data_10048
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution Structure of the UBA Domain of Human Tudor Domain Containing Protein 3
;
_BMRB_accession_number 10048
_BMRB_flat_file_name bmr10048.str
_Entry_type original
_Submission_date 2006-11-09
_Accession_date 2006-11-09
_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 Kamatari Y. . .
2 Tochio N. . .
3 Nakanishi T. . .
4 Miyamoto K. . .
5 Li H. . .
6 Kobayashi N. . .
7 Tomizawa T. . .
8 Koshiba S. . .
9 Inoue M. . .
10 Kigawa T. . .
11 Yokoyama S. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 319
"13C chemical shifts" 237
"15N chemical shifts" 59
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2008-08-13 original author .
stop_
_Original_release_date 2008-08-13
save_
#############################
# Citation for this entry #
#############################
save_citation_1
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Solution Structure of the UBA Domain of Human Tudor Domain Containing Protein 3'
_Citation_status 'in preparation'
_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 Kamatari Y. . .
2 Tochio N. . .
3 Nakanishi T. . .
4 Miyamoto K. . .
5 Li H. . .
6 Kobayashi N. . .
7 Tomizawa T. . .
8 Koshiba S. . .
9 Inoue M. . .
10 Kigawa T. . .
11 Yokoyama S. . .
stop_
_Journal_abbreviation .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first .
_Page_last .
_Year .
_Details .
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name 'Tudor domain containing protein 3'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Tudor domain containing protein 3' $entity_1
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state 'protein monomer'
_System_paramagnetic no
_System_thiol_state 'all free'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_entity_1
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'UBA domain'
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 63
_Mol_residue_sequence
;
GSSGSSGVDEKALKHITEMG
FSKEASRQALMDNGNNLEAA
LNVLLTSNKQKPVMGPPSGP
SSG
;
loop_
_Residue_seq_code
_Residue_label
1 GLY 2 SER 3 SER 4 GLY 5 SER
6 SER 7 GLY 8 VAL 9 ASP 10 GLU
11 LYS 12 ALA 13 LEU 14 LYS 15 HIS
16 ILE 17 THR 18 GLU 19 MET 20 GLY
21 PHE 22 SER 23 LYS 24 GLU 25 ALA
26 SER 27 ARG 28 GLN 29 ALA 30 LEU
31 MET 32 ASP 33 ASN 34 GLY 35 ASN
36 ASN 37 LEU 38 GLU 39 ALA 40 ALA
41 LEU 42 ASN 43 VAL 44 LEU 45 LEU
46 THR 47 SER 48 ASN 49 LYS 50 GLN
51 LYS 52 PRO 53 VAL 54 MET 55 GLY
56 PRO 57 PRO 58 SER 59 GLY 60 PRO
61 SER 62 SER 63 GLY
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-07-08
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 1WJI "Solution Structure Of The Uba Domain Of Human Tudor Domain Containing Protein 3" 100.00 63 100.00 100.00 1.82e-35
DBJ BAB14950 "unnamed protein product [Homo sapiens]" 79.37 651 100.00 100.00 4.21e-24
DBJ BAJ17879 "tudor domain containing 3 [synthetic construct]" 79.37 651 100.00 100.00 4.21e-24
DBJ BAK63800 "tudor domain-containing protein 3 [Pan troglodytes]" 79.37 533 100.00 100.00 1.84e-24
EMBL CAD97894 "hypothetical protein [Homo sapiens]" 79.37 651 100.00 100.00 4.21e-24
EMBL CAL37786 "hypothetical protein [synthetic construct]" 79.37 651 100.00 100.00 4.21e-24
GB AAH30514 "Tudor domain containing 3 [Homo sapiens]" 79.37 651 100.00 100.00 4.21e-24
GB AAH60876 "Tudor domain containing 3 [Homo sapiens]" 79.37 650 100.00 100.00 4.07e-24
GB ACC94142 "tudor domain-containing protein 3 [Homo sapiens]" 79.37 744 100.00 100.00 5.71e-24
GB AIC52422 "TDRD3, partial [synthetic construct]" 79.37 651 100.00 100.00 4.21e-24
GB EAW52079 "tudor domain containing 3, isoform CRA_a [Homo sapiens]" 79.37 651 100.00 100.00 4.21e-24
REF NP_001139542 "tudor domain-containing protein 3 isoform 1 [Homo sapiens]" 79.37 744 100.00 100.00 5.71e-24
REF NP_001139543 "tudor domain-containing protein 3 isoform 2 [Homo sapiens]" 79.37 651 100.00 100.00 4.21e-24
REF NP_110421 "tudor domain-containing protein 3 isoform 2 [Homo sapiens]" 79.37 651 100.00 100.00 4.21e-24
REF XP_002808194 "PREDICTED: LOW QUALITY PROTEIN: tudor domain-containing protein 3-like [Macaca mulatta]" 79.37 651 100.00 100.00 4.29e-24
REF XP_003257452 "PREDICTED: tudor domain-containing protein 3 isoform X2 [Nomascus leucogenys]" 79.37 651 100.00 100.00 4.08e-24
SP Q9H7E2 "RecName: Full=Tudor domain-containing protein 3" 79.37 651 100.00 100.00 4.21e-24
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$entity_1 human 9606 Eukaryota Metazoa Homo sapiens
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
$entity_1 'cell free synthesis' . . . . plasmid P040301-26
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
$entity_1 1.04 mM '[U-13C; U-15N]'
d-Tris-HCl 20 mM .
NaCl 100 mM .
d-DTT 1 mM .
NaN3 0.02 % .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_software_1
_Saveframe_category software
_Name xwinnmr
_Version 2.6
loop_
_Vendor
_Address
_Electronic_address
Bruker . .
stop_
loop_
_Task
collection
stop_
_Details .
save_
save_software_2
_Saveframe_category software
_Name NMRPipe
_Version 20020425
loop_
_Vendor
_Address
_Electronic_address
'Delaglio, F.' . .
stop_
loop_
_Task
processing
stop_
_Details .
save_
save_software_3
_Saveframe_category software
_Name NMRView
_Version 5.0.4
loop_
_Vendor
_Address
_Electronic_address
'Johnson, B. A.' . .
stop_
loop_
_Task
'data analysis'
stop_
_Details .
save_
save_software_4
_Saveframe_category software
_Name Kujira
_Version 0.8998
loop_
_Vendor
_Address
_Electronic_address
'Kobayashi, N.' . .
stop_
loop_
_Task
'data analysis'
stop_
_Details .
save_
save_software_5
_Saveframe_category software
_Name CYANA
_Version 2.0.17
loop_
_Vendor
_Address
_Electronic_address
'Guntert, P.' . .
stop_
loop_
_Task
refinement
'structure solution'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_3D_13C-separated_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 13C-separated NOESY'
_Sample_label $sample_1
save_
save_3D_15N-separated_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 15N-separated NOESY'
_Sample_label $sample_1
save_
save_3D_13C-separated_NOESY
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 13C-separated NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_3D_15N-separated_NOESY
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 15N-separated NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_condition_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 120 0.1 mM
pH 7.0 0.05 pH
pressure 1 0.001 atm
temperature 298 0.1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_reference_1
_Saveframe_category chemical_shift_reference
_Details
;
Chemical shift reference of 1H was based on the proton of water (4.784ppm at
298K) and then those of 15N and 13C were calculated based on their gyromagnetic
ratios.
;
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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.0 . indirect . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 . 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_chemical_shift_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'3D 13C-separated NOESY'
'3D 15N-separated NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $condition_1
_Chem_shift_reference_set_label $reference_1
_Mol_system_component_name 'Tudor domain containing protein 3'
_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 6 6 SER HA H 4.504 0.030 1
2 6 6 SER HB2 H 3.921 0.030 2
3 6 6 SER C C 174.869 0.300 1
4 6 6 SER CA C 58.718 0.300 1
5 6 6 SER CB C 64.038 0.300 1
6 7 7 GLY H H 8.302 0.030 1
7 7 7 GLY HA2 H 3.995 0.030 1
8 7 7 GLY HA3 H 3.995 0.030 1
9 7 7 GLY C C 173.647 0.300 1
10 7 7 GLY CA C 45.131 0.300 1
11 7 7 GLY N N 110.186 0.300 1
12 8 8 VAL H H 7.969 0.030 1
13 8 8 VAL HA H 4.406 0.030 1
14 8 8 VAL HB H 2.041 0.030 1
15 8 8 VAL HG1 H 0.940 0.030 1
16 8 8 VAL HG2 H 0.878 0.030 1
17 8 8 VAL C C 174.964 0.300 1
18 8 8 VAL CA C 60.935 0.300 1
19 8 8 VAL CB C 33.680 0.300 1
20 8 8 VAL CG1 C 22.344 0.300 2
21 8 8 VAL CG2 C 21.795 0.300 2
22 8 8 VAL N N 118.958 0.300 1
23 9 9 ASP H H 8.190 0.030 1
24 9 9 ASP HA H 4.560 0.030 1
25 9 9 ASP HB2 H 2.735 0.030 2
26 9 9 ASP HB3 H 2.599 0.030 2
27 9 9 ASP C C 176.419 0.300 1
28 9 9 ASP CA C 53.834 0.300 1
29 9 9 ASP CB C 41.244 0.300 1
30 9 9 ASP N N 125.037 0.300 1
31 10 10 GLU H H 8.832 0.030 1
32 10 10 GLU HA H 3.936 0.030 1
33 10 10 GLU HB2 H 2.137 0.030 2
34 10 10 GLU HB3 H 2.017 0.030 2
35 10 10 GLU HG2 H 2.297 0.030 2
36 10 10 GLU HG3 H 2.447 0.030 2
37 10 10 GLU C C 179.046 0.300 1
38 10 10 GLU CA C 59.325 0.300 1
39 10 10 GLU CB C 29.610 0.300 1
40 10 10 GLU CG C 36.393 0.300 1
41 10 10 GLU N N 127.601 0.300 1
42 11 11 LYS H H 8.240 0.030 1
43 11 11 LYS HA H 4.098 0.030 1
44 11 11 LYS HB2 H 2.012 0.030 2
45 11 11 LYS HB3 H 1.927 0.030 2
46 11 11 LYS HG2 H 1.570 0.030 2
47 11 11 LYS HG3 H 1.420 0.030 2
48 11 11 LYS HD2 H 1.741 0.030 1
49 11 11 LYS HD3 H 1.741 0.030 1
50 11 11 LYS HE2 H 3.036 0.030 1
51 11 11 LYS HE3 H 3.036 0.030 1
52 11 11 LYS C C 179.327 0.300 1
53 11 11 LYS CA C 59.435 0.300 1
54 11 11 LYS CB C 31.712 0.300 1
55 11 11 LYS CG C 25.341 0.300 1
56 11 11 LYS CD C 29.177 0.300 1
57 11 11 LYS CE C 42.020 0.300 1
58 11 11 LYS N N 121.507 0.300 1
59 12 12 ALA H H 7.943 0.030 1
60 12 12 ALA HA H 4.131 0.030 1
61 12 12 ALA HB H 1.456 0.030 1
62 12 12 ALA C C 178.894 0.300 1
63 12 12 ALA CA C 54.578 0.300 1
64 12 12 ALA CB C 18.610 0.300 1
65 12 12 ALA N N 124.456 0.300 1
66 13 13 LEU H H 8.246 0.030 1
67 13 13 LEU HA H 3.809 0.030 1
68 13 13 LEU HB2 H 1.903 0.030 2
69 13 13 LEU HB3 H 1.346 0.030 2
70 13 13 LEU HG H 1.608 0.030 1
71 13 13 LEU HD1 H 0.873 0.030 1
72 13 13 LEU HD2 H 0.898 0.030 1
73 13 13 LEU C C 178.704 0.300 1
74 13 13 LEU CA C 58.265 0.300 1
75 13 13 LEU CB C 42.019 0.300 1
76 13 13 LEU CG C 26.804 0.300 1
77 13 13 LEU CD1 C 25.013 0.300 2
78 13 13 LEU CD2 C 25.983 0.300 2
79 13 13 LEU N N 118.143 0.300 1
80 14 14 LYS H H 7.827 0.030 1
81 14 14 LYS HA H 4.074 0.030 1
82 14 14 LYS HB2 H 1.936 0.030 1
83 14 14 LYS HB3 H 1.936 0.030 1
84 14 14 LYS HG2 H 1.485 0.030 2
85 14 14 LYS HG3 H 1.401 0.030 2
86 14 14 LYS HD2 H 1.733 0.030 2
87 14 14 LYS HD3 H 1.670 0.030 2
88 14 14 LYS HE2 H 2.998 0.030 1
89 14 14 LYS HE3 H 2.998 0.030 1
90 14 14 LYS C C 177.539 0.300 1
91 14 14 LYS CA C 59.031 0.300 1
92 14 14 LYS CB C 32.444 0.300 1
93 14 14 LYS CG C 24.794 0.300 1
94 14 14 LYS CD C 29.324 0.300 1
95 14 14 LYS CE C 42.242 0.300 1
96 14 14 LYS N N 119.978 0.300 1
97 15 15 HIS H H 7.744 0.030 1
98 15 15 HIS HA H 4.268 0.030 1
99 15 15 HIS HB2 H 3.400 0.030 2
100 15 15 HIS HB3 H 3.218 0.030 2
101 15 15 HIS HD2 H 6.802 0.030 1
102 15 15 HIS HE1 H 7.978 0.030 1
103 15 15 HIS C C 177.519 0.300 1
104 15 15 HIS CA C 59.235 0.300 1
105 15 15 HIS CB C 30.314 0.300 1
106 15 15 HIS CD2 C 119.638 0.300 1
107 15 15 HIS CE1 C 138.267 0.300 1
108 15 15 HIS N N 117.630 0.300 1
109 16 16 ILE H H 8.156 0.030 1
110 16 16 ILE HA H 3.870 0.030 1
111 16 16 ILE HB H 1.839 0.030 1
112 16 16 ILE HG12 H 2.041 0.030 2
113 16 16 ILE HG13 H 0.861 0.030 2
114 16 16 ILE HG2 H 0.931 0.030 1
115 16 16 ILE HD1 H 0.749 0.030 1
116 16 16 ILE C C 179.434 0.300 1
117 16 16 ILE CA C 65.930 0.300 1
118 16 16 ILE CB C 38.841 0.300 1
119 16 16 ILE CG1 C 29.077 0.300 1
120 16 16 ILE CG2 C 19.443 0.300 1
121 16 16 ILE CD1 C 13.856 0.300 1
122 16 16 ILE N N 116.860 0.300 1
123 17 17 THR H H 8.630 0.030 1
124 17 17 THR HA H 4.597 0.030 1
125 17 17 THR HB H 4.337 0.030 1
126 17 17 THR HG2 H 1.302 0.030 1
127 17 17 THR C C 179.910 0.300 1
128 17 17 THR CA C 65.251 0.300 1
129 17 17 THR CB C 69.108 0.300 1
130 17 17 THR CG2 C 21.904 0.300 1
131 17 17 THR N N 113.477 0.300 1
132 18 18 GLU H H 8.220 0.030 1
133 18 18 GLU HA H 4.135 0.030 1
134 18 18 GLU HB2 H 2.194 0.030 2
135 18 18 GLU HB3 H 2.069 0.030 2
136 18 18 GLU HG2 H 2.339 0.030 2
137 18 18 GLU HG3 H 2.555 0.030 2
138 18 18 GLU C C 178.005 0.300 1
139 18 18 GLU CA C 58.718 0.300 1
140 18 18 GLU CB C 29.053 0.300 1
141 18 18 GLU CG C 37.324 0.300 1
142 18 18 GLU N N 123.193 0.300 1
143 19 19 MET H H 7.636 0.030 1
144 19 19 MET HA H 4.353 0.030 1
145 19 19 MET HB2 H 2.370 0.030 2
146 19 19 MET HB3 H 2.511 0.030 2
147 19 19 MET HG2 H 2.848 0.030 2
148 19 19 MET HG3 H 2.569 0.030 2
149 19 19 MET HE H 2.148 0.030 1
150 19 19 MET C C 176.300 0.300 1
151 19 19 MET CA C 56.501 0.300 1
152 19 19 MET CB C 33.048 0.300 1
153 19 19 MET CG C 32.530 0.300 1
154 19 19 MET CE C 17.259 0.300 1
155 19 19 MET N N 117.209 0.300 1
156 20 20 GLY H H 7.883 0.030 1
157 20 20 GLY HA2 H 4.116 0.030 2
158 20 20 GLY HA3 H 3.575 0.030 2
159 20 20 GLY C C 173.870 0.300 1
160 20 20 GLY CA C 44.907 0.300 1
161 20 20 GLY N N 105.116 0.300 1
162 21 21 PHE H H 6.760 0.030 1
163 21 21 PHE HA H 4.598 0.030 1
164 21 21 PHE HB2 H 2.998 0.030 2
165 21 21 PHE HB3 H 2.678 0.030 2
166 21 21 PHE HD1 H 7.364 0.030 1
167 21 21 PHE HD2 H 7.364 0.030 1
168 21 21 PHE HE1 H 7.196 0.030 1
169 21 21 PHE HE2 H 7.196 0.030 1
170 21 21 PHE HZ H 7.125 0.030 1
171 21 21 PHE C C 175.521 0.300 1
172 21 21 PHE CA C 57.845 0.300 1
173 21 21 PHE CB C 40.686 0.300 1
174 21 21 PHE CD1 C 132.259 0.300 1
175 21 21 PHE CD2 C 132.259 0.300 1
176 21 21 PHE CE1 C 131.361 0.300 1
177 21 21 PHE CE2 C 131.361 0.300 1
178 21 21 PHE CZ C 129.425 0.300 1
179 21 21 PHE N N 118.757 0.300 1
180 22 22 SER H H 9.025 0.030 1
181 22 22 SER HA H 4.419 0.030 1
182 22 22 SER HB2 H 4.129 0.030 2
183 22 22 SER HB3 H 4.376 0.030 2
184 22 22 SER C C 176.620 0.300 1
185 22 22 SER CA C 57.917 0.300 1
186 22 22 SER CB C 64.502 0.300 1
187 22 22 SER N N 117.237 0.300 1
188 23 23 LYS H H 9.356 0.030 1
189 23 23 LYS HA H 3.854 0.030 1
190 23 23 LYS HB2 H 1.957 0.030 2
191 23 23 LYS HB3 H 1.883 0.030 2
192 23 23 LYS HG2 H 1.477 0.030 1
193 23 23 LYS HG3 H 1.477 0.030 1
194 23 23 LYS HD2 H 1.759 0.030 1
195 23 23 LYS HD3 H 1.759 0.030 1
196 23 23 LYS HE2 H 3.011 0.030 1
197 23 23 LYS HE3 H 3.011 0.030 1
198 23 23 LYS C C 178.238 0.300 1
199 23 23 LYS CA C 60.763 0.300 1
200 23 23 LYS CB C 32.182 0.300 1
201 23 23 LYS CG C 25.392 0.300 1
202 23 23 LYS CD C 29.573 0.300 1
203 23 23 LYS CE C 42.020 0.300 1
204 23 23 LYS N N 126.756 0.300 1
205 24 24 GLU H H 8.895 0.030 1
206 24 24 GLU HA H 4.071 0.030 1
207 24 24 GLU HB2 H 2.080 0.030 2
208 24 24 GLU HB3 H 1.983 0.030 2
209 24 24 GLU HG2 H 2.303 0.030 2
210 24 24 GLU HG3 H 2.447 0.030 2
211 24 24 GLU C C 179.110 0.300 1
212 24 24 GLU CA C 60.012 0.300 1
213 24 24 GLU CB C 28.853 0.300 1
214 24 24 GLU CG C 36.554 0.300 1
215 24 24 GLU N N 118.325 0.300 1
216 25 25 ALA H H 7.979 0.030 1
217 25 25 ALA HA H 4.130 0.030 1
218 25 25 ALA HB H 1.450 0.030 1
219 25 25 ALA C C 181.140 0.300 1
220 25 25 ALA CA C 54.837 0.300 1
221 25 25 ALA CB C 18.364 0.300 1
222 25 25 ALA N N 122.597 0.300 1
223 26 26 SER H H 8.265 0.030 1
224 26 26 SER HA H 3.976 0.030 1
225 26 26 SER HB2 H 3.912 0.030 2
226 26 26 SER HB3 H 3.494 0.030 2
227 26 26 SER C C 174.972 0.300 1
228 26 26 SER CA C 62.955 0.300 1
229 26 26 SER CB C 63.137 0.300 1
230 26 26 SER N N 115.953 0.300 1
231 27 27 ARG H H 8.408 0.030 1
232 27 27 ARG HA H 3.768 0.030 1
233 27 27 ARG HB2 H 1.892 0.030 1
234 27 27 ARG HB3 H 1.892 0.030 1
235 27 27 ARG HG2 H 1.637 0.030 2
236 27 27 ARG HG3 H 1.552 0.030 2
237 27 27 ARG HD2 H 3.225 0.030 1
238 27 27 ARG HD3 H 3.225 0.030 1
239 27 27 ARG HE H 7.545 0.030 1
240 27 27 ARG C C 177.737 0.300 1
241 27 27 ARG CA C 60.012 0.300 1
242 27 27 ARG CB C 30.291 0.300 1
243 27 27 ARG CG C 27.970 0.300 1
244 27 27 ARG CD C 43.348 0.300 1
245 27 27 ARG N N 121.644 0.300 1
246 27 27 ARG NE N 83.705 0.300 1
247 28 28 GLN H H 7.751 0.030 1
248 28 28 GLN HA H 3.848 0.030 1
249 28 28 GLN HB2 H 2.157 0.030 2
250 28 28 GLN HB3 H 2.064 0.030 2
251 28 28 GLN HG2 H 2.414 0.030 2
252 28 28 GLN HG3 H 2.358 0.030 2
253 28 28 GLN HE21 H 6.784 0.030 2
254 28 28 GLN HE22 H 7.998 0.030 2
255 28 28 GLN C C 177.158 0.300 1
256 28 28 GLN CA C 58.588 0.300 1
257 28 28 GLN CB C 28.550 0.300 1
258 28 28 GLN CG C 33.390 0.300 1
259 28 28 GLN N N 118.002 0.300 1
260 28 28 GLN NE2 N 115.559 0.300 1
261 29 29 ALA H H 7.910 0.030 1
262 29 29 ALA HA H 4.188 0.030 1
263 29 29 ALA HB H 1.391 0.030 1
264 29 29 ALA C C 181.022 0.300 1
265 29 29 ALA CA C 55.031 0.300 1
266 29 29 ALA CB C 17.881 0.300 1
267 29 29 ALA N N 119.542 0.300 1
268 30 30 LEU H H 7.979 0.030 1
269 30 30 LEU HA H 3.841 0.030 1
270 30 30 LEU HB2 H 1.909 0.030 2
271 30 30 LEU HB3 H 1.674 0.030 2
272 30 30 LEU HG H 1.502 0.030 1
273 30 30 LEU HD1 H 0.752 0.030 1
274 30 30 LEU HD2 H 0.647 0.030 1
275 30 30 LEU C C 179.480 0.300 1
276 30 30 LEU CA C 58.588 0.300 1
277 30 30 LEU CB C 41.603 0.300 1
278 30 30 LEU CG C 27.714 0.300 1
279 30 30 LEU CD1 C 25.740 0.300 2
280 30 30 LEU CD2 C 23.312 0.300 2
281 30 30 LEU N N 118.602 0.300 1
282 31 31 MET H H 8.488 0.030 1
283 31 31 MET HA H 4.109 0.030 1
284 31 31 MET HB2 H 2.121 0.030 1
285 31 31 MET HB3 H 2.121 0.030 1
286 31 31 MET HG2 H 2.641 0.030 2
287 31 31 MET HG3 H 2.509 0.030 2
288 31 31 MET HE H 2.040 0.030 1
289 31 31 MET C C 179.379 0.300 1
290 31 31 MET CA C 58.792 0.300 1
291 31 31 MET CB C 32.204 0.300 1
292 31 31 MET CG C 32.043 0.300 1
293 31 31 MET CE C 16.474 0.300 1
294 31 31 MET N N 120.248 0.300 1
295 32 32 ASP H H 8.476 0.030 1
296 32 32 ASP HA H 4.566 0.030 1
297 32 32 ASP HB2 H 2.666 0.030 2
298 32 32 ASP HB3 H 2.713 0.030 2
299 32 32 ASP C C 176.738 0.300 1
300 32 32 ASP CA C 55.945 0.300 1
301 32 32 ASP CB C 41.039 0.300 1
302 32 32 ASP N N 118.066 0.300 1
303 33 33 ASN H H 7.356 0.030 1
304 33 33 ASN HA H 5.033 0.030 1
305 33 33 ASN HB2 H 2.908 0.030 2
306 33 33 ASN HB3 H 2.559 0.030 2
307 33 33 ASN HD21 H 6.942 0.030 2
308 33 33 ASN HD22 H 8.561 0.030 2
309 33 33 ASN C C 176.034 0.300 1
310 33 33 ASN CA C 53.155 0.300 1
311 33 33 ASN CB C 39.484 0.300 1
312 33 33 ASN N N 115.755 0.300 1
313 33 33 ASN ND2 N 115.343 0.300 1
314 34 34 GLY H H 8.011 0.030 1
315 34 34 GLY HA2 H 3.791 0.030 2
316 34 34 GLY HA3 H 4.027 0.030 2
317 34 34 GLY C C 174.951 0.300 1
318 34 34 GLY CA C 48.086 0.300 1
319 34 34 GLY N N 109.492 0.300 1
320 35 35 ASN H H 9.010 0.030 1
321 35 35 ASN HA H 4.046 0.030 1
322 35 35 ASN HB2 H 3.039 0.030 2
323 35 35 ASN HB3 H 2.961 0.030 2
324 35 35 ASN HD21 H 6.775 0.030 2
325 35 35 ASN HD22 H 7.469 0.030 2
326 35 35 ASN C C 172.836 0.300 1
327 35 35 ASN CA C 54.807 0.300 1
328 35 35 ASN CB C 38.084 0.300 1
329 35 35 ASN N N 111.570 0.300 1
330 35 35 ASN ND2 N 112.369 0.300 1
331 36 36 ASN H H 7.405 0.030 1
332 36 36 ASN HA H 4.715 0.030 1
333 36 36 ASN HB2 H 3.077 0.030 2
334 36 36 ASN HB3 H 2.768 0.030 2
335 36 36 ASN HD21 H 7.093 0.030 2
336 36 36 ASN HD22 H 7.735 0.030 2
337 36 36 ASN C C 174.346 0.300 1
338 36 36 ASN CA C 53.349 0.300 1
339 36 36 ASN CB C 39.825 0.300 1
340 36 36 ASN N N 117.420 0.300 1
341 36 36 ASN ND2 N 113.171 0.300 1
342 37 37 LEU H H 8.546 0.030 1
343 37 37 LEU HA H 3.780 0.030 1
344 37 37 LEU HB2 H 1.725 0.030 2
345 37 37 LEU HB3 H 1.602 0.030 2
346 37 37 LEU HG H 1.522 0.030 1
347 37 37 LEU HD1 H 0.881 0.030 1
348 37 37 LEU HD2 H 0.724 0.030 1
349 37 37 LEU C C 177.144 0.300 1
350 37 37 LEU CA C 59.268 0.300 1
351 37 37 LEU CB C 42.473 0.300 1
352 37 37 LEU CG C 27.281 0.300 1
353 37 37 LEU CD1 C 25.009 0.300 1
354 37 37 LEU CD2 C 25.009 0.300 1
355 37 37 LEU N N 129.168 0.300 1
356 38 38 GLU H H 8.286 0.030 1
357 38 38 GLU HA H 3.854 0.030 1
358 38 38 GLU HB2 H 2.096 0.030 2
359 38 38 GLU HB3 H 2.009 0.030 2
360 38 38 GLU HG2 H 2.283 0.030 1
361 38 38 GLU HG3 H 2.283 0.030 1
362 38 38 GLU C C 179.033 0.300 1
363 38 38 GLU CA C 60.195 0.300 1
364 38 38 GLU CB C 29.080 0.300 1
365 38 38 GLU CG C 36.893 0.300 1
366 38 38 GLU N N 117.943 0.300 1
367 39 39 ALA H H 8.208 0.030 1
368 39 39 ALA HA H 4.132 0.030 1
369 39 39 ALA HB H 1.459 0.030 1
370 39 39 ALA C C 180.275 0.300 1
371 39 39 ALA CA C 54.578 0.300 1
372 39 39 ALA CB C 18.621 0.300 1
373 39 39 ALA N N 121.879 0.300 1
374 40 40 ALA H H 8.284 0.030 1
375 40 40 ALA HA H 3.863 0.030 1
376 40 40 ALA HB H 1.242 0.030 1
377 40 40 ALA C C 178.880 0.300 1
378 40 40 ALA CA C 55.063 0.300 1
379 40 40 ALA CB C 18.415 0.300 1
380 40 40 ALA N N 120.281 0.300 1
381 41 41 LEU H H 8.542 0.030 1
382 41 41 LEU HA H 3.809 0.030 1
383 41 41 LEU HB2 H 1.742 0.030 2
384 41 41 LEU HB3 H 1.550 0.030 2
385 41 41 LEU HG H 1.656 0.030 1
386 41 41 LEU HD1 H 0.916 0.030 1
387 41 41 LEU HD2 H 0.918 0.030 1
388 41 41 LEU C C 178.312 0.300 1
389 41 41 LEU CA C 57.780 0.300 1
390 41 41 LEU CB C 41.786 0.300 1
391 41 41 LEU CG C 27.262 0.300 1
392 41 41 LEU CD1 C 25.044 0.300 1
393 41 41 LEU CD2 C 25.044 0.300 1
394 41 41 LEU N N 117.275 0.300 1
395 42 42 ASN H H 7.906 0.030 1
396 42 42 ASN HA H 4.436 0.030 1
397 42 42 ASN HB2 H 2.815 0.030 2
398 42 42 ASN HB3 H 2.855 0.030 2
399 42 42 ASN HD21 H 7.629 0.030 2
400 42 42 ASN HD22 H 6.934 0.030 2
401 42 42 ASN C C 178.331 0.300 1
402 42 42 ASN CA C 56.680 0.300 1
403 42 42 ASN CB C 38.463 0.300 1
404 42 42 ASN N N 116.085 0.300 1
405 42 42 ASN ND2 N 112.870 0.300 1
406 43 43 VAL H H 7.584 0.030 1
407 43 43 VAL HA H 3.788 0.030 1
408 43 43 VAL HB H 2.208 0.030 1
409 43 43 VAL HG1 H 1.097 0.030 1
410 43 43 VAL HG2 H 0.957 0.030 1
411 43 43 VAL C C 178.514 0.300 1
412 43 43 VAL CA C 65.833 0.300 1
413 43 43 VAL CB C 31.653 0.300 1
414 43 43 VAL CG1 C 22.426 0.300 2
415 43 43 VAL CG2 C 20.836 0.300 2
416 43 43 VAL N N 118.874 0.300 1
417 44 44 LEU H H 7.750 0.030 1
418 44 44 LEU HA H 3.884 0.030 1
419 44 44 LEU HB2 H 1.218 0.030 2
420 44 44 LEU HB3 H 0.468 0.030 2
421 44 44 LEU HG H 1.380 0.030 1
422 44 44 LEU HD1 H 0.260 0.030 1
423 44 44 LEU HD2 H 0.556 0.030 1
424 44 44 LEU C C 179.343 0.300 1
425 44 44 LEU CA C 57.424 0.300 1
426 44 44 LEU CB C 40.985 0.300 1
427 44 44 LEU CG C 26.419 0.300 1
428 44 44 LEU CD1 C 26.585 0.300 2
429 44 44 LEU CD2 C 22.021 0.300 2
430 44 44 LEU N N 122.451 0.300 1
431 45 45 LEU H H 8.514 0.030 1
432 45 45 LEU HA H 4.323 0.030 1
433 45 45 LEU HB2 H 1.914 0.030 2
434 45 45 LEU HB3 H 1.602 0.030 2
435 45 45 LEU HG H 1.828 0.030 1
436 45 45 LEU HD1 H 1.086 0.030 1
437 45 45 LEU HD2 H 0.962 0.030 1
438 45 45 LEU C C 179.095 0.300 1
439 45 45 LEU CA C 57.004 0.300 1
440 45 45 LEU CB C 42.322 0.300 1
441 45 45 LEU CG C 27.284 0.300 1
442 45 45 LEU CD1 C 23.332 0.300 2
443 45 45 LEU CD2 C 25.629 0.300 2
444 45 45 LEU N N 118.606 0.300 1
445 46 46 THR H H 7.726 0.030 1
446 46 46 THR HA H 4.309 0.030 1
447 46 46 THR HB H 4.362 0.030 1
448 46 46 THR HG2 H 1.269 0.030 1
449 46 46 THR C C 175.623 0.300 1
450 46 46 THR CA C 63.634 0.300 1
451 46 46 THR CB C 69.690 0.300 1
452 46 46 THR CG2 C 21.459 0.300 1
453 46 46 THR N N 111.621 0.300 1
454 47 47 SER H H 7.958 0.030 1
455 47 47 SER HA H 4.448 0.030 1
456 47 47 SER HB2 H 3.988 0.030 1
457 47 47 SER HB3 H 3.988 0.030 1
458 47 47 SER C C 174.729 0.300 1
459 47 47 SER CA C 59.559 0.300 1
460 47 47 SER CB C 63.752 0.300 1
461 47 47 SER N N 117.146 0.300 1
462 48 48 ASN H H 8.213 0.030 1
463 48 48 ASN HA H 4.782 0.030 1
464 48 48 ASN HB2 H 2.933 0.030 2
465 48 48 ASN HB3 H 2.879 0.030 2
466 48 48 ASN HD21 H 6.965 0.030 2
467 48 48 ASN HD22 H 7.692 0.030 2
468 48 48 ASN C C 175.303 0.300 1
469 48 48 ASN CA C 53.672 0.300 1
470 48 48 ASN CB C 38.992 0.300 1
471 48 48 ASN N N 120.115 0.300 1
472 48 48 ASN ND2 N 112.689 0.300 1
473 49 49 LYS H H 8.106 0.030 1
474 49 49 LYS HA H 4.302 0.030 1
475 49 49 LYS HB2 H 1.906 0.030 2
476 49 49 LYS HB3 H 1.813 0.030 2
477 49 49 LYS HG2 H 1.509 0.030 2
478 49 49 LYS HG3 H 1.449 0.030 2
479 49 49 LYS HD2 H 1.727 0.030 1
480 49 49 LYS HD3 H 1.727 0.030 1
481 49 49 LYS HE2 H 3.043 0.030 2
482 49 49 LYS HE3 H 2.999 0.030 2
483 49 49 LYS C C 176.640 0.300 1
484 49 49 LYS CA C 56.667 0.300 1
485 49 49 LYS CB C 32.714 0.300 1
486 49 49 LYS CG C 24.926 0.300 1
487 49 49 LYS CD C 29.051 0.300 1
488 49 49 LYS CE C 42.269 0.300 1
489 49 49 LYS N N 120.472 0.300 1
490 50 50 GLN H H 8.262 0.030 1
491 50 50 GLN HA H 4.308 0.030 1
492 50 50 GLN HB2 H 2.108 0.030 2
493 50 50 GLN HB3 H 1.993 0.030 2
494 50 50 GLN HG2 H 2.358 0.030 1
495 50 50 GLN HG3 H 2.358 0.030 1
496 50 50 GLN HE21 H 6.858 0.030 2
497 50 50 GLN HE22 H 7.518 0.030 2
498 50 50 GLN C C 175.707 0.300 1
499 50 50 GLN CA C 55.708 0.300 1
500 50 50 GLN CB C 29.458 0.300 1
501 50 50 GLN CG C 33.891 0.300 1
502 50 50 GLN N N 120.369 0.300 1
503 50 50 GLN NE2 N 112.412 0.300 1
504 51 51 LYS H H 8.277 0.030 1
505 51 51 LYS HA H 4.587 0.030 1
506 51 51 LYS HB2 H 1.835 0.030 2
507 51 51 LYS HB3 H 1.729 0.030 2
508 51 51 LYS HG2 H 1.503 0.030 2
509 51 51 LYS HG3 H 1.465 0.030 2
510 51 51 LYS HD2 H 1.713 0.030 2
511 51 51 LYS C C 174.373 0.300 1
512 51 51 LYS CA C 54.352 0.300 1
513 51 51 LYS CB C 32.495 0.300 1
514 51 51 LYS CG C 24.664 0.300 1
515 51 51 LYS CD C 29.194 0.300 1
516 51 51 LYS N N 123.996 0.300 1
517 52 52 PRO HA H 4.448 0.030 1
518 52 52 PRO HB2 H 2.259 0.030 2
519 52 52 PRO HB3 H 1.865 0.030 2
520 52 52 PRO HG2 H 1.998 0.030 2
521 52 52 PRO HG3 H 2.037 0.030 2
522 52 52 PRO HD2 H 3.638 0.030 2
523 52 52 PRO HD3 H 3.822 0.030 2
524 52 52 PRO C C 176.771 0.300 1
525 52 52 PRO CA C 63.031 0.300 1
526 52 52 PRO CB C 32.145 0.300 1
527 52 52 PRO CG C 27.413 0.300 1
528 52 52 PRO CD C 50.650 0.300 1
529 53 53 VAL H H 8.278 0.030 1
530 53 53 VAL HA H 4.066 0.030 1
531 53 53 VAL HB H 2.051 0.030 1
532 53 53 VAL HG1 H 0.967 0.030 1
533 53 53 VAL HG2 H 0.935 0.030 1
534 53 53 VAL C C 176.281 0.300 1
535 53 53 VAL CA C 62.437 0.300 1
536 53 53 VAL CB C 32.739 0.300 1
537 53 53 VAL CG1 C 20.673 0.300 2
538 53 53 VAL CG2 C 21.222 0.300 2
539 53 53 VAL N N 120.945 0.300 1
540 54 54 MET H H 8.451 0.030 1
541 54 54 MET HA H 4.567 0.030 1
542 54 54 MET HB2 H 2.107 0.030 2
543 54 54 MET HB3 H 2.012 0.030 2
544 54 54 MET HG2 H 2.509 0.030 2
545 54 54 MET HG3 H 2.642 0.030 2
546 54 54 MET HE H 2.092 0.030 1
547 54 54 MET C C 176.195 0.300 1
548 54 54 MET CA C 55.160 0.300 1
549 54 54 MET CB C 33.173 0.300 1
550 54 54 MET CG C 32.064 0.300 1
551 54 54 MET CE C 16.910 0.300 1
552 54 54 MET N N 124.530 0.300 1
553 55 55 GLY H H 8.234 0.030 1
554 55 55 GLY HA2 H 4.182 0.030 2
555 55 55 GLY HA3 H 3.995 0.030 2
556 55 55 GLY C C 170.991 0.300 1
557 55 55 GLY CA C 44.532 0.300 1
558 55 55 GLY N N 110.573 0.300 1
559 56 56 PRO HA H 4.724 0.030 1
560 56 56 PRO HB2 H 2.339 0.030 2
561 56 56 PRO HB3 H 1.941 0.030 2
562 56 56 PRO HG2 H 2.035 0.030 1
563 56 56 PRO HG3 H 2.035 0.030 1
564 56 56 PRO HD2 H 3.639 0.030 2
565 56 56 PRO HD3 H 3.599 0.030 2
566 56 56 PRO CA C 61.507 0.300 1
567 56 56 PRO CB C 30.879 0.300 1
568 56 56 PRO CG C 27.201 0.300 1
569 56 56 PRO CD C 49.660 0.300 1
570 57 57 PRO HA H 4.481 0.030 1
571 57 57 PRO HB2 H 2.308 0.030 2
572 57 57 PRO HB3 H 1.976 0.030 2
573 57 57 PRO HG2 H 2.049 0.030 1
574 57 57 PRO HG3 H 2.049 0.030 1
575 57 57 PRO HD2 H 3.825 0.030 2
576 57 57 PRO HD3 H 3.669 0.030 2
577 57 57 PRO C C 177.111 0.300 1
578 57 57 PRO CA C 63.246 0.300 1
579 57 57 PRO CB C 32.155 0.300 1
580 57 57 PRO CG C 27.374 0.300 1
581 57 57 PRO CD C 50.484 0.300 1
582 58 58 SER H H 8.390 0.030 1
583 58 58 SER HB2 H 3.883 0.030 1
584 58 58 SER HB3 H 3.883 0.030 1
585 58 58 SER C C 174.707 0.300 1
586 58 58 SER CA C 58.209 0.300 1
587 58 58 SER CB C 64.123 0.300 1
588 58 58 SER N N 115.863 0.300 1
589 60 60 PRO HA H 4.473 0.030 1
590 60 60 PRO HB2 H 2.300 0.030 2
591 60 60 PRO HB3 H 1.982 0.030 2
592 60 60 PRO HG2 H 2.033 0.030 1
593 60 60 PRO HG3 H 2.033 0.030 1
594 60 60 PRO HD2 H 3.640 0.030 2
595 60 60 PRO HD3 H 3.598 0.030 2
596 60 60 PRO C C 177.425 0.300 1
597 60 60 PRO CA C 63.343 0.300 1
598 60 60 PRO CB C 32.258 0.300 1
599 60 60 PRO CG C 27.142 0.300 1
600 60 60 PRO CD C 49.673 0.300 1
601 61 61 SER H H 8.522 0.030 1
602 61 61 SER C C 174.707 0.300 1
603 61 61 SER CA C 58.338 0.300 1
604 61 61 SER CB C 63.972 0.300 1
605 61 61 SER N N 116.392 0.300 1
606 62 62 SER HA H 4.498 0.030 1
607 62 62 SER HB2 H 3.924 0.030 2
608 62 62 SER HB3 H 3.882 0.030 2
609 62 62 SER C C 173.960 0.300 1
610 62 62 SER CA C 58.427 0.300 1
611 62 62 SER CB C 64.114 0.300 1
612 63 63 GLY H H 8.046 0.030 1
613 63 63 GLY C C 179.023 0.300 1
614 63 63 GLY CA C 46.282 0.300 1
615 63 63 GLY N N 116.889 0.300 1
stop_
save_