data_4758
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
A novel killer toxin-like protein, SKLP, is a member of the single-domain
beta-gamma crystallin family proteins
;
_BMRB_accession_number 4758
_BMRB_flat_file_name bmr4758.str
_Entry_type original
_Submission_date 2000-06-12
_Accession_date 2000-06-12
_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 Ohki Shin-ya . .
2 Kariya Eri . .
3 Hiraga Kazumi . .
4 Wakamiya Akiko . .
5 Isobe Toshiaki . .
6 Oda Kohei . .
7 Kainosho Masatsune . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 364
"13C chemical shifts" 254
"15N chemical shifts" 86
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-05-01 original author .
stop_
_Original_release_date 2001-05-01
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
NMR Structure of Streptomyces Killer Toxin-like Protein, SKLP: Further Evidence
for the Wide Distribution of Single-domain Betagamma-crystallin Superfamily
Proteins
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 20566721
_PubMed_ID 11114251
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Ohki Shin-ya . .
2 Kariya Eri . .
3 Hiraga Kazumi . .
4 Wakamiya Akiko . .
5 Isobe Toshiaki . .
6 Oda Kohei . .
7 Kainosho Masatsune . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of Molecular Biology'
_Journal_volume 305
_Journal_issue 1
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 109
_Page_last 120
_Year 2001
_Details .
loop_
_Keyword
'killer toxin-like protein'
stop_
save_
##################################
# Molecular system description #
##################################
save_SKLP_system
_Saveframe_category molecular_system
_Mol_system_name SKLP
_Abbreviation_common SKLP
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'SKLP monomer' $SKLP
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_SKLP
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'yeast killer toxin-like protein'
_Abbreviation_common SKLP
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 84
_Mol_residue_sequence
;
IDHVPCRGGENFLKIWSHSG
GQQSVDCYANRGRIDFGGWW
VDKISTGNNDLIYYDANGDS
VRVDRWHDITYPNRPPKVNS
IEIL
;
loop_
_Residue_seq_code
_Residue_label
1 ILE 2 ASP 3 HIS 4 VAL 5 PRO
6 CYS 7 ARG 8 GLY 9 GLY 10 GLU
11 ASN 12 PHE 13 LEU 14 LYS 15 ILE
16 TRP 17 SER 18 HIS 19 SER 20 GLY
21 GLY 22 GLN 23 GLN 24 SER 25 VAL
26 ASP 27 CYS 28 TYR 29 ALA 30 ASN
31 ARG 32 GLY 33 ARG 34 ILE 35 ASP
36 PHE 37 GLY 38 GLY 39 TRP 40 TRP
41 VAL 42 ASP 43 LYS 44 ILE 45 SER
46 THR 47 GLY 48 ASN 49 ASN 50 ASP
51 LEU 52 ILE 53 TYR 54 TYR 55 ASP
56 ALA 57 ASN 58 GLY 59 ASP 60 SER
61 VAL 62 ARG 63 VAL 64 ASP 65 ARG
66 TRP 67 HIS 68 ASP 69 ILE 70 THR
71 TYR 72 PRO 73 ASN 74 ARG 75 PRO
76 PRO 77 LYS 78 VAL 79 ASN 80 SER
81 ILE 82 GLU 83 ILE 84 LEU
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2014-05-12
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 1F53 "Nmr Structure Of Killer Toxin-Like Protein Sklp" 100.00 84 100.00 100.00 4.47e-54
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$SKLP 'Streptomyces sp. F-287' 1883 Eubacteria . Streptomyces 'sp. F-287'
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
$SKLP 'purified from the natural source' . . . . .
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
$SKLP 1.0 mM .
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_3
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 800
_Details .
save_
#######################
# Sample conditions #
#######################
save_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.0 0.08 n/a
temperature 303 1 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 C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449519
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . .
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329112
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_shifts_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'SKLP monomer'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 1 ILE C C 167.00 . 1
2 . 1 ILE CA C 56.70 . 1
3 . 1 ILE HA H 4.26 . 1
4 . 1 ILE CB C 36.23 . 1
5 . 1 ILE HB H 1.56 . 1
6 . 1 ILE HG12 H 0.81 . 1
7 . 1 ILE HG13 H 1.90 . 1
8 . 1 ILE HG2 H 0.75 . 1
9 . 1 ILE HD1 H 0.66 . 1
10 . 2 ASP N N 126.55 . 1
11 . 2 ASP C C 171.52 . 1
12 . 2 ASP CA C 50.82 . 1
13 . 2 ASP HA H 5.06 . 1
14 . 2 ASP CB C 42.73 . 1
15 . 2 ASP HB2 H 2.47 . 1
16 . 2 ASP HB3 H 2.27 . 1
17 . 3 HIS N N 123.91 . 1
18 . 3 HIS C C 172.18 . 1
19 . 3 HIS CA C 52.17 . 1
20 . 3 HIS HA H 4.69 . 1
21 . 3 HIS CB C 27.14 . 1
22 . 3 HIS HB2 H 3.35 . 1
23 . 3 HIS HB3 H 2.83 . 1
24 . 4 VAL N N 121.81 . 1
25 . 4 VAL CA C 55.55 . 1
26 . 4 VAL HA H 4.63 . 1
27 . 4 VAL CB C 30.70 . 1
28 . 4 VAL HB H 1.77 . 1
29 . 4 VAL HG1 H 0.57 . 1
30 . 4 VAL HG2 H -0.26 . 1
31 . 4 VAL CG1 C 19.85 . 1
32 . 4 VAL CG2 C 14.85 . 1
33 . 5 PRO C C 175.60 . 1
34 . 5 PRO CA C 60.23 . 1
35 . 5 PRO HA H 4.17 . 1
36 . 5 PRO CB C 29.53 . 1
37 . 5 PRO HB2 H 2.21 . 1
38 . 5 PRO HB3 H 1.65 . 1
39 . 5 PRO HG2 H 1.99 . 1
40 . 5 PRO HG3 H 1.80 . 1
41 . 5 PRO HD2 H 1.80 . 1
42 . 5 PRO HD3 H 3.44 . 1
43 . 6 CYS N N 121.43 . 1
44 . 6 CYS C C 173.17 . 1
45 . 6 CYS CA C 52.10 . 1
46 . 6 CYS HA H 4.42 . 1
47 . 6 CYS CB C 38.04 . 1
48 . 6 CYS HB2 H 2.95 . 1
49 . 6 CYS HB3 H 2.71 . 1
50 . 7 ARG N N 120.16 . 1
51 . 7 ARG C C 173.92 . 1
52 . 7 ARG CA C 53.61 . 1
53 . 7 ARG HA H 4.45 . 1
54 . 7 ARG CB C 29.74 . 1
55 . 7 ARG HB2 H 1.82 . 1
56 . 7 ARG HB3 H 1.71 . 1
57 . 7 ARG HG2 H 1.53 . 1
58 . 7 ARG HG3 H 1.47 . 1
59 . 7 ARG HD2 H 3.14 . 1
60 . 7 ARG HD3 H 3.05 . 1
61 . 8 GLY N N 110.60 . 1
62 . 8 GLY C C 172.38 . 1
63 . 8 GLY CA C 43.82 . 1
64 . 8 GLY HA2 H 3.98 . 1
65 . 9 GLY N N 109.62 . 1
66 . 9 GLY C C 171.72 . 1
67 . 9 GLY CA C 43.36 . 1
68 . 9 GLY HA2 H 3.89 . 1
69 . 10 GLU N N 118.02 . 1
70 . 10 GLU C C 174.15 . 1
71 . 10 GLU CA C 53.48 . 1
72 . 10 GLU HA H 4.36 . 1
73 . 10 GLU CB C 28.22 . 1
74 . 10 GLU HB2 H 1.50 . 1
75 . 10 GLU HB3 H 1.45 . 1
76 . 10 GLU HG2 H 2.09 . 1
77 . 11 ASN N N 117.70 . 1
78 . 11 ASN C C 172.67 . 1
79 . 11 ASN CA C 51.05 . 1
80 . 11 ASN HA H 4.80 . 1
81 . 11 ASN CB C 36.66 . 1
82 . 11 ASN HB2 H 2.80 . 1
83 . 11 ASN HD21 H 7.94 . 1
84 . 11 ASN HD22 H 7.21 . 1
85 . 11 ASN ND2 N 113.67 . 1
86 . 12 PHE N N 117.41 . 1
87 . 12 PHE C C 173.32 . 1
88 . 12 PHE CA C 53.48 . 1
89 . 12 PHE HA H 4.95 . 1
90 . 12 PHE CB C 36.65 . 1
91 . 12 PHE HB2 H 3.38 . 1
92 . 12 PHE HB3 H 2.73 . 1
93 . 12 PHE HD1 H 7.24 . 1
94 . 12 PHE HE1 H 7.39 . 1
95 . 13 LEU N N 122.09 . 1
96 . 13 LEU C C 172.21 . 1
97 . 13 LEU CA C 53.33 . 1
98 . 13 LEU HA H 4.69 . 1
99 . 13 LEU CB C 40.49 . 1
100 . 13 LEU HB2 H 1.96 . 1
101 . 13 LEU HB3 H 1.39 . 1
102 . 13 LEU HG H 1.61 . 1
103 . 13 LEU HD1 H 0.98 . 1
104 . 13 LEU HD2 H 0.78 . 1
105 . 13 LEU CD1 C 24.68 . 1
106 . 13 LEU CD2 C 25.96 . 1
107 . 14 LYS N N 131.13 . 1
108 . 14 LYS C C 172.05 . 1
109 . 14 LYS CA C 53.35 . 1
110 . 14 LYS HA H 5.35 . 1
111 . 14 LYS CB C 35.06 . 1
112 . 14 LYS HB2 H 1.84 . 1
113 . 14 LYS HB3 H 1.54 . 1
114 . 14 LYS HG2 H 0.95 . 1
115 . 14 LYS HG3 H 0.12 . 1
116 . 14 LYS HD2 H 1.43 . 1
117 . 14 LYS HD3 H 0.96 . 1
118 . 14 LYS HE2 H 2.67 . 1
119 . 14 LYS HE3 H 2.30 . 1
120 . 15 ILE N N 123.57 . 1
121 . 15 ILE C C 173.39 . 1
122 . 15 ILE CA C 58.57 . 1
123 . 15 ILE HA H 5.15 . 1
124 . 15 ILE CB C 40.47 . 1
125 . 15 ILE HB H 1.90 . 1
126 . 15 ILE HG12 H 1.02 . 1
127 . 15 ILE HG13 H 1.67 . 1
128 . 15 ILE HG2 H 1.08 . 1
129 . 15 ILE HD1 H 0.54 . 1
130 . 16 TRP N N 134.50 . 1
131 . 16 TRP C C 173.23 . 1
132 . 16 TRP CA C 56.11 . 1
133 . 16 TRP HA H 5.60 . 1
134 . 16 TRP CB C 30.23 . 1
135 . 16 TRP HB2 H 3.75 . 1
136 . 16 TRP HB3 H 3.57 . 1
137 . 16 TRP HE3 H 7.74 . 1
138 . 16 TRP HZ2 H 7.27 . 1
139 . 16 TRP HZ3 H 6.99 . 1
140 . 16 TRP HH2 H 7.51 . 1
141 . 17 SER N N 118.77 . 1
142 . 17 SER C C 171.94 . 1
143 . 17 SER CA C 56.12 . 1
144 . 17 SER HA H 6.22 . 1
145 . 17 SER CB C 66.30 . 1
146 . 17 SER HB2 H 4.39 . 1
147 . 17 SER HB3 H 4.15 . 1
148 . 18 HIS N N 112.75 . 1
149 . 18 HIS C C 170.76 . 1
150 . 18 HIS CA C 54.36 . 1
151 . 18 HIS HA H 5.84 . 1
152 . 18 HIS CB C 30.52 . 1
153 . 18 HIS HB2 H 3.48 . 1
154 . 18 HIS HB3 H 3.32 . 1
155 . 19 SER N N 112.64 . 1
156 . 19 SER C C 173.75 . 1
157 . 19 SER CA C 55.89 . 1
158 . 19 SER HA H 4.25 . 1
159 . 19 SER CB C 58.89 . 1
160 . 19 SER HB2 H 2.27 . 1
161 . 19 SER HB3 H 1.80 . 1
162 . 20 GLY N N 118.80 . 1
163 . 20 GLY C C 172.98 . 1
164 . 20 GLY CA C 45.15 . 1
165 . 20 GLY HA2 H 3.92 . 1
166 . 20 GLY HA3 H 3.75 . 1
167 . 21 GLY N N 112.00 . 1
168 . 21 GLY C C 171.83 . 1
169 . 21 GLY CA C 43.22 . 1
170 . 21 GLY HA2 H 4.02 . 1
171 . 21 GLY HA3 H 3.90 . 1
172 . 22 GLN N N 119.69 . 1
173 . 22 GLN C C 172.65 . 1
174 . 22 GLN CA C 52.80 . 1
175 . 22 GLN HA H 4.69 . 1
176 . 22 GLN CB C 29.34 . 1
177 . 22 GLN HB2 H 2.34 . 1
178 . 22 GLN HB3 H 2.14 . 1
179 . 22 GLN HG2 H 2.49 . 1
180 . 23 GLN N N 119.84 . 1
181 . 23 GLN C C 173.56 . 1
182 . 23 GLN CA C 52.81 . 1
183 . 23 GLN HA H 5.52 . 1
184 . 23 GLN CB C 30.09 . 1
185 . 23 GLN HB2 H 2.53 . 1
186 . 23 GLN HB3 H 2.21 . 1
187 . 23 GLN HG2 H 2.48 . 1
188 . 24 SER N N 116.22 . 1
189 . 24 SER C C 170.94 . 1
190 . 24 SER CA C 55.67 . 1
191 . 24 SER HA H 4.77 . 1
192 . 24 SER CB C 62.98 . 1
193 . 24 SER HB2 H 3.58 . 1
194 . 24 SER HB3 H 3.47 . 1
195 . 25 VAL N N 127.53 . 1
196 . 25 VAL C C 172.90 . 1
197 . 25 VAL CA C 59.76 . 1
198 . 25 VAL HA H 4.79 . 1
199 . 25 VAL CB C 31.11 . 1
200 . 25 VAL HB H 1.72 . 1
201 . 25 VAL HG1 H 0.23 . 1
202 . 25 VAL HG2 H 0.71 . 1
203 . 25 VAL CG1 C 18.61 . 1
204 . 25 VAL CG2 C 18.99 . 1
205 . 26 ASP N N 125.18 . 1
206 . 26 ASP C C 171.00 . 1
207 . 26 ASP CA C 51.48 . 1
208 . 26 ASP HA H 5.21 . 1
209 . 26 ASP CB C 45.05 . 1
210 . 26 ASP HB2 H 2.53 . 1
211 . 26 ASP HB3 H 2.33 . 1
212 . 27 CYS N N 117.33 . 1
213 . 27 CYS C C 170.31 . 1
214 . 27 CYS CA C 54.82 . 1
215 . 27 CYS HA H 6.02 . 1
216 . 27 CYS CB C 44.79 . 1
217 . 27 CYS HB2 H 2.80 . 1
218 . 27 CYS HB3 H 2.72 . 1
219 . 28 TYR N N 116.77 . 1
220 . 28 TYR C C 171.28 . 1
221 . 28 TYR CA C 54.07 . 1
222 . 28 TYR HA H 5.48 . 1
223 . 28 TYR CB C 41.83 . 1
224 . 28 TYR HB2 H 2.79 . 1
225 . 28 TYR HB3 H 2.40 . 1
226 . 28 TYR HD1 H 6.63 . 1
227 . 28 TYR HE1 H 6.40 . 1
228 . 29 ALA N N 119.99 . 1
229 . 29 ALA C C 174.19 . 1
230 . 29 ALA CA C 49.04 . 1
231 . 29 ALA HA H 4.64 . 1
232 . 29 ALA CB C 21.85 . 1
233 . 29 ALA HB H 1.25 . 1
234 . 30 ASN N N 111.06 . 1
235 . 30 ASN C C 170.24 . 1
236 . 30 ASN CA C 53.19 . 1
237 . 30 ASN HA H 4.37 . 1
238 . 30 ASN CB C 36.00 . 1
239 . 30 ASN HB2 H 3.66 . 1
240 . 30 ASN HB3 H 2.80 . 1
241 . 30 ASN HD21 H 8.00 . 1
242 . 30 ASN HD22 H 7.15 . 1
243 . 30 ASN ND2 N 116.00 . 1
244 . 31 ARG N N 114.59 . 1
245 . 31 ARG C C 176.20 . 1
246 . 31 ARG CA C 54.87 . 1
247 . 31 ARG HA H 4.00 . 1
248 . 31 ARG CB C 29.39 . 1
249 . 31 ARG HB2 H 1.82 . 1
250 . 31 ARG HB3 H 1.70 . 1
251 . 31 ARG HG2 H 1.58 . 1
252 . 31 ARG HG3 H 1.74 . 1
253 . 31 ARG HD2 H 3.25 . 1
254 . 32 GLY N N 113.73 . 1
255 . 32 GLY C C 168.01 . 1
256 . 32 GLY CA C 42.11 . 1
257 . 32 GLY HA2 H 4.60 . 1
258 . 32 GLY HA3 H 3.90 . 1
259 . 33 ARG N N 119.86 . 1
260 . 33 ARG C C 172.58 . 1
261 . 33 ARG CA C 52.16 . 1
262 . 33 ARG HA H 5.59 . 1
263 . 33 ARG CB C 31.76 . 1
264 . 33 ARG HB2 H 1.74 . 1
265 . 33 ARG HB3 H 1.38 . 1
266 . 33 ARG HG2 H 1.50 . 1
267 . 33 ARG HG3 H 1.47 . 1
268 . 33 ARG HD2 H 2.90 . 1
269 . 33 ARG HD3 H 2.85 . 1
270 . 34 ILE N N 125.38 . 1
271 . 34 ILE C C 170.55 . 1
272 . 34 ILE CA C 57.57 . 1
273 . 34 ILE HA H 4.62 . 1
274 . 34 ILE CB C 40.51 . 1
275 . 34 ILE HB H 1.67 . 1
276 . 34 ILE HG12 H 1.46 . 1
277 . 34 ILE HG13 H 1.40 . 1
278 . 34 ILE HG2 H 0.66 . 1
279 . 34 ILE HD1 H 0.97 . 1
280 . 35 ASP N N 124.48 . 1
281 . 35 ASP C C 172.90 . 1
282 . 35 ASP CA C 53.23 . 1
283 . 35 ASP HA H 4.64 . 1
284 . 35 ASP CB C 39.17 . 1
285 . 35 ASP HB2 H 2.71 . 1
286 . 35 ASP HB3 H 2.60 . 1
287 . 36 PHE N N 125.16 . 1
288 . 36 PHE C C 174.49 . 1
289 . 36 PHE CA C 55.24 . 1
290 . 36 PHE HA H 4.47 . 1
291 . 36 PHE CB C 40.96 . 1
292 . 36 PHE HB2 H 2.75 . 1
293 . 36 PHE HB3 H 2.55 . 1
294 . 36 PHE HD1 H 7.14 . 1
295 . 36 PHE HE1 H 7.34 . 1
296 . 36 PHE HZ H 7.60 . 1
297 . 37 GLY N N 104.61 . 1
298 . 37 GLY C C 173.46 . 1
299 . 37 GLY CA C 43.90 . 1
300 . 37 GLY HA2 H 3.86 . 1
301 . 37 GLY HA3 H 3.77 . 1
302 . 38 GLY N N 107.20 . 1
303 . 38 GLY C C 172.55 . 1
304 . 38 GLY CA C 44.63 . 1
305 . 38 GLY HA2 H 3.87 . 1
306 . 38 GLY HA3 H 3.48 . 1
307 . 39 TRP N N 119.73 . 1
308 . 39 TRP C C 171.99 . 1
309 . 39 TRP CA C 56.23 . 1
310 . 39 TRP HA H 4.38 . 1
311 . 39 TRP CB C 27.34 . 1
312 . 39 TRP HB2 H 3.24 . 1
313 . 39 TRP HB3 H 2.84 . 1
314 . 39 TRP HE3 H 7.89 . 1
315 . 39 TRP HZ2 H 7.36 . 1
316 . 39 TRP HZ3 H 7.20 . 1
317 . 39 TRP HH2 H 7.55 . 1
318 . 40 TRP N N 120.45 . 1
319 . 40 TRP C C 174.22 . 1
320 . 40 TRP CA C 55.99 . 1
321 . 40 TRP HA H 5.08 . 1
322 . 40 TRP CB C 27.42 . 1
323 . 40 TRP HB2 H 2.45 . 1
324 . 40 TRP HB3 H 2.03 . 1
325 . 40 TRP HE3 H 7.41 . 1
326 . 40 TRP HZ2 H 6.69 . 1
327 . 40 TRP HH2 H 7.02 . 1
328 . 41 VAL N N 122.75 . 1
329 . 41 VAL C C 170.29 . 1
330 . 41 VAL CA C 61.26 . 1
331 . 41 VAL HA H 4.23 . 1
332 . 41 VAL CB C 31.13 . 1
333 . 41 VAL HB H 1.60 . 1
334 . 41 VAL HG1 H 0.90 . 1
335 . 41 VAL HG2 H 0.67 . 1
336 . 41 VAL CG1 C 19.97 . 1
337 . 41 VAL CG2 C 22.45 . 1
338 . 42 ASP N N 123.38 . 1
339 . 42 ASP C C 175.40 . 1
340 . 42 ASP CA C 54.36 . 1
341 . 42 ASP HA H 4.95 . 1
342 . 42 ASP CB C 42.01 . 1
343 . 42 ASP HB2 H 2.83 . 1
344 . 42 ASP HB3 H 2.43 . 1
345 . 43 LYS N N 119.85 . 1
346 . 43 LYS C C 171.52 . 1
347 . 43 LYS CA C 53.94 . 1
348 . 43 LYS HA H 5.33 . 1
349 . 43 LYS CB C 32.55 . 1
350 . 43 LYS HB2 H 1.73 . 1
351 . 43 LYS HB3 H 1.54 . 1
352 . 43 LYS HG2 H 0.74 . 1
353 . 43 LYS HG3 H -0.24 . 1
354 . 43 LYS HD2 H 1.19 . 1
355 . 43 LYS HD3 H 0.94 . 1
356 . 43 LYS HE2 H 2.10 . 1
357 . 43 LYS HE3 H 2.00 . 1
358 . 44 ILE N N 125.07 . 1
359 . 44 ILE C C 172.23 . 1
360 . 44 ILE CA C 58.94 . 1
361 . 44 ILE HA H 5.05 . 1
362 . 44 ILE CB C 41.35 . 1
363 . 44 ILE HB H 1.70 . 1
364 . 44 ILE HG12 H 0.90 . 1
365 . 44 ILE HD1 H 0.83 . 1
366 . 45 SER N N 122.66 . 1
367 . 45 SER C C 173.84 . 1
368 . 45 SER CA C 54.43 . 1
369 . 45 SER HA H 5.95 . 1
370 . 45 SER CB C 62.72 . 1
371 . 45 SER HB2 H 4.32 . 1
372 . 45 SER HB3 H 4.06 . 1
373 . 46 THR N N 116.63 . 1
374 . 46 THR C C 174.03 . 1
375 . 46 THR CA C 61.77 . 1
376 . 46 THR HA H 4.19 . 1
377 . 46 THR CB C 66.40 . 1
378 . 46 THR HB H 5.05 . 1
379 . 46 THR HG2 H 1.18 . 1
380 . 47 GLY N N 110.02 . 1
381 . 47 GLY C C 172.55 . 1
382 . 47 GLY CA C 43.23 . 1
383 . 47 GLY HA2 H 3.45 . 1
384 . 47 GLY HA3 H 3.19 . 1
385 . 48 ASN N N 123.08 . 1
386 . 48 ASN C C 172.03 . 1
387 . 48 ASN CA C 49.57 . 1
388 . 48 ASN HA H 3.91 . 1
389 . 48 ASN CB C 35.28 . 1
390 . 48 ASN HB2 H 2.79 . 1
391 . 48 ASN HB3 H 2.62 . 1
392 . 48 ASN HD21 H 7.67 . 1
393 . 48 ASN HD22 H 7.00 . 1
394 . 48 ASN ND2 N 109.49 . 1
395 . 49 ASN N N 115.44 . 1
396 . 49 ASN C C 169.75 . 1
397 . 49 ASN CA C 50.76 . 1
398 . 49 ASN HA H 4.76 . 1
399 . 49 ASN CB C 40.38 . 1
400 . 49 ASN HB2 H 2.79 . 1
401 . 49 ASN HB3 H 2.32 . 1
402 . 49 ASN HD21 H 7.77 . 1
403 . 49 ASN HD22 H 6.96 . 1
404 . 49 ASN ND2 N 116.35 . 1
405 . 50 ASP N N 120.45 . 1
406 . 50 ASP C C 171.42 . 1
407 . 50 ASP CA C 51.69 . 1
408 . 50 ASP HA H 4.99 . 1
409 . 50 ASP CB C 40.90 . 1
410 . 50 ASP HB2 H 2.56 . 1
411 . 51 LEU N N 124.62 . 1
412 . 51 LEU C C 173.60 . 1
413 . 51 LEU CA C 50.93 . 1
414 . 51 LEU HA H 5.34 . 1
415 . 51 LEU CB C 45.01 . 1
416 . 51 LEU HB2 H 2.07 . 1
417 . 51 LEU HB3 H 1.16 . 1
418 . 51 LEU HG H 1.45 . 1
419 . 51 LEU HD1 H 0.85 . 1
420 . 51 LEU HD2 H 0.93 . 1
421 . 51 LEU CD1 C 22.29 . 1
422 . 51 LEU CD2 C 26.18 . 1
423 . 52 ILE N N 123.85 . 1
424 . 52 ILE C C 172.77 . 1
425 . 52 ILE CA C 58.24 . 1
426 . 52 ILE HA H 4.88 . 1
427 . 52 ILE CB C 38.83 . 1
428 . 52 ILE HB H 1.44 . 1
429 . 52 ILE HG12 H 0.68 . 1
430 . 52 ILE HG2 H 0.23 . 1
431 . 52 ILE HD1 H 0.74 . 1
432 . 53 TYR N N 121.48 . 1
433 . 53 TYR C C 170.05 . 1
434 . 53 TYR CA C 52.06 . 1
435 . 53 TYR HA H 5.42 . 1
436 . 53 TYR CB C 39.43 . 1
437 . 53 TYR HB2 H 3.24 . 1
438 . 53 TYR HB3 H 2.36 . 1
439 . 53 TYR HD1 H 6.59 . 1
440 . 53 TYR HE1 H 6.45 . 1
441 . 54 TYR N N 119.12 . 1
442 . 54 TYR C C 174.33 . 1
443 . 54 TYR CA C 54.46 . 1
444 . 54 TYR HA H 5.17 . 1
445 . 54 TYR CB C 37.07 . 1
446 . 54 TYR HB2 H 2.93 . 1
447 . 54 TYR HB3 H 2.82 . 1
448 . 54 TYR HD1 H 6.85 . 1
449 . 54 TYR HE1 H 6.63 . 1
450 . 55 ASP N N 124.85 . 1
451 . 55 ASP C C 175.95 . 1
452 . 55 ASP CA C 50.65 . 1
453 . 55 ASP HA H 5.26 . 1
454 . 55 ASP CB C 40.65 . 1
455 . 55 ASP HB2 H 3.29 . 1
456 . 55 ASP HB3 H 2.69 . 1
457 . 56 ALA N N 122.43 . 1
458 . 56 ALA C C 175.96 . 1
459 . 56 ALA CA C 51.84 . 1
460 . 56 ALA HA H 4.15 . 1
461 . 56 ALA CB C 16.39 . 1
462 . 56 ALA HB H 1.33 . 1
463 . 57 ASN N N 115.94 . 1
464 . 57 ASN C C 173.71 . 1
465 . 57 ASN CA C 50.88 . 1
466 . 57 ASN HA H 4.79 . 1
467 . 57 ASN CB C 36.66 . 1
468 . 57 ASN HB2 H 3.03 . 1
469 . 57 ASN HB3 H 2.95 . 1
470 . 57 ASN HD21 H 8.10 . 1
471 . 57 ASN HD22 H 6.97 . 1
472 . 57 ASN ND2 N 113.37 . 1
473 . 58 GLY N N 108.07 . 1
474 . 58 GLY C C 172.32 . 1
475 . 58 GLY CA C 42.95 . 1
476 . 58 GLY HA2 H 4.36 . 1
477 . 58 GLY HA3 H 3.75 . 1
478 . 59 ASP N N 122.46 . 1
479 . 59 ASP C C 172.79 . 1
480 . 59 ASP CA C 52.37 . 1
481 . 59 ASP HA H 4.80 . 1
482 . 59 ASP CB C 39.24 . 1
483 . 59 ASP HB2 H 2.82 . 1
484 . 59 ASP HB3 H 2.56 . 1
485 . 60 SER N N 114.93 . 1
486 . 60 SER C C 171.69 . 1
487 . 60 SER CA C 53.53 . 1
488 . 60 SER HA H 5.06 . 1
489 . 60 SER CB C 63.72 . 1
490 . 60 SER HB2 H 3.44 . 1
491 . 60 SER HB3 H 3.27 . 1
492 . 61 VAL N N 124.37 . 1
493 . 61 VAL C C 170.86 . 1
494 . 61 VAL CA C 59.29 . 1
495 . 61 VAL HA H 3.77 . 1
496 . 61 VAL CB C 32.03 . 1
497 . 61 VAL HB H 0.05 . 1
498 . 61 VAL HG1 H 0.60 . 1
499 . 61 VAL HG2 H 0.52 . 1
500 . 61 VAL CG1 C 18.82 . 1
501 . 61 VAL CG2 C 18.76 . 1
502 . 62 ARG N N 125.88 . 1
503 . 62 ARG C C 174.14 . 1
504 . 62 ARG CA C 51.87 . 1
505 . 62 ARG HA H 5.17 . 1
506 . 62 ARG CB C 29.44 . 1
507 . 62 ARG HB2 H 1.70 . 1
508 . 62 ARG HB3 H 1.47 . 1
509 . 62 ARG HG2 H 1.29 . 1
510 . 62 ARG HG3 H 1.45 . 1
511 . 62 ARG HD2 H 3.03 . 1
512 . 62 ARG HD3 H 3.01 . 1
513 . 63 VAL N N 128.20 . 1
514 . 63 VAL C C 171.74 . 1
515 . 63 VAL CA C 59.54 . 1
516 . 63 VAL HA H 4.06 . 1
517 . 63 VAL CB C 31.45 . 1
518 . 63 VAL HB H 1.96 . 1
519 . 63 VAL HG1 H 1.06 . 1
520 . 63 VAL HG2 H 0.94 . 1
521 . 63 VAL CG1 C 20.53 . 1
522 . 63 VAL CG2 C 18.12 . 1
523 . 64 ASP N N 125.53 . 1
524 . 64 ASP C C 175.08 . 1
525 . 64 ASP CA C 52.44 . 1
526 . 64 ASP HA H 4.93 . 1
527 . 64 ASP CB C 40.81 . 1
528 . 64 ASP HB2 H 2.13 . 1
529 . 64 ASP HB3 H 2.81 . 1
530 . 65 ARG N N 118.66 . 1
531 . 65 ARG C C 175.17 . 1
532 . 65 ARG CA C 54.07 . 1
533 . 65 ARG HA H 4.46 . 1
534 . 65 ARG CB C 28.42 . 1
535 . 65 ARG HB2 H 1.45 . 1
536 . 65 ARG HB3 H 1.36 . 1
537 . 65 ARG HG2 H 1.60 . 1
538 . 65 ARG HG3 H 1.55 . 1
539 . 65 ARG HD2 H 3.30 . 1
540 . 65 ARG HD3 H 2.99 . 1
541 . 66 TRP N N 122.45 . 1
542 . 66 TRP C C 173.81 . 1
543 . 66 TRP CA C 54.27 . 1
544 . 66 TRP HA H 4.70 . 1
545 . 66 TRP CB C 24.29 . 1
546 . 66 TRP HB2 H 3.37 . 1
547 . 67 HIS N N 115.86 . 1
548 . 67 HIS C C 170.60 . 1
549 . 67 HIS CA C 53.71 . 1
550 . 67 HIS HA H 4.97 . 1
551 . 67 HIS CB C 29.90 . 1
552 . 67 HIS HB2 H 3.28 . 1
553 . 67 HIS HB3 H 2.95 . 1
554 . 68 ASP N N 122.49 . 1
555 . 68 ASP C C 172.99 . 1
556 . 68 ASP CA C 51.00 . 1
557 . 68 ASP HA H 5.96 . 1
558 . 68 ASP CB C 40.25 . 1
559 . 68 ASP HB2 H 2.66 . 1
560 . 68 ASP HB3 H 2.52 . 1
561 . 69 ILE N N 123.66 . 1
562 . 69 ILE C C 171.81 . 1
563 . 69 ILE CA C 56.95 . 1
564 . 69 ILE HA H 4.60 . 1
565 . 69 ILE CB C 39.06 . 1
566 . 69 ILE HB H 1.70 . 1
567 . 69 ILE HG12 H 1.40 . 1
568 . 69 ILE HG13 H 1.11 . 1
569 . 69 ILE HG2 H 0.66 . 1
570 . 69 ILE HD1 H 0.97 . 1
571 . 70 THR N N 116.02 . 1
572 . 70 THR C C 170.67 . 1
573 . 70 THR CA C 57.42 . 1
574 . 70 THR HA H 4.80 . 1
575 . 70 THR CB C 68.96 . 1
576 . 70 THR HB H 4.07 . 1
577 . 70 THR HG2 H 1.07 . 1
578 . 71 TYR N N 119.22 . 1
579 . 71 TYR CA C 52.78 . 1
580 . 71 TYR HA H 5.22 . 1
581 . 71 TYR CB C 36.63 . 1
582 . 71 TYR HB2 H 3.27 . 1
583 . 71 TYR HB3 H 3.03 . 1
584 . 71 TYR HD1 H 7.08 . 1
585 . 71 TYR HE1 H 6.63 . 1
586 . 72 PRO C C 174.85 . 1
587 . 72 PRO CA C 62.14 . 1
588 . 72 PRO HA H 4.38 . 1
589 . 72 PRO CB C 30.02 . 1
590 . 72 PRO HB2 H 2.30 . 1
591 . 72 PRO HB3 H 1.93 . 1
592 . 72 PRO HG2 H 2.28 . 1
593 . 72 PRO HG3 H 1.99 . 1
594 . 72 PRO HD2 H 3.44 . 1
595 . 73 ASN N N 113.69 . 1
596 . 73 ASN C C 172.07 . 1
597 . 73 ASN CA C 51.49 . 1
598 . 73 ASN HA H 4.90 . 1
599 . 73 ASN CB C 38.43 . 1
600 . 73 ASN HB2 H 2.82 . 1
601 . 73 ASN HD21 H 7.87 . 1
602 . 73 ASN HD22 H 7.19 . 1
603 . 73 ASN ND2 N 113.70 . 1
604 . 74 ARG N N 119.83 . 1
605 . 74 ARG CA C 52.36 . 1
606 . 74 ARG HA H 4.51 . 1
607 . 74 ARG CB C 27.74 . 1
608 . 74 ARG HB2 H 1.92 . 1
609 . 74 ARG HB3 H 1.77 . 1
610 . 74 ARG HG2 H 1.60 . 1
611 . 74 ARG HD2 H 3.26 . 1
612 . 75 PRO HA H 4.80 . 1
613 . 75 PRO HB2 H 2.60 . 1
614 . 75 PRO HB3 H 2.13 . 1
615 . 75 PRO HG2 H 1.98 . 1
616 . 75 PRO HD2 H 3.68 . 1
617 . 75 PRO HD3 H 3.40 . 1
618 . 76 PRO C C 173.00 . 1
619 . 76 PRO CA C 59.83 . 1
620 . 76 PRO HA H 4.50 . 1
621 . 76 PRO CB C 29.61 . 1
622 . 76 PRO HB2 H 2.12 . 1
623 . 76 PRO HB3 H 1.46 . 1
624 . 76 PRO HG2 H 1.40 . 1
625 . 76 PRO HG3 H 1.36 . 1
626 . 76 PRO HD2 H 3.26 . 1
627 . 76 PRO HD3 H 2.86 . 1
628 . 77 LYS N N 124.16 . 1
629 . 77 LYS C C 173.55 . 1
630 . 77 LYS CA C 53.80 . 1
631 . 77 LYS HA H 3.75 . 1
632 . 77 LYS CB C 30.29 . 1
633 . 77 LYS HB2 H 1.47 . 1
634 . 77 LYS HB3 H 0.73 . 1
635 . 77 LYS HG2 H 0.26 . 1
636 . 77 LYS HG3 H -0.06 . 1
637 . 77 LYS HD2 H 1.19 . 1
638 . 77 LYS HD3 H 1.14 . 1
639 . 77 LYS HE2 H 2.56 . 1
640 . 77 LYS HE3 H 2.50 . 1
641 . 78 VAL N N 126.51 . 1
642 . 78 VAL C C 172.79 . 1
643 . 78 VAL CA C 62.01 . 1
644 . 78 VAL HA H 4.03 . 1
645 . 78 VAL CB C 30.62 . 1
646 . 78 VAL HB H 1.80 . 1
647 . 78 VAL HG1 H 0.56 . 1
648 . 78 VAL HG2 H 0.35 . 1
649 . 78 VAL CG1 C 21.07 . 1
650 . 78 VAL CG2 C 21.56 . 1
651 . 79 ASN N N 125.65 . 1
652 . 79 ASN C C 175.25 . 1
653 . 79 ASN CA C 51.78 . 1
654 . 79 ASN HA H 4.90 . 1
655 . 79 ASN CB C 37.46 . 1
656 . 79 ASN HB2 H 2.86 . 1
657 . 79 ASN HB3 H 2.56 . 1
658 . 79 ASN HD21 H 7.50 . 1
659 . 79 ASN HD22 H 6.99 . 1
660 . 79 ASN ND2 N 108.94 . 1
661 . 80 SER N N 113.69 . 1
662 . 80 SER C C 169.58 . 1
663 . 80 SER CA C 55.99 . 1
664 . 80 SER HA H 5.13 . 1
665 . 80 SER CB C 62.69 . 1
666 . 80 SER HB2 H 3.87 . 1
667 . 80 SER HB3 H 3.77 . 1
668 . 81 ILE N N 115.99 . 1
669 . 81 ILE C C 171.01 . 1
670 . 81 ILE CA C 57.61 . 1
671 . 81 ILE HA H 4.95 . 1
672 . 81 ILE CB C 40.32 . 1
673 . 81 ILE HB H 1.38 . 1
674 . 81 ILE HG12 H 1.14 . 1
675 . 81 ILE HG13 H 0.49 . 1
676 . 81 ILE HG2 H 0.31 . 1
677 . 81 ILE HD1 H -0.34 . 1
678 . 82 GLU N N 122.86 . 1
679 . 82 GLU C C 172.42 . 1
680 . 82 GLU CA C 52.09 . 1
681 . 82 GLU HA H 5.40 . 1
682 . 82 GLU CB C 32.12 . 1
683 . 82 GLU HB2 H 2.26 . 1
684 . 82 GLU HB3 H 1.85 . 1
685 . 82 GLU HG2 H 1.92 . 1
686 . 83 ILE N N 126.33 . 1
687 . 83 ILE C C 174.85 . 1
688 . 83 ILE CA C 59.29 . 1
689 . 83 ILE HA H 4.63 . 1
690 . 83 ILE CB C 36.00 . 1
691 . 83 ILE HB H 2.03 . 1
692 . 83 ILE HG12 H 1.57 . 1
693 . 83 ILE HG2 H 1.01 . 1
694 . 83 ILE HD1 H 0.76 . 1
695 . 84 LEU N N 135.64 . 1
696 . 84 LEU CA C 54.80 . 1
697 . 84 LEU HA H 4.15 . 1
698 . 84 LEU CB C 41.16 . 1
699 . 84 LEU HB2 H 1.62 . 1
700 . 84 LEU HB3 H 1.58 . 1
701 . 84 LEU HG H 1.48 . 1
702 . 84 LEU HD1 H 0.75 . 1
703 . 84 LEU CD1 C 22.98 . 1
704 . 84 LEU CD2 C 20.25 . 1
stop_
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