data_5539 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure and Stability of the Full-Length Excisionase (Xis) from Bacteriophage HK022 ; _BMRB_accession_number 5539 _BMRB_flat_file_name bmr5539.str _Entry_type original _Submission_date 2002-09-25 _Accession_date 2002-09-25 _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 Rogov Vladimir . . 2 Luecke C. . . 3 Muresanu Lucia . . 4 Wienk Hans . . 5 Kleinhaus Ioana . . 6 Werner Karla . . 7 Loehr Frank . . 8 Pristovsek Primoz . . 9 Rueterjans Heinz . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 469 "13C chemical shifts" 309 "15N chemical shifts" 72 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-07-08 update author 'update the chemical shift table' 2004-02-14 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure and Stability of the Full-Length Excisionase from Bacteriophage HK022 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14653811 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rogov Vladimir V . 2 Luecke C. . . 3 Muresanu Lucia . . 4 Wienk Hans . . 5 Kleinhaus Ioana . . 6 Werner Karla . . 7 Loehr Frank . . 8 Pristovsek Primoz . . 9 Rueterjans Heinz . . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_volume 270 _Journal_issue 24 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4846 _Page_last 4858 _Year 2003 _Details . save_ ################################## # Molecular system description # ################################## save_system_Xis _Saveframe_category molecular_system _Mol_system_name 'Xis C28S' _Abbreviation_common Xis _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'xis monomer' $xis_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function excisionase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_xis_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common excisionase _Abbreviation_common xis _Molecular_mass 8640 _Mol_thiol_state 'not present' _Details 'Unusual isoaspartyl-glycine linkage at position Asn66-Gly67.' ############################## # Polymer residue sequence # ############################## _Residue_count 72 _Mol_residue_sequence ; MYLTLQEWNARQRRPRSLET VRRWVRESRIFPPPVKDGRE YLFHESAVKVDLNRPVTGSL LKRIRNGKKAKS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 TYR 3 LEU 4 THR 5 LEU 6 GLN 7 GLU 8 TRP 9 ASN 10 ALA 11 ARG 12 GLN 13 ARG 14 ARG 15 PRO 16 ARG 17 SER 18 LEU 19 GLU 20 THR 21 VAL 22 ARG 23 ARG 24 TRP 25 VAL 26 ARG 27 GLU 28 SER 29 ARG 30 ILE 31 PHE 32 PRO 33 PRO 34 PRO 35 VAL 36 LYS 37 ASP 38 GLY 39 ARG 40 GLU 41 TYR 42 LEU 43 PHE 44 HIS 45 GLU 46 SER 47 ALA 48 VAL 49 LYS 50 VAL 51 ASP 52 LEU 53 ASN 54 ARG 55 PRO 56 VAL 57 THR 58 GLY 59 SER 60 LEU 61 LEU 62 LYS 63 ARG 64 ILE 65 ARG 66 ASN 67 GLY 68 LYS 69 LYS 70 ALA 71 LYS 72 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1LX8 "Regulation Of Directionality In Bacteriophage Lambda Site- Specific Recombination: Structure Of The Xis Protein" 76.39 55 100.00 100.00 2.69e-31 PDB 1PM6 "Solution Structure Of Full-Length Excisionase (Xis) From Bacteriophage Hk022" 100.00 72 100.00 100.00 1.21e-43 PDB 1RH6 "Bacteriophage Lambda Excisionase (Xis)-Dna Complex" 76.39 55 100.00 100.00 2.69e-31 PDB 2IEF "Structure Of The Cooperative Excisionase (Xis)-Dna Complex Reveals A Micronucleoprotein Filament" 76.39 55 100.00 100.00 2.69e-31 PDB 2OG0 "Crystal Structure Of The Lambda Xis-Dna Complex" 72.22 52 100.00 100.00 6.84e-29 DBJ BAB34224 "excisionase [Escherichia coli O157:H7 str. Sakai]" 100.00 72 98.61 98.61 4.24e-43 DBJ BAI24153 "putative excisionase [Escherichia coli O26:H11 str. 11368]" 100.00 72 98.61 98.61 4.24e-43 DBJ BAI26429 "excisionase [Escherichia coli O26:H11 str. 11368]" 100.00 72 97.22 97.22 3.28e-42 DBJ BAI36808 "predicted excisionase [Escherichia coli O111:H- str. 11128]" 100.00 72 97.22 97.22 3.28e-42 EMBL CAA36222 "unnamed protein product [Enterobacteria phage HK022]" 100.00 72 98.61 98.61 4.24e-43 EMBL CAB38714 "excisionase-like protein [Enterobacteria phage H19J]" 100.00 72 98.61 98.61 4.24e-43 EMBL CAP75450 "excisionase [Escherichia coli LF82]" 100.00 72 97.22 97.22 3.07e-42 EMBL CAS08199 "predicted excisionase [Escherichia coli O127:H6 str. E2348/69]" 100.00 72 98.61 98.61 4.24e-43 EMBL CAS08528 "predicted excisionase [Escherichia coli O127:H6 str. E2348/69]" 100.00 72 98.61 98.61 4.24e-43 GB AAA67901 "excisionase [Phage 434]" 100.00 72 98.61 98.61 4.24e-43 GB AAA96563 "xis (excision;72) [Enterobacteria phage lambda]" 100.00 72 97.22 97.22 2.03e-42 GB AAF30378 "excisionase [Enterobacteria phage HK022]" 100.00 72 98.61 98.61 4.24e-43 GB AAF31117 "excisionase [Enterobacteria phage HK97]" 100.00 72 98.61 98.61 4.24e-43 GB AAL09848 "excisionase [CRIM helper plasmid pAH57]" 100.00 72 97.22 97.22 2.03e-42 REF NP_037687 "excisionase [Enterobacteria phage HK022]" 100.00 72 98.61 98.61 4.24e-43 REF NP_037721 "excisionase [Enterobacteria phage HK97]" 100.00 72 98.61 98.61 4.24e-43 REF NP_040610 "Excisionase [Enterobacteria phage lambda]" 100.00 72 97.22 97.22 2.03e-42 REF NP_308828 "excisionase [Escherichia coli O157:H7 str. Sakai]" 100.00 72 98.61 98.61 4.24e-43 REF WP_001303849 "MULTISPECIES: excisionase [Enterobacteriaceae]" 100.00 72 98.61 98.61 4.24e-43 SP P03699 "RecName: Full=Excisionase [Enterobacteria phage lambda]" 100.00 72 97.22 97.22 2.03e-42 SP P68926 "RecName: Full=Excisionase [Phage 434]" 100.00 72 98.61 98.61 4.24e-43 SP P68927 "RecName: Full=Excisionase [Enterobacteria phage HK022]" 100.00 72 98.61 98.61 4.24e-43 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $xis_monomer 'Enterobacteria phage HK022' 10742 Viruses . 'Lambda-like viruses' 'Enterobacteria phage HK022' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $xis_monomer 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3)* pET14 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $xis_monomer . mM 0.8 1.2 '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 97.0 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 _Details . save_ ####################### # Sample conditions # ####################### save_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.3 pH temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'xis monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET HA H 4.37 0.01 1 2 . 1 MET HB2 H 1.83 0.01 1 3 . 1 MET HB3 H 1.83 0.01 1 4 . 1 MET HG2 H 2.32 0.01 1 5 . 1 MET HG3 H 2.32 0.01 1 6 . 1 MET C C 174.6 0.1 1 7 . 1 MET CA C 55.9 0.1 1 8 . 1 MET CB C 33.3 0.1 1 9 . 1 MET CG C 31.7 0.1 1 10 . 2 TYR H H 8.17 0.01 1 11 . 2 TYR HA H 4.99 0.01 1 12 . 2 TYR HB2 H 2.83 0.01 2 13 . 2 TYR HB3 H 2.78 0.01 2 14 . 2 TYR HD1 H 6.88 0.01 1 15 . 2 TYR HD2 H 6.88 0.01 1 16 . 2 TYR HE1 H 6.69 0.01 1 17 . 2 TYR HE2 H 6.69 0.01 1 18 . 2 TYR C C 175.3 0.1 1 19 . 2 TYR CA C 57.2 0.1 1 20 . 2 TYR CB C 41.3 0.1 1 21 . 2 TYR N N 119.1 0.1 1 22 . 3 LEU H H 9.66 0.01 1 23 . 3 LEU HA H 4.97 0.01 1 24 . 3 LEU HB2 H 1.83 0.01 1 25 . 3 LEU HB3 H 1.90 0.01 1 26 . 3 LEU HG H 1.68 0.01 1 27 . 3 LEU HD1 H 0.87 0.01 1 28 . 3 LEU HD2 H 0.97 0.01 1 29 . 3 LEU C C 177.4 0.1 1 30 . 3 LEU CA C 53.3 0.1 1 31 . 3 LEU CB C 45.7 0.1 1 32 . 3 LEU CG C 26.9 0.1 1 33 . 3 LEU CD1 C 23.0 0.1 1 34 . 3 LEU CD2 C 26.5 0.1 1 35 . 3 LEU N N 122.3 0.1 1 36 . 4 THR H H 8.85 0.01 1 37 . 4 THR HA H 4.82 0.01 1 38 . 4 THR HB H 4.91 0.01 1 39 . 4 THR HG2 H 1.43 0.01 1 40 . 4 THR C C 174.9 0.1 1 41 . 4 THR CA C 61.9 0.1 1 42 . 4 THR CB C 71.2 0.1 1 43 . 4 THR CG2 C 22.2 0.1 1 44 . 4 THR N N 111.7 0.1 1 45 . 5 LEU H H 8.67 0.01 1 46 . 5 LEU HA H 3.54 0.01 1 47 . 5 LEU HB2 H 2.03 0.01 1 48 . 5 LEU HB3 H 1.94 0.01 1 49 . 5 LEU HG H 1.61 0.01 1 50 . 5 LEU HD1 H 1.03 0.01 1 51 . 5 LEU HD2 H 0.91 0.01 1 52 . 5 LEU C C 179.0 0.1 1 53 . 5 LEU CA C 60.4 0.1 1 54 . 5 LEU CB C 42.9 0.1 1 55 . 5 LEU CG C 27.3 0.1 1 56 . 5 LEU CD1 C 27.2 0.1 1 57 . 5 LEU CD2 C 25.6 0.1 1 58 . 5 LEU N N 122.5 0.1 1 59 . 6 GLN H H 9.02 0.01 1 60 . 6 GLN HA H 3.99 0.01 1 61 . 6 GLN HB2 H 2.15 0.01 2 62 . 6 GLN HB3 H 2.10 0.01 2 63 . 6 GLN HG2 H 2.62 0.01 2 64 . 6 GLN HG3 H 2.49 0.01 2 65 . 6 GLN HE21 H 7.53 0.01 2 66 . 6 GLN HE22 H 6.99 0.01 2 67 . 6 GLN C C 179.2 0.1 1 68 . 6 GLN CA C 60.0 0.1 1 69 . 6 GLN CB C 28.3 0.1 1 70 . 6 GLN CG C 34.4 0.1 1 71 . 6 GLN N N 117.0 0.1 1 72 . 6 GLN NE2 N 111.7 0.1 1 73 . 7 GLU H H 7.86 0.01 1 74 . 7 GLU HA H 4.03 0.01 1 75 . 7 GLU HB2 H 2.40 0.01 2 76 . 7 GLU HB3 H 1.99 0.01 2 77 . 7 GLU HG2 H 2.40 0.01 1 78 . 7 GLU HG3 H 2.31 0.01 1 79 . 7 GLU C C 178.9 0.1 1 80 . 7 GLU CA C 58.9 0.1 1 81 . 7 GLU CB C 31.1 0.1 1 82 . 7 GLU CG C 37.2 0.1 1 83 . 7 GLU N N 121.4 0.1 1 84 . 8 TRP H H 9.05 0.01 1 85 . 8 TRP HA H 3.76 0.01 1 86 . 8 TRP HB2 H 2.80 0.01 1 87 . 8 TRP HB3 H 2.74 0.01 1 88 . 8 TRP HD1 H 7.09 0.01 1 89 . 8 TRP HE1 H 9.97 0.01 1 90 . 8 TRP HE3 H 6.94 0.01 1 91 . 8 TRP HZ2 H 7.19 0.01 1 92 . 8 TRP HZ3 H 7.14 0.01 1 93 . 8 TRP HH2 H 7.14 0.01 1 94 . 8 TRP C C 179.4 0.1 1 95 . 8 TRP CA C 63.0 0.1 1 96 . 8 TRP CB C 28.1 0.1 1 97 . 8 TRP N N 120.4 0.1 1 98 . 8 TRP NE1 N 130.2 0.1 1 99 . 9 ASN H H 8.66 0.01 1 100 . 9 ASN HA H 3.98 0.01 1 101 . 9 ASN HB2 H 2.93 0.01 2 102 . 9 ASN HB3 H 2.72 0.01 2 103 . 9 ASN HD21 H 7.68 0.01 1 104 . 9 ASN HD22 H 8.10 0.01 1 105 . 9 ASN C C 176.5 0.1 1 106 . 9 ASN CA C 56.3 0.1 1 107 . 9 ASN CB C 39.9 0.1 1 108 . 9 ASN N N 117.7 0.1 1 109 . 9 ASN ND2 N 114.9 0.1 1 110 . 10 ALA H H 7.60 0.01 1 111 . 10 ALA HA H 4.01 0.01 1 112 . 10 ALA HB H 1.50 0.01 1 113 . 10 ALA C C 178.5 0.1 1 114 . 10 ALA CA C 54.1 0.1 1 115 . 10 ALA CB C 18.6 0.1 1 116 . 10 ALA N N 116.6 0.1 1 117 . 11 ARG H H 7.09 0.01 1 118 . 11 ARG HA H 4.25 0.01 1 119 . 11 ARG HB2 H 1.64 0.01 1 120 . 11 ARG HB3 H 1.88 0.01 1 121 . 11 ARG HG2 H 1.75 0.01 2 122 . 11 ARG HG3 H 1.66 0.01 2 123 . 11 ARG HD2 H 3.11 0.01 1 124 . 11 ARG HD3 H 3.08 0.01 1 125 . 11 ARG C C 176.8 0.1 1 126 . 11 ARG CA C 55.9 0.1 1 127 . 11 ARG CB C 30.8 0.1 1 128 . 11 ARG CG C 27.1 0.1 1 129 . 11 ARG CD C 44.2 0.1 1 130 . 11 ARG N N 114.4 0.1 1 131 . 12 GLN H H 7.13 0.01 1 132 . 12 GLN HA H 3.85 0.01 1 133 . 12 GLN HB2 H 1.62 0.01 1 134 . 12 GLN HB3 H 1.94 0.01 1 135 . 12 GLN HG2 H 1.85 0.01 1 136 . 12 GLN HG3 H 1.58 0.01 1 137 . 12 GLN HE21 H 6.31 0.01 1 138 . 12 GLN HE22 H 6.31 0.01 1 139 . 12 GLN C C 175.5 0.1 1 140 . 12 GLN CA C 54.6 0.1 1 141 . 12 GLN CB C 29.1 0.1 1 142 . 12 GLN CG C 33.1 0.1 1 143 . 12 GLN N N 118.7 0.1 1 144 . 12 GLN NE2 N 115.4 0.1 1 145 . 13 ARG H H 8.45 0.01 1 146 . 13 ARG HA H 3.97 0.01 1 147 . 13 ARG HB2 H 1.83 0.01 1 148 . 13 ARG HB3 H 1.83 0.01 1 149 . 13 ARG HG2 H 1.66 0.01 1 150 . 13 ARG HG3 H 1.74 0.01 1 151 . 13 ARG HD2 H 3.27 0.01 1 152 . 13 ARG HD3 H 3.27 0.01 1 153 . 13 ARG C C 177.6 0.1 1 154 . 13 ARG CA C 59.1 0.1 1 155 . 13 ARG CB C 29.7 0.1 1 156 . 13 ARG CG C 27.4 0.1 1 157 . 13 ARG CD C 43.2 0.1 1 158 . 13 ARG N N 121.2 0.1 1 159 . 14 ARG H H 7.99 0.01 1 160 . 14 ARG HA H 4.70 0.01 1 161 . 14 ARG HB2 H 1.67 0.01 2 162 . 14 ARG HB3 H 1.49 0.01 2 163 . 14 ARG HG2 H 1.48 0.01 1 164 . 14 ARG HG3 H 1.48 0.01 1 165 . 14 ARG HD2 H 3.16 0.01 1 166 . 14 ARG HD3 H 3.16 0.01 1 167 . 14 ARG C C 177.6 0.1 1 168 . 14 ARG CA C 52.6 0.1 1 169 . 14 ARG CB C 31.1 0.1 1 170 . 14 ARG N N 116.5 0.1 1 171 . 15 PRO HA H 4.17 0.01 1 172 . 15 PRO HB2 H 1.69 0.01 1 173 . 15 PRO HB3 H 2.16 0.01 1 174 . 15 PRO HG2 H 1.99 0.01 1 175 . 15 PRO HG3 H 1.99 0.01 1 176 . 15 PRO HD2 H 3.47 0.01 1 177 . 15 PRO HD3 H 3.57 0.01 1 178 . 15 PRO C C 176.8 0.1 1 179 . 15 PRO CA C 63.5 0.1 1 180 . 15 PRO CB C 32.7 0.1 1 181 . 15 PRO CG C 27.7 0.1 1 182 . 15 PRO CD C 51.0 0.1 1 183 . 16 ARG H H 8.90 0.01 1 184 . 16 ARG HA H 4.98 0.01 1 185 . 16 ARG HB2 H 2.01 0.01 1 186 . 16 ARG HB3 H 1.35 0.01 1 187 . 16 ARG HG2 H 1.96 0.01 1 188 . 16 ARG HG3 H 1.96 0.01 1 189 . 16 ARG HD2 H 3.34 0.01 2 190 . 16 ARG HD3 H 3.25 0.01 2 191 . 16 ARG C C 176.8 0.1 1 192 . 16 ARG CA C 51.6 0.1 1 193 . 16 ARG CB C 32.6 0.1 1 194 . 16 ARG CG C 27.0 0.1 1 195 . 16 ARG CD C 40.8 0.1 1 196 . 16 ARG N N 123.7 0.1 1 197 . 17 SER H H 9.14 0.01 1 198 . 17 SER HA H 4.40 0.01 1 199 . 17 SER HB2 H 4.12 0.01 1 200 . 17 SER HB3 H 4.26 0.01 1 201 . 17 SER C C 175.3 0.1 1 202 . 17 SER CA C 58.7 0.1 1 203 . 17 SER CB C 63.9 0.1 1 204 . 17 SER N N 116.9 0.1 1 205 . 18 LEU H H 8.71 0.01 1 206 . 18 LEU HA H 3.83 0.01 1 207 . 18 LEU HB2 H 1.80 0.01 2 208 . 18 LEU HB3 H 1.46 0.01 2 209 . 18 LEU HG H 1.81 0.01 1 210 . 18 LEU HD1 H 0.86 0.01 1 211 . 18 LEU HD2 H 1.01 0.01 1 212 . 18 LEU C C 179.3 0.1 1 213 . 18 LEU CA C 58.5 0.1 1 214 . 18 LEU CB C 40.4 0.1 1 215 . 18 LEU CG C 27.1 0.1 1 216 . 18 LEU CD1 C 22.8 0.1 1 217 . 18 LEU CD2 C 25.4 0.1 1 218 . 18 LEU N N 121.8 0.1 1 219 . 19 GLU H H 8.48 0.01 1 220 . 19 GLU HA H 3.93 0.01 1 221 . 19 GLU HB2 H 2.04 0.01 2 222 . 19 GLU HB3 H 1.90 0.01 2 223 . 19 GLU HG2 H 2.36 0.01 2 224 . 19 GLU HG3 H 2.28 0.01 2 225 . 19 GLU C C 179.4 0.1 1 226 . 19 GLU CA C 59.8 0.1 1 227 . 19 GLU CB C 29.1 0.1 1 228 . 19 GLU CG C 36.6 0.1 1 229 . 19 GLU N N 116.7 0.1 1 230 . 20 THR H H 7.62 0.01 1 231 . 20 THR HA H 3.53 0.01 1 232 . 20 THR HB H 4.04 0.01 1 233 . 20 THR HG2 H 0.29 0.01 1 234 . 20 THR C C 174.1 0.1 1 235 . 20 THR CA C 66.6 0.1 1 236 . 20 THR CB C 67.5 0.1 1 237 . 20 THR CG2 C 21.6 0.1 1 238 . 20 THR N N 120.0 0.1 1 239 . 21 VAL H H 7.23 0.01 1 240 . 21 VAL HA H 3.10 0.01 1 241 . 21 VAL HB H 1.96 0.01 1 242 . 21 VAL HG1 H 1.07 0.01 1 243 . 21 VAL HG2 H 0.81 0.01 1 244 . 21 VAL C C 178.2 0.1 1 245 . 21 VAL CA C 66.5 0.1 1 246 . 21 VAL CB C 31.3 0.1 1 247 . 21 VAL CG1 C 23.2 0.1 1 248 . 21 VAL CG2 C 22.2 0.1 1 249 . 21 VAL N N 119.5 0.1 1 250 . 22 ARG H H 8.42 0.01 1 251 . 22 ARG HA H 3.71 0.01 1 252 . 22 ARG HB2 H 1.90 0.01 2 253 . 22 ARG HB3 H 1.82 0.01 2 254 . 22 ARG HG2 H 1.85 0.01 2 255 . 22 ARG HG3 H 1.53 0.01 2 256 . 22 ARG HD2 H 3.27 0.01 2 257 . 22 ARG HD3 H 3.19 0.01 2 258 . 22 ARG C C 179.2 0.1 1 259 . 22 ARG CA C 60.6 0.1 1 260 . 22 ARG CB C 30.2 0.1 1 261 . 22 ARG CG C 30.0 0.1 1 262 . 22 ARG CD C 43.6 0.1 1 263 . 22 ARG N N 117.0 0.1 1 264 . 23 ARG H H 7.68 0.01 1 265 . 23 ARG HA H 3.98 0.01 1 266 . 23 ARG HB2 H 2.20 0.01 2 267 . 23 ARG HB3 H 1.77 0.01 2 268 . 23 ARG HG2 H 1.59 0.01 1 269 . 23 ARG HG3 H 1.59 0.01 1 270 . 23 ARG HD2 H 3.42 0.01 2 271 . 23 ARG HD3 H 3.19 0.01 2 272 . 23 ARG C C 177.8 0.1 1 273 . 23 ARG CA C 60.2 0.1 1 274 . 23 ARG CB C 28.7 0.1 1 275 . 23 ARG CG C 27.7 0.1 1 276 . 23 ARG CD C 43.6 0.1 1 277 . 23 ARG N N 122.3 0.1 1 278 . 24 TRP H H 8.28 0.01 1 279 . 24 TRP HA H 4.56 0.01 1 280 . 24 TRP HB2 H 2.88 0.01 1 281 . 24 TRP HB3 H 3.93 0.01 1 282 . 24 TRP HD1 H 7.05 0.01 1 283 . 24 TRP HE1 H 10.71 0.01 1 284 . 24 TRP HE3 H 7.59 0.01 1 285 . 24 TRP HZ2 H 7.52 0.01 1 286 . 24 TRP HZ3 H 7.46 0.01 1 287 . 24 TRP HH2 H 7.36 0.01 1 288 . 24 TRP C C 179.3 0.1 1 289 . 24 TRP CA C 58.5 0.1 1 290 . 24 TRP CB C 28.9 0.1 1 291 . 24 TRP N N 120.2 0.1 1 292 . 24 TRP NE1 N 130.2 0.1 1 293 . 25 VAL H H 8.09 0.01 1 294 . 25 VAL HA H 3.52 0.01 1 295 . 25 VAL HB H 2.08 0.01 1 296 . 25 VAL HG1 H 0.26 0.01 1 297 . 25 VAL HG2 H 0.79 0.01 1 298 . 25 VAL C C 180.4 0.1 1 299 . 25 VAL CA C 66.7 0.1 1 300 . 25 VAL CB C 31.3 0.1 1 301 . 25 VAL CG1 C 20.6 0.1 1 302 . 25 VAL CG2 C 23.6 0.1 1 303 . 25 VAL N N 118.0 0.1 1 304 . 26 ARG H H 8.06 0.01 1 305 . 26 ARG HA H 4.14 0.01 1 306 . 26 ARG HB2 H 2.09 0.01 1 307 . 26 ARG HB3 H 2.09 0.01 1 308 . 26 ARG HG2 H 1.87 0.01 2 309 . 26 ARG HG3 H 1.75 0.01 2 310 . 26 ARG HD2 H 3.35 0.01 2 311 . 26 ARG HD3 H 3.29 0.01 2 312 . 26 ARG C C 178.5 0.1 1 313 . 26 ARG CA C 59.6 0.1 1 314 . 26 ARG CB C 30.2 0.1 1 315 . 26 ARG CG C 28.1 0.1 1 316 . 26 ARG CD C 43.8 0.1 1 317 . 26 ARG N N 122.8 0.1 1 318 . 27 GLU H H 8.35 0.01 1 319 . 27 GLU HA H 4.31 0.01 1 320 . 27 GLU HB2 H 2.33 0.01 2 321 . 27 GLU HB3 H 2.08 0.01 2 322 . 27 GLU HG2 H 2.65 0.01 2 323 . 27 GLU HG3 H 2.28 0.01 2 324 . 27 GLU C C 175.2 0.1 1 325 . 27 GLU CA C 56.3 0.1 1 326 . 27 GLU CB C 30.2 0.1 1 327 . 27 GLU CG C 36.9 0.1 1 328 . 27 GLU N N 117.5 0.1 1 329 . 28 SER H H 7.96 0.01 1 330 . 28 SER HA H 4.32 0.01 1 331 . 28 SER HB2 H 4.20 0.01 2 332 . 28 SER HB3 H 4.14 0.01 2 333 . 28 SER C C 175.3 0.1 1 334 . 28 SER CA C 59.1 0.1 1 335 . 28 SER CB C 60.9 0.1 1 336 . 28 SER N N 111.9 0.1 1 337 . 29 ARG H H 8.33 0.01 1 338 . 29 ARG HA H 4.40 0.01 1 339 . 29 ARG HB2 H 1.41 0.01 1 340 . 29 ARG HB3 H 2.26 0.01 1 341 . 29 ARG HG2 H 1.79 0.01 2 342 . 29 ARG HG3 H 1.57 0.01 2 343 . 29 ARG HD2 H 3.27 0.01 2 344 . 29 ARG HD3 H 3.16 0.01 2 345 . 29 ARG C C 174.2 0.1 1 346 . 29 ARG CA C 55.2 0.1 1 347 . 29 ARG CB C 30.8 0.1 1 348 . 29 ARG CG C 27.4 0.1 1 349 . 29 ARG CD C 43.8 0.1 1 350 . 29 ARG N N 114.5 0.1 1 351 . 30 ILE H H 7.47 0.01 1 352 . 30 ILE HA H 4.85 0.01 1 353 . 30 ILE HB H 1.57 0.01 1 354 . 30 ILE HG12 H 1.10 0.01 1 355 . 30 ILE HG13 H 1.10 0.01 1 356 . 30 ILE HG2 H 0.43 0.01 1 357 . 30 ILE HD1 H 0.71 0.01 1 358 . 30 ILE C C 175.1 0.1 1 359 . 30 ILE CA C 58.1 0.1 1 360 . 30 ILE CB C 38.0 0.1 1 361 . 30 ILE CG1 C 26.7 0.1 1 362 . 30 ILE CG2 C 17.2 0.1 1 363 . 30 ILE CD1 C 11.4 0.1 1 364 . 30 ILE N N 117.4 0.1 1 365 . 31 PHE H H 9.08 0.01 1 366 . 31 PHE HA H 4.52 0.01 1 367 . 31 PHE HB2 H 2.77 0.01 1 368 . 31 PHE HB3 H 2.85 0.01 1 369 . 31 PHE HD1 H 7.19 0.01 1 370 . 31 PHE HD2 H 7.19 0.01 1 371 . 31 PHE HE1 H 7.33 0.01 1 372 . 31 PHE HE2 H 7.33 0.01 1 373 . 31 PHE HZ H 7.33 0.01 1 374 . 31 PHE C C 173.7 0.1 1 375 . 31 PHE CA C 55.4 0.1 1 376 . 31 PHE CB C 43.8 0.1 1 377 . 31 PHE N N 128.0 0.1 1 378 . 32 PRO HA H 3.66 0.01 1 379 . 32 PRO HB2 H 1.58 0.01 1 380 . 32 PRO HB3 H 1.96 0.01 1 381 . 32 PRO HG2 H 1.40 0.01 2 382 . 32 PRO HG3 H 1.29 0.01 2 383 . 32 PRO HD2 H 3.06 0.01 1 384 . 32 PRO HD3 H 3.40 0.01 1 385 . 32 PRO CA C 61.5 0.1 1 386 . 32 PRO CB C 32.1 0.1 1 387 . 32 PRO CG C 25.3 0.1 1 388 . 32 PRO CD C 49.7 0.1 1 389 . 33 PRO HA H 4.34 0.01 1 390 . 33 PRO HB2 H 1.84 0.01 1 391 . 33 PRO HB3 H 2.25 0.01 1 392 . 33 PRO HG2 H 2.11 0.01 2 393 . 33 PRO HG3 H 2.08 0.01 2 394 . 33 PRO HD2 H 3.54 0.01 2 395 . 33 PRO HD3 H 3.44 0.01 2 396 . 33 PRO CA C 61.1 0.1 1 397 . 33 PRO CB C 30.7 0.1 1 398 . 33 PRO CG C 27.8 0.1 1 399 . 33 PRO CD C 50.0 0.1 1 400 . 34 PRO HA H 4.52 0.01 1 401 . 34 PRO HB2 H 1.22 0.01 2 402 . 34 PRO HB3 H 1.00 0.01 2 403 . 34 PRO HG2 H 1.15 0.01 2 404 . 34 PRO HG3 H 0.69 0.01 2 405 . 34 PRO HD2 H 3.40 0.01 1 406 . 34 PRO HD3 H 3.23 0.01 1 407 . 34 PRO C C 175.9 0.1 1 408 . 34 PRO CA C 62.3 0.1 1 409 . 34 PRO CB C 32.6 0.1 1 410 . 34 PRO CG C 27.1 0.1 1 411 . 34 PRO CD C 50.2 0.1 1 412 . 35 VAL H H 8.60 0.01 1 413 . 35 VAL HA H 4.22 0.01 1 414 . 35 VAL HB H 1.83 0.01 1 415 . 35 VAL HG1 H 0.78 0.01 1 416 . 35 VAL HG2 H 0.75 0.01 1 417 . 35 VAL C C 175.0 0.1 1 418 . 35 VAL CA C 60.8 0.1 1 419 . 35 VAL CB C 34.3 0.1 1 420 . 35 VAL CG1 C 21.0 0.1 1 421 . 35 VAL CG2 C 20.6 0.1 1 422 . 35 VAL N N 119.9 0.1 1 423 . 36 LYS H H 8.52 0.01 1 424 . 36 LYS HA H 4.33 0.01 1 425 . 36 LYS HB2 H 1.69 0.01 2 426 . 36 LYS HB3 H 1.40 0.01 2 427 . 36 LYS HG2 H 0.86 0.01 1 428 . 36 LYS HG3 H 1.02 0.01 1 429 . 36 LYS HD2 H 1.41 0.01 1 430 . 36 LYS HD3 H 1.41 0.01 1 431 . 36 LYS HE2 H 2.71 0.01 1 432 . 36 LYS HE3 H 2.79 0.01 1 433 . 36 LYS C C 175.8 0.1 1 434 . 36 LYS CA C 56.1 0.1 1 435 . 36 LYS CB C 33.5 0.1 1 436 . 36 LYS CG C 24.8 0.1 1 437 . 36 LYS CD C 29.3 0.1 1 438 . 36 LYS CE C 42.0 0.1 1 439 . 36 LYS N N 126.4 0.1 1 440 . 37 ASP H H 8.48 0.01 1 441 . 37 ASP HA H 4.68 0.01 1 442 . 37 ASP HB2 H 2.19 0.01 1 443 . 37 ASP HB3 H 2.55 0.01 1 444 . 37 ASP C C 175.9 0.1 1 445 . 37 ASP CA C 53.1 0.1 1 446 . 37 ASP CB C 42.1 0.1 1 447 . 37 ASP N N 127.6 0.1 1 448 . 38 GLY H H 8.59 0.01 1 449 . 38 GLY HA2 H 3.58 0.01 1 450 . 38 GLY HA3 H 4.01 0.01 1 451 . 38 GLY C C 175.9 0.1 1 452 . 38 GLY CA C 47.0 0.1 1 453 . 38 GLY N N 114.4 0.1 1 454 . 39 ARG H H 8.95 0.01 1 455 . 39 ARG HA H 4.26 0.01 1 456 . 39 ARG HB2 H 1.99 0.01 2 457 . 39 ARG HB3 H 1.76 0.01 2 458 . 39 ARG HG2 H 1.64 0.01 1 459 . 39 ARG HG3 H 1.64 0.01 1 460 . 39 ARG HD2 H 3.24 0.01 1 461 . 39 ARG HD3 H 3.24 0.01 1 462 . 39 ARG C C 175.8 0.1 1 463 . 39 ARG CA C 56.3 0.1 1 464 . 39 ARG CB C 30.8 0.1 1 465 . 39 ARG CG C 27.2 0.1 1 466 . 39 ARG CD C 43.3 0.1 1 467 . 39 ARG N N 125.8 0.1 1 468 . 40 GLU H H 7.82 0.01 1 469 . 40 GLU HA H 4.63 0.01 1 470 . 40 GLU HB2 H 2.17 0.01 2 471 . 40 GLU HB3 H 2.02 0.01 2 472 . 40 GLU HG2 H 2.39 0.01 2 473 . 40 GLU HG3 H 2.31 0.01 2 474 . 40 GLU C C 174.9 0.1 1 475 . 40 GLU CA C 54.6 0.1 1 476 . 40 GLU CB C 32.4 0.1 1 477 . 40 GLU CG C 35.9 0.1 1 478 . 40 GLU N N 119.6 0.1 1 479 . 41 TYR H H 8.56 0.01 1 480 . 41 TYR HA H 5.01 0.01 1 481 . 41 TYR HB2 H 2.82 0.01 1 482 . 41 TYR HB3 H 2.61 0.01 1 483 . 41 TYR HD1 H 6.88 0.01 1 484 . 41 TYR HD2 H 6.88 0.01 1 485 . 41 TYR HE1 H 6.74 0.01 1 486 . 41 TYR HE2 H 6.74 0.01 1 487 . 41 TYR C C 175.0 0.1 1 488 . 41 TYR CA C 58.1 0.1 1 489 . 41 TYR CB C 42.1 0.1 1 490 . 41 TYR N N 119.8 0.1 1 491 . 42 LEU H H 9.14 0.01 1 492 . 42 LEU HA H 5.18 0.01 1 493 . 42 LEU HB2 H 1.53 0.01 1 494 . 42 LEU HB3 H 1.17 0.01 1 495 . 42 LEU HG H 1.47 0.01 1 496 . 42 LEU HD1 H 0.76 0.01 1 497 . 42 LEU HD2 H 0.67 0.01 1 498 . 42 LEU C C 175.9 0.1 1 499 . 42 LEU CA C 53.3 0.1 1 500 . 42 LEU CB C 43.8 0.1 1 501 . 42 LEU CG C 26.8 0.1 1 502 . 42 LEU CD1 C 22.9 0.1 1 503 . 42 LEU CD2 C 25.6 0.1 1 504 . 42 LEU N N 121.8 0.1 1 505 . 43 PHE H H 10.04 0.01 1 506 . 43 PHE HA H 4.60 0.01 1 507 . 43 PHE HB2 H 2.77 0.01 2 508 . 43 PHE HB3 H 2.46 0.01 2 509 . 43 PHE HD1 H 6.28 0.01 1 510 . 43 PHE HD2 H 6.28 0.01 1 511 . 43 PHE HE1 H 6.28 0.01 1 512 . 43 PHE HE2 H 6.28 0.01 1 513 . 43 PHE HZ H 6.46 0.01 1 514 . 43 PHE C C 175.9 0.1 1 515 . 43 PHE CA C 55.8 0.1 1 516 . 43 PHE CB C 41.0 0.1 1 517 . 43 PHE N N 123.5 0.1 1 518 . 44 HIS H H 9.07 0.01 1 519 . 44 HIS HA H 4.02 0.01 1 520 . 44 HIS HB2 H 2.87 0.01 1 521 . 44 HIS HB3 H 2.73 0.01 1 522 . 44 HIS HD2 H 6.74 0.01 1 523 . 44 HIS HE1 H 7.72 0.01 1 524 . 44 HIS C C 177.6 0.1 1 525 . 44 HIS CA C 58.7 0.1 1 526 . 44 HIS CB C 31.5 0.1 1 527 . 44 HIS N N 124.4 0.1 1 528 . 45 GLU H H 8.32 0.01 1 529 . 45 GLU HA H 4.09 0.01 1 530 . 45 GLU HB2 H 2.10 0.01 2 531 . 45 GLU HB3 H 1.95 0.01 2 532 . 45 GLU HG2 H 2.21 0.01 2 533 . 45 GLU HG3 H 2.15 0.01 2 534 . 45 GLU C C 177.2 0.1 1 535 . 45 GLU CA C 59.6 0.1 1 536 . 45 GLU CB C 29.1 0.1 1 537 . 45 GLU CG C 35.4 0.1 1 538 . 45 GLU N N 124.8 0.1 1 539 . 46 SER H H 9.62 0.01 1 540 . 46 SER HA H 4.67 0.01 1 541 . 46 SER HB2 H 4.09 0.01 1 542 . 46 SER HB3 H 4.09 0.01 1 543 . 46 SER C C 175.0 0.1 1 544 . 46 SER CA C 58.2 0.1 1 545 . 46 SER CB C 64.1 0.1 1 546 . 46 SER N N 115.7 0.1 1 547 . 47 ALA H H 8.31 0.01 1 548 . 47 ALA HA H 4.92 0.01 1 549 . 47 ALA HB H 1.42 0.01 1 550 . 47 ALA C C 178.5 0.1 1 551 . 47 ALA CA C 53.1 0.1 1 552 . 47 ALA CB C 18.7 0.1 1 553 . 47 ALA N N 124.8 0.1 1 554 . 48 VAL H H 8.81 0.01 1 555 . 48 VAL HA H 5.16 0.01 1 556 . 48 VAL HB H 2.33 0.01 1 557 . 48 VAL HG1 H 1.15 0.01 1 558 . 48 VAL HG2 H 1.02 0.01 1 559 . 48 VAL C C 174.2 0.1 1 560 . 48 VAL CA C 59.3 0.1 1 561 . 48 VAL CB C 36.7 0.1 1 562 . 48 VAL CG1 C 21.7 0.1 1 563 . 48 VAL CG2 C 18.6 0.1 1 564 . 48 VAL N N 116.3 0.1 1 565 . 49 LYS H H 8.52 0.01 1 566 . 49 LYS HA H 4.90 0.01 1 567 . 49 LYS HB2 H 1.49 0.01 1 568 . 49 LYS HB3 H 1.32 0.01 1 569 . 49 LYS HG2 H 0.73 0.01 2 570 . 49 LYS HG3 H 0.28 0.01 2 571 . 49 LYS HD2 H 0.46 0.01 1 572 . 49 LYS HD3 H 0.37 0.01 1 573 . 49 LYS HE2 H 2.25 0.01 2 574 . 49 LYS HE3 H 1.90 0.01 2 575 . 49 LYS C C 176.7 0.1 1 576 . 49 LYS CA C 55.5 0.1 1 577 . 49 LYS CB C 32.6 0.1 1 578 . 49 LYS CG C 23.5 0.1 1 579 . 49 LYS CD C 28.5 0.1 1 580 . 49 LYS CE C 41.1 0.1 1 581 . 49 LYS N N 122.9 0.1 1 582 . 50 VAL H H 8.80 0.01 1 583 . 50 VAL HA H 4.27 0.01 1 584 . 50 VAL HB H 1.99 0.01 1 585 . 50 VAL HG1 H 0.79 0.01 1 586 . 50 VAL HG2 H 0.85 0.01 1 587 . 50 VAL C C 175.0 0.1 1 588 . 50 VAL CA C 60.9 0.1 1 589 . 50 VAL CB C 33.9 0.1 1 590 . 50 VAL CG1 C 20.0 0.1 1 591 . 50 VAL CG2 C 21.7 0.1 1 592 . 50 VAL N N 125.8 0.1 1 593 . 51 ASP H H 8.37 0.01 1 594 . 51 ASP HA H 4.63 0.01 1 595 . 51 ASP HB2 H 2.49 0.01 1 596 . 51 ASP HB3 H 2.70 0.01 1 597 . 51 ASP C C 176.1 0.1 1 598 . 51 ASP CA C 53.9 0.1 1 599 . 51 ASP CB C 41.9 0.1 1 600 . 51 ASP N N 123.9 0.1 1 601 . 52 LEU H H 8.33 0.01 1 602 . 52 LEU HA H 4.26 0.01 1 603 . 52 LEU HB2 H 1.58 0.01 1 604 . 52 LEU HB3 H 1.58 0.01 1 605 . 52 LEU HG H 1.58 0.01 1 606 . 52 LEU HD1 H 0.92 0.01 2 607 . 52 LEU HD2 H 0.84 0.01 2 608 . 52 LEU C C 177.1 0.1 1 609 . 52 LEU CA C 55.5 0.1 1 610 . 52 LEU CB C 42.5 0.1 1 611 . 52 LEU CG C 27.0 0.1 1 612 . 52 LEU CD1 C 24.9 0.1 2 613 . 52 LEU CD2 C 23.3 0.1 2 614 . 52 LEU N N 122.6 0.1 1 615 . 53 ASN H H 8.49 0.01 1 616 . 53 ASN HA H 4.65 0.01 1 617 . 53 ASN HB2 H 2.79 0.01 1 618 . 53 ASN HB3 H 2.79 0.01 1 619 . 53 ASN HD21 H 7.63 0.01 2 620 . 53 ASN HD22 H 6.89 0.01 2 621 . 53 ASN C C 174.7 0.1 1 622 . 53 ASN CA C 53.3 0.1 1 623 . 53 ASN CB C 38.8 0.1 1 624 . 53 ASN N N 118.5 0.1 1 625 . 53 ASN ND2 N 113.3 0.1 1 626 . 54 ARG H H 7.95 0.01 1 627 . 54 ARG HA H 4.70 0.01 1 628 . 54 ARG HB2 H 1.85 0.01 2 629 . 54 ARG HB3 H 1.69 0.01 2 630 . 54 ARG HG2 H 1.69 0.01 1 631 . 54 ARG HG3 H 1.69 0.01 1 632 . 54 ARG HD2 H 3.22 0.01 1 633 . 54 ARG HD3 H 3.22 0.01 1 634 . 54 ARG C C 173.8 0.1 1 635 . 54 ARG CA C 53.9 0.1 1 636 . 54 ARG CB C 30.4 0.1 1 637 . 54 ARG N N 121.6 0.1 1 638 . 55 PRO HA H 4.47 0.01 1 639 . 55 PRO HB2 H 2.28 0.01 2 640 . 55 PRO HB3 H 1.88 0.01 2 641 . 55 PRO HG2 H 2.00 0.01 1 642 . 55 PRO HG3 H 2.00 0.01 1 643 . 55 PRO HD2 H 3.75 0.01 2 644 . 55 PRO HD3 H 3.61 0.01 2 645 . 55 PRO C C 177.0 0.1 1 646 . 55 PRO CA C 63.2 0.1 1 647 . 55 PRO CB C 32.1 0.1 1 648 . 55 PRO CG C 27.5 0.1 1 649 . 55 PRO CD C 50.6 0.1 1 650 . 56 VAL H H 8.32 0.01 1 651 . 56 VAL HA H 4.14 0.01 1 652 . 56 VAL HB H 2.07 0.01 1 653 . 56 VAL HG1 H 0.93 0.01 1 654 . 56 VAL HG2 H 0.91 0.01 1 655 . 56 VAL C C 176.4 0.1 1 656 . 56 VAL CA C 62.6 0.1 1 657 . 56 VAL CB C 32.6 0.1 1 658 . 56 VAL CG1 C 20.6 0.1 1 659 . 56 VAL CG2 C 21.4 0.1 1 660 . 56 VAL N N 120.7 0.1 1 661 . 57 THR H H 8.05 0.01 1 662 . 57 THR HA H 4.38 0.01 1 663 . 57 THR HB H 4.26 0.01 1 664 . 57 THR HG2 H 1.22 0.01 1 665 . 57 THR C C 175.1 0.1 1 666 . 57 THR CA C 61.9 0.1 1 667 . 57 THR CB C 70.1 0.1 1 668 . 57 THR CG2 C 21.5 0.1 1 669 . 57 THR N N 117.3 0.1 1 670 . 58 GLY H H 8.47 0.01 1 671 . 58 GLY HA2 H 4.04 0.01 1 672 . 58 GLY HA3 H 4.04 0.01 1 673 . 58 GLY C C 174.7 0.1 1 674 . 58 GLY CA C 45.7 0.1 1 675 . 58 GLY N N 111.1 0.1 1 676 . 59 SER H H 8.27 0.01 1 677 . 59 SER HA H 4.40 0.01 1 678 . 59 SER HB2 H 3.87 0.01 1 679 . 59 SER HB3 H 3.87 0.01 1 680 . 59 SER C C 175.2 0.1 1 681 . 59 SER CA C 59.2 0.1 1 682 . 59 SER CB C 63.8 0.1 1 683 . 59 SER N N 116.0 0.1 1 684 . 60 LEU H H 8.22 0.01 1 685 . 60 LEU HA H 4.30 0.01 1 686 . 60 LEU HB2 H 1.64 0.01 1 687 . 60 LEU HB3 H 1.64 0.01 1 688 . 60 LEU HG H 1.65 0.01 1 689 . 60 LEU HD1 H 0.93 0.01 2 690 . 60 LEU HD2 H 0.88 0.01 2 691 . 60 LEU C C 177.6 0.1 1 692 . 60 LEU CA C 55.9 0.1 1 693 . 60 LEU CB C 42.0 0.1 1 694 . 60 LEU CG C 27.1 0.1 1 695 . 60 LEU CD1 C 24.6 0.1 2 696 . 60 LEU CD2 C 23.9 0.1 2 697 . 60 LEU N N 124.0 0.1 1 698 . 61 LEU H H 7.96 0.01 1 699 . 61 LEU HA H 4.26 0.01 1 700 . 61 LEU HB2 H 1.65 0.01 1 701 . 61 LEU HB3 H 1.65 0.01 1 702 . 61 LEU HG H 1.65 0.01 1 703 . 61 LEU HD1 H 0.91 0.01 2 704 . 61 LEU HD2 H 0.86 0.01 2 705 . 61 LEU C C 177.6 0.1 1 706 . 61 LEU CA C 55.9 0.1 1 707 . 61 LEU CB C 42.2 0.1 1 708 . 61 LEU CG C 27.2 0.1 1 709 . 61 LEU CD1 C 25.0 0.1 2 710 . 61 LEU CD2 C 23.6 0.1 2 711 . 61 LEU N N 121.2 0.1 1 712 . 62 LYS H H 8.02 0.01 1 713 . 62 LYS HA H 4.24 0.01 1 714 . 62 LYS HB2 H 1.80 0.01 1 715 . 62 LYS HB3 H 1.80 0.01 1 716 . 62 LYS HG2 H 1.46 0.01 1 717 . 62 LYS HG3 H 1.46 0.01 1 718 . 62 LYS HD2 H 1.68 0.01 1 719 . 62 LYS HD3 H 1.68 0.01 1 720 . 62 LYS HE2 H 3.02 0.01 1 721 . 62 LYS HE3 H 3.21 0.01 1 722 . 62 LYS C C 176.7 0.1 1 723 . 62 LYS CA C 57.0 0.1 1 724 . 62 LYS CB C 33.0 0.1 1 725 . 62 LYS CG C 24.9 0.1 1 726 . 62 LYS CD C 29.3 0.1 1 727 . 62 LYS CE C 42.2 0.1 1 728 . 62 LYS N N 121.1 0.1 1 729 . 63 ARG H H 8.16 0.01 1 730 . 63 ARG HA H 4.32 0.01 1 731 . 63 ARG HB2 H 1.81 0.01 1 732 . 63 ARG HB3 H 1.81 0.01 1 733 . 63 ARG HG2 H 1.63 0.01 1 734 . 63 ARG HG3 H 1.63 0.01 1 735 . 63 ARG HD2 H 3.20 0.01 1 736 . 63 ARG HD3 H 3.20 0.01 1 737 . 63 ARG C C 176.6 0.1 1 738 . 63 ARG CA C 56.7 0.1 1 739 . 63 ARG CB C 30.7 0.1 1 740 . 63 ARG CG C 27.1 0.1 1 741 . 63 ARG CD C 43.4 0.1 1 742 . 63 ARG N N 121.4 0.1 1 743 . 64 ILE H H 8.16 0.01 1 744 . 64 ILE HA H 4.18 0.01 1 745 . 64 ILE HB H 1.86 0.01 1 746 . 64 ILE HG12 H 1.47 0.01 2 747 . 64 ILE HG13 H 1.20 0.01 2 748 . 64 ILE HG2 H 0.88 0.01 1 749 . 64 ILE HD1 H 0.85 0.01 1 750 . 64 ILE C C 176.0 0.1 1 751 . 64 ILE CA C 61.1 0.1 1 752 . 64 ILE CB C 38.6 0.1 1 753 . 64 ILE CG1 C 27.3 0.1 1 754 . 64 ILE CG2 C 17.6 0.1 1 755 . 64 ILE CD1 C 12.8 0.1 1 756 . 64 ILE N N 121.8 0.1 1 757 . 65 ARG H H 8.38 0.01 1 758 . 65 ARG HA H 4.42 0.01 1 759 . 65 ARG HB2 H 1.91 0.01 2 760 . 65 ARG HB3 H 1.75 0.01 2 761 . 65 ARG HG2 H 1.64 0.01 1 762 . 65 ARG HG3 H 1.64 0.01 1 763 . 65 ARG HD2 H 3.21 0.01 1 764 . 65 ARG HD3 H 3.21 0.01 1 765 . 65 ARG C C 174.9 0.1 1 766 . 65 ARG CA C 55.9 0.1 1 767 . 65 ARG CB C 31.1 0.1 1 768 . 65 ARG CG C 27.2 0.1 1 769 . 65 ARG CD C 43.6 0.1 1 770 . 65 ARG N N 125.6 0.1 1 771 . 66 ASN H H 8.10 0.01 1 772 . 66 ASN HA H 4.51 0.01 1 773 . 66 ASN HB2 H 2.79 0.01 2 774 . 66 ASN HB3 H 2.72 0.01 2 775 . 66 ASN C C 176.4 0.1 1 776 . 66 ASN CA C 54.8 0.1 1 777 . 66 ASN CB C 41.4 0.1 1 778 . 66 ASN N N 126.1 0.1 1 779 . 67 GLY H H 8.39 0.01 1 780 . 67 GLY HA2 H 3.95 0.01 1 781 . 67 GLY HA3 H 3.95 0.01 1 782 . 67 GLY C C 174.7 0.1 1 783 . 67 GLY CA C 45.7 0.1 1 784 . 67 GLY N N 113.9 0.1 1 785 . 68 LYS H H 8.32 0.01 1 786 . 68 LYS HA H 4.34 0.01 1 787 . 68 LYS HB2 H 1.83 0.01 2 788 . 68 LYS HB3 H 1.73 0.01 2 789 . 68 LYS HG2 H 1.42 0.01 1 790 . 68 LYS HG3 H 1.42 0.01 1 791 . 68 LYS HD2 H 1.73 0.01 1 792 . 68 LYS HD3 H 1.73 0.01 1 793 . 68 LYS HE2 H 3.00 0.01 1 794 . 68 LYS HE3 H 3.00 0.01 1 795 . 68 LYS C C 176.9 0.1 1 796 . 68 LYS CA C 56.5 0.1 1 797 . 68 LYS CB C 33.2 0.1 1 798 . 68 LYS CG C 24.8 0.1 1 799 . 68 LYS CD C 29.1 0.1 1 800 . 68 LYS CE C 42.0 0.1 1 801 . 68 LYS N N 120.8 0.1 1 802 . 69 LYS H H 8.34 0.01 1 803 . 69 LYS HA H 4.31 0.01 1 804 . 69 LYS HB2 H 1.83 0.01 2 805 . 69 LYS HB3 H 1.73 0.01 2 806 . 69 LYS HG2 H 1.46 0.01 1 807 . 69 LYS HG3 H 1.46 0.01 1 808 . 69 LYS HD2 H 1.73 0.01 1 809 . 69 LYS HD3 H 1.73 0.01 1 810 . 69 LYS HE2 H 3.02 0.01 1 811 . 69 LYS HE3 H 3.02 0.01 1 812 . 69 LYS C C 176.3 0.1 1 813 . 69 LYS CA C 56.3 0.1 1 814 . 69 LYS CB C 33.2 0.1 1 815 . 69 LYS CG C 24.8 0.1 1 816 . 69 LYS CD C 29.2 0.1 1 817 . 69 LYS CE C 42.1 0.1 1 818 . 69 LYS N N 122.8 0.1 1 819 . 70 ALA H H 8.33 0.01 1 820 . 70 ALA HA H 4.33 0.01 1 821 . 70 ALA HB H 1.41 0.01 1 822 . 70 ALA C C 177.6 0.1 1 823 . 70 ALA CA C 52.5 0.1 1 824 . 70 ALA CB C 19.6 0.1 1 825 . 70 ALA N N 126.0 0.1 1 826 . 71 LYS H H 8.31 0.01 1 827 . 71 LYS HA H 4.37 0.01 1 828 . 71 LYS HB2 H 1.91 0.01 2 829 . 71 LYS HB3 H 1.79 0.01 2 830 . 71 LYS HG2 H 1.48 0.01 1 831 . 71 LYS HG3 H 1.48 0.01 1 832 . 71 LYS HD2 H 1.73 0.01 1 833 . 71 LYS HD3 H 1.73 0.01 1 834 . 71 LYS HE2 H 3.03 0.01 1 835 . 71 LYS HE3 H 3.03 0.01 1 836 . 71 LYS C C 175.8 0.1 1 837 . 71 LYS CA C 56.5 0.1 1 838 . 71 LYS CB C 33.2 0.1 1 839 . 71 LYS CG C 24.8 0.1 1 840 . 71 LYS CD C 29.2 0.1 1 841 . 71 LYS CE C 42.2 0.1 1 842 . 71 LYS N N 121.2 0.1 1 843 . 72 SER H H 7.99 0.01 1 844 . 72 SER HA H 4.33 0.01 1 845 . 72 SER HB2 H 3.91 0.01 1 846 . 72 SER HB3 H 3.91 0.01 1 847 . 72 SER C C 178.7 0.1 1 848 . 72 SER CA C 60.0 0.1 1 849 . 72 SER CB C 64.9 0.1 1 850 . 72 SER N N 122.8 0.1 1 stop_ save_