data_27247
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Backbone assignments of domain swapped dimer of engineered hairpin loop3 mutant of single chain Monellin
;
_BMRB_accession_number 27247
_BMRB_flat_file_name bmr27247.str
_Entry_type original
_Submission_date 2017-09-08
_Accession_date 2017-09-08
_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 Surana Parag . .
2 Nandwani Neha . .
3 Udgaonkar Jayant B. .
4 Gosavi Shachi . .
5 Das Ranabir . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 90
"13C chemical shifts" 256
"15N chemical shifts" 90
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2019-02-08 original BMRB .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
27246 'Backbone assignments of domain swapped dimer of engineered hairpin loop3 mutant of single chain Monellin'
stop_
_Original_release_date 2017-09-11
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
A five-residue motif for the design of domain swapping in proteins.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 30692525
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Nandwani Neha . .
2 Surana Parag . .
3 Negi Hitendra . .
4 Mascarenhas Nahren M. .
5 Udgaonkar Jayant B. .
6 Das Ranabir . .
7 Gosavi Shachi . .
stop_
_Journal_abbreviation 'Nat. Commun.'
_Journal_name_full 'Nature communications'
_Journal_volume 10
_Journal_issue 1
_Journal_ISSN 2041-1723
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 452
_Page_last 452
_Year 2019
_Details .
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name 'domain swapped dimer'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'single chain monellin, 1' $single_chain_monellin
'single chain monellin, 2' $single_chain_monellin
stop_
_System_molecular_weight 23000
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_single_chain_monellin
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common single_chain_monellin
_Molecular_mass 11479
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 100
_Mol_residue_sequence
;
MGEWEIIDIGPFTQNLGKFA
VDEENKIGQYGRLTFNKVIR
PCMKKTIYENEGFREIKGYE
YQLYVYASDKLFRADISEQV
VAGGRKLLRFNGPVPPPSTP
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 GLY 3 GLU 4 TRP 5 GLU
6 ILE 7 ILE 8 ASP 9 ILE 10 GLY
11 PRO 12 PHE 13 THR 14 GLN 15 ASN
16 LEU 17 GLY 18 LYS 19 PHE 20 ALA
21 VAL 22 ASP 23 GLU 24 GLU 25 ASN
26 LYS 27 ILE 28 GLY 29 GLN 30 TYR
31 GLY 32 ARG 33 LEU 34 THR 35 PHE
36 ASN 37 LYS 38 VAL 39 ILE 40 ARG
41 PRO 42 CYS 43 MET 44 LYS 45 LYS
46 THR 47 ILE 48 TYR 49 GLU 50 ASN
51 GLU 52 GLY 53 PHE 54 ARG 55 GLU
56 ILE 57 LYS 58 GLY 59 TYR 60 GLU
61 TYR 62 GLN 63 LEU 64 TYR 65 VAL
66 TYR 67 ALA 68 SER 69 ASP 70 LYS
71 LEU 72 PHE 73 ARG 74 ALA 75 ASP
76 ILE 77 SER 78 GLU 79 GLN 80 VAL
81 VAL 82 ALA 83 GLY 84 GLY 85 ARG
86 LYS 87 LEU 88 LEU 89 ARG 90 PHE
91 ASN 92 GLY 93 PRO 94 VAL 95 PRO
96 PRO 97 PRO 98 SER 99 THR 100 PRO
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
$single_chain_monellin 'serendipity berry' 3457 Eukaryota Viridiplantae Dioscoreophyllum cumminsi
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
$single_chain_monellin 'recombinant technology' . Escherichia coli . pET22b+
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
$single_chain_monellin 350 uM '[U-13C; U-15N]'
stop_
save_
############################
# Computer software used #
############################
save_TOPSPIN
_Saveframe_category software
_Name TOPSPIN
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Bruker Biospin' . .
stop_
loop_
_Task
collection
stop_
_Details .
save_
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . .
stop_
loop_
_Task
processing
stop_
_Details .
save_
save_SPARKY
_Saveframe_category software
_Name SPARKY
_Version .
loop_
_Vendor
_Address
_Electronic_address
Goddard . .
stop_
loop_
_Task
'chemical shift assignment'
'peak picking'
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_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_HNCA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCA'
_Sample_label $sample_1
save_
save_3D_HNCACB_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCACB'
_Sample_label $sample_1
save_
save_3D_CBCA(CO)NH_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D CBCA(CO)NH'
_Sample_label $sample_1
save_
save_3D_HN(CO)CA_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HN(CO)CA'
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details '10mM Sodium Phosphate pH 7.0'
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 10 . 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
DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000
DSS N 15 'methyl protons' ppm 0.00 na 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_
_Software_label
$TOPSPIN
$NMRPipe
$SPARKY
stop_
loop_
_Experiment_label
'2D 1H-15N HSQC'
'3D HNCO'
'3D HNCA'
'3D HNCACB'
'3D CBCA(CO)NH'
'3D HN(CO)CA'
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 'single chain monellin, 1'
_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 2 2 GLY H H 8.035 0.000 .
2 2 2 GLY C C 170.970 0.000 .
3 2 2 GLY CA C 42.793 0.049 .
4 2 2 GLY N N 112.151 0.000 .
5 3 3 GLU H H 8.672 0.005 .
6 3 3 GLU C C 173.289 0.000 .
7 3 3 GLU CA C 54.203 0.005 .
8 3 3 GLU CB C 27.575 0.000 .
9 3 3 GLU N N 120.430 0.049 .
10 4 4 TRP H H 8.144 0.006 .
11 4 4 TRP CA C 54.281 0.082 .
12 4 4 TRP CB C 28.190 0.000 .
13 4 4 TRP N N 119.915 0.052 .
14 5 5 GLU H H 9.418 0.000 .
15 5 5 GLU CA C 51.785 0.024 .
16 5 5 GLU N N 123.332 0.000 .
17 6 6 ILE H H 8.649 0.005 .
18 6 6 ILE C C 174.535 0.000 .
19 6 6 ILE CA C 58.551 0.054 .
20 6 6 ILE CB C 35.603 0.000 .
21 6 6 ILE N N 124.092 0.000 .
22 7 7 ILE H H 8.560 0.007 .
23 7 7 ILE C C 171.602 0.000 .
24 7 7 ILE CA C 56.657 0.025 .
25 7 7 ILE CB C 38.080 0.005 .
26 7 7 ILE N N 122.955 0.108 .
27 8 8 ASP H H 8.118 0.004 .
28 8 8 ASP C C 173.430 0.000 .
29 8 8 ASP CA C 51.020 0.055 .
30 8 8 ASP CB C 39.089 0.071 .
31 8 8 ASP N N 119.819 0.034 .
32 9 9 ILE H H 8.089 0.007 .
33 9 9 ILE C C 173.791 0.000 .
34 9 9 ILE CA C 57.109 0.027 .
35 9 9 ILE CB C 34.751 0.104 .
36 9 9 ILE N N 114.749 0.151 .
37 10 10 GLY H H 8.035 0.005 .
38 10 10 GLY CA C 42.519 0.013 .
39 10 10 GLY N N 112.076 0.049 .
40 11 11 PRO C C 175.630 0.000 .
41 11 11 PRO CA C 63.370 0.002 .
42 11 11 PRO CB C 29.579 0.000 .
43 12 12 PHE H H 8.490 0.002 .
44 12 12 PHE C C 175.027 0.000 .
45 12 12 PHE CA C 59.055 0.075 .
46 12 12 PHE CB C 36.068 0.009 .
47 12 12 PHE N N 118.045 0.046 .
48 13 13 THR H H 7.532 0.007 .
49 13 13 THR C C 174.610 0.000 .
50 13 13 THR CA C 62.660 0.028 .
51 13 13 THR CB C 65.728 0.017 .
52 13 13 THR N N 114.933 0.049 .
53 14 14 GLN H H 8.409 0.004 .
54 14 14 GLN C C 175.579 0.000 .
55 14 14 GLN CA C 55.934 0.041 .
56 14 14 GLN CB C 24.589 0.055 .
57 14 14 GLN N N 119.965 0.041 .
58 15 15 ASN H H 7.825 0.003 .
59 15 15 ASN C C 175.560 0.000 .
60 15 15 ASN CA C 53.229 0.043 .
61 15 15 ASN CB C 35.219 0.112 .
62 15 15 ASN N N 116.695 0.057 .
63 16 16 LEU H H 7.302 0.005 .
64 16 16 LEU C C 175.846 0.000 .
65 16 16 LEU CA C 55.092 0.031 .
66 16 16 LEU CB C 39.659 0.058 .
67 16 16 LEU N N 121.778 0.022 .
68 17 17 GLY H H 7.652 0.005 .
69 17 17 GLY C C 171.177 0.000 .
70 17 17 GLY CA C 44.972 0.045 .
71 17 17 GLY N N 106.393 0.049 .
72 18 18 LYS H H 7.339 0.004 .
73 18 18 LYS C C 175.312 0.000 .
74 18 18 LYS CA C 57.085 0.028 .
75 18 18 LYS CB C 29.291 0.086 .
76 18 18 LYS N N 122.847 0.048 .
77 19 19 PHE H H 7.648 0.005 .
78 19 19 PHE C C 173.311 0.000 .
79 19 19 PHE CA C 58.078 0.044 .
80 19 19 PHE CB C 35.145 0.050 .
81 19 19 PHE N N 119.433 0.057 .
82 20 20 ALA H H 8.061 0.004 .
83 20 20 ALA C C 175.563 0.000 .
84 20 20 ALA CA C 52.457 0.079 .
85 20 20 ALA CB C 15.177 0.060 .
86 20 20 ALA N N 120.152 0.063 .
87 21 21 VAL H H 7.680 0.004 .
88 21 21 VAL C C 173.903 0.000 .
89 21 21 VAL CA C 64.256 0.039 .
90 21 21 VAL CB C 28.781 0.285 .
91 21 21 VAL N N 116.014 0.054 .
92 22 22 ASP H H 8.408 0.006 .
93 22 22 ASP C C 177.543 0.000 .
94 22 22 ASP CA C 54.876 0.054 .
95 22 22 ASP CB C 37.015 0.049 .
96 22 22 ASP N N 121.186 0.019 .
97 23 23 GLU H H 8.206 0.005 .
98 23 23 GLU C C 177.061 0.000 .
99 23 23 GLU CA C 55.679 0.023 .
100 23 23 GLU CB C 27.185 0.071 .
101 23 23 GLU N N 118.402 0.077 .
102 24 24 GLU H H 8.305 0.005 .
103 24 24 GLU C C 177.098 0.000 .
104 24 24 GLU CA C 54.773 0.029 .
105 24 24 GLU CB C 24.054 0.102 .
106 24 24 GLU N N 123.591 0.059 .
107 25 25 ASN H H 8.685 0.003 .
108 25 25 ASN C C 175.324 0.000 .
109 25 25 ASN CA C 52.042 0.089 .
110 25 25 ASN CB C 34.639 0.064 .
111 25 25 ASN N N 121.269 0.062 .
112 26 26 LYS H H 7.085 0.004 .
113 26 26 LYS C C 174.916 0.000 .
114 26 26 LYS CA C 56.241 0.055 .
115 26 26 LYS CB C 29.716 0.077 .
116 26 26 LYS N N 118.878 0.057 .
117 27 27 ILE H H 7.159 0.005 .
118 27 27 ILE C C 176.178 0.000 .
119 27 27 ILE CA C 60.661 0.046 .
120 27 27 ILE CB C 35.379 0.024 .
121 27 27 ILE N N 119.200 0.040 .
122 28 28 GLY H H 8.122 0.004 .
123 28 28 GLY C C 173.728 0.000 .
124 28 28 GLY CA C 43.714 0.025 .
125 28 28 GLY N N 104.484 0.062 .
126 29 29 GLN H H 7.032 0.004 .
127 29 29 GLN C C 173.564 0.000 .
128 29 29 GLN CA C 55.621 0.109 .
129 29 29 GLN CB C 25.925 0.089 .
130 29 29 GLN N N 119.929 0.043 .
131 30 30 TYR H H 8.604 0.004 .
132 30 30 TYR C C 172.870 0.000 .
133 30 30 TYR CA C 54.396 0.054 .
134 30 30 TYR CB C 36.011 0.006 .
135 30 30 TYR N N 117.010 0.052 .
136 31 31 GLY H H 7.202 0.004 .
137 31 31 GLY C C 170.369 0.000 .
138 31 31 GLY CA C 42.014 0.036 .
139 31 31 GLY N N 106.628 0.074 .
140 32 32 ARG H H 8.372 0.004 .
141 32 32 ARG C C 173.289 0.000 .
142 32 32 ARG CA C 53.079 0.078 .
143 32 32 ARG CB C 26.491 0.085 .
144 32 32 ARG N N 122.902 0.056 .
145 33 33 LEU H H 9.485 0.006 .
146 33 33 LEU C C 175.144 0.000 .
147 33 33 LEU CA C 50.879 0.055 .
148 33 33 LEU CB C 42.946 0.043 .
149 33 33 LEU N N 129.863 0.071 .
150 34 34 THR H H 8.347 0.004 .
151 34 34 THR C C 171.232 0.000 .
152 34 34 THR CA C 58.030 0.039 .
153 34 34 THR CB C 67.585 0.018 .
154 34 34 THR N N 117.412 0.044 .
155 35 35 PHE H H 9.364 0.006 .
156 35 35 PHE C C 170.921 0.000 .
157 35 35 PHE CA C 57.600 0.037 .
158 35 35 PHE CB C 36.522 0.055 .
159 35 35 PHE N N 127.652 0.049 .
160 36 36 ASN H H 8.305 0.004 .
161 36 36 ASN C C 170.169 0.000 .
162 36 36 ASN CA C 51.932 0.063 .
163 36 36 ASN CB C 38.300 0.006 .
164 36 36 ASN N N 125.532 0.047 .
165 37 37 LYS H H 7.027 0.005 .
166 37 37 LYS C C 170.813 0.000 .
167 37 37 LYS CA C 53.911 0.028 .
168 37 37 LYS CB C 30.409 0.012 .
169 37 37 LYS N N 110.237 0.051 .
170 38 38 VAL H H 9.274 0.005 .
171 38 38 VAL C C 173.715 0.000 .
172 38 38 VAL CA C 59.079 0.041 .
173 38 38 VAL CB C 30.337 0.069 .
174 38 38 VAL N N 121.709 0.068 .
175 39 39 ILE H H 7.738 0.006 .
176 39 39 ILE C C 171.204 0.000 .
177 39 39 ILE CA C 56.813 0.058 .
178 39 39 ILE CB C 38.527 0.030 .
179 39 39 ILE N N 117.889 0.059 .
180 40 40 ARG H H 8.176 0.006 .
181 40 40 ARG CA C 52.272 0.029 .
182 40 40 ARG CB C 27.232 0.000 .
183 40 40 ARG N N 118.740 0.062 .
184 41 41 PRO C C 116.153 57.553 .
185 41 41 PRO CA C 58.624 0.059 .
186 41 41 PRO CB C 31.738 0.000 .
187 42 42 CYS H H 8.972 0.003 .
188 42 42 CYS C C 170.446 0.000 .
189 42 42 CYS CA C 55.821 0.034 .
190 42 42 CYS CB C 25.979 0.109 .
191 42 42 CYS N N 125.024 0.049 .
192 43 43 MET H H 8.972 0.000 .
193 43 43 MET C C 172.074 0.000 .
194 43 43 MET CA C 50.964 0.062 .
195 43 43 MET CB C 30.417 0.000 .
196 43 43 MET N N 125.007 0.000 .
197 44 44 LYS H H 9.702 0.005 .
198 44 44 LYS C C 171.371 0.000 .
199 44 44 LYS CA C 51.847 0.100 .
200 44 44 LYS CB C 35.512 0.000 .
201 44 44 LYS N N 123.086 0.016 .
202 45 45 LYS H H 9.299 0.004 .
203 45 45 LYS C C 172.516 0.000 .
204 45 45 LYS CA C 51.487 0.025 .
205 45 45 LYS CB C 31.973 0.000 .
206 45 45 LYS N N 129.864 0.080 .
207 46 46 THR H H 8.469 0.006 .
208 46 46 THR C C 169.28 0 .
209 46 46 THR CA C 60.498 0.067 .
210 46 46 THR CB C 66.436 0.018 .
211 46 46 THR N N 123.018 0.028 .
212 47 47 ILE H H 8.269 0.002 .
213 47 47 ILE C C 171.968 0 .
214 47 47 ILE CA C 56.665 0.033 .
215 47 47 ILE CB C 34.685 0.018 .
216 47 47 ILE N N 127.136 0.09 .
217 48 48 TYR H H 8.509 0.007 .
218 48 48 TYR C C 173.577 0 .
219 48 48 TYR CA C 54.497 0.127 .
220 48 48 TYR CB C 38.055 0.064 .
221 48 48 TYR N N 125.954 0.061 .
222 49 49 GLU H H 8.688 0.006 .
223 49 49 GLU C C 173.465 0 .
224 49 49 GLU CA C 54.393 0.03 .
225 49 49 GLU CB C 28.017 0 .
226 49 49 GLU N N 121.291 0.094 .
227 50 50 ASN H H 9.094 0 .
228 50 50 ASN C C 172.239 0 .
229 50 50 ASN CA C 51.019 0.043 .
230 50 50 ASN CB C 36.632 0 .
231 50 50 ASN N N 120.532 0 .
232 51 51 GLU H H 8.306 0.006 .
233 51 51 GLU C C 173.643 0 .
234 51 51 GLU CA C 53.942 0.074 .
235 51 51 GLU CB C 27.128 0.104 .
236 51 51 GLU N N 118.84 0.064 .
237 52 52 GLY H H 8.336 0.004 .
238 52 52 GLY C C 172.04 0 .
239 52 52 GLY CA C 43.092 0.074 .
240 52 52 GLY N N 108.353 0.054 .
241 53 53 PHE H H 8.096 0.003 .
242 53 53 PHE N N 108.712 0.051 .
243 54 54 ARG H H 8.204 0 .
244 54 54 ARG N N 119.112 0 .
245 55 55 GLU H H 8.249 0 .
246 55 55 GLU C C 173.007 0 .
247 55 55 GLU CA C 52.967 0 .
248 55 55 GLU CB C 30.359 0 .
249 55 55 GLU N N 120.155 0 .
250 56 56 ILE H H 8.485 0.004 .
251 56 56 ILE C C 172.63 0 .
252 56 56 ILE CA C 60.379 0.062 .
253 56 56 ILE CB C 36.384 0 .
254 56 56 ILE N N 124.873 0.064 .
255 57 57 LYS H H 8.879 0.006 .
256 57 57 LYS C C 174.062 0 .
257 57 57 LYS CA C 52.283 0.039 .
258 57 57 LYS CB C 31.662 0.026 .
259 57 57 LYS N N 124.395 0.082 .
260 58 58 GLY H H 7.369 0.004 .
261 58 58 GLY C C 180.41 0 .
262 58 58 GLY CA C 42.999 0.047 .
263 58 58 GLY N N 108.119 0.063 .
264 59 59 TYR H H 8.622 0.002 .
265 59 59 TYR C C 172.58 0 .
266 59 59 TYR CA C 52.865 0.042 .
267 59 59 TYR CB C 41.306 0.027 .
268 59 59 TYR N N 114.625 0.08 .
269 60 60 GLU H H 8.71 0.005 .
270 60 60 GLU C C 171.524 0 .
271 60 60 GLU CA C 52.241 0.061 .
272 60 60 GLU CB C 31.465 0.05 .
273 60 60 GLU N N 120.965 0.065 .
274 61 61 TYR H H 9.481 0.008 .
275 61 61 TYR C C 173.465 0 .
276 61 61 TYR CA C 53.424 0 .
277 61 61 TYR CB C 39.859 0 .
278 61 61 TYR N N 119.176 0.042 .
279 62 62 GLN H H 9.092 0.004 .
280 62 62 GLN C C 172.586 0 .
281 62 62 GLN CA C 52.605 0.03 .
282 62 62 GLN CB C 27.87 0.014 .
283 62 62 GLN N N 120.693 0.065 .
284 63 63 LEU H H 9.272 0.003 .
285 63 63 LEU C C 173.996 0 .
286 63 63 LEU CA C 51.04 0.032 .
287 63 63 LEU CB C 43.494 0.002 .
288 63 63 LEU N N 124.114 0.042 .
289 64 64 TYR H H 9.776 0.009 .
290 64 64 TYR C C 171.529 0 .
291 64 64 TYR CA C 55.943 0.031 .
292 64 64 TYR CB C 37.34 0.047 .
293 64 64 TYR N N 124.877 0.012 .
294 65 65 VAL H H 9.128 0.005 .
295 65 65 VAL C C 171.703 0 .
296 65 65 VAL CA C 56.847 0.037 .
297 65 65 VAL CB C 33.313 0.091 .
298 65 65 VAL N N 121.393 0.052 .
299 66 66 TYR H H 9.398 0.004 .
300 66 66 TYR C C 173.065 0 .
301 66 66 TYR CA C 55.166 0.085 .
302 66 66 TYR CB C 37.273 0.029 .
303 66 66 TYR N N 127.326 0.08 .
304 67 67 ALA H H 9.823 0.004 .
305 67 67 ALA C C 173.5 0 .
306 67 67 ALA CA C 48.384 0.034 .
307 67 67 ALA CB C 20.12 0.065 .
308 67 67 ALA N N 127.901 0.044 .
309 68 68 SER H H 9.339 0.006 .
310 68 68 SER C C 171.193 0 .
311 68 68 SER CA C 57.372 0.067 .
312 68 68 SER CB C 59.263 0.063 .
313 68 68 SER N N 117.76 0.045 .
314 69 69 ASP H H 9.08 0.004 .
315 69 69 ASP C C 171.915 0 .
316 69 69 ASP CA C 53.383 0.066 .
317 69 69 ASP CB C 37.012 0.033 .
318 69 69 ASP N N 110.066 0.027 .
319 70 70 LYS H H 8.157 0.004 .
320 70 70 LYS C C 169.685 0 .
321 70 70 LYS CA C 52.13 0.046 .
322 70 70 LYS CB C 33.543 0.037 .
323 70 70 LYS N N 121.377 0.033 .
324 71 71 LEU H H 8.003 0.004 .
325 71 71 LEU C C 171.347 0 .
326 71 71 LEU CA C 50.906 0.029 .
327 71 71 LEU CB C 39.795 0.033 .
328 71 71 LEU N N 122.948 0.028 .
329 72 72 PHE H H 8.947 0.005 .
330 72 72 PHE C C 171.809 0 .
331 72 72 PHE CA C 53.682 0.044 .
332 72 72 PHE CB C 40.033 0.058 .
333 72 72 PHE N N 123.318 0.073 .
334 73 73 ARG H H 8.579 0.004 .
335 73 73 ARG C C 172.327 0 .
336 73 73 ARG CA C 50.817 0.058 .
337 73 73 ARG CB C 28.481 0.054 .
338 73 73 ARG N N 120.442 0.068 .
339 74 74 ALA H H 8.471 0.004 .
340 74 74 ALA C C 171.851 0 .
341 74 74 ALA CA C 47.045 0.075 .
342 74 74 ALA CB C 20.076 0.109 .
343 74 74 ALA N N 126.448 0.091 .
344 75 75 ASP H H 8.583 0.005 .
345 75 75 ASP C C 173.171 0 .
346 75 75 ASP CA C 49.878 0.056 .
347 75 75 ASP CB C 40.539 0.086 .
348 75 75 ASP N N 122.011 0.045 .
349 76 76 ILE H H 9.064 0.004 .
350 76 76 ILE C C 171.591 0 .
351 76 76 ILE CA C 56.545 0.018 .
352 76 76 ILE CB C 41.61 0.029 .
353 76 76 ILE N N 123.532 0.037 .
354 77 77 SER H H 9.332 0.005 .
355 77 77 SER C C 170.23 0 .
356 77 77 SER CA C 53.515 0.016 .
357 77 77 SER CB C 63.669 0.06 .
358 77 77 SER N N 120.229 0.053 .
359 78 78 GLU H H 8.991 0.006 .
360 78 78 GLU C C 172.58 0 .
361 78 78 GLU CA C 52.854 0.049 .
362 78 78 GLU CB C 32.517 0.125 .
363 78 78 GLU N N 122.523 0.06 .
364 79 79 GLN H H 8.577 0.004 .
365 79 79 GLN C C 172.637 0 .
366 79 79 GLN CA C 52.519 0.077 .
367 79 79 GLN CB C 27.981 0.063 .
368 79 79 GLN N N 124.238 0.053 .
369 80 80 VAL H H 7.653 0.004 .
370 80 80 VAL C C 171.727 0 .
371 80 80 VAL CA C 58.514 0.035 .
372 80 80 VAL CB C 31.6 0.06 .
373 80 80 VAL N N 120.674 0.087 .
374 81 81 VAL H H 8.382 0.008 .
375 81 81 VAL C C 172.298 0 .
376 81 81 VAL CA C 58.279 0.022 .
377 81 81 VAL CB C 31.336 0.037 .
378 81 81 VAL N N 122.894 0.051 .
379 82 82 ALA H H 8.55 0.01 .
380 82 82 ALA C C 175.061 0 .
381 82 82 ALA CA C 49.103 0.064 .
382 82 82 ALA CB C 17.37 0.047 .
383 82 82 ALA N N 129.01 0.033 .
384 83 83 GLY H H 8.598 0.006 .
385 83 83 GLY C C 170.753 0 .
386 83 83 GLY CA C 42.226 0.042 .
387 83 83 GLY N N 109.99 0.032 .
388 84 84 GLY H H 8.3 0.004 .
389 84 84 GLY C C 171.319 0 .
390 84 84 GLY CA C 43.551 0.031 .
391 84 84 GLY N N 109.036 0.026 .
392 85 85 ARG H H 8.109 0.003 .
393 85 85 ARG C C 173.327 0 .
394 85 85 ARG CA C 53.033 0.038 .
395 85 85 ARG CB C 29.834 0.047 .
396 85 85 ARG N N 120.405 0.043 .
397 86 86 LYS H H 8.924 0.006 .
398 86 86 LYS C C 172.236 0 .
399 86 86 LYS CA C 52.614 0.105 .
400 86 86 LYS CB C 33.934 0.052 .
401 86 86 LYS N N 121.742 0.044 .
402 87 87 LEU H H 9.338 0.005 .
403 87 87 LEU C C 172.813 0 .
404 87 87 LEU CA C 52.293 0.046 .
405 87 87 LEU CB C 40.267 0.071 .
406 87 87 LEU N N 126.015 0.024 .
407 88 88 LEU H H 9.198 0.005 .
408 88 88 LEU C C 174.968 0 .
409 88 88 LEU CA C 53.549 0.024 .
410 88 88 LEU CB C 40.212 0.097 .
411 88 88 LEU N N 128.935 0.051 .
412 89 89 ARG H H 7.479 0.005 .
413 89 89 ARG C C 170.813 0 .
414 89 89 ARG CA C 52.896 0.022 .
415 89 89 ARG CB C 31.183 0.054 .
416 89 89 ARG N N 113.932 0.041 .
417 90 90 PHE H H 8.639 0.006 .
418 90 90 PHE C C 171.24 0 .
419 90 90 PHE CA C 55.136 0.045 .
420 90 90 PHE CB C 39.966 0.11 .
421 90 90 PHE N N 126.516 0.061 .
422 91 91 ASN H H 8.797 0.003 .
423 91 91 ASN C C 169.898 0 .
424 91 91 ASN CA C 50.096 0.038 .
425 91 91 ASN CB C 40.581 0.071 .
426 91 91 ASN N N 124.241 0.056 .
427 92 92 GLY H H 8.132 0.006 .
428 92 92 GLY CA C 41.967 0.022 .
429 92 92 GLY N N 107.621 0.06 .
430 93 93 PRO C C 173.903 0 .
431 93 93 PRO CA C 59.094 0.022 .
432 93 93 PRO CB C 31.901 0.06 .
433 94 94 VAL H H 8.49 0.004 .
434 94 94 VAL CA C 55.081 0.001 .
435 94 94 VAL CB C 29.452 0 .
436 94 94 VAL N N 118.058 0.021 .
stop_
save_