data_1478
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Two-Dimensional 1H Nuclear Magnetic Resonance Study of AaH IT, an Anti-Insect
Toxin from the Scorpion Androctonus australis Hector. Sequential Resonance
Assignments and Folding of the Polypeptide Chain
;
_BMRB_accession_number 1478
_BMRB_flat_file_name bmr1478.str
_Entry_type update
_Submission_date 1995-07-31
_Accession_date 1996-03-25
_Entry_origination BMRB
_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 Darbon H. . .
2 Weber C. . .
3 Braun Werner . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 378
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2010-06-14 revision BMRB 'Complete natural source information'
1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format'
1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format'
1995-07-31 original BMRB 'Last release in original BMRB flat-file format'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full
;
Darbon, H., Weber, C., Braun, Werner,
"Two-Dimensional 1H Nuclear Magnetic Resonance Study of AaH IT, an
Anti-Insect Toxin from the Scorpion Androctonus australis Hector.
Sequential Resonance Assignments and Folding of the Polypeptide Chain,"
Biochemistry 30, 1836-1845 (1991).
;
_Citation_title
;
Two-Dimensional 1H Nuclear Magnetic Resonance Study of AaH IT, an Anti-Insect
Toxin from the Scorpion Androctonus australis Hector. Sequential Resonance
Assignments and Folding of the Polypeptide Chain
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Darbon H. . .
2 Weber C. . .
3 Braun Werner . .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 30
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1836
_Page_last 1845
_Year 1991
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_toxin_AaH_IT
_Saveframe_category molecular_system
_Mol_system_name 'toxin AaH IT'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'toxin AaH IT' $toxin_AaH_IT
stop_
_System_molecular_weight .
_System_oligomer_state ?
_System_paramagnetic ?
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_toxin_AaH_IT
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'toxin AaH IT'
_Molecular_mass .
_Mol_thiol_state .
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 70
_Mol_residue_sequence
;
KKNGYAVDSSGKAPECLLSN
YCNNQCTKVHYADKGYCCLL
SCYCFGLNDDKKVLEISDTR
KSYCDTTIIN
;
loop_
_Residue_seq_code
_Residue_label
1 LYS 2 LYS 3 ASN 4 GLY 5 TYR
6 ALA 7 VAL 8 ASP 9 SER 10 SER
11 GLY 12 LYS 13 ALA 14 PRO 15 GLU
16 CYS 17 LEU 18 LEU 19 SER 20 ASN
21 TYR 22 CYS 23 ASN 24 ASN 25 GLN
26 CYS 27 THR 28 LYS 29 VAL 30 HIS
31 TYR 32 ALA 33 ASP 34 LYS 35 GLY
36 TYR 37 CYS 38 CYS 39 LEU 40 LEU
41 SER 42 CYS 43 TYR 44 CYS 45 PHE
46 GLY 47 LEU 48 ASN 49 ASP 50 ASP
51 LYS 52 LYS 53 VAL 54 LEU 55 GLU
56 ILE 57 SER 58 ASP 59 THR 60 ARG
61 LYS 62 SER 63 TYR 64 CYS 65 ASP
66 THR 67 THR 68 ILE 69 ILE 70 ASN
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-07-01
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
DBJ BAN64141 "AahIT toxin, partial [synthetic construct]" 100.00 70 98.57 100.00 6.91e-41
EMBL CAA41265 "Hector insect toxin (plasmid) [synthetic construct]" 100.00 108 100.00 100.00 1.08e-42
GB AAA29950 "neurotoxin AaH IT1 [Androctonus australis]" 100.00 88 98.57 100.00 2.31e-41
GB AAA29951 "neurotoxin AaH IT1 precursor, partial [Androctonus australis]" 100.00 88 98.57 100.00 2.55e-41
PIR XISR1A "insect toxin 1 - Sahara scorpion [Androctonus australis]" 100.00 70 100.00 100.00 1.96e-41
PRF 0804800E "toxin AaH IT,insect" 100.00 70 100.00 100.00 1.96e-41
SP P01497 "RecName: Full=Beta-insect excitatory toxin 1; AltName: Full=AaH IT1; Short=AaH IT; Short=AaHIT; Short=AaHIT1; Short=AaIT1; Flag" 100.00 88 98.57 100.00 2.55e-41
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Strain
_Fraction
$toxin_AaH_IT scorpion 6858 Eukaryota Metazoa Androctonus australis Hector venom
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
$toxin_AaH_IT 'not available' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_one
_Saveframe_category sample
_Sample_type solution
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_list
_Saveframe_category NMR_spectrometer
_Manufacturer unknown
_Model unknown
_Field_strength 0
_Details 'spectrometer information not available'
save_
#############################
# NMR applied experiments #
#############################
save__1
_Saveframe_category NMR_applied_experiment
_Sample_label $sample_one
save_
#######################
# Sample conditions #
#######################
save_sample_condition_set_one
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 5.2 . na
temperature 295 . K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_shift_reference_par_set_one
_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_citation_label
_Correction_value_citation_label
TSP H . . ppm 0 . . . . . $entry_citation $entry_citation
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_assignment_data_set_one
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_one
stop_
_Sample_conditions_label $sample_condition_set_one
_Chem_shift_reference_set_label $chem_shift_reference_par_set_one
_Mol_system_component_name 'toxin AaH IT'
_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 LYS H H 8.45 . 1
2 . 1 LYS HA H 4.89 . 1
3 . 1 LYS HB2 H 1.98 . 2
4 . 1 LYS HB3 H 2.09 . 2
5 . 2 LYS H H 9.5 . 1
6 . 2 LYS HA H 4.82 . 1
7 . 2 LYS HB2 H 1.76 . 2
8 . 2 LYS HB3 H 1.88 . 2
9 . 3 ASN H H 8.54 . 1
10 . 3 ASN HA H 5.42 . 1
11 . 3 ASN HB2 H 2.55 . 2
12 . 3 ASN HB3 H 2.65 . 2
13 . 3 ASN HD21 H 7.12 . 2
14 . 3 ASN HD22 H 7.83 . 2
15 . 4 GLY H H 7.98 . 1
16 . 4 GLY HA2 H 3.33 . 2
17 . 4 GLY HA3 H 3.76 . 2
18 . 5 TYR H H 9.58 . 1
19 . 5 TYR HA H 5.06 . 1
20 . 5 TYR HB2 H 2.65 . 2
21 . 5 TYR HB3 H 2.85 . 2
22 . 5 TYR HD1 H 7.38 . 1
23 . 5 TYR HD2 H 7.38 . 1
24 . 5 TYR HE1 H 7.04 . 1
25 . 5 TYR HE2 H 7.04 . 1
26 . 6 ALA H H 6.47 . 1
27 . 6 ALA HA H 4.27 . 1
28 . 6 ALA HB H .62 . 1
29 . 7 VAL H H 7.03 . 1
30 . 7 VAL HA H 4.64 . 1
31 . 7 VAL HB H 1.8 . 1
32 . 7 VAL HG1 H .7 . 1
33 . 7 VAL HG2 H .7 . 1
34 . 8 ASP H H 8.21 . 1
35 . 8 ASP HA H 4.86 . 1
36 . 8 ASP HB2 H 3.45 . 2
37 . 8 ASP HB3 H 2.94 . 2
38 . 9 SER H H 8.6 . 1
39 . 9 SER HA H 4.25 . 1
40 . 9 SER HB2 H 4.05 . 2
41 . 9 SER HB3 H 4 . 2
42 . 10 SER H H 8.58 . 1
43 . 10 SER HA H 4.57 . 1
44 . 10 SER HB2 H 3.96 . 2
45 . 10 SER HB3 H 4.06 . 2
46 . 11 GLY H H 8.25 . 1
47 . 11 GLY HA2 H 4.26 . 2
48 . 11 GLY HA3 H 3.49 . 2
49 . 12 LYS H H 7.83 . 1
50 . 12 LYS HA H 4.59 . 1
51 . 12 LYS HB2 H 1.71 . 2
52 . 12 LYS HB3 H 1.81 . 2
53 . 12 LYS HG2 H 1.32 . 1
54 . 12 LYS HG3 H 1.32 . 1
55 . 12 LYS HD2 H 1.66 . 1
56 . 12 LYS HD3 H 1.66 . 1
57 . 12 LYS HE2 H 3 . 1
58 . 12 LYS HE3 H 3 . 1
59 . 13 ALA H H 8.78 . 1
60 . 13 ALA HA H 5.18 . 1
61 . 13 ALA HB H 1.25 . 1
62 . 14 PRO HA H 4.51 . 1
63 . 14 PRO HB2 H 1.92 . 2
64 . 14 PRO HB3 H 2.65 . 2
65 . 14 PRO HG2 H 2.14 . 2
66 . 14 PRO HG3 H 2.29 . 2
67 . 14 PRO HD2 H 3.9 . 2
68 . 14 PRO HD3 H 4.15 . 2
69 . 15 GLU H H 9.21 . 1
70 . 15 GLU HA H 4.3 . 1
71 . 15 GLU HB2 H 1.86 . 2
72 . 15 GLU HB3 H 1.94 . 2
73 . 16 CYS H H 8.59 . 1
74 . 16 CYS HA H 4.57 . 1
75 . 16 CYS HB2 H 2.77 . 2
76 . 16 CYS HB3 H 2.85 . 2
77 . 17 LEU H H 9.83 . 1
78 . 17 LEU HA H 3.92 . 1
79 . 17 LEU HB2 H 1.45 . 2
80 . 17 LEU HB3 H 1.87 . 2
81 . 17 LEU HG H 1.78 . 1
82 . 17 LEU HD1 H .61 . 2
83 . 17 LEU HD2 H .71 . 2
84 . 18 LEU H H 8.14 . 1
85 . 18 LEU HA H 4.07 . 1
86 . 18 LEU HB2 H 1.92 . 2
87 . 18 LEU HB3 H 2.22 . 2
88 . 18 LEU HG H 1.38 . 1
89 . 18 LEU HD1 H .85 . 2
90 . 18 LEU HD2 H .94 . 2
91 . 19 SER H H 8.18 . 1
92 . 19 SER HA H 4.36 . 1
93 . 19 SER HB2 H 4.06 . 2
94 . 19 SER HB3 H 4.29 . 2
95 . 20 ASN H H 9.1 . 1
96 . 20 ASN HA H 4.19 . 1
97 . 20 ASN HB2 H 2.87 . 2
98 . 20 ASN HB3 H 2.97 . 2
99 . 20 ASN HD21 H 7.11 . 2
100 . 20 ASN HD22 H 7.76 . 2
101 . 21 TYR H H 7.74 . 1
102 . 21 TYR HA H 4.44 . 1
103 . 21 TYR HB2 H 3.05 . 2
104 . 21 TYR HB3 H 3.45 . 2
105 . 21 TYR HD1 H 7.15 . 1
106 . 21 TYR HD2 H 7.15 . 1
107 . 21 TYR HE1 H 6.88 . 1
108 . 21 TYR HE2 H 6.88 . 1
109 . 22 CYS H H 7.99 . 1
110 . 22 CYS HA H 4.27 . 1
111 . 22 CYS HB2 H 2.86 . 2
112 . 22 CYS HB3 H 2.9 . 2
113 . 23 ASN H H 8.36 . 1
114 . 23 ASN HA H 3.92 . 1
115 . 23 ASN HB2 H 1.75 . 2
116 . 23 ASN HB3 H 1.95 . 2
117 . 24 ASN H H 8.11 . 1
118 . 24 ASN HA H 4.08 . 1
119 . 24 ASN HB2 H 2.45 . 2
120 . 24 ASN HB3 H 2.66 . 2
121 . 25 GLN H H 8.53 . 1
122 . 25 GLN HA H 4.42 . 1
123 . 25 GLN HB2 H 1.68 . 2
124 . 25 GLN HB3 H 1.84 . 2
125 . 26 CYS H H 8.91 . 1
126 . 26 CYS HA H 4.26 . 1
127 . 26 CYS HB2 H 2.83 . 2
128 . 26 CYS HB3 H 4.11 . 2
129 . 27 THR H H 7.69 . 1
130 . 27 THR HA H 4.35 . 1
131 . 27 THR HB H 4.11 . 1
132 . 27 THR HG2 H 1.19 . 1
133 . 28 LYS H H 8.46 . 1
134 . 28 LYS HA H 4.11 . 1
135 . 28 LYS HB2 H 1.9 . 2
136 . 28 LYS HB3 H 1.75 . 2
137 . 29 VAL H H 7.66 . 1
138 . 29 VAL HA H 3.74 . 1
139 . 29 VAL HB H 1.96 . 1
140 . 29 VAL HG1 H .23 . 2
141 . 29 VAL HG2 H .81 . 2
142 . 30 HIS H H 6.4 . 1
143 . 30 HIS HA H 4.62 . 1
144 . 30 HIS HB2 H 3.16 . 2
145 . 30 HIS HB3 H 3.22 . 2
146 . 30 HIS HD1 H 7.82 . 1
147 . 30 HIS HD2 H 6.81 . 1
148 . 30 HIS HE1 H 7.45 . 1
149 . 31 TYR H H 6.68 . 1
150 . 31 TYR HA H 4.44 . 1
151 . 31 TYR HB2 H 3.1 . 2
152 . 31 TYR HB3 H 3.37 . 2
153 . 31 TYR HD1 H 7.03 . 1
154 . 31 TYR HD2 H 7.03 . 1
155 . 31 TYR HE1 H 6.83 . 1
156 . 31 TYR HE2 H 6.83 . 1
157 . 32 ALA H H 8.45 . 1
158 . 32 ALA HA H 4.55 . 1
159 . 32 ALA HB H 1.28 . 1
160 . 33 ASP H H 8.39 . 1
161 . 33 ASP HA H 4.55 . 1
162 . 33 ASP HB2 H 2.64 . 2
163 . 33 ASP HB3 H 2.58 . 2
164 . 34 LYS H H 7.83 . 1
165 . 34 LYS HA H 4.75 . 1
166 . 34 LYS HB2 H 2.13 . 2
167 . 34 LYS HB3 H 1.93 . 2
168 . 34 LYS HG2 H 1.19 . 2
169 . 34 LYS HG3 H 1.32 . 2
170 . 34 LYS HD2 H 1.47 . 1
171 . 34 LYS HD3 H 1.47 . 1
172 . 34 LYS HE2 H 2.34 . 2
173 . 34 LYS HE3 H 2.56 . 2
174 . 35 GLY H H 9.05 . 1
175 . 35 GLY HA2 H 5.34 . 2
176 . 35 GLY HA3 H 4.27 . 2
177 . 36 TYR H H 9.5 . 1
178 . 36 TYR HA H 5.02 . 1
179 . 36 TYR HB2 H 2.68 . 2
180 . 36 TYR HB3 H 3.28 . 2
181 . 36 TYR HD1 H 7.19 . 1
182 . 36 TYR HD2 H 7.19 . 1
183 . 36 TYR HE1 H 6.76 . 1
184 . 36 TYR HE2 H 6.76 . 1
185 . 37 CYS H H 8.9 . 1
186 . 37 CYS HA H 4.95 . 1
187 . 37 CYS HB2 H 2.92 . 2
188 . 37 CYS HB3 H 2.75 . 2
189 . 38 CYS H H 8.09 . 1
190 . 38 CYS HA H 4.56 . 1
191 . 38 CYS HB2 H 3.24 . 2
192 . 38 CYS HB3 H 2.75 . 2
193 . 39 LEU H H 8.31 . 1
194 . 39 LEU HA H 4.48 . 1
195 . 39 LEU HB2 H 1.5 . 2
196 . 39 LEU HB3 H 1.55 . 2
197 . 39 LEU HG H 1.55 . 1
198 . 39 LEU HD1 H .89 . 2
199 . 39 LEU HD2 H .92 . 2
200 . 40 LEU H H 8.02 . 1
201 . 40 LEU HA H 4.85 . 1
202 . 40 LEU HB2 H 1.84 . 2
203 . 40 LEU HB3 H 1.95 . 2
204 . 40 LEU HG H 1.69 . 1
205 . 40 LEU HD1 H 1.01 . 2
206 . 40 LEU HD2 H 1.03 . 2
207 . 41 SER H H 7.61 . 1
208 . 41 SER HA H 5.51 . 1
209 . 41 SER HB2 H 3.42 . 2
210 . 41 SER HB3 H 3.47 . 2
211 . 42 CYS H H 8.29 . 1
212 . 42 CYS HA H 5.2 . 1
213 . 42 CYS HB2 H 2.89 . 2
214 . 42 CYS HB3 H 2.79 . 2
215 . 43 TYR H H 9.59 . 1
216 . 43 TYR HA H 4.11 . 1
217 . 43 TYR HB2 H 2.62 . 2
218 . 43 TYR HB3 H 2.72 . 2
219 . 43 TYR HD1 H 5.55 . 1
220 . 43 TYR HD2 H 5.55 . 1
221 . 43 TYR HE1 H 6 . 1
222 . 43 TYR HE2 H 6 . 1
223 . 44 CYS H H 8.31 . 1
224 . 44 CYS HA H 5.54 . 1
225 . 44 CYS HB2 H 3 . 2
226 . 44 CYS HB3 H 2.41 . 2
227 . 45 PHE H H 8.9 . 1
228 . 45 PHE HA H 4.95 . 1
229 . 45 PHE HB2 H 2.95 . 2
230 . 45 PHE HB3 H 3.08 . 2
231 . 45 PHE HD1 H 7.18 . 1
232 . 45 PHE HD2 H 7.18 . 1
233 . 45 PHE HE1 H 7.65 . 1
234 . 45 PHE HE2 H 7.65 . 1
235 . 45 PHE HZ H 7.53 . 1
236 . 46 GLY H H 8.36 . 1
237 . 46 GLY HA2 H 3.67 . 2
238 . 46 GLY HA3 H 4.25 . 2
239 . 47 LEU H H 8.95 . 1
240 . 47 LEU HA H 4.26 . 1
241 . 47 LEU HB2 H 1.54 . 2
242 . 47 LEU HB3 H 1.65 . 2
243 . 47 LEU HG H 1.34 . 1
244 . 47 LEU HD1 H .39 . 2
245 . 47 LEU HD2 H .76 . 2
246 . 48 ASN H H 8.6 . 1
247 . 48 ASN HA H 4.58 . 1
248 . 48 ASN HB2 H 2.8 . 2
249 . 48 ASN HB3 H 2.86 . 2
250 . 48 ASN HD21 H 7.1 . 2
251 . 48 ASN HD22 H 7.92 . 2
252 . 49 ASP H H 8 . 1
253 . 49 ASP HA H 4.42 . 1
254 . 49 ASP HB2 H 2.65 . 2
255 . 49 ASP HB3 H 2.5 . 2
256 . 50 ASP H H 8.52 . 1
257 . 50 ASP HA H 4.51 . 1
258 . 50 ASP HB2 H 2.63 . 2
259 . 50 ASP HB3 H 2.72 . 2
260 . 51 LYS H H 7.5 . 1
261 . 51 LYS HA H 4.17 . 1
262 . 51 LYS HB2 H 2.57 . 2
263 . 51 LYS HB3 H 1.94 . 2
264 . 51 LYS HG2 H 1.45 . 1
265 . 51 LYS HG3 H 1.45 . 1
266 . 51 LYS HD2 H 1.51 . 2
267 . 51 LYS HD3 H 1.62 . 2
268 . 51 LYS HE2 H 2.56 . 1
269 . 51 LYS HE3 H 2.56 . 1
270 . 52 LYS H H 8.72 . 1
271 . 52 LYS HA H 4.34 . 1
272 . 52 LYS HB2 H 1.73 . 2
273 . 52 LYS HB3 H 1.68 . 2
274 . 52 LYS HG2 H 1.36 . 1
275 . 52 LYS HG3 H 1.36 . 1
276 . 53 VAL H H 8.39 . 1
277 . 53 VAL HA H 5.1 . 1
278 . 53 VAL HB H 2.24 . 1
279 . 53 VAL HG1 H .36 . 2
280 . 53 VAL HG2 H .76 . 2
281 . 54 LEU H H 8.03 . 1
282 . 54 LEU HA H 4.18 . 1
283 . 54 LEU HB2 H 1.54 . 2
284 . 54 LEU HB3 H 1.61 . 2
285 . 54 LEU HG H 1.61 . 1
286 . 54 LEU HD1 H .7 . 2
287 . 54 LEU HD2 H .76 . 2
288 . 55 GLU H H 8.74 . 1
289 . 55 GLU HA H 4.37 . 1
290 . 55 GLU HB2 H 1.61 . 2
291 . 55 GLU HB3 H 2.02 . 2
292 . 55 GLU HG2 H 2.25 . 2
293 . 55 GLU HG3 H 2.35 . 2
294 . 56 ILE H H 8.11 . 1
295 . 56 ILE HA H 4.9 . 1
296 . 56 ILE HB H 2.08 . 1
297 . 56 ILE HG12 H 1.41 . 2
298 . 56 ILE HG13 H 1.59 . 2
299 . 56 ILE HG2 H 1.08 . 1
300 . 56 ILE HD1 H 1.06 . 1
301 . 57 SER H H 8.79 . 1
302 . 57 SER HA H 4.41 . 1
303 . 57 SER HB2 H 4.08 . 2
304 . 57 SER HB3 H 4.51 . 2
305 . 58 ASP H H 9.15 . 1
306 . 58 ASP HA H 4.51 . 1
307 . 58 ASP HB2 H 2.92 . 2
308 . 58 ASP HB3 H 2.98 . 2
309 . 59 THR H H 8.11 . 1
310 . 59 THR HA H 4.06 . 1
311 . 59 THR HB H 4.12 . 1
312 . 59 THR HG2 H 1.37 . 1
313 . 60 ARG H H 7.68 . 1
314 . 60 ARG HA H 4.1 . 1
315 . 60 ARG HB2 H 1.95 . 2
316 . 60 ARG HB3 H 2.08 . 2
317 . 60 ARG HG2 H 1.7 . 2
318 . 60 ARG HG3 H 1.82 . 2
319 . 60 ARG HD2 H 3.34 . 2
320 . 60 ARG HD3 H 3.42 . 2
321 . 61 LYS H H 8.44 . 1
322 . 61 LYS HA H 3.75 . 1
323 . 61 LYS HB2 H 2.01 . 2
324 . 61 LYS HB3 H 1.88 . 2
325 . 61 LYS HG2 H 1.53 . 1
326 . 61 LYS HG3 H 1.53 . 1
327 . 61 LYS HD2 H 1.75 . 2
328 . 61 LYS HD3 H 1.85 . 2
329 . 61 LYS HE2 H 3.09 . 1
330 . 61 LYS HE3 H 3.09 . 1
331 . 62 SER H H 8.24 . 1
332 . 62 SER HA H 4.24 . 1
333 . 62 SER HB2 H 3.98 . 2
334 . 62 SER HB3 H 4.03 . 2
335 . 63 TYR H H 7.92 . 1
336 . 63 TYR HA H 4.05 . 1
337 . 63 TYR HB2 H 3.1 . 2
338 . 63 TYR HB3 H 3.15 . 2
339 . 63 TYR HD1 H 6.96 . 1
340 . 63 TYR HD2 H 6.96 . 1
341 . 63 TYR HE1 H 6.85 . 1
342 . 63 TYR HE2 H 6.85 . 1
343 . 64 CYS H H 8.53 . 1
344 . 64 CYS HA H 4.08 . 1
345 . 64 CYS HB2 H 2.95 . 2
346 . 64 CYS HB3 H 2.86 . 2
347 . 65 ASP H H 8.91 . 1
348 . 65 ASP HA H 4.86 . 1
349 . 65 ASP HB2 H 3.43 . 2
350 . 65 ASP HB3 H 3.48 . 2
351 . 66 THR H H 7.49 . 1
352 . 66 THR HA H 4.4 . 1
353 . 66 THR HB H 4.26 . 1
354 . 66 THR HG2 H 1.25 . 1
355 . 67 THR H H 7.51 . 1
356 . 67 THR HA H 4 . 1
357 . 67 THR HB H 3.88 . 1
358 . 67 THR HG2 H 1 . 1
359 . 68 ILE H H 7.21 . 1
360 . 68 ILE HA H 3.68 . 1
361 . 68 ILE HB H 1.29 . 1
362 . 68 ILE HG12 H .84 . 2
363 . 68 ILE HG13 H 1.11 . 2
364 . 68 ILE HG2 H .54 . 1
365 . 68 ILE HD1 H .5 . 1
366 . 69 ILE H H 7.62 . 1
367 . 69 ILE HA H 4.06 . 1
368 . 69 ILE HB H 1.78 . 1
369 . 69 ILE HG12 H .98 . 2
370 . 69 ILE HG13 H 1.34 . 2
371 . 69 ILE HG2 H .83 . 1
372 . 69 ILE HD1 H .74 . 1
373 . 70 ASN H H 7.93 . 1
374 . 70 ASN HA H 4.43 . 1
375 . 70 ASN HB2 H 2.6 . 2
376 . 70 ASN HB3 H 2.73 . 2
377 . 70 ASN HD21 H 7.04 . 2
378 . 70 ASN HD22 H 7.83 . 2
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