data_5458 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N assignments of the ribosome recycling factor from Thermus thermophillus ; _BMRB_accession_number 5458 _BMRB_flat_file_name bmr5458.str _Entry_type original _Submission_date 2002-07-09 _Accession_date 2002-07-09 _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 Blake Brain K. . 2 Ito Koichi . . 3 Nakamura Yoshikazu . . 4 Alam Steven L. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 178 "13C chemical shifts" 541 "15N chemical shifts" 178 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-12-27 original author . stop_ _Original_release_date 2002-12-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 13C, and 15N assignments of the ribosome recycling factor from Thermus thermophillus ; _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 Blake Brain K. . 2 Ito Koichi . . 3 Nakamura Yoshikazu . . 4 Alam Steven L. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 81 _Page_last 82 _Year 2002 _Details . loop_ _Keyword Ribosome 'recycling RRF' translation termination stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Ito K, Fujiwara T, Toyoda T, Nakamura Y. Elongation Factor G Paricipates in Ribosome Disassembly by Interacting with Ribosome Recycling Factor at Their tRNA-Mimicry Domains. Mol Cell. 2002 Jun;9(6):1263-72 ; _Citation_title 'Elongation factor G participates in ribosome disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 12086623 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ito Koichi . . 2 Fujiwara Toshinobu . . 3 Toyoda Tomohiko . . 4 Nakamura Yoshikazu . . stop_ _Journal_abbreviation 'Mol. Cell' _Journal_name_full 'Molecular cell' _Journal_volume 9 _Journal_issue 6 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 1263 _Page_last 1272 _Year 2002 _Details ; Elongation factor G (EF-G) is a G protein with motor function that drives two target molecules, a tRNA in the translating ribosome and the ribosome recycling factor (RRF) in the post-termination complex. How G protein motor action is transmitted to RRF is unknown. Thermus thermophilus RRF is nonfunctional in Escherichia coli. It became functional upon introducing a plasmid expressing E. coli EF-G with surface changes in its tRNA-mimic domain or by replacing the E. coli EF-G tRNA-mimic domain by the Thermus domain. Thermus RRF could also be activated by introducing surface substitutions in its anticodon arm-mimic region. These gain-of-function phenotypes depend on the combination of heterologous EF-G and RRF alleles. These mutational studies suggest that EF-G motor action is transmitted to RRF by specific surface contacts between the domains that mimic the anticodon arm. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Fujiwara T, Ito K, Nakamura Y. Functional mapping of ribosome-contact sites in the ribosome recycling factor: a structural view from a tRNA mimic. RNA. 2001 Jan;7(1):64-70 ; _Citation_title 'Functional mapping of ribosome-contact sites in the ribosome recycling factor: a structural view from a tRNA mimic.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11214182 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fujiwara T. . . 2 Ito K. . . 3 Nakamura Y. . . stop_ _Journal_abbreviation RNA _Journal_name_full 'RNA (New York, N.Y.)' _Journal_volume 7 _Journal_issue 1 _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 64 _Page_last 70 _Year 2001 _Details ; Ribosome recycling factor (RRF) is required for disassembly of the posttermination complex of the ribosome after release of polypeptides. The crystal structure of RRF resembles a tRNA shape, with an architecturally different flexibility compared with tRNA, but its structure-and-function relationships are unknown. We here found that an RRF variant defective in ribosome binding regains the binding capacity through 20 independent secondary changes occurring in three topologically distinct regions of RRF. Because two of these regions are equivalent to the tip of the anticodon stem and the upper surface of the acceptor stem of tRNA, RRF may interact with the ribosome in a way similar to tRNA, spanning 30S and 50S subunits, to exert its action for splitting the ribosome. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Toyoda T, Tin OF, Ito K, Fujiwara T, Kumasaka T, Yamamoto M, Garber MB, Nakamura Y. Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch. RNA. 2000 Oct;6(10):1432-44 ; _Citation_title 'Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11073219 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Toyoda T. . . 2 Tin O.F. F. . 3 Ito K. . . 4 Fujiwara T. . . 5 Kumasaka T. . . 6 Yamamoto M. . . 7 Garber M.B. B. . 8 Nakamura Y. . . stop_ _Journal_abbreviation RNA _Journal_name_full 'RNA (New York, N.Y.)' _Journal_volume 6 _Journal_issue 10 _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 1432 _Page_last 1444 _Year 2000 _Details ; Ribosome recycling factor (RRF), in concert with elongation factor EF-G, is required for disassembly of the posttermination complex of the ribosome after release of polypeptides. The crystal structure of Thermus thermophilus RRF was determined at 2.6 A resolution. It is a tRNA-like L-shaped molecule consisting of two domains: a long three-helix bundle (domain 1) and a three-layer beta/alpha/beta sandwich (domain 2). Although the individual domain structures are similar to those of Thermotoga maritima RRF (Selmer et al., Science, 1999, 286:2349-2352), the interdomain angle differs by 33 degrees in two molecules, suggesting that the hinge between two domains is potentially flexible and responsive to different conditions of crystal packing. The hinge connects hydrophobic junctions of domains 1 and 2. The structure-based genetic analysis revealed the strong correlation between the hinge flexibility and the in vivo function of RRF. First, altering the hinge flexibility by making alanine or serine substitutions for large-size residues conserved at the hinge loop and nearby in domain 1 frequently gave rise to gain of function except a Pro residue conserved at the hinge loop. Second, the hinge defect resulting from a too relaxed hinge structure can be compensated for by secondary alterations in domain 1 that seem to increase the hydrophobic contact between domain 1 and the hinge loop. These results show that the hinge flexibility is vital for the function of RRF and that the steric interaction between the hinge loop and domains 1 and 2 restricts the interdomain angle and/or the hinge flexibility. These results indicate that RRF possesses an architectural difference from tRNA regardless of a resemblance to tRNA shape: RRF has a "gooseneck" elbow, whereas the tRNA elbow is rigid, and the direction of flex of RRF and tRNA is at a nearly right angle to each other. Moreover, surface electrostatic potentials of the two RRF proteins are dissimilar and do not mimic the surface potential of tRNA or EF-G. These properties will add a new insight into RRF, suggesting that RRF is more than a simple tRNA mimic. ; save_ ################################## # Molecular system description # ################################## save_system_RRF _Saveframe_category molecular_system _Mol_system_name 'Ribosome Recycling Factor' _Abbreviation_common RRF _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RRF $RRF stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'dissociates protein translational posttermination complex' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_RRF _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ribosome recycling factor' _Abbreviation_common RRF _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 185 _Mol_residue_sequence ; MTLKELYAETRSHMQKSLEV LEHNLAGLRTGRANPALLLH LKVEYYGAHVPLNQIATVTA PDPRTLVVQSWDQNALKAIE KAIRDSDLGLNPSNKGDALY INIPPLTEERRKDLVRAVRQ YAEEGRVAIRNIRREALDKL KKLAKELHLSEDETKRAEAE IQKITDEFIAKADQLAEKKE QEILG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 LEU 4 LYS 5 GLU 6 LEU 7 TYR 8 ALA 9 GLU 10 THR 11 ARG 12 SER 13 HIS 14 MET 15 GLN 16 LYS 17 SER 18 LEU 19 GLU 20 VAL 21 LEU 22 GLU 23 HIS 24 ASN 25 LEU 26 ALA 27 GLY 28 LEU 29 ARG 30 THR 31 GLY 32 ARG 33 ALA 34 ASN 35 PRO 36 ALA 37 LEU 38 LEU 39 LEU 40 HIS 41 LEU 42 LYS 43 VAL 44 GLU 45 TYR 46 TYR 47 GLY 48 ALA 49 HIS 50 VAL 51 PRO 52 LEU 53 ASN 54 GLN 55 ILE 56 ALA 57 THR 58 VAL 59 THR 60 ALA 61 PRO 62 ASP 63 PRO 64 ARG 65 THR 66 LEU 67 VAL 68 VAL 69 GLN 70 SER 71 TRP 72 ASP 73 GLN 74 ASN 75 ALA 76 LEU 77 LYS 78 ALA 79 ILE 80 GLU 81 LYS 82 ALA 83 ILE 84 ARG 85 ASP 86 SER 87 ASP 88 LEU 89 GLY 90 LEU 91 ASN 92 PRO 93 SER 94 ASN 95 LYS 96 GLY 97 ASP 98 ALA 99 LEU 100 TYR 101 ILE 102 ASN 103 ILE 104 PRO 105 PRO 106 LEU 107 THR 108 GLU 109 GLU 110 ARG 111 ARG 112 LYS 113 ASP 114 LEU 115 VAL 116 ARG 117 ALA 118 VAL 119 ARG 120 GLN 121 TYR 122 ALA 123 GLU 124 GLU 125 GLY 126 ARG 127 VAL 128 ALA 129 ILE 130 ARG 131 ASN 132 ILE 133 ARG 134 ARG 135 GLU 136 ALA 137 LEU 138 ASP 139 LYS 140 LEU 141 LYS 142 LYS 143 LEU 144 ALA 145 LYS 146 GLU 147 LEU 148 HIS 149 LEU 150 SER 151 GLU 152 ASP 153 GLU 154 THR 155 LYS 156 ARG 157 ALA 158 GLU 159 ALA 160 GLU 161 ILE 162 GLN 163 LYS 164 ILE 165 THR 166 ASP 167 GLU 168 PHE 169 ILE 170 ALA 171 LYS 172 ALA 173 ASP 174 GLN 175 LEU 176 ALA 177 GLU 178 LYS 179 LYS 180 GLU 181 GLN 182 GLU 183 ILE 184 LEU 185 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-11-16 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 1EH1 "Ribosome Recycling Factor From Thermus Thermophilus" 100.00 185 100.00 100.00 1.15e-128 PDB 2QBE "Crystal Structure Of The Bacterial Ribosome From Escherichia Coli In Complex With Ribosome Recycling Factor (Rrf). This File Co" 100.00 185 100.00 100.00 1.15e-128 PDB 2QBG "Crystal Structure Of The Bacterial Ribosome From Escherichia Coli In Complex With Ribosome Recycling Factor (Rrf). This File Co" 100.00 185 100.00 100.00 1.15e-128 PDB 2QBI "Crystal Structure Of The Bacterial Ribosome From Escherichia Coli In Complex With Gentamicin And Ribosome Recycling Factor (Rrf" 100.00 185 100.00 100.00 1.15e-128 PDB 2QBK "Crystal Structure Of The Bacterial Ribosome From Escherichia Coli In Complex With Gentamicin And Ribosome Recycling Factor (Rrf" 100.00 185 100.00 100.00 1.15e-128 PDB 2V46 "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" 100.00 185 100.00 100.00 1.15e-128 PDB 2V48 "Structure Of The Ribosome Recycling Factor Bound To The Thermus Thermophilus 70s Ribosome With Mrna, Asl-Phe And Trna-Fmet (Par" 100.00 185 100.00 100.00 1.15e-128 PDB 2Z4L "Crystal Structure Of The Bacterial Ribosome From Escherichia Coli In Complex With Paromomycin And Ribosome Recycling Factor (Rr" 100.00 185 100.00 100.00 1.15e-128 PDB 2Z4N "Crystal Structure Of The Bacterial Ribosome From Escherichia Coli In Complex With Paromomycin And Ribosome Recycling Factor (Rr" 100.00 185 100.00 100.00 1.15e-128 PDB 3J0D "Models For The T. Thermophilus Ribosome Recycling Factor Bound To The E. Coli Post-termination Complex" 100.00 185 100.00 100.00 1.15e-128 PDB 3J0E "Models For The T. Thermophilus Ribosome Recycling Factor And The E. Coli Elongation Factor G Bound To The E. Coli Post-terminat" 100.00 185 100.00 100.00 1.15e-128 DBJ BAA76865 "frr [Thermus thermophilus]" 100.00 185 100.00 100.00 1.15e-128 DBJ BAD70681 "ribosome recycling factor (Rrf) [Thermus thermophilus HB8]" 100.00 185 100.00 100.00 1.15e-128 GB AAS80854 "ribosome recycling factor (rrf) [Thermus thermophilus HB27]" 100.00 185 100.00 100.00 1.15e-128 GB AEG33280 "Ribosome-recycling factor [Thermus thermophilus SG0.5JP17-16]" 100.00 185 98.92 98.92 9.14e-127 GB AFH39081 "ribosome recycling factor [Thermus thermophilus JL-18]" 100.00 185 98.38 98.92 3.07e-126 GB EIA39843 "ribosome recycling factor [Thermus sp. RL]" 100.00 185 97.84 97.84 6.49e-125 REF WP_008630695 "ribosome recycling factor [Thermus sp. RL]" 100.00 185 97.84 97.84 6.49e-125 REF WP_011172951 "ribosome recycling factor [Thermus thermophilus]" 100.00 185 100.00 100.00 1.15e-128 REF WP_014510208 "ribosome recycling factor [Thermus thermophilus]" 100.00 185 98.92 98.92 9.14e-127 REF WP_014629718 "ribosome recycling factor [Thermus thermophilus]" 100.00 185 98.38 98.92 3.07e-126 REF YP_004481 "ribosome recycling factor [Thermus thermophilus HB27]" 100.00 185 100.00 100.00 1.15e-128 SP Q72KE0 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Thermus thermophilus HB27]" 100.00 185 100.00 100.00 1.15e-128 SP Q9WX76 "RecName: Full=Ribosome-recycling factor; Short=RRF; AltName: Full=Ribosome-releasing factor [Thermus thermophilus HB8]" 100.00 185 100.00 100.00 1.15e-128 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $RRF . 274 Bacteria . Thermus thermophillus frr 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 $RRF 'recombinant technology' . . . . . 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 $RRF 1.05 mM '[U-98% 13C; U-98% 15N]' NH4Cl 50 mM . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RRF 1.05 mM '[U-98% 15N]' NH4Cl 50 mM . D2O 10 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RRF 1.05 mM '[U-98% 2H; U-98% 13C; U-98% 15N]' NH4Cl 50 mM . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 1.1 loop_ _Task 'peak picking' 'peak assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 750 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITY _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_CBCA(CO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_(H)C(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH _Sample_label . save_ save_1H-15N_NOESY_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name (H)C(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_10 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 .1 na temperature 310 0.1 K 'ionic strength' 0.10 0.02 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 . . . 1.000000000 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 . loop_ _Experiment_label '1H-15N HSQC' HNCA HN(CO)CA HNCO HN(CA)CO CBCA(CO)NH HNCACB (H)C(CO)NH '1H-15N NOESY' '1H-15N TOCSY' stop_ _Sample_conditions_label $Ex-cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name RRF _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET CA C 55.5 0.05 1 2 . 1 MET CB C 34.7 0.05 1 3 . 2 THR N N 113.9 0.05 1 4 . 2 THR H H 8.38 0.01 1 5 . 2 THR CA C 60.1 0.05 1 6 . 2 THR CB C 71.8 0.05 1 7 . 2 THR C C 175.4 0.05 1 8 . 3 LEU N N 120.6 0.05 1 9 . 3 LEU H H 8.76 0.01 1 10 . 3 LEU CA C 58.3 0.05 1 11 . 3 LEU CB C 41.1 0.05 1 12 . 3 LEU C C 177.5 0.05 1 13 . 4 LYS N N 115.6 0.05 1 14 . 4 LYS H H 8.03 0.01 1 15 . 4 LYS CA C 60.4 0.05 1 16 . 4 LYS CB C 32.6 0.05 1 17 . 4 LYS C C 180.4 0.05 1 18 . 5 GLU N N 119.4 0.05 1 19 . 5 GLU H H 7.68 0.01 1 20 . 5 GLU CA C 59.3 0.05 1 21 . 5 GLU CB C 30.5 0.05 1 22 . 5 GLU C C 179.0 0.05 1 23 . 6 LEU N N 123.8 0.05 1 24 . 6 LEU H H 8.08 0.01 1 25 . 6 LEU CA C 58.5 0.05 1 26 . 6 LEU CB C 41.0 0.05 1 27 . 6 LEU C C 181.3 0.05 1 28 . 7 TYR N N 123.3 0.05 1 29 . 7 TYR H H 8.75 0.01 1 30 . 7 TYR CA C 59.0 0.05 1 31 . 7 TYR CB C 36.5 0.05 1 32 . 7 TYR C C 178.4 0.05 1 33 . 8 ALA N N 121.7 0.05 1 34 . 8 ALA H H 8.13 0.01 1 35 . 8 ALA CA C 55.7 0.05 1 36 . 8 ALA CB C 18.5 0.05 1 37 . 8 ALA C C 180.8 0.05 1 38 . 9 GLU N N 120.7 0.05 1 39 . 9 GLU H H 8.79 0.01 1 40 . 9 GLU CA C 59.7 0.05 1 41 . 9 GLU CB C 30.2 0.05 1 42 . 9 GLU C C 178.1 0.05 1 43 . 10 THR N N 117.3 0.05 1 44 . 10 THR H H 8.26 0.01 1 45 . 10 THR CA C 68.4 0.05 1 46 . 10 THR C C 175.9 0.05 1 47 . 11 ARG N N 119.9 0.05 1 48 . 11 ARG H H 8.33 0.01 1 49 . 11 ARG CA C 60.7 0.05 1 50 . 11 ARG CB C 30.7 0.05 1 51 . 11 ARG C C 177.6 0.05 1 52 . 12 SER N N 114.0 0.05 1 53 . 12 SER H H 8.32 0.01 1 54 . 12 SER CA C 62.1 0.05 1 55 . 12 SER CB C 63.0 0.05 1 56 . 12 SER C C 177.9 0.05 1 57 . 13 HIS N N 119.9 0.05 1 58 . 13 HIS H H 8.59 0.01 1 59 . 13 HIS CA C 58.7 0.05 1 60 . 13 HIS CB C 30.5 0.05 1 61 . 13 HIS C C 178.9 0.05 1 62 . 14 MET N N 121.2 0.05 1 63 . 14 MET H H 8.38 0.01 1 64 . 14 MET CA C 61.1 0.05 1 65 . 14 MET CB C 30.2 0.05 1 66 . 14 MET C C 177.3 0.05 1 67 . 15 GLN N N 121.0 0.05 1 68 . 15 GLN H H 8.63 0.01 1 69 . 15 GLN CA C 59.3 0.05 1 70 . 15 GLN CB C 27.9 0.05 1 71 . 15 GLN C C 178.5 0.05 1 72 . 16 LYS N N 119.3 0.05 1 73 . 16 LYS H H 7.87 0.01 1 74 . 16 LYS CA C 59.4 0.05 1 75 . 16 LYS CB C 31.8 0.05 1 76 . 16 LYS C C 179.5 0.05 1 77 . 17 SER N N 115.6 0.05 1 78 . 17 SER H H 7.72 0.01 1 79 . 17 SER CA C 63.2 0.05 1 80 . 17 SER C C 177.5 0.05 1 81 . 18 LEU N N 124.9 0.05 1 82 . 18 LEU H H 8.45 0.01 1 83 . 18 LEU CA C 57.7 0.05 1 84 . 18 LEU CB C 42.2 0.05 1 85 . 18 LEU C C 178.8 0.05 1 86 . 19 GLU N N 120.2 0.05 1 87 . 19 GLU H H 8.37 0.01 1 88 . 19 GLU CA C 59.8 0.05 1 89 . 19 GLU CB C 29.4 0.05 1 90 . 19 GLU C C 179.7 0.05 1 91 . 20 VAL N N 121.8 0.05 1 92 . 20 VAL H H 7.94 0.01 1 93 . 20 VAL CA C 67.0 0.05 1 94 . 20 VAL CB C 32.2 0.05 1 95 . 20 VAL C C 178.2 0.05 1 96 . 21 LEU N N 121.2 0.05 1 97 . 21 LEU H H 7.65 0.01 1 98 . 21 LEU CA C 58.8 0.05 1 99 . 21 LEU CB C 41.3 0.05 1 100 . 21 LEU C C 178.3 0.05 1 101 . 22 GLU N N 119.3 0.05 1 102 . 22 GLU H H 8.98 0.01 1 103 . 22 GLU CA C 60.9 0.05 1 104 . 22 GLU CB C 29.9 0.05 1 105 . 22 GLU C C 179.3 0.05 1 106 . 23 HIS N N 118.7 0.05 1 107 . 23 HIS H H 8.45 0.01 1 108 . 23 HIS CA C 59.3 0.05 1 109 . 23 HIS CB C 29.1 0.05 1 110 . 23 HIS C C 177.9 0.05 1 111 . 24 ASN N N 120.3 0.05 1 112 . 24 ASN H H 8.60 0.01 1 113 . 24 ASN CA C 55.6 0.05 1 114 . 24 ASN CB C 36.5 0.05 1 115 . 24 ASN C C 178.3 0.05 1 116 . 25 LEU N N 118.1 0.05 1 117 . 25 LEU H H 8.54 0.01 1 118 . 25 LEU CA C 57.6 0.05 1 119 . 25 LEU CB C 41.5 0.05 1 120 . 25 LEU C C 179.0 0.05 1 121 . 26 ALA N N 120.9 0.05 1 122 . 26 ALA H H 8.26 0.01 1 123 . 26 ALA CA C 54.6 0.05 1 124 . 26 ALA CB C 18.5 0.05 1 125 . 26 ALA C C 179.1 0.05 1 126 . 27 GLY N N 102.2 0.05 1 127 . 27 GLY H H 7.35 0.01 1 128 . 27 GLY CA C 45.5 0.05 1 129 . 27 GLY C C 174.2 0.05 1 130 . 28 LEU N N 119.6 0.05 1 131 . 28 LEU H H 7.19 0.01 1 132 . 28 LEU CA C 54.3 0.05 1 133 . 28 LEU CB C 42.4 0.05 1 134 . 28 LEU C C 176.6 0.05 1 135 . 29 ARG N N 125.3 0.05 1 136 . 29 ARG H H 8.65 0.01 1 137 . 29 ARG CA C 56.5 0.05 1 138 . 29 ARG CB C 30.2 0.05 1 139 . 29 ARG C C 175.3 0.05 1 140 . 30 THR N N 111.2 0.05 1 141 . 30 THR H H 8.15 0.01 1 142 . 30 THR CA C 61.4 0.05 1 143 . 30 THR CB C 70.0 0.05 1 144 . 30 THR C C 174.8 0.05 1 145 . 31 GLY N N 108.3 0.05 1 146 . 31 GLY H H 8.59 0.01 1 147 . 31 GLY CA C 46.1 0.05 1 148 . 31 GLY C C 173.4 0.05 1 149 . 32 ARG N N 118.2 0.05 1 150 . 32 ARG H H 7.77 0.01 1 151 . 32 ARG CA C 54.7 0.05 1 152 . 32 ARG CB C 32.7 0.05 1 153 . 32 ARG C C 175.8 0.05 1 154 . 33 ALA N N 125.3 0.05 1 155 . 33 ALA H H 8.76 0.01 1 156 . 33 ALA CA C 53.6 0.05 1 157 . 33 ALA CB C 19.4 0.05 1 158 . 33 ALA C C 176.1 0.05 1 159 . 34 ASN N N 120.8 0.05 1 160 . 34 ASN H H 7.86 0.01 1 161 . 34 ASN CA C 50.2 0.05 1 162 . 34 ASN CB C 40.6 0.05 1 163 . 34 ASN C C 173.9 0.05 1 164 . 35 PRO CA C 65.6 0.05 1 165 . 35 PRO CB C 32.9 0.05 1 166 . 35 PRO C C 176.7 0.05 1 167 . 36 ALA N N 117.2 0.05 1 168 . 36 ALA H H 8.11 0.01 1 169 . 36 ALA CA C 55.0 0.05 1 170 . 36 ALA CB C 18.7 0.05 1 171 . 36 ALA C C 178.4 0.05 1 172 . 37 LEU N N 116.7 0.05 1 173 . 37 LEU H H 7.83 0.01 1 174 . 37 LEU CA C 57.5 0.05 1 175 . 37 LEU CB C 43.6 0.05 1 176 . 37 LEU C C 177.3 0.05 1 177 . 38 LEU N N 111.5 0.05 1 178 . 38 LEU H H 7.34 0.01 1 179 . 38 LEU CA C 54.5 0.05 1 180 . 38 LEU CB C 44.6 0.05 1 181 . 38 LEU C C 177.8 0.05 1 182 . 39 LEU N N 115.7 0.05 1 183 . 39 LEU H H 7.38 0.01 1 184 . 39 LEU CA C 58.9 0.05 1 185 . 39 LEU CB C 42.9 0.05 1 186 . 39 LEU C C 176.5 0.05 1 187 . 40 HIS N N 112.7 0.05 1 188 . 40 HIS H H 8.14 0.01 1 189 . 40 HIS CA C 55.4 0.05 1 190 . 40 HIS CB C 30.2 0.05 1 191 . 40 HIS C C 175.7 0.05 1 192 . 41 LEU N N 123.3 0.05 1 193 . 41 LEU H H 7.40 0.01 1 194 . 41 LEU CA C 56.0 0.05 1 195 . 41 LEU CB C 43.3 0.05 1 196 . 41 LEU C C 176.1 0.05 1 197 . 42 LYS N N 123.4 0.05 1 198 . 42 LYS H H 8.43 0.01 1 199 . 42 LYS CA C 56.0 0.05 1 200 . 42 LYS CB C 33.5 0.05 1 201 . 42 LYS C C 175.9 0.05 1 202 . 43 VAL N N 123.7 0.05 1 203 . 43 VAL H H 9.27 0.01 1 204 . 43 VAL CA C 60.8 0.05 1 205 . 43 VAL CB C 35.0 0.05 1 206 . 43 VAL C C 174.8 0.05 1 207 . 44 GLU N N 127.6 0.05 1 208 . 44 GLU H H 8.55 0.01 1 209 . 44 GLU CA C 56.7 0.05 1 210 . 44 GLU CB C 29.5 0.05 1 211 . 44 GLU C C 174.9 0.05 1 212 . 45 TYR N N 130.2 0.05 1 213 . 45 TYR H H 9.10 0.01 1 214 . 45 TYR CA C 57.3 0.05 1 215 . 45 TYR CB C 41.5 0.05 1 216 . 45 TYR C C 174.1 0.05 1 217 . 46 TYR N N 125.0 0.05 1 218 . 46 TYR H H 8.72 0.01 1 219 . 46 TYR CA C 59.5 0.05 1 220 . 46 TYR CB C 36.1 0.05 1 221 . 46 TYR C C 176.3 0.05 1 222 . 47 GLY N N 104.5 0.05 1 223 . 47 GLY H H 8.50 0.01 1 224 . 47 GLY CA C 45.9 0.05 1 225 . 47 GLY C C 173.4 0.05 1 226 . 48 ALA N N 123.6 0.05 1 227 . 48 ALA H H 7.76 0.01 1 228 . 48 ALA CA C 50.6 0.05 1 229 . 48 ALA CB C 21.8 0.05 1 230 . 48 ALA C C 175.6 0.05 1 231 . 49 HIS N N 119.8 0.05 1 232 . 49 HIS H H 8.61 0.01 1 233 . 49 HIS CA C 56.2 0.05 1 234 . 49 HIS CB C 31.0 0.05 1 235 . 49 HIS C C 175.6 0.05 1 236 . 50 VAL N N 121.3 0.05 1 237 . 50 VAL H H 9.24 0.01 1 238 . 50 VAL CA C 58.1 0.05 1 239 . 50 VAL CB C 34.2 0.05 1 240 . 50 VAL C C 172.7 0.05 1 241 . 51 PRO CA C 62.7 0.05 1 242 . 51 PRO CB C 32.4 0.05 1 243 . 51 PRO C C 178.6 0.05 1 244 . 52 LEU N N 125.4 0.05 1 245 . 52 LEU H H 8.81 0.01 1 246 . 52 LEU CA C 60.1 0.05 1 247 . 52 LEU CB C 41.8 0.05 1 248 . 52 LEU C C 178.0 0.05 1 249 . 53 ASN N N 111.7 0.05 1 250 . 53 ASN H H 8.21 0.01 1 251 . 53 ASN CA C 55.0 0.05 1 252 . 53 ASN CB C 38.5 0.05 1 253 . 53 ASN C C 175.7 0.05 1 254 . 54 GLN N N 117.6 0.05 1 255 . 54 GLN H H 8.18 0.01 1 256 . 54 GLN CA C 57.5 0.05 1 257 . 54 GLN CB C 29.9 0.05 1 258 . 54 GLN C C 177.3 0.05 1 259 . 55 ILE N N 109.9 0.05 1 260 . 55 ILE H H 7.73 0.01 1 261 . 55 ILE CA C 60.5 0.05 1 262 . 55 ILE CB C 41.0 0.05 1 263 . 55 ILE C C 173.3 0.05 1 264 . 56 ALA N N 124.3 0.05 1 265 . 56 ALA H H 7.95 0.01 1 266 . 56 ALA CA C 51.5 0.05 1 267 . 56 ALA CB C 23.2 0.05 1 268 . 56 ALA C C 175.3 0.05 1 269 . 57 THR N N 110.8 0.05 1 270 . 57 THR H H 8.71 0.01 1 271 . 57 THR CA C 60.6 0.05 1 272 . 57 THR CB C 71.5 0.05 1 273 . 57 THR C C 173.9 0.05 1 274 . 58 VAL N N 123.6 0.05 1 275 . 58 VAL H H 8.66 0.01 1 276 . 58 VAL CA C 60.8 0.05 1 277 . 58 VAL CB C 34.5 0.05 1 278 . 58 VAL C C 174.8 0.05 1 279 . 59 THR N N 118.5 0.05 1 280 . 59 THR H H 9.01 0.01 1 281 . 59 THR CA C 60.0 0.05 1 282 . 59 THR CB C 72.6 0.05 1 283 . 59 THR C C 172.4 0.05 1 284 . 60 ALA N N 123.5 0.05 1 285 . 60 ALA H H 8.70 0.01 1 286 . 60 ALA CA C 48.6 0.05 1 287 . 60 ALA CB C 20.4 0.05 1 288 . 60 ALA C C 175.2 0.05 1 289 . 61 PRO CA C 64.5 0.05 1 290 . 61 PRO CB C 32.4 0.05 1 291 . 61 PRO C C 175.9 0.05 1 292 . 62 ASP N N 115.2 0.05 1 293 . 62 ASP H H 7.90 0.01 1 294 . 62 ASP CA C 52.8 0.05 1 295 . 62 ASP CB C 41.4 0.05 1 296 . 62 ASP C C 174.2 0.05 1 297 . 63 PRO CA C 65.1 0.05 1 298 . 63 PRO CB C 33.1 0.05 1 299 . 63 PRO C C 176.8 0.05 1 300 . 64 ARG N N 115.7 0.05 1 301 . 64 ARG H H 8.56 0.01 1 302 . 64 ARG CA C 55.1 0.05 1 303 . 64 ARG CB C 32.2 0.05 1 304 . 64 ARG C C 175.7 0.05 1 305 . 65 THR N N 118.3 0.05 1 306 . 65 THR H H 7.52 0.01 1 307 . 65 THR CA C 62.9 0.05 1 308 . 65 THR CB C 71.8 0.05 1 309 . 65 THR C C 172.9 0.05 1 310 . 66 LEU N N 121.9 0.05 1 311 . 66 LEU H H 8.84 0.01 1 312 . 66 LEU CA C 53.0 0.05 1 313 . 66 LEU CB C 46.7 0.05 1 314 . 66 LEU C C 175.2 0.05 1 315 . 67 VAL N N 121.5 0.05 1 316 . 67 VAL H H 9.03 0.01 1 317 . 67 VAL CA C 60.9 0.05 1 318 . 67 VAL CB C 34.0 0.05 1 319 . 67 VAL C C 175.7 0.05 1 320 . 68 VAL N N 127.5 0.05 1 321 . 68 VAL H H 9.07 0.01 1 322 . 68 VAL CA C 60.5 0.05 1 323 . 68 VAL CB C 33.9 0.05 1 324 . 68 VAL C C 174.7 0.05 1 325 . 69 GLN N N 125.0 0.05 1 326 . 69 GLN H H 8.69 0.01 1 327 . 69 GLN CA C 55.0 0.05 1 328 . 69 GLN CB C 33.4 0.05 1 329 . 69 GLN C C 174.2 0.05 1 330 . 70 SER N N 114.6 0.05 1 331 . 70 SER H H 8.36 0.01 1 332 . 70 SER CA C 57.5 0.05 1 333 . 70 SER CB C 64.8 0.05 1 334 . 70 SER C C 173.8 0.05 1 335 . 71 TRP N N 123.7 0.05 1 336 . 71 TRP H H 7.68 0.01 1 337 . 71 TRP CA C 58.3 0.05 1 338 . 71 TRP CB C 28.7 0.05 1 339 . 71 TRP NE1 N 129.9 0.05 1 340 . 71 TRP HE1 H 10.30 0.01 1 341 . 71 TRP C C 175.7 0.05 1 342 . 72 ASP N N 119.9 0.05 1 343 . 72 ASP H H 7.86 0.01 1 344 . 72 ASP CA C 52.6 0.05 1 345 . 72 ASP CB C 41.8 0.05 1 346 . 72 ASP C C 177.2 0.05 1 347 . 73 GLN N N 126.6 0.05 1 348 . 73 GLN H H 9.24 0.01 1 349 . 73 GLN CA C 59.4 0.05 1 350 . 73 GLN CB C 28.7 0.05 1 351 . 73 GLN C C 178.7 0.05 1 352 . 74 ASN N N 117.2 0.05 1 353 . 74 ASN H H 8.66 0.01 1 354 . 74 ASN CA C 56.1 0.05 1 355 . 74 ASN CB C 38.4 0.05 1 356 . 74 ASN C C 178.1 0.05 1 357 . 75 ALA N N 123.1 0.05 1 358 . 75 ALA H H 7.96 0.01 1 359 . 75 ALA CA C 54.5 0.05 1 360 . 75 ALA CB C 18.5 0.05 1 361 . 75 ALA C C 179.0 0.05 1 362 . 76 LEU N N 116.7 0.05 1 363 . 76 LEU H H 7.52 0.01 1 364 . 76 LEU CA C 58.8 0.05 1 365 . 76 LEU CB C 41.6 0.05 1 366 . 76 LEU C C 179.1 0.05 1 367 . 77 LYS N N 118.0 0.05 1 368 . 77 LYS H H 7.89 0.01 1 369 . 77 LYS CA C 59.6 0.05 1 370 . 77 LYS CB C 32.3 0.05 1 371 . 77 LYS C C 179.1 0.05 1 372 . 78 ALA N N 123.5 0.05 1 373 . 78 ALA H H 7.65 0.01 1 374 . 78 ALA CA C 55.2 0.05 1 375 . 78 ALA CB C 18.6 0.05 1 376 . 78 ALA C C 181.2 0.05 1 377 . 79 ILE N N 121.3 0.05 1 378 . 79 ILE H H 8.58 0.01 1 379 . 79 ILE CA C 65.8 0.05 1 380 . 79 ILE CB C 38.4 0.05 1 381 . 79 ILE C C 176.8 0.05 1 382 . 80 GLU N N 121.0 0.05 1 383 . 80 GLU H H 8.63 0.01 1 384 . 80 GLU CA C 61.1 0.05 1 385 . 80 GLU CB C 29.7 0.05 1 386 . 80 GLU C C 177.9 0.05 1 387 . 81 LYS N N 118.4 0.05 1 388 . 81 LYS H H 7.67 0.01 1 389 . 81 LYS CA C 59.9 0.05 1 390 . 81 LYS CB C 33.0 0.05 1 391 . 81 LYS C C 177.4 0.05 1 392 . 82 ALA N N 120.2 0.05 1 393 . 82 ALA H H 7.96 0.01 1 394 . 82 ALA CA C 55.3 0.05 1 395 . 82 ALA CB C 19.4 0.05 1 396 . 82 ALA C C 181.0 0.05 1 397 . 83 ILE N N 116.3 0.05 1 398 . 83 ILE H H 8.54 0.01 1 399 . 83 ILE CA C 65.8 0.05 1 400 . 83 ILE CB C 38.8 0.05 1 401 . 83 ILE C C 179.8 0.05 1 402 . 84 ARG N N 123.2 0.05 1 403 . 84 ARG H H 8.68 0.01 1 404 . 84 ARG CA C 60.6 0.05 1 405 . 84 ARG CB C 30.2 0.05 1 406 . 84 ARG C C 177.8 0.05 1 407 . 85 ASP N N 117.5 0.05 1 408 . 85 ASP H H 8.53 0.01 1 409 . 85 ASP CA C 55.4 0.05 1 410 . 85 ASP CB C 40.9 0.05 1 411 . 85 ASP C C 176.8 0.05 1 412 . 86 SER N N 115.9 0.05 1 413 . 86 SER H H 7.60 0.01 1 414 . 86 SER CA C 59.6 0.05 1 415 . 86 SER CB C 65.2 0.05 1 416 . 86 SER C C 173.8 0.05 1 417 . 87 ASP N N 118.6 0.05 1 418 . 87 ASP H H 8.51 0.01 1 419 . 87 ASP CA C 54.3 0.05 1 420 . 87 ASP CB C 40.4 0.05 1 421 . 87 ASP C C 177.3 0.05 1 422 . 88 LEU N N 118.1 0.05 1 423 . 88 LEU H H 8.18 0.01 1 424 . 88 LEU CA C 56.9 0.05 1 425 . 88 LEU CB C 43.7 0.05 1 426 . 88 LEU C C 178.2 0.05 1 427 . 89 GLY N N 107.9 0.05 1 428 . 89 GLY H H 8.50 0.01 1 429 . 89 GLY CA C 46.8 0.05 1 430 . 89 GLY C C 174.5 0.05 1 431 . 90 LEU N N 117.2 0.05 1 432 . 90 LEU H H 7.54 0.01 1 433 . 90 LEU CA C 53.3 0.05 1 434 . 90 LEU CB C 44.7 0.05 1 435 . 90 LEU C C 175.8 0.05 1 436 . 91 ASN N N 118.6 0.05 1 437 . 91 ASN H H 8.91 0.01 1 438 . 91 ASN CA C 50.4 0.05 1 439 . 91 ASN CB C 40.0 0.05 1 440 . 91 ASN C C 172.8 0.05 1 441 . 92 PRO CA C 62.7 0.05 1 442 . 92 PRO CB C 33.6 0.05 1 443 . 92 PRO C C 175.0 0.05 1 444 . 93 SER N N 116.3 0.05 1 445 . 93 SER H H 9.00 0.01 1 446 . 93 SER CA C 57.2 0.05 1 447 . 93 SER CB C 64.8 0.05 1 448 . 93 SER C C 174.0 0.05 1 449 . 94 ASN N N 126.2 0.05 1 450 . 94 ASN H H 9.28 0.01 1 451 . 94 ASN CA C 53.7 0.05 1 452 . 94 ASN CB C 39.2 0.05 1 453 . 94 ASN C C 175.7 0.05 1 454 . 95 LYS N N 126.6 0.05 1 455 . 95 LYS H H 8.61 0.01 1 456 . 95 LYS CA C 55.5 0.05 1 457 . 95 LYS CB C 32.9 0.05 1 458 . 95 LYS C C 176.6 0.05 1 459 . 96 GLY N N 113.2 0.05 1 460 . 96 GLY H H 9.07 0.01 1 461 . 96 GLY CA C 47.2 0.05 1 462 . 96 GLY C C 174.4 0.05 1 463 . 97 ASP N N 119.8 0.05 1 464 . 97 ASP H H 8.52 0.01 1 465 . 97 ASP CA C 53.8 0.05 1 466 . 97 ASP CB C 40.6 0.05 1 467 . 97 ASP C C 175.1 0.05 1 468 . 98 ALA N N 119.1 0.05 1 469 . 98 ALA H H 7.60 0.01 1 470 . 98 ALA CA C 51.5 0.05 1 471 . 98 ALA CB C 22.6 0.05 1 472 . 98 ALA C C 175.9 0.05 1 473 . 99 LEU N N 117.3 0.05 1 474 . 99 LEU H H 8.88 0.01 1 475 . 99 LEU CA C 53.1 0.05 1 476 . 99 LEU CB C 44.5 0.05 1 477 . 99 LEU C C 175.3 0.05 1 478 . 100 TYR N N 123.4 0.05 1 479 . 100 TYR H H 9.23 0.01 1 480 . 100 TYR CA C 57.9 0.05 1 481 . 100 TYR CB C 40.8 0.05 1 482 . 100 TYR C C 176.1 0.05 1 483 . 101 ILE N N 124.6 0.05 1 484 . 101 ILE H H 9.51 0.01 1 485 . 101 ILE CA C 60.7 0.05 1 486 . 101 ILE CB C 40.8 0.05 1 487 . 101 ILE C C 173.8 0.05 1 488 . 102 ASN N N 126.1 0.05 1 489 . 102 ASN H H 8.87 0.01 1 490 . 102 ASN CA C 53.3 0.05 1 491 . 102 ASN CB C 40.3 0.05 1 492 . 102 ASN C C 174.4 0.05 1 493 . 103 ILE N N 127.3 0.05 1 494 . 103 ILE H H 8.81 0.01 1 495 . 103 ILE CA C 56.6 0.05 1 496 . 103 ILE CB C 37.4 0.05 1 497 . 103 ILE C C 173.9 0.05 1 498 . 105 PRO CA C 62.5 0.05 1 499 . 105 PRO CB C 32.5 0.05 1 500 . 105 PRO C C 177.5 0.05 1 501 . 106 LEU N N 121.2 0.05 1 502 . 106 LEU H H 8.69 0.01 1 503 . 106 LEU CA C 54.9 0.05 1 504 . 106 LEU CB C 43.9 0.05 1 505 . 106 LEU C C 178.1 0.05 1 506 . 107 THR N N 112.1 0.05 1 507 . 107 THR H H 7.71 0.01 1 508 . 107 THR CA C 60.7 0.05 1 509 . 107 THR CB C 71.1 0.05 1 510 . 107 THR C C 175.6 0.05 1 511 . 108 GLU N N 122.2 0.05 1 512 . 108 GLU H H 9.11 0.01 1 513 . 108 GLU CA C 60.3 0.05 1 514 . 108 GLU CB C 29.6 0.05 1 515 . 108 GLU C C 179.0 0.05 1 516 . 109 GLU N N 117.8 0.05 1 517 . 109 GLU H H 8.89 0.01 1 518 . 109 GLU CA C 60.2 0.05 1 519 . 109 GLU CB C 29.4 0.05 1 520 . 109 GLU C C 178.8 0.05 1 521 . 110 ARG N N 119.5 0.05 1 522 . 110 ARG H H 7.67 0.01 1 523 . 110 ARG CA C 58.4 0.05 1 524 . 110 ARG CB C 30.4 0.05 1 525 . 110 ARG C C 178.9 0.05 1 526 . 111 ARG N N 119.2 0.05 1 527 . 111 ARG H H 8.59 0.01 1 528 . 111 ARG CA C 61.0 0.05 1 529 . 111 ARG CB C 30.8 0.05 1 530 . 111 ARG C C 178.0 0.05 1 531 . 112 LYS N N 117.1 0.05 1 532 . 112 LYS H H 8.01 0.01 1 533 . 112 LYS CA C 60.2 0.05 1 534 . 112 LYS CB C 32.4 0.05 1 535 . 112 LYS C C 179.8 0.05 1 536 . 113 ASP N N 120.4 0.05 1 537 . 113 ASP H H 7.90 0.01 1 538 . 113 ASP CA C 57.7 0.05 1 539 . 113 ASP CB C 41.4 0.05 1 540 . 113 ASP C C 179.3 0.05 1 541 . 114 LEU N N 122.0 0.05 1 542 . 114 LEU H H 8.54 0.01 1 543 . 114 LEU CA C 58.2 0.05 1 544 . 114 LEU CB C 43.1 0.05 1 545 . 114 LEU C C 179.1 0.05 1 546 . 115 VAL N N 119.7 0.05 1 547 . 115 VAL H H 8.44 0.01 1 548 . 115 VAL CA C 68.1 0.05 1 549 . 115 VAL CB C 31.8 0.05 1 550 . 115 VAL C C 177.9 0.05 1 551 . 116 ARG N N 119.3 0.05 1 552 . 116 ARG H H 7.83 0.01 1 553 . 116 ARG CA C 60.2 0.05 1 554 . 116 ARG CB C 29.7 0.05 1 555 . 116 ARG C C 179.1 0.05 1 556 . 117 ALA N N 122.3 0.05 1 557 . 117 ALA H H 7.92 0.01 1 558 . 117 ALA CA C 55.4 0.05 1 559 . 117 ALA CB C 18.3 0.05 1 560 . 117 ALA C C 179.6 0.05 1 561 . 118 VAL N N 118.7 0.05 1 562 . 118 VAL H H 8.49 0.01 1 563 . 118 VAL CA C 67.6 0.05 1 564 . 118 VAL CB C 31.8 0.05 1 565 . 118 VAL C C 177.9 0.05 1 566 . 119 ARG N N 117.3 0.05 1 567 . 119 ARG H H 8.31 0.01 1 568 . 119 ARG CA C 60.0 0.05 1 569 . 119 ARG CB C 29.9 0.05 1 570 . 119 ARG C C 179.8 0.05 1 571 . 120 GLN N N 122.0 0.05 1 572 . 120 GLN H H 8.44 0.01 1 573 . 120 GLN CA C 59.3 0.05 1 574 . 120 GLN CB C 28.3 0.05 1 575 . 120 GLN C C 179.0 0.05 1 576 . 121 TYR N N 119.3 0.05 1 577 . 121 TYR H H 8.72 0.01 1 578 . 121 TYR CA C 60.2 0.05 1 579 . 121 TYR CB C 37.2 0.05 1 580 . 121 TYR C C 180.0 0.05 1 581 . 122 ALA N N 123.0 0.05 1 582 . 122 ALA H H 9.25 0.01 1 583 . 122 ALA CA C 56.1 0.05 1 584 . 122 ALA CB C 18.6 0.05 1 585 . 122 ALA C C 179.0 0.05 1 586 . 123 GLU N N 119.3 0.05 1 587 . 123 GLU H H 8.17 0.01 1 588 . 123 GLU CA C 59.5 0.05 1 589 . 123 GLU CB C 28.9 0.05 1 590 . 123 GLU C C 178.6 0.05 1 591 . 124 GLU N N 119.0 0.05 1 592 . 124 GLU H H 8.34 0.01 1 593 . 124 GLU CA C 60.1 0.05 1 594 . 124 GLU CB C 29.7 0.05 1 595 . 124 GLU C C 180.6 0.05 1 596 . 125 GLY N N 108.4 0.05 1 597 . 125 GLY H H 8.52 0.01 1 598 . 125 GLY CA C 47.4 0.05 1 599 . 125 GLY C C 175.2 0.05 1 600 . 126 ARG N N 121.9 0.05 1 601 . 126 ARG H H 8.72 0.01 1 602 . 126 ARG CA C 61.2 0.05 1 603 . 126 ARG CB C 30.4 0.05 1 604 . 126 ARG C C 178.8 0.05 1 605 . 127 VAL N N 120.3 0.05 1 606 . 127 VAL H H 8.87 0.01 1 607 . 127 VAL CA C 67.2 0.05 1 608 . 127 VAL CB C 32.1 0.05 1 609 . 127 VAL C C 178.6 0.05 1 610 . 128 ALA N N 122.5 0.05 1 611 . 128 ALA H H 8.08 0.01 1 612 . 128 ALA CA C 55.9 0.05 1 613 . 128 ALA CB C 18.1 0.05 1 614 . 128 ALA C C 181.3 0.05 1 615 . 129 ILE N N 119.8 0.05 1 616 . 129 ILE H H 8.36 0.01 1 617 . 129 ILE CA C 66.4 0.05 1 618 . 129 ILE CB C 38.6 0.05 1 619 . 129 ILE C C 178.4 0.05 1 620 . 130 ARG N N 119.9 0.05 1 621 . 130 ARG H H 8.87 0.01 1 622 . 130 ARG CA C 61.0 0.05 1 623 . 130 ARG CB C 30.0 0.05 1 624 . 130 ARG C C 179.9 0.05 1 625 . 131 ASN N N 122.2 0.05 1 626 . 131 ASN H H 8.88 0.01 1 627 . 131 ASN CA C 56.4 0.05 1 628 . 131 ASN CB C 38.1 0.05 1 629 . 131 ASN C C 177.9 0.05 1 630 . 132 ILE N N 123.8 0.05 1 631 . 132 ILE H H 8.17 0.01 1 632 . 132 ILE CA C 65.2 0.05 1 633 . 132 ILE CB C 37.6 0.05 1 634 . 132 ILE C C 178.4 0.05 1 635 . 133 ARG N N 121.6 0.05 1 636 . 133 ARG H H 8.21 0.01 1 637 . 133 ARG CA C 60.4 0.05 1 638 . 133 ARG CB C 28.5 0.05 1 639 . 133 ARG C C 177.1 0.05 1 640 . 134 ARG N N 118.6 0.05 1 641 . 134 ARG H H 7.87 0.01 1 642 . 134 ARG CA C 60.2 0.05 1 643 . 134 ARG CB C 30.1 0.05 1 644 . 134 ARG C C 179.0 0.05 1 645 . 135 GLU N N 119.7 0.05 1 646 . 135 GLU H H 8.18 0.01 1 647 . 135 GLU CA C 59.8 0.05 1 648 . 135 GLU CB C 30.0 0.05 1 649 . 135 GLU C C 179.5 0.05 1 650 . 136 ALA N N 124.1 0.05 1 651 . 136 ALA H H 8.96 0.01 1 652 . 136 ALA CA C 55.7 0.05 1 653 . 136 ALA CB C 19.6 0.05 1 654 . 136 ALA C C 180.1 0.05 1 655 . 137 LEU N N 118.2 0.05 1 656 . 137 LEU H H 8.66 0.01 1 657 . 137 LEU CA C 57.9 0.05 1 658 . 137 LEU CB C 41.4 0.05 1 659 . 137 LEU C C 180.4 0.05 1 660 . 138 ASP N N 122.5 0.05 1 661 . 138 ASP H H 8.26 0.01 1 662 . 138 ASP CA C 58.0 0.05 1 663 . 138 ASP CB C 40.7 0.05 1 664 . 138 ASP C C 179.8 0.05 1 665 . 139 LYS N N 121.6 0.05 1 666 . 139 LYS H H 8.34 0.01 1 667 . 139 LYS CA C 60.3 0.05 1 668 . 139 LYS CB C 35.0 0.05 1 669 . 139 LYS C C 179.7 0.05 1 670 . 140 LEU N N 121.6 0.05 1 671 . 140 LEU H H 8.91 0.01 1 672 . 140 LEU CA C 58.2 0.05 1 673 . 140 LEU CB C 41.7 0.05 1 674 . 140 LEU C C 177.3 0.05 1 675 . 141 LYS N N 118.0 0.05 1 676 . 141 LYS H H 7.87 0.01 1 677 . 141 LYS CA C 60.1 0.05 1 678 . 141 LYS CB C 32.5 0.05 1 679 . 141 LYS C C 179.6 0.05 1 680 . 142 LYS N N 118.3 0.05 1 681 . 142 LYS H H 7.28 0.01 1 682 . 142 LYS CA C 59.5 0.05 1 683 . 142 LYS CB C 33.0 0.05 1 684 . 142 LYS C C 179.3 0.05 1 685 . 143 LEU N N 122.2 0.05 1 686 . 143 LEU H H 8.67 0.01 1 687 . 143 LEU CA C 58.1 0.05 1 688 . 143 LEU CB C 42.7 0.05 1 689 . 143 LEU C C 178.7 0.05 1 690 . 144 ALA N N 120.4 0.05 1 691 . 144 ALA H H 9.35 0.01 1 692 . 144 ALA CA C 55.6 0.05 1 693 . 144 ALA CB C 18.9 0.05 1 694 . 144 ALA C C 180.4 0.05 1 695 . 145 LYS N N 115.8 0.05 1 696 . 145 LYS H H 7.17 0.01 1 697 . 145 LYS CA C 58.7 0.05 1 698 . 145 LYS CB C 32.8 0.05 1 699 . 145 LYS C C 179.3 0.05 1 700 . 146 GLU N N 120.6 0.05 1 701 . 146 GLU H H 7.94 0.01 1 702 . 146 GLU CA C 59.4 0.05 1 703 . 146 GLU CB C 30.5 0.05 1 704 . 146 GLU C C 178.5 0.05 1 705 . 147 LEU N N 115.1 0.05 1 706 . 147 LEU H H 8.65 0.01 1 707 . 147 LEU CA C 54.6 0.05 1 708 . 147 LEU CB C 42.2 0.05 1 709 . 147 LEU C C 176.7 0.05 1 710 . 148 HIS N N 115.6 0.05 1 711 . 148 HIS H H 7.59 0.01 1 712 . 148 HIS CA C 56.4 0.05 1 713 . 148 HIS CB C 26.3 0.05 1 714 . 148 HIS C C 175.2 0.05 1 715 . 149 LEU N N 117.0 0.05 1 716 . 149 LEU H H 8.14 0.01 1 717 . 149 LEU CA C 55.3 0.05 1 718 . 149 LEU CB C 42.7 0.05 1 719 . 149 LEU C C 178.6 0.05 1 720 . 150 SER N N 119.1 0.05 1 721 . 150 SER H H 9.36 0.01 1 722 . 150 SER CA C 57.6 0.05 1 723 . 150 SER CB C 65.7 0.05 1 724 . 150 SER C C 176.2 0.05 1 725 . 151 GLU N N 124.2 0.05 1 726 . 151 GLU H H 9.35 0.01 1 727 . 151 GLU CA C 60.6 0.05 1 728 . 151 GLU CB C 29.6 0.05 1 729 . 151 GLU C C 179.0 0.05 1 730 . 152 ASP N N 118.2 0.05 1 731 . 152 ASP H H 8.64 0.01 1 732 . 152 ASP CA C 57.9 0.05 1 733 . 152 ASP CB C 41.4 0.05 1 734 . 152 ASP C C 179.2 0.05 1 735 . 153 GLU N N 119.6 0.05 1 736 . 153 GLU H H 8.02 0.01 1 737 . 153 GLU CA C 59.6 0.05 1 738 . 153 GLU CB C 31.2 0.05 1 739 . 153 GLU C C 179.9 0.05 1 740 . 154 THR N N 118.1 0.05 1 741 . 154 THR H H 8.61 0.01 1 742 . 154 THR CA C 68.0 0.05 1 743 . 154 THR C C 176.4 0.05 1 744 . 155 LYS N N 122.2 0.05 1 745 . 155 LYS H H 8.46 0.01 1 746 . 155 LYS CA C 59.7 0.05 1 747 . 155 LYS CB C 32.3 0.05 1 748 . 155 LYS C C 180.4 0.05 1 749 . 156 ARG N N 120.5 0.05 1 750 . 156 ARG H H 8.10 0.01 1 751 . 156 ARG CA C 59.7 0.05 1 752 . 156 ARG CB C 30.3 0.05 1 753 . 156 ARG C C 178.9 0.05 1 754 . 157 ALA N N 124.4 0.05 1 755 . 157 ALA H H 8.00 0.01 1 756 . 157 ALA CA C 55.0 0.05 1 757 . 157 ALA CB C 21.1 0.05 1 758 . 157 ALA C C 180.3 0.05 1 759 . 158 GLU N N 119.7 0.05 1 760 . 158 GLU H H 8.67 0.01 1 761 . 158 GLU CA C 60.5 0.05 1 762 . 158 GLU CB C 29.8 0.05 1 763 . 158 GLU C C 179.7 0.05 1 764 . 159 ALA N N 121.6 0.05 1 765 . 159 ALA H H 8.09 0.01 1 766 . 159 ALA CA C 55.1 0.05 1 767 . 159 ALA CB C 18.0 0.05 1 768 . 159 ALA C C 180.8 0.05 1 769 . 160 GLU N N 122.2 0.05 1 770 . 160 GLU H H 8.25 0.01 1 771 . 160 GLU CA C 59.3 0.05 1 772 . 160 GLU CB C 29.0 0.05 1 773 . 160 GLU C C 179.4 0.05 1 774 . 161 ILE N N 119.3 0.05 1 775 . 161 ILE H H 8.33 0.01 1 776 . 161 ILE CA C 65.0 0.05 1 777 . 161 ILE CB C 37.4 0.05 1 778 . 161 ILE C C 179.8 0.05 1 779 . 162 GLN N N 124.0 0.05 1 780 . 162 GLN H H 8.65 0.01 1 781 . 162 GLN CA C 59.3 0.05 1 782 . 162 GLN CB C 28.2 0.05 1 783 . 162 GLN C C 176.8 0.05 1 784 . 163 LYS N N 121.4 0.05 1 785 . 163 LYS H H 8.36 0.01 1 786 . 163 LYS CA C 60.3 0.05 1 787 . 163 LYS CB C 32.6 0.05 1 788 . 163 LYS C C 180.2 0.05 1 789 . 164 ILE N N 120.9 0.05 1 790 . 164 ILE H H 8.32 0.01 1 791 . 164 ILE CA C 66.3 0.05 1 792 . 164 ILE CB C 39.7 0.05 1 793 . 164 ILE C C 177.6 0.05 1 794 . 165 THR N N 116.0 0.05 1 795 . 165 THR H H 8.11 0.01 1 796 . 165 THR CA C 68.4 0.05 1 797 . 165 THR CB C 73.0 0.05 1 798 . 165 THR C C 176.2 0.05 1 799 . 166 ASP N N 121.2 0.05 1 800 . 166 ASP H H 8.97 0.01 1 801 . 166 ASP CA C 58.0 0.05 1 802 . 166 ASP CB C 40.5 0.05 1 803 . 166 ASP C C 179.6 0.05 1 804 . 167 GLU N N 122.2 0.05 1 805 . 167 GLU H H 8.20 0.01 1 806 . 167 GLU CA C 59.5 0.05 1 807 . 167 GLU CB C 29.6 0.05 1 808 . 167 GLU C C 179.3 0.05 1 809 . 168 PHE N N 118.7 0.05 1 810 . 168 PHE H H 8.30 0.01 1 811 . 168 PHE CA C 64.5 0.05 1 812 . 168 PHE CB C 39.5 0.05 1 813 . 168 PHE C C 178.3 0.05 1 814 . 169 ILE N N 122.4 0.05 1 815 . 169 ILE H H 9.26 0.01 1 816 . 169 ILE CA C 64.1 0.05 1 817 . 169 ILE CB C 36.1 0.05 1 818 . 169 ILE C C 177.4 0.05 1 819 . 170 ALA N N 120.0 0.05 1 820 . 170 ALA H H 7.96 0.01 1 821 . 170 ALA CA C 55.5 0.05 1 822 . 170 ALA CB C 17.9 0.05 1 823 . 170 ALA C C 181.4 0.05 1 824 . 171 LYS N N 118.2 0.05 1 825 . 171 LYS H H 7.84 0.01 1 826 . 171 LYS CA C 60.1 0.05 1 827 . 171 LYS CB C 33.5 0.05 1 828 . 171 LYS C C 179.2 0.05 1 829 . 172 ALA N N 124.8 0.05 1 830 . 172 ALA H H 8.56 0.01 1 831 . 172 ALA CA C 56.0 0.05 1 832 . 172 ALA CB C 17.2 0.05 1 833 . 172 ALA C C 178.9 0.05 1 834 . 173 ASP N N 118.3 0.05 1 835 . 173 ASP H H 8.86 0.01 1 836 . 173 ASP CA C 57.9 0.05 1 837 . 173 ASP CB C 40.2 0.05 1 838 . 173 ASP C C 179.9 0.05 1 839 . 174 GLN N N 120.0 0.05 1 840 . 174 GLN H H 8.27 0.01 1 841 . 174 GLN CA C 59.3 0.05 1 842 . 174 GLN CB C 29.1 0.05 1 843 . 174 GLN C C 179.0 0.05 1 844 . 175 LEU N N 120.9 0.05 1 845 . 175 LEU H H 8.20 0.01 1 846 . 175 LEU CA C 58.4 0.05 1 847 . 175 LEU CB C 42.6 0.05 1 848 . 175 LEU C C 180.1 0.05 1 849 . 176 ALA N N 121.4 0.05 1 850 . 176 ALA H H 8.25 0.01 1 851 . 176 ALA CA C 55.6 0.05 1 852 . 176 ALA CB C 19.0 0.05 1 853 . 176 ALA C C 179.2 0.05 1 854 . 177 GLU N N 119.7 0.05 1 855 . 177 GLU H H 8.59 0.01 1 856 . 177 GLU CA C 59.9 0.05 1 857 . 177 GLU CB C 29.9 0.05 1 858 . 177 GLU C C 179.3 0.05 1 859 . 178 LYS N N 118.6 0.05 1 860 . 178 LYS H H 8.24 0.01 1 861 . 178 LYS CA C 59.5 0.05 1 862 . 178 LYS CB C 32.5 0.05 1 863 . 178 LYS C C 179.7 0.05 1 864 . 179 LYS N N 119.9 0.05 1 865 . 179 LYS H H 7.90 0.01 1 866 . 179 LYS CA C 57.0 0.05 1 867 . 179 LYS CB C 30.6 0.05 1 868 . 179 LYS C C 178.7 0.05 1 869 . 180 GLU N N 119.7 0.05 1 870 . 180 GLU H H 8.70 0.01 1 871 . 180 GLU CA C 61.6 0.05 1 872 . 180 GLU CB C 29.6 0.05 1 873 . 180 GLU C C 178.5 0.05 1 874 . 181 GLN N N 116.6 0.05 1 875 . 181 GLN H H 8.26 0.01 1 876 . 181 GLN CA C 59.2 0.05 1 877 . 181 GLN CB C 28.3 0.05 1 878 . 181 GLN C C 179.2 0.05 1 879 . 182 GLU N N 119.9 0.05 1 880 . 182 GLU H H 7.92 0.01 1 881 . 182 GLU CA C 59.3 0.05 1 882 . 182 GLU CB C 30.6 0.05 1 883 . 182 GLU C C 179.1 0.05 1 884 . 183 ILE N N 119.6 0.05 1 885 . 183 ILE H H 8.01 0.01 1 886 . 183 ILE CA C 65.1 0.05 1 887 . 183 ILE CB C 39.1 0.05 1 888 . 183 ILE C C 176.8 0.05 1 889 . 184 LEU N N 118.0 0.05 1 890 . 184 LEU H H 8.14 0.01 1 891 . 184 LEU CA C 56.4 0.05 1 892 . 184 LEU CB C 42.8 0.05 1 893 . 184 LEU C C 177.5 0.05 1 894 . 185 GLY N N 113.3 0.05 1 895 . 185 GLY H H 7.72 0.01 1 896 . 185 GLY CA C 46.9 0.05 1 897 . 185 GLY C C 179.1 0.05 1 stop_ save_