data_4424
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR Structure of the N-terminal Domain of Saccharomyces cerevisiae RNase HI
Reveals a Fold with a Strong Resemblance to the N-terminal Domain of Ribosomal
Protein L9
;
_BMRB_accession_number 4424
_BMRB_flat_file_name bmr4424.str
_Entry_type original
_Submission_date 1999-09-29
_Accession_date 1999-09-30
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details .
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Evans S. P. .
2 Bycroft M. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 311
"13C chemical shifts" 190
"15N chemical shifts" 58
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
1999-12-23 original author .
stop_
_Original_release_date 1999-12-23
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
NMR Structure of the N-terminal Domain of Saccharomyces cerevisiae RNase HI
Reveals a Fold with a Strong Resemblance to the N-terminal Domain of Ribosomal
Protein L
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 99380410
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Evans S. P. .
2 Bycroft M. . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_volume 291
_Journal_issue 3
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 661
_Page_last 669
_Year 1999
_Details .
loop_
_Keyword
'Ribonuclease HI N-terminal domain'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full .
_Citation_title 'The non-RNase H domain of Saccharomyces cerevisiae RNase H1 binds double-stranded RNA: magnesium modulates the switch between double-stranded RNA binding and RNase H activity.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 7489497
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Cerritelli 'S. M.' M. .
2 Crouch 'R. J.' J. .
stop_
_Journal_abbreviation RNA
_Journal_name_full 'RNA (New York, N.Y.)'
_Journal_volume 1
_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 246
_Page_last 259
_Year 1995
_Details
;
Eukaryotic ribonucleases H of known sequence are composed of an RNase H domain
similar in size and sequence to that of Escherichia coli RNase HI and
additional domains of unknown function. The RNase H1 of Saccharomyces
cerevisiae has such an RNase H domain at its C-terminus. Here we show that the
N-terminal non-RNase H portion of the yeast RNase H1 binds tightly to
double-stranded RNA (dsRNA) and RNA-DNA hybrids even in the absence of the
RNase H domain. Two copies of a sequence with limited similarity to the
dsRNA-binding motif are present in this N-terminus. When the first of these
sequences is altered, the protein no longer binds tightly to dsRNA and exhibits
an increase in RNase H activity. Unlike other dsRNA-binding proteins,
increasing the Mg2+ concentration from 0.5 mM to 5 mM inhibits binding of RNase
H1 to dsRNA; yet a protein missing the RNase H domain binds strongly to dsRNA
even at the higher Mg2+ concentration. These results suggest that binding to
dsRNA and RNase H activity are mutually exclusive, and the Mg2+ concentration
is critical for switching between the activities. Changes in the Mg2+
concentration or proteolytic severing of the dsRNA-binding domain could alter
the activity or location of the RNase H and may govern access of the enzyme to
the substrate. Sequences similar to the dsRNA-binding motif are present in
other eukaryotic RNases H and the transactivating protein of cauliflower mosaic
virus, suggesting that these proteins may also bind to dsRNA.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full .
_Citation_title 'Selective cloning of genes encoding RNase H from Salmonella typhimurium, Saccharomyces cerevisiae and Escherichia coli rnh mutant.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 1650910
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Itaya M. . .
2 McKelvin D. . .
3 Chatterjie 'S. K.' K. .
4 Crouch 'R. J.' J. .
stop_
_Journal_abbreviation 'Mol. Gen. Genet.'
_Journal_name_full 'Molecular & general genetics : MGG'
_Journal_volume 227
_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 438
_Page_last 445
_Year 1991
_Details
;
We have cloned genes encoding RNase H from Escherichia coli rnh mutants,
Salmonella typhimurium and Saccharomyces cerevisiae. Selection was accomplished
by suppression of the temperature-sensitive growth phenotype of Escherichia
coli strains containing the rnh-339::cat and either recB270 (Ts) or recC271
(Ts) mutations. RNases H from E. coli and S. typhimurium contained 155 amino
acid residues and differed at only 11 positions. The S. cerevisiae and E. coli
RNases H were about 30% homologous. A comparison of the amino acid sequences of
several RNases H from cellular and retroviral sources revealed some strongly
conserved regions as well as variable regions; the carboxyl-terminus was
particularly variable. The overlapping, divergent promoter gene organization
found in E. coli was observed to be present in S. typhimurium.
;
save_
##################################
# Molecular system description #
##################################
save_system_RNase_HI
_Saveframe_category molecular_system
_Mol_system_name 'ribonuclease HI'
_Abbreviation_common 'RNase HI'
_Enzyme_commission_number 3.1.26.4
loop_
_Mol_system_component_name
_Mol_label
'RNase HI' $RNase_HI
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'fully reduced'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_RNase_HI
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'ribonuclease HI'
_Abbreviation_common 'RNase HI'
_Molecular_mass .
_Mol_thiol_state 'fully reduced'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 63
_Mol_residue_sequence
;
GSARQGNFYAVRKGRETGIY
NTWNECKNQVDGYGGAIYKK
FNSYEQAKSFLGQPNTTSNY
GSS
;
loop_
_Residue_seq_code
_Residue_label
1 GLY 2 SER 3 ALA 4 ARG 5 GLN
6 GLY 7 ASN 8 PHE 9 TYR 10 ALA
11 VAL 12 ARG 13 LYS 14 GLY 15 ARG
16 GLU 17 THR 18 GLY 19 ILE 20 TYR
21 ASN 22 THR 23 TRP 24 ASN 25 GLU
26 CYS 27 LYS 28 ASN 29 GLN 30 VAL
31 ASP 32 GLY 33 TYR 34 GLY 35 GLY
36 ALA 37 ILE 38 TYR 39 LYS 40 LYS
41 PHE 42 ASN 43 SER 44 TYR 45 GLU
46 GLN 47 ALA 48 LYS 49 SER 50 PHE
51 LEU 52 GLY 53 GLN 54 PRO 55 ASN
56 THR 57 THR 58 SER 59 ASN 60 TYR
61 GLY 62 SER 63 SER
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-07-14
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 1QHK "N-Terminal Domain Of Saccharomyces Cerevisiae Rnase Hi Reveals A Fold With A Resemblance To The N-Terminal Domain Of Ribosomal " 73.02 47 100.00 100.00 2.98e-24
DBJ GAA25685 "K7_Rnh1p [Saccharomyces cerevisiae Kyokai no. 7]" 96.83 348 100.00 100.00 6.57e-34
EMBL CAA90205 "Rnh1p [Saccharomyces cerevisiae]" 96.83 348 100.00 100.00 6.99e-34
EMBL CAY82065 "Rnh1p [Saccharomyces cerevisiae EC1118]" 96.83 348 100.00 100.00 6.99e-34
GB AHY76689 "Rnh1p [Saccharomyces cerevisiae YJM993]" 96.83 348 100.00 100.00 6.99e-34
GB AJP40928 "Rnh1p [Saccharomyces cerevisiae YJM1078]" 96.83 348 100.00 100.00 6.99e-34
GB AJS62100 "Rnh1p [Saccharomyces cerevisiae YJM189]" 96.83 348 100.00 100.00 6.99e-34
GB AJS62535 "Rnh1p [Saccharomyces cerevisiae YJM193]" 96.83 348 98.36 98.36 3.41e-33
GB AJS62973 "Rnh1p [Saccharomyces cerevisiae YJM195]" 96.83 348 100.00 100.00 6.57e-34
REF NP_013961 "Rnh1p [Saccharomyces cerevisiae S288c]" 96.83 348 100.00 100.00 6.99e-34
SP Q04740 "RecName: Full=Ribonuclease H; Short=RNase H" 96.83 348 100.00 100.00 6.99e-34
TPG DAA10134 "TPA: Rnh1p [Saccharomyces cerevisiae S288c]" 96.83 348 100.00 100.00 6.99e-34
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$RNase_HI 'Baker's yeast' 4932 Eukaryota Fungi Saccharomyces cerevisiae
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
$RNase_HI 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3)C41 .
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
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$RNase_HI . mM 1.0 3.0 '[U-13C; U-15N]'
stop_
save_
############################
# Computer software used #
############################
save_FELIX
_Saveframe_category software
_Name FELIX
_Version 2.3
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_Sample_label $sample_1
save_
save_COSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name COSY
_Sample_label $sample_1
save_
save_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TOCSY
_Sample_label $sample_1
save_
save_HBHA(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HBHA(CO)NH
_Sample_label $sample_1
save_
save_CBCA(CO)NH_5
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label $sample_1
save_
save_HNCACB_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label $sample_1
save_
save_HCCH-TOCSY_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_Sample_label $sample_1
save_
save_HNHA_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HNHA
_Sample_label $sample_1
save_
save_HNHB_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HNHB
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name COSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HBHA(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HNHA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HNHB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 3.6 0.2 n/a
temperature 298 0.3 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_shift_ref
_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
TSP H 1 'methyl protons' ppm 0.00 internal direct . internal . .
DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530
DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118
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_chem_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chem_shift_ref
_Mol_system_component_name 'RNase HI'
_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 GLY H H 8.72 . 1
2 . 1 GLY HA2 H 3.58 . 1
3 . 1 GLY HA3 H 3.58 . 1
4 . 1 GLY CA C 41.46 . 1
5 . 1 GLY N N 121.52 . 1
6 . 2 SER H H 8.65 . 1
7 . 2 SER HA H 4.41 . 1
8 . 2 SER HB2 H 3.76 . 1
9 . 2 SER HB3 H 3.76 . 1
10 . 2 SER CA C 55.63 . 1
11 . 2 SER CB C 61.70 . 1
12 . 2 SER N N 117.89 . 1
13 . 3 ALA H H 8.53 . 1
14 . 3 ALA HA H 4.27 . 1
15 . 3 ALA HB H 1.27 . 1
16 . 3 ALA CA C 50.16 . 1
17 . 3 ALA CB C 17.05 . 1
18 . 3 ALA N N 128.53 . 1
19 . 4 ARG H H 8.45 . 1
20 . 4 ARG HA H 4.25 . 1
21 . 4 ARG HB2 H 1.65 . 2
22 . 4 ARG HB3 H 1.71 . 2
23 . 4 ARG HG2 H 1.48 . 1
24 . 4 ARG HG3 H 1.48 . 1
25 . 4 ARG HD2 H 3.06 . 1
26 . 4 ARG HD3 H 3.06 . 1
27 . 4 ARG CA C 53.57 . 1
28 . 4 ARG CB C 28.59 . 1
29 . 4 ARG CG C 24.67 . 1
30 . 4 ARG CD C 41.34 . 1
31 . 4 ARG N N 123.00 . 1
32 . 5 GLN H H 8.47 . 1
33 . 5 GLN HA H 4.50 . 1
34 . 5 GLN HB2 H 2.03 . 1
35 . 5 GLN HB3 H 1.92 . 1
36 . 5 GLN HG2 H 2.28 . 1
37 . 5 GLN HG3 H 2.28 . 1
38 . 5 GLN CA C 53.49 . 1
39 . 5 GLN CB C 27.78 . 1
40 . 5 GLN CG C 31.56 . 1
41 . 5 GLN N N 124.48 . 1
42 . 6 GLY H H 8.42 . 1
43 . 6 GLY HA2 H 3.90 . 2
44 . 6 GLY HA3 H 3.70 . 2
45 . 6 GLY CA C 42.70 . 1
46 . 6 GLY N N 112.56 . 1
47 . 7 ASN H H 7.88 . 1
48 . 7 ASN HA H 4.79 . 1
49 . 7 ASN HB2 H 2.10 . 1
50 . 7 ASN HB3 H 2.44 . 1
51 . 7 ASN CA C 50.14 . 1
52 . 7 ASN CB C 39.34 . 1
53 . 7 ASN N N 119.56 . 1
54 . 8 PHE H H 8.34 . 1
55 . 8 PHE HA H 4.80 . 1
56 . 8 PHE HB2 H 2.50 . 1
57 . 8 PHE HB3 H 2.50 . 1
58 . 8 PHE HD1 H 6.97 . 1
59 . 8 PHE HD2 H 6.97 . 1
60 . 8 PHE HE1 H 7.32 . 1
61 . 8 PHE HE2 H 7.32 . 1
62 . 8 PHE CA C 54.20 . 1
63 . 8 PHE CB C 39.35 . 1
64 . 8 PHE CD1 C 129.97 . 1
65 . 8 PHE CD2 C 129.97 . 1
66 . 8 PHE CE1 C 130.72 . 1
67 . 8 PHE CE2 C 130.72 . 1
68 . 8 PHE N N 119.07 . 1
69 . 9 TYR H H 9.68 . 1
70 . 9 TYR HA H 4.86 . 1
71 . 9 TYR HB2 H 2.98 . 1
72 . 9 TYR HB3 H 2.98 . 1
73 . 9 TYR HD1 H 7.04 . 1
74 . 9 TYR HD2 H 7.04 . 1
75 . 9 TYR HE1 H 6.77 . 1
76 . 9 TYR HE2 H 6.77 . 1
77 . 9 TYR CA C 55.37 . 1
78 . 9 TYR CB C 37.07 . 1
79 . 9 TYR CD1 C 131.21 . 1
80 . 9 TYR CD2 C 131.21 . 1
81 . 9 TYR CE1 C 115.72 . 1
82 . 9 TYR CE2 C 115.72 . 1
83 . 9 TYR N N 124.58 . 1
84 . 10 ALA H H 9.40 . 1
85 . 10 ALA HA H 5.16 . 1
86 . 10 ALA HB H 1.60 . 1
87 . 10 ALA CA C 48.57 . 1
88 . 10 ALA CB C 19.81 . 1
89 . 10 ALA N N 130.08 . 1
90 . 11 VAL H H 9.57 . 1
91 . 11 VAL HA H 4.52 . 1
92 . 11 VAL HB H 2.30 . 1
93 . 11 VAL HG2 H 0.66 . 2
94 . 11 VAL HG1 H 0.95 . 2
95 . 11 VAL CA C 59.78 . 1
96 . 11 VAL CB C 31.10 . 1
97 . 11 VAL CG1 C 19.28 . 1
98 . 11 VAL CG2 C 21.20 . 1
99 . 11 VAL N N 126.87 . 1
100 . 12 ARG H H 8.41 . 1
101 . 12 ARG HA H 4.33 . 1
102 . 12 ARG HB2 H 1.48 . 1
103 . 12 ARG HB3 H 1.48 . 1
104 . 12 ARG CA C 53.50 . 1
105 . 12 ARG CB C 28.34 . 1
106 . 12 ARG N N 128.51 . 1
107 . 15 ARG CA C 58.63 . 1
108 . 15 ARG CB C 27.20 . 1
109 . 16 GLU H H 7.09 . 1
110 . 16 GLU HA H 4.39 . 1
111 . 16 GLU HB2 H 1.62 . 2
112 . 16 GLU HB3 H 1.81 . 2
113 . 16 GLU HG2 H 2.20 . 2
114 . 16 GLU HG3 H 2.29 . 2
115 . 16 GLU CA C 52.27 . 1
116 . 16 GLU CB C 28.19 . 1
117 . 16 GLU N N 117.06 . 1
118 . 17 THR CA C 58.53 . 1
119 . 17 THR CB C 68.25 . 1
120 . 18 GLY H H 8.28 . 1
121 . 18 GLY HA2 H 4.19 . 2
122 . 18 GLY HA3 H 3.61 . 2
123 . 18 GLY CA C 42.11 . 1
124 . 18 GLY N N 108.63 . 1
125 . 19 ILE H H 8.04 . 1
126 . 19 ILE HA H 4.77 . 1
127 . 19 ILE HB H 1.48 . 1
128 . 19 ILE HG12 H 0.52 . 1
129 . 19 ILE HG13 H 0.52 . 1
130 . 19 ILE HG2 H 0.84 . 1
131 . 19 ILE HD1 H 0.33 . 1
132 . 19 ILE CA C 57.86 . 1
133 . 19 ILE CB C 37.18 . 1
134 . 19 ILE CG1 C 27.05 . 1
135 . 19 ILE CG2 C 16.74 . 1
136 . 19 ILE CD1 C 11.17 . 1
137 . 19 ILE N N 121.26 . 1
138 . 20 TYR H H 9.46 . 1
139 . 20 TYR HA H 4.90 . 1
140 . 20 TYR HB2 H 3.19 . 1
141 . 20 TYR HB3 H 2.48 . 1
142 . 20 TYR HD1 H 7.04 . 1
143 . 20 TYR HD2 H 7.04 . 1
144 . 20 TYR HE1 H 6.52 . 1
145 . 20 TYR HE2 H 6.52 . 1
146 . 20 TYR CA C 54.41 . 1
147 . 20 TYR CB C 39.65 . 1
148 . 20 TYR CD1 C 131.48 . 1
149 . 20 TYR CD2 C 131.48 . 1
150 . 20 TYR CE1 C 115.33 . 1
151 . 20 TYR CE2 C 115.33 . 1
152 . 20 TYR N N 128.54 . 1
153 . 21 ASN H H 9.43 . 1
154 . 21 ASN HA H 5.17 . 1
155 . 21 ASN HB2 H 2.88 . 1
156 . 21 ASN HB3 H 2.88 . 1
157 . 21 ASN CA C 51.59 . 1
158 . 21 ASN CB C 37.67 . 1
159 . 21 ASN N N 121.37 . 1
160 . 22 THR H H 7.42 . 1
161 . 22 THR HA H 4.81 . 1
162 . 22 THR HB H 4.41 . 1
163 . 22 THR HG2 H 1.15 . 1
164 . 22 THR CA C 56.58 . 1
165 . 22 THR CB C 70.36 . 1
166 . 22 THR CG2 C 19.58 . 1
167 . 22 THR N N 107.61 . 1
168 . 23 TRP H H 9.05 . 1
169 . 23 TRP HA H 3.59 . 1
170 . 23 TRP HB2 H 3.18 . 2
171 . 23 TRP HB3 H 2.84 . 2
172 . 23 TRP HZ2 H 7.36 . 1
173 . 23 TRP HH2 H 6.89 . 1
174 . 23 TRP CA C 55.63 . 1
175 . 23 TRP CB C 26.96 . 1
176 . 23 TRP CZ2 C 112.44 . 1
177 . 23 TRP CH2 C 121.80 . 1
178 . 23 TRP N N 125.95 . 1
179 . 24 ASN H H 8.56 . 1
180 . 24 ASN HA H 3.53 . 1
181 . 24 ASN HB2 H 2.44 . 1
182 . 24 ASN HB3 H 2.44 . 1
183 . 24 ASN CA C 53.85 . 1
184 . 24 ASN CB C 35.31 . 1
185 . 24 ASN N N 117.83 . 1
186 . 25 GLU H H 7.22 . 1
187 . 25 GLU HA H 3.65 . 1
188 . 25 GLU HB2 H 1.90 . 1
189 . 25 GLU HB3 H 1.90 . 1
190 . 25 GLU HG2 H 2.14 . 1
191 . 25 GLU HG3 H 2.14 . 1
192 . 25 GLU CA C 55.83 . 1
193 . 25 GLU CB C 28.17 . 1
194 . 25 GLU CG C 34.72 . 1
195 . 25 GLU N N 117.50 . 1
196 . 26 CYS H H 7.03 . 1
197 . 26 CYS HA H 3.02 . 1
198 . 26 CYS HB2 H 2.34 . 2
199 . 26 CYS HB3 H 1.93 . 2
200 . 26 CYS CA C 59.54 . 1
201 . 26 CYS CB C 24.02 . 1
202 . 26 CYS N N 120.91 . 1
203 . 27 LYS H H 8.39 . 1
204 . 27 LYS HA H 2.80 . 1
205 . 27 LYS HB2 H 0.15 . 1
206 . 27 LYS HB3 H 0.67 . 1
207 . 27 LYS HG2 H 0.77 . 1
208 . 27 LYS HG3 H 0.77 . 1
209 . 27 LYS HD2 H 1.29 . 1
210 . 27 LYS HD3 H 1.29 . 1
211 . 27 LYS CA C 56.45 . 1
212 . 27 LYS CB C 28.47 . 1
213 . 27 LYS CG C 22.42 . 1
214 . 27 LYS CD C 26.86 . 1
215 . 27 LYS CE C 39.55 . 1
216 . 27 LYS N N 122.00 . 1
217 . 28 ASN H H 6.93 . 1
218 . 28 ASN HA H 4.16 . 1
219 . 28 ASN HB2 H 2.47 . 1
220 . 28 ASN HB3 H 2.47 . 1
221 . 28 ASN CA C 52.86 . 1
222 . 28 ASN CB C 35.29 . 1
223 . 28 ASN N N 117.01 . 1
224 . 29 GLN H H 7.60 . 1
225 . 29 GLN HA H 4.51 . 1
226 . 29 GLN HB2 H 2.02 . 2
227 . 29 GLN HB3 H 1.67 . 2
228 . 29 GLN HG2 H 2.42 . 1
229 . 29 GLN HG3 H 2.42 . 1
230 . 29 GLN CA C 52.10 . 1
231 . 29 GLN CB C 26.10 . 1
232 . 29 GLN CG C 28.00 . 1
233 . 29 GLN N N 115.89 . 1
234 . 30 VAL H H 7.06 . 1
235 . 30 VAL HA H 4.44 . 1
236 . 30 VAL HB H 2.03 . 1
237 . 30 VAL HG2 H 0.71 . 2
238 . 30 VAL HG1 H 0.32 . 2
239 . 30 VAL CA C 58.89 . 1
240 . 30 VAL CB C 31.31 . 1
241 . 30 VAL CG1 C 20.11 . 1
242 . 30 VAL CG2 C 15.38 . 1
243 . 30 VAL N N 109.31 . 1
244 . 31 ASP H H 8.61 . 1
245 . 31 ASP HA H 4.40 . 1
246 . 31 ASP HB2 H 2.47 . 1
247 . 31 ASP HB3 H 2.47 . 1
248 . 31 ASP CA C 53.83 . 1
249 . 31 ASP CB C 38.06 . 1
250 . 31 ASP N N 126.87 . 1
251 . 32 GLY H H 9.24 . 1
252 . 32 GLY HA2 H 3.98 . 2
253 . 32 GLY HA3 H 3.68 . 2
254 . 32 GLY CA C 43.80 . 1
255 . 32 GLY N N 117.79 . 1
256 . 33 TYR H H 7.78 . 1
257 . 33 TYR HA H 4.36 . 1
258 . 33 TYR HB2 H 3.18 . 2
259 . 33 TYR HB3 H 2.15 . 2
260 . 33 TYR HD1 H 6.77 . 1
261 . 33 TYR HD2 H 6.77 . 1
262 . 33 TYR HE1 H 6.58 . 1
263 . 33 TYR HE2 H 6.58 . 1
264 . 33 TYR CA C 54.40 . 1
265 . 33 TYR CB C 37.07 . 1
266 . 33 TYR CD1 C 131.50 . 1
267 . 33 TYR CD2 C 131.50 . 1
268 . 33 TYR CE1 C 115.63 . 1
269 . 33 TYR CE2 C 115.63 . 1
270 . 33 TYR N N 125.02 . 1
271 . 34 GLY H H 8.52 . 1
272 . 34 GLY HA2 H 3.77 . 2
273 . 34 GLY HA3 H 3.41 . 2
274 . 34 GLY CA C 44.37 . 1
275 . 34 GLY N N 120.21 . 1
276 . 35 GLY H H 8.92 . 1
277 . 35 GLY HA2 H 3.82 . 2
278 . 35 GLY HA3 H 3.73 . 2
279 . 35 GLY CA C 43.40 . 1
280 . 35 GLY N N 115.03 . 1
281 . 36 ALA H H 7.61 . 1
282 . 36 ALA HA H 4.08 . 1
283 . 36 ALA HB H 1.76 . 1
284 . 36 ALA CA C 50.67 . 1
285 . 36 ALA CB C 17.77 . 1
286 . 36 ALA N N 121.38 . 1
287 . 37 ILE H H 9.02 . 1
288 . 37 ILE HA H 4.62 . 1
289 . 37 ILE HB H 1.61 . 1
290 . 37 ILE HG12 H 1.17 . 1
291 . 37 ILE HG13 H 1.17 . 1
292 . 37 ILE HG2 H 0.94 . 1
293 . 37 ILE HD1 H 0.83 . 1
294 . 37 ILE CA C 58.12 . 1
295 . 37 ILE CB C 39.43 . 1
296 . 37 ILE CG1 C 23.89 . 1
297 . 37 ILE CG2 C 15.48 . 1
298 . 37 ILE CD1 C 11.07 . 1
299 . 37 ILE N N 122.41 . 1
300 . 38 TYR H H 8.74 . 1
301 . 38 TYR HA H 6.10 . 1
302 . 38 TYR HB2 H 3.01 . 2
303 . 38 TYR HB3 H 2.92 . 2
304 . 38 TYR HD1 H 6.89 . 1
305 . 38 TYR HD2 H 6.89 . 1
306 . 38 TYR HE1 H 6.95 . 1
307 . 38 TYR HE2 H 6.95 . 1
308 . 38 TYR CA C 53.32 . 1
309 . 38 TYR CB C 40.38 . 1
310 . 38 TYR CD1 C 131.38 . 1
311 . 38 TYR CD2 C 131.38 . 1
312 . 38 TYR CE1 C 116.19 . 1
313 . 38 TYR CE2 C 116.19 . 1
314 . 38 TYR N N 127.69 . 1
315 . 39 LYS H H 8.72 . 1
316 . 39 LYS HA H 4.00 . 1
317 . 39 LYS HB2 H 0.88 . 1
318 . 39 LYS HB3 H 0.47 . 1
319 . 39 LYS HG2 H 0.27 . 1
320 . 39 LYS HG3 H 0.27 . 1
321 . 39 LYS HD2 H 0.74 . 1
322 . 39 LYS HD3 H 0.74 . 1
323 . 39 LYS CA C 54.25 . 1
324 . 39 LYS CB C 34.73 . 1
325 . 39 LYS CG C 23.04 . 1
326 . 39 LYS CD C 28.60 . 1
327 . 39 LYS CE C 39.91 . 1
328 . 39 LYS N N 123.09 . 1
329 . 40 LYS H H 8.07 . 1
330 . 40 LYS HA H 4.52 . 1
331 . 40 LYS HB2 H 1.29 . 1
332 . 40 LYS HB3 H 1.29 . 1
333 . 40 LYS HG2 H 0.27 . 1
334 . 40 LYS HG3 H 0.27 . 1
335 . 40 LYS HD2 H 0.72 . 1
336 . 40 LYS HD3 H 0.72 . 1
337 . 40 LYS CA C 53.24 . 1
338 . 40 LYS CB C 32.22 . 1
339 . 40 LYS CG C 22.21 . 1
340 . 40 LYS CD C 28.60 . 1
341 . 40 LYS CE C 39.67 . 1
342 . 40 LYS N N 127.43 . 1
343 . 41 PHE H H 9.17 . 1
344 . 41 PHE HA H 4.73 . 1
345 . 41 PHE HB2 H 3.31 . 2
346 . 41 PHE HB3 H 2.59 . 2
347 . 41 PHE HD1 H 7.13 . 1
348 . 41 PHE HD2 H 7.13 . 1
349 . 41 PHE HE1 H 6.87 . 1
350 . 41 PHE HE2 H 6.87 . 1
351 . 41 PHE CA C 54.71 . 1
352 . 41 PHE CB C 42.59 . 1
353 . 41 PHE CD1 C 130.04 . 1
354 . 41 PHE CD2 C 130.04 . 1
355 . 41 PHE CE1 C 128.80 . 1
356 . 41 PHE CE2 C 128.80 . 1
357 . 41 PHE N N 124.96 . 1
358 . 42 ASN H H 9.11 . 1
359 . 42 ASN HA H 5.30 . 1
360 . 42 ASN HB2 H 2.90 . 1
361 . 42 ASN HB3 H 2.90 . 1
362 . 42 ASN CA C 50.74 . 1
363 . 42 ASN CB C 37.06 . 1
364 . 42 ASN N N 119.50 . 1
365 . 43 SER H H 7.37 . 1
366 . 43 SER HA H 4.72 . 1
367 . 43 SER HB2 H 4.01 . 2
368 . 43 SER HB3 H 3.72 . 2
369 . 43 SER CA C 53.61 . 1
370 . 43 SER CB C 63.48 . 1
371 . 43 SER N N 112.89 . 1
372 . 44 TYR H H 8.61 . 1
373 . 44 TYR HA H 2.86 . 1
374 . 44 TYR HB2 H 2.37 . 2
375 . 44 TYR HB3 H 2.14 . 2
376 . 44 TYR HD1 H 6.64 . 1
377 . 44 TYR HD2 H 6.64 . 1
378 . 44 TYR HE1 H 6.63 . 1
379 . 44 TYR HE2 H 6.63 . 1
380 . 44 TYR CA C 59.22 . 1
381 . 44 TYR CB C 35.92 . 1
382 . 44 TYR CD1 C 130.80 . 1
383 . 44 TYR CD2 C 130.80 . 1
384 . 44 TYR CE1 C 115.86 . 1
385 . 44 TYR CE2 C 115.86 . 1
386 . 44 TYR N N 130.00 . 1
387 . 45 GLU H H 8.68 . 1
388 . 45 GLU HA H 3.54 . 1
389 . 45 GLU HB2 H 1.78 . 1
390 . 45 GLU HB3 H 1.78 . 1
391 . 45 GLU HG2 H 2.20 . 1
392 . 45 GLU HG3 H 2.20 . 1
393 . 45 GLU CA C 57.43 . 1
394 . 45 GLU CB C 26.06 . 1
395 . 45 GLU CG C 32.62 . 1
396 . 45 GLU N N 118.98 . 1
397 . 46 GLN H H 7.31 . 1
398 . 46 GLN HA H 3.65 . 1
399 . 46 GLN HB2 H 1.72 . 1
400 . 46 GLN HB3 H 1.72 . 1
401 . 46 GLN HG2 H 2.20 . 1
402 . 46 GLN HG3 H 2.20 . 1
403 . 46 GLN CA C 56.04 . 1
404 . 46 GLN CB C 26.96 . 1
405 . 46 GLN CG C 32.37 . 1
406 . 46 GLN N N 119.92 . 1
407 . 47 ALA H H 6.92 . 1
408 . 47 ALA HA H 3.11 . 1
409 . 47 ALA HB H 1.10 . 1
410 . 47 ALA CA C 51.82 . 1
411 . 47 ALA CB C 15.84 . 1
412 . 47 ALA N N 124.75 . 1
413 . 48 LYS H H 8.17 . 1
414 . 48 LYS HA H 3.45 . 1
415 . 48 LYS HB2 H 1.43 . 2
416 . 48 LYS HB3 H 1.13 . 2
417 . 48 LYS HG2 H 1.02 . 1
418 . 48 LYS HG3 H 1.02 . 1
419 . 48 LYS HD2 H 0.32 . 1
420 . 48 LYS HD3 H 0.32 . 1
421 . 48 LYS CA C 57.74 . 1
422 . 48 LYS CB C 29.31 . 1
423 . 48 LYS CG C 26.35 . 1
424 . 48 LYS CD C 33.65 . 1
425 . 48 LYS CE C 36.36 . 1
426 . 48 LYS N N 119.86 . 1
427 . 49 SER H H 7.76 . 1
428 . 49 SER HA H 3.97 . 1
429 . 49 SER HB2 H 3.65 . 1
430 . 49 SER HB3 H 3.65 . 1
431 . 49 SER CA C 56.75 . 1
432 . 49 SER CB C 60.82 . 1
433 . 49 SER N N 117.13 . 1
434 . 50 PHE H H 7.42 . 1
435 . 50 PHE HA H 4.15 . 1
436 . 50 PHE HB2 H 3.00 . 2
437 . 50 PHE HB3 H 2.84 . 2
438 . 50 PHE HD1 H 7.29 . 1
439 . 50 PHE HD2 H 7.29 . 1
440 . 50 PHE HE1 H 7.18 . 1
441 . 50 PHE HE2 H 7.18 . 1
442 . 50 PHE HZ H 7.32 . 1
443 . 50 PHE CA C 58.28 . 1
444 . 50 PHE CB C 37.83 . 1
445 . 50 PHE CD1 C 129.45 . 1
446 . 50 PHE CD2 C 129.45 . 1
447 . 50 PHE CE1 C 129.90 . 1
448 . 50 PHE CE2 C 129.90 . 1
449 . 50 PHE CZ C 130.72 . 1
450 . 50 PHE N N 124.17 . 1
451 . 51 LEU H H 7.52 . 1
452 . 51 LEU HA H 3.72 . 1
453 . 51 LEU HB2 H 1.57 . 1
454 . 51 LEU HB3 H 1.65 . 1
455 . 51 LEU HG H 1.77 . 1
456 . 51 LEU HD1 H 0.76 . 2
457 . 51 LEU HD2 H 0.73 . 2
458 . 51 LEU CA C 54.14 . 1
459 . 51 LEU CB C 39.41 . 1
460 . 51 LEU CG C 24.73 . 1
461 . 51 LEU CD1 C 23.16 . 1
462 . 51 LEU CD2 C 21.26 . 1
463 . 51 LEU N N 118.71 . 1
464 . 52 GLY H H 7.53 . 1
465 . 52 GLY HA2 H 3.86 . 2
466 . 52 GLY HA3 H 3.67 . 2
467 . 52 GLY CA C 42.82 . 1
468 . 52 GLY N N 106.66 . 1
469 . 53 GLN H H 7.70 . 1
470 . 53 GLN HA H 4.45 . 1
471 . 53 GLN HB2 H 1.92 . 1
472 . 53 GLN HB3 H 1.73 . 1
473 . 53 GLN HG2 H 2.31 . 1
474 . 53 GLN HG3 H 2.31 . 1
475 . 53 GLN CA C 51.28 . 1
476 . 53 GLN CB C 26.34 . 1
477 . 53 GLN CG C 31.14 . 1
478 . 53 GLN N N 122.66 . 1
479 . 54 PRO HA H 4.53 . 1
480 . 54 PRO HB2 H 2.10 . 2
481 . 54 PRO HB3 H 1.80 . 2
482 . 54 PRO HG2 H 1.89 . 1
483 . 54 PRO HG3 H 1.89 . 1
484 . 54 PRO HD2 H 3.65 . 2
485 . 54 PRO HD3 H 3.53 . 2
486 . 54 PRO CA C 60.93 . 1
487 . 54 PRO CB C 30.05 . 1
488 . 54 PRO CG C 25.03 . 1
489 . 54 PRO CD C 48.32 . 1
490 . 55 ASN H H 8.55 . 1
491 . 55 ASN HA H 4.62 . 1
492 . 55 ASN HB2 H 2.73 . 2
493 . 55 ASN HB3 H 2.68 . 2
494 . 55 ASN CA C 51.01 . 1
495 . 55 ASN CB C 36.50 . 1
496 . 55 ASN N N 120.67 . 1
497 . 56 THR H H 8.13 . 1
498 . 56 THR HA H 4.36 . 1
499 . 56 THR HB H 4.23 . 1
500 . 56 THR HG2 H 1.24 . 1
501 . 56 THR CA C 59.03 . 1
502 . 56 THR CB C 67.28 . 1
503 . 56 THR CG2 C 19.37 . 1
504 . 56 THR N N 115.82 . 1
505 . 57 THR H H 8.22 . 1
506 . 57 THR HA H 4.31 . 1
507 . 57 THR HB H 4.18 . 1
508 . 57 THR HG2 H 1.04 . 1
509 . 57 THR CA C 60.25 . 1
510 . 57 THR CB C 68.25 . 1
511 . 57 THR CG2 C 19.48 . 1
512 . 57 THR N N 116.78 . 1
513 . 58 SER H H 8.30 . 1
514 . 58 SER HA H 4.32 . 1
515 . 58 SER HB2 H 3.69 . 1
516 . 58 SER HB3 H 3.69 . 1
517 . 58 SER CA C 55.64 . 1
518 . 58 SER CB C 61.35 . 1
519 . 58 SER N N 119.92 . 1
520 . 59 ASN H H 8.41 . 1
521 . 59 ASN HA H 4.62 . 1
522 . 59 ASN HB2 H 2.65 . 2
523 . 59 ASN HB3 H 2.59 . 2
524 . 59 ASN CA C 51.03 . 1
525 . 59 ASN CB C 36.29 . 1
526 . 59 ASN N N 122.75 . 1
527 . 60 TYR H H 8.20 . 1
528 . 60 TYR HA H 4.44 . 1
529 . 60 TYR HB2 H 3.00 . 2
530 . 60 TYR HB3 H 2.84 . 2
531 . 60 TYR HD1 H 7.10 . 1
532 . 60 TYR HD2 H 7.10 . 1
533 . 60 TYR HE1 H 6.80 . 1
534 . 60 TYR HE2 H 6.80 . 1
535 . 60 TYR CA C 56.00 . 1
536 . 60 TYR CB C 36.29 . 1
537 . 60 TYR CD1 C 131.19 . 1
538 . 60 TYR CD2 C 131.19 . 1
539 . 60 TYR CE1 C 116.07 . 1
540 . 60 TYR CE2 C 116.07 . 1
541 . 60 TYR N N 122.90 . 1
542 . 61 GLY H H 8.31 . 1
543 . 61 GLY HA2 H 3.82 . 1
544 . 61 GLY HA3 H 3.82 . 1
545 . 61 GLY CA C 42.90 . 1
546 . 61 GLY N N 112.94 . 1
547 . 62 SER H H 8.14 . 1
548 . 62 SER HA H 4.43 . 1
549 . 62 SER HB2 H 3.78 . 1
550 . 62 SER HB3 H 3.78 . 1
551 . 62 SER CA C 56.28 . 1
552 . 62 SER CB C 62.43 . 1
553 . 62 SER N N 117.90 . 1
554 . 63 SER H H 8.12 . 1
555 . 63 SER HA H 4.40 . 1
556 . 63 SER HB2 H 2.91 . 1
557 . 63 SER HB3 H 2.91 . 1
558 . 63 SER CA C 57.48 . 1
559 . 63 SER N N 124.09 . 1
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