data_4988
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Three Dimensional Solution Structure of Huwentoxin-II BY 2D 1H-NMR
;
_BMRB_accession_number 4988
_BMRB_flat_file_name bmr4988.str
_Entry_type original
_Submission_date 2001-04-12
_Accession_date 2001-04-17
_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 Shu Qin . .
2 Lu Shan-yun . .
3 Gu Xiao-chen . .
4 Liang Song-ping . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 249
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-05-11 original BMRB .
stop_
_Original_release_date 2001-04-17
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Three-dimensional Solution Structure Determination of Huwentoxin-II by 2D 1H-NMR
;
_Citation_status submitted
_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 Shu Q. . .
2 Lu S. Y. .
3 Gu X. C. .
4 Liang S. P. .
stop_
_Journal_abbreviation .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first .
_Page_last .
_Year .
_Details .
loop_
_Keyword
'disulfide bonds'
'insecticidal toxin'
neurotoxin
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Q. SHU, S.Y. LU, X.C. GU, S.P. LIANG.
Sequence-specific assignment of 1H-NMR resonance and
determination of the secondary structure of HWTX-II.
Acta Biochim. et Biophys. Sinica 2001,33: 65
;
_Citation_title
;
Sequence-specific Assignment of (1)H-NMR Resonance and Determination of the Secondary Structure of HWTX-II.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12053191
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Shu . . .
2 Lu . Y. .
3 Gu . C. .
4 Liang . P. .
stop_
_Journal_abbreviation 'Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao'
_Journal_name_full 'Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica'
_Journal_volume 33
_Journal_issue 1
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 65
_Page_last 70
_Year 2001
_Details
;
Huwentoxin-II (HWTX-II)is an insecticidal peptide purified from the venom of
spider Selenocosmia huwena. The structure of this toxin in solution was
investigated using 2D-NMR. The complete sequence-specific assignments of proton
resonance in the (1)H-NMR spectra of HWTX-II were obtained by analyzing a
series of 2D spectrum, including COSY, DQF-COSY, TOCSY and NOESY. All the
backbone protons and side chain protons, except epsilonNH(2) protons of Lys
residues, were identified by d(alphaN), d(alpha&dgr);, d(NN) and d(betaN)
connectivities. The results provide a basis for further determination of the
solution conformation of HWTX-II. Furthermore the secondary structure of
HWTX-II was determined from NMR data. It contained mainly extended
conformation, especially a double-stranded anti-parallel beta-sheet with
Trp27--Cys29 and Cys34--Lys36 at the C terminal, and it lacked helix. These
characters of the secondary structure of HWTX-II were similar to those spider
toxins which structure in solution had been reported.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full
;
Q.SHU,R.H.HUANG,S.P.LIANG
Assignment of disulfide bonds of huwentoxin-ii by Edman
degradation sequencing and stepwise thiol modification.
Eur. J. Biochem. 2001, 268(8):2301-2307
;
_Citation_title
;
Assignment of the disulfide bonds of huwentoxin-II by Edman degradation sequencing and stepwise thiol modification.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 11298747
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Shu Q . .
2 Huang R . .
3 Liang S . .
stop_
_Journal_abbreviation 'Eur. J. Biochem.'
_Journal_name_full 'European journal of biochemistry / FEBS'
_Journal_volume 268
_Journal_issue 8
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 2301
_Page_last 2307
_Year 2001
_Details
;
A novel strategy combining Edman degradation and thiol modification was
developed to assign the three disulfides of huwentoxin-II (HWTX-II), an
insecticidal peptide purified from the venom of the spider Selenocosmia huwena.
Phenylthiohydantoin (Pth) derivatives of Cys and the elimination product,
dehydroalanine (DeltaSer), can be observed in the Cys cycles during Edman
degradation of native HWTX-II. The appearance of two products indicates that
the disulfides of HWTX-II were split and that the free thiol group of the
second half cystine has been generated. Information about the nature of the
disulfide bridges of HWTX-II could be obtained from the sequencing signal if
the nascent thiols were modified stepwise by 4-vinylpyridine. Using this method
the disulfide bridges of HWTX-II were assigned as Cys4-Cys18, Cys8-Cys29 and
Cys23-Cys34, which is different from that seen in HWTX-I, a neurotoxic peptide
from the same spider. Using this strategy, one can assign the disulfide bonds
of small proteins by sequencing and modification n - 1 times, where n is the
number of disulfide bonds in the protein. The above assignment of the disulfide
bonds of HWTX-II was confirmed by MALDI-TOF MS of tryptic fragments of HWTX-II.
Some disulfide interchanging during proteolysis was observed by monitoring the
kinetics of proteolysis of HWTX-II by MALDI-TOF MS.
;
save_
save_ref_3
_Saveframe_category citation
_Citation_full
;
Purification and characterization of huwentoxin-II,
a neurotoxic peptide from the venom of the Chinese
bird spider Selenocosmia huwena.
J. Pept. Res. 1999 May;53(5):486-491
;
_Citation_title
;
Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 10424342
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Shu Q . .
2 Liang 'S P' P. .
stop_
_Journal_abbreviation 'J. Pept. Res.'
_Journal_name_full 'The journal of peptide research : official journal of the American Peptide Society'
_Journal_volume 53
_Journal_issue 5
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 486
_Page_last 491
_Year 1999
_Details
;
A neurotoxic peptide, huwentoxin-II (HWTX-II), was purified from the venom of
the Chinese bird spider Selenocosmia huwena by ion exchange chromatography and
reversed phase HPLC. The toxin can reversibly paralyse cockroaches for several
hours, with an ED50 of 127 +/- 54 microg/g. HWTX-II blocks neuromuscular
transmission in an isolated mouse phrenic nerve diaphragm preparation and acts
cooperatively to potentiate the activity of huwentoxin-I. The complete amino
sequence of HWTX-II was determined and found to consist of 37 amino acid
residues, including six Cys residues. There is microheterogeneity (Ile/Gln) in
position 10, and mass spectrometry indicated that the two isoproteins have a
tendency to dimerize. It was determined by mass spectrometry that the six Cys
residues are involved in three disulphide bonds. The sequence of HWTX-II is
highly homologous with ESTX, a toxin from the tarantula Eurypefina
californicum.
;
save_
##################################
# Molecular system description #
##################################
save_system_HWTX-II
_Saveframe_category molecular_system
_Mol_system_name HUWENTOXIN-II
_Abbreviation_common HWTX-II
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'HUWENTOXIN-II(Ile, 10)' $HUWENTOXIN-II
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
loop_
_Biological_function
neurotoxin
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_HUWENTOXIN-II
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Huwentoxin-II
_Abbreviation_common HWTX-II
_Molecular_mass 4284.3
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 37
_Mol_residue_sequence
;
LFECSFSCEIEKEGDKPCKK
KKCKGGWKCKFNMCVKV
;
loop_
_Residue_seq_code
_Residue_label
1 LEU 2 PHE 3 GLU 4 CYS 5 SER
6 PHE 7 SER 8 CYS 9 GLU 10 ILE
11 GLU 12 LYS 13 GLU 14 GLY 15 ASP
16 LYS 17 PRO 18 CYS 19 LYS 20 LYS
21 LYS 22 LYS 23 CYS 24 LYS 25 GLY
26 GLY 27 TRP 28 LYS 29 CYS 30 LYS
31 PHE 32 ASN 33 MET 34 CYS 35 VAL
36 LYS 37 VAL
stop_
_Sequence_homology_query_date 2008-08-19
_Sequence_homology_query_revised_last_date 2008-08-19
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 1I25 'Three Dimensional Solution Structure Of Huwentoxin-Ii By 2d 1h-Nmr' 100.00 37 100.00 100.00 1.67e-11
GenBank AAP33076 'huwentoxin-II precursor [Ornithoctonus huwena]' 100.00 85 100.00 100.00 4.89e-13
GenBank ABY77725 'HWTX-IIa precursor [Ornithoctonus huwena]' 97.30 85 100.00 100.00 2.00e-12
GenBank ABY77726 'HWTX-IIb precursor [Ornithoctonus huwena]' 100.00 85 100.00 100.00 4.89e-13
GenBank ABY77727 'HWTX-IIc precursor [Ornithoctonus huwena]' 97.30 85 100.00 100.00 1.89e-12
GenBank ABY77732 'HWTX-VIIIa precursor [Ornithoctonus huwena]' 97.30 84 100.00 100.00 2.23e-12
SWISS-PROT P68421 'Huwentoxin-7 precursor (Huwentoxin-VII) (HwTx-VII)' 100.00 84 100.00 100.00 5.78e-13
SWISS-PROT P82959 'Huwentoxin-2 form 1 precursor (Huwentoxin-II) (HwTx-II)' 100.00 85 100.00 100.00 4.89e-13
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
$HUWENTOXIN-II 'Chinese bird spider' 29017 Eukaryota Metazoa Selenocosmia huwena 'venom gland'
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
$HUWENTOXIN-II '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
$HUWENTOXIN-II 4 mM .
'phosphate buffer' 20 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$HUWENTOXIN-II 4 mM .
'phosphate buffer' 20 mM .
D2O 100 % .
stop_
save_
############################
# Computer software used #
############################
save_FELIX
_Saveframe_category software
_Name FELIX
_Version 98.0
loop_
_Task
'data analysis'
stop_
_Details 'Molecular Simulations, Inc.'
save_
save_X-PLOR
_Saveframe_category software
_Name X-PLOR
_Version 3.851
loop_
_Task
refinement
stop_
_Details Brunger
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_Sample_label .
save_
save_DQF-COSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name DQF-COSY
_Sample_label .
save_
save_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TOCSY
_Sample_label .
save_
save_E-COSY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name E-COSY
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 20 0.02 mM
pH 5.4 0.2 n/a
pressure 1 . atm
temperature 300 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
TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal .
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_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
NOESY
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'HUWENTOXIN-II(Ile, 10)'
_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 LEU HA H 3.93 0.02 1
2 . 1 LEU HB2 H 1.56 0.02 1
3 . 1 LEU HB3 H 1.56 0.02 1
4 . 1 LEU HG H 1.59 0.02 1
5 . 1 LEU HD1 H 0.78 0.02 2
6 . 1 LEU HD2 H 0.80 0.02 2
7 . 2 PHE H H 8.48 0.02 1
8 . 2 PHE HA H 4.77 0.02 1
9 . 2 PHE HB2 H 3.00 0.02 2
10 . 2 PHE HB3 H 3.25 0.02 2
11 . 2 PHE HD1 H 7.33 0.02 1
12 . 2 PHE HD2 H 7.33 0.02 1
13 . 2 PHE HE1 H 7.37 0.02 1
14 . 2 PHE HE2 H 7.37 0.02 1
15 . 2 PHE HZ H 7.32 0.02 1
16 . 3 GLU H H 8.73 0.02 1
17 . 3 GLU HA H 4.54 0.02 1
18 . 3 GLU HB2 H 1.96 0.02 1
19 . 3 GLU HB3 H 1.96 0.02 1
20 . 3 GLU HG2 H 2.25 0.02 2
21 . 3 GLU HG3 H 2.57 0.02 2
22 . 4 CYS H H 9.60 0.02 1
23 . 4 CYS HA H 4.31 0.02 1
24 . 4 CYS HB2 H 2.61 0.02 2
25 . 4 CYS HB3 H 3.50 0.02 2
26 . 5 SER H H 9.95 0.02 1
27 . 5 SER HA H 4.06 0.02 1
28 . 5 SER HB2 H 3.51 0.02 2
29 . 5 SER HB3 H 3.81 0.02 2
30 . 6 PHE H H 9.75 0.02 1
31 . 6 PHE HA H 4.69 0.02 1
32 . 6 PHE HB2 H 3.06 0.02 2
33 . 6 PHE HB3 H 3.19 0.02 2
34 . 6 PHE HD1 H 7.26 0.02 1
35 . 6 PHE HD2 H 7.26 0.02 1
36 . 6 PHE HE1 H 7.36 0.02 1
37 . 6 PHE HE2 H 7.36 0.02 1
38 . 6 PHE HZ H 7.44 0.02 1
39 . 7 SER H H 7.96 0.02 1
40 . 7 SER HA H 4.48 0.02 1
41 . 7 SER HB2 H 3.93 0.02 1
42 . 7 SER HB3 H 3.93 0.02 1
43 . 8 CYS H H 7.48 0.02 1
44 . 8 CYS HA H 5.27 0.02 1
45 . 8 CYS HB2 H 2.57 0.02 2
46 . 8 CYS HB3 H 3.61 0.02 2
47 . 9 GLU H H 9.29 0.02 1
48 . 9 GLU HA H 4.57 0.02 1
49 . 9 GLU HB2 H 2.20 0.02 1
50 . 9 GLU HB3 H 2.20 0.02 1
51 . 9 GLU HG2 H 2.31 0.02 1
52 . 9 GLU HG3 H 2.31 0.02 1
53 . 10 ILE H H 8.09 0.02 1
54 . 10 ILE HA H 4.24 0.02 1
55 . 10 ILE HB H 2.01 0.02 1
56 . 10 ILE HG12 H 1.22 0.02 2
57 . 10 ILE HG13 H 1.55 0.02 2
58 . 10 ILE HG2 H 1.03 0.02 1
59 . 10 ILE HD1 H 0.91 0.02 1
60 . 11 GLU H H 8.44 0.02 1
61 . 11 GLU HA H 4.47 0.02 1
62 . 11 GLU HB2 H 1.88 0.02 2
63 . 11 GLU HB3 H 2.79 0.02 2
64 . 11 GLU HG2 H 2.03 0.02 2
65 . 11 GLU HG3 H 2.39 0.02 2
66 . 12 LYS H H 7.80 0.02 1
67 . 12 LYS HA H 4.92 0.02 1
68 . 12 LYS HB2 H 1.55 0.02 2
69 . 12 LYS HB3 H 1.64 0.02 2
70 . 12 LYS HG2 H 1.09 0.02 2
71 . 12 LYS HG3 H 1.18 0.02 2
72 . 12 LYS HD2 H 1.56 0.02 1
73 . 12 LYS HD3 H 1.56 0.02 1
74 . 12 LYS HE2 H 2.84 0.02 1
75 . 12 LYS HE3 H 2.84 0.02 1
76 . 13 GLU H H 8.45 0.02 1
77 . 13 GLU HA H 4.49 0.02 1
78 . 13 GLU HB2 H 2.07 0.02 1
79 . 13 GLU HB3 H 2.07 0.02 1
80 . 13 GLU HG2 H 2.34 0.02 1
81 . 13 GLU HG3 H 2.34 0.02 1
82 . 14 GLY H H 9.20 0.02 1
83 . 14 GLY HA2 H 3.79 0.02 2
84 . 14 GLY HA3 H 3.98 0.02 2
85 . 15 ASP H H 8.80 0.02 1
86 . 15 ASP HA H 4.52 0.02 1
87 . 15 ASP HB2 H 2.76 0.02 2
88 . 15 ASP HB3 H 2.87 0.02 2
89 . 16 LYS H H 7.88 0.02 1
90 . 16 LYS HA H 4.94 0.02 1
91 . 16 LYS HB2 H 1.94 0.02 1
92 . 16 LYS HB3 H 1.94 0.02 1
93 . 16 LYS HG2 H 1.51 0.02 2
94 . 16 LYS HG3 H 1.58 0.02 2
95 . 16 LYS HD2 H 1.77 0.02 1
96 . 16 LYS HD3 H 1.77 0.02 1
97 . 16 LYS HE2 H 3.08 0.02 1
98 . 16 LYS HE3 H 3.08 0.02 1
99 . 17 PRO HA H 4.92 0.02 1
100 . 17 PRO HB2 H 1.90 0.02 2
101 . 17 PRO HB3 H 2.40 0.02 2
102 . 17 PRO HG2 H 2.00 0.02 2
103 . 17 PRO HG3 H 2.12 0.02 2
104 . 17 PRO HD2 H 3.77 0.02 2
105 . 17 PRO HD3 H 3.98 0.02 2
106 . 18 CYS H H 7.96 0.02 1
107 . 18 CYS HA H 4.65 0.02 1
108 . 18 CYS HB2 H 3.02 0.02 2
109 . 18 CYS HB3 H 3.06 0.02 2
110 . 19 LYS H H 8.50 0.02 1
111 . 19 LYS HA H 4.46 0.02 1
112 . 19 LYS HB2 H 1.49 0.02 2
113 . 19 LYS HB3 H 1.61 0.02 2
114 . 19 LYS HG2 H 1.38 0.02 2
115 . 19 LYS HG3 H 1.68 0.02 2
116 . 19 LYS HD2 H 1.49 0.02 1
117 . 19 LYS HD3 H 1.49 0.02 1
118 . 19 LYS HE2 H 2.95 0.02 1
119 . 19 LYS HE3 H 2.95 0.02 1
120 . 20 LYS H H 8.93 0.02 1
121 . 20 LYS HA H 3.72 0.02 1
122 . 20 LYS HB2 H 1.44 0.02 1
123 . 20 LYS HB3 H 1.44 0.02 1
124 . 20 LYS HG2 H 1.22 0.02 2
125 . 20 LYS HG3 H 1.31 0.02 2
126 . 20 LYS HD2 H 1.60 0.02 1
127 . 20 LYS HD3 H 1.60 0.02 1
128 . 20 LYS HE2 H 2.94 0.02 1
129 . 20 LYS HE3 H 2.94 0.02 1
130 . 21 LYS H H 8.43 0.02 1
131 . 21 LYS HA H 4.06 0.02 1
132 . 21 LYS HB2 H 1.26 0.02 2
133 . 21 LYS HB3 H 1.41 0.02 2
134 . 21 LYS HG2 H 1.01 0.02 2
135 . 21 LYS HG3 H 1.08 0.02 2
136 . 21 LYS HD2 H 1.30 0.02 2
137 . 21 LYS HD3 H 1.38 0.02 2
138 . 21 LYS HE2 H 2.88 0.02 1
139 . 21 LYS HE3 H 2.88 0.02 1
140 . 22 LYS H H 8.24 0.02 1
141 . 22 LYS HA H 4.34 0.02 1
142 . 22 LYS HB2 H 1.69 0.02 2
143 . 22 LYS HB3 H 1.75 0.02 2
144 . 22 LYS HG2 H 1.42 0.02 2
145 . 22 LYS HG3 H 1.52 0.02 2
146 . 22 LYS HD2 H 1.69 0.02 1
147 . 22 LYS HD3 H 1.69 0.02 1
148 . 22 LYS HE2 H 3.04 0.02 1
149 . 22 LYS HE3 H 3.04 0.02 1
150 . 23 CYS H H 8.89 0.02 1
151 . 23 CYS HA H 4.66 0.02 1
152 . 23 CYS HB2 H 2.55 0.02 2
153 . 23 CYS HB3 H 3.10 0.02 2
154 . 24 LYS H H 8.56 0.02 1
155 . 24 LYS HA H 4.18 0.02 1
156 . 24 LYS HB2 H 1.38 0.02 2
157 . 24 LYS HB3 H 1.72 0.02 2
158 . 24 LYS HG2 H 1.30 0.02 1
159 . 24 LYS HG3 H 1.30 0.02 1
160 . 24 LYS HD2 H 1.36 0.02 2
161 . 24 LYS HD3 H 1.44 0.02 2
162 . 24 LYS HE2 H 2.71 0.02 1
163 . 24 LYS HE3 H 2.71 0.02 1
164 . 25 GLY H H 8.50 0.02 1
165 . 25 GLY HA2 H 3.84 0.02 2
166 . 25 GLY HA3 H 4.05 0.02 2
167 . 26 GLY H H 8.96 0.02 1
168 . 26 GLY HA2 H 3.70 0.02 2
169 . 26 GLY HA3 H 4.43 0.02 2
170 . 27 TRP H H 8.74 0.02 1
171 . 27 TRP HA H 5.27 0.02 1
172 . 27 TRP HB2 H 2.96 0.02 2
173 . 27 TRP HB3 H 3.55 0.02 2
174 . 27 TRP HD1 H 7.13 0.02 1
175 . 27 TRP HE1 H 10.38 0.02 1
176 . 27 TRP HE3 H 7.15 0.02 1
177 . 27 TRP HZ2 H 7.52 0.02 1
178 . 27 TRP HZ3 H 7.17 0.02 1
179 . 27 TRP HH2 H 7.27 0.02 1
180 . 28 LYS H H 9.69 0.02 1
181 . 28 LYS HA H 4.75 0.02 1
182 . 28 LYS HB2 H 1.66 0.02 2
183 . 28 LYS HB3 H 1.72 0.02 2
184 . 28 LYS HG2 H 1.28 0.02 2
185 . 28 LYS HG3 H 1.34 0.02 2
186 . 28 LYS HD2 H 1.64 0.02 1
187 . 28 LYS HD3 H 1.64 0.02 1
188 . 28 LYS HE2 H 2.91 0.02 1
189 . 28 LYS HE3 H 2.91 0.02 1
190 . 29 CYS H H 8.90 0.02 1
191 . 29 CYS HA H 5.07 0.02 1
192 . 29 CYS HB2 H 3.01 0.02 2
193 . 29 CYS HB3 H 3.10 0.02 2
194 . 30 LYS H H 9.68 0.02 1
195 . 30 LYS HA H 4.41 0.02 1
196 . 30 LYS HB2 H 1.52 0.02 2
197 . 30 LYS HB3 H 1.66 0.02 2
198 . 30 LYS HG2 H 1.01 0.02 2
199 . 30 LYS HG3 H 1.14 0.02 2
200 . 30 LYS HD2 H 1.54 0.02 1
201 . 30 LYS HD3 H 1.54 0.02 1
202 . 30 LYS HE2 H 2.76 0.02 1
203 . 30 LYS HE3 H 2.76 0.02 1
204 . 31 PHE H H 9.10 0.02 1
205 . 31 PHE HA H 4.34 0.02 1
206 . 31 PHE HB2 H 3.26 0.02 2
207 . 31 PHE HB3 H 3.32 0.02 2
208 . 31 PHE HD1 H 7.30 0.02 1
209 . 31 PHE HD2 H 7.30 0.02 1
210 . 31 PHE HE1 H 7.41 0.02 1
211 . 31 PHE HE2 H 7.41 0.02 1
212 . 31 PHE HZ H 7.35 0.02 1
213 . 32 ASN H H 8.76 0.02 1
214 . 32 ASN HA H 4.29 0.02 1
215 . 32 ASN HB2 H 2.56 0.02 2
216 . 32 ASN HB3 H 3.65 0.02 2
217 . 32 ASN HD21 H 7.29 0.02 2
218 . 32 ASN HD22 H 7.89 0.02 2
219 . 33 MET H H 7.90 0.02 1
220 . 33 MET HA H 5.06 0.02 1
221 . 33 MET HB2 H 2.13 0.02 1
222 . 33 MET HB3 H 2.13 0.02 1
223 . 33 MET HG2 H 2.68 0.02 2
224 . 33 MET HG3 H 2.76 0.02 2
225 . 33 MET HE H 2.16 0.02 1
226 . 34 CYS H H 9.27 0.02 1
227 . 34 CYS HA H 5.37 0.02 1
228 . 34 CYS HB2 H 2.91 0.02 2
229 . 34 CYS HB3 H 3.04 0.02 2
230 . 35 VAL H H 9.87 0.02 1
231 . 35 VAL HA H 4.80 0.02 1
232 . 35 VAL HB H 2.18 0.02 1
233 . 35 VAL HG1 H 1.00 0.02 2
234 . 35 VAL HG2 H 1.07 0.02 2
235 . 36 LYS H H 8.13 0.02 1
236 . 36 LYS HA H 3.30 0.02 1
237 . 36 LYS HB2 H 0.40 0.02 2
238 . 36 LYS HB3 H 1.23 0.02 2
239 . 36 LYS HG2 H 0.54 0.02 2
240 . 36 LYS HG3 H 0.74 0.02 2
241 . 36 LYS HD2 H 1.15 0.02 1
242 . 36 LYS HD3 H 1.15 0.02 1
243 . 36 LYS HE2 H 2.79 0.02 1
244 . 36 LYS HE3 H 2.79 0.02 1
245 . 37 VAL H H 7.58 0.02 1
246 . 37 VAL HA H 3.82 0.02 1
247 . 37 VAL HB H 1.96 0.02 1
248 . 37 VAL HG1 H 0.76 0.02 2
249 . 37 VAL HG2 H 0.85 0.02 2
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