data_4705 ####################### # 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 ; 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_ _BMRB_accession_number 4705 _BMRB_flat_file_name bmr4705.str _Entry_type new _Submission_date 2000-03-30 _Accession_date 2000-03-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 172 '13C chemical shifts' 332 '15N chemical shifts' 172 stop_ loop_ _Related_BMRB_accession_number _Relationship 4704 apo-BCX stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _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 _MEDLINE_UI_code . 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 _Page_first 512 _Page_last 524 _Year 2000 loop_ _Keyword '1H and 15N assigned chemical shifts' 'BCX (Bacillus circulans xylanase)' 'Order parameters' 'Relaxation dynamics' 'Xylanase' 'Glycosyl-enzyme intermediate' stop_ 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 DNP-2FXb $DNP-2FXb stop_ _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_ save_ ######################## # Monomeric polymers # ######################## save_BCX _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "xylanase" _Name_variant . _Abbreviation_common BCX _Molecular_mass 20396 _Mol_thiol_state 'not present' ############################## # 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 4704 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_ ############# # Ligands # ############# save_DNP-2FXb _Saveframe_category ligand _Mol_type non-polymer _Abbreviation_common DNP-2FXb _Name_IUPAC 2-deoxy-2-fluoro-beta-xylobioside _PDB_code . _Mol_paramagnetic no _Mol_aromatic no save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single covalent DNP-2FXb . C1 C BCX 78 GLU OE2 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_2FXb-BCX _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BCX 0.9 mM '[U-99% 13C; U-99% 15N]' $DNP-2FXb 2 mg . stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version 95 loop_ _Task ; data processing peak assignments ; stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Unity _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; HNCACB CBCACONH ; save_ ####################### # Sample conditions # ####################### save_Conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.4 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 _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.00 external_to_the_sample direct cylindrical external_to_the_sample parallel_to_Bo . DSS C 13 'methyl carbons' ppm 0.00 external_to_the_sample direct cylindrical external_to_the_sample parallel_to_Bo . NH4Cl N 15 'nitrogen' ppm 29.43 external_to_the_sample 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 loop_ _Sample_label $2FXb-BCX stop_ _Sample_conditions_label $Conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name BCX loop_ _Atom_shift_assign_ID _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 8.422 0.020 1 2 3 THR CA C 61.602 0.300 1 3 3 THR CB C 69.294 0.300 1 4 3 THR N N 116.767 0.200 1 5 4 ASP H H 8.074 0.020 1 6 4 ASP CA C 53.585 0.300 1 7 4 ASP CB C 42.282 0.300 1 8 4 ASP N N 120.351 0.200 1 9 5 TYR H H 7.817 0.020 1 10 5 TYR CA C 58.155 0.300 1 11 5 TYR CB C 42.116 0.300 1 12 5 TYR N N 122.268 0.200 1 13 6 TRP H H 7.367 0.020 1 14 6 TRP CA C 54.128 0.300 1 15 6 TRP CB C 32.395 0.300 1 16 6 TRP N N 133.457 0.200 1 17 7 GLN H H 8.037 0.020 1 18 7 GLN CA C 52.031 0.300 1 19 7 GLN CB C 28.942 0.300 1 20 7 GLN N N 129.024 0.200 1 21 8 ASN H H 7.977 0.020 1 22 8 ASN CA C 52.691 0.300 1 23 8 ASN CB C 37.137 0.300 1 24 8 ASN N N 126.091 0.200 1 25 9 TRP H H 8.332 0.020 1 26 9 TRP CA C 57.160 0.300 1 27 9 TRP CB C 31.598 0.300 1 28 9 TRP N N 127.496 0.200 1 29 10 THR H H 7.175 0.020 1 30 10 THR CA C 57.509 0.300 1 31 10 THR CB C 70.132 0.300 1 32 10 THR N N 121.061 0.200 1 33 11 ASP H H 7.489 0.020 1 34 11 ASP CA C 53.423 0.300 1 35 11 ASP CB C 40.086 0.300 1 36 11 ASP N N 124.410 0.200 1 37 12 GLY H H 8.467 0.020 1 38 12 GLY CA C 44.755 0.300 1 39 12 GLY N N 110.442 0.200 1 40 13 GLY H H 8.399 0.020 1 41 13 GLY CA C 45.687 0.300 1 42 13 GLY N N 111.076 0.200 1 43 14 GLY H H 8.494 0.020 1 44 14 GLY CA C 46.539 0.300 1 45 14 GLY N N 115.083 0.200 1 46 15 ILE H H 8.067 0.020 1 47 15 ILE CA C 59.998 0.300 1 48 15 ILE CB C 40.635 0.300 1 49 15 ILE N N 122.471 0.200 1 50 16 VAL H H 8.488 0.020 1 51 16 VAL CA C 62.064 0.300 1 52 16 VAL CB C 32.873 0.300 1 53 16 VAL N N 128.980 0.200 1 54 17 ASN H H 8.702 0.020 1 55 17 ASN CA C 51.949 0.300 1 56 17 ASN CB C 38.393 0.300 1 57 17 ASN N N 127.739 0.200 1 58 18 ALA H H 8.698 0.020 1 59 18 ALA CA C 50.784 0.300 1 60 18 ALA CB C 21.987 0.300 1 61 18 ALA N N 131.542 0.200 1 62 19 VAL H H 9.412 0.020 1 63 19 VAL CA C 62.371 0.300 1 64 19 VAL CB C 34.190 0.300 1 65 19 VAL N N 126.497 0.200 1 66 20 ASN H H 8.288 0.020 1 67 20 ASN CA C 51.630 0.300 1 68 20 ASN CB C 35.661 0.300 1 69 20 ASN N N 127.838 0.200 1 70 21 GLY H H 7.211 0.020 1 71 21 GLY CA C 44.055 0.300 1 72 21 GLY N N 114.889 0.200 1 73 22 SER H H 8.336 0.020 1 74 22 SER CA C 58.503 0.300 1 75 22 SER CB C 63.494 0.300 1 76 22 SER N N 114.747 0.200 1 77 23 GLY H H 8.908 0.020 1 78 23 GLY CA C 47.378 0.300 1 79 23 GLY N N 115.334 0.200 1 80 24 GLY H H 9.320 0.020 1 81 24 GLY CA C 45.978 0.300 1 82 24 GLY N N 117.780 0.200 1 83 25 ASN H H 8.217 0.020 1 84 25 ASN CA C 54.243 0.300 1 85 25 ASN CB C 42.823 0.300 1 86 25 ASN N N 120.675 0.200 1 87 26 TYR H H 9.677 0.020 1 88 26 TYR CA C 57.394 0.300 1 89 26 TYR CB C 42.821 0.300 1 90 26 TYR N N 126.157 0.200 1 91 27 SER H H 8.750 0.020 1 92 27 SER CA C 56.490 0.300 1 93 27 SER CB C 66.510 0.300 1 94 27 SER N N 113.214 0.200 1 95 28 VAL H H 9.139 0.020 1 96 28 VAL CA C 60.933 0.300 1 97 28 VAL CB C 34.892 0.300 1 98 28 VAL N N 120.590 0.200 1 99 29 ASN H H 8.463 0.020 1 100 29 ASN CA C 53.020 0.300 1 101 29 ASN CB C 41.716 0.300 1 102 29 ASN N N 127.831 0.200 1 103 30 TRP H H 9.376 0.020 1 104 30 TRP CA C 55.454 0.300 1 105 30 TRP CB C 33.044 0.300 1 106 30 TRP N N 126.993 0.200 1 107 31 SER H H 9.227 0.020 1 108 31 SER CA C 57.308 0.300 1 109 31 SER CB C 64.864 0.300 1 110 31 SER N N 117.951 0.200 1 111 33 THR H H 8.194 0.020 1 112 33 THR CA C 62.891 0.300 1 113 33 THR CB C 71.168 0.300 1 114 33 THR N N 107.757 0.200 1 115 34 GLY H H 7.369 0.020 1 116 34 GLY CA C 46.372 0.300 1 117 34 GLY N N 107.164 0.200 1 118 35 ASN H H 9.919 0.020 1 119 35 ASN CA C 51.464 0.300 1 120 35 ASN CB C 42.920 0.300 1 121 35 ASN N N 129.705 0.200 1 122 37 VAL H H 9.203 0.020 1 123 37 VAL CA C 62.937 0.300 1 124 37 VAL CB C 36.208 0.300 1 125 37 VAL N N 120.689 0.200 1 126 40 LYS H H 6.474 0.020 1 127 40 LYS CA C 54.743 0.300 1 128 40 LYS CB C 38.752 0.300 1 129 40 LYS N N 117.214 0.200 1 130 41 GLY H H 7.854 0.020 1 131 41 GLY CA C 47.493 0.300 1 132 41 GLY N N 110.013 0.200 1 133 42 TRP H H 9.676 0.020 1 134 42 TRP CA C 59.757 0.300 1 135 42 TRP CB C 32.653 0.300 1 136 42 TRP N N 131.961 0.200 1 137 43 THR H H 10.223 0.020 1 138 43 THR CA C 65.994 0.300 1 139 43 THR CB C 69.382 0.300 1 140 43 THR N N 125.188 0.200 1 141 44 THR H H 7.957 0.020 1 142 44 THR CA C 60.741 0.300 1 143 44 THR CB C 70.231 0.300 1 144 44 THR N N 116.007 0.200 1 145 45 GLY H H 8.148 0.020 1 146 45 GLY CA C 45.783 0.300 1 147 45 GLY N N 111.376 0.200 1 148 46 SER H H 6.894 0.020 1 149 46 SER CA C 52.283 0.300 1 150 46 SER CB C 65.506 0.300 1 151 46 SER N N 111.268 0.200 1 152 47 PRO CA C 60.037 0.300 1 153 47 PRO CB C 29.496 0.300 1 154 48 PHE H H 7.185 0.020 1 155 48 PHE CA C 55.469 0.300 1 156 48 PHE CB C 39.368 0.300 1 157 48 PHE N N 114.873 0.200 1 158 49 ARG H H 6.598 0.020 1 159 49 ARG CA C 56.785 0.300 1 160 49 ARG CB C 31.592 0.300 1 161 49 ARG N N 123.401 0.200 1 162 50 THR H H 8.571 0.020 1 163 50 THR CA C 62.262 0.300 1 164 50 THR CB C 69.137 0.300 1 165 50 THR N N 126.254 0.200 1 166 51 ILE H H 8.719 0.020 1 167 51 ILE CA C 62.506 0.300 1 168 51 ILE CB C 40.490 0.300 1 169 51 ILE N N 130.413 0.200 1 170 52 ASN H H 8.736 0.020 1 171 52 ASN CA C 51.032 0.300 1 172 52 ASN CB C 40.129 0.300 1 173 52 ASN N N 127.710 0.200 1 174 53 TYR H H 8.581 0.020 1 175 53 TYR CA C 56.648 0.300 1 176 53 TYR CB C 41.625 0.300 1 177 53 TYR N N 116.924 0.200 1 178 54 ASN H H 8.864 0.020 1 179 54 ASN CA C 53.004 0.300 1 180 54 ASN CB C 40.876 0.300 1 181 54 ASN N N 118.002 0.200 1 182 55 ALA H H 9.642 0.020 1 183 55 ALA CA C 50.142 0.300 1 184 55 ALA CB C 18.486 0.300 1 185 55 ALA N N 134.031 0.200 1 186 56 GLY H H 8.309 0.020 1 187 56 GLY CA C 46.885 0.300 1 188 56 GLY N N 117.914 0.200 1 189 57 VAL H H 8.219 0.020 1 190 57 VAL CA C 62.370 0.300 1 191 57 VAL CB C 35.779 0.300 1 192 57 VAL N N 119.119 0.200 1 193 58 TRP H H 9.033 0.020 1 194 58 TRP CA C 55.906 0.300 1 195 58 TRP CB C 31.320 0.300 1 196 58 TRP N N 129.487 0.200 1 197 59 ALA H H 8.025 0.020 1 198 59 ALA CA C 49.631 0.300 1 199 59 ALA CB C 18.482 0.300 1 200 59 ALA N N 129.689 0.200 1 201 60 PRO CA C 63.589 0.300 1 202 60 PRO CB C 31.147 0.300 1 203 61 ASN H H 9.293 0.020 1 204 61 ASN CA C 51.713 0.300 1 205 61 ASN CB C 37.476 0.300 1 206 61 ASN N N 126.885 0.200 1 207 62 GLY H H 8.104 0.020 1 208 62 GLY CA C 44.285 0.300 1 209 62 GLY N N 110.775 0.200 1 210 63 ASN H H 8.822 0.020 1 211 63 ASN CA C 53.696 0.300 1 212 63 ASN CB C 38.133 0.300 1 213 63 ASN N N 124.917 0.200 1 214 64 GLY H H 8.071 0.020 1 215 64 GLY CA C 46.239 0.300 1 216 64 GLY N N 118.912 0.200 1 217 65 TYR H H 9.914 0.020 1 218 65 TYR CA C 53.748 0.300 1 219 65 TYR CB C 42.660 0.300 1 220 65 TYR N N 120.034 0.200 1 221 66 LEU H H 8.028 0.020 1 222 66 LEU CA C 53.892 0.300 1 223 66 LEU CB C 40.595 0.300 1 224 66 LEU N N 128.195 0.200 1 225 67 THR H H 8.958 0.020 1 226 67 THR CA C 57.953 0.300 1 227 67 THR CB C 72.045 0.300 1 228 67 THR N N 123.130 0.200 1 229 68 LEU H H 9.392 0.020 1 230 68 LEU CA C 56.513 0.300 1 231 68 LEU CB C 42.782 0.300 1 232 68 LEU N N 135.335 0.200 1 233 69 TYR H H 9.389 0.020 1 234 69 TYR CA C 56.759 0.300 1 235 69 TYR CB C 44.069 0.300 1 236 69 TYR N N 134.525 0.200 1 237 70 GLY H H 6.383 0.020 1 238 70 GLY CA C 45.372 0.300 1 239 70 GLY N N 115.523 0.200 1 240 71 TRP H H 6.216 0.020 1 241 71 TRP CA C 54.642 0.300 1 242 71 TRP CB C 35.670 0.300 1 243 71 TRP N N 112.041 0.200 1 244 72 THR H H 8.935 0.020 1 245 72 THR CA C 60.728 0.300 1 246 72 THR CB C 72.517 0.300 1 247 72 THR N N 113.686 0.200 1 248 73 ARG H H 8.872 0.020 1 249 73 ARG CA C 55.531 0.300 1 250 73 ARG CB C 33.752 0.300 1 251 73 ARG N N 118.172 0.200 1 252 74 SER H H 8.635 0.020 1 253 74 SER CA C 57.490 0.300 1 254 74 SER CB C 61.746 0.300 1 255 74 SER N N 112.048 0.200 1 256 75 PRO CA C 62.104 0.300 1 257 75 PRO CB C 33.841 0.300 1 258 76 LEU H H 7.821 0.020 1 259 76 LEU CA C 54.652 0.300 1 260 76 LEU CB C 42.344 0.300 1 261 76 LEU N N 121.395 0.200 1 262 77 ILE H H 8.118 0.020 1 263 77 ILE CA C 58.933 0.300 1 264 77 ILE CB C 41.678 0.300 1 265 77 ILE N N 131.736 0.200 1 266 78 GLU H H 7.352 0.020 1 267 78 GLU CA C 52.348 0.300 1 268 78 GLU CB C 32.280 0.300 1 269 78 GLU N N 130.228 0.200 1 270 79 TYR H H 7.772 0.020 1 271 79 TYR CA C 54.509 0.300 1 272 79 TYR CB C 42.393 0.300 1 273 79 TYR N N 125.102 0.200 1 274 80 TYR H H 8.075 0.020 1 275 80 TYR CA C 57.251 0.300 1 276 80 TYR CB C 45.043 0.300 1 277 80 TYR N N 116.532 0.200 1 278 81 VAL H H 7.669 0.020 1 279 81 VAL CA C 62.799 0.300 1 280 81 VAL CB C 32.337 0.300 1 281 81 VAL N N 119.548 0.200 1 282 82 VAL H H 9.608 0.020 1 283 82 VAL CA C 62.895 0.300 1 284 82 VAL CB C 33.622 0.300 1 285 82 VAL N N 127.862 0.200 1 286 83 ASP H H 8.497 0.020 1 287 83 ASP CA C 54.848 0.300 1 288 83 ASP CB C 43.574 0.300 1 289 83 ASP N N 130.154 0.200 1 290 84 SER H H 8.263 0.020 1 291 84 SER CA C 57.614 0.300 1 292 84 SER CB C 61.652 0.300 1 293 84 SER N N 110.238 0.200 1 294 85 TRP H H 7.745 0.020 1 295 85 TRP CA C 57.269 0.300 1 296 85 TRP CB C 29.487 0.300 1 297 85 TRP N N 121.050 0.200 1 298 86 GLY H H 9.381 0.020 1 299 86 GLY CA C 44.975 0.300 1 300 86 GLY N N 112.257 0.200 1 301 87 THR H H 8.025 0.020 1 302 87 THR CA C 63.290 0.300 1 303 87 THR CB C 68.748 0.300 1 304 87 THR N N 119.180 0.200 1 305 88 TYR H H 8.165 0.020 1 306 88 TYR CA C 56.529 0.300 1 307 88 TYR CB C 40.684 0.300 1 308 88 TYR N N 123.663 0.200 1 309 89 ARG H H 8.141 0.020 1 310 89 ARG CA C 51.742 0.300 1 311 89 ARG CB C 30.494 0.300 1 312 89 ARG N N 134.217 0.200 1 313 90 PRO CA C 62.642 0.300 1 314 90 PRO CB C 30.336 0.300 1 315 91 THR H H 5.931 0.020 1 316 91 THR CA C 58.529 0.300 1 317 91 THR CB C 71.581 0.300 1 318 91 THR N N 107.277 0.200 1 319 92 GLY H H 5.225 0.020 1 320 92 GLY CA C 46.039 0.300 1 321 92 GLY N N 108.390 0.200 1 322 93 THR H H 8.946 0.020 1 323 93 THR CA C 64.026 0.300 1 324 93 THR CB C 68.192 0.300 1 325 93 THR N N 125.769 0.200 1 326 94 TYR H H 9.049 0.020 1 327 94 TYR CA C 59.622 0.300 1 328 94 TYR CB C 39.148 0.300 1 329 94 TYR N N 132.079 0.200 1 330 95 LYS H H 8.465 0.020 1 331 95 LYS CA C 53.504 0.300 1 332 95 LYS CB C 33.665 0.300 1 333 95 LYS N N 126.050 0.200 1 334 96 GLY H H 5.562 0.020 1 335 96 GLY CA C 44.479 0.300 1 336 96 GLY N N 104.300 0.200 1 337 97 THR H H 8.123 0.020 1 338 97 THR CA C 60.009 0.300 1 339 97 THR CB C 74.118 0.300 1 340 97 THR N N 111.152 0.200 1 341 98 VAL H H 9.340 0.020 1 342 98 VAL CA C 59.667 0.300 1 343 98 VAL CB C 34.901 0.300 1 344 98 VAL N N 121.977 0.200 1 345 99 LYS H H 8.474 0.020 1 346 99 LYS CA C 54.848 0.300 1 347 99 LYS CB C 33.259 0.300 1 348 99 LYS N N 130.137 0.200 1 349 100 SER H H 8.741 0.020 1 350 100 SER CA C 59.073 0.300 1 351 100 SER CB C 64.155 0.300 1 352 100 SER N N 118.013 0.200 1 353 101 ASP H H 9.665 0.020 1 354 101 ASP CA C 55.660 0.300 1 355 101 ASP CB C 41.648 0.300 1 356 101 ASP N N 125.842 0.200 1 357 102 GLY H H 8.844 0.020 1 358 102 GLY CA C 45.994 0.300 1 359 102 GLY N N 107.287 0.200 1 360 103 GLY H H 8.228 0.020 1 361 103 GLY CA C 43.228 0.300 1 362 103 GLY N N 110.451 0.200 1 363 104 THR H H 8.049 0.020 1 364 104 THR CA C 62.475 0.300 1 365 104 THR CB C 69.648 0.300 1 366 104 THR N N 117.873 0.200 1 367 105 TYR H H 9.786 0.020 1 368 105 TYR CA C 55.975 0.300 1 369 105 TYR CB C 39.610 0.300 1 370 105 TYR N N 127.722 0.200 1 371 106 ASP H H 8.802 0.020 1 372 106 ASP CA C 54.479 0.300 1 373 106 ASP CB C 45.080 0.300 1 374 106 ASP N N 123.432 0.200 1 375 107 ILE H H 8.388 0.020 1 376 107 ILE CA C 59.511 0.300 1 377 107 ILE CB C 39.569 0.300 1 378 107 ILE N N 123.088 0.200 1 379 108 TYR H H 9.146 0.020 1 380 108 TYR CA C 54.616 0.300 1 381 108 TYR CB C 43.682 0.300 1 382 108 TYR N N 124.314 0.200 1 383 109 THR H H 8.217 0.020 1 384 109 THR CA C 59.900 0.300 1 385 109 THR CB C 71.525 0.300 1 386 109 THR N N 109.790 0.200 1 387 110 THR H H 8.934 0.020 1 388 110 THR CA C 61.540 0.300 1 389 110 THR CB C 73.019 0.300 1 390 110 THR N N 115.743 0.200 1 391 111 THR H H 8.462 0.020 1 392 111 THR CA C 61.921 0.300 1 393 111 THR CB C 71.262 0.300 1 394 111 THR N N 117.119 0.200 1 395 112 ARG H H 8.122 0.020 1 396 112 ARG CA C 53.008 0.300 1 397 112 ARG CB C 31.606 0.300 1 398 112 ARG N N 126.189 0.200 1 399 113 TYR H H 8.162 0.020 1 400 113 TYR CA C 56.323 0.300 1 401 113 TYR CB C 40.871 0.300 1 402 113 TYR N N 120.435 0.200 1 403 114 ASN H H 7.886 0.020 1 404 114 ASN CA C 54.042 0.300 1 405 114 ASN CB C 37.249 0.300 1 406 114 ASN N N 121.769 0.200 1 407 115 ALA H H 9.544 0.020 1 408 115 ALA CA C 50.128 0.300 1 409 115 ALA CB C 22.269 0.300 1 410 115 ALA N N 124.069 0.200 1 411 116 PRO CA C 62.865 0.300 1 412 116 PRO CB C 32.206 0.300 1 413 117 SER H H 8.877 0.020 1 414 117 SER CA C 56.738 0.300 1 415 117 SER CB C 67.910 0.300 1 416 117 SER N N 115.447 0.200 1 417 119 ASP H H 7.455 0.020 1 418 119 ASP CA C 53.774 0.300 1 419 119 ASP CB C 42.149 0.300 1 420 119 ASP N N 121.486 0.200 1 421 120 GLY H H 7.018 0.020 1 422 120 GLY CA C 45.001 0.300 1 423 120 GLY N N 109.895 0.200 1 424 121 ASP H H 8.267 0.020 1 425 121 ASP CA C 55.992 0.300 1 426 121 ASP CB C 41.628 0.300 1 427 121 ASP N N 119.432 0.200 1 428 122 ARG H H 8.231 0.020 1 429 122 ARG CA C 54.968 0.300 1 430 122 ARG CB C 30.635 0.300 1 431 122 ARG N N 121.589 0.200 1 432 123 THR H H 9.165 0.020 1 433 123 THR CA C 60.358 0.300 1 434 123 THR CB C 73.266 0.300 1 435 123 THR N N 117.144 0.200 1 436 124 THR H H 8.338 0.020 1 437 124 THR CA C 61.075 0.300 1 438 124 THR CB C 71.410 0.300 1 439 124 THR N N 119.283 0.200 1 440 125 PHE H H 7.870 0.020 1 441 125 PHE CA C 55.781 0.300 1 442 125 PHE CB C 39.233 0.300 1 443 125 PHE N N 123.099 0.200 1 444 126 THR H H 7.384 0.020 1 445 126 THR CA C 62.249 0.300 1 446 126 THR CB C 69.877 0.300 1 447 126 THR N N 117.731 0.200 1 448 127 GLN H H 9.005 0.020 1 449 127 GLN CA C 53.115 0.300 1 450 127 GLN CB C 30.848 0.300 1 451 127 GLN N N 124.160 0.200 1 452 128 TYR H H 7.789 0.020 1 453 128 TYR CA C 51.916 0.300 1 454 128 TYR CB C 38.337 0.300 1 455 128 TYR N N 123.342 0.200 1 456 129 TRP H H 8.458 0.020 1 457 129 TRP CA C 55.998 0.300 1 458 129 TRP CB C 32.660 0.300 1 459 129 TRP N N 118.590 0.200 1 460 130 SER H H 8.911 0.020 1 461 130 SER CA C 58.366 0.300 1 462 130 SER CB C 66.216 0.300 1 463 130 SER N N 121.711 0.200 1 464 131 VAL H H 10.313 0.020 1 465 131 VAL CA C 61.277 0.300 1 466 131 VAL CB C 35.360 0.300 1 467 131 VAL N N 125.679 0.200 1 468 132 ARG H H 9.053 0.020 1 469 132 ARG CA C 58.762 0.300 1 470 132 ARG CB C 30.164 0.300 1 471 132 ARG N N 107.004 0.200 1 472 133 GLN H H 9.050 0.020 1 473 133 GLN CA C 60.125 0.300 1 474 133 GLN CB C 28.391 0.300 1 475 133 GLN N N 123.647 0.200 1 476 134 THR H H 7.506 0.020 1 477 134 THR CA C 58.988 0.300 1 478 134 THR CB C 71.509 0.300 1 479 134 THR N N 108.029 0.200 1 480 135 LYS H H 8.591 0.020 1 481 135 LYS CA C 58.410 0.300 1 482 135 LYS CB C 32.330 0.300 1 483 135 LYS N N 126.123 0.200 1 484 136 ARG H H 9.051 0.020 1 485 136 ARG CA C 55.072 0.300 1 486 136 ARG CB C 32.595 0.300 1 487 136 ARG N N 128.448 0.200 1 488 137 PRO CA C 63.124 0.300 1 489 137 PRO CB C 33.390 0.300 1 490 138 THR H H 8.501 0.020 1 491 138 THR CA C 60.357 0.300 1 492 138 THR CB C 69.997 0.300 1 493 138 THR N N 115.575 0.200 1 494 139 GLY H H 9.073 0.020 1 495 139 GLY CA C 45.718 0.300 1 496 139 GLY N N 115.135 0.200 1 497 140 SER H H 7.451 0.020 1 498 140 SER CA C 56.119 0.300 1 499 140 SER CB C 65.049 0.300 1 500 140 SER N N 114.563 0.200 1 501 141 ASN H H 8.733 0.020 1 502 141 ASN CA C 54.485 0.300 1 503 141 ASN CB C 37.027 0.300 1 504 141 ASN N N 123.571 0.200 1 505 142 ALA H H 9.365 0.020 1 506 142 ALA CA C 51.137 0.300 1 507 142 ALA CB C 21.397 0.300 1 508 142 ALA N N 131.219 0.200 1 509 143 THR H H 7.253 0.020 1 510 143 THR CA C 60.957 0.300 1 511 143 THR CB C 72.167 0.300 1 512 143 THR N N 113.656 0.200 1 513 144 ILE H H 9.510 0.020 1 514 144 ILE CA C 61.545 0.300 1 515 144 ILE CB C 41.023 0.300 1 516 144 ILE N N 126.611 0.200 1 517 145 THR H H 10.560 0.020 1 518 145 THR CA C 61.602 0.300 1 519 145 THR CB C 66.010 0.300 1 520 145 THR N N 132.734 0.200 1 521 146 PHE H H 7.550 0.020 1 522 146 PHE CA C 59.674 0.300 1 523 146 PHE CB C 39.260 0.300 1 524 146 PHE N N 129.040 0.200 1 525 147 SER H H 9.010 0.020 1 526 147 SER CA C 60.931 0.300 1 527 147 SER CB C 62.255 0.300 1 528 147 SER N N 116.030 0.200 1 529 148 ASN H H 7.140 0.020 1 530 148 ASN CA C 55.019 0.300 1 531 148 ASN CB C 36.413 0.300 1 532 148 ASN N N 119.458 0.200 1 533 149 HIS H H 6.734 0.020 1 534 149 HIS CA C 59.376 0.300 1 535 149 HIS CB C 29.877 0.300 1 536 149 HIS N N 123.438 0.200 1 537 150 VAL H H 7.199 0.020 1 538 150 VAL CA C 66.414 0.300 1 539 150 VAL CB C 31.506 0.300 1 540 150 VAL N N 119.004 0.200 1 541 151 ASN H H 7.935 0.020 1 542 151 ASN CA C 55.809 0.300 1 543 151 ASN CB C 37.786 0.300 1 544 151 ASN N N 117.817 0.200 1 545 152 ALA H H 7.317 0.020 1 546 152 ALA CA C 54.814 0.300 1 547 152 ALA CB C 18.472 0.300 1 548 152 ALA N N 126.356 0.200 1 549 153 TRP H H 9.308 0.020 1 550 153 TRP CA C 58.524 0.300 1 551 153 TRP CB C 27.587 0.300 1 552 153 TRP N N 123.763 0.200 1 553 154 LYS H H 8.326 0.020 1 554 154 LYS CA C 60.383 0.300 1 555 154 LYS CB C 32.328 0.300 1 556 154 LYS N N 123.411 0.200 1 557 155 SER H H 7.751 0.020 1 558 155 SER CA C 61.071 0.300 1 559 155 SER CB C 62.475 0.300 1 560 155 SER N N 117.663 0.200 1 561 156 HIS H H 7.502 0.020 1 562 156 HIS CA C 54.994 0.300 1 563 156 HIS CB C 28.618 0.300 1 564 156 HIS N N 119.604 0.200 1 565 157 GLY H H 7.796 0.020 1 566 157 GLY CA C 46.135 0.300 1 567 157 GLY N N 108.904 0.200 1 568 158 MET H H 7.805 0.020 1 569 158 MET CA C 53.825 0.300 1 570 158 MET CB C 33.184 0.300 1 571 158 MET N N 123.394 0.200 1 572 159 ASN H H 8.046 0.020 1 573 159 ASN CA C 53.084 0.300 1 574 159 ASN CB C 39.542 0.300 1 575 159 ASN N N 121.366 0.200 1 576 160 LEU H H 9.095 0.020 1 577 160 LEU CA C 54.271 0.300 1 578 160 LEU CB C 43.005 0.300 1 579 160 LEU N N 130.086 0.200 1 580 161 GLY H H 7.026 0.020 1 581 161 GLY CA C 45.258 0.300 1 582 161 GLY N N 107.210 0.200 1 583 162 SER H H 7.449 0.020 1 584 162 SER CA C 58.598 0.300 1 585 162 SER CB C 64.151 0.300 1 586 162 SER N N 110.726 0.200 1 587 163 ASN H H 7.647 0.020 1 588 163 ASN CA C 51.517 0.300 1 589 163 ASN CB C 39.936 0.300 1 590 163 ASN N N 122.442 0.200 1 591 164 TRP H H 9.087 0.020 1 592 164 TRP CA C 59.985 0.300 1 593 164 TRP CB C 29.638 0.300 1 594 164 TRP N N 129.529 0.200 1 595 165 ALA H H 7.298 0.020 1 596 165 ALA CA C 49.764 0.300 1 597 165 ALA CB C 18.258 0.300 1 598 165 ALA N N 128.479 0.200 1 599 166 TYR H H 6.121 0.020 1 600 166 TYR CA C 57.742 0.300 1 601 166 TYR CB C 38.375 0.300 1 602 166 TYR N N 117.120 0.200 1 603 167 GLN H H 8.752 0.020 1 604 167 GLN CA C 55.183 0.300 1 605 167 GLN CB C 35.284 0.300 1 606 167 GLN N N 124.618 0.200 1 607 168 VAL H H 10.195 0.020 1 608 168 VAL CA C 58.286 0.300 1 609 168 VAL CB C 36.684 0.300 1 610 168 VAL N N 119.654 0.200 1 611 169 MET H H 8.429 0.020 1 612 169 MET CA C 54.667 0.300 1 613 169 MET CB C 32.374 0.300 1 614 169 MET N N 122.575 0.200 1 615 170 ALA H H 9.836 0.020 1 616 170 ALA CA C 51.955 0.300 1 617 170 ALA CB C 23.767 0.300 1 618 170 ALA N N 135.814 0.200 1 619 171 THR H H 9.032 0.020 1 620 171 THR CA C 62.320 0.300 1 621 171 THR CB C 72.157 0.300 1 622 171 THR N N 115.067 0.200 1 623 172 GLU H H 8.746 0.020 1 624 172 GLU CA C 52.410 0.300 1 625 172 GLU CB C 31.818 0.300 1 626 172 GLU N N 129.087 0.200 1 627 173 GLY H H 5.983 0.020 1 628 173 GLY CA C 43.526 0.300 1 629 173 GLY N N 111.177 0.200 1 630 174 TYR H H 6.948 0.020 1 631 174 TYR CA C 56.736 0.300 1 632 174 TYR CB C 40.465 0.300 1 633 174 TYR N N 119.118 0.200 1 634 175 GLN H H 7.378 0.020 1 635 175 GLN CA C 55.651 0.300 1 636 175 GLN CB C 25.501 0.300 1 637 175 GLN N N 125.084 0.200 1 638 176 SER H H 7.491 0.020 1 639 176 SER CA C 55.704 0.300 1 640 176 SER CB C 67.971 0.300 1 641 176 SER N N 111.677 0.200 1 642 177 SER H H 7.558 0.020 1 643 177 SER CA C 56.258 0.300 1 644 177 SER CB C 66.806 0.300 1 645 177 SER N N 112.327 0.200 1 646 178 GLY H H 7.470 0.020 1 647 178 GLY CA C 44.714 0.300 1 648 178 GLY N N 108.642 0.200 1 649 179 SER H H 6.364 0.020 1 650 179 SER CA C 57.296 0.300 1 651 179 SER CB C 66.627 0.300 1 652 179 SER N N 113.606 0.200 1 653 180 SER H H 9.467 0.020 1 654 180 SER CA C 56.544 0.300 1 655 180 SER CB C 67.173 0.300 1 656 180 SER N N 117.681 0.200 1 657 181 ASN H H 9.163 0.020 1 658 181 ASN CA C 54.769 0.300 1 659 181 ASN CB C 41.136 0.300 1 660 181 ASN N N 126.515 0.200 1 661 182 VAL H H 8.530 0.020 1 662 182 VAL CA C 61.082 0.300 1 663 182 VAL CB C 36.591 0.300 1 664 182 VAL N N 126.916 0.200 1 665 183 THR H H 8.529 0.020 1 666 183 THR CA C 62.628 0.300 1 667 183 THR CB C 70.361 0.300 1 668 183 THR N N 124.274 0.200 1 669 184 VAL H H 8.487 0.020 1 670 184 VAL CA C 61.507 0.300 1 671 184 VAL CB C 35.560 0.300 1 672 184 VAL N N 129.935 0.200 1 673 185 TRP H H 9.456 0.020 1 674 185 TRP CA C 59.949 0.300 1 675 185 TRP CB C 30.333 0.300 1 676 185 TRP N N 133.935 0.200 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 8762143 save_