 1 443 . 56 GLU HG3 H 2.459 0.02 1 444 . 57 GLU N N 121.476 0.02 1 445 . 57 GLU H H 8.747 0.02 1 446 . 57 GLU CA C 55.428 0.02 1 447 . 57 GLU HA H 5.348 0.001 1 448 . 57 GLU CB C 30.796 0.02 1 449 . 57 GLU HB2 H 2.018 0.02 1 450 . 57 GLU HB3 H 1.943 0.02 1 451 . 57 GLU CG C 37.429 0.02 1 452 . 57 GLU HG2 H 2.320 0.02 1 453 . 57 GLU HG3 H 2.124 0.004 1 454 . 58 GLN N N 120.228 0.02 1 455 . 58 GLN H H 9.184 0.02 1 456 . 58 GLN CA C 53.342 0.02 1 457 . 58 GLN HA H 4.604 0.002 1 458 . 58 GLN CB C 31.583 0.02 1 459 . 58 GLN HB2 H 2.208 0.02 1 460 . 58 GLN HB3 H 1.271 0.02 1 461 . 58 GLN CG C 32.179 0.02 1 462 . 58 GLN HG2 H 1.919 0.004 2 463 . 58 GLN NE2 N 109.203 0.02 1 464 . 58 GLN HE21 H 7.183 0.02 1 465 . 58 GLN HE22 H 6.687 0.02 1 466 . 59 ASN N N 116.945 0.02 1 467 . 59 ASN H H 9.297 0.02 1 468 . 59 ASN CA C 53.404 0.02 1 469 . 59 ASN HA H 4.884 0.003 1 470 . 59 ASN CB C 37.623 0.02 1 471 . 59 ASN HB2 H 3.064 0.02 1 472 . 59 ASN HB3 H 2.663 0.02 1 473 . 60 LEU N N 122.786 0.02 1 474 . 60 LEU H H 8.501 0.02 1 475 . 60 LEU CA C 58.060 0.02 1 476 . 60 LEU HA H 3.747 0.02 1 477 . 60 LEU CB C 42.001 0.02 1 478 . 60 LEU HB2 H 1.750 0.006 1 479 . 60 LEU HB3 H 1.559 0.005 1 480 . 60 LEU CG C 27.465 0.02 1 481 . 60 LEU HG H 1.110 0.02 1 482 . 60 LEU HD1 H 0.837 0.003 1 483 . 60 LEU HD2 H 0.711 0.02 1 484 . 60 LEU CD1 C 25.164 0.02 1 485 . 60 LEU CD2 C 21.825 0.02 1 486 . 61 SER N N 108.271 0.02 1 487 . 61 SER H H 8.839 0.02 1 488 . 61 SER CA C 60.086 0.02 1 489 . 61 SER HA H 4.232 0.02 1 490 . 61 SER CB C 62.833 0.02 1 491 . 61 SER HB2 H 4.112 0.02 1 492 . 61 SER HB3 H 3.884 0.02 1 493 . 62 ASP N N 117.242 0.02 1 494 . 62 ASP H H 7.648 0.02 1 495 . 62 ASP CA C 54.440 0.02 1 496 . 62 ASP HA H 4.941 0.006 1 497 . 62 ASP CB C 41.119 0.02 1 498 . 62 ASP HB2 H 3.065 0.02 1 499 . 62 ASP HB3 H 2.876 0.02 1 500 . 63 LEU N N 117.610 0.02 1 501 . 63 LEU H H 7.147 0.02 1 502 . 63 LEU CA C 54.957 0.02 1 503 . 63 LEU HA H 4.167 0.02 1 504 . 63 LEU CB C 42.381 0.02 1 505 . 63 LEU HB2 H 1.620 0.02 1 506 . 63 LEU HB3 H 0.713 0.02 1 507 . 63 LEU CG C 25.780 0.02 1 508 . 63 LEU HG H 1.490 0.001 1 509 . 63 LEU HD1 H -0.204 0.001 1 510 . 63 LEU HD2 H 0.297 0.001 1 511 . 63 LEU CD1 C 24.200 0.02 1 512 . 63 LEU CD2 C 21.528 0.02 1 513 . 64 LEU N N 119.184 0.02 1 514 . 64 LEU H H 8.504 0.02 1 515 . 64 LEU CA C 52.947 0.02 1 516 . 64 LEU HA H 4.966 0.02 1 517 . 64 LEU CB C 43.807 0.02 1 518 . 64 LEU HB2 H 1.684 0.001 1 519 . 64 LEU HB3 H 1.684 0.02 1 520 . 64 LEU CG C 27.094 0.02 1 521 . 64 LEU HG H 1.683 0.02 1 522 . 64 LEU HD1 H 0.888 0.02 1 523 . 64 LEU HD2 H 0.951 0.003 1 524 . 64 LEU CD1 C 25.449 0.02 1 525 . 64 LEU CD2 C 23.378 0.02 1 526 . 65 SER N N 112.987 0.02 1 527 . 65 SER H H 8.554 0.02 1 528 . 65 SER CA C 57.546 0.02 1 529 . 65 SER HA H 4.849 0.001 1 530 . 65 SER CB C 62.205 0.02 1 531 . 65 SER HB2 H 4.031 0.02 1 532 . 65 SER HB3 H 3.909 0.02 1 533 . 66 PRO CD C 50.298 0.02 1 534 . 66 PRO CA C 62.814 0.02 1 535 . 66 PRO HA H 4.401 0.007 1 536 . 66 PRO CB C 31.734 0.02 1 537 . 66 PRO HB2 H 2.057 0.02 1 538 . 66 PRO HB3 H 2.056 0.001 1 539 . 66 PRO CG C 27.519 0.02 1 540 . 66 PRO HG2 H 2.064 0.007 1 541 . 66 PRO HG3 H 1.993 0.006 1 542 . 66 PRO HD2 H 4.027 0.02 2 543 . 67 ILE N N 118.882 0.02 1 544 . 67 ILE H H 8.403 0.02 1 545 . 67 ILE CA C 61.026 0.02 1 546 . 67 ILE HA H 4.119 0.002 1 547 . 67 ILE CB C 38.428 0.02 1 548 . 67 ILE HB H 1.847 0.02 1 549 . 67 ILE HG2 H 0.917 0.02 1 550 . 67 ILE CG2 C 17.298 0.02 1 551 . 67 ILE CG1 C 26.871 0.02 1 552 . 67 ILE HG12 H 1.516 0.02 1 553 . 67 ILE HG13 H 1.190 0.02 1 554 . 67 ILE HD1 H 0.868 0.02 1 555 . 67 ILE CD1 C 12.564 0.02 1 556 . 68 CYS N N 122.007 0.02 1 557 . 68 CYS H H 8.528 0.02 1 558 . 68 CYS CA C 58.255 0.02 1 559 . 68 CYS HA H 4.497 0.006 1 560 . 68 CYS CB C 27.751 0.02 1 561 . 68 CYS HB2 H 2.913 0.006 1 562 . 68 CYS HB3 H 2.913 0.006 1 stop_ save_