data_26809
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Xenopus laevis Nucleoplasmin Tail domain assigned chemical shifts
;
_BMRB_accession_number 26809
_BMRB_flat_file_name bmr26809.str
_Entry_type original
_Submission_date 2016-05-31
_Accession_date 2016-05-31
_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 Warren Christopher . .
2 Shechter David . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 170
"13C chemical shifts" 174
"15N chemical shifts" 52
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2017-11-16 original BMRB .
stop_
_Original_release_date 2016-05-31
save_
#############################
# Citation for this entry #
#############################
save_citation_1
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
DYNAMIC INTRAMOLECULAR REGULATION OF THE HISTONE CHAPERONE NUCLEOPLASMIN CONTROLS HISTONE BINDING AND RELEASE
;
_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 Warren Christopher . .
2 Shechter David . .
3 Warren Christopher . .
stop_
_Journal_abbreviation 'Not known'
_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 'Npm Tail Monomer'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Npm Tail' $Npm2_Tail_Domain
stop_
_System_molecular_weight .
_System_physical_state 'partially disordered'
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_Npm2_Tail_Domain
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Npm2_Tail_Domain
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 77
_Mol_residue_sequence
;
MEEDYSWAEEEDEGEEEEEE
EEDPESPPKAVKRPAATKKA
GQAKKKKLDKEDESSEEDSP
TKKGKGAGRGRKPAAKK
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 119 MET 2 120 GLU 3 121 GLU 4 122 ASP 5 123 TYR
6 124 SER 7 125 TRP 8 126 ALA 9 127 GLU 10 128 GLU
11 129 GLU 12 130 ASP 13 131 GLU 14 132 GLY 15 133 GLU
16 134 GLU 17 135 GLU 18 136 GLU 19 137 GLU 20 138 GLU
21 139 GLU 22 140 GLU 23 141 ASP 24 142 PRO 25 143 GLU
26 144 SER 27 145 PRO 28 146 PRO 29 147 LYS 30 148 ALA
31 149 VAL 32 150 LYS 33 151 ARG 34 152 PRO 35 153 ALA
36 154 ALA 37 155 THR 38 156 LYS 39 157 LYS 40 158 ALA
41 159 GLY 42 160 GLN 43 161 ALA 44 162 LYS 45 163 LYS
46 164 LYS 47 165 LYS 48 166 LEU 49 167 ASP 50 168 LYS
51 169 GLU 52 170 ASP 53 171 GLU 54 172 SER 55 173 SER
56 174 GLU 57 175 GLU 58 176 ASP 59 177 SER 60 178 PRO
61 179 THR 62 180 LYS 63 181 LYS 64 182 GLY 65 183 LYS
66 184 GLY 67 185 ALA 68 186 GLY 69 187 ARG 70 188 GLY
71 189 ARG 72 190 LYS 73 191 PRO 74 192 ALA 75 193 ALA
76 194 LYS 77 195 LYS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$Npm2_Tail_Domain 'African clawed frog' 8355 Eukaryota Metazoa Xenopus laevis
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
$Npm2_Tail_Domain 'recombinant technology' . Escherichia coli . pRUTH5-GST-Npm2Tail
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
$Npm2_Tail_Domain 860 mM '[U-13C; U-15N]'
'sodium phosphate' 25 mM 'natural abundance'
'sodium chloride' 25 mM 'natural abundance'
EDTA 1 mM 'natural abundance'
TSP 0.05 mM 'natural abundance'
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Vendor
_Address
_Electronic_address
CCPN . .
stop_
loop_
_Task
'peak picking'
processing
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_BrukerDRX600
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 600
_Details .
save_
save_VarianInova600
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $sample_1
save_
save_3D_HNCO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCO'
_Sample_label $sample_1
save_
save_3D_HN(CA)CO_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HN(CA)CO'
_Sample_label $sample_1
save_
save_3D_HNCA_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCA'
_Sample_label $sample_1
save_
save_3D_HN(CO)CA_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HN(CO)CA'
_Sample_label $sample_1
save_
save_3D_CBCA(CO)NH_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CBCA(CO)NH'
_Sample_label $sample_1
save_
save_3D_HNCACB_7
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCACB'
_Sample_label $sample_1
save_
save_3D_HBHA(CO)NH_8
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HBHA(CO)NH'
_Sample_label $sample_1
save_
save_2D_1H-13C_HSQC_9
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-13C HSQC'
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 25 . mM
pH 7.0 . pH
pressure 1 . atm
temperature 298 . K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_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 C 13 'methyl protons' ppm 0.00 internal indirect . . . 0.251449530
TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000
TSP N 15 'methyl protons' ppm 0.00 internal 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_assigned_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-15N HSQC'
'3D HNCO'
'3D HN(CA)CO'
'3D HNCA'
'3D HN(CO)CA'
'3D CBCA(CO)NH'
'3D HNCACB'
'3D HBHA(CO)NH'
'2D 1H-13C HSQC'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference_1
_Mol_system_component_name 'Npm Tail'
_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
1 121 3 GLU H H 8.595 . 1
2 121 3 GLU HA H 4.214 . 1
3 121 3 GLU HB2 H 1.943 . 1
4 121 3 GLU HB3 H 1.874 . 1
5 121 3 GLU C C 175.83 . 1
6 121 3 GLU CA C 56.83 . 1
7 121 3 GLU CB C 30.27 . 1
8 121 3 GLU N N 121.75 . 1
9 122 4 ASP H H 8.289 . 1
10 122 4 ASP HA H 4.544 . 1
11 122 4 ASP HB2 H 2.623 . 1
12 122 4 ASP HB3 H 2.575 . 1
13 122 4 ASP C C 175.84 . 1
14 122 4 ASP CA C 54.10 . 1
15 122 4 ASP CB C 41.43 . 1
16 122 4 ASP N N 121.04 . 1
17 123 5 TYR H H 8.134 . 1
18 123 5 TYR HA H 4.474 . 1
19 123 5 TYR HB2 H 2.926 . 1
20 123 5 TYR HB3 H 2.832 . 1
21 123 5 TYR C C 175.83 . 1
22 123 5 TYR CA C 57.81 . 1
23 123 5 TYR CB C 38.44 . 1
24 123 5 TYR N N 121.36 . 1
25 124 6 SER H H 8.170 . 1
26 124 6 SER HA H 4.355 . 1
27 124 6 SER HB2 H 3.769 . 1
28 124 6 SER C C 173.96 . 1
29 124 6 SER CA C 58.55 . 1
30 124 6 SER CB C 63.77 . 1
31 124 6 SER N N 117.82 . 1
32 125 7 TRP H H 7.936 . 1
33 125 7 TRP HA H 4.619 . 1
34 125 7 TRP HB2 H 3.278 . 1
35 125 7 TRP HE1 H 10.183 . 1
36 125 7 TRP C C 175.75 . 1
37 125 7 TRP CA C 57.19 . 1
38 125 7 TRP CB C 29.76 . 1
39 125 7 TRP N N 122.97 . 1
40 125 7 TRP NE1 N 129.70 . 1
41 126 8 ALA H H 7.914 . 1
42 126 8 ALA HA H 4.236 . 1
43 126 8 ALA HB H 1.217 . 1
44 126 8 ALA C C 177.22 . 1
45 126 8 ALA CA C 52.39 . 1
46 126 8 ALA CB C 19.60 . 1
47 126 8 ALA N N 125.64 . 1
48 127 9 GLU H H 8.155 . 1
49 127 9 GLU C C 176.54 . 1
50 127 9 GLU CA C 56.63 . 1
51 127 9 GLU CB C 30.30 . 1
52 127 9 GLU N N 120.07 . 1
53 130 12 ASP H H 8.431 . 1
54 130 12 ASP HA H 4.636 . 1
55 130 12 ASP HB2 H 2.717 . 1
56 130 12 ASP HB3 H 2.624 . 1
57 130 12 ASP C C 176.08 . 1
58 130 12 ASP CA C 54.30 . 1
59 130 12 ASP CB C 41.60 . 1
60 130 12 ASP N N 121.98 . 1
61 131 13 GLU H H 8.508 . 1
62 131 13 GLU HA H 4.310 . 1
63 131 13 GLU HB2 H 2.109 . 1
64 131 13 GLU HB3 H 1.961 . 1
65 131 13 GLU C C 177.00 . 1
66 131 13 GLU CA C 56.65 . 1
67 131 13 GLU CB C 30.77 . 1
68 131 13 GLU N N 122.16 . 1
69 132 14 GLY H H 8.495 . 1
70 132 14 GLY HA2 H 3.983 . 1
71 132 14 GLY C C 173.96 . 1
72 132 14 GLY CA C 45.37 . 1
73 132 14 GLY N N 109.80 . 1
74 133 15 GLU H H 8.337 . 1
75 133 15 GLU C C 176.54 . 1
76 133 15 GLU CA C 56.19 . 1
77 133 15 GLU CB C 30.78 . 1
78 133 15 GLU N N 120.39 . 1
79 140 22 GLU HA H 4.261 . 1
80 140 22 GLU HB2 H 2.010 . 1
81 140 22 GLU HB3 H 1.919 . 1
82 140 22 GLU C C 175.91 . 1
83 140 22 GLU CA C 56.54 . 1
84 140 22 GLU CB C 30.77 . 1
85 141 23 ASP H H 8.583 . 1
86 141 23 ASP C C 175.37 . 1
87 141 23 ASP CA C 51.83 . 1
88 141 23 ASP CB C 41.89 . 1
89 141 23 ASP N N 123.32 . 1
90 142 24 PRO HA H 4.448 . 1
91 142 24 PRO HB2 H 2.349 . 1
92 142 24 PRO HB3 H 2.018 . 1
93 142 24 PRO C C 177.47 . 1
94 142 24 PRO CA C 64.08 . 1
95 142 24 PRO CB C 32.31 . 1
96 143 25 GLU H H 8.429 . 1
97 143 25 GLU HA H 4.309 . 1
98 143 25 GLU HB2 H 2.174 . 1
99 143 25 GLU HB3 H 1.967 . 1
100 143 25 GLU C C 176.54 . 1
101 143 25 GLU CA C 56.39 . 1
102 143 25 GLU CB C 29.77 . 1
103 143 25 GLU N N 117.63 . 1
104 144 26 SER H H 7.791 . 1
105 144 26 SER C C 172.01 . 1
106 144 26 SER CA C 56.70 . 1
107 144 26 SER CB C 63.28 . 1
108 144 26 SER N N 116.76 . 1
109 146 28 PRO HA H 4.425 . 1
110 146 28 PRO HB2 H 2.347 . 1
111 146 28 PRO HB3 H 1.918 . 1
112 146 28 PRO C C 177.28 . 1
113 146 28 PRO CA C 63.11 . 1
114 146 28 PRO CB C 32.04 . 1
115 147 29 LYS H H 8.684 . 1
116 147 29 LYS HA H 4.262 . 1
117 147 29 LYS HB2 H 1.850 . 1
118 147 29 LYS HB3 H 1.776 . 1
119 147 29 LYS C C 176.54 . 1
120 147 29 LYS CA C 56.42 . 1
121 147 29 LYS CB C 33.31 . 1
122 147 29 LYS N N 122.33 . 1
123 148 30 ALA H H 8.286 . 1
124 148 30 ALA HA H 4.331 . 1
125 148 30 ALA HB H 1.381 . 1
126 148 30 ALA C C 177.47 . 1
127 148 30 ALA CA C 52.45 . 1
128 148 30 ALA CB C 19.55 . 1
129 148 30 ALA N N 124.46 . 1
130 149 31 VAL H H 8.028 . 1
131 149 31 VAL HA H 4.096 . 1
132 149 31 VAL HB H 2.039 . 1
133 149 31 VAL C C 175.94 . 1
134 149 31 VAL CA C 62.12 . 1
135 149 31 VAL CB C 33.06 . 1
136 149 31 VAL N N 119.21 . 1
137 150 32 LYS H H 8.423 . 1
138 150 32 LYS C C 176.07 . 1
139 150 32 LYS CA C 56.18 . 1
140 150 32 LYS CB C 33.31 . 1
141 150 32 LYS N N 125.57 . 1
142 152 34 PRO HA H 4.402 . 1
143 152 34 PRO HB2 H 2.310 . 1
144 152 34 PRO HB3 H 1.920 . 1
145 152 34 PRO C C 176.74 . 1
146 152 34 PRO CA C 63.20 . 1
147 152 34 PRO CB C 32.24 . 1
148 153 35 ALA H H 8.461 . 1
149 153 35 ALA HA H 4.285 . 1
150 153 35 ALA HB H 1.406 . 1
151 153 35 ALA C C 177.71 . 1
152 153 35 ALA CA C 52.63 . 1
153 153 35 ALA CB C 19.50 . 1
154 153 35 ALA N N 124.43 . 1
155 154 36 ALA H H 8.382 . 1
156 154 36 ALA HA H 4.356 . 1
157 154 36 ALA HB H 1.415 . 1
158 154 36 ALA C C 177.95 . 1
159 154 36 ALA CA C 52.65 . 1
160 154 36 ALA CB C 19.60 . 1
161 154 36 ALA N N 123.31 . 1
162 155 37 THR H H 8.096 . 1
163 155 37 THR HA H 4.302 . 1
164 155 37 THR HB H 1.406 . 1
165 155 37 THR C C 174.66 . 1
166 155 37 THR CA C 62.02 . 1
167 155 37 THR CB C 69.87 . 1
168 155 37 THR N N 113.29 . 1
169 156 38 LYS H H 8.350 . 1
170 156 38 LYS HA H 4.285 . 1
171 156 38 LYS HB2 H 1.803 . 1
172 156 38 LYS HB3 H 1.754 . 1
173 156 38 LYS C C 176.54 . 1
174 156 38 LYS CA C 56.41 . 1
175 156 38 LYS CB C 33.25 . 1
176 156 38 LYS N N 123.95 . 1
177 157 39 LYS H H 8.411 . 1
178 157 39 LYS HA H 4.284 . 1
179 157 39 LYS HB2 H 1.827 . 1
180 157 39 LYS HB3 H 1.742 . 1
181 157 39 LYS C C 176.30 . 1
182 157 39 LYS CA C 56.40 . 1
183 157 39 LYS CB C 33.30 . 1
184 157 39 LYS N N 123.52 . 1
185 158 40 ALA H H 8.401 . 1
186 158 40 ALA HA H 4.323 . 1
187 158 40 ALA HB H 1.408 . 1
188 158 40 ALA C C 178.40 . 1
189 158 40 ALA CA C 52.87 . 1
190 158 40 ALA CB C 19.29 . 1
191 158 40 ALA N N 125.47 . 1
192 159 41 GLY H H 8.465 . 1
193 159 41 GLY HA2 H 3.958 . 1
194 159 41 GLY C C 174.42 . 1
195 159 41 GLY CA C 45.41 . 1
196 159 41 GLY N N 108.40 . 1
197 160 42 GLN H H 8.203 . 1
198 160 42 GLN HA H 4.332 . 1
199 160 42 GLN HB2 H 2.118 . 1
200 160 42 GLN HB3 H 1.991 . 1
201 160 42 GLN HE21 H 7.606 . 1
202 160 42 GLN HE22 H 6.934 . 1
203 160 42 GLN C C 175.90 . 1
204 160 42 GLN CA C 55.92 . 1
205 160 42 GLN CB C 29.77 . 1
206 160 42 GLN N N 119.81 . 1
207 160 42 GLN NE2 N 112.71 . 1
208 161 43 ALA H H 8.387 . 1
209 161 43 ALA HA H 4.295 . 1
210 161 43 ALA HB H 1.404 . 1
211 161 43 ALA C C 177.83 . 1
212 161 43 ALA CA C 52.87 . 1
213 161 43 ALA CB C 19.26 . 1
214 161 43 ALA N N 125.27 . 1
215 162 44 LYS H H 8.316 . 1
216 162 44 LYS C C 176.71 . 1
217 162 44 LYS CA C 56.36 . 1
218 162 44 LYS CB C 33.28 . 1
219 162 44 LYS N N 120.80 . 1
220 165 47 LYS HA H 4.305 . 1
221 165 47 LYS HB2 H 1.826 . 1
222 165 47 LYS HB3 H 1.757 . 1
223 165 47 LYS C C 176.43 . 1
224 165 47 LYS CA C 56.40 . 1
225 165 47 LYS CB C 33.29 . 1
226 166 48 LEU H H 8.401 . 1
227 166 48 LEU HA H 4.377 . 1
228 166 48 LEU HB2 H 1.625 . 1
229 166 48 LEU C C 177.00 . 1
230 166 48 LEU CA C 55.04 . 1
231 166 48 LEU CB C 42.46 . 1
232 166 48 LEU N N 124.03 . 1
233 167 49 ASP H H 8.388 . 1
234 167 49 ASP HA H 4.589 . 1
235 167 49 ASP HB2 H 2.716 . 1
236 167 49 ASP HB3 H 2.621 . 1
237 167 49 ASP C C 176.10 . 1
238 167 49 ASP CA C 54.53 . 1
239 167 49 ASP CB C 41.43 . 1
240 167 49 ASP N N 121.54 . 1
241 168 50 LYS H H 8.222 . 1
242 168 50 LYS C C 176.64 . 1
243 168 50 LYS CA C 56.40 . 1
244 168 50 LYS CB C 33.30 . 1
245 168 50 LYS N N 120.88 . 1
246 171 53 GLU HA H 4.331 . 1
247 171 53 GLU HB2 H 2.112 . 1
248 171 53 GLU HB3 H 1.968 . 1
249 171 53 GLU C C 176.62 . 1
250 171 53 GLU CA C 56.80 . 1
251 171 53 GLU CB C 30.27 . 1
252 172 54 SER H H 8.429 . 1
253 172 54 SER HA H 4.495 . 1
254 172 54 SER HB2 H 3.910 . 1
255 172 54 SER C C 174.68 . 1
256 172 54 SER CA C 58.62 . 1
257 172 54 SER CB C 63.79 . 1
258 172 54 SER N N 116.86 . 1
259 173 55 SER H H 8.409 . 1
260 173 55 SER C C 174.70 . 1
261 173 55 SER CA C 58.51 . 1
262 173 55 SER CB C 63.78 . 1
263 173 55 SER N N 118.04 . 1
264 175 57 GLU H H 8.409 . 1
265 175 57 GLU HA H 4.260 . 1
266 175 57 GLU HB2 H 2.063 . 1
267 175 57 GLU HB3 H 1.949 . 1
268 175 57 GLU C C 176.30 . 1
269 175 57 GLU CA C 56.87 . 1
270 175 57 GLU CB C 30.27 . 1
271 175 57 GLU N N 121.23 . 1
272 176 58 ASP H H 8.344 . 1
273 176 58 ASP HA H 4.636 . 1
274 176 58 ASP HB2 H 2.693 . 1
275 176 58 ASP HB3 H 2.626 . 1
276 176 58 ASP C C 175.85 . 1
277 176 58 ASP CA C 54.38 . 1
278 176 58 ASP CB C 41.43 . 1
279 176 58 ASP N N 120.82 . 1
280 177 59 SER H H 8.114 . 1
281 177 59 SER C C 173.49 . 1
282 177 59 SER CA C 56.40 . 1
283 177 59 SER CB C 63.78 . 1
284 177 59 SER N N 116.60 . 1
285 178 60 PRO HA H 4.495 . 1
286 178 60 PRO HB2 H 2.356 . 1
287 178 60 PRO HB3 H 1.989 . 1
288 178 60 PRO C C 177.61 . 1
289 178 60 PRO CA C 64.10 . 1
290 178 60 PRO CB C 32.28 . 1
291 179 61 THR H H 8.054 . 1
292 179 61 THR HA H 4.299 . 1
293 179 61 THR HB H 4.241 . 1
294 179 61 THR C C 174.89 . 1
295 179 61 THR CA C 62.27 . 1
296 179 61 THR CB C 69.37 . 1
297 179 61 THR N N 112.22 . 1
298 180 62 LYS H H 8.097 . 1
299 180 62 LYS HA H 4.331 . 1
300 180 62 LYS HB2 H 1.874 . 1
301 180 62 LYS HB3 H 1.794 . 1
302 180 62 LYS C C 176.53 . 1
303 180 62 LYS CA C 56.63 . 1
304 180 62 LYS CB C 32.83 . 1
305 180 62 LYS N N 123.34 . 1
306 181 63 LYS H H 8.313 . 1
307 181 63 LYS HA H 4.310 . 1
308 181 63 LYS HB2 H 1.852 . 1
309 181 63 LYS HB3 H 1.780 . 1
310 181 63 LYS C C 177.24 . 1
311 181 63 LYS CA C 56.63 . 1
312 181 63 LYS CB C 33.30 . 1
313 181 63 LYS N N 122.20 . 1
314 182 64 GLY H H 8.450 . 1
315 182 64 GLY C C 174.19 . 1
316 182 64 GLY CA C 45.37 . 1
317 182 64 GLY N N 110.01 . 1
318 183 65 LYS HA H 4.550 . 1
319 183 65 LYS HB2 H 1.898 . 1
320 183 65 LYS HB3 H 1.779 . 1
321 183 65 LYS C C 176.97 . 1
322 183 65 LYS CA C 56.40 . 1
323 183 65 LYS CB C 30.77 . 1
324 184 66 GLY H H 8.550 . 1
325 184 66 GLY HA2 H 3.957 . 1
326 184 66 GLY C C 173.96 . 1
327 184 66 GLY CA C 45.38 . 1
328 184 66 GLY N N 109.87 . 1
329 185 67 ALA H H 8.263 . 1
330 185 67 ALA HA H 4.333 . 1
331 185 67 ALA HB H 1.405 . 1
332 185 67 ALA C C 178.41 . 1
333 185 67 ALA CA C 52.66 . 1
334 185 67 ALA CB C 19.60 . 1
335 185 67 ALA N N 123.77 . 1
336 186 68 GLY H H 8.501 . 1
337 186 68 GLY C C 174.43 . 1
338 186 68 GLY CA C 45.38 . 1
339 186 68 GLY N N 108.23 . 1
340 187 69 ARG HA H 4.332 . 1
341 187 69 ARG HB2 H 1.873 . 1
342 187 69 ARG HB3 H 1.775 . 1
343 187 69 ARG C C 177.46 . 1
344 187 69 ARG CA C 56.60 . 1
345 187 69 ARG CB C 32.97 . 1
346 188 70 GLY H H 8.584 . 1
347 188 70 GLY HA2 H 3.959 . 1
348 188 70 GLY C C 173.97 . 1
349 188 70 GLY CA C 45.39 . 1
350 188 70 GLY N N 110.18 . 1
351 189 71 ARG H H 8.218 . 1
352 189 71 ARG HA H 4.357 . 1
353 189 71 ARG HB2 H 1.826 . 1
354 189 71 ARG HB3 H 1.732 . 1
355 189 71 ARG C C 176.26 . 1
356 189 71 ARG CA C 55.88 . 1
357 189 71 ARG CB C 31.23 . 1
358 189 71 ARG N N 120.63 . 1
359 190 72 LYS H H 8.475 . 1
360 190 72 LYS C C 174.43 . 1
361 190 72 LYS CA C 54.29 . 1
362 190 72 LYS CB C 32.57 . 1
363 190 72 LYS N N 124.38 . 1
364 191 73 PRO HA H 4.401 . 1
365 191 73 PRO HB2 H 2.302 . 1
366 191 73 PRO HB3 H 1.909 . 1
367 191 73 PRO C C 176.54 . 1
368 191 73 PRO CA C 63.22 . 1
369 191 73 PRO CB C 32.29 . 1
370 192 74 ALA H H 8.423 . 1
371 192 74 ALA HA H 4.269 . 1
372 192 74 ALA HB H 1.383 . 1
373 192 74 ALA C C 177.48 . 1
374 192 74 ALA CA C 52.37 . 1
375 192 74 ALA CB C 19.59 . 1
376 192 74 ALA N N 124.70 . 1
377 193 75 ALA H H 8.309 . 1
378 193 75 ALA HA H 4.296 . 1
379 193 75 ALA HB H 1.393 . 1
380 193 75 ALA C C 177.51 . 1
381 193 75 ALA CA C 52.41 . 1
382 193 75 ALA CB C 19.62 . 1
383 193 75 ALA N N 123.74 . 1
384 194 76 LYS H H 8.318 . 1
385 194 76 LYS HA H 4.308 . 1
386 194 76 LYS HB2 H 1.861 . 1
387 194 76 LYS HB3 H 1.756 . 1
388 194 76 LYS C C 175.60 . 1
389 194 76 LYS CA C 56.35 . 1
390 194 76 LYS CB C 33.30 . 1
391 194 76 LYS N N 121.69 . 1
392 195 77 LYS H H 8.004 . 1
393 195 77 LYS C C 181.23 . 1
394 195 77 LYS CA C 57.81 . 1
395 195 77 LYS CB C 33.81 . 1
396 195 77 LYS N N 128.39 . 1
stop_
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