data_4996
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR-Based Structure of the Conserved Protein MTH865 from the Archea
Methanobacterium thermoautotrophicum
;
_BMRB_accession_number 4996
_BMRB_flat_file_name bmr4996.str
_Entry_type original
_Submission_date 2001-04-20
_Accession_date 2001-04-23
_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 Lee Gregory M. .
2 Edwards Aled M. .
3 Arrowsmith Cheryl H. .
4 McIntosh Lawrence P. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 442
"13C chemical shifts" 324
"15N chemical shifts" 81
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-10-08 original author .
stop_
_Original_release_date 2001-10-08
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the Editor: NMR-Based Structure of the Conserved Protein MTH865 from
the Archaeon Methanobacterium thermoautotrophicum
;
_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 Lee Gregory M. .
2 Edwards Aled M. .
3 Arrowsmith Cheryl H. .
4 McIntosh Lawrence P. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 21
_Journal_issue 1
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 63
_Page_last 66
_Year 2001
_Details .
loop_
_Keyword
'helical bundle'
'heternuclear NMR'
'structural proteomics'
'Methanobacterium thermoautotrophicum'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_MTH865
_Saveframe_category molecular_system
_Mol_system_name MTH865
_Abbreviation_common MTH865
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
MTH865 $MTH865
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all free'
loop_
_Biological_function
'conserved archeal protein'
'unknown function'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_MTH865
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Methanobacterium thermoautotrophicum open reading frame 865'
_Abbreviation_common MTH865
_Molecular_mass 8675
_Mol_thiol_state 'all free'
_Details
;
Includes GSH at N-terminal from proteolytic
cleavage of His6-affinity tag.
;
##############################
# Polymer residue sequence #
##############################
_Residue_count 84
_Mol_residue_sequence
;
GSHMKMGVKEDIRGQIIGAL
AGADFPINSPEELMAALPNG
PDTTCKSGDVELKASDAGQV
LTADDFPFKSAEEVADTIVN
KAGL
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 -3 GLY 2 -2 SER 3 -1 HIS 4 1 MET 5 2 LYS
6 3 MET 7 4 GLY 8 5 VAL 9 6 LYS 10 7 GLU
11 8 ASP 12 9 ILE 13 10 ARG 14 11 GLY 15 12 GLN
16 13 ILE 17 14 ILE 18 15 GLY 19 16 ALA 20 17 LEU
21 18 ALA 22 19 GLY 23 20 ALA 24 21 ASP 25 22 PHE
26 23 PRO 27 24 ILE 28 25 ASN 29 26 SER 30 27 PRO
31 28 GLU 32 29 GLU 33 30 LEU 34 31 MET 35 32 ALA
36 33 ALA 37 34 LEU 38 35 PRO 39 36 ASN 40 37 GLY
41 38 PRO 42 39 ASP 43 40 THR 44 41 THR 45 42 CYS
46 43 LYS 47 44 SER 48 45 GLY 49 46 ASP 50 47 VAL
51 48 GLU 52 49 LEU 53 50 LYS 54 51 ALA 55 52 SER
56 53 ASP 57 54 ALA 58 55 GLY 59 56 GLN 60 57 VAL
61 58 LEU 62 59 THR 63 60 ALA 64 61 ASP 65 62 ASP
66 63 PHE 67 64 PRO 68 65 PHE 69 66 LYS 70 67 SER
71 68 ALA 72 69 GLU 73 70 GLU 74 71 VAL 75 72 ALA
76 73 ASP 77 74 THR 78 75 ILE 79 76 VAL 80 77 ASN
81 78 LYS 82 79 ALA 83 80 GLY 84 81 LEU
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 1IIO "Nmr-Based Structure Of The Conserved Protein Mth865 From The Archea Methanobacterium Thermoautotrophicum" 100.00 84 100.00 100.00 2.32e-52
DBJ BAM70032 "conserved hypothetical protein [Methanothermobacter thermautotrophicus CaT2]" 94.05 79 100.00 100.00 6.20e-48
EMBL CAA48863 "unnamed protein product [Methanothermobacter thermautotrophicus]" 94.05 79 100.00 100.00 6.20e-48
EMBL CAA48865 "unnamed protein product [Methanothermobacter thermautotrophicus]" 94.05 79 100.00 100.00 6.20e-48
GB AAB85363 "conserved protein [Methanothermobacter thermautotrophicus str. Delta H]" 96.43 81 100.00 100.00 1.47e-49
REF NP_276002 "hypothetical protein MTH865 [Methanothermobacter thermautotrophicus str. Delta H]" 96.43 81 100.00 100.00 1.47e-49
REF WP_010876498 "hypothetical protein [Methanothermobacter thermautotrophicus]" 96.43 81 100.00 100.00 1.47e-49
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$MTH865 'Methanothermobacter thermautotrophicus' 145262 Archaea Euryarchaeota Methanothermobacter thermautotrophicus
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_type
_Vector_name
$MTH865 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET15b
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_15N-labeled_sample
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$MTH865 0.5 mM '[U-100% 15N]'
stop_
save_
save_13C_15N-labeled_sample
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$MTH865 0.5 mM '[U-100% 13C; U-100% 15N]'
stop_
save_
save_10%_13C-labeled_sample
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$MTH865 0.5 mM '[U-10% 13C; U-100% 15N]'
stop_
save_
############################
# Computer software used #
############################
save_Felix
_Saveframe_category software
_Name Felix
_Version 2000
loop_
_Task
'raw data processing'
'peak picking'
'peak assignments'
stop_
_Details
;
Molecular Simulations, Inc.,
San Diego, CA
;
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UNITY
_Field_strength 500
_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 Varian
_Model INOVA
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_500MHz_Unity_housed_at_Univ._of_British_Columbia_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '500MHz Unity housed at Univ. of British Columbia'
_Sample_label .
save_
save_600MHz_INOVA_housed_at_Univ._of_Toronto_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '600MHz INOVA housed at Univ. of Toronto'
_Sample_label .
save_
save_800MHz_INOVA_housed_at_Univ._of_Alberta_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '800MHz INOVA housed at Univ. of Alberta'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_condition_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.51 0.05 n/a
temperature 303 2 K
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_shifts
_Saveframe_category assigned_chemical_shifts
_Details 'Residues Gly-3 to Met1 unobserved in the spectra.'
loop_
_Sample_label
$15N-labeled_sample
$13C_15N-labeled_sample
$10%_13C-labeled_sample
stop_
_Sample_conditions_label $condition_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name MTH865
_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 . 5 LYS H H 8.411 0.020 1
2 . 5 LYS HA H 4.302 0.020 1
3 . 5 LYS HB2 H 1.846 0.020 2
4 . 5 LYS HB3 H 1.779 0.020 2
5 . 5 LYS HG2 H 1.446 0.020 2
6 . 5 LYS HG3 H 1.498 0.020 2
7 . 5 LYS HD2 H 1.712 0.020 1
8 . 5 LYS HD3 H 1.712 0.020 1
9 . 5 LYS HE2 H 3.074 0.020 1
10 . 5 LYS HE3 H 3.074 0.020 1
11 . 5 LYS C C 176.445 0.300 1
12 . 5 LYS CA C 56.225 0.300 1
13 . 5 LYS CB C 33.012 0.300 1
14 . 5 LYS CG C 24.058 0.300 1
15 . 5 LYS CD C 29.065 0.300 1
16 . 5 LYS CE C 42.304 0.300 1
17 . 5 LYS N N 122.806 0.200 1
18 . 6 MET H H 8.391 0.020 1
19 . 6 MET HA H 4.413 0.020 1
20 . 6 MET HB2 H 2.025 0.020 1
21 . 6 MET HB3 H 2.025 0.020 1
22 . 6 MET HG2 H 2.567 0.020 1
23 . 6 MET HG3 H 2.567 0.020 1
24 . 6 MET HE H 2.069 0.020 1
25 . 6 MET C C 176.610 0.300 1
26 . 6 MET CA C 56.031 0.300 1
27 . 6 MET CB C 33.645 0.300 1
28 . 6 MET CG C 31.965 0.300 1
29 . 6 MET CE C 17.131 0.300 1
30 . 6 MET N N 122.119 0.200 1
31 . 7 GLY H H 8.545 0.020 1
32 . 7 GLY HA2 H 4.012 0.020 2
33 . 7 GLY HA3 H 4.101 0.020 2
34 . 7 GLY C C 175.346 0.300 1
35 . 7 GLY CA C 45.254 0.300 1
36 . 7 GLY N N 110.963 0.200 1
37 . 8 VAL H H 7.964 0.020 1
38 . 8 VAL HA H 3.864 0.020 1
39 . 8 VAL HB H 2.069 0.020 1
40 . 8 VAL HG1 H 0.975 0.020 1
41 . 8 VAL HG2 H 1.064 0.020 1
42 . 8 VAL C C 177.882 0.300 1
43 . 8 VAL CA C 65.460 0.300 1
44 . 8 VAL CB C 32.300 0.300 1
45 . 8 VAL CG1 C 21.746 0.300 1
46 . 8 VAL CG2 C 22.118 0.300 1
47 . 8 VAL N N 120.588 0.200 1
48 . 9 LYS H H 8.358 0.020 1
49 . 9 LYS HA H 3.605 0.020 1
50 . 9 LYS HB2 H 1.824 0.020 2
51 . 9 LYS HB3 H 1.758 0.020 2
52 . 9 LYS HG2 H 1.198 0.020 2
53 . 9 LYS HG3 H 1.148 0.020 2
54 . 9 LYS HD2 H 1.644 0.020 1
55 . 9 LYS HD3 H 1.644 0.020 1
56 . 9 LYS HE2 H 2.737 0.020 2
57 . 9 LYS HE3 H 2.895 0.020 2
58 . 9 LYS C C 177.533 0.300 1
59 . 9 LYS CA C 60.818 0.300 1
60 . 9 LYS CB C 32.401 0.300 1
61 . 9 LYS CG C 25.152 0.300 1
62 . 9 LYS CD C 29.537 0.300 1
63 . 9 LYS CE C 42.297 0.300 1
64 . 9 LYS N N 119.275 0.200 1
65 . 10 GLU H H 8.192 0.020 1
66 . 10 GLU HA H 3.915 0.020 1
67 . 10 GLU HB2 H 2.001 0.020 1
68 . 10 GLU HB3 H 2.001 0.020 1
69 . 10 GLU HG2 H 2.287 0.020 2
70 . 10 GLU HG3 H 2.443 0.020 2
71 . 10 GLU C C 179.161 0.300 1
72 . 10 GLU CA C 59.310 0.300 1
73 . 10 GLU CB C 29.211 0.300 1
74 . 10 GLU CG C 36.816 0.300 1
75 . 10 GLU N N 116.650 0.200 1
76 . 11 ASP H H 8.213 0.020 1
77 . 11 ASP HA H 4.503 0.020 1
78 . 11 ASP HB2 H 2.905 0.020 2
79 . 11 ASP HB3 H 2.805 0.020 2
80 . 11 ASP C C 179.048 0.300 1
81 . 11 ASP CA C 56.317 0.300 1
82 . 11 ASP CB C 41.281 0.300 1
83 . 11 ASP N N 121.463 0.200 1
84 . 12 ILE H H 8.587 0.020 1
85 . 12 ILE HA H 3.386 0.020 1
86 . 12 ILE HB H 1.891 0.020 1
87 . 12 ILE HG12 H 1.094 0.020 2
88 . 12 ILE HG13 H 1.504 0.020 2
89 . 12 ILE HG2 H 0.658 0.020 1
90 . 12 ILE HD1 H 0.529 0.020 1
91 . 12 ILE C C 177.422 0.300 1
92 . 12 ILE CA C 64.840 0.300 1
93 . 12 ILE CB C 35.879 0.300 1
94 . 12 ILE CG1 C 29.517 0.300 1
95 . 12 ILE CG2 C 17.548 0.300 1
96 . 12 ILE CD1 C 11.702 0.300 1
97 . 12 ILE N N 119.306 0.200 1
98 . 13 ARG H H 8.557 0.020 1
99 . 13 ARG HA H 3.654 0.020 1
100 . 13 ARG HB2 H 1.891 0.020 1
101 . 13 ARG HB3 H 1.980 0.020 1
102 . 13 ARG HG2 H 1.399 0.020 1
103 . 13 ARG HG3 H 1.399 0.020 1
104 . 13 ARG HD2 H 3.211 0.020 2
105 . 13 ARG HD3 H 3.065 0.020 2
106 . 13 ARG HE H 6.516 0.020 1
107 . 13 ARG C C 178.118 0.300 1
108 . 13 ARG CA C 60.449 0.300 1
109 . 13 ARG CB C 30.691 0.300 1
110 . 13 ARG CG C 28.301 0.300 1
111 . 13 ARG CD C 43.346 0.300 1
112 . 13 ARG N N 119.650 0.200 1
113 . 13 ARG NE N 113.835 0.200 1
114 . 14 GLY H H 7.994 0.020 1
115 . 14 GLY HA2 H 4.146 0.020 2
116 . 14 GLY HA3 H 3.788 0.020 2
117 . 14 GLY C C 177.366 0.300 1
118 . 14 GLY CA C 47.162 0.300 1
119 . 14 GLY N N 103.900 0.200 1
120 . 15 GLN H H 8.158 0.020 1
121 . 15 GLN HA H 4.180 0.020 1
122 . 15 GLN HB2 H 2.148 0.020 1
123 . 15 GLN HB3 H 2.337 0.020 1
124 . 15 GLN HG2 H 2.672 0.020 2
125 . 15 GLN HG3 H 2.394 0.020 2
126 . 15 GLN HE21 H 7.238 0.020 1
127 . 15 GLN HE22 H 7.070 0.020 1
128 . 15 GLN C C 179.427 0.300 1
129 . 15 GLN CA C 58.864 0.300 1
130 . 15 GLN CB C 29.795 0.300 1
131 . 15 GLN CG C 35.168 0.300 1
132 . 15 GLN N N 122.931 0.200 1
133 . 15 GLN NE2 N 112.494 0.200 1
134 . 16 ILE H H 8.292 0.020 1
135 . 16 ILE HA H 3.418 0.020 1
136 . 16 ILE HB H 1.882 0.020 1
137 . 16 ILE HG12 H 2.025 0.020 1
138 . 16 ILE HG13 H 2.025 0.020 1
139 . 16 ILE HG2 H 0.640 0.020 1
140 . 16 ILE HD1 H 0.685 0.020 1
141 . 16 ILE C C 176.821 0.300 1
142 . 16 ILE CA C 65.809 0.300 1
143 . 16 ILE CB C 37.740 0.300 1
144 . 16 ILE CG1 C 29.667 0.300 1
145 . 16 ILE CG2 C 17.608 0.300 1
146 . 16 ILE CD1 C 14.605 0.300 1
147 . 16 ILE N N 122.440 0.200 1
148 . 17 ILE H H 7.860 0.020 1
149 . 17 ILE HA H 3.364 0.020 1
150 . 17 ILE HB H 1.801 0.020 1
151 . 17 ILE HG12 H 1.742 0.020 2
152 . 17 ILE HG13 H 0.512 0.020 2
153 . 17 ILE HG2 H 0.822 0.020 1
154 . 17 ILE HD1 H 0.819 0.020 1
155 . 17 ILE C C 179.497 0.300 1
156 . 17 ILE CA C 66.327 0.300 1
157 . 17 ILE CB C 38.377 0.300 1
158 . 17 ILE CG1 C 30.239 0.300 1
159 . 17 ILE CG2 C 17.417 0.300 1
160 . 17 ILE CD1 C 14.616 0.300 1
161 . 17 ILE N N 118.088 0.200 1
162 . 18 GLY H H 8.234 0.020 1
163 . 18 GLY HA2 H 3.878 0.020 1
164 . 18 GLY HA3 H 3.878 0.020 1
165 . 18 GLY C C 176.565 0.300 1
166 . 18 GLY CA C 47.072 0.300 1
167 . 18 GLY N N 105.306 0.200 1
168 . 19 ALA H H 7.933 0.020 1
169 . 19 ALA HA H 4.257 0.020 1
170 . 19 ALA HB H 1.446 0.020 1
171 . 19 ALA C C 178.025 0.300 1
172 . 19 ALA CA C 53.755 0.300 1
173 . 19 ALA CB C 18.355 0.300 1
174 . 19 ALA N N 123.744 0.200 1
175 . 20 LEU H H 7.288 0.020 1
176 . 20 LEU HA H 4.493 0.020 1
177 . 20 LEU HB2 H 1.820 0.020 1
178 . 20 LEU HB3 H 1.945 0.020 1
179 . 20 LEU HG H 1.690 0.020 1
180 . 20 LEU HD1 H 0.819 0.020 1
181 . 20 LEU HD2 H 0.707 0.020 1
182 . 20 LEU C C 177.031 0.300 1
183 . 20 LEU CA C 53.635 0.300 1
184 . 20 LEU CB C 43.345 0.300 1
185 . 20 LEU CG C 27.535 0.300 1
186 . 20 LEU CD1 C 27.266 0.300 1
187 . 20 LEU CD2 C 23.594 0.300 1
188 . 20 LEU N N 115.369 0.200 1
189 . 21 ALA H H 7.404 0.020 1
190 . 21 ALA HA H 4.257 0.020 1
191 . 21 ALA HB H 1.529 0.020 1
192 . 21 ALA C C 179.003 0.300 1
193 . 21 ALA CA C 54.857 0.300 1
194 . 21 ALA CB C 18.823 0.300 1
195 . 21 ALA N N 123.775 0.200 1
196 . 22 GLY H H 8.711 0.020 1
197 . 22 GLY HA2 H 4.190 0.020 2
198 . 22 GLY HA3 H 3.855 0.020 2
199 . 22 GLY C C 174.258 0.300 1
200 . 22 GLY CA C 44.889 0.300 1
201 . 22 GLY N N 107.963 0.200 1
202 . 23 ALA H H 7.653 0.020 1
203 . 23 ALA HA H 4.235 0.020 1
204 . 23 ALA HB H 1.197 0.020 1
205 . 23 ALA C C 176.173 0.300 1
206 . 23 ALA CA C 51.880 0.300 1
207 . 23 ALA CB C 20.222 0.300 1
208 . 23 ALA N N 123.337 0.200 1
209 . 24 ASP H H 8.317 0.020 1
210 . 24 ASP HA H 4.738 0.020 1
211 . 24 ASP HB2 H 2.446 0.020 1
212 . 24 ASP HB3 H 2.585 0.020 1
213 . 24 ASP C C 173.867 0.300 1
214 . 24 ASP CA C 53.679 0.300 1
215 . 24 ASP CB C 41.519 0.300 1
216 . 24 ASP N N 120.463 0.200 1
217 . 25 PHE H H 8.192 0.020 1
218 . 25 PHE HA H 4.168 0.020 1
219 . 25 PHE HB2 H 2.739 0.020 1
220 . 25 PHE HB3 H 2.899 0.020 1
221 . 25 PHE HD1 H 7.240 0.020 1
222 . 25 PHE HD2 H 7.240 0.020 1
223 . 25 PHE HE1 H 7.105 0.020 1
224 . 25 PHE HE2 H 7.105 0.020 1
225 . 25 PHE HZ H 6.906 0.020 1
226 . 25 PHE CA C 56.830 0.300 1
227 . 25 PHE CB C 40.666 0.300 1
228 . 25 PHE CD1 C 131.894 0.300 1
229 . 25 PHE CD2 C 131.894 0.300 1
230 . 25 PHE CE1 C 130.758 0.300 1
231 . 25 PHE CE2 C 130.758 0.300 1
232 . 25 PHE CZ C 127.833 0.300 1
233 . 25 PHE N N 120.119 0.200 1
234 . 26 PRO HA H 5.128 0.020 1
235 . 26 PRO HB2 H 2.417 0.020 2
236 . 26 PRO HB3 H 2.063 0.020 2
237 . 26 PRO HG2 H 2.002 0.020 1
238 . 26 PRO HG3 H 2.002 0.020 1
239 . 26 PRO HD2 H 3.709 0.020 2
240 . 26 PRO HD3 H 3.637 0.020 2
241 . 26 PRO C C 174.973 0.300 1
242 . 26 PRO CA C 62.145 0.300 1
243 . 26 PRO CB C 35.826 0.300 1
244 . 26 PRO CG C 25.377 0.300 1
245 . 26 PRO CD C 50.835 0.300 1
246 . 27 ILE H H 8.649 0.020 1
247 . 27 ILE HA H 4.436 0.020 1
248 . 27 ILE HB H 1.868 0.020 1
249 . 27 ILE HG12 H 0.865 0.020 2
250 . 27 ILE HG13 H 1.260 0.020 2
251 . 27 ILE HG2 H 1.177 0.020 1
252 . 27 ILE HD1 H 0.429 0.020 1
253 . 27 ILE C C 177.070 0.300 1
254 . 27 ILE CA C 61.182 0.300 1
255 . 27 ILE CB C 40.030 0.300 1
256 . 27 ILE CG1 C 27.496 0.300 1
257 . 27 ILE CG2 C 18.236 0.300 1
258 . 27 ILE CD1 C 13.930 0.300 1
259 . 27 ILE N N 119.931 0.200 1
260 . 28 ASN H H 9.313 0.020 1
261 . 28 ASN HA H 4.888 0.020 1
262 . 28 ASN HB2 H 2.918 0.020 1
263 . 28 ASN HB3 H 2.784 0.020 1
264 . 28 ASN HD21 H 8.006 0.020 1
265 . 28 ASN HD22 H 6.532 0.020 1
266 . 28 ASN C C 174.223 0.300 1
267 . 28 ASN CA C 55.160 0.300 1
268 . 28 ASN CB C 40.966 0.300 1
269 . 28 ASN N N 124.962 0.200 1
270 . 28 ASN ND2 N 113.806 0.200 1
271 . 29 SER H H 7.404 0.020 1
272 . 29 SER HA H 3.932 0.020 1
273 . 29 SER HB2 H 4.041 0.020 1
274 . 29 SER HB3 H 3.654 0.020 1
275 . 29 SER CA C 55.719 0.300 1
276 . 29 SER CB C 64.000 0.300 1
277 . 29 SER N N 112.775 0.200 1
278 . 30 PRO HA H 4.123 0.020 1
279 . 30 PRO HB2 H 1.965 0.020 2
280 . 30 PRO HB3 H 2.380 0.020 2
281 . 30 PRO HG2 H 2.090 0.020 2
282 . 30 PRO HG3 H 1.824 0.020 2
283 . 30 PRO HD2 H 3.587 0.020 1
284 . 30 PRO HD3 H 3.587 0.020 1
285 . 30 PRO C C 177.821 0.300 1
286 . 30 PRO CA C 65.216 0.300 1
287 . 30 PRO CB C 31.696 0.300 1
288 . 30 PRO CG C 27.500 0.300 1
289 . 30 PRO CD C 50.352 0.300 1
290 . 31 GLU H H 8.659 0.020 1
291 . 31 GLU HA H 3.922 0.020 1
292 . 31 GLU HB2 H 2.017 0.020 1
293 . 31 GLU HB3 H 1.877 0.020 1
294 . 31 GLU HG2 H 2.408 0.020 2
295 . 31 GLU HG3 H 2.214 0.020 2
296 . 31 GLU C C 180.003 0.300 1
297 . 31 GLU CA C 60.643 0.300 1
298 . 31 GLU CB C 28.675 0.300 1
299 . 31 GLU CG C 37.132 0.300 1
300 . 31 GLU N N 117.556 0.200 1
301 . 32 GLU H H 7.653 0.020 1
302 . 32 GLU HA H 4.023 0.020 1
303 . 32 GLU HB2 H 2.100 0.020 1
304 . 32 GLU HB3 H 2.203 0.020 1
305 . 32 GLU HG2 H 2.339 0.020 1
306 . 32 GLU HG3 H 2.339 0.020 1
307 . 32 GLU C C 179.002 0.300 1
308 . 32 GLU CA C 58.754 0.300 1
309 . 32 GLU CB C 31.001 0.300 1
310 . 32 GLU CG C 37.308 0.300 1
311 . 32 GLU N N 119.869 0.200 1
312 . 33 LEU H H 7.891 0.020 1
313 . 33 LEU HA H 4.079 0.020 1
314 . 33 LEU HB2 H 2.449 0.020 2
315 . 33 LEU HB3 H 1.556 0.020 2
316 . 33 LEU HG H 1.569 0.020 1
317 . 33 LEU HD1 H 0.874 0.020 1
318 . 33 LEU HD2 H 0.863 0.020 1
319 . 33 LEU C C 177.063 0.300 1
320 . 33 LEU CA C 58.210 0.300 1
321 . 33 LEU CB C 41.659 0.300 1
322 . 33 LEU CG C 27.572 0.300 1
323 . 33 LEU CD1 C 24.090 0.300 1
324 . 33 LEU CD2 C 26.091 0.300 1
325 . 33 LEU N N 121.431 0.200 1
326 . 34 MET H H 8.151 0.020 1
327 . 34 MET HA H 4.146 0.020 1
328 . 34 MET HB2 H 2.235 0.020 1
329 . 34 MET HB3 H 1.675 0.020 1
330 . 34 MET HG2 H 2.920 0.020 2
331 . 34 MET HG3 H 2.784 0.020 2
332 . 34 MET HE H 2.028 0.020 1
333 . 34 MET C C 178.696 0.300 1
334 . 34 MET CA C 56.933 0.300 1
335 . 34 MET CB C 32.588 0.300 1
336 . 34 MET CG C 33.248 0.300 1
337 . 34 MET CE C 18.533 0.300 1
338 . 34 MET N N 113.744 0.200 1
339 . 35 ALA H H 7.528 0.020 1
340 . 35 ALA HA H 4.168 0.020 1
341 . 35 ALA HB H 1.437 0.020 1
342 . 35 ALA C C 178.106 0.300 1
343 . 35 ALA CA C 53.520 0.300 1
344 . 35 ALA CB C 18.823 0.300 1
345 . 35 ALA N N 117.650 0.200 1
346 . 36 ALA H H 7.362 0.020 1
347 . 36 ALA HA H 4.212 0.020 1
348 . 36 ALA HB H 1.405 0.020 1
349 . 36 ALA C C 177.410 0.300 1
350 . 36 ALA CA C 52.348 0.300 1
351 . 36 ALA CB C 19.937 0.300 1
352 . 36 ALA N N 118.931 0.200 1
353 . 37 LEU H H 7.072 0.020 1
354 . 37 LEU HA H 4.584 0.020 1
355 . 37 LEU HB2 H 1.724 0.020 1
356 . 37 LEU HB3 H 1.599 0.020 1
357 . 37 LEU HG H 2.069 0.020 1
358 . 37 LEU HD1 H 0.738 0.020 1
359 . 37 LEU HD2 H 0.693 0.020 1
360 . 37 LEU CA C 52.466 0.300 1
361 . 37 LEU CB C 41.897 0.300 1
362 . 37 LEU CG C 25.982 0.300 1
363 . 37 LEU CD1 C 27.964 0.300 1
364 . 37 LEU CD2 C 23.595 0.300 1
365 . 37 LEU N N 117.890 0.200 1
366 . 38 PRO HA H 4.358 0.020 1
367 . 38 PRO HB2 H 2.476 0.020 2
368 . 38 PRO HB3 H 1.947 0.020 2
369 . 38 PRO HG2 H 2.270 0.020 2
370 . 38 PRO HG3 H 2.203 0.020 2
371 . 38 PRO HD2 H 3.605 0.020 2
372 . 38 PRO HD3 H 4.324 0.020 2
373 . 38 PRO C C 177.328 0.300 1
374 . 38 PRO CA C 65.437 0.300 1
375 . 38 PRO CB C 32.195 0.300 1
376 . 38 PRO CG C 27.721 0.300 1
377 . 38 PRO CD C 50.633 0.300 1
378 . 39 ASN H H 7.528 0.020 1
379 . 39 ASN HA H 5.240 0.020 1
380 . 39 ASN HB2 H 2.248 0.020 1
381 . 39 ASN HB3 H 2.971 0.020 1
382 . 39 ASN HD21 H 7.494 0.020 1
383 . 39 ASN HD22 H 6.914 0.020 1
384 . 39 ASN C C 175.898 0.300 1
385 . 39 ASN CA C 51.199 0.300 1
386 . 39 ASN CB C 39.756 0.300 1
387 . 39 ASN N N 112.978 0.200 1
388 . 39 ASN ND2 N 111.681 0.200 1
389 . 40 GLY H H 7.653 0.020 1
390 . 40 GLY HA2 H 4.391 0.020 1
391 . 40 GLY HA3 H 4.190 0.020 1
392 . 40 GLY CA C 45.367 0.300 1
393 . 40 GLY N N 108.869 0.200 1
394 . 41 PRO HA H 4.352 0.020 1
395 . 41 PRO HB2 H 2.471 0.020 2
396 . 41 PRO HB3 H 1.951 0.020 2
397 . 41 PRO HG2 H 2.069 0.020 2
398 . 41 PRO HG3 H 1.962 0.020 2
399 . 41 PRO HD2 H 4.034 0.020 2
400 . 41 PRO HD3 H 3.632 0.020 2
401 . 41 PRO C C 175.173 0.300 1
402 . 41 PRO CA C 64.437 0.300 1
403 . 41 PRO CB C 32.208 0.300 1
404 . 41 PRO CG C 27.111 0.300 1
405 . 41 PRO CD C 51.226 0.300 1
406 . 42 ASP H H 7.321 0.020 1
407 . 42 ASP HA H 4.669 0.020 1
408 . 42 ASP HB2 H 2.627 0.020 1
409 . 42 ASP HB3 H 2.895 0.020 1
410 . 42 ASP C C 176.231 0.300 1
411 . 42 ASP CA C 54.561 0.300 1
412 . 42 ASP CB C 41.326 0.300 1
413 . 42 ASP N N 114.088 0.200 1
414 . 43 THR H H 7.715 0.020 1
415 . 43 THR HA H 4.092 0.020 1
416 . 43 THR HB H 4.012 0.020 1
417 . 43 THR HG2 H 1.260 0.020 1
418 . 43 THR CA C 65.044 0.300 1
419 . 43 THR CB C 69.115 0.300 1
420 . 43 THR CG2 C 20.641 0.300 1
421 . 43 THR N N 119.369 0.200 1
422 . 44 THR H H 9.085 0.020 1
423 . 44 THR HA H 5.079 0.020 1
424 . 44 THR HB H 3.958 0.020 1
425 . 44 THR HG2 H 1.064 0.020 1
426 . 44 THR CA C 61.301 0.300 1
427 . 44 THR CB C 71.296 0.300 1
428 . 44 THR CG2 C 21.435 0.300 1
429 . 44 THR N N 123.650 0.200 1
430 . 45 CYS H H 8.732 0.020 1
431 . 45 CYS HA H 4.694 0.020 1
432 . 45 CYS HB2 H 2.583 0.020 1
433 . 45 CYS HB3 H 2.717 0.020 1
434 . 45 CYS C C 181.200 0.300 1
435 . 45 CYS CA C 57.558 0.300 1
436 . 45 CYS CB C 30.433 0.300 1
437 . 45 CYS N N 124.556 0.200 1
438 . 46 LYS H H 8.617 0.020 1
439 . 46 LYS HA H 5.266 0.020 1
440 . 46 LYS HB2 H 1.757 0.020 2
441 . 46 LYS HB3 H 1.608 0.020 2
442 . 46 LYS HG2 H 1.232 0.020 1
443 . 46 LYS HG3 H 1.232 0.020 1
444 . 46 LYS HD2 H 1.623 0.020 2
445 . 46 LYS HD3 H 1.658 0.020 2
446 . 46 LYS HE2 H 2.962 0.020 2
447 . 46 LYS HE3 H 2.902 0.020 2
448 . 46 LYS C C 175.554 0.300 1
449 . 46 LYS CA C 55.153 0.300 1
450 . 46 LYS CB C 36.598 0.300 1
451 . 46 LYS CG C 25.017 0.300 1
452 . 46 LYS CD C 29.604 0.300 1
453 . 46 LYS CE C 42.298 0.300 1
454 . 46 LYS N N 123.244 0.200 1
455 . 47 SER H H 8.836 0.020 1
456 . 47 SER HA H 4.436 0.020 1
457 . 47 SER HB2 H 3.647 0.020 1
458 . 47 SER HB3 H 3.431 0.020 1
459 . 47 SER C C 174.599 0.300 1
460 . 47 SER CA C 57.595 0.300 1
461 . 47 SER CB C 63.405 0.300 1
462 . 47 SER N N 120.994 0.200 1
463 . 48 GLY H H 9.043 0.020 1
464 . 48 GLY HA2 H 3.945 0.020 2
465 . 48 GLY HA3 H 3.654 0.020 2
466 . 48 GLY C C 174.784 0.300 1
467 . 48 GLY CA C 47.333 0.300 1
468 . 48 GLY N N 117.806 0.200 1
469 . 49 ASP H H 8.753 0.020 1
470 . 49 ASP HA H 4.686 0.020 1
471 . 49 ASP HB2 H 2.650 0.020 1
472 . 49 ASP HB3 H 2.806 0.020 1
473 . 49 ASP C C 175.710 0.300 1
474 . 49 ASP CA C 54.277 0.300 1
475 . 49 ASP CB C 41.064 0.300 1
476 . 49 ASP N N 125.994 0.200 1
477 . 50 VAL H H 8.268 0.020 1
478 . 50 VAL HA H 4.041 0.020 1
479 . 50 VAL HB H 2.248 0.020 1
480 . 50 VAL HG1 H 0.774 0.020 1
481 . 50 VAL HG2 H 1.031 0.020 1
482 . 50 VAL C C 174.074 0.300 1
483 . 50 VAL CA C 62.956 0.300 1
484 . 50 VAL CB C 32.638 0.300 1
485 . 50 VAL CG1 C 20.938 0.300 1
486 . 50 VAL CG2 C 21.847 0.300 1
487 . 50 VAL N N 122.620 0.200 1
488 . 51 GLU H H 8.400 0.020 1
489 . 51 GLU HA H 4.927 0.020 1
490 . 51 GLU HB2 H 1.860 0.020 2
491 . 51 GLU HB3 H 1.779 0.020 2
492 . 51 GLU HG2 H 2.069 0.020 2
493 . 51 GLU HG3 H 1.905 0.020 2
494 . 51 GLU C C 174.372 0.300 1
495 . 51 GLU CA C 54.655 0.300 1
496 . 51 GLU CB C 33.276 0.300 1
497 . 51 GLU CG C 37.028 0.300 1
498 . 51 GLU N N 126.619 0.200 1
499 . 52 LEU H H 8.836 0.020 1
500 . 52 LEU HA H 4.715 0.020 1
501 . 52 LEU HB2 H 1.556 0.020 2
502 . 52 LEU HB3 H 1.198 0.020 2
503 . 52 LEU HG H 1.377 0.020 1
504 . 52 LEU HD1 H 0.797 0.020 1
505 . 52 LEU HD2 H 0.636 0.020 1
506 . 52 LEU CA C 54.039 0.300 1
507 . 52 LEU CB C 45.277 0.300 1
508 . 52 LEU CG C 27.595 0.300 1
509 . 52 LEU CD1 C 24.453 0.300 1
510 . 52 LEU CD2 C 25.552 0.300 1
511 . 52 LEU N N 125.806 0.200 1
512 . 53 LYS H H 8.397 0.020 1
513 . 53 LYS HA H 4.707 0.020 1
514 . 53 LYS HB2 H 1.910 0.020 1
515 . 53 LYS HB3 H 1.910 0.020 1
516 . 53 LYS HG2 H 1.384 0.020 1
517 . 53 LYS HG3 H 1.384 0.020 1
518 . 53 LYS HD2 H 1.803 0.020 1
519 . 53 LYS HD3 H 1.803 0.020 1
520 . 53 LYS HE2 H 3.195 0.020 2
521 . 53 LYS HE3 H 3.038 0.020 2
522 . 53 LYS C C 178.289 0.300 1
523 . 53 LYS CA C 55.045 0.300 1
524 . 53 LYS CB C 34.151 0.300 1
525 . 53 LYS CG C 24.833 0.300 1
526 . 53 LYS CD C 26.541 0.300 1
527 . 53 LYS N N 127.518 0.200 1
528 . 54 ALA H H 9.095 0.020 1
529 . 54 ALA HA H 3.864 0.020 1
530 . 54 ALA HB H 1.426 0.020 1
531 . 54 ALA C C 178.752 0.300 1
532 . 54 ALA CA C 55.858 0.300 1
533 . 54 ALA CB C 19.419 0.300 1
534 . 54 ALA N N 127.775 0.200 1
535 . 55 SER H H 8.421 0.020 1
536 . 55 SER HA H 4.123 0.020 1
537 . 55 SER HB2 H 3.989 0.020 1
538 . 55 SER HB3 H 3.900 0.020 1
539 . 55 SER CA C 60.551 0.300 1
540 . 55 SER CB C 61.384 0.300 1
541 . 55 SER N N 111.181 0.200 1
542 . 56 ASP H H 7.134 0.020 1
543 . 56 ASP HA H 4.614 0.020 1
544 . 56 ASP HB2 H 2.969 0.020 1
545 . 56 ASP HB3 H 2.775 0.020 1
546 . 56 ASP C C 174.540 0.300 1
547 . 56 ASP CA C 56.817 0.300 1
548 . 56 ASP CB C 40.618 0.300 1
549 . 56 ASP N N 122.431 0.200 1
550 . 57 ALA H H 8.069 0.020 1
551 . 57 ALA HA H 4.056 0.020 1
552 . 57 ALA HB H 1.361 0.020 1
553 . 57 ALA C C 179.061 0.300 1
554 . 57 ALA CA C 54.457 0.300 1
555 . 57 ALA CB C 18.296 0.300 1
556 . 57 ALA N N 123.025 0.200 1
557 . 58 GLY H H 8.545 0.020 1
558 . 58 GLY HA2 H 3.878 0.020 2
559 . 58 GLY HA3 H 3.744 0.020 2
560 . 58 GLY C C 175.193 0.300 1
561 . 58 GLY CA C 46.442 0.300 1
562 . 58 GLY N N 101.318 0.200 1
563 . 59 GLN H H 7.332 0.020 1
564 . 59 GLN HA H 4.332 0.020 1
565 . 59 GLN HB2 H 2.236 0.020 2
566 . 59 GLN HB3 H 2.321 0.020 2
567 . 59 GLN HG2 H 2.560 0.020 2
568 . 59 GLN HG3 H 2.653 0.020 2
569 . 59 GLN HE21 H 7.455 0.020 1
570 . 59 GLN HE22 H 6.861 0.020 1
571 . 59 GLN C C 177.246 0.300 1
572 . 59 GLN CA C 57.248 0.300 1
573 . 59 GLN CB C 29.349 0.300 1
574 . 59 GLN CG C 34.285 0.300 1
575 . 59 GLN N N 115.775 0.200 1
576 . 59 GLN NE2 N 111.963 0.200 1
577 . 60 VAL H H 7.321 0.020 1
578 . 60 VAL HA H 4.498 0.020 1
579 . 60 VAL HB H 2.359 0.020 1
580 . 60 VAL HG1 H 0.975 0.020 1
581 . 60 VAL HG2 H 0.998 0.020 1
582 . 60 VAL C C 175.696 0.300 1
583 . 60 VAL CA C 61.206 0.300 1
584 . 60 VAL CB C 31.954 0.300 1
585 . 60 VAL CG1 C 21.539 0.300 1
586 . 60 VAL CG2 C 19.540 0.300 1
587 . 60 VAL N N 109.963 0.200 1
588 . 61 LEU H H 7.175 0.020 1
589 . 61 LEU HA H 4.715 0.020 1
590 . 61 LEU HB2 H 2.091 0.020 1
591 . 61 LEU HB3 H 1.600 0.020 1
592 . 61 LEU HG H 2.037 0.020 1
593 . 61 LEU HD1 H 0.886 0.020 1
594 . 61 LEU HD2 H 0.817 0.020 1
595 . 61 LEU C C 176.835 0.300 1
596 . 61 LEU CA C 54.099 0.300 1
597 . 61 LEU CB C 42.971 0.300 1
598 . 61 LEU CG C 26.253 0.300 1
599 . 61 LEU CD1 C 26.192 0.300 1
600 . 61 LEU CD2 C 23.378 0.300 1
601 . 61 LEU N N 120.494 0.200 1
602 . 62 THR H H 9.459 0.020 1
603 . 62 THR HA H 4.838 0.020 1
604 . 62 THR HB H 4.547 0.020 1
605 . 62 THR HG2 H 1.197 0.020 1
606 . 62 THR C C 175.990 0.300 1
607 . 62 THR CA C 59.507 0.300 1
608 . 62 THR CB C 71.837 0.300 1
609 . 62 THR CG2 C 22.121 0.300 1
610 . 62 THR N N 114.431 0.200 1
611 . 63 ALA H H 8.753 0.020 1
612 . 63 ALA HA H 4.212 0.020 1
613 . 63 ALA HB H 1.509 0.020 1
614 . 63 ALA C C 179.676 0.300 1
615 . 63 ALA CA C 55.478 0.300 1
616 . 63 ALA CB C 18.763 0.300 1
617 . 63 ALA N N 122.088 0.200 1
618 . 64 ASP H H 7.985 0.020 1
619 . 64 ASP HA H 4.525 0.020 1
620 . 64 ASP HB2 H 2.484 0.020 1
621 . 64 ASP HB3 H 2.717 0.020 1
622 . 64 ASP C C 176.365 0.300 1
623 . 64 ASP CA C 55.079 0.300 1
624 . 64 ASP CB C 40.632 0.300 1
625 . 64 ASP N N 112.650 0.200 1
626 . 65 ASP H H 7.943 0.020 1
627 . 65 ASP HA H 4.235 0.020 1
628 . 65 ASP HB2 H 2.560 0.020 1
629 . 65 ASP HB3 H 2.318 0.020 1
630 . 65 ASP C C 173.512 0.300 1
631 . 65 ASP CA C 55.984 0.300 1
632 . 65 ASP CB C 42.033 0.300 1
633 . 65 ASP N N 118.275 0.200 1
634 . 66 PHE H H 6.947 0.020 1
635 . 66 PHE HA H 3.587 0.020 1
636 . 66 PHE HB2 H 2.784 0.020 1
637 . 66 PHE HB3 H 2.784 0.020 1
638 . 66 PHE HD1 H 7.370 0.020 1
639 . 66 PHE HD2 H 7.370 0.020 1
640 . 66 PHE HE1 H 7.121 0.020 1
641 . 66 PHE HE2 H 7.121 0.020 1
642 . 66 PHE HZ H 7.010 0.020 1
643 . 66 PHE CA C 55.470 0.300 1
644 . 66 PHE CB C 40.060 0.300 1
645 . 66 PHE CD1 C 133.063 0.300 1
646 . 66 PHE CD2 C 133.063 0.300 1
647 . 66 PHE CE1 C 130.758 0.300 1
648 . 66 PHE CE2 C 130.758 0.300 1
649 . 66 PHE CZ C 127.803 0.300 1
650 . 66 PHE N N 114.088 0.200 1
651 . 67 PRO HA H 4.994 0.020 1
652 . 67 PRO HB2 H 1.820 0.020 2
653 . 67 PRO HB3 H 2.774 0.020 2
654 . 67 PRO HG2 H 2.025 0.020 2
655 . 67 PRO HG3 H 1.847 0.020 2
656 . 67 PRO HD2 H 3.584 0.020 1
657 . 67 PRO HD3 H 3.584 0.020 1
658 . 67 PRO C C 175.947 0.300 1
659 . 67 PRO CA C 61.685 0.300 1
660 . 67 PRO CB C 36.092 0.300 1
661 . 67 PRO CG C 24.777 0.300 1
662 . 67 PRO CD C 50.388 0.300 1
663 . 68 PHE H H 8.808 0.020 1
664 . 68 PHE HA H 5.173 0.020 1
665 . 68 PHE HB2 H 2.851 0.020 1
666 . 68 PHE HB3 H 3.169 0.020 1
667 . 68 PHE HD1 H 6.984 0.020 1
668 . 68 PHE HD2 H 6.984 0.020 1
669 . 68 PHE HE1 H 6.669 0.020 1
670 . 68 PHE HE2 H 6.669 0.020 1
671 . 68 PHE HZ H 6.719 0.020 1
672 . 68 PHE C C 177.237 0.300 1
673 . 68 PHE CA C 56.851 0.300 1
674 . 68 PHE CB C 43.467 0.300 1
675 . 68 PHE CD1 C 131.359 0.300 1
676 . 68 PHE CD2 C 131.359 0.300 1
677 . 68 PHE CE1 C 131.059 0.300 1
678 . 68 PHE CE2 C 131.059 0.300 1
679 . 68 PHE CZ C 128.304 0.300 1
680 . 68 PHE N N 116.619 0.200 1
681 . 69 LYS H H 9.687 0.020 1
682 . 69 LYS HA H 4.413 0.020 1
683 . 69 LYS HB2 H 1.958 0.020 1
684 . 69 LYS HB3 H 1.958 0.020 1
685 . 69 LYS HG2 H 1.489 0.020 2
686 . 69 LYS HG3 H 1.557 0.020 2
687 . 69 LYS HD2 H 1.779 0.020 1
688 . 69 LYS HD3 H 1.779 0.020 1
689 . 69 LYS HE2 H 3.007 0.020 2
690 . 69 LYS HE3 H 3.053 0.020 2
691 . 69 LYS C C 175.425 0.300 1
692 . 69 LYS CA C 57.334 0.300 1
693 . 69 LYS CB C 33.026 0.300 1
694 . 69 LYS CG C 25.169 0.300 1
695 . 69 LYS CD C 28.872 0.300 1
696 . 69 LYS CE C 41.477 0.300 1
697 . 69 LYS N N 121.119 0.200 1
698 . 70 SER H H 7.300 0.020 1
699 . 70 SER HA H 3.303 0.020 1
700 . 70 SER HB2 H 3.900 0.020 1
701 . 70 SER HB3 H 3.699 0.020 1
702 . 70 SER C C 173.377 0.300 1
703 . 70 SER CA C 56.033 0.300 1
704 . 70 SER CB C 66.164 0.300 1
705 . 70 SER N N 110.775 0.200 1
706 . 71 ALA H H 8.566 0.020 1
707 . 71 ALA HA H 3.766 0.020 1
708 . 71 ALA HB H 1.415 0.020 1
709 . 71 ALA C C 178.546 0.300 1
710 . 71 ALA CA C 54.766 0.300 1
711 . 71 ALA CB C 19.995 0.300 1
712 . 71 ALA N N 124.119 0.200 1
713 . 72 GLU H H 8.836 0.020 1
714 . 72 GLU HA H 3.598 0.020 1
715 . 72 GLU HB2 H 1.958 0.020 1
716 . 72 GLU HB3 H 1.833 0.020 1
717 . 72 GLU HG2 H 2.403 0.020 2
718 . 72 GLU HG3 H 2.152 0.020 2
719 . 72 GLU C C 177.345 0.300 1
720 . 72 GLU CA C 60.673 0.300 1
721 . 72 GLU CB C 28.744 0.300 1
722 . 72 GLU CG C 37.361 0.300 1
723 . 72 GLU N N 117.338 0.200 1
724 . 73 GLU H H 7.362 0.020 1
725 . 73 GLU HA H 4.168 0.020 1
726 . 73 GLU HB2 H 2.203 0.020 2
727 . 73 GLU HB3 H 2.449 0.020 2
728 . 73 GLU HG2 H 2.493 0.020 2
729 . 73 GLU HG3 H 2.382 0.020 2
730 . 73 GLU C C 179.845 0.300 1
731 . 73 GLU CA C 59.220 0.300 1
732 . 73 GLU CB C 31.027 0.300 1
733 . 73 GLU CG C 36.206 0.300 1
734 . 73 GLU N N 117.838 0.200 1
735 . 74 VAL H H 7.238 0.020 1
736 . 74 VAL HA H 2.484 0.020 1
737 . 74 VAL HB H 1.851 0.020 1
738 . 74 VAL HG1 H 0.388 0.020 1
739 . 74 VAL HG2 H 0.575 0.020 1
740 . 74 VAL C C 176.401 0.300 1
741 . 74 VAL CA C 65.192 0.300 1
742 . 74 VAL CB C 31.070 0.300 1
743 . 74 VAL CG1 C 22.076 0.300 1
744 . 74 VAL CG2 C 21.627 0.300 1
745 . 74 VAL N N 118.619 0.200 1
746 . 75 ALA H H 7.998 0.020 1
747 . 75 ALA HA H 3.709 0.020 1
748 . 75 ALA HB H 1.446 0.020 1
749 . 75 ALA C C 178.553 0.300 1
750 . 75 ALA CA C 55.678 0.300 1
751 . 75 ALA CB C 20.783 0.300 1
752 . 75 ALA N N 120.056 0.200 1
753 . 76 ASP H H 8.659 0.020 1
754 . 76 ASP HA H 4.324 0.020 1
755 . 76 ASP HB2 H 2.717 0.020 1
756 . 76 ASP HB3 H 2.538 0.020 1
757 . 76 ASP C C 178.391 0.300 1
758 . 76 ASP CA C 57.474 0.300 1
759 . 76 ASP CB C 40.949 0.300 1
760 . 76 ASP N N 115.900 0.200 1
761 . 77 THR H H 7.765 0.020 1
762 . 77 THR HA H 4.041 0.020 1
763 . 77 THR HB H 4.257 0.020 1
764 . 77 THR HG2 H 1.243 0.020 1
765 . 77 THR C C 176.045 0.300 1
766 . 77 THR CA C 67.228 0.300 1
767 . 77 THR CB C 68.108 0.300 1
768 . 77 THR CG2 C 21.875 0.300 1
769 . 77 THR N N 115.556 0.200 1
770 . 78 ILE H H 8.296 0.020 1
771 . 78 ILE HA H 3.439 0.020 1
772 . 78 ILE HB H 1.737 0.020 1
773 . 78 ILE HG12 H 1.862 0.020 2
774 . 78 ILE HG13 H 0.803 0.020 2
775 . 78 ILE HG2 H 0.636 0.020 1
776 . 78 ILE HD1 H 0.596 0.020 1
777 . 78 ILE C C 177.639 0.300 1
778 . 78 ILE CA C 66.686 0.300 1
779 . 78 ILE CB C 37.586 0.300 1
780 . 78 ILE CG1 C 30.027 0.300 1
781 . 78 ILE CG2 C 17.579 0.300 1
782 . 78 ILE CD1 C 13.543 0.300 1
783 . 78 ILE N N 119.306 0.200 1
784 . 79 VAL H H 8.400 0.020 1
785 . 79 VAL HA H 3.766 0.020 1
786 . 79 VAL HB H 2.173 0.020 1
787 . 79 VAL HG1 H 0.953 0.020 1
788 . 79 VAL HG2 H 1.064 0.020 1
789 . 79 VAL C C 177.712 0.300 1
790 . 79 VAL CA C 66.322 0.300 1
791 . 79 VAL CB C 31.194 0.300 1
792 . 79 VAL CG1 C 21.804 0.300 1
793 . 79 VAL CG2 C 20.000 0.300 1
794 . 79 VAL N N 111.400 0.200 1
795 . 80 ASN H H 7.757 0.020 1
796 . 80 ASN HA H 4.619 0.020 1
797 . 80 ASN HB2 H 3.029 0.020 1
798 . 80 ASN HB3 H 2.828 0.020 1
799 . 80 ASN HD21 H 7.606 0.020 1
800 . 80 ASN HD22 H 6.905 0.020 1
801 . 80 ASN C C 178.731 0.300 1
802 . 80 ASN CA C 55.741 0.300 1
803 . 80 ASN CB C 38.596 0.300 1
804 . 80 ASN N N 117.931 0.200 1
805 . 80 ASN ND2 N 112.900 0.200 1
806 . 81 LYS H H 8.483 0.020 1
807 . 81 LYS HA H 4.207 0.020 1
808 . 81 LYS HB2 H 1.868 0.020 2
809 . 81 LYS HB3 H 1.801 0.020 2
810 . 81 LYS HG2 H 1.422 0.020 1
811 . 81 LYS HG3 H 1.422 0.020 1
812 . 81 LYS HD2 H 1.645 0.020 2
813 . 81 LYS HD3 H 1.687 0.020 2
814 . 81 LYS HE2 H 2.739 0.020 2
815 . 81 LYS HE3 H 2.895 0.020 2
816 . 81 LYS C C 177.873 0.300 1
817 . 81 LYS CA C 59.319 0.300 1
818 . 81 LYS CB C 32.011 0.300 1
819 . 81 LYS CG C 26.999 0.300 1
820 . 81 LYS CD C 29.840 0.300 1
821 . 81 LYS CE C 42.281 0.300 1
822 . 81 LYS N N 119.869 0.200 1
823 . 82 ALA H H 8.369 0.020 1
824 . 82 ALA HA H 4.330 0.020 1
825 . 82 ALA HB H 1.393 0.020 1
826 . 82 ALA C C 177.567 0.300 1
827 . 82 ALA CA C 52.500 0.300 1
828 . 82 ALA CB C 18.822 0.300 1
829 . 82 ALA N N 119.056 0.200 1
830 . 83 GLY H H 7.684 0.020 1
831 . 83 GLY HA2 H 3.922 0.020 1
832 . 83 GLY HA3 H 3.922 0.020 1
833 . 83 GLY C C 174.536 0.300 1
834 . 83 GLY CA C 46.808 0.300 1
835 . 83 GLY N N 105.869 0.200 1
836 . 84 LEU H H 7.217 0.020 1
837 . 84 LEU HA H 4.056 0.020 1
838 . 84 LEU HB2 H 1.623 0.020 1
839 . 84 LEU HB3 H 1.444 0.020 1
840 . 84 LEU HG H 1.544 0.020 1
841 . 84 LEU HD1 H 0.819 0.020 1
842 . 84 LEU HD2 H 0.797 0.020 1
843 . 84 LEU CA C 56.320 0.300 1
844 . 84 LEU CB C 42.948 0.300 1
845 . 84 LEU CD1 C 26.797 0.300 1
846 . 84 LEU CD2 C 22.996 0.300 1
847 . 84 LEU N N 123.587 0.200 1
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