data_4704 #Corrected using PDB structure: 1BCX_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 36 F CA 66.86 55.98 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 84 S CB 57.75 66.54 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A -0.24 0.15 N/A -1.40 0.10 # #bmr4704.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4704.str file): #HA CA CB CO N HN #N/A -0.05 -0.05 N/A -1.40 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.12 +/-0.13 N/A +/-0.30 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.962 0.996 N/A 0.912 0.790 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.776 0.799 N/A 1.959 0.380 # ####################### # 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 4704 _BMRB_flat_file_name bmr4704.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' 177 '13C chemical shifts' 341 '15N chemical shifts' 177 stop_ loop_ _Related_BMRB_accession_number _Relationship 4705 2FXb-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 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_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1AXK "B Chain B, Engineered Bacillus Bifunctional Enzyme Gluxyn-1" . PDB 1BCX "Xylanase (Inactive Form, Endo-Beta-1,4-Xylanase) (E.C.3.2.1.8) Mutant With Glu 172 Replaced By Cys (E172c) Complexed With Xylobiose" . PDB 1C5I "A Chain A, Hydrogen Bonding And Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change The Ph Optimum Of A Glycosidase" . PDB 1C5H "A Chain A, Hydrogen Bonding And Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change The Ph Optimum Of A Glycosidase" . PDB 1XNB "Xylanase (Endo-1,4-Beta-Xylanase) (E.C.3.2.1.8)" . PDB 1BVV "Sugar Ring Distortion In The Glycosyl-Enzyme Intermediate Of A Family G11 XYLANASE" . PDB 2BVV "A Chain A, Sugar Ring Distortion In The Glycosyl-Enzyme Intermediate Of A Family G11 XYLANASE" . 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-03-11 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 1BCX "Xylanase (Inactive Form,Endo-Beta-1,4-Xylanase) (E.C.3.2.1.8) Mutant With Glu172 Replaced By Cys (E172c) Complexed With Xylobiose" 100.00 185 98 99 1e-110 PDB 1BVV "Sugar Ring Distortion In The Glycosyl-EnzymeIntermediate Of A Family G11 XYLANASE" 100.00 185 99 100 1e-111 PDB 1C5H "A Chain A, Hydrogen Bonding And Catalysis: AnUnexpected Explanation For How A Single Amino AcidSubstitution Can Change The Ph Optimum Of A Glycosidase" 100.00 185 98 100 1e-111 PDB 1C5I "A Chain A, Hydrogen Bonding And Catalysis: AnUnexpected Explanation For How A Single Amino AcidSubstitution Can Change The Ph Optimum Of A Glycosidase" 100.00 185 98 100 1e-111 PDB 1HV0 "A Chain A, Dissecting ElectrostaticInteractions And The Ph-Dependent Activity Of A Family11 Glycosidase" 100.00 185 98 100 1e-111 PDB 1HV1 "A Chain A, Dissecting ElectrostaticInteractions And The Ph-Dependent Activity Of A Family11 Glycosidase" 100.00 185 98 99 1e-111 PDB 1XNB "Xylanase (Endo-1,4-Beta-Xylanase)(E.C.3.2.1.8)" 100.00 185 99 100 1e-111 PDB 2BVV "A Chain A, Sugar Ring Distortion In TheGlycosyl-Enzyme Intermediate Of A Family G11 XYLANASE" 100.00 185 98 100 1e-111 PDB 1XNC "Xylanase (Endo-1,4-Beta-Xylanase)(E.C.3.2.1.8) Mutant With Ser 100 Replaced By Cys AndAsn 148 Replaced By Cys (S100c,N148c)" 100.00 185 98 99 1e-110 PDB 1AXK "A Chain A, Engineered Bacillus BifunctionalEnzyme Gluxyn-1" 46.95 394 99 100 10e-113 EMBL CAA41783.1 "endo-1, 4-beta-xylanase [Bacillus sp.YA-14]" 86.85 213 99 100 10e-113 EMBL CAA84276.1 "xylanase [Bacillus subtilis]" 86.85 213 99 100 10e-113 EMBL CAB13776.1 "endo-1,4-beta-xylanase [Bacillussubtilis subsp. subtilis str. 168]" 86.85 213 99 100 10e-113 EMBL CAA30553.1 "unnamed protein product [Bacilluscirculans]" 86.85 213 99 100 1e-111 GenBank AAA22897.1 "xylanase (EC 3.2.1.8)" 86.85 213 99 100 10e-113 GenBank AAB84458.1 "xylanase [Bacillus subtilis]" 86.85 213 99 100 10e-113 GenBank AAM08359.1 "endo-1,4-xylanase [Bacillus subtilis]" 86.85 213 99 99 1e-110 GenBank AAM08360.1 "endo-1,4-xylanase [Bacillus circulans]" 86.85 213 99 99 1e-111 PIR I40569 "endo-1,4-beta-xylanase (EC 3.2.1.8) Aprecursor - Bacillus subtilis" 86.85 213 99 100 10e-113 PIR S48126 "endo-1,4-beta-xylanase (EC 3.2.1.8) Sprecursor - Bacillus sp. (strain YA-14)" 86.85 213 99 100 10e-113 PIR S01734 "endo-1,4-beta-xylanase (EC 3.2.1.8) Aprecursor [validated] - Bacillus circulans" 86.85 213 99 100 1e-111 PRF 1209158A xylanase 86.85 213 99 100 10e-113 REF NP_389765.1 "endo-1,4-beta-xylanase [Bacillussubtilis]" 86.85 213 99 100 10e-113 SWISS-PROT P18429 "XYNA_BACSU Endo-1,4-beta-xylanase A precursor(Xylanase A) (1,4-beta-D-xylan xylanohydrolase A)" 86.85 213 99 100 10e-113 SWISS-PROT P09850 "XYNA_BACCI Endo-1,4-beta-xylanase precursor(Xylanase) (1,4-beta-D-xylan xylanohydrolase)" 86.85 213 99 100 1e-111 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 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_ 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 5.7 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 _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 # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_assignment_one _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $apo-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 8.37 0.020 1 2 3 THR CA C 61.65 0.300 1 3 3 THR CB C 69.65 0.300 1 4 3 THR N N 114.90 0.200 1 5 4 ASP H H 8.02 0.020 1 6 4 ASP CA C 53.55 0.300 1 7 4 ASP CB C 42.25 0.300 1 8 4 ASP N N 119.00 0.200 1 9 5 TYR H H 7.84 0.020 1 10 5 TYR CA C 58.35 0.300 1 11 5 TYR CB C 42.25 0.300 1 12 5 TYR N N 120.80 0.200 1 13 6 TRP H H 7.40 0.020 1 14 6 TRP CA C 54.55 0.300 1 15 6 TRP CB C 32.85 0.300 1 16 6 TRP N N 132.20 0.200 1 17 7 GLN H H 8.13 0.020 1 18 7 GLN CA C 52.55 0.300 1 19 7 GLN CB C 29.95 0.300 1 20 7 GLN N N 127.50 0.200 1 21 8 ASN H H 7.98 0.020 1 22 8 ASN CA C 52.55 0.300 1 23 8 ASN CB C 37.25 0.300 1 24 8 ASN N N 124.00 0.200 1 25 9 TRP H H 8.60 0.020 1 26 9 TRP CA C 57.45 0.300 1 27 9 TRP CB C 31.45 0.300 1 28 9 TRP N N 126.10 0.200 1 29 10 THR H H 7.10 0.020 1 30 10 THR CA C 57.75 0.300 1 32 10 THR N N 119.50 0.200 1 33 11 ASP H H 7.50 0.020 1 34 11 ASP CA C 53.65 0.300 1 36 11 ASP N N 122.70 0.200 1 37 12 GLY H H 8.44 0.020 1 38 12 GLY CA C 44.75 0.300 1 39 12 GLY N N 109.20 0.200 1 40 13 GLY H H 8.47 0.020 1 41 13 GLY CA C 45.05 0.300 1 42 13 GLY N N 109.60 0.200 1 43 14 GLY H H 8.48 0.020 1 44 14 GLY CA C 46.35 0.300 1 45 14 GLY N N 112.40 0.200 1 46 15 ILE H H 8.18 0.020 1 47 15 ILE CA C 60.15 0.300 1 48 15 ILE CB C 40.85 0.300 1 49 15 ILE N N 121.30 0.200 1 50 16 VAL H H 8.46 0.020 1 51 16 VAL CA C 62.45 0.300 1 52 16 VAL CB C 33.05 0.300 1 53 16 VAL N N 127.40 0.200 1 54 17 ASN H H 8.75 0.020 1 55 17 ASN CA C 52.05 0.300 1 56 17 ASN CB C 38.65 0.300 1 57 17 ASN N N 126.40 0.200 1 58 18 ALA H H 8.79 0.020 1 59 18 ALA CA C 50.05 0.300 1 60 18 ALA CB C 22.05 0.300 1 61 18 ALA N N 130.00 0.200 1 62 19 VAL H H 9.40 0.020 1 63 19 VAL CA C 62.35 0.300 1 65 19 VAL N N 124.70 0.200 1 66 20 ASN H H 8.35 0.020 1 67 20 ASN CA C 51.75 0.300 1 68 20 ASN CB C 35.55 0.300 1 69 20 ASN N N 126.20 0.200 1 70 21 GLY H H 7.23 0.020 1 71 21 GLY CA C 44.15 0.300 1 72 21 GLY N N 113.30 0.200 1 73 22 SER H H 8.30 0.020 1 74 22 SER CA C 58.75 0.300 1 76 22 SER N N 112.90 0.200 1 77 23 GLY H H 8.90 0.020 1 78 23 GLY CA C 47.45 0.300 1 79 23 GLY N N 113.70 0.200 1 80 24 GLY H H 9.30 0.020 1 81 24 GLY CA C 46.05 0.300 1 82 24 GLY N N 116.00 0.200 1 83 25 ASN H H 8.18 0.020 1 84 25 ASN CA C 54.35 0.300 1 85 25 ASN CB C 42.85 0.300 1 86 25 ASN N N 119.10 0.200 1 87 26 TYR H H 9.74 0.020 1 88 26 TYR CA C 57.75 0.300 1 89 26 TYR CB C 42.85 0.300 1 90 26 TYR N N 125.50 0.200 1 91 27 SER H H 8.75 0.020 1 92 27 SER CA C 56.65 0.300 1 93 27 SER CB C 66.55 0.300 1 94 27 SER N N 111.60 0.200 1 95 28 VAL H H 9.18 0.020 1 96 28 VAL CA C 61.15 0.300 1 97 28 VAL CB C 34.85 0.300 1 98 28 VAL N N 119.20 0.200 1 99 29 ASN H H 8.48 0.020 1 100 29 ASN CA C 53.25 0.300 1 101 29 ASN CB C 41.75 0.300 1 102 29 ASN N N 126.30 0.200 1 103 30 TRP H H 9.16 0.020 1 104 30 TRP CA C 55.85 0.300 1 105 30 TRP CB C 32.95 0.300 1 106 30 TRP N N 125.50 0.200 1 107 31 SER H H 9.23 0.020 1 108 31 SER CA C 57.45 0.300 1 109 31 SER CB C 65.05 0.300 1 110 31 SER N N 116.30 0.200 1 111 32 ASN H H 8.32 0.020 1 112 32 ASN CA C 54.35 0.300 1 114 32 ASN N N 126.10 0.200 1 115 33 THR H H 8.33 0.020 1 116 33 THR CA C 63.15 0.300 1 117 33 THR CB C 71.45 0.300 1 118 33 THR N N 106.10 0.200 1 119 34 GLY H H 7.61 0.020 1 120 34 GLY CA C 46.45 0.300 1 121 34 GLY N N 106.00 0.200 1 122 35 ASN H H 9.68 0.020 1 123 35 ASN CA C 52.55 0.300 1 124 35 ASN CB C 41.95 0.300 1 125 35 ASN N N 127.80 0.200 1 126 36 PHE H H 7.76 0.020 1 127 36 PHE CA C 67.05 0.300 1 128 36 PHE CB C 41.75 0.300 1 129 36 PHE N N 119.60 0.200 1 130 37 VAL H H 9.16 0.020 1 131 37 VAL CA C 62.85 0.300 1 133 37 VAL N N 119.90 0.200 1 134 38 VAL H H 8.60 0.020 1 135 38 VAL CA C 58.65 0.300 1 136 38 VAL CB C 36.65 0.300 1 137 38 VAL N N 127.10 0.200 1 138 39 GLY H H 8.40 0.020 1 139 39 GLY CA C 45.75 0.300 1 140 39 GLY N N 108.70 0.200 1 141 40 LYS H H 6.44 0.020 1 142 40 LYS CA C 54.75 0.300 1 143 40 LYS CB C 38.65 0.300 1 144 40 LYS N N 115.60 0.200 1 145 41 GLY H H 7.93 0.020 1 146 41 GLY CA C 47.45 0.300 1 147 41 GLY N N 108.20 0.200 1 148 42 TRP H H 9.61 0.020 1 149 42 TRP CA C 59.85 0.300 1 150 42 TRP CB C 32.55 0.300 1 151 42 TRP N N 130.10 0.200 1 152 43 THR H H 10.24 0.020 1 153 43 THR CA C 66.15 0.300 1 155 43 THR N N 123.60 0.200 1 156 44 THR H H 8.50 0.020 1 157 44 THR CA C 60.55 0.300 1 158 44 THR CB C 70.25 0.300 1 159 44 THR N N 114.30 0.200 1 160 45 GLY H H 8.18 0.020 1 161 45 GLY CA C 45.95 0.300 1 163 46 SER H H 6.82 0.020 1 164 46 SER CA C 52.25 0.300 1 165 46 SER CB C 65.65 0.300 1 166 46 SER N N 109.60 0.200 1 167 47 PRO CA C 62.95 0.300 1 168 47 PRO CB C 31.35 0.300 1 169 48 PHE H H 7.19 0.020 1 170 48 PHE CA C 55.65 0.300 1 171 48 PHE CB C 39.35 0.300 1 172 48 PHE N N 113.40 0.200 1 173 49 ARG H H 6.58 0.020 1 174 49 ARG CA C 57.05 0.300 1 175 49 ARG CB C 31.55 0.300 1 176 49 ARG N N 121.80 0.200 1 177 50 THR H H 8.57 0.020 1 178 50 THR CA C 62.55 0.300 1 179 50 THR CB C 69.25 0.300 1 180 50 THR N N 124.60 0.200 1 181 51 ILE H H 8.70 0.020 1 182 51 ILE CA C 62.35 0.300 1 183 51 ILE CB C 40.05 0.300 1 184 51 ILE N N 128.90 0.200 1 185 52 ASN H H 8.77 0.020 1 186 52 ASN CA C 51.05 0.300 1 187 52 ASN CB C 39.95 0.300 1 188 52 ASN N N 126.30 0.200 1 189 53 TYR H H 8.61 0.020 1 190 53 TYR CA C 56.85 0.300 1 191 53 TYR CB C 41.05 0.300 1 192 53 TYR N N 115.50 0.200 1 193 54 ASN H H 8.91 0.020 1 194 54 ASN CA C 53.05 0.300 1 196 54 ASN N N 116.70 0.200 1 197 55 ALA H H 9.67 0.020 1 198 55 ALA CA C 50.25 0.300 1 199 55 ALA CB C 18.15 0.300 1 200 55 ALA N N 132.60 0.200 1 201 56 GLY H H 8.32 0.020 1 202 56 GLY CA C 47.05 0.300 1 203 56 GLY N N 116.10 0.200 1 204 57 VAL H H 8.20 0.020 1 205 57 VAL CA C 62.45 0.300 1 206 57 VAL CB C 35.75 0.300 1 207 57 VAL N N 117.50 0.200 1 208 58 TRP H H 8.99 0.020 1 209 58 TRP CA C 56.25 0.300 1 210 58 TRP CB C 30.95 0.300 1 212 59 ALA H H 8.05 0.020 1 213 59 ALA CA C 49.65 0.300 1 214 59 ALA CB C 18.35 0.300 1 215 59 ALA N N 128.20 0.200 1 216 60 PRO CA C 63.55 0.300 1 218 61 ASN H H 9.31 0.020 1 219 61 ASN CA C 51.95 0.300 1 220 61 ASN CB C 37.45 0.300 1 221 61 ASN N N 125.10 0.200 1 222 62 GLY H H 8.13 0.020 1 223 62 GLY CA C 44.35 0.300 1 224 62 GLY N N 108.90 0.200 1 225 63 ASN H H 8.91 0.020 1 226 63 ASN CA C 53.75 0.300 1 227 63 ASN CB C 37.95 0.300 1 228 63 ASN N N 123.20 0.200 1 229 64 GLY H H 8.04 0.020 1 230 64 GLY CA C 46.35 0.300 1 231 64 GLY N N 117.50 0.200 1 232 65 TYR H H 9.68 0.020 1 233 65 TYR CA C 54.05 0.300 1 234 65 TYR CB C 42.55 0.300 1 235 65 TYR N N 118.10 0.200 1 236 66 LEU H H 7.95 0.020 1 237 66 LEU CA C 54.15 0.300 1 238 66 LEU CB C 40.65 0.300 1 239 66 LEU N N 126.40 0.200 1 240 67 THR H H 8.95 0.020 1 241 67 THR CA C 58.05 0.300 1 242 67 THR CB C 72.55 0.300 1 243 67 THR N N 121.60 0.200 1 244 68 LEU H H 9.31 0.020 1 245 68 LEU CA C 56.05 0.300 1 247 68 LEU N N 133.60 0.200 1 248 69 TYR H H 9.62 0.020 1 249 69 TYR CA C 56.45 0.300 1 250 69 TYR CB C 43.35 0.300 1 251 69 TYR N N 132.90 0.200 1 252 70 GLY H H 6.40 0.020 1 253 70 GLY CA C 45.55 0.300 1 254 70 GLY N N 112.00 0.200 1 255 71 TRP H H 6.11 0.020 1 256 71 TRP CA C 55.05 0.300 1 257 71 TRP CB C 35.35 0.300 1 258 71 TRP N N 110.50 0.200 1 259 72 THR H H 9.13 0.020 1 260 72 THR CA C 60.65 0.300 1 261 72 THR CB C 72.85 0.300 1 262 72 THR N N 112.40 0.200 1 263 73 ARG H H 8.87 0.020 1 264 73 ARG CA C 55.35 0.300 1 265 73 ARG CB C 33.35 0.300 1 267 74 SER H H 8.57 0.020 1 268 74 SER CA C 57.75 0.300 1 269 74 SER CB C 61.95 0.300 1 270 74 SER N N 110.20 0.200 1 271 75 PRO CA C 63.15 0.300 1 272 75 PRO CB C 34.75 0.300 1 273 76 LEU H H 7.76 0.020 1 274 76 LEU CA C 54.85 0.300 1 275 76 LEU CB C 42.55 0.300 1 276 76 LEU N N 119.00 0.200 1 277 77 ILE H H 8.10 0.020 1 278 77 ILE CA C 59.05 0.300 1 279 77 ILE CB C 41.15 0.300 1 280 77 ILE N N 129.70 0.200 1 281 78 GLU H H 7.42 0.020 1 282 78 GLU CA C 52.85 0.300 1 283 78 GLU CB C 32.05 0.300 1 284 78 GLU N N 128.80 0.200 1 285 79 TYR H H 7.71 0.020 1 286 79 TYR CA C 54.55 0.300 1 287 79 TYR CB C 42.45 0.300 1 288 79 TYR N N 122.60 0.200 1 289 80 TYR H H 8.15 0.020 1 290 80 TYR CA C 56.95 0.300 1 291 80 TYR CB C 44.55 0.300 1 292 80 TYR N N 114.50 0.200 1 293 81 VAL H H 8.08 0.020 1 294 81 VAL CA C 62.65 0.300 1 295 81 VAL CB C 32.15 0.300 1 296 81 VAL N N 120.00 0.200 1 297 82 VAL H H 9.63 0.020 1 298 82 VAL CA C 62.85 0.300 1 299 82 VAL CB C 33.85 0.300 1 300 82 VAL N N 126.80 0.200 1 301 83 ASP H H 8.40 0.020 1 302 83 ASP CA C 54.85 0.300 1 303 83 ASP CB C 43.55 0.300 1 304 83 ASP N N 128.50 0.200 1 305 84 SER H H 8.23 0.020 1 306 84 SER CA C 57.55 0.300 1 308 84 SER N N 108.20 0.200 1 309 85 TRP H H 7.74 0.020 1 310 85 TRP CA C 57.25 0.300 1 311 85 TRP CB C 29.35 0.300 1 312 85 TRP N N 119.50 0.200 1 313 86 GLY H H 9.34 0.020 1 314 86 GLY CA C 45.05 0.300 1 315 86 GLY N N 110.50 0.200 1 316 87 THR H H 8.05 0.020 1 317 87 THR CA C 63.45 0.300 1 318 87 THR CB C 68.95 0.300 1 319 87 THR N N 117.50 0.200 1 320 88 TYR H H 8.18 0.020 1 321 88 TYR CA C 56.65 0.300 1 322 88 TYR CB C 40.85 0.300 1 324 89 ARG H H 8.07 0.020 1 325 89 ARG CA C 51.65 0.300 1 326 89 ARG CB C 30.25 0.300 1 327 89 ARG N N 132.40 0.200 1 328 90 PRO CA C 62.95 0.300 1 330 91 THR H H 6.03 0.020 1 331 91 THR CA C 58.65 0.300 1 332 91 THR CB C 71.95 0.300 1 333 91 THR N N 105.30 0.200 1 334 92 GLY H H 5.22 0.020 1 335 92 GLY CA C 46.05 0.300 1 336 92 GLY N N 107.10 0.200 1 337 93 THR H H 9.02 0.020 1 338 93 THR CA C 64.15 0.300 1 339 93 THR CB C 68.55 0.300 1 340 93 THR N N 124.30 0.200 1 341 94 TYR H H 9.09 0.020 1 342 94 TYR CA C 59.95 0.300 1 344 94 TYR N N 130.60 0.200 1 345 95 LYS H H 8.47 0.020 1 346 95 LYS CA C 53.85 0.300 1 347 95 LYS CB C 33.45 0.300 1 348 95 LYS N N 124.30 0.200 1 349 96 GLY H H 5.61 0.020 1 350 96 GLY CA C 44.85 0.300 1 351 96 GLY N N 103.20 0.200 1 352 97 THR H H 8.13 0.020 1 353 97 THR CA C 60.15 0.300 1 354 97 THR CB C 74.25 0.300 1 355 97 THR N N 108.90 0.200 1 356 98 VAL H H 9.29 0.020 1 357 98 VAL CA C 59.65 0.300 1 358 98 VAL CB C 34.75 0.300 1 359 98 VAL N N 119.60 0.200 1 360 99 LYS H H 8.51 0.020 1 361 99 LYS CA C 54.85 0.300 1 362 99 LYS CB C 32.95 0.300 1 363 99 LYS N N 128.90 0.200 1 364 100 SER H H 8.75 0.020 1 365 100 SER CA C 59.35 0.300 1 367 100 SER N N 116.60 0.200 1 368 101 ASP H H 9.66 0.020 1 369 101 ASP CA C 55.75 0.300 1 371 101 ASP N N 124.20 0.200 1 372 102 GLY H H 8.84 0.020 1 373 102 GLY CA C 46.05 0.300 1 374 102 GLY N N 105.50 0.200 1 375 103 GLY H H 8.23 0.020 1 376 103 GLY CA C 43.35 0.300 1 377 103 GLY N N 109.00 0.200 1 378 104 THR H H 8.06 0.020 1 379 104 THR CA C 62.65 0.300 1 380 104 THR CB C 69.95 0.300 1 381 104 THR N N 116.10 0.200 1 382 105 TYR H H 9.81 0.020 1 383 105 TYR CA C 56.05 0.300 1 384 105 TYR CB C 39.55 0.300 1 385 105 TYR N N 126.00 0.200 1 386 106 ASP H H 8.81 0.020 1 387 106 ASP CA C 54.45 0.300 1 388 106 ASP CB C 44.85 0.300 1 389 106 ASP N N 121.80 0.200 1 390 107 ILE H H 8.45 0.020 1 391 107 ILE CA C 59.55 0.300 1 392 107 ILE CB C 39.35 0.300 1 393 107 ILE N N 121.50 0.200 1 394 108 TYR H H 9.19 0.020 1 395 108 TYR CA C 54.75 0.300 1 396 108 TYR CB C 43.35 0.300 1 397 108 TYR N N 122.80 0.200 1 398 109 THR H H 8.36 0.020 1 399 109 THR CA C 59.95 0.300 1 400 109 THR CB C 71.75 0.300 1 401 109 THR N N 108.60 0.200 1 402 110 THR H H 8.84 0.020 1 403 110 THR CA C 61.65 0.300 1 404 110 THR CB C 73.05 0.300 1 405 110 THR N N 114.40 0.200 1 406 111 THR H H 8.49 0.020 1 407 111 THR CA C 62.35 0.300 1 408 111 THR CB C 71.35 0.300 1 409 111 THR N N 117.00 0.200 1 410 112 ARG H H 8.32 0.020 1 411 112 ARG CA C 53.55 0.300 1 412 112 ARG CB C 30.85 0.300 1 413 112 ARG N N 125.70 0.200 1 414 113 TYR H H 8.16 0.020 1 415 113 TYR CA C 56.65 0.300 1 416 113 TYR CB C 40.65 0.300 1 417 113 TYR N N 119.60 0.200 1 418 114 ASN H H 8.01 0.020 1 419 114 ASN CA C 54.05 0.300 1 420 114 ASN CB C 37.15 0.300 1 422 115 ALA H H 9.31 0.020 1 423 115 ALA CA C 50.05 0.300 1 424 115 ALA CB C 21.95 0.300 1 425 115 ALA N N 122.70 0.200 1 426 116 PRO CA C 62.95 0.300 1 427 116 PRO CB C 31.35 0.300 1 428 117 SER H H 8.64 0.020 1 429 117 SER CA C 56.45 0.300 1 430 117 SER CB C 68.15 0.300 1 431 117 SER N N 115.40 0.200 1 432 118 ILE H H 4.03 0.020 1 433 118 ILE CA C 63.05 0.300 1 435 118 ILE N N 112.20 0.200 1 436 119 ASP H H 7.21 0.020 1 437 119 ASP CA C 54.05 0.300 1 438 119 ASP CB C 42.05 0.300 1 439 119 ASP N N 119.50 0.200 1 440 120 GLY H H 7.21 0.020 1 441 120 GLY CA C 45.05 0.300 1 442 120 GLY N N 108.10 0.200 1 443 121 ASP H H 8.11 0.020 1 444 121 ASP CA C 55.25 0.300 1 445 121 ASP CB C 41.45 0.300 1 446 121 ASP N N 117.90 0.200 1 447 122 ARG H H 8.26 0.020 1 448 122 ARG CA C 55.35 0.300 1 449 122 ARG CB C 30.65 0.300 1 450 122 ARG N N 120.40 0.200 1 451 123 THR H H 9.03 0.020 1 452 123 THR CA C 60.55 0.300 1 453 123 THR CB C 72.35 0.300 1 454 123 THR N N 116.80 0.200 1 455 124 THR H H 8.30 0.020 1 456 124 THR CA C 60.65 0.300 1 457 124 THR CB C 71.65 0.300 1 458 124 THR N N 118.20 0.200 1 459 125 PHE H H 8.16 0.020 1 460 125 PHE CA C 55.95 0.300 1 461 125 PHE CB C 39.65 0.300 1 462 125 PHE N N 122.20 0.200 1 463 126 THR H H 7.48 0.020 1 464 126 THR CA C 62.35 0.300 1 465 126 THR CB C 70.35 0.300 1 466 126 THR N N 116.60 0.200 1 467 127 GLN H H 8.97 0.020 1 468 127 GLN CA C 52.95 0.300 1 469 127 GLN CB C 31.25 0.300 1 470 127 GLN N N 121.20 0.200 1 471 128 TYR H H 8.08 0.020 1 472 128 TYR CA C 51.85 0.300 1 473 128 TYR CB C 37.65 0.300 1 474 128 TYR N N 122.00 0.200 1 475 129 TRP H H 8.64 0.020 1 476 129 TRP CA C 56.05 0.300 1 477 129 TRP CB C 32.45 0.300 1 478 129 TRP N N 117.70 0.200 1 479 130 SER H H 9.13 0.020 1 480 130 SER CA C 58.35 0.300 1 481 130 SER CB C 66.65 0.300 1 482 130 SER N N 120.00 0.200 1 483 131 VAL H H 10.28 0.020 1 484 131 VAL CA C 61.45 0.300 1 485 131 VAL CB C 35.05 0.300 1 486 131 VAL N N 124.20 0.200 1 487 132 ARG H H 9.07 0.020 1 488 132 ARG CA C 58.85 0.300 1 489 132 ARG CB C 29.95 0.300 1 490 132 ARG N N 136.20 0.200 1 491 133 GLN H H 9.06 0.020 1 492 133 GLN CA C 60.25 0.300 1 493 133 GLN CB C 27.85 0.300 1 494 133 GLN N N 122.20 0.200 1 495 134 THR H H 7.51 0.020 1 496 134 THR CA C 59.15 0.300 1 497 134 THR CB C 71.75 0.300 1 498 134 THR N N 106.00 0.200 1 499 135 LYS H H 8.59 0.020 1 500 135 LYS CA C 58.65 0.300 1 501 135 LYS CB C 32.45 0.300 1 503 136 ARG H H 8.99 0.020 1 504 136 ARG CA C 55.25 0.300 1 505 136 ARG CB C 32.95 0.300 1 506 136 ARG N N 126.70 0.200 1 507 137 PRO CA C 63.75 0.300 1 509 138 THR H H 8.51 0.020 1 510 138 THR CA C 60.65 0.300 1 511 138 THR CB C 70.25 0.300 1 512 138 THR N N 114.00 0.200 1 513 139 GLY H H 9.08 0.020 1 514 139 GLY CA C 45.55 0.300 1 515 139 GLY N N 113.50 0.200 1 516 140 SER H H 7.47 0.020 1 517 140 SER CA C 56.25 0.300 1 518 140 SER CB C 65.35 0.300 1 519 140 SER N N 112.90 0.200 1 520 141 ASN H H 8.74 0.020 1 521 141 ASN CA C 54.55 0.300 1 522 141 ASN CB C 36.95 0.300 1 523 141 ASN N N 121.80 0.200 1 524 142 ALA H H 9.40 0.020 1 525 142 ALA CA C 50.95 0.300 1 526 142 ALA CB C 20.95 0.300 1 527 142 ALA N N 129.80 0.200 1 528 143 THR H H 7.30 0.020 1 529 143 THR CA C 60.95 0.300 1 530 143 THR CB C 72.35 0.300 1 531 143 THR N N 111.60 0.200 1 532 144 ILE H H 9.54 0.020 1 533 144 ILE CA C 61.25 0.300 1 534 144 ILE CB C 40.85 0.300 1 535 144 ILE N N 125.00 0.200 1 536 145 THR H H 10.58 0.020 1 537 145 THR CA C 61.55 0.300 1 538 145 THR CB C 66.15 0.300 1 539 145 THR N N 131.40 0.200 1 540 146 PHE H H 7.60 0.020 1 541 146 PHE CA C 60.15 0.300 1 542 146 PHE CB C 39.25 0.300 1 543 146 PHE N N 128.10 0.200 1 544 147 SER H H 8.96 0.020 1 545 147 SER CA C 61.35 0.300 1 546 147 SER CB C 62.35 0.300 1 547 147 SER N N 114.20 0.200 1 548 148 ASN H H 7.25 0.020 1 549 148 ASN CA C 55.15 0.300 1 550 148 ASN CB C 35.95 0.300 1 551 148 ASN N N 118.10 0.200 1 552 149 HIS H H 6.70 0.020 1 553 149 HIS CA C 59.65 0.300 1 554 149 HIS CB C 29.65 0.300 1 555 149 HIS N N 121.90 0.200 1 556 150 VAL H H 7.17 0.020 1 557 150 VAL CA C 66.65 0.300 1 558 150 VAL CB C 31.35 0.300 1 559 150 VAL N N 117.30 0.200 1 560 151 ASN H H 7.98 0.020 1 561 151 ASN CA C 56.15 0.300 1 562 151 ASN CB C 37.65 0.300 1 563 151 ASN N N 116.30 0.200 1 564 152 ALA H H 7.36 0.020 1 565 152 ALA CA C 54.95 0.300 1 566 152 ALA CB C 18.35 0.300 1 567 152 ALA N N 124.90 0.200 1 568 153 TRP H H 9.24 0.020 1 569 153 TRP CA C 58.55 0.300 1 570 153 TRP CB C 27.15 0.300 1 571 153 TRP N N 122.30 0.200 1 572 154 LYS H H 8.33 0.020 1 573 154 LYS CA C 60.55 0.300 1 574 154 LYS CB C 31.95 0.300 1 575 154 LYS N N 121.90 0.200 1 576 155 SER H H 7.79 0.020 1 577 155 SER CA C 61.15 0.300 1 579 155 SER N N 116.20 0.200 1 580 156 HIS H H 7.53 0.020 1 581 156 HIS CA C 55.55 0.300 1 582 156 HIS CB C 28.85 0.300 1 583 156 HIS N N 118.30 0.200 1 584 157 GLY H H 7.85 0.020 1 585 157 GLY CA C 46.15 0.300 1 586 157 GLY N N 107.50 0.200 1 587 158 MET H H 7.81 0.020 1 588 158 MET CA C 54.15 0.300 1 589 158 MET CB C 32.65 0.300 1 590 158 MET N N 121.60 0.200 1 591 159 ASN H H 8.08 0.020 1 592 159 ASN CA C 53.15 0.300 1 594 159 ASN N N 119.50 0.200 1 595 160 LEU H H 9.14 0.020 1 596 160 LEU CA C 54.45 0.300 1 597 160 LEU CB C 43.25 0.300 1 598 160 LEU N N 128.50 0.200 1 599 161 GLY H H 7.08 0.020 1 600 161 GLY CA C 45.45 0.300 1 601 161 GLY N N 105.40 0.200 1 602 162 SER H H 7.46 0.020 1 603 162 SER CA C 58.65 0.300 1 604 162 SER CB C 64.55 0.300 1 605 162 SER N N 109.20 0.200 1 606 163 ASN H H 7.75 0.020 1 607 163 ASN CA C 51.75 0.300 1 608 163 ASN CB C 40.15 0.300 1 609 163 ASN N N 121.10 0.200 1 610 164 TRP H H 9.08 0.020 1 611 164 TRP CA C 59.85 0.300 1 612 164 TRP CB C 29.45 0.300 1 613 164 TRP N N 128.00 0.200 1 614 165 ALA H H 7.36 0.020 1 615 165 ALA CA C 49.85 0.300 1 616 165 ALA CB C 17.95 0.300 1 617 165 ALA N N 126.80 0.200 1 618 166 TYR H H 6.12 0.020 1 619 166 TYR CA C 57.85 0.300 1 620 166 TYR CB C 38.35 0.300 1 621 166 TYR N N 115.60 0.200 1 622 167 GLN H H 8.61 0.020 1 623 167 GLN CA C 55.25 0.300 1 624 167 GLN CB C 34.85 0.300 1 625 167 GLN N N 122.70 0.200 1 626 168 VAL H H 9.99 0.020 1 627 168 VAL CA C 59.15 0.300 1 628 168 VAL CB C 36.75 0.300 1 629 168 VAL N N 119.50 0.200 1 630 169 MET H H 8.52 0.020 1 631 169 MET CA C 54.85 0.300 1 632 169 MET CB C 32.05 0.300 1 633 169 MET N N 122.70 0.200 1 634 170 ALA H H 9.83 0.020 1 635 170 ALA CA C 52.25 0.300 1 636 170 ALA CB C 23.35 0.300 1 637 170 ALA N N 134.40 0.200 1 638 171 THR H H 9.14 0.020 1 639 171 THR CA C 62.55 0.300 1 641 171 THR N N 114.10 0.200 1 642 172 GLU H H 8.69 0.020 1 643 172 GLU CA C 52.75 0.300 1 644 172 GLU CB C 31.75 0.300 1 645 172 GLU N N 125.90 0.200 1 646 173 GLY H H 6.01 0.020 1 647 173 GLY CA C 44.45 0.300 1 648 173 GLY N N 108.60 0.200 1 649 174 TYR H H 7.03 0.020 1 650 174 TYR CA C 56.65 0.300 1 651 174 TYR CB C 40.35 0.300 1 652 174 TYR N N 117.10 0.200 1 653 175 GLN H H 7.62 0.020 1 654 175 GLN CA C 56.45 0.300 1 655 175 GLN CB C 25.85 0.300 1 656 175 GLN N N 123.00 0.200 1 657 176 SER H H 7.63 0.020 1 658 176 SER CA C 56.35 0.300 1 660 176 SER N N 110.90 0.200 1 661 177 SER H H 7.58 0.020 1 662 177 SER CA C 56.35 0.300 1 663 177 SER CB C 67.05 0.300 1 664 177 SER N N 110.90 0.200 1 665 178 GLY H H 7.54 0.020 1 666 178 GLY CA C 44.75 0.300 1 667 178 GLY N N 107.30 0.200 1 668 179 SER H H 6.30 0.020 1 669 179 SER CA C 57.55 0.300 1 670 179 SER CB C 66.75 0.300 1 671 179 SER N N 111.90 0.200 1 672 180 SER H H 9.50 0.020 1 673 180 SER CA C 56.85 0.300 1 674 180 SER CB C 67.15 0.300 1 675 180 SER N N 116.20 0.200 1 676 181 ASN H H 9.16 0.020 1 677 181 ASN CA C 55.05 0.300 1 678 181 ASN CB C 41.05 0.300 1 679 181 ASN N N 125.20 0.200 1 680 182 VAL H H 8.60 0.020 1 681 182 VAL CA C 61.05 0.300 1 682 182 VAL CB C 36.15 0.300 1 683 182 VAL N N 125.40 0.200 1 684 183 THR H H 8.54 0.020 1 685 183 THR CA C 62.15 0.300 1 686 183 THR CB C 70.65 0.300 1 687 183 THR N N 122.60 0.200 1 688 184 VAL H H 8.52 0.020 1 692 185 TRP H H 9.51 0.020 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 8762143 save_