data_4704 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate ; _BMRB_accession_number 4704 _BMRB_flat_file_name bmr4704.str _Entry_type original _Submission_date 2000-03-30 _Accession_date 2000-03-30 _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 Connelly Gregory P. . 2 Withers Stephen G. . 3 McIntosh Lawrence P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 177 "13C chemical shifts" 341 "15N chemical shifts" 177 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-05-08 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 4705 2FXb-BCX stop_ _Original_release_date 2000-05-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate ; _Citation_status published _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 Connelly Gregory P. . 2 Withers Stephen G. . 3 McIntosh Lawrence P. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 9 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 512 _Page_last 524 _Year 2000 _Details . loop_ _Keyword '1H and 15N assigned chemical shifts' 'BCX (Bacillus circulans xylanase)' 'Order parameters' 'Relaxation dynamics' Xylanase 'Glycosyl-enzyme intermediate' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full . _Citation_title 'Secondary structure and NMR assignments of Bacillus circulans xylanase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8762143 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Plesniak 'L. A.' A. . 2 Wakarchuk 'W. W.' W. . 3 McIntosh 'L. P.' P. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 5 _Journal_issue 6 _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 1118 _Page_last 1135 _Year 1996 _Details ; Bacillus circulans xylanase (BCX) is a member of the family of low molecular weight endo-beta-(1,4)-xylanases. The main-chain 1H, 13C, and 15N resonances of this 20.4-kDa enzyme were assigned using heteronuclear NMR experiments recorded on a combination of selectively and uniformly labeled protein samples. Using chemical shift, NOE, J coupling, and amide hydrogen exchange information, 14 beta-strands, arranged in a network of three beta-sheets, and a single alpha-helix were identified in BCX. The NMR-derived secondary structure and beta-sheet topology agree closely with that observed in the crystal structure of this protein. The HN of Ile 118 has a strongly upfield-shifted resonance at 4.03 ppm, indicative of a potential amide-aromatic hydrogen bond to the indole ring of Trp 71. This interaction, which is conserved in all low molecular weight xylanases of known structure, may play an important role in establishing the active site conformation of these enzymes. Following hen egg white and bacteriophage T4 lysozymes, B. circulans xylanase represents the third family of beta-glycanases for which extensive NMR assignments have been reported. These assignments provide the background for detailed studies of the mechanism of carbohydrate recognition and hydrolysis by this bacterial xylanase. ; save_ ################################## # Molecular system description # ################################## save_system_BCX _Saveframe_category molecular_system _Mol_system_name xylanase _Abbreviation_common BCX _Enzyme_commission_number 3.2.1.8 loop_ _Mol_system_component_name _Mol_label BCX $BCX stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'hydrolyzes beta-1,4 linkages in xylan' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BCX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common xylanase _Abbreviation_common BCX _Molecular_mass 20396 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 185 _Mol_residue_sequence ; ASTDYWQNWTDGGGIVNAVN GSGGNYSVNWSNTGNFVVGK GWTTGSPFRTINYNAGVWAP NGNGYLTLYGWTRSPLIEYY VVDSWGTYRPTGTYKGTVKS DGGTYDIYTTTRYNAPSIDG DRTTFTQYWSVRQTKRPTGS NATITFSNHVNAWKSHGMNL GSNWAYQVMATEGYQSSGSS NVTVW ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 SER 3 THR 4 ASP 5 TYR 6 TRP 7 GLN 8 ASN 9 TRP 10 THR 11 ASP 12 GLY 13 GLY 14 GLY 15 ILE 16 VAL 17 ASN 18 ALA 19 VAL 20 ASN 21 GLY 22 SER 23 GLY 24 GLY 25 ASN 26 TYR 27 SER 28 VAL 29 ASN 30 TRP 31 SER 32 ASN 33 THR 34 GLY 35 ASN 36 PHE 37 VAL 38 VAL 39 GLY 40 LYS 41 GLY 42 TRP 43 THR 44 THR 45 GLY 46 SER 47 PRO 48 PHE 49 ARG 50 THR 51 ILE 52 ASN 53 TYR 54 ASN 55 ALA 56 GLY 57 VAL 58 TRP 59 ALA 60 PRO 61 ASN 62 GLY 63 ASN 64 GLY 65 TYR 66 LEU 67 THR 68 LEU 69 TYR 70 GLY 71 TRP 72 THR 73 ARG 74 SER 75 PRO 76 LEU 77 ILE 78 GLU 79 TYR 80 TYR 81 VAL 82 VAL 83 ASP 84 SER 85 TRP 86 GLY 87 THR 88 TYR 89 ARG 90 PRO 91 THR 92 GLY 93 THR 94 TYR 95 LYS 96 GLY 97 THR 98 VAL 99 LYS 100 SER 101 ASP 102 GLY 103 GLY 104 THR 105 TYR 106 ASP 107 ILE 108 TYR 109 THR 110 THR 111 THR 112 ARG 113 TYR 114 ASN 115 ALA 116 PRO 117 SER 118 ILE 119 ASP 120 GLY 121 ASP 122 ARG 123 THR 124 THR 125 PHE 126 THR 127 GLN 128 TYR 129 TRP 130 SER 131 VAL 132 ARG 133 GLN 134 THR 135 LYS 136 ARG 137 PRO 138 THR 139 GLY 140 SER 141 ASN 142 ALA 143 THR 144 ILE 145 THR 146 PHE 147 SER 148 ASN 149 HIS 150 VAL 151 ASN 152 ALA 153 TRP 154 LYS 155 SER 156 HIS 157 GLY 158 MET 159 ASN 160 LEU 161 GLY 162 SER 163 ASN 164 TRP 165 ALA 166 TYR 167 GLN 168 VAL 169 MET 170 ALA 171 THR 172 GLU 173 GLY 174 TYR 175 GLN 176 SER 177 SER 178 GLY 179 SER 180 SER 181 ASN 182 VAL 183 THR 184 VAL 185 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 4705 xylanase 100.00 185 100.00 100.00 2.67e-125 PDB 1AXK "Engineered Bacillus Bifunctional Enzyme Gluxyn-1" 100.00 394 99.46 100.00 1.30e-122 PDB 1BCX "Mutational And Crystallographic Analyses Of The Active Site Residues Of The Bacillus Circulans Xylanase" 100.00 185 98.38 99.46 2.87e-123 PDB 1BVV "Sugar Ring Distortion In The Glycosyl-Enzyme Intermediate Of A Family G11 XYLANASE" 100.00 185 98.92 100.00 1.91e-124 PDB 1C5H "Hydrogen Bonding And Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change The Ph Optimum Of" 100.00 185 98.38 100.00 6.28e-124 PDB 1C5I "Hydrogen Bonding And Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change The Ph Optimum Of" 100.00 185 98.38 100.00 6.28e-124 PDB 1HV0 "Dissecting Electrostatic Interactions And The Ph-Dependent Activity Of A Family 11 Glycosidase" 100.00 185 98.38 100.00 4.67e-124 PDB 1HV1 "Dissecting Electrostatic Interactions And The Ph-Dependent Activity Of A Family 11 Glycosidase" 100.00 185 98.38 99.46 1.57e-123 PDB 1XNB "High-Resolution Structures Of Xylanases From B. Circulans And T. Harzianum Identify A New Folding Pattern And Implications For " 100.00 185 98.92 100.00 1.91e-124 PDB 1XNC "Thermostabilization Of The Bacillus Circulans Xylanase, By The Introduction Of Disulfide Bonds" 100.00 185 97.84 98.92 4.54e-123 PDB 1XXN "Crystal Structure Of A Mesophilic Xylanase A From Bacillus Subtilis 1a1" 100.00 185 99.46 100.00 6.83e-125 PDB 2B42 "Crystal Structure Of The Triticum Xylanse Inhibitor-I In Complex With Bacillus Subtilis Xylanase" 100.00 185 98.92 100.00 1.91e-124 PDB 2B45 "Crystal Structure Of An Engineered Uninhibited Bacillus Subtilis Xylanase In Free State" 100.00 185 97.84 98.92 5.99e-122 PDB 2B46 "Crystal Structure Of An Engineered Uninhibited Bacillus Subtilis Xylanase In Substrate Bound State" 100.00 185 98.38 98.92 2.10e-122 PDB 2BVV "Sugar Ring Distortion In The Glycosyl-Enzyme Intermediate Of A Family G11 XYLANASE" 100.00 185 98.38 100.00 4.67e-124 PDB 2DCY "Crystal Structure Of Bacillus Subtilis Family-11 Xylanase" 100.00 185 99.46 100.00 6.83e-125 PDB 2DCZ "Thermal Stabilization Of Bacillus Subtilis Family-11 Xylanase By Directed Evolution" 100.00 185 97.84 98.38 1.78e-122 PDB 2QZ3 "Crystal Structure Of A Glycoside Hydrolase Family 11 Xylanase From Bacillus Subtilis In Complex With Xylotetraose" 100.00 185 98.92 99.46 5.69e-124 PDB 2Z79 "High Resolution Crystal Structure Of A Glycoside Hydrolase Family 11 Xylanase Of Bacillus Subtilis" 100.00 185 98.92 99.46 5.69e-124 PDB 3EXU "A Glycoside Hydrolase Family 11 Xylanase With An Extended Thumb Region" 100.00 185 98.38 98.92 2.10e-122 PDB 3HD8 "Crystal Structure Of The Triticum Aestivum Xylanase Inhibitor-Iia In Complex With Bacillus Subtilis Xylanase" 100.00 185 98.92 100.00 1.91e-124 PDB 3VZJ "Crystal Structure Of The Bacillus Circulans Endo-beta-(1,4)-xylanase (bcx) E172h Mutant" 100.00 185 98.38 99.46 1.31e-123 PDB 3VZK "Crystal Structure Of The Bacillus Circulans Endo-beta-(1,4)-xylanase (bcx) N35e Mutant" 100.00 185 98.38 99.46 9.21e-124 PDB 3VZL "Crystal Structure Of The Bacillus Circulans Endo-beta-(1,4)-xylanase (bcx) N35h Mutant" 100.00 185 98.38 100.00 8.72e-124 PDB 3VZM "Crystal Structure Of The Bacillus Circulans Endo-beta-(1,4)-xylanase (bcx) E172h Mutant With Glu78 Covalently Bonded To 2-deoxy" 100.00 185 98.38 99.46 1.31e-123 PDB 3VZN "Crystal Structure Of The Bacillus Circulans Endo-beta-(1,4)-xylanase (bcx) N35e Mutant With Glu78 Covalently Bonded To 2-deoxy-" 100.00 185 98.38 99.46 9.21e-124 PDB 3VZO "Crystal Structure Of The Bacillus Circulans Endo-beta-(1,4)-xylanase (bcx) N35h Mutant With Glu78 Covalently Bonded To 2-deoxy-" 100.00 185 98.38 100.00 8.72e-124 DBJ BAH28803 "xylanase [Bacillus subtilis]" 100.00 213 100.00 100.00 1.41e-126 DBJ BAM52542 "endo-1,4-beta-xylanase [Bacillus subtilis BEST7613]" 100.00 213 99.46 100.00 3.95e-126 DBJ BAM58117 "endo-1,4-beta-xylanase [Bacillus subtilis BEST7003]" 100.00 213 99.46 100.00 3.95e-126 EMBL CAA30553 "unnamed protein product [Bacillus circulans]" 100.00 213 98.92 100.00 1.06e-125 EMBL CAA41783 "endo-1, 4-beta-xylanase [Bacillus sp. YA-14]" 100.00 213 99.46 100.00 5.79e-126 EMBL CAA84276 "xylanase [Bacillus subtilis]" 100.00 213 99.46 100.00 6.74e-126 EMBL CAB13776 "endo-1,4-beta-xylanase [Bacillus subtilis subsp. subtilis str. 168]" 100.00 213 99.46 100.00 3.95e-126 EMBL CCU58510 "Chain A, Crystal Structure Of A Mesophilic Xylanase A From Bacillus Subtilis 1a1 [Bacillus subtilis E1]" 100.00 213 100.00 100.00 1.41e-126 GB AAA22897 "xylanase (EC 3.2.1.8) [Bacillus subtilis]" 100.00 213 99.46 100.00 3.95e-126 GB AAB84458 "xylanase [Bacillus subtilis]" 100.00 213 99.46 100.00 3.95e-126 GB AAM08359 "endo-1,4-xylanase [Bacillus subtilis]" 100.00 213 98.92 99.46 6.54e-125 GB AAM08360 "endo-1,4-xylanase [Bacillus circulans]" 100.00 213 98.92 98.92 4.68e-124 GB AAW83159 "1,4-beta-xylanase, partial [synthetic construct]" 100.00 185 99.46 100.00 6.83e-125 PRF 1209158A xylanase 100.00 213 99.46 100.00 3.95e-126 REF NP_389765 "endo-1,4-beta-xylanase A [Bacillus subtilis subsp. subtilis str. 168]" 100.00 213 99.46 100.00 3.95e-126 REF WP_003231377 "MULTISPECIES: endo-1,4-beta-xylanase A [Bacillus]" 100.00 213 99.46 100.00 3.95e-126 REF WP_014477026 "endo-1,4-beta-xylanase A [Bacillus subtilis]" 100.00 213 98.92 100.00 1.73e-125 REF WP_014664226 "endo-1,4-beta-xylanase [Bacillus sp. JS]" 100.00 213 98.38 99.46 7.54e-125 REF WP_015251938 "MULTISPECIES: endo-1,4-beta-xylanase A [Bacillus]" 100.00 213 100.00 100.00 1.41e-126 SP P09850 "RecName: Full=Endo-1,4-beta-xylanase; Short=Xylanase; AltName: Full=1,4-beta-D-xylan xylanohydrolase; Flags: Precursor" 100.00 213 98.92 100.00 1.06e-125 SP P18429 "RecName: Full=Endo-1,4-beta-xylanase A; Short=Xylanase A; AltName: Full=1,4-beta-D-xylan xylanohydrolase A; Flags: Precursor" 100.00 213 99.46 100.00 3.95e-126 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BCX 'Bacillus circulans' 1397 Eubacteria . Bacillus circulans 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 $BCX 'recombinant technology' 'E. coli' Escherichia coli K12 plasmid . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_apo-BCX _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BCX 0.9 mM '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 95 loop_ _Task ; data processing peak assignments ; stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCACB_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $apo-BCX save_ save_CBCACONH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label $apo-BCX save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.7 0.1 n/a temperature 303 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; Referenced to 2.9 M NH4Cl in 1 M HCl at 29.43 ppm. This yields 15N shifts 1.6 ppm greater than obtained using liquid NH3 HN, N, CA, and CB shifts for the free (apo) BCX, as originally reported in Plesniak, Wakarchuk, and McIntosh, Protein Science, 5, 1118-1135, 1996 HN, N, CA, and CB shifts for BCX covalently modified with 2-deoxy-2fluoro-xylobiose at Glu78 (2FXb-BCX). These shifts correspond to the primary reference of Connelly, Withers, and McIntosh, Protein Science. Original assignments reported in Plesniak, Wakarchuk and McIntosh, Protein Sceince, 5: 1118-1135 (1996) ; 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 DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo DSS C 13 'methyl carbons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo NH4Cl N 15 nitrogen ppm 29.43 external direct cylindrical external_to_the_sample parallel_to_Bo stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCACB CBCACONH stop_ loop_ _Sample_label $apo-BCX stop_ _Sample_conditions_label $Conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BCX _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 . 3 THR H H 8.370 0.020 1 2 . 3 THR CA C 61.700 0.300 1 3 . 3 THR CB C 69.700 0.300 1 4 . 3 THR N N 116.300 0.200 1 5 . 4 ASP H H 8.020 0.020 1 6 . 4 ASP CA C 53.600 0.300 1 7 . 4 ASP CB C 42.300 0.300 1 8 . 4 ASP N N 120.400 0.200 1 9 . 5 TYR H H 7.840 0.020 1 10 . 5 TYR CA C 58.400 0.300 1 11 . 5 TYR CB C 42.300 0.300 1 12 . 5 TYR N N 122.200 0.200 1 13 . 6 TRP H H 7.400 0.020 1 14 . 6 TRP CA C 54.600 0.300 1 15 . 6 TRP CB C 32.900 0.300 1 16 . 6 TRP N N 133.600 0.200 1 17 . 7 GLN H H 8.130 0.020 1 18 . 7 GLN CA C 52.600 0.300 1 19 . 7 GLN CB C 30.000 0.300 1 20 . 7 GLN N N 128.900 0.200 1 21 . 8 ASN H H 7.980 0.020 1 22 . 8 ASN CA C 52.600 0.300 1 23 . 8 ASN CB C 37.300 0.300 1 24 . 8 ASN N N 125.400 0.200 1 25 . 9 TRP H H 8.600 0.020 1 26 . 9 TRP CA C 57.500 0.300 1 27 . 9 TRP CB C 31.500 0.300 1 28 . 9 TRP N N 127.500 0.200 1 29 . 10 THR H H 7.100 0.020 1 30 . 10 THR CA C 57.800 0.300 1 31 . 10 THR CB C 70.500 0.300 1 32 . 10 THR N N 120.900 0.200 1 33 . 11 ASP H H 7.500 0.020 1 34 . 11 ASP CA C 53.700 0.300 1 35 . 11 ASP CB C 40.200 0.300 1 36 . 11 ASP N N 124.100 0.200 1 37 . 12 GLY H H 8.440 0.020 1 38 . 12 GLY CA C 44.800 0.300 1 39 . 12 GLY N N 110.600 0.200 1 40 . 13 GLY H H 8.470 0.020 1 41 . 13 GLY CA C 45.100 0.300 1 42 . 13 GLY N N 111.000 0.200 1 43 . 14 GLY H H 8.480 0.020 1 44 . 14 GLY CA C 46.400 0.300 1 45 . 14 GLY N N 113.800 0.200 1 46 . 15 ILE H H 8.180 0.020 1 47 . 15 ILE CA C 60.200 0.300 1 48 . 15 ILE CB C 40.900 0.300 1 49 . 15 ILE N N 122.700 0.200 1 50 . 16 VAL H H 8.460 0.020 1 51 . 16 VAL CA C 62.500 0.300 1 52 . 16 VAL CB C 33.100 0.300 1 53 . 16 VAL N N 128.800 0.200 1 54 . 17 ASN H H 8.750 0.020 1 55 . 17 ASN CA C 52.100 0.300 1 56 . 17 ASN CB C 38.700 0.300 1 57 . 17 ASN N N 127.800 0.200 1 58 . 18 ALA H H 8.790 0.020 1 59 . 18 ALA CA C 50.100 0.300 1 60 . 18 ALA CB C 22.100 0.300 1 61 . 18 ALA N N 131.400 0.200 1 62 . 19 VAL H H 9.400 0.020 1 63 . 19 VAL CA C 62.400 0.300 1 64 . 19 VAL CB C 34.000 0.300 1 65 . 19 VAL N N 126.100 0.200 1 66 . 20 ASN H H 8.350 0.020 1 67 . 20 ASN CA C 51.800 0.300 1 68 . 20 ASN CB C 35.600 0.300 1 69 . 20 ASN N N 127.600 0.200 1 70 . 21 GLY H H 7.230 0.020 1 71 . 21 GLY CA C 44.200 0.300 1 72 . 21 GLY N N 114.700 0.200 1 73 . 22 SER H H 8.300 0.020 1 74 . 22 SER CA C 58.800 0.300 1 75 . 22 SER CB C 63.800 0.300 1 76 . 22 SER N N 114.300 0.200 1 77 . 23 GLY H H 8.900 0.020 1 78 . 23 GLY CA C 47.500 0.300 1 79 . 23 GLY N N 115.100 0.200 1 80 . 24 GLY H H 9.300 0.020 1 81 . 24 GLY CA C 46.100 0.300 1 82 . 24 GLY N N 117.400 0.200 1 83 . 25 ASN H H 8.180 0.020 1 84 . 25 ASN CA C 54.400 0.300 1 85 . 25 ASN CB C 42.900 0.300 1 86 . 25 ASN N N 120.500 0.200 1 87 . 26 TYR H H 9.740 0.020 1 88 . 26 TYR CA C 57.800 0.300 1 89 . 26 TYR CB C 42.900 0.300 1 90 . 26 TYR N N 126.900 0.200 1 91 . 27 SER H H 8.750 0.020 1 92 . 27 SER CA C 56.700 0.300 1 93 . 27 SER CB C 66.600 0.300 1 94 . 27 SER N N 113.000 0.200 1 95 . 28 VAL H H 9.180 0.020 1 96 . 28 VAL CA C 61.200 0.300 1 97 . 28 VAL CB C 34.900 0.300 1 98 . 28 VAL N N 120.600 0.200 1 99 . 29 ASN H H 8.480 0.020 1 100 . 29 ASN CA C 53.300 0.300 1 101 . 29 ASN CB C 41.800 0.300 1 102 . 29 ASN N N 127.700 0.200 1 103 . 30 TRP H H 9.160 0.020 1 104 . 30 TRP CA C 55.900 0.300 1 105 . 30 TRP CB C 33.000 0.300 1 106 . 30 TRP N N 126.900 0.200 1 107 . 31 SER H H 9.230 0.020 1 108 . 31 SER CA C 57.500 0.300 1 109 . 31 SER CB C 65.100 0.300 1 110 . 31 SER N N 117.700 0.200 1 111 . 32 ASN H H 8.320 0.020 1 112 . 32 ASN CA C 54.400 0.300 1 113 . 32 ASN CB C 37.700 0.300 1 114 . 32 ASN N N 127.500 0.200 1 115 . 33 THR H H 8.330 0.020 1 116 . 33 THR CA C 63.200 0.300 1 117 . 33 THR CB C 71.500 0.300 1 118 . 33 THR N N 107.500 0.200 1 119 . 34 GLY H H 7.610 0.020 1 120 . 34 GLY CA C 46.500 0.300 1 121 . 34 GLY N N 107.400 0.200 1 122 . 35 ASN H H 9.680 0.020 1 123 . 35 ASN CA C 52.600 0.300 1 124 . 35 ASN CB C 42.000 0.300 1 125 . 35 ASN N N 129.200 0.200 1 126 . 36 PHE H H 7.760 0.020 1 127 . 36 PHE CA C 67.100 0.300 1 128 . 36 PHE CB C 41.800 0.300 1 129 . 36 PHE N N 121.000 0.200 1 130 . 37 VAL H H 9.160 0.020 1 131 . 37 VAL CA C 62.900 0.300 1 132 . 37 VAL CB C 35.500 0.300 1 133 . 37 VAL N N 121.300 0.200 1 134 . 38 VAL H H 8.600 0.020 1 135 . 38 VAL CA C 58.700 0.300 1 136 . 38 VAL CB C 36.700 0.300 1 137 . 38 VAL N N 128.500 0.200 1 138 . 39 GLY H H 8.400 0.020 1 139 . 39 GLY CA C 45.800 0.300 1 140 . 39 GLY N N 110.100 0.200 1 141 . 40 LYS H H 6.440 0.020 1 142 . 40 LYS CA C 54.800 0.300 1 143 . 40 LYS CB C 38.700 0.300 1 144 . 40 LYS N N 117.000 0.200 1 145 . 41 GLY H H 7.930 0.020 1 146 . 41 GLY CA C 47.500 0.300 1 147 . 41 GLY N N 109.600 0.200 1 148 . 42 TRP H H 9.610 0.020 1 149 . 42 TRP CA C 59.900 0.300 1 150 . 42 TRP CB C 32.600 0.300 1 151 . 42 TRP N N 131.500 0.200 1 152 . 43 THR H H 10.240 0.020 1 153 . 43 THR CA C 66.200 0.300 1 154 . 43 THR CB C 69.700 0.300 1 155 . 43 THR N N 125.000 0.200 1 156 . 44 THR H H 8.500 0.020 1 157 . 44 THR CA C 60.600 0.300 1 158 . 44 THR CB C 70.300 0.300 1 159 . 44 THR N N 115.700 0.200 1 160 . 45 GLY H H 8.180 0.020 1 161 . 45 GLY CA C 46.000 0.300 1 162 . 45 GLY N N 111.400 0.200 1 163 . 46 SER H H 6.820 0.020 1 164 . 46 SER CA C 52.300 0.300 1 165 . 46 SER CB C 65.700 0.300 1 166 . 46 SER N N 111.000 0.200 1 167 . 47 PRO CA C 63.000 0.300 1 168 . 47 PRO CB C 31.400 0.300 1 169 . 48 PHE H H 7.190 0.020 1 170 . 48 PHE CA C 55.700 0.300 1 171 . 48 PHE CB C 39.400 0.300 1 172 . 48 PHE N N 114.800 0.200 1 173 . 49 ARG H H 6.580 0.020 1 174 . 49 ARG CA C 57.100 0.300 1 175 . 49 ARG CB C 31.600 0.300 1 176 . 49 ARG N N 123.200 0.200 1 177 . 50 THR H H 8.570 0.020 1 178 . 50 THR CA C 62.600 0.300 1 179 . 50 THR CB C 69.300 0.300 1 180 . 50 THR N N 126.000 0.200 1 181 . 51 ILE H H 8.700 0.020 1 182 . 51 ILE CA C 62.400 0.300 1 183 . 51 ILE CB C 40.100 0.300 1 184 . 51 ILE N N 130.300 0.200 1 185 . 52 ASN H H 8.770 0.020 1 186 . 52 ASN CA C 51.100 0.300 1 187 . 52 ASN CB C 40.000 0.300 1 188 . 52 ASN N N 127.700 0.200 1 189 . 53 TYR H H 8.610 0.020 1 190 . 53 TYR CA C 56.900 0.300 1 191 . 53 TYR CB C 41.100 0.300 1 192 . 53 TYR N N 116.900 0.200 1 193 . 54 ASN H H 8.910 0.020 1 194 . 54 ASN CA C 53.100 0.300 1 195 . 54 ASN CB C 40.900 0.300 1 196 . 54 ASN N N 118.100 0.200 1 197 . 55 ALA H H 9.670 0.020 1 198 . 55 ALA CA C 50.300 0.300 1 199 . 55 ALA CB C 18.200 0.300 1 200 . 55 ALA N N 134.000 0.200 1 201 . 56 GLY H H 8.320 0.020 1 202 . 56 GLY CA C 47.100 0.300 1 203 . 56 GLY N N 117.500 0.200 1 204 . 57 VAL H H 8.200 0.020 1 205 . 57 VAL CA C 62.500 0.300 1 206 . 57 VAL CB C 35.800 0.300 1 207 . 57 VAL N N 118.900 0.200 1 208 . 58 TRP H H 8.990 0.020 1 209 . 58 TRP CA C 56.300 0.300 1 210 . 58 TRP CB C 31.000 0.300 1 211 . 58 TRP N N 129.100 0.200 1 212 . 59 ALA H H 8.050 0.020 1 213 . 59 ALA CA C 49.700 0.300 1 214 . 59 ALA CB C 18.400 0.300 1 215 . 59 ALA N N 129.600 0.200 1 216 . 60 PRO CA C 63.600 0.300 1 217 . 60 PRO CB C 31.200 0.300 1 218 . 61 ASN H H 9.310 0.020 1 219 . 61 ASN CA C 52.000 0.300 1 220 . 61 ASN CB C 37.500 0.300 1 221 . 61 ASN N N 126.500 0.200 1 222 . 62 GLY H H 8.130 0.020 1 223 . 62 GLY CA C 44.400 0.300 1 224 . 62 GLY N N 110.300 0.200 1 225 . 63 ASN H H 8.910 0.020 1 226 . 63 ASN CA C 53.800 0.300 1 227 . 63 ASN CB C 38.000 0.300 1 228 . 63 ASN N N 124.600 0.200 1 229 . 64 GLY H H 8.040 0.020 1 230 . 64 GLY CA C 46.400 0.300 1 231 . 64 GLY N N 118.900 0.200 1 232 . 65 TYR H H 9.680 0.020 1 233 . 65 TYR CA C 54.100 0.300 1 234 . 65 TYR CB C 42.600 0.300 1 235 . 65 TYR N N 119.500 0.200 1 236 . 66 LEU H H 7.950 0.020 1 237 . 66 LEU CA C 54.200 0.300 1 238 . 66 LEU CB C 40.700 0.300 1 239 . 66 LEU N N 127.800 0.200 1 240 . 67 THR H H 8.950 0.020 1 241 . 67 THR CA C 58.100 0.300 1 242 . 67 THR CB C 72.600 0.300 1 243 . 67 THR N N 123.000 0.200 1 244 . 68 LEU H H 9.310 0.020 1 245 . 68 LEU CA C 56.100 0.300 1 246 . 68 LEU CB C 43.300 0.300 1 247 . 68 LEU N N 135.000 0.200 1 248 . 69 TYR H H 9.620 0.020 1 249 . 69 TYR CA C 56.500 0.300 1 250 . 69 TYR CB C 43.400 0.300 1 251 . 69 TYR N N 134.300 0.200 1 252 . 70 GLY H H 6.400 0.020 1 253 . 70 GLY CA C 45.600 0.300 1 254 . 70 GLY N N 113.400 0.200 1 255 . 71 TRP H H 6.110 0.020 1 256 . 71 TRP CA C 55.100 0.300 1 257 . 71 TRP CB C 35.400 0.300 1 258 . 71 TRP N N 111.900 0.200 1 259 . 72 THR H H 9.130 0.020 1 260 . 72 THR CA C 60.700 0.300 1 261 . 72 THR CB C 72.900 0.300 1 262 . 72 THR N N 113.800 0.200 1 263 . 73 ARG H H 8.870 0.020 1 264 . 73 ARG CA C 55.400 0.300 1 265 . 73 ARG CB C 33.400 0.300 1 266 . 73 ARG N N 118.000 0.200 1 267 . 74 SER H H 8.570 0.020 1 268 . 74 SER CA C 57.800 0.300 1 269 . 74 SER CB C 62.000 0.300 1 270 . 74 SER N N 111.600 0.200 1 271 . 75 PRO CA C 63.200 0.300 1 272 . 75 PRO CB C 34.800 0.300 1 273 . 76 LEU H H 7.760 0.020 1 274 . 76 LEU CA C 54.900 0.300 1 275 . 76 LEU CB C 42.600 0.300 1 276 . 76 LEU N N 120.400 0.200 1 277 . 77 ILE H H 8.100 0.020 1 278 . 77 ILE CA C 59.100 0.300 1 279 . 77 ILE CB C 41.200 0.300 1 280 . 77 ILE N N 131.100 0.200 1 281 . 78 GLU H H 7.420 0.020 1 282 . 78 GLU CA C 52.900 0.300 1 283 . 78 GLU CB C 32.100 0.300 1 284 . 78 GLU N N 130.200 0.200 1 285 . 79 TYR H H 7.710 0.020 1 286 . 79 TYR CA C 54.600 0.300 1 287 . 79 TYR CB C 42.500 0.300 1 288 . 79 TYR N N 124.000 0.200 1 289 . 80 TYR H H 8.150 0.020 1 290 . 80 TYR CA C 57.000 0.300 1 291 . 80 TYR CB C 44.600 0.300 1 292 . 80 TYR N N 115.900 0.200 1 293 . 81 VAL H H 8.080 0.020 1 294 . 81 VAL CA C 62.700 0.300 1 295 . 81 VAL CB C 32.200 0.300 1 296 . 81 VAL N N 121.400 0.200 1 297 . 82 VAL H H 9.630 0.020 1 298 . 82 VAL CA C 62.900 0.300 1 299 . 82 VAL CB C 33.900 0.300 1 300 . 82 VAL N N 128.200 0.200 1 301 . 83 ASP H H 8.400 0.020 1 302 . 83 ASP CA C 54.900 0.300 1 303 . 83 ASP CB C 43.600 0.300 1 304 . 83 ASP N N 129.900 0.200 1 305 . 84 SER H H 8.230 0.020 1 306 . 84 SER CA C 57.600 0.300 1 307 . 84 SER CB C 57.600 0.300 1 308 . 84 SER N N 109.600 0.200 1 309 . 85 TRP H H 7.740 0.020 1 310 . 85 TRP CA C 57.300 0.300 1 311 . 85 TRP CB C 29.400 0.300 1 312 . 85 TRP N N 120.900 0.200 1 313 . 86 GLY H H 9.340 0.020 1 314 . 86 GLY CA C 45.100 0.300 1 315 . 86 GLY N N 111.900 0.200 1 316 . 87 THR H H 8.050 0.020 1 317 . 87 THR CA C 63.500 0.300 1 318 . 87 THR CB C 69.000 0.300 1 319 . 87 THR N N 118.900 0.200 1 320 . 88 TYR H H 8.180 0.020 1 321 . 88 TYR CA C 56.700 0.300 1 322 . 88 TYR CB C 40.900 0.300 1 323 . 88 TYR N N 123.600 0.200 1 324 . 89 ARG H H 8.070 0.020 1 325 . 89 ARG CA C 51.700 0.300 1 326 . 89 ARG CB C 30.300 0.300 1 327 . 89 ARG N N 133.800 0.200 1 328 . 90 PRO CA C 63.000 0.300 1 329 . 90 PRO CB C 30.300 0.300 1 330 . 91 THR H H 6.030 0.020 1 331 . 91 THR CA C 58.700 0.300 1 332 . 91 THR CB C 72.000 0.300 1 333 . 91 THR N N 106.700 0.200 1 334 . 92 GLY H H 5.220 0.020 1 335 . 92 GLY CA C 46.100 0.300 1 336 . 92 GLY N N 108.500 0.200 1 337 . 93 THR H H 9.020 0.020 1 338 . 93 THR CA C 64.200 0.300 1 339 . 93 THR CB C 68.600 0.300 1 340 . 93 THR N N 125.700 0.200 1 341 . 94 TYR H H 9.090 0.020 1 342 . 94 TYR CA C 60.000 0.300 1 343 . 94 TYR CB C 39.200 0.300 1 344 . 94 TYR N N 132.000 0.200 1 345 . 95 LYS H H 8.470 0.020 1 346 . 95 LYS CA C 53.900 0.300 1 347 . 95 LYS CB C 33.500 0.300 1 348 . 95 LYS N N 125.700 0.200 1 349 . 96 GLY H H 5.610 0.020 1 350 . 96 GLY CA C 44.900 0.300 1 351 . 96 GLY N N 104.600 0.200 1 352 . 97 THR H H 8.130 0.020 1 353 . 97 THR CA C 60.200 0.300 1 354 . 97 THR CB C 74.300 0.300 1 355 . 97 THR N N 110.300 0.200 1 356 . 98 VAL H H 9.290 0.020 1 357 . 98 VAL CA C 59.700 0.300 1 358 . 98 VAL CB C 34.800 0.300 1 359 . 98 VAL N N 121.000 0.200 1 360 . 99 LYS H H 8.510 0.020 1 361 . 99 LYS CA C 54.900 0.300 1 362 . 99 LYS CB C 33.000 0.300 1 363 . 99 LYS N N 130.300 0.200 1 364 . 100 SER H H 8.750 0.020 1 365 . 100 SER CA C 59.400 0.300 1 366 . 100 SER CB C 64.400 0.300 1 367 . 100 SER N N 118.000 0.200 1 368 . 101 ASP H H 9.660 0.020 1 369 . 101 ASP CA C 55.800 0.300 1 370 . 101 ASP CB C 41.700 0.300 1 371 . 101 ASP N N 125.600 0.200 1 372 . 102 GLY H H 8.840 0.020 1 373 . 102 GLY CA C 46.100 0.300 1 374 . 102 GLY N N 106.900 0.200 1 375 . 103 GLY H H 8.230 0.020 1 376 . 103 GLY CA C 43.400 0.300 1 377 . 103 GLY N N 110.400 0.200 1 378 . 104 THR H H 8.060 0.020 1 379 . 104 THR CA C 62.700 0.300 1 380 . 104 THR CB C 70.000 0.300 1 381 . 104 THR N N 117.500 0.200 1 382 . 105 TYR H H 9.810 0.020 1 383 . 105 TYR CA C 56.100 0.300 1 384 . 105 TYR CB C 39.600 0.300 1 385 . 105 TYR N N 127.400 0.200 1 386 . 106 ASP H H 8.810 0.020 1 387 . 106 ASP CA C 54.500 0.300 1 388 . 106 ASP CB C 44.900 0.300 1 389 . 106 ASP N N 123.200 0.200 1 390 . 107 ILE H H 8.450 0.020 1 391 . 107 ILE CA C 59.600 0.300 1 392 . 107 ILE CB C 39.400 0.300 1 393 . 107 ILE N N 122.900 0.200 1 394 . 108 TYR H H 9.190 0.020 1 395 . 108 TYR CA C 54.800 0.300 1 396 . 108 TYR CB C 43.400 0.300 1 397 . 108 TYR N N 124.200 0.200 1 398 . 109 THR H H 8.360 0.020 1 399 . 109 THR CA C 60.000 0.300 1 400 . 109 THR CB C 71.800 0.300 1 401 . 109 THR N N 110.000 0.200 1 402 . 110 THR H H 8.840 0.020 1 403 . 110 THR CA C 61.700 0.300 1 404 . 110 THR CB C 73.100 0.300 1 405 . 110 THR N N 115.800 0.200 1 406 . 111 THR H H 8.490 0.020 1 407 . 111 THR CA C 62.400 0.300 1 408 . 111 THR CB C 71.400 0.300 1 409 . 111 THR N N 118.400 0.200 1 410 . 112 ARG H H 8.320 0.020 1 411 . 112 ARG CA C 53.600 0.300 1 412 . 112 ARG CB C 30.900 0.300 1 413 . 112 ARG N N 127.100 0.200 1 414 . 113 TYR H H 8.160 0.020 1 415 . 113 TYR CA C 56.700 0.300 1 416 . 113 TYR CB C 40.700 0.300 1 417 . 113 TYR N N 121.000 0.200 1 418 . 114 ASN H H 8.010 0.020 1 419 . 114 ASN CA C 54.100 0.300 1 420 . 114 ASN CB C 37.200 0.300 1 421 . 114 ASN N N 122.300 0.200 1 422 . 115 ALA H H 9.310 0.020 1 423 . 115 ALA CA C 50.100 0.300 1 424 . 115 ALA CB C 22.000 0.300 1 425 . 115 ALA N N 124.100 0.200 1 426 . 116 PRO CA C 63.000 0.300 1 427 . 116 PRO CB C 31.400 0.300 1 428 . 117 SER H H 8.640 0.020 1 429 . 117 SER CA C 56.500 0.300 1 430 . 117 SER CB C 68.200 0.300 1 431 . 117 SER N N 116.800 0.200 1 432 . 118 ILE H H 4.030 0.020 1 433 . 118 ILE CA C 63.100 0.300 1 434 . 118 ILE CB C 36.400 0.300 1 435 . 118 ILE N N 113.600 0.200 1 436 . 119 ASP H H 7.210 0.020 1 437 . 119 ASP CA C 54.100 0.300 1 438 . 119 ASP CB C 42.100 0.300 1 439 . 119 ASP N N 120.900 0.200 1 440 . 120 GLY H H 7.210 0.020 1 441 . 120 GLY CA C 45.100 0.300 1 442 . 120 GLY N N 109.500 0.200 1 443 . 121 ASP H H 8.110 0.020 1 444 . 121 ASP CA C 55.300 0.300 1 445 . 121 ASP CB C 41.500 0.300 1 446 . 121 ASP N N 119.300 0.200 1 447 . 122 ARG H H 8.260 0.020 1 448 . 122 ARG CA C 55.400 0.300 1 449 . 122 ARG CB C 30.700 0.300 1 450 . 122 ARG N N 121.800 0.200 1 451 . 123 THR H H 9.030 0.020 1 452 . 123 THR CA C 60.600 0.300 1 453 . 123 THR CB C 72.400 0.300 1 454 . 123 THR N N 118.200 0.200 1 455 . 124 THR H H 8.300 0.020 1 456 . 124 THR CA C 60.700 0.300 1 457 . 124 THR CB C 71.700 0.300 1 458 . 124 THR N N 119.600 0.200 1 459 . 125 PHE H H 8.160 0.020 1 460 . 125 PHE CA C 56.000 0.300 1 461 . 125 PHE CB C 39.700 0.300 1 462 . 125 PHE N N 123.600 0.200 1 463 . 126 THR H H 7.480 0.020 1 464 . 126 THR CA C 62.400 0.300 1 465 . 126 THR CB C 70.400 0.300 1 466 . 126 THR N N 118.000 0.200 1 467 . 127 GLN H H 8.970 0.020 1 468 . 127 GLN CA C 53.000 0.300 1 469 . 127 GLN CB C 31.300 0.300 1 470 . 127 GLN N N 122.600 0.200 1 471 . 128 TYR H H 8.080 0.020 1 472 . 128 TYR CA C 51.900 0.300 1 473 . 128 TYR CB C 37.700 0.300 1 474 . 128 TYR N N 123.400 0.200 1 475 . 129 TRP H H 8.640 0.020 1 476 . 129 TRP CA C 56.100 0.300 1 477 . 129 TRP CB C 32.500 0.300 1 478 . 129 TRP N N 119.100 0.200 1 479 . 130 SER H H 9.130 0.020 1 480 . 130 SER CA C 58.400 0.300 1 481 . 130 SER CB C 66.700 0.300 1 482 . 130 SER N N 121.400 0.200 1 483 . 131 VAL H H 10.280 0.020 1 484 . 131 VAL CA C 61.500 0.300 1 485 . 131 VAL CB C 35.100 0.300 1 486 . 131 VAL N N 125.600 0.200 1 487 . 132 ARG H H 9.070 0.020 1 488 . 132 ARG CA C 58.900 0.300 1 489 . 132 ARG CB C 30.000 0.300 1 490 . 132 ARG N N 137.600 0.200 1 491 . 133 GLN H H 9.060 0.020 1 492 . 133 GLN CA C 60.300 0.300 1 493 . 133 GLN CB C 27.900 0.300 1 494 . 133 GLN N N 123.600 0.200 1 495 . 134 THR H H 7.510 0.020 1 496 . 134 THR CA C 59.200 0.300 1 497 . 134 THR CB C 71.800 0.300 1 498 . 134 THR N N 107.400 0.200 1 499 . 135 LYS H H 8.590 0.020 1 500 . 135 LYS CA C 58.700 0.300 1 501 . 135 LYS CB C 32.500 0.300 1 502 . 135 LYS N N 126.000 0.200 1 503 . 136 ARG H H 8.990 0.020 1 504 . 136 ARG CA C 55.300 0.300 1 505 . 136 ARG CB C 33.000 0.300 1 506 . 136 ARG N N 128.100 0.200 1 507 . 137 PRO CA C 63.800 0.300 1 508 . 137 PRO CB C 32.000 0.300 1 509 . 138 THR H H 8.510 0.020 1 510 . 138 THR CA C 60.700 0.300 1 511 . 138 THR CB C 70.300 0.300 1 512 . 138 THR N N 115.400 0.200 1 513 . 139 GLY H H 9.080 0.020 1 514 . 139 GLY CA C 45.600 0.300 1 515 . 139 GLY N N 114.900 0.200 1 516 . 140 SER H H 7.470 0.020 1 517 . 140 SER CA C 56.300 0.300 1 518 . 140 SER CB C 65.400 0.300 1 519 . 140 SER N N 114.300 0.200 1 520 . 141 ASN H H 8.740 0.020 1 521 . 141 ASN CA C 54.600 0.300 1 522 . 141 ASN CB C 37.000 0.300 1 523 . 141 ASN N N 123.200 0.200 1 524 . 142 ALA H H 9.400 0.020 1 525 . 142 ALA CA C 51.000 0.300 1 526 . 142 ALA CB C 21.000 0.300 1 527 . 142 ALA N N 131.200 0.200 1 528 . 143 THR H H 7.300 0.020 1 529 . 143 THR CA C 61.000 0.300 1 530 . 143 THR CB C 72.400 0.300 1 531 . 143 THR N N 113.000 0.200 1 532 . 144 ILE H H 9.540 0.020 1 533 . 144 ILE CA C 61.300 0.300 1 534 . 144 ILE CB C 40.900 0.300 1 535 . 144 ILE N N 126.400 0.200 1 536 . 145 THR H H 10.580 0.020 1 537 . 145 THR CA C 61.600 0.300 1 538 . 145 THR CB C 66.200 0.300 1 539 . 145 THR N N 132.800 0.200 1 540 . 146 PHE H H 7.600 0.020 1 541 . 146 PHE CA C 60.200 0.300 1 542 . 146 PHE CB C 39.300 0.300 1 543 . 146 PHE N N 129.500 0.200 1 544 . 147 SER H H 8.960 0.020 1 545 . 147 SER CA C 61.400 0.300 1 546 . 147 SER CB C 62.400 0.300 1 547 . 147 SER N N 115.600 0.200 1 548 . 148 ASN H H 7.250 0.020 1 549 . 148 ASN CA C 55.200 0.300 1 550 . 148 ASN CB C 36.000 0.300 1 551 . 148 ASN N N 119.500 0.200 1 552 . 149 HIS H H 6.700 0.020 1 553 . 149 HIS CA C 59.700 0.300 1 554 . 149 HIS CB C 29.700 0.300 1 555 . 149 HIS N N 123.300 0.200 1 556 . 150 VAL H H 7.170 0.020 1 557 . 150 VAL CA C 66.700 0.300 1 558 . 150 VAL CB C 31.400 0.300 1 559 . 150 VAL N N 118.700 0.200 1 560 . 151 ASN H H 7.980 0.020 1 561 . 151 ASN CA C 56.200 0.300 1 562 . 151 ASN CB C 37.700 0.300 1 563 . 151 ASN N N 117.700 0.200 1 564 . 152 ALA H H 7.360 0.020 1 565 . 152 ALA CA C 55.000 0.300 1 566 . 152 ALA CB C 18.400 0.300 1 567 . 152 ALA N N 126.300 0.200 1 568 . 153 TRP H H 9.240 0.020 1 569 . 153 TRP CA C 58.600 0.300 1 570 . 153 TRP CB C 27.200 0.300 1 571 . 153 TRP N N 123.700 0.200 1 572 . 154 LYS H H 8.330 0.020 1 573 . 154 LYS CA C 60.600 0.300 1 574 . 154 LYS CB C 32.000 0.300 1 575 . 154 LYS N N 123.300 0.200 1 576 . 155 SER H H 7.790 0.020 1 577 . 155 SER CA C 61.200 0.300 1 578 . 155 SER CB C 62.700 0.300 1 579 . 155 SER N N 117.600 0.200 1 580 . 156 HIS H H 7.530 0.020 1 581 . 156 HIS CA C 55.600 0.300 1 582 . 156 HIS CB C 28.900 0.300 1 583 . 156 HIS N N 119.700 0.200 1 584 . 157 GLY H H 7.850 0.020 1 585 . 157 GLY CA C 46.200 0.300 1 586 . 157 GLY N N 108.900 0.200 1 587 . 158 MET H H 7.810 0.020 1 588 . 158 MET CA C 54.200 0.300 1 589 . 158 MET CB C 32.700 0.300 1 590 . 158 MET N N 123.000 0.200 1 591 . 159 ASN H H 8.080 0.020 1 592 . 159 ASN CA C 53.200 0.300 1 593 . 159 ASN CB C 39.800 0.300 1 594 . 159 ASN N N 120.900 0.200 1 595 . 160 LEU H H 9.140 0.020 1 596 . 160 LEU CA C 54.500 0.300 1 597 . 160 LEU CB C 43.300 0.300 1 598 . 160 LEU N N 129.900 0.200 1 599 . 161 GLY H H 7.080 0.020 1 600 . 161 GLY CA C 45.500 0.300 1 601 . 161 GLY N N 106.800 0.200 1 602 . 162 SER H H 7.460 0.020 1 603 . 162 SER CA C 58.700 0.300 1 604 . 162 SER CB C 64.600 0.300 1 605 . 162 SER N N 110.600 0.200 1 606 . 163 ASN H H 7.750 0.020 1 607 . 163 ASN CA C 51.800 0.300 1 608 . 163 ASN CB C 40.200 0.300 1 609 . 163 ASN N N 122.500 0.200 1 610 . 164 TRP H H 9.080 0.020 1 611 . 164 TRP CA C 59.900 0.300 1 612 . 164 TRP CB C 29.500 0.300 1 613 . 164 TRP N N 129.400 0.200 1 614 . 165 ALA H H 7.360 0.020 1 615 . 165 ALA CA C 49.900 0.300 1 616 . 165 ALA CB C 18.000 0.300 1 617 . 165 ALA N N 128.200 0.200 1 618 . 166 TYR H H 6.120 0.020 1 619 . 166 TYR CA C 57.900 0.300 1 620 . 166 TYR CB C 38.400 0.300 1 621 . 166 TYR N N 117.000 0.200 1 622 . 167 GLN H H 8.610 0.020 1 623 . 167 GLN CA C 55.300 0.300 1 624 . 167 GLN CB C 34.900 0.300 1 625 . 167 GLN N N 124.100 0.200 1 626 . 168 VAL H H 9.990 0.020 1 627 . 168 VAL CA C 59.200 0.300 1 628 . 168 VAL CB C 36.800 0.300 1 629 . 168 VAL N N 120.900 0.200 1 630 . 169 MET H H 8.520 0.020 1 631 . 169 MET CA C 54.900 0.300 1 632 . 169 MET CB C 32.100 0.300 1 633 . 169 MET N N 124.100 0.200 1 634 . 170 ALA H H 9.830 0.020 1 635 . 170 ALA CA C 52.300 0.300 1 636 . 170 ALA CB C 23.400 0.300 1 637 . 170 ALA N N 135.800 0.200 1 638 . 171 THR H H 9.140 0.020 1 639 . 171 THR CA C 62.600 0.300 1 640 . 171 THR CB C 72.000 0.300 1 641 . 171 THR N N 115.500 0.200 1 642 . 172 GLU H H 8.690 0.020 1 643 . 172 GLU CA C 52.800 0.300 1 644 . 172 GLU CB C 31.800 0.300 1 645 . 172 GLU N N 127.300 0.200 1 646 . 173 GLY H H 6.010 0.020 1 647 . 173 GLY CA C 44.500 0.300 1 648 . 173 GLY N N 110.000 0.200 1 649 . 174 TYR H H 7.030 0.020 1 650 . 174 TYR CA C 56.700 0.300 1 651 . 174 TYR CB C 40.400 0.300 1 652 . 174 TYR N N 118.500 0.200 1 653 . 175 GLN H H 7.620 0.020 1 654 . 175 GLN CA C 56.500 0.300 1 655 . 175 GLN CB C 25.900 0.300 1 656 . 175 GLN N N 124.400 0.200 1 657 . 176 SER H H 7.630 0.020 1 658 . 176 SER CA C 56.400 0.300 1 659 . 176 SER CB C 68.300 0.300 1 660 . 176 SER N N 112.300 0.200 1 661 . 177 SER H H 7.580 0.020 1 662 . 177 SER CA C 56.400 0.300 1 663 . 177 SER CB C 67.100 0.300 1 664 . 177 SER N N 112.300 0.200 1 665 . 178 GLY H H 7.540 0.020 1 666 . 178 GLY CA C 44.800 0.300 1 667 . 178 GLY N N 108.700 0.200 1 668 . 179 SER H H 6.300 0.020 1 669 . 179 SER CA C 57.600 0.300 1 670 . 179 SER CB C 66.800 0.300 1 671 . 179 SER N N 113.300 0.200 1 672 . 180 SER H H 9.500 0.020 1 673 . 180 SER CA C 56.900 0.300 1 674 . 180 SER CB C 67.200 0.300 1 675 . 180 SER N N 117.600 0.200 1 676 . 181 ASN H H 9.160 0.020 1 677 . 181 ASN CA C 55.100 0.300 1 678 . 181 ASN CB C 41.100 0.300 1 679 . 181 ASN N N 126.600 0.200 1 680 . 182 VAL H H 8.600 0.020 1 681 . 182 VAL CA C 61.100 0.300 1 682 . 182 VAL CB C 36.200 0.300 1 683 . 182 VAL N N 126.800 0.200 1 684 . 183 THR H H 8.540 0.020 1 685 . 183 THR CA C 62.200 0.300 1 686 . 183 THR CB C 70.700 0.300 1 687 . 183 THR N N 124.000 0.200 1 688 . 184 VAL H H 8.520 0.020 1 689 . 184 VAL CA C 62.000 0.300 1 690 . 184 VAL CB C 35.600 0.300 1 691 . 184 VAL N N 130.100 0.200 1 692 . 185 TRP H H 9.510 0.020 1 693 . 185 TRP CA C 60.100 0.300 1 694 . 185 TRP CB C 30.200 0.300 1 695 . 185 TRP N N 133.900 0.200 1 stop_ save_