data_4218
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution structure of toxin 2 from centruroides noxius hoffmann,a beta scorpion
neurotoxin acting on sodium channels
;
_BMRB_accession_number 4218
_BMRB_flat_file_name bmr4218.str
_Entry_type original
_Submission_date 1998-07-01
_Accession_date 1998-07-01
_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 PINTAR A. . .
2 POSSANI L. D. .
3 DELEPIERRE M. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 336
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2008-07-10 update BMRB 'Updating non-standard residue'
2008-03-24 update BMRB .
2000-05-04 original author .
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Solution structure of toxin 2 from centruroides noxius Hoffmann, a beta-scorpion
neurotoxin acting on sodium channels
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 99182423
_PubMed_ID 10080898
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 PINTAR A. . .
2 POSSANI L. D. .
3 DELEPIERRE M. . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of Molecular biology'
_Journal_volume 287
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 359
_Page_last 367
_Year 1999
_Details .
loop_
_Keyword
'Centruroides noxius'
neurotoxin
'scorpion toxin'
'sodium channels'
stop_
save_
##################################
# Molecular system description #
##################################
save_system-T2CNH
_Saveframe_category molecular_system
_Mol_system_name 'Toxin 2 from Centruroides noxius hoffmann'
_Abbreviation_common T2CNH
_Enzyme_commission_number 5.3.4.1
loop_
_Mol_system_component_name
_Mol_label
T2CNH $T2CNH
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_T2CNH
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Toxin 2 from Centruroides noxius hoffmann'
_Abbreviation_common T2CNH
_Molecular_mass .
_Mol_thiol_state 'all disulfide bond'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 67
_Mol_residue_sequence
;
KEGYLVDKNTGCKYECLKLG
DNDYCLRECKQQYGKGAGGY
CYAFACWCTHLYEQAIVWPL
PNKRCSX
;
loop_
_Residue_seq_code
_Residue_label
1 LYS 2 GLU 3 GLY 4 TYR 5 LEU
6 VAL 7 ASP 8 LYS 9 ASN 10 THR
11 GLY 12 CYS 13 LYS 14 TYR 15 GLU
16 CYS 17 LEU 18 LYS 19 LEU 20 GLY
21 ASP 22 ASN 23 ASP 24 TYR 25 CYS
26 LEU 27 ARG 28 GLU 29 CYS 30 LYS
31 GLN 32 GLN 33 TYR 34 GLY 35 LYS
36 GLY 37 ALA 38 GLY 39 GLY 40 TYR
41 CYS 42 TYR 43 ALA 44 PHE 45 ALA
46 CYS 47 TRP 48 CYS 49 THR 50 HIS
51 LEU 52 TYR 53 GLU 54 GLN 55 ALA
56 ILE 57 VAL 58 TRP 59 PRO 60 LEU
61 PRO 62 ASN 63 LYS 64 ARG 65 CYS
66 SER 67 NH2
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-10-13
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 1CN2 "Solution Structure Of Toxin 2 From Centruroides Noxius Hoffmann, A Beta Scorpion Neurotoxin Acting On Sodium Channels, Nmr, 15 " 98.51 67 100.00 100.00 1.39e-39
PDB 2YBR "Crystal Structure Of The Human Derived Single Chain Antibody Fragment (scfv) 9004g In Complex With Cn2 Toxin From The Scorpion " 98.51 66 100.00 100.00 1.35e-39
PDB 2YC1 "Crystal Structure Of The Human Derived Single Chain Antibody Fragment (scfv) 9004g In Complex With Cn2 Toxin From The Scorpion " 98.51 66 100.00 100.00 1.35e-39
GB AAB21461 "toxin 2, Cn2 [Centruroides noxius=scorpions, Hoffmann, venom, Peptide, 66 aa]" 98.51 66 96.97 96.97 5.16e-37
GB AAB36086 "Na+ channel-specific toxin 2, partial [Centruroides noxius]" 98.51 84 100.00 100.00 5.80e-40
GB AAR08045 "beta-toxin [Centruroides noxius]" 97.01 64 98.46 98.46 2.04e-36
SP P01495 "RecName: Full=Beta-mammal toxin Cn2; Short=Toxin 2; AltName: Full=Toxin II.9.2.2; Flags: Precursor" 98.51 84 100.00 100.00 5.80e-40
stop_
save_
######################
# Polymer residues #
######################
save_chem_comp_NH2
_Saveframe_category polymer_residue
_Mol_type non-polymer
_Name_common 'AMINO GROUP'
_BMRB_code .
_PDB_code NH2
_Standard_residue_derivative .
_Molecular_mass 16.023
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Wed Jul 13 13:32:02 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
N N N . 0 . ?
HN1 HN1 H . 0 . ?
HN2 HN2 H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING N HN1 ? ?
SING N HN2 ? ?
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Organ
_Secretion
$T2CNH 'Mexican scorpion' 6878 Eukaryota Metazoa Centruroides noxius heart 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
$T2CNH '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
$T2CNH 1 mM .
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Unity
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 4.0 . n/a
pressure 1 . atm
temperature 303 . K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_shift_ref
_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
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . $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_chem_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chem_shift_ref
_Mol_system_component_name T2CNH
_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 HA H 4.091 0.03 1
2 . 1 LYS HB2 H 1.775 0.03 2
3 . 1 LYS HB3 H 1.508 0.03 2
4 . 1 LYS HG2 H 0.992 0.03 1
5 . 1 LYS HG3 H 0.992 0.03 1
6 . 1 LYS HD2 H 1.591 0.03 1
7 . 1 LYS HD3 H 1.591 0.03 1
8 . 2 GLU H H 8.007 0.03 1
9 . 2 GLU HA H 4.605 0.03 1
10 . 2 GLU HB2 H 2.138 0.03 2
11 . 2 GLU HB3 H 1.865 0.03 2
12 . 2 GLU HG2 H 2.338 0.03 2
13 . 2 GLU HG3 H 2.233 0.03 2
14 . 3 GLY H H 7.245 0.03 1
15 . 3 GLY HA2 H 3.352 0.03 2
16 . 3 GLY HA3 H 1.827 0.03 2
17 . 4 TYR H H 9.181 0.03 1
18 . 4 TYR HA H 4.932 0.03 1
19 . 4 TYR HB2 H 3.152 0.03 2
20 . 4 TYR HB3 H 3.048 0.03 2
21 . 4 TYR HE1 H 7.355 0.03 1
22 . 4 TYR HE2 H 7.355 0.03 1
23 . 4 TYR HD1 H 7.602 0.03 1
24 . 4 TYR HD2 H 7.602 0.03 1
25 . 5 LEU H H 7.720 0.03 1
26 . 5 LEU HA H 4.587 0.03 1
27 . 5 LEU HB2 H 1.854 0.03 2
28 . 5 LEU HB3 H 1.702 0.03 2
29 . 5 LEU HG H 1.421 0.03 1
30 . 5 LEU HD1 H 0.651 0.03 2
31 . 5 LEU HD2 H 0.067 0.03 2
32 . 6 VAL H H 7.104 0.03 1
33 . 6 VAL HA H 5.213 0.03 1
34 . 6 VAL HB H 2.059 0.03 1
35 . 6 VAL HG1 H 1.059 0.03 2
36 . 6 VAL HG2 H 0.808 0.03 2
37 . 7 ASP H H 8.581 0.03 1
38 . 7 ASP HA H 4.909 0.03 1
39 . 7 ASP HB2 H 3.190 0.03 2
40 . 7 ASP HB3 H 2.497 0.03 2
41 . 8 LYS H H 9.090 0.03 1
42 . 8 LYS HA H 3.977 0.03 1
43 . 8 LYS HB2 H 1.903 0.03 2
44 . 8 LYS HB3 H 1.863 0.03 2
45 . 8 LYS HG2 H 1.584 0.03 2
46 . 8 LYS HG3 H 1.475 0.03 2
47 . 8 LYS HD2 H 1.753 0.03 1
48 . 8 LYS HD3 H 1.753 0.03 1
49 . 9 ASN H H 8.778 0.03 1
50 . 9 ASN HA H 4.728 0.03 1
51 . 9 ASN HB2 H 3.016 0.03 2
52 . 9 ASN HB3 H 2.842 0.03 2
53 . 10 THR H H 7.868 0.03 1
54 . 10 THR HA H 4.473 0.03 1
55 . 10 THR HB H 4.566 0.03 1
56 . 10 THR HG2 H 1.172 0.03 1
57 . 11 GLY H H 8.817 0.03 1
58 . 11 GLY HA2 H 4.301 0.03 2
59 . 11 GLY HA3 H 3.574 0.03 2
60 . 12 CYS H H 8.100 0.03 1
61 . 12 CYS HA H 4.988 0.03 1
62 . 12 CYS HB2 H 3.591 0.03 2
63 . 12 CYS HB3 H 2.904 0.03 2
64 . 14 TYR H H 9.240 0.03 1
65 . 14 TYR HA H 4.643 0.03 1
66 . 14 TYR HB2 H 2.884 0.03 1
67 . 14 TYR HB3 H 2.884 0.03 1
68 . 14 TYR HE1 H 6.618 0.03 1
69 . 14 TYR HE2 H 6.618 0.03 1
70 . 14 TYR HD1 H 7.061 0.03 1
71 . 14 TYR HD2 H 7.061 0.03 1
72 . 16 CYS H H 8.192 0.03 1
73 . 16 CYS HA H 4.846 0.03 1
74 . 16 CYS HB2 H 3.327 0.03 2
75 . 16 CYS HB3 H 3.163 0.03 2
76 . 17 LEU H H 8.266 0.03 1
77 . 17 LEU HA H 4.671 0.03 1
78 . 17 LEU HG H 1.252 0.03 1
79 . 17 LEU HD1 H 0.524 0.03 2
80 . 17 LEU HD2 H 0.373 0.03 2
81 . 19 LEU H H 8.310 0.03 1
82 . 19 LEU HA H 3.690 0.03 1
83 . 19 LEU HB2 H 1.718 0.03 2
84 . 19 LEU HB3 H 1.393 0.03 2
85 . 19 LEU HG H 1.492 0.03 1
86 . 19 LEU HD1 H 0.734 0.03 2
87 . 19 LEU HD2 H 0.124 0.03 2
88 . 20 GLY H H 9.046 0.03 1
89 . 20 GLY HA2 H 4.337 0.03 2
90 . 20 GLY HA3 H 3.682 0.03 2
91 . 21 ASP H H 8.581 0.03 1
92 . 21 ASP HA H 4.676 0.03 1
93 . 21 ASP HB2 H 2.806 0.03 2
94 . 21 ASP HB3 H 2.693 0.03 2
95 . 22 ASN H H 9.166 0.03 1
96 . 22 ASN HA H 4.842 0.03 1
97 . 22 ASN HB2 H 3.023 0.03 2
98 . 22 ASN HB3 H 2.675 0.03 2
99 . 23 ASP H H 9.057 0.03 1
100 . 23 ASP HA H 4.555 0.03 1
101 . 23 ASP HB2 H 2.793 0.03 1
102 . 23 ASP HB3 H 2.793 0.03 1
103 . 24 TYR H H 8.065 0.03 1
104 . 24 TYR HA H 4.353 0.03 1
105 . 24 TYR HB2 H 3.282 0.03 2
106 . 24 TYR HB3 H 3.420 0.03 2
107 . 24 TYR HE1 H 6.888 0.03 1
108 . 24 TYR HE2 H 6.888 0.03 1
109 . 24 TYR HD1 H 7.119 0.03 1
110 . 24 TYR HD2 H 7.119 0.03 1
111 . 25 CYS H H 8.215 0.03 1
112 . 25 CYS HA H 4.246 0.03 1
113 . 25 CYS HB2 H 2.495 0.03 2
114 . 25 CYS HB3 H 2.732 0.03 2
115 . 26 LEU H H 8.261 0.03 1
116 . 26 LEU HA H 3.741 0.03 1
117 . 26 LEU HB2 H 1.754 0.03 2
118 . 26 LEU HB3 H 2.061 0.03 2
119 . 26 LEU HG H 1.584 0.03 1
120 . 26 LEU HD1 H 1.066 0.03 2
121 . 26 LEU HD2 H 1.191 0.03 2
122 . 27 ARG H H 8.054 0.03 1
123 . 27 ARG HA H 3.882 0.03 1
124 . 27 ARG HB2 H 1.843 0.03 2
125 . 27 ARG HB3 H 1.999 0.03 2
126 . 27 ARG HG2 H 1.184 0.03 2
127 . 27 ARG HG3 H 1.590 0.03 2
128 . 28 GLU H H 8.379 0.03 1
129 . 28 GLU HA H 3.873 0.03 1
130 . 28 GLU HB2 H 1.435 0.03 2
131 . 28 GLU HB3 H 1.680 0.03 2
132 . 28 GLU HG2 H 1.982 0.03 1
133 . 28 GLU HG3 H 1.982 0.03 1
134 . 29 CYS H H 8.712 0.03 1
135 . 29 CYS HA H 4.343 0.03 1
136 . 29 CYS HB2 H 2.797 0.03 2
137 . 29 CYS HB3 H 2.992 0.03 2
138 . 30 LYS H H 7.995 0.03 1
139 . 30 LYS HA H 4.542 0.03 1
140 . 30 LYS HB2 H 1.657 0.03 2
141 . 30 LYS HB3 H 1.788 0.03 2
142 . 30 LYS HG2 H 1.584 0.03 1
143 . 30 LYS HG3 H 1.584 0.03 1
144 . 31 GLN H H 8.212 0.03 1
145 . 31 GLN HA H 3.915 0.03 1
146 . 31 GLN HB2 H 2.112 0.03 1
147 . 31 GLN HB3 H 2.112 0.03 1
148 . 31 GLN HG2 H 2.391 0.03 1
149 . 31 GLN HG3 H 2.391 0.03 1
150 . 32 GLN H H 7.480 0.03 1
151 . 32 GLN HA H 4.138 0.03 1
152 . 32 GLN HB2 H 1.265 0.03 2
153 . 32 GLN HB3 H 1.590 0.03 2
154 . 32 GLN HG2 H 1.761 0.03 1
155 . 32 GLN HG3 H 1.761 0.03 1
156 . 33 TYR H H 8.324 0.03 1
157 . 33 TYR HA H 4.989 0.03 1
158 . 33 TYR HB2 H 2.657 0.03 2
159 . 33 TYR HB3 H 3.385 0.03 2
160 . 33 TYR HE1 H 6.873 0.03 1
161 . 33 TYR HE2 H 6.873 0.03 1
162 . 33 TYR HD1 H 7.240 0.03 1
163 . 33 TYR HD2 H 7.240 0.03 1
164 . 34 GLY H H 7.878 0.03 1
165 . 34 GLY HA2 H 4.710 0.03 2
166 . 34 GLY HA3 H 3.915 0.03 2
167 . 35 LYS H H 8.274 0.03 1
168 . 35 LYS HA H 3.871 0.03 1
169 . 35 LYS HB2 H 1.904 0.03 1
170 . 35 LYS HB3 H 1.904 0.03 1
171 . 35 LYS HG2 H 1.516 0.03 3
172 . 35 LYS HG3 H 1.516 0.03 3
173 . 36 GLY H H 8.693 0.03 1
174 . 36 GLY HA2 H 4.085 0.03 2
175 . 36 GLY HA3 H 3.747 0.03 2
176 . 37 ALA H H 7.735 0.03 1
177 . 37 ALA HA H 4.627 0.03 1
178 . 37 ALA HB H 1.386 0.03 1
179 . 38 GLY H H 7.831 0.03 1
180 . 38 GLY HA2 H 4.540 0.03 2
181 . 38 GLY HA3 H 3.498 0.03 2
182 . 39 GLY H H 7.921 0.03 1
183 . 39 GLY HA2 H 4.884 0.03 2
184 . 39 GLY HA3 H 4.615 0.03 2
185 . 40 TYR H H 8.941 0.03 1
186 . 40 TYR HA H 4.837 0.03 1
187 . 40 TYR HB2 H 3.305 0.03 2
188 . 40 TYR HB3 H 3.102 0.03 2
189 . 40 TYR HE1 H 6.547 0.03 1
190 . 40 TYR HE2 H 6.547 0.03 1
191 . 40 TYR HD1 H 6.866 0.03 1
192 . 40 TYR HD2 H 6.866 0.03 1
193 . 41 CYS H H 9.296 0.03 1
194 . 41 CYS HA H 5.212 0.03 1
195 . 41 CYS HB2 H 3.872 0.03 2
196 . 41 CYS HB3 H 2.991 0.03 2
197 . 42 TYR H H 9.460 0.03 1
198 . 42 TYR HA H 4.953 0.03 1
199 . 42 TYR HB2 H 2.956 0.03 2
200 . 42 TYR HB3 H 2.734 0.03 2
201 . 42 TYR HE1 H 6.401 0.03 1
202 . 42 TYR HE2 H 6.401 0.03 1
203 . 42 TYR HD1 H 6.828 0.03 1
204 . 42 TYR HD2 H 6.828 0.03 1
205 . 43 ALA H H 9.052 0.03 1
206 . 43 ALA HA H 3.482 0.03 1
207 . 43 ALA HB H 1.031 0.03 1
208 . 44 PHE H H 6.233 0.03 1
209 . 44 PHE HA H 4.130 0.03 1
210 . 44 PHE HB2 H 3.289 0.03 1
211 . 44 PHE HB3 H 3.289 0.03 1
212 . 44 PHE HD1 H 7.330 0.03 1
213 . 44 PHE HD2 H 7.330 0.03 1
214 . 44 PHE HE1 H 7.370 0.03 1
215 . 44 PHE HE2 H 7.370 0.03 1
216 . 45 ALA H H 8.121 0.03 1
217 . 45 ALA HA H 5.496 0.03 1
218 . 45 ALA HB H 1.320 0.03 1
219 . 46 CYS H H 8.713 0.03 1
220 . 46 CYS HA H 5.295 0.03 1
221 . 46 CYS HB2 H 2.840 0.03 2
222 . 46 CYS HB3 H 2.702 0.03 2
223 . 47 TRP H H 9.739 0.03 1
224 . 47 TRP HA H 4.622 0.03 1
225 . 47 TRP HB2 H 2.813 0.03 2
226 . 47 TRP HB3 H 2.580 0.03 2
227 . 47 TRP HD1 H 6.168 0.03 1
228 . 47 TRP HE3 H 5.508 0.03 1
229 . 47 TRP HE1 H 10.173 0.03 1
230 . 47 TRP HZ3 H 6.648 0.03 1
231 . 47 TRP HZ2 H 7.124 0.03 1
232 . 47 TRP HH2 H 7.050 0.03 1
233 . 48 CYS H H 8.637 0.03 1
234 . 48 CYS HA H 5.671 0.03 1
235 . 48 CYS HB2 H 3.283 0.03 2
236 . 48 CYS HB3 H 2.231 0.03 2
237 . 49 THR H H 8.051 0.03 1
238 . 49 THR HA H 4.537 0.03 1
239 . 49 THR HB H 4.090 0.03 1
240 . 49 THR HG2 H 1.184 0.03 1
241 . 50 HIS H H 8.830 0.03 1
242 . 50 HIS HA H 4.082 0.03 1
243 . 50 HIS HB2 H 3.468 0.03 2
244 . 50 HIS HB3 H 3.424 0.03 2
245 . 50 HIS HD2 H 7.221 0.03 1
246 . 50 HIS HE1 H 8.586 0.03 1
247 . 51 LEU H H 8.163 0.03 1
248 . 51 LEU HA H 4.182 0.03 1
249 . 51 LEU HB2 H 0.926 0.03 2
250 . 51 LEU HB3 H 0.698 0.03 2
251 . 51 LEU HG H 0.878 0.03 1
252 . 51 LEU HD1 H 0.034 0.03 2
253 . 51 LEU HD2 H -0.401 0.03 2
254 . 52 TYR H H 7.849 0.03 1
255 . 52 TYR HA H 4.585 0.03 1
256 . 52 TYR HB2 H 3.287 0.03 2
257 . 52 TYR HB3 H 3.181 0.03 2
258 . 52 TYR HE1 H 7.001 0.03 1
259 . 52 TYR HE2 H 7.001 0.03 1
260 . 52 TYR HD1 H 7.328 0.03 1
261 . 52 TYR HD2 H 7.328 0.03 1
262 . 53 GLU H H 8.712 0.03 1
263 . 53 GLU HA H 3.794 0.03 1
264 . 53 GLU HB2 H 2.055 0.03 1
265 . 53 GLU HB3 H 2.055 0.03 1
266 . 53 GLU HG2 H 2.440 0.03 1
267 . 53 GLU HG3 H 2.440 0.03 1
268 . 54 GLN H H 7.844 0.03 1
269 . 54 GLN HA H 4.335 0.03 1
270 . 54 GLN HB2 H 2.323 0.03 2
271 . 54 GLN HB3 H 2.024 0.03 2
272 . 54 GLN HG2 H 2.444 0.03 1
273 . 54 GLN HG3 H 2.444 0.03 1
274 . 55 ALA H H 7.375 0.03 1
275 . 55 ALA HA H 4.007 0.03 1
276 . 55 ALA HB H 0.837 0.03 1
277 . 56 ILE H H 8.597 0.03 1
278 . 56 ILE HA H 4.238 0.03 1
279 . 56 ILE HB H 1.868 0.03 1
280 . 56 ILE HG2 H 0.873 0.03 1
281 . 56 ILE HG12 H 1.298 0.03 1
282 . 56 ILE HG13 H 1.298 0.03 1
283 . 56 ILE HD1 H 0.930 0.03 1
284 . 57 VAL H H 8.197 0.03 1
285 . 57 VAL HA H 4.629 0.03 1
286 . 57 VAL HB H 2.307 0.03 1
287 . 57 VAL HG1 H 0.690 0.03 2
288 . 57 VAL HG2 H 0.116 0.03 2
289 . 58 TRP H H 8.552 0.03 1
290 . 58 TRP HA H 4.093 0.03 1
291 . 58 TRP HB2 H 3.029 0.03 2
292 . 58 TRP HB3 H 3.441 0.03 2
293 . 58 TRP HD1 H 7.316 0.03 1
294 . 58 TRP HE1 H 10.125 0.03 1
295 . 58 TRP HZ2 H 7.638 0.03 1
296 . 59 PRO HA H 3.686 0.03 1
297 . 59 PRO HB2 H 1.402 0.03 2
298 . 59 PRO HB3 H 1.313 0.03 2
299 . 59 PRO HG2 H 1.087 0.03 1
300 . 59 PRO HG3 H 1.087 0.03 1
301 . 59 PRO HD2 H 3.390 0.03 2
302 . 59 PRO HD3 H 3.190 0.03 2
303 . 60 LEU H H 8.867 0.03 1
304 . 60 LEU HA H 4.581 0.03 1
305 . 60 LEU HB2 H 1.920 0.03 2
306 . 60 LEU HB3 H 1.638 0.03 2
307 . 60 LEU HG H 1.719 0.03 1
308 . 60 LEU HD1 H 0.959 0.03 2
309 . 60 LEU HD2 H 0.873 0.03 2
310 . 61 PRO HA H 4.188 0.03 1
311 . 61 PRO HB2 H 2.266 0.03 2
312 . 61 PRO HB3 H 1.887 0.03 2
313 . 61 PRO HG2 H 2.049 0.03 1
314 . 61 PRO HG3 H 2.049 0.03 1
315 . 61 PRO HD2 H 3.884 0.03 2
316 . 61 PRO HD3 H 3.739 0.03 2
317 . 62 ASN H H 8.309 0.03 1
318 . 62 ASN HA H 4.682 0.03 1
319 . 62 ASN HB2 H 2.868 0.03 1
320 . 62 ASN HB3 H 2.868 0.03 1
321 . 63 LYS H H 7.048 0.03 1
322 . 63 LYS HA H 4.517 0.03 1
323 . 64 ARG H H 8.581 0.03 1
324 . 64 ARG HA H 4.493 0.03 1
325 . 64 ARG HB2 H 1.819 0.03 2
326 . 64 ARG HB3 H 1.722 0.03 2
327 . 64 ARG HG2 H 1.612 0.03 1
328 . 64 ARG HG3 H 1.612 0.03 1
329 . 65 CYS H H 8.812 0.03 1
330 . 65 CYS HA H 4.769 0.03 1
331 . 65 CYS HB2 H 3.299 0.03 2
332 . 65 CYS HB3 H 3.142 0.03 2
333 . 66 SER H H 8.793 0.03 1
334 . 66 SER HA H 4.516 0.03 1
335 . 66 SER HB2 H 3.980 0.03 2
336 . 66 SER HB3 H 3.933 0.03 2
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