data_5935 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific 1H, 13C and 15N resonance assignments of rat liver fructose-2,6-bisphosphatase domain ; _BMRB_accession_number 5935 _BMRB_flat_file_name bmr5935.str _Entry_type original _Submission_date 2003-09-05 _Accession_date 2003-09-08 _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 Zangger Klaus . . 2 Pervushin Konstantin . . 3 Sterk Heinz . . 4 Lange Alex J. . 5 Okar David A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 163 "13C chemical shifts" 558 "15N chemical shifts" 163 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-10-06 original author . stop_ _Original_release_date 2003-10-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Sequence-specific 1H, 13C and 15N resonance assignments of rat liver fructose-2,6-bisphosphatase domain ; _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 Zangger Klaus . . 2 Pervushin Konstantin . . 3 Sterk Heinz . . 4 Lange Alex J. . 5 Okar David A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 281 _Page_last 282 _Year 2003 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister G.W. W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Johnson, B. A., and Blevins, R. A. (1994) J.Biomol.NMR 4, 603-614. ; _Citation_title . _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_3 _Saveframe_category citation _Citation_full ; Lee, Y. H., Ogata, C., Pflugrath, J. W., Levitt, D. G., Sarma, R., Banaszak, L. J., and Pilkis, S. J. (1996) Biochemistry 35(19), 6010-9. ; _Citation_title 'Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8634242 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee Y.H. H. . 2 Ogata C. . . 3 Pflugrath J.W. W. . 4 Levitt D.G. G. . 5 Sarma R. . . 6 Banaszak L.J. J. . 7 Pilkis S.J. J. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 35 _Journal_issue 19 _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 6010 _Page_last 6019 _Year 1996 _Details ; The crystal structure of the recombinant fructose-2,6-bisphosphatase domain, which covers the residues between 251 and 440 of the rat liver bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, was determined by multiwavelength anomalous dispersion phasing and refined at 2.5 A resolution. The selenomethionine-substituted protein was induced in the methionine auxotroph, Escherichia coli DL41DE3, purified, and crystallized in a manner similar to that of the native protein. Phase information was calculated using the multiwavelength anomalous dispersion data collected at the X-ray wavelengths near the absorption edge of the K-shell alpha electrons of selenium. The fructose-2,6-bisphosphatase domain has a core alpha/beta structure which consists of six stacked beta-strands, four parallel and two antiparallel. The core beta-sheet is surrounded by nine alpha-helices. The catalytic site, as defined by a bound phosphate ion, is positioned near the C-terminal end of the beta-sheet and close to the N-terminal end of an alpha-helix. The active site pocket is funnel-shaped. The narrow opening of the funnel is wide enough for a water molecule to pass. The key catalytic residues, including His7, His141, and Glu76, are near each other at the active site and probably function as general acids and/or bases during a catalytic cycle. The inorganic phosphate molecule is bound to an anion trap formed by Arg6, His7, Arg56, and His141. The core structure of the Fru-2,6-P2ase is similar to that of the yeast phosphoglycerate mutase and the rat prostatic acid phosphatase. However, the structure of one of the loops near the active site is completely different from the other family members, perhaps reflecting functional differences and the nanomolar range affinity of Fru-2,6-P2ase for its substrate. The imidazole rings of the two key catalytic residues, His7 and His141, are not parallel as in the yeast phosphoglycerate mutase. The crystal structure is used to interpret the existing chemical data already available for the bisphosphatase domain. In addition, the crystal structure is compared with two other proteins that belong to the histidine phosphatase family. ; save_ save_ref_4 _Saveframe_category citation _Citation_full ; Hasemann, C. A., Istvan, E. S., Uyeda, K., and Deisenhofer, J. (1996) Structure 4(9), 1017-29. ; _Citation_title 'The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8805587 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hasemann C.A. A. . 2 Istvan E.S. S. . 3 Uyeda K. . . 4 Deisenhofer J. . . stop_ _Journal_abbreviation Structure _Journal_name_full 'Structure (London, England : 1993)' _Journal_volume 4 _Journal_issue 9 _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 1017 _Page_last 1029 _Year 1996 _Details ; BACKGROUND. Glucose homeostasis is maintained by the processes of glycolysis and gluconeogenesis. The importance of these pathways is demonstrated by the severe and life threatening effects observed in various forms of diabetes. The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. Thus this bifunctional enzyme plays an indirect yet key role in the regulation of glucose metabolism. RESULTS. We have determined the 2.0 A crystal structure of the rat testis isozyme of this bifunctional enzyme. The enzyme is a homodimer of 55 kDa subunits arranged in a head-to-head fashion, with each monomer consisting of independent kinase and phosphatase domains. The location of ATPgammaS and inorganic phosphate in the kinase and phosphatase domains, respectively, allow us to locate and describe the active sites of both domains. CONCLUSIONS. The kinase domain is clearly related to the superfamily of mononucleotide binding proteins, with a particularly close relationship to the adenylate kinases and the nucleotide-binding portion of the G proteins. This is in disagreement with the broad speculation that this domain would resemble phosphofructokinase. The phosphatase domain is structurally related to a family of proteins which includes the cofactor independent phosphoglycerate mutases and acid phosphatases. ; save_ ################################## # Molecular system description # ################################## save_system_FBP-2 _Saveframe_category molecular_system _Mol_system_name fructose-2,6-bisphosphatase _Abbreviation_common FBP-2 _Enzyme_commission_number 3.1.3.46 loop_ _Mol_system_component_name _Mol_label 'FBP-2 monomer' $FBP-2_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function phosphatase stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FBP-2_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Fructose-2,6-bisphosphatase _Abbreviation_common FBP-2 _Molecular_mass 25554 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 221 _Mol_residue_sequence ; MRSIYLCRHGESELNLRGRI GGDSGLSARGKQYAYALANF IRSQGISSLKVWTSHMKRTI QTAEALGVPYEQWKALNEID AGVCEEMTYEEIQEHYPEEF ALRDQDKYRYRYPKGESYED LVQRLEPVIMELERQENVLV ICHQAVMRCLLAYFLDKSSD ELPYLKCPLHTVLKLTPVAY GCRVESIYLNVEAVNTHRDK PENVDITREAEEALDTVPAH Y ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 SER 4 ILE 5 TYR 6 LEU 7 CYS 8 ARG 9 HIS 10 GLY 11 GLU 12 SER 13 GLU 14 LEU 15 ASN 16 LEU 17 ARG 18 GLY 19 ARG 20 ILE 21 GLY 22 GLY 23 ASP 24 SER 25 GLY 26 LEU 27 SER 28 ALA 29 ARG 30 GLY 31 LYS 32 GLN 33 TYR 34 ALA 35 TYR 36 ALA 37 LEU 38 ALA 39 ASN 40 PHE 41 ILE 42 ARG 43 SER 44 GLN 45 GLY 46 ILE 47 SER 48 SER 49 LEU 50 LYS 51 VAL 52 TRP 53 THR 54 SER 55 HIS 56 MET 57 LYS 58 ARG 59 THR 60 ILE 61 GLN 62 THR 63 ALA 64 GLU 65 ALA 66 LEU 67 GLY 68 VAL 69 PRO 70 TYR 71 GLU 72 GLN 73 TRP 74 LYS 75 ALA 76 LEU 77 ASN 78 GLU 79 ILE 80 ASP 81 ALA 82 GLY 83 VAL 84 CYS 85 GLU 86 GLU 87 MET 88 THR 89 TYR 90 GLU 91 GLU 92 ILE 93 GLN 94 GLU 95 HIS 96 TYR 97 PRO 98 GLU 99 GLU 100 PHE 101 ALA 102 LEU 103 ARG 104 ASP 105 GLN 106 ASP 107 LYS 108 TYR 109 ARG 110 TYR 111 ARG 112 TYR 113 PRO 114 LYS 115 GLY 116 GLU 117 SER 118 TYR 119 GLU 120 ASP 121 LEU 122 VAL 123 GLN 124 ARG 125 LEU 126 GLU 127 PRO 128 VAL 129 ILE 130 MET 131 GLU 132 LEU 133 GLU 134 ARG 135 GLN 136 GLU 137 ASN 138 VAL 139 LEU 140 VAL 141 ILE 142 CYS 143 HIS 144 GLN 145 ALA 146 VAL 147 MET 148 ARG 149 CYS 150 LEU 151 LEU 152 ALA 153 TYR 154 PHE 155 LEU 156 ASP 157 LYS 158 SER 159 SER 160 ASP 161 GLU 162 LEU 163 PRO 164 TYR 165 LEU 166 LYS 167 CYS 168 PRO 169 LEU 170 HIS 171 THR 172 VAL 173 LEU 174 LYS 175 LEU 176 THR 177 PRO 178 VAL 179 ALA 180 TYR 181 GLY 182 CYS 183 ARG 184 VAL 185 GLU 186 SER 187 ILE 188 TYR 189 LEU 190 ASN 191 VAL 192 GLU 193 ALA 194 VAL 195 ASN 196 THR 197 HIS 198 ARG 199 ASP 200 LYS 201 PRO 202 GLU 203 ASN 204 VAL 205 ASP 206 ILE 207 THR 208 ARG 209 GLU 210 ALA 211 GLU 212 GLU 213 ALA 214 LEU 215 ASP 216 THR 217 VAL 218 PRO 219 ALA 220 HIS 221 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1C7Z "Regulatory Complex Of Fructose-2,6-bisphosphatase" 86.43 191 100.00 100.00 4.81e-138 PDB 1C80 "Regulatory Complex Of Fructose-2,6-bisphosphatase" 86.43 191 100.00 100.00 4.81e-138 PDB 1C81 "Michaelis Complex Of Fructose-2,6-bisphosphatase" 86.43 191 100.00 100.00 4.81e-138 PDB 1FBT "The Bisphosphatase Domain Of The Bifunctional Rat Liver 6- Phosphofructo-2-KinaseFRUCTOSE-2,6-Bisphosphatase" 85.97 190 97.89 97.89 7.18e-133 PDB 1TIP "The Bisphosphatase Domain Of The Bifunctional Rat Liver 6- Phosphofructo-2-kinase/fructose-2,6-bisphosphatase" 86.43 191 99.48 99.48 8.16e-137 DBJ BAE21271 "unnamed protein product [Mus musculus]" 99.55 448 99.09 99.09 7.66e-157 DBJ BAG36785 "unnamed protein product [Homo sapiens]" 99.55 471 97.27 99.09 3.08e-154 DBJ BAG62397 "unnamed protein product [Homo sapiens]" 99.55 406 97.27 99.09 3.52e-155 EMBL CAA33606 "unnamed protein product [Rattus norvegicus]" 99.55 448 100.00 100.00 1.19e-158 EMBL CAA33607 "6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase [Rattus norvegicus]" 99.55 471 100.00 100.00 2.65e-158 EMBL CAA68694 "unnamed protein product [Rattus norvegicus]" 99.55 471 100.00 100.00 2.65e-158 GB AAA30696 "6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase [Bos taurus]" 99.55 471 97.27 99.09 6.93e-153 GB AAA40624 "6-phosphofructo 2-kinase/fructose 2, 6-bisphosphatase, partial [Rattus norvegicus]" 99.55 304 100.00 100.00 7.52e-160 GB AAA79008 "6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase [Rattus norvegicus]" 99.55 471 100.00 100.00 2.93e-158 GB AAB19845 "fructose-2,6-bisphosphatase [Bos taurus]" 99.55 471 97.27 99.09 6.93e-153 GB AAH96077 "PFKFB1 protein [Homo sapiens]" 63.35 271 97.86 99.29 5.81e-94 PIR S77704 "6-phosphofructo-2-kinase (EC 2.7.1.105) / fructose-2, 6-bisphosphate 2-phosphatase (EC 3.1.3.46) clone 5c, skeletal muscle - ra" 99.55 469 100.00 100.00 5.56e-158 REF NP_001257992 "6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 isoform 2 [Rattus norvegicus]" 99.55 469 100.00 100.00 5.56e-158 REF NP_001257993 "6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 isoform 3 [Rattus norvegicus]" 99.55 427 100.00 100.00 2.05e-158 REF NP_001258733 "6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 isoform 2 [Homo sapiens]" 99.55 449 97.27 99.09 1.24e-154 REF NP_001258734 "6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 isoform 3 [Homo sapiens]" 99.55 406 97.27 99.09 3.52e-155 REF NP_002616 "6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 isoform 1 [Homo sapiens]" 99.55 471 97.27 99.09 3.08e-154 SP P07953 "RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; Short=6PF-2-K/Fru-2,6-P2ase 1; Short=PFK/FBPase 1; AltNam" 99.55 471 100.00 100.00 2.65e-158 SP P16118 "RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; Short=6PF-2-K/Fru-2,6-P2ase 1; Short=PFK/FBPase 1; AltNam" 99.55 471 97.27 99.09 3.08e-154 SP P49872 "RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; Short=6PF-2-K/Fru-2,6-P2ase 1; Short=PFK/FBPase 1; AltNam" 99.55 471 97.27 99.09 6.93e-153 SP P70266 "RecName: Full=6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1; Short=6PF-2-K/Fru-2,6-P2ase 1; Short=PFK/FBPase 1; AltNam" 99.55 471 99.09 99.09 1.28e-156 TPG DAA12796 "TPA: 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 1 [Bos taurus]" 99.55 471 97.73 99.55 4.01e-155 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Organ $FBP-2_monomer Rat 10116 Eukaryota Metazoa Rattus norvegicus liver stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name _Details $FBP-2_monomer 'recombinant technology' . . . . . 'Expressed in E.Coli BL21(DE3) cells.' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FBP-2_monomer 2.7 mM '[U-95% 13C; U-95 15N]' 'sodium phosphate' 100 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $FBP-2_monomer 1.5 mM . 'sodium phosphate' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 03/2002 loop_ _Task processing stop_ _Details ; F.Delaglio, S.Grzesiek, G.W.Vuister, G.Zhu, J.Pfeifer and A.Bax, J.Biomol. NMR 6, 277-293 (1995). ; save_ save_NMRView _Saveframe_category software _Name NMRView _Version 5.0.3 loop_ _Task analysis stop_ _Details ; B.A.Johnson and R.A.Blevins J.Biomol. NMR 4, 603-614 (1994). ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_NMR_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'A cryo-probe was used on the Bruker Avance 600.' save_ ############################# # NMR applied experiments # ############################# save_TROSY_versions_used_for_all_experiments;_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'TROSY versions used for all experiments;' _Sample_label . save_ save_2H_decoupling_used_on_triply-labeled_sample._2 _Saveframe_category NMR_applied_experiment _Experiment_name '2H decoupling used on triply-labeled sample.' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 298 1 K 'ionic strength' 1.2 0.05 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; For residues 219-221 a second set of resonances with slightly different chemical shifts was observed. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'FBP-2 monomer' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ARG CA C 55.816 0.05 1 2 . 2 ARG CB C 30.362 0.05 1 3 . 2 ARG C C 175.541 0.05 1 4 . 3 SER N N 114.229 0.05 1 5 . 3 SER H H 8.215 0.02 1 6 . 3 SER CA C 57.816 0.05 1 7 . 3 SER CB C 65.772 0.05 1 8 . 3 SER C C 171.241 0.05 1 9 . 4 ILE N N 121.294 0.05 1 10 . 4 ILE H H 8.326 0.02 1 11 . 4 ILE CA C 58.584 0.05 1 12 . 4 ILE CB C 39.760 0.05 1 13 . 4 ILE C C 174.005 0.05 1 14 . 5 TYR N N 125.148 0.05 1 15 . 5 TYR H H 9.519 0.02 1 16 . 5 TYR CA C 55.611 0.05 1 17 . 5 TYR CB C 40.013 0.05 1 18 . 5 TYR C C 174.340 0.05 1 19 . 6 LEU N N 122.294 0.05 1 20 . 6 LEU H H 9.451 0.02 1 21 . 6 LEU CA C 52.437 0.05 1 22 . 6 LEU CB C 45.054 0.05 1 23 . 7 CYS CA C 60.826 0.05 1 24 . 7 CYS C C 177.528 0.05 1 25 . 8 ARG N N 119.519 0.05 1 26 . 8 ARG H H 8.260 0.02 1 27 . 8 ARG CA C 54.889 0.05 1 28 . 8 ARG CB C 32.817 0.05 1 29 . 8 ARG C C 177.584 0.05 1 30 . 9 HIS N N 111.659 0.05 1 31 . 9 HIS H H 6.450 0.02 1 32 . 9 HIS CA C 53.511 0.05 1 33 . 9 HIS CB C 29.078 0.05 1 34 . 9 HIS C C 174.645 0.05 1 35 . 10 GLY N N 106.721 0.05 1 36 . 10 GLY H H 8.304 0.02 1 37 . 10 GLY CA C 46.290 0.05 1 38 . 11 GLU CA C 58.563 0.05 1 39 . 11 GLU CB C 31.838 0.05 1 40 . 11 GLU C C 173.927 0.05 1 41 . 12 SER N N 123.864 0.05 1 42 . 12 SER H H 9.643 0.02 1 43 . 12 SER CA C 56.183 0.05 1 44 . 12 SER CB C 66.430 0.05 1 45 . 12 SER C C 175.449 0.05 1 46 . 13 GLU N N 119.367 0.05 1 47 . 13 GLU H H 8.800 0.02 1 48 . 13 GLU CA C 59.257 0.05 1 49 . 13 GLU CB C 29.176 0.05 1 50 . 13 GLU C C 179.817 0.05 1 51 . 14 LEU N N 120.096 0.05 1 52 . 14 LEU H H 8.132 0.02 1 53 . 14 LEU CA C 56.535 0.05 1 54 . 14 LEU CB C 40.187 0.05 1 55 . 15 ASN CA C 54.682 0.05 1 56 . 16 LEU N N 125.866 0.05 1 57 . 16 LEU H H 7.791 0.02 1 58 . 16 LEU CA C 57.292 0.05 1 59 . 16 LEU CB C 37.176 0.05 1 60 . 16 LEU C C 178.009 0.05 1 61 . 17 ARG N N 114.850 0.05 1 62 . 17 ARG H H 7.038 0.02 1 63 . 17 ARG CA C 54.831 0.05 1 64 . 17 ARG CB C 30.222 0.05 1 65 . 17 ARG C C 175.837 0.05 1 66 . 18 GLY N N 109.090 0.05 1 67 . 18 GLY H H 7.940 0.02 1 68 . 18 GLY CA C 45.786 0.05 1 69 . 18 GLY C C 173.893 0.05 1 70 . 19 ARG N N 116.798 0.05 1 71 . 19 ARG H H 7.653 0.02 1 72 . 19 ARG CA C 54.640 0.05 1 73 . 19 ARG CB C 31.670 0.05 1 74 . 19 ARG C C 176.681 0.05 1 75 . 20 ILE CA C 60.841 0.05 1 76 . 20 ILE C C 176.370 0.05 1 77 . 21 GLY N N 109.612 0.05 1 78 . 21 GLY H H 8.872 0.02 1 79 . 21 GLY CA C 45.865 0.05 1 80 . 21 GLY C C 176.188 0.05 1 81 . 22 GLY N N 110.375 0.05 1 82 . 22 GLY H H 9.802 0.02 1 83 . 22 GLY CA C 43.966 0.05 1 84 . 22 GLY C C 173.139 0.05 1 85 . 23 ASP N N 119.367 0.05 1 86 . 23 ASP H H 9.175 0.02 1 87 . 23 ASP CA C 52.181 0.05 1 88 . 23 ASP CB C 39.270 0.05 1 89 . 24 SER CA C 57.520 0.05 1 90 . 24 SER CB C 66.209 0.05 1 91 . 24 SER C C 175.358 0.05 1 92 . 25 GLY N N 106.773 0.05 1 93 . 25 GLY H H 8.835 0.02 1 94 . 25 GLY CA C 42.665 0.05 1 95 . 25 GLY C C 173.006 0.05 1 96 . 26 LEU N N 114.871 0.05 1 97 . 26 LEU H H 8.125 0.02 1 98 . 26 LEU CA C 54.823 0.05 1 99 . 26 LEU CB C 42.104 0.05 1 100 . 26 LEU C C 179.141 0.05 1 101 . 27 SER N N 118.594 0.05 1 102 . 27 SER H H 9.701 0.02 1 103 . 27 SER CA C 56.327 0.05 1 104 . 27 SER CB C 65.944 0.05 1 105 . 28 ALA CA C 54.309 0.05 1 106 . 29 ARG N N 119.688 0.05 1 107 . 29 ARG H H 8.116 0.02 1 108 . 29 ARG CA C 57.925 0.05 1 109 . 29 ARG CB C 30.055 0.05 1 110 . 29 ARG C C 175.911 0.05 1 111 . 30 GLY N N 109.614 0.05 1 112 . 30 GLY H H 8.533 0.02 1 113 . 30 GLY CA C 43.473 0.05 1 114 . 30 GLY C C 173.453 0.05 1 115 . 31 LYS CA C 59.883 0.05 1 116 . 31 LYS C C 174.163 0.05 1 117 . 32 GLN N N 127.017 0.05 1 118 . 32 GLN H H 8.646 0.02 1 119 . 32 GLN CA C 58.557 0.05 1 120 . 32 GLN CB C 32.426 0.05 1 121 . 32 GLN C C 180.203 0.05 1 122 . 33 TYR N N 120.750 0.05 1 123 . 33 TYR H H 8.607 0.02 1 124 . 33 TYR CA C 60.107 0.05 1 125 . 33 TYR CB C 35.763 0.05 1 126 . 34 ALA N N 123.927 0.05 1 127 . 34 ALA H H 7.938 0.02 1 128 . 34 ALA CA C 54.831 0.05 1 129 . 34 ALA CB C 17.071 0.05 1 130 . 34 ALA C C 179.213 0.05 1 131 . 35 TYR N N 116.065 0.05 1 132 . 35 TYR H H 7.438 0.02 1 133 . 35 TYR CA C 60.547 0.05 1 134 . 35 TYR CB C 36.854 0.05 1 135 . 35 TYR C C 178.779 0.05 1 136 . 36 ALA N N 124.299 0.05 1 137 . 36 ALA H H 7.913 0.02 1 138 . 36 ALA CA C 54.339 0.05 1 139 . 36 ALA CB C 17.388 0.05 1 140 . 36 ALA C C 179.291 0.05 1 141 . 37 LEU CA C 56.736 0.05 1 142 . 37 LEU C C 177.719 0.05 1 143 . 38 ALA N N 121.882 0.05 1 144 . 38 ALA H H 7.665 0.02 1 145 . 38 ALA CA C 54.855 0.05 1 146 . 38 ALA CB C 17.315 0.05 1 147 . 38 ALA C C 179.797 0.05 1 148 . 39 ASN N N 115.948 0.05 1 149 . 39 ASN H H 7.578 0.02 1 150 . 39 ASN CA C 55.800 0.05 1 151 . 39 ASN CB C 37.457 0.05 1 152 . 39 ASN C C 177.611 0.05 1 153 . 40 PHE N N 122.571 0.05 1 154 . 40 PHE H H 8.417 0.02 1 155 . 40 PHE CA C 60.825 0.05 1 156 . 40 PHE CB C 38.384 0.05 1 157 . 40 PHE C C 178.180 0.05 1 158 . 41 ILE N N 119.981 0.05 1 159 . 41 ILE H H 8.818 0.02 1 160 . 41 ILE CA C 61.853 0.05 1 161 . 41 ILE CB C 34.884 0.05 1 162 . 42 ARG N N 124.617 0.05 1 163 . 42 ARG H H 8.225 0.02 1 164 . 42 ARG CA C 59.318 0.05 1 165 . 42 ARG CB C 28.937 0.05 1 166 . 42 ARG C C 179.033 0.05 1 167 . 43 SER N N 114.229 0.05 1 168 . 43 SER H H 7.731 0.02 1 169 . 43 SER CA C 60.134 0.05 1 170 . 43 SER CB C 62.788 0.05 1 171 . 43 SER C C 175.226 0.05 1 172 . 44 GLN N N 118.083 0.05 1 173 . 44 GLN H H 7.309 0.02 1 174 . 44 GLN CA C 55.320 0.05 1 175 . 44 GLN CB C 28.386 0.05 1 176 . 44 GLN C C 176.938 0.05 1 177 . 45 GLY N N 107.163 0.05 1 178 . 45 GLY H H 7.399 0.02 1 179 . 45 GLY CA C 46.981 0.05 1 180 . 45 GLY C C 174.475 0.05 1 181 . 46 ILE N N 120.652 0.05 1 182 . 46 ILE H H 8.377 0.02 1 183 . 46 ILE CA C 60.362 0.05 1 184 . 46 ILE CB C 37.537 0.05 1 185 . 46 ILE C C 176.592 0.05 1 186 . 47 SER N N 122.701 0.05 1 187 . 47 SER H H 8.557 0.02 1 188 . 47 SER CA C 59.356 0.05 1 189 . 47 SER CB C 62.744 0.05 1 190 . 47 SER C C 174.490 0.05 1 191 . 48 SER N N 116.281 0.05 1 192 . 48 SER H H 8.227 0.02 1 193 . 48 SER CA C 57.047 0.05 1 194 . 48 SER CB C 62.018 0.05 1 195 . 48 SER C C 173.267 0.05 1 196 . 49 LEU N N 123.543 0.05 1 197 . 49 LEU H H 7.884 0.02 1 198 . 49 LEU CA C 54.692 0.05 1 199 . 49 LEU CB C 42.632 0.05 1 200 . 49 LEU C C 176.251 0.05 1 201 . 50 LYS N N 126.089 0.05 1 202 . 50 LYS H H 7.802 0.02 1 203 . 50 LYS CA C 53.860 0.05 1 204 . 50 LYS CB C 33.285 0.05 1 205 . 50 LYS C C 174.830 0.05 1 206 . 51 VAL N N 121.937 0.05 1 207 . 51 VAL H H 8.773 0.02 1 208 . 51 VAL CA C 61.037 0.05 1 209 . 51 VAL CB C 32.477 0.05 1 210 . 51 VAL C C 174.492 0.05 1 211 . 52 TRP N N 129.512 0.05 1 212 . 52 TRP H H 9.531 0.02 1 213 . 52 TRP CA C 52.437 0.05 1 214 . 52 TRP CB C 33.014 0.05 1 215 . 52 TRP C C 174.954 0.05 1 216 . 53 THR N N 111.895 0.05 1 217 . 53 THR H H 9.337 0.02 1 218 . 53 THR CA C 59.958 0.05 1 219 . 53 THR CB C 69.736 0.05 1 220 . 53 THR C C 174.995 0.05 1 221 . 54 SER N N 114.893 0.05 1 222 . 54 SER H H 7.592 0.02 1 223 . 54 SER CA C 56.258 0.05 1 224 . 54 SER CB C 63.980 0.05 1 225 . 54 SER C C 173.743 0.05 1 226 . 55 HIS N N 114.330 0.05 1 227 . 55 HIS H H 8.571 0.02 1 228 . 55 HIS CA C 56.278 0.05 1 229 . 55 HIS CB C 30.727 0.05 1 230 . 55 HIS C C 176.030 0.05 1 231 . 56 MET CA C 54.997 0.05 1 232 . 56 MET C C 178.477 0.05 1 233 . 57 LYS N N 114.696 0.05 1 234 . 57 LYS H H 7.251 0.02 1 235 . 57 LYS CA C 60.366 0.05 1 236 . 57 LYS CB C 30.564 0.05 1 237 . 57 LYS C C 175.376 0.05 1 238 . 58 ARG N N 111.692 0.05 1 239 . 58 ARG H H 7.000 0.02 1 240 . 58 ARG CA C 56.471 0.05 1 241 . 58 ARG CB C 31.384 0.05 1 242 . 59 THR CA C 64.438 0.05 1 243 . 59 THR C C 175.698 0.05 1 244 . 60 ILE N N 128.935 0.05 1 245 . 60 ILE H H 7.332 0.02 1 246 . 60 ILE CA C 65.817 0.05 1 247 . 60 ILE CB C 37.796 0.05 1 248 . 60 ILE C C 177.529 0.05 1 249 . 61 GLN N N 115.282 0.05 1 250 . 61 GLN H H 9.181 0.02 1 251 . 61 GLN CA C 58.183 0.05 1 252 . 61 GLN CB C 28.208 0.05 1 253 . 61 GLN C C 179.373 0.05 1 254 . 62 THR N N 112.205 0.05 1 255 . 62 THR H H 6.852 0.02 1 256 . 62 THR CA C 65.818 0.05 1 257 . 62 THR CB C 68.185 0.05 1 258 . 62 THR C C 173.730 0.05 1 259 . 63 ALA N N 121.878 0.05 1 260 . 63 ALA H H 7.728 0.02 1 261 . 63 ALA CA C 53.755 0.05 1 262 . 63 ALA CB C 17.049 0.05 1 263 . 63 ALA C C 181.025 0.05 1 264 . 64 GLU N N 119.367 0.05 1 265 . 64 GLU H H 8.533 0.02 1 266 . 64 GLU CA C 58.626 0.05 1 267 . 64 GLU CB C 29.051 0.05 1 268 . 64 GLU C C 177.592 0.05 1 269 . 65 ALA N N 117.440 0.05 1 270 . 65 ALA H H 6.717 0.02 1 271 . 65 ALA CA C 52.940 0.05 1 272 . 65 ALA CB C 18.355 0.05 1 273 . 65 ALA C C 178.075 0.05 1 274 . 66 LEU N N 116.798 0.05 1 275 . 66 LEU H H 7.933 0.02 1 276 . 66 LEU CA C 56.496 0.05 1 277 . 66 LEU CB C 41.141 0.05 1 278 . 66 LEU C C 177.687 0.05 1 279 . 67 GLY N N 104.594 0.05 1 280 . 67 GLY H H 7.460 0.02 1 281 . 67 GLY CA C 45.881 0.05 1 282 . 67 GLY C C 173.407 0.05 1 283 . 68 VAL N N 112.302 0.05 1 284 . 68 VAL H H 7.151 0.02 1 285 . 68 VAL CA C 57.625 0.05 1 286 . 68 VAL CB C 32.141 0.05 1 287 . 68 VAL C C 173.502 0.05 1 288 . 70 TYR CA C 54.194 0.05 1 289 . 70 TYR CB C 40.980 0.05 1 290 . 70 TYR C C 174.896 0.05 1 291 . 71 GLU N N 119.463 0.05 1 292 . 71 GLU H H 7.939 0.02 1 293 . 71 GLU CA C 53.362 0.05 1 294 . 71 GLU CB C 33.116 0.05 1 295 . 72 GLN CA C 54.162 0.05 1 296 . 72 GLN CB C 29.517 0.05 1 297 . 72 GLN C C 176.744 0.05 1 298 . 73 TRP N N 123.864 0.05 1 299 . 73 TRP H H 9.351 0.02 1 300 . 73 TRP CA C 54.998 0.05 1 301 . 73 TRP CB C 29.371 0.05 1 302 . 73 TRP C C 176.540 0.05 1 303 . 74 LYS N N 129.002 0.05 1 304 . 74 LYS H H 8.809 0.02 1 305 . 74 LYS CA C 58.574 0.05 1 306 . 74 LYS CB C 30.691 0.05 1 307 . 74 LYS C C 179.324 0.05 1 308 . 75 ALA N N 119.367 0.05 1 309 . 75 ALA H H 8.777 0.02 1 310 . 75 ALA CA C 53.907 0.05 1 311 . 75 ALA CB C 18.373 0.05 1 312 . 75 ALA C C 176.687 0.05 1 313 . 76 LEU N N 109.090 0.05 1 314 . 76 LEU H H 6.934 0.02 1 315 . 76 LEU CA C 53.864 0.05 1 316 . 76 LEU CB C 41.645 0.05 1 317 . 76 LEU C C 176.659 0.05 1 318 . 77 ASN N N 117.588 0.05 1 319 . 77 ASN H H 7.582 0.02 1 320 . 77 ASN CA C 53.715 0.05 1 321 . 77 ASN CB C 37.490 0.05 1 322 . 77 ASN C C 175.398 0.05 1 323 . 78 GLU N N 119.340 0.05 1 324 . 78 GLU H H 5.719 0.02 1 325 . 78 GLU CA C 52.864 0.05 1 326 . 78 GLU CB C 27.288 0.05 1 327 . 78 GLU C C 174.202 0.05 1 328 . 79 ILE N N 124.786 0.05 1 329 . 79 ILE H H 8.335 0.02 1 330 . 79 ILE CA C 61.519 0.05 1 331 . 79 ILE CB C 38.725 0.05 1 332 . 79 ILE C C 174.938 0.05 1 333 . 80 ASP N N 128.038 0.05 1 334 . 80 ASP H H 7.913 0.02 1 335 . 80 ASP CA C 55.679 0.05 1 336 . 80 ASP CB C 37.393 0.05 1 337 . 80 ASP C C 180.909 0.05 1 338 . 81 ALA CA C 50.644 0.05 1 339 . 81 ALA C C 177.436 0.05 1 340 . 82 GLY N N 110.441 0.05 1 341 . 82 GLY H H 9.122 0.02 1 342 . 82 GLY CA C 45.778 0.05 1 343 . 82 GLY C C 178.357 0.05 1 344 . 83 VAL N N 120.886 0.05 1 345 . 83 VAL H H 8.352 0.02 1 346 . 83 VAL CA C 62.965 0.05 1 347 . 83 VAL CB C 31.355 0.05 1 348 . 83 VAL C C 174.700 0.05 1 349 . 84 CYS N N 116.156 0.05 1 350 . 84 CYS H H 7.678 0.02 1 351 . 84 CYS CA C 54.798 0.05 1 352 . 84 CYS CB C 40.832 0.05 1 353 . 84 CYS C C 174.066 0.05 1 354 . 85 GLU N N 121.294 0.05 1 355 . 85 GLU H H 9.315 0.02 1 356 . 85 GLU CA C 54.115 0.05 1 357 . 85 GLU CB C 32.223 0.05 1 358 . 85 GLU C C 174.755 0.05 1 359 . 86 GLU N N 122.150 0.05 1 360 . 86 GLU H H 8.534 0.02 1 361 . 86 GLU CA C 54.034 0.05 1 362 . 86 GLU CB C 29.479 0.05 1 363 . 86 GLU C C 176.823 0.05 1 364 . 87 MET CA C 54.104 0.05 1 365 . 87 MET C C 178.203 0.05 1 366 . 88 THR N N 120.304 0.05 1 367 . 88 THR H H 7.164 0.02 1 368 . 88 THR CA C 56.791 0.05 1 369 . 88 THR C C 178.708 0.05 1 370 . 91 GLU CA C 55.731 0.05 1 371 . 91 GLU CB C 29.783 0.05 1 372 . 91 GLU C C 179.377 0.05 1 373 . 92 ILE N N 121.888 0.05 1 374 . 92 ILE H H 8.399 0.02 1 375 . 92 ILE CA C 66.587 0.05 1 376 . 92 ILE CB C 29.228 0.05 1 377 . 92 ILE C C 177.544 0.05 1 378 . 93 GLN N N 118.107 0.05 1 379 . 93 GLN H H 7.864 0.02 1 380 . 93 GLN CA C 56.791 0.05 1 381 . 93 GLN C C 176.753 0.05 1 382 . 94 GLU CA C 61.438 0.05 1 383 . 94 GLU CB C 33.402 0.05 1 384 . 94 GLU C C 173.330 0.05 1 385 . 95 HIS N N 121.409 0.05 1 386 . 95 HIS H H 7.893 0.02 1 387 . 95 HIS CA C 58.726 0.05 1 388 . 95 HIS CB C 33.637 0.05 1 389 . 95 HIS C C 174.615 0.05 1 390 . 97 PRO CA C 63.560 0.05 1 391 . 97 PRO CB C 29.000 0.05 1 392 . 97 PRO C C 177.463 0.05 1 393 . 98 GLU N N 117.459 0.05 1 394 . 98 GLU H H 8.554 0.02 1 395 . 98 GLU CA C 57.816 0.05 1 396 . 98 GLU CB C 29.522 0.05 1 397 . 98 GLU C C 175.733 0.05 1 398 . 113 PRO CA C 61.914 0.05 1 399 . 113 PRO CB C 36.191 0.05 1 400 . 113 PRO C C 179.223 0.05 1 401 . 114 LYS N N 120.730 0.05 1 402 . 114 LYS H H 7.815 0.02 1 403 . 114 LYS CA C 59.254 0.05 1 404 . 114 LYS CB C 29.103 0.05 1 405 . 114 LYS C C 178.966 0.05 1 406 . 115 GLY N N 111.368 0.05 1 407 . 115 GLY H H 8.679 0.02 1 408 . 115 GLY CA C 48.324 0.05 1 409 . 115 GLY C C 176.754 0.05 1 410 . 116 GLU N N 121.678 0.05 1 411 . 116 GLU H H 8.362 0.02 1 412 . 116 GLU CA C 59.609 0.05 1 413 . 117 SER CA C 60.522 0.05 1 414 . 117 SER C C 179.564 0.05 1 415 . 118 TYR N N 120.780 0.05 1 416 . 118 TYR H H 7.970 0.02 1 417 . 118 TYR CA C 58.040 0.05 1 418 . 118 TYR CB C 28.945 0.05 1 419 . 118 TYR C C 178.979 0.05 1 420 . 119 GLU N N 118.107 0.05 1 421 . 119 GLU H H 7.361 0.02 1 422 . 119 GLU CA C 58.111 0.05 1 423 . 119 GLU C C 180.064 0.05 1 424 . 120 ASP N N 123.221 0.05 1 425 . 120 ASP H H 9.043 0.02 1 426 . 120 ASP CA C 56.739 0.05 1 427 . 120 ASP C C 179.373 0.05 1 428 . 121 LEU N N 125.231 0.05 1 429 . 121 LEU H H 7.977 0.02 1 430 . 121 LEU CA C 57.258 0.05 1 431 . 121 LEU CB C 40.813 0.05 1 432 . 121 LEU C C 177.536 0.05 1 433 . 122 VAL N N 119.367 0.05 1 434 . 122 VAL H H 8.640 0.02 1 435 . 122 VAL CA C 67.036 0.05 1 436 . 122 VAL CB C 31.193 0.05 1 437 . 122 VAL C C 179.350 0.05 1 438 . 123 GLN N N 116.156 0.05 1 439 . 123 GLN H H 7.266 0.02 1 440 . 123 GLN CA C 58.442 0.05 1 441 . 123 GLN CB C 27.517 0.05 1 442 . 123 GLN C C 179.522 0.05 1 443 . 124 ARG CA C 57.236 0.05 1 444 . 124 ARG CB C 29.075 0.05 1 445 . 124 ARG C C 176.941 0.05 1 446 . 125 LEU N N 116.435 0.05 1 447 . 125 LEU H H 7.930 0.02 1 448 . 125 LEU CA C 54.459 0.05 1 449 . 125 LEU CB C 41.638 0.05 1 450 . 125 LEU C C 177.943 0.05 1 451 . 126 GLU N N 122.579 0.05 1 452 . 126 GLU H H 7.433 0.02 1 453 . 126 GLU CA C 61.676 0.05 1 454 . 126 GLU CB C 26.542 0.05 1 455 . 126 GLU C C 175.039 0.05 1 456 . 127 PRO CA C 65.407 0.05 1 457 . 127 PRO CB C 30.788 0.05 1 458 . 127 PRO C C 179.808 0.05 1 459 . 128 VAL N N 117.440 0.05 1 460 . 128 VAL H H 7.010 0.02 1 461 . 128 VAL CA C 64.328 0.05 1 462 . 128 VAL CB C 30.192 0.05 1 463 . 128 VAL C C 177.553 0.05 1 464 . 129 ILE N N 120.780 0.05 1 465 . 129 ILE H H 7.811 0.02 1 466 . 129 ILE CA C 64.948 0.05 1 467 . 129 ILE CB C 36.115 0.05 1 468 . 129 ILE C C 177.592 0.05 1 469 . 130 MET N N 115.513 0.05 1 470 . 130 MET H H 7.807 0.02 1 471 . 130 MET CA C 58.184 0.05 1 472 . 130 MET CB C 31.660 0.05 1 473 . 130 MET C C 179.018 0.05 1 474 . 131 GLU CA C 58.124 0.05 1 475 . 131 GLU CB C 29.320 0.05 1 476 . 132 LEU N N 123.221 0.05 1 477 . 132 LEU H H 9.041 0.02 1 478 . 132 LEU CA C 58.020 0.05 1 479 . 132 LEU CB C 41.301 0.05 1 480 . 132 LEU C C 179.275 0.05 1 481 . 133 GLU N N 114.229 0.05 1 482 . 133 GLU H H 7.848 0.02 1 483 . 133 GLU CA C 58.194 0.05 1 484 . 133 GLU CB C 28.980 0.05 1 485 . 133 GLU C C 177.322 0.05 1 486 . 134 ARG N N 116.156 0.05 1 487 . 134 ARG H H 7.506 0.02 1 488 . 134 ARG CA C 55.621 0.05 1 489 . 134 ARG CB C 30.127 0.05 1 490 . 134 ARG C C 176.574 0.05 1 491 . 135 GLN N N 118.083 0.05 1 492 . 135 GLN H H 7.409 0.02 1 493 . 135 GLN CA C 53.366 0.05 1 494 . 135 GLN CB C 28.914 0.05 1 495 . 135 GLN C C 174.710 0.05 1 496 . 136 GLU N N 119.367 0.05 1 497 . 136 GLU H H 8.298 0.02 1 498 . 136 GLU CA C 57.088 0.05 1 499 . 136 GLU CB C 32.181 0.05 1 500 . 136 GLU C C 175.374 0.05 1 501 . 137 ASN N N 116.156 0.05 1 502 . 137 ASN H H 8.048 0.02 1 503 . 137 ASN CA C 52.840 0.05 1 504 . 137 ASN CB C 40.733 0.05 1 505 . 137 ASN C C 174.430 0.05 1 506 . 138 VAL N N 122.258 0.05 1 507 . 138 VAL H H 7.743 0.02 1 508 . 138 VAL CA C 59.287 0.05 1 509 . 138 VAL CB C 34.857 0.05 1 510 . 138 VAL C C 172.075 0.05 1 511 . 139 LEU N N 129.644 0.05 1 512 . 139 LEU H H 9.061 0.02 1 513 . 139 LEU CA C 52.702 0.05 1 514 . 139 LEU CB C 43.262 0.05 1 515 . 139 LEU C C 172.921 0.05 1 516 . 140 VAL N N 127.711 0.05 1 517 . 140 VAL H H 9.233 0.02 1 518 . 140 VAL CA C 60.700 0.05 1 519 . 140 VAL CB C 31.681 0.05 1 520 . 140 VAL CG2 C 26.014 0.05 2 521 . 140 VAL CG1 C 16.679 0.05 2 522 . 140 VAL C C 174.245 0.05 1 523 . 141 ILE N N 123.299 0.05 1 524 . 141 ILE H H 7.760 0.02 1 525 . 141 ILE CA C 62.981 0.05 1 526 . 141 ILE C C 175.736 0.05 1 527 . 142 CYS N N 130.287 0.05 1 528 . 142 CYS H H 7.910 0.02 1 529 . 142 CYS CA C 53.267 0.05 1 530 . 142 CYS C C 182.725 0.05 1 531 . 143 HIS CA C 57.668 0.05 1 532 . 143 HIS CB C 30.943 0.05 1 533 . 143 HIS C C 173.349 0.05 1 534 . 144 GLN N N 118.409 0.05 1 535 . 144 GLN H H 6.944 0.02 1 536 . 144 GLN CA C 58.687 0.05 1 537 . 144 GLN CB C 30.473 0.05 1 538 . 144 GLN C C 176.751 0.05 1 539 . 145 ALA N N 115.047 0.05 1 540 . 145 ALA H H 8.348 0.02 1 541 . 145 ALA CA C 58.551 0.05 1 542 . 145 ALA CB C 25.947 0.05 1 543 . 145 ALA C C 175.104 0.05 1 544 . 146 VAL N N 118.403 0.05 1 545 . 146 VAL H H 7.555 0.02 1 546 . 146 VAL CA C 56.938 0.05 1 547 . 146 VAL CB C 33.573 0.05 1 548 . 146 VAL C C 176.566 0.05 1 549 . 147 MET N N 115.820 0.05 1 550 . 147 MET H H 7.355 0.02 1 551 . 147 MET CA C 58.072 0.05 1 552 . 147 MET CB C 28.961 0.05 1 553 . 147 MET C C 178.177 0.05 1 554 . 148 ARG N N 118.261 0.05 1 555 . 148 ARG H H 7.304 0.02 1 556 . 148 ARG CA C 61.262 0.05 1 557 . 148 ARG C C 176.733 0.05 1 558 . 149 CYS N N 125.378 0.05 1 559 . 149 CYS H H 7.930 0.02 1 560 . 149 CYS CA C 57.191 0.05 1 561 . 149 CYS CB C 30.123 0.05 1 562 . 150 LEU CA C 54.799 0.05 1 563 . 150 LEU CB C 41.921 0.05 1 564 . 150 LEU CG C 24.196 0.05 1 565 . 150 LEU CD1 C 22.021 0.05 2 566 . 150 LEU C C 179.587 0.05 1 567 . 151 LEU N N 125.757 0.05 1 568 . 151 LEU H H 7.806 0.02 1 569 . 151 LEU CA C 55.505 0.05 1 570 . 151 LEU CB C 41.571 0.05 1 571 . 151 LEU C C 180.849 0.05 1 572 . 152 ALA CA C 51.717 0.05 1 573 . 152 ALA CB C 18.384 0.05 1 574 . 152 ALA C C 177.538 0.05 1 575 . 153 TYR N N 121.475 0.05 1 576 . 153 TYR H H 8.146 0.02 1 577 . 153 TYR CA C 54.627 0.05 1 578 . 153 TYR CB C 41.276 0.05 1 579 . 153 TYR C C 177.193 0.05 1 580 . 154 PHE CA C 61.402 0.05 1 581 . 154 PHE CB C 38.754 0.05 1 582 . 154 PHE C C 173.329 0.05 1 583 . 155 LEU N N 131.027 0.05 1 584 . 155 LEU H H 9.083 0.02 1 585 . 155 LEU CA C 53.694 0.05 1 586 . 155 LEU CB C 40.752 0.05 1 587 . 155 LEU C C 175.650 0.05 1 588 . 156 ASP N N 119.673 0.05 1 589 . 156 ASP H H 7.433 0.02 1 590 . 156 ASP CA C 54.875 0.05 1 591 . 156 ASP CB C 38.526 0.05 1 592 . 156 ASP C C 175.643 0.05 1 593 . 157 LYS N N 115.513 0.05 1 594 . 157 LYS H H 8.277 0.02 1 595 . 157 LYS CA C 52.744 0.05 1 596 . 157 LYS CB C 31.771 0.05 1 597 . 157 LYS C C 176.570 0.05 1 598 . 158 SER N N 118.083 0.05 1 599 . 158 SER H H 8.945 0.02 1 600 . 158 SER CA C 57.286 0.05 1 601 . 158 SER CB C 64.544 0.05 1 602 . 158 SER C C 175.600 0.05 1 603 . 159 SER N N 117.440 0.05 1 604 . 159 SER H H 8.649 0.02 1 605 . 159 SER CA C 60.889 0.05 1 606 . 159 SER CB C 64.450 0.05 1 607 . 159 SER C C 175.628 0.05 1 608 . 160 ASP CA C 55.498 0.05 1 609 . 160 ASP C C 175.164 0.05 1 610 . 161 GLU N N 127.075 0.05 1 611 . 161 GLU H H 7.949 0.02 1 612 . 161 GLU CA C 57.681 0.05 1 613 . 161 GLU C C 181.117 0.05 1 614 . 163 PRO CA C 64.556 0.05 1 615 . 163 PRO CB C 29.133 0.05 1 616 . 163 PRO C C 173.776 0.05 1 617 . 164 TYR N N 113.247 0.05 1 618 . 164 TYR H H 7.633 0.02 1 619 . 164 TYR CA C 56.863 0.05 1 620 . 164 TYR CB C 38.953 0.05 1 621 . 164 TYR C C 175.909 0.05 1 622 . 165 LEU N N 119.975 0.05 1 623 . 165 LEU H H 7.105 0.02 1 624 . 165 LEU CA C 55.478 0.05 1 625 . 165 LEU CB C 40.385 0.05 1 626 . 165 LEU C C 177.180 0.05 1 627 . 166 LYS N N 123.221 0.05 1 628 . 166 LYS H H 8.653 0.02 1 629 . 166 LYS CA C 56.740 0.05 1 630 . 166 LYS CB C 31.398 0.05 1 631 . 166 LYS C C 176.033 0.05 1 632 . 167 CYS N N 123.525 0.05 1 633 . 167 CYS H H 9.089 0.02 1 634 . 167 CYS CA C 55.140 0.05 1 635 . 167 CYS CB C 31.418 0.05 1 636 . 170 HIS CA C 54.186 0.05 1 637 . 170 HIS C C 172.158 0.05 1 638 . 171 THR N N 113.336 0.05 1 639 . 171 THR H H 7.338 0.02 1 640 . 171 THR CA C 61.129 0.05 1 641 . 171 THR CB C 71.443 0.05 1 642 . 171 THR C C 173.657 0.05 1 643 . 172 VAL N N 128.488 0.05 1 644 . 172 VAL H H 9.290 0.02 1 645 . 172 VAL CA C 60.256 0.05 1 646 . 172 VAL CB C 32.834 0.05 1 647 . 172 VAL C C 173.545 0.05 1 648 . 173 LEU CA C 52.437 0.05 1 649 . 173 LEU CB C 41.731 0.05 1 650 . 173 LEU C C 174.661 0.05 1 651 . 174 LYS N N 124.711 0.05 1 652 . 174 LYS H H 9.120 0.02 1 653 . 174 LYS CA C 54.230 0.05 1 654 . 174 LYS CB C 34.431 0.05 1 655 . 174 LYS C C 174.947 0.05 1 656 . 175 LEU N N 131.824 0.05 1 657 . 175 LEU H H 9.561 0.02 1 658 . 175 LEU CA C 53.174 0.05 1 659 . 175 LEU CB C 42.131 0.05 1 660 . 175 LEU C C 176.087 0.05 1 661 . 176 THR N N 116.474 0.05 1 662 . 176 THR H H 8.492 0.02 1 663 . 176 THR CA C 58.114 0.05 1 664 . 176 THR CB C 70.270 0.05 1 665 . 176 THR C C 176.088 0.05 1 666 . 177 PRO CA C 63.194 0.05 1 667 . 177 PRO CB C 31.446 0.05 1 668 . 177 PRO C C 176.071 0.05 1 669 . 178 VAL N N 118.725 0.05 1 670 . 178 VAL H H 8.189 0.02 1 671 . 178 VAL CA C 59.381 0.05 1 672 . 178 VAL CB C 33.940 0.05 1 673 . 178 VAL C C 176.063 0.05 1 674 . 179 ALA N N 122.911 0.05 1 675 . 179 ALA H H 8.301 0.02 1 676 . 179 ALA CA C 54.772 0.05 1 677 . 179 ALA CB C 18.269 0.05 1 678 . 179 ALA C C 178.213 0.05 1 679 . 180 TYR N N 112.918 0.05 1 680 . 180 TYR H H 7.442 0.02 1 681 . 180 TYR CA C 56.473 0.05 1 682 . 180 TYR CB C 36.517 0.05 1 683 . 180 TYR C C 175.022 0.05 1 684 . 181 GLY N N 109.614 0.05 1 685 . 181 GLY H H 7.549 0.02 1 686 . 181 GLY CA C 45.321 0.05 1 687 . 181 GLY C C 172.219 0.05 1 688 . 182 CYS N N 121.405 0.05 1 689 . 182 CYS H H 8.437 0.02 1 690 . 182 CYS CA C 58.387 0.05 1 691 . 182 CYS CB C 29.171 0.05 1 692 . 182 CYS C C 173.079 0.05 1 693 . 183 ARG N N 127.075 0.05 1 694 . 183 ARG H H 8.487 0.02 1 695 . 183 ARG CA C 54.998 0.05 1 696 . 183 ARG CB C 30.540 0.05 1 697 . 183 ARG C C 175.251 0.05 1 698 . 184 VAL N N 122.518 0.05 1 699 . 184 VAL H H 8.509 0.02 1 700 . 184 VAL CA C 60.264 0.05 1 701 . 184 VAL CB C 33.740 0.05 1 702 . 184 VAL C C 174.702 0.05 1 703 . 185 GLU N N 127.992 0.05 1 704 . 185 GLU H H 8.661 0.02 1 705 . 185 GLU CA C 54.182 0.05 1 706 . 185 GLU CB C 32.467 0.05 1 707 . 185 GLU CG C 35.685 0.05 1 708 . 185 GLU C C 174.277 0.05 1 709 . 186 SER N N 118.725 0.05 1 710 . 186 SER H H 8.665 0.02 1 711 . 186 SER CA C 56.717 0.05 1 712 . 186 SER CB C 63.185 0.05 1 713 . 186 SER C C 174.214 0.05 1 714 . 187 ILE N N 128.808 0.05 1 715 . 187 ILE H H 9.392 0.02 1 716 . 187 ILE CA C 60.690 0.05 1 717 . 187 ILE CB C 37.960 0.05 1 718 . 187 ILE C C 174.538 0.05 1 719 . 188 TYR N N 128.770 0.05 1 720 . 188 TYR H H 8.899 0.02 1 721 . 188 TYR CA C 56.279 0.05 1 722 . 188 TYR CB C 39.002 0.05 1 723 . 189 LEU CA C 51.849 0.05 1 724 . 189 LEU C C 176.426 0.05 1 725 . 190 ASN N N 127.685 0.05 1 726 . 190 ASN H H 7.753 0.02 1 727 . 190 ASN CA C 56.056 0.05 1 728 . 190 ASN C C 177.053 0.05 1 729 . 191 VAL N N 115.251 0.05 1 730 . 191 VAL H H 7.470 0.02 1 731 . 191 VAL CA C 62.834 0.05 1 732 . 191 VAL C C 176.764 0.05 1 733 . 192 GLU N N 120.973 0.05 1 734 . 192 GLU H H 8.432 0.02 1 735 . 192 GLU CA C 56.066 0.05 1 736 . 192 GLU CG C 35.385 0.05 1 737 . 192 GLU C C 176.123 0.05 1 738 . 193 ALA N N 124.506 0.05 1 739 . 193 ALA H H 8.450 0.02 1 740 . 193 ALA CA C 52.326 0.05 1 741 . 193 ALA CB C 27.821 0.05 1 742 . 193 ALA C C 176.876 0.05 1 743 . 194 VAL N N 119.492 0.05 1 744 . 194 VAL H H 8.394 0.02 1 745 . 194 VAL CA C 55.940 0.05 1 746 . 194 VAL CB C 32.565 0.05 1 747 . 194 VAL C C 176.671 0.05 1 748 . 195 ASN N N 127.396 0.05 1 749 . 195 ASN H H 9.666 0.02 1 750 . 195 ASN CA C 59.455 0.05 1 751 . 195 ASN C C 176.460 0.05 1 752 . 196 THR N N 117.963 0.05 1 753 . 196 THR H H 7.415 0.02 1 754 . 196 THR CA C 58.559 0.05 1 755 . 197 HIS CA C 55.749 0.05 1 756 . 198 ARG N N 117.963 0.05 1 757 . 198 ARG H H 7.274 0.02 1 758 . 198 ARG CA C 57.041 0.05 1 759 . 198 ARG CB C 30.597 0.05 1 760 . 198 ARG C C 177.803 0.05 1 761 . 199 ASP N N 121.157 0.05 1 762 . 199 ASP H H 7.749 0.02 1 763 . 199 ASP CA C 60.641 0.05 1 764 . 199 ASP CB C 40.656 0.05 1 765 . 199 ASP C C 173.712 0.05 1 766 . 200 LYS N N 114.854 0.05 1 767 . 200 LYS H H 7.488 0.02 1 768 . 200 LYS CA C 55.558 0.05 1 769 . 200 LYS CB C 39.997 0.05 1 770 . 200 LYS C C 178.264 0.05 1 771 . 201 PRO CA C 62.718 0.05 1 772 . 201 PRO CG C 26.244 0.05 1 773 . 202 GLU N N 120.652 0.05 1 774 . 202 GLU H H 8.541 0.02 1 775 . 202 GLU CA C 56.099 0.05 1 776 . 202 GLU CB C 29.592 0.05 1 777 . 202 GLU CG C 35.424 0.05 1 778 . 202 GLU C C 176.199 0.05 1 779 . 203 ASN N N 119.429 0.05 1 780 . 203 ASN H H 8.382 0.02 1 781 . 203 ASN CA C 52.739 0.05 1 782 . 203 ASN CB C 35.197 0.05 1 783 . 203 ASN C C 174.913 0.05 1 784 . 204 VAL N N 119.427 0.05 1 785 . 204 VAL H H 7.966 0.02 1 786 . 204 VAL CA C 61.658 0.05 1 787 . 204 VAL CB C 31.903 0.05 1 788 . 204 VAL CG1 C 19.966 0.05 2 789 . 204 VAL C C 175.559 0.05 1 790 . 205 ASP N N 123.767 0.05 1 791 . 205 ASP H H 8.331 0.02 1 792 . 205 ASP CA C 53.801 0.05 1 793 . 205 ASP CB C 40.435 0.05 1 794 . 205 ASP C C 176.368 0.05 1 795 . 206 ILE N N 120.652 0.05 1 796 . 206 ILE H H 8.031 0.02 1 797 . 206 ILE CA C 60.950 0.05 1 798 . 206 ILE CB C 37.791 0.05 1 799 . 206 ILE CG1 C 26.072 0.05 2 800 . 206 ILE CD1 C 12.045 0.05 1 801 . 206 ILE CG2 C 16.713 0.05 2 802 . 206 ILE C C 176.591 0.05 1 803 . 207 THR N N 117.440 0.05 1 804 . 207 THR H H 8.205 0.02 1 805 . 207 THR CA C 62.031 0.05 1 806 . 207 THR CB C 68.966 0.05 1 807 . 207 THR CG2 C 20.773 0.05 1 808 . 207 THR C C 174.611 0.05 1 809 . 208 ARG N N 123.314 0.05 1 810 . 208 ARG H H 8.161 0.02 1 811 . 208 ARG CA C 55.657 0.05 1 812 . 208 ARG CB C 29.862 0.05 1 813 . 208 ARG CG C 26.039 0.05 1 814 . 208 ARG CD C 42.544 0.05 1 815 . 208 ARG C C 176.283 0.05 1 816 . 209 GLU N N 121.319 0.05 1 817 . 209 GLU H H 8.389 0.02 1 818 . 209 GLU CA C 56.326 0.05 1 819 . 209 GLU CB C 29.382 0.05 1 820 . 209 GLU CG C 35.393 0.05 1 821 . 209 GLU C C 176.419 0.05 1 822 . 210 ALA N N 124.017 0.05 1 823 . 210 ALA H H 8.241 0.02 1 824 . 210 ALA CA C 52.386 0.05 1 825 . 210 ALA CB C 18.461 0.05 1 826 . 210 ALA C C 177.836 0.05 1 827 . 211 GLU N N 119.974 0.05 1 828 . 211 GLU H H 8.272 0.02 1 829 . 211 GLU CA C 56.397 0.05 1 830 . 211 GLU CB C 29.464 0.05 1 831 . 211 GLU CG C 35.569 0.05 1 832 . 211 GLU C C 176.544 0.05 1 833 . 212 GLU N N 121.687 0.05 1 834 . 212 GLU H H 8.275 0.02 1 835 . 212 GLU CA C 56.132 0.05 1 836 . 212 GLU CB C 29.354 0.05 1 837 . 212 GLU C C 176.136 0.05 1 838 . 213 ALA N N 124.942 0.05 1 839 . 213 ALA H H 8.196 0.02 1 840 . 213 ALA CA C 51.846 0.05 1 841 . 213 ALA CB C 19.625 0.05 1 842 . 213 ALA C C 177.398 0.05 1 843 . 214 LEU N N 121.941 0.05 1 844 . 214 LEU H H 8.192 0.02 1 845 . 214 LEU CA C 54.666 0.05 1 846 . 214 LEU CB C 41.256 0.05 1 847 . 214 LEU CG C 23.861 0.05 1 848 . 214 LEU CD1 C 22.625 0.05 2 849 . 214 LEU C C 177.320 0.05 1 850 . 215 ASP N N 120.287 0.05 1 851 . 215 ASP H H 8.247 0.02 1 852 . 215 ASP CA C 53.860 0.05 1 853 . 215 ASP CB C 40.430 0.05 1 854 . 215 ASP C C 176.455 0.05 1 855 . 216 THR N N 113.789 0.05 1 856 . 216 THR H H 7.925 0.02 1 857 . 216 THR CA C 61.402 0.05 1 858 . 216 THR CB C 69.128 0.05 1 859 . 216 THR CG2 C 20.794 0.05 1 860 . 216 THR C C 174.305 0.05 1 861 . 217 VAL N N 123.995 0.05 1 862 . 217 VAL H H 8.054 0.02 1 863 . 217 VAL CA C 59.609 0.05 1 864 . 217 VAL CB C 31.583 0.05 1 865 . 217 VAL C C 174.320 0.05 1 866 . 218 PRO CA C 62.644 0.05 1 867 . 218 PRO CB C 31.297 0.05 1 868 . 218 PRO CG C 26.362 0.05 1 869 . 218 PRO CD C 50.255 0.05 1 870 . 219 ALA N N 123.887 0.05 1 871 . 219 ALA H H 8.227 0.02 1 872 . 219 ALA CA C 51.877 0.05 1 873 . 219 ALA CB C 18.540 0.05 1 874 . 219 ALA C C 177.069 0.05 1 875 . 220 HIS N N 118.030 0.05 1 876 . 220 HIS H H 7.998 0.02 1 877 . 220 HIS CA C 55.259 0.05 1 878 . 220 HIS CB C 29.923 0.05 1 879 . 220 HIS C C 173.586 0.05 1 880 . 221 TYR N N 126.433 0.05 1 881 . 221 TYR H H 7.690 0.02 1 882 . 221 TYR CA C 58.926 0.05 1 883 . 221 TYR CB C 38.557 0.05 1 884 . 221 TYR C C 180.437 0.05 1 stop_ save_