data_4966
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H and 13C Chemical Shift Assignments for Cardiotoxin A3 from Naja Atra at
Neutral pH
;
_BMRB_accession_number 4966
_BMRB_flat_file_name bmr4966.str
_Entry_type original
_Submission_date 2001-03-06
_Accession_date 2001-03-06
_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 Sue Shih-Che . .
2 Jarrell Harold C. .
3 Brisson Jean-Robert . .
4 Wu Wen-guey . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 366
"13C chemical shifts" 59
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-03-09 original BMRB .
stop_
_Original_release_date 2001-03-06
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Dynamic Characterization of the Water binding loop in the P-type Cardiotoxin:
Implication for the role of the bound Water Molecule
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 21526408
_PubMed_ID 11669614
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Sue Shih-Che . .
2 Jarrell Harold C. .
3 Brisson Jean-Robert . .
4 Wu Wen-guey . .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 40
_Journal_issue 43
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 12782
_Page_last 12794
_Year 2001
_Details
;
This paper describes a comprehensive NMR analysis of the structure and
dynamics of P-type cardiotoxin and its bound water by using triple-quantum
17O NMR, NOE/ROE 2D NMR, and 13C T1 relaxation.
;
loop_
_Keyword
'13C relaxation'
'17O NMR'
Cardiotoxin
'bound water molecule'
'order parameter'
'residence time'
'triple-quantum filtered'
'water binding loop'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Bhaskaran R, Huang CC, Chang DK, Yu C.
Cardiotoxin III from the Taiwan cobra (Naja naja atra). Determination
of structure in solution and comparison with short neurotoxins.
J Mol Biol. 1994 Jan 28;235(4):1291-301.
;
_Citation_title
;
Cardiotoxin III from the Taiwan cobra (Naja naja atra). Determination of structure in solution and comparison with short neurotoxins.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8308891
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Bhaskaran R . .
2 Huang 'C C' C. .
3 Chang 'D K' K. .
4 Yu C . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of molecular biology'
_Journal_volume 235
_Journal_issue 4
_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 1291
_Page_last 1301
_Year 1994
_Details
;
The structure in solution of cardiotoxin III, a membrane toxin purified from the
venom of the Taiwan cobra, Naja naja atra, is reported. Sequence-specific
assignment of 1H-NMR lines was completed and the NMR data show the presence of
a triple and a double-stranded antiparallel beta-sheet. Many NOE cross peaks
identified in NOESY spectra were applied as distance constraints based on a
hybrid distance geometry/dynamical simulated annealing technique; 20 structures
were found within a single family. The average value of atomic RMS differences
between the 20 structures and their geometric mean is 0.087 nm for the backbone
atoms and 0.152 nm for all heavy atoms; they are 0.055 nm and 0.12 nm,
respectively for the segments of secondary structure. In these selected
structures the backbone of the polypeptide chain folds such that five strands
emerge from a globular head. Three major loops link these strands to form a
double and a triple-stranded antiparallel beta-sheet. Comparison of the
structures of the toxin in solution with the X-ray crystal structure of its
homologous protein, cardiotoxin V4II from Naja mossambica mossambica, showed
good agreement between the structures except at segments of the turns. As the
functions of short neurotoxins and cardiotoxins are distinct, despite their
similar secondary structural patterns and tertiary folding, a comparative
analysis has been carried out between cardiotoxin III and short neurotoxins of
known structures. We discuss their structural features in order to clarify
relationships between their structure and function.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full
;
Chiang CM, Chang SL, Lin HJ, Wu WG.
The role of acidic amino acid residues in the structural stability of snake
cardiotoxins.
Biochemistry. 1996 Jul 16;35(28):9177-86.
;
_Citation_title
;
The role of acidic amino acid residues in the structural stability of snake cardiotoxins.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8703923
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Chiang 'C M' M. .
2 Chang 'S L' L. .
3 Lin 'H J' J. .
4 Wu 'W G' G. .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 35
_Journal_issue 28
_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 9177
_Page_last 9186
_Year 1996
_Details
;
We have recently shown that membrane-related activities of cardiotoxin V from
Naja naja atra (CTX A5) are diminished at acidic pH although the overall
beta-sheet structure of the molecule is maintained. In order to understand more
about the mechanism of inactivation of CTX at acidic pH, we studied the effect
of pH and denaturing reagents on the structural stability of CTX. We found,
first, pH-induced structural transitions occurred in CTX A5 at two pH values as
judged by the CD ellipticity around 195 nm: an increase in the beta-sheet
content occurred around pH 4 and followed by a decrease, therein, around pH 2.
The pKa of three acidic amino acid residues in CTX A5, i.e., Glu-17, Asp-42,
and Asp-59, were determined to be 4.0, 3.2, and below 2.3, respectively, by NMR
spectroscopy. The low pKa value of Asp-59 implies salt bridge formation between
Lys-2 and Asp-59. Thus, electrostatic interaction may stabilize the three loop
structure in addition to the hydrogen bonds between N- and C-termini of CTX
molecule. Second, 2,2,2-trifluoroethanol (TFE) and guanidinium chloride
(GdmHCI) were found to induce alpha-helical and random coil formation,
respectively, in CTX A5 and eight other beta-sheet CTXs. Comparison of the
relative potencies of TFE and GdmHCI to induce structural changes suggests that
the amino acid residue located at position 17 plays a role in the structural
stability. Specifically, CTXs containing negatively charged Glu-17 are least
stable. It is suggested that Glu-17 may perturb the interaction between Lys-2
and Asp-59, and thus the overall stability of beta-sheet, in the presence of
denaturing reagent. In conclusion, the perturbed structural stability of CTXs
may partially explain the lower activity CTX exhibits at acidic pH. A
structural model to account for the unfolding and refolding of CTX molecules
without the breaking of disulfide bonds is also proposed.
;
save_
##################################
# Molecular system description #
##################################
save_system_CTX_A3
_Saveframe_category molecular_system
_Mol_system_name 'Cardiotoxin A3'
_Abbreviation_common 'CTX A3'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'cardiotoxin A3' $CTX_A3
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
loop_
_Biological_function
'depolarization of muscular cell'
hemolysis
'heparin binding protien'
'membrane binding protein'
'protein with one bound water'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_CTX_A3
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Cardiotoxin A3'
_Abbreviation_common 'CTX A3'
_Molecular_mass 6741
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 60
_Mol_residue_sequence
;
LKCNKLVPLFYKTCPAGKNL
CYKMFMVATPKVPVKRGCID
VCPKSSLLVKYVCCNTDRCN
;
loop_
_Residue_seq_code
_Residue_label
1 LEU 2 LYS 3 CYS 4 ASN 5 LYS
6 LEU 7 VAL 8 PRO 9 LEU 10 PHE
11 TYR 12 LYS 13 THR 14 CYS 15 PRO
16 ALA 17 GLY 18 LYS 19 ASN 20 LEU
21 CYS 22 TYR 23 LYS 24 MET 25 PHE
26 MET 27 VAL 28 ALA 29 THR 30 PRO
31 LYS 32 VAL 33 PRO 34 VAL 35 LYS
36 ARG 37 GLY 38 CYS 39 ILE 40 ASP
41 VAL 42 CYS 43 PRO 44 LYS 45 SER
46 SER 47 LEU 48 LEU 49 VAL 50 LYS
51 TYR 52 VAL 53 CYS 54 CYS 55 ASN
56 THR 57 ASP 58 ARG 59 CYS 60 ASN
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
BMRB 15305 cardiotoxin_A3 100.00 60 100.00 100.00 9.64e-26
PDB 1H0J 'Structural Basis Of The Membrane-Induced Cardiotoxin A3 Oligomerization' 100.00 60 100.00 100.00 9.64e-26
PDB 1I02 'Nmr Structure Of Ctx A3 At Neutral Ph (20 Structures)' 100.00 60 100.00 100.00 9.64e-26
PDB 1XT3 'Structure Basis Of Venom Citrate-Dependent Heparin Sulfate- Mediated Cell Surface Retention Of Cobra Cardiotoxin A3' 100.00 60 100.00 100.00 9.64e-26
PDB 2BHI 'Crystal Structure Of Taiwan Cobra Cardiotoxin A3 Complexed With Sulfogalactoceramide' 100.00 60 100.00 100.00 9.64e-26
PDB 2CRS 'Cardiotoxin Iii From Taiwan Cobra (Naja Naja Atra) Determination Of Structure In Solution And Comparison With Short Neurotoxins' 100.00 60 100.00 100.00 9.64e-26
PDB 2CRT 'Cardiotoxin Iii From Taiwan Cobra (Naja Naja Atra) Determination Of Structure In Solution And Comparison With Short Neurotoxins' 100.00 60 100.00 100.00 9.64e-26
EMBL CAA07686 'cardiotoxin 3 precursor protein [Naja atra]' 100.00 81 100.00 100.00 3.15e-26
EMBL CAA90963 'cardiotoxin 3 [Naja naja]' 100.00 81 98.33 98.33 3.32e-25
EMBL CAB42053 'cardiotoxin-31 [Naja atra]' 100.00 81 98.33 100.00 9.41e-26
EMBL CAB42055 'cardiotoxin-3 [Naja atra]' 100.00 81 100.00 100.00 2.54e-26
GenBank AAA49386 cardiotoxin 100.00 81 100.00 100.00 2.37e-26
GenBank AAB01541 'cardiotoxin III' 100.00 81 100.00 100.00 3.15e-26
GenBank AAB18382 "cardiotoxin 3' [Naja atra]" 100.00 81 100.00 100.00 3.15e-26
GenBank AAB18383 'cardiotoxin 3a [Naja atra]' 100.00 81 98.33 100.00 9.41e-26
GenBank AAB25733 'cardiotoxin isoform 3, cytotoxin isoform 3, CTX-3 [Naja naja=Formosan cobra, ssp. atra, venom, Peptide, 60 aa]' 100.00 60 100.00 100.00 9.64e-26
PIR JK0222 'cytotoxin 10 - monocled cobra' 100.00 60 100.00 100.00 9.64e-26
PRF 0406231A toxin,cardio 100.00 60 100.00 100.00 9.64e-26
PRF 2207174B cardiotoxin:ISOTYPE=III 100.00 81 98.33 98.33 3.32e-25
SWISS-PROT O93471 'Cardiotoxin-1 precursor (CTX-1) (Ctx1)' 100.00 81 98.33 100.00 8.23e-26
SWISS-PROT O93473 'Cardiotoxin-4a precursor (CTX-4a) (Ctx4a)' 100.00 81 98.33 98.33 1.16e-25
SWISS-PROT P60301 'Cardiotoxin-A3 precursor (CTX-A3) (Cardiotoxin 3) (CTX-3) (Cardiotoxin analog III) (CTX III) (Cytotoxin-3)' 100.00 81 100.00 100.00 3.15e-26
SWISS-PROT P60302 'Cardiotoxin-3 precursor (CTX-3) (Ctx3)' 100.00 81 100.00 100.00 3.15e-26
SWISS-PROT P60303 'Cytotoxin-4 precursor (Cytotoxin IV)' 100.00 81 100.00 100.00 3.15e-26
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Secretion
_Details
$CTX_A3 'Taiwan cobra' 8656 Eukaryota Metazoa cobra 'naja atra' venom
;
Cobra Venom were purchased from Sigma. Further purification by open column and
HPLC was proceeded to get pure cardiotoxin A3 compound.
;
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
_Details
$CTX_A3 'purified from the natural source' . . . . . 'purified from cobra venom'
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details '10mM phosphate buffer was added to maintain the pH value at 6.0.'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$CTX_A3 5 mM .
'phosphate buffer' 10 mM .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name XWINNMR
_Version 2.01
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer BRUKER
_Model DRX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer BRUKER
_Model DMX
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_COSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name COSY
_Sample_label .
save_
save_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_Sample_label .
save_
save_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TOCSY
_Sample_label .
save_
save_HSQC_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HSQC
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_CTX_A3_condition
_Saveframe_category sample_conditions
_Details
;
There is no indication of protein aggregation or degradation
as judged by the 1H NMR spectral quailty during the experimental
(25C, up to week) and storage time (4C, up to months). The
assignments of 13C have been collected from the natural abundance
nucleii.
;
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 0.03 0.005 M
pH 5.96 0.05 n/a
pressure 1.013 . atm
temperature 300 0.5 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 . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
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
;
The chemical Shift of Cardiotoxin A3 at pH 3.0 have been determinted in 1994.
But it was later demonstrated that the assignments were based on at least 9
wrongly assigned signals out of the 60 amino acid residues.
The correct assignment of all proton resonance were achieved now at pH 6.0
and 27C.
;
loop_
_Experiment_label
COSY
NOESY
TOCSY
HSQC
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $CTX_A3_condition
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'cardiotoxin A3'
_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 4.175 0.01 1
2 . 1 LEU HB2 H 1.595 0.01 1
3 . 1 LEU HB3 H 1.536 0.01 1
4 . 1 LEU HG H 1.580 0.01 1
5 . 1 LEU HD1 H 0.844 0.01 2
6 . 1 LEU HD2 H 0.777 0.01 2
7 . 1 LEU CA C 52.260 0.15 1
8 . 2 LYS H H 8.638 0.01 1
9 . 2 LYS HA H 5.483 0.01 1
10 . 2 LYS HB2 H 1.417 0.01 1
11 . 2 LYS HB3 H 1.417 0.01 1
12 . 2 LYS HG2 H 1.255 0.01 1
13 . 2 LYS HG3 H 1.255 0.01 1
14 . 2 LYS HE2 H 2.864 0.01 1
15 . 2 LYS HE3 H 2.864 0.01 1
16 . 2 LYS CA C 51.867 0.15 1
17 . 3 CYS H H 8.861 0.01 1
18 . 3 CYS HA H 5.164 0.01 1
19 . 3 CYS HB2 H 2.867 0.01 2
20 . 3 CYS HB3 H 2.470 0.01 2
21 . 3 CYS CA C 49.495 0.15 1
22 . 4 ASN H H 9.676 0.01 1
23 . 4 ASN HA H 5.077 0.01 1
24 . 4 ASN HB2 H 2.771 0.01 2
25 . 4 ASN HB3 H 2.325 0.01 2
26 . 4 ASN HD21 H 7.711 0.01 2
27 . 4 ASN HD22 H 6.557 0.01 2
28 . 4 ASN CA C 52.225 0.15 1
29 . 5 LYS H H 8.009 0.01 1
30 . 5 LYS HA H 4.266 0.01 1
31 . 5 LYS HB2 H 1.620 0.01 1
32 . 5 LYS HB3 H 1.620 0.01 1
33 . 5 LYS HG2 H 1.401 0.01 2
34 . 5 LYS HG3 H 1.261 0.01 2
35 . 5 LYS HD2 H 2.206 0.01 1
36 . 5 LYS HD3 H 2.206 0.01 1
37 . 5 LYS HE2 H 2.919 0.01 1
38 . 5 LYS HE3 H 2.919 0.01 1
39 . 5 LYS CA C 52.828 0.15 1
40 . 6 LEU H H 8.338 0.01 1
41 . 6 LEU HA H 3.677 0.01 1
42 . 6 LEU HB2 H 1.672 0.01 2
43 . 6 LEU HB3 H 1.597 0.01 2
44 . 6 LEU HG H 1.828 0.01 1
45 . 6 LEU HD1 H 0.876 0.01 1
46 . 6 LEU HD2 H 0.720 0.01 1
47 . 6 LEU CA C 56.869 0.15 1
48 . 7 VAL H H 7.654 0.01 1
49 . 7 VAL HA H 4.422 0.01 1
50 . 7 VAL HB H 2.276 0.01 1
51 . 7 VAL HG1 H 1.053 0.01 1
52 . 7 VAL HG2 H 1.053 0.01 1
53 . 7 VAL CA C 57.482 0.15 1
54 . 8 PRO HA H 4.544 0.01 1
55 . 8 PRO HB2 H 2.173 0.01 2
56 . 8 PRO HB3 H 1.984 0.01 2
57 . 8 PRO HG2 H 1.842 0.01 1
58 . 8 PRO HG3 H 1.842 0.01 1
59 . 8 PRO HD2 H 4.052 0.01 2
60 . 8 PRO HD3 H 3.845 0.01 2
61 . 8 PRO CA C 63.358 0.15 1
62 . 9 LEU H H 6.625 0.01 1
63 . 9 LEU HA H 3.959 0.01 1
64 . 9 LEU HB2 H 1.033 0.01 1
65 . 9 LEU HB3 H 1.033 0.01 1
66 . 9 LEU HG H 1.333 0.01 1
67 . 9 LEU HD1 H 0.757 0.01 2
68 . 9 LEU HD2 H 0.719 0.01 2
69 . 9 LEU CA C 54.089 0.15 1
70 . 10 PHE H H 8.139 0.01 1
71 . 10 PHE HA H 4.858 0.01 1
72 . 10 PHE HB2 H 3.228 0.01 2
73 . 10 PHE HB3 H 2.858 0.01 2
74 . 10 PHE HD1 H 7.289 0.01 1
75 . 10 PHE HD2 H 7.289 0.01 1
76 . 10 PHE HE1 H 7.352 0.01 1
77 . 10 PHE HE2 H 7.352 0.01 1
78 . 10 PHE HZ H 7.324 0.01 1
79 . 10 PHE CA C 53.465 0.15 1
80 . 11 TYR H H 8.206 0.01 1
81 . 11 TYR HA H 5.443 0.01 1
82 . 11 TYR HB2 H 2.928 0.01 2
83 . 11 TYR HB3 H 2.686 0.01 2
84 . 11 TYR HD1 H 6.750 0.01 1
85 . 11 TYR HD2 H 6.750 0.01 1
86 . 11 TYR HE1 H 6.806 0.01 1
87 . 11 TYR HE2 H 6.806 0.01 1
88 . 11 TYR CA C 53.309 0.15 1
89 . 12 LYS H H 9.085 0.01 1
90 . 12 LYS HA H 4.829 0.01 1
91 . 12 LYS HB2 H 1.707 0.01 1
92 . 12 LYS HB3 H 1.707 0.01 1
93 . 12 LYS HG2 H 1.384 0.01 2
94 . 12 LYS HG3 H 1.196 0.01 2
95 . 12 LYS HD2 H 1.859 0.01 1
96 . 12 LYS HD3 H 1.859 0.01 1
97 . 12 LYS CA C 51.549 0.15 1
98 . 13 THR H H 8.869 0.01 1
99 . 13 THR HA H 4.712 0.01 1
100 . 13 THR HB H 4.072 0.01 1
101 . 13 THR HG2 H 1.277 0.01 1
102 . 13 THR CA C 60.720 0.15 1
103 . 14 CYS H H 9.179 0.01 1
104 . 14 CYS HA H 4.995 0.01 1
105 . 14 CYS HB2 H 3.549 0.01 2
106 . 14 CYS HB3 H 2.835 0.01 2
107 . 14 CYS CA C 49.552 0.15 1
108 . 15 PRO HA H 4.635 0.01 1
109 . 15 PRO HB2 H 2.419 0.01 2
110 . 15 PRO HB3 H 2.194 0.01 2
111 . 15 PRO HG2 H 1.982 0.01 2
112 . 15 PRO HG3 H 1.903 0.01 2
113 . 15 PRO HD2 H 3.458 0.01 2
114 . 15 PRO HD3 H 4.106 0.01 2
115 . 15 PRO CA C 59.919 0.15 1
116 . 16 ALA H H 8.473 0.01 1
117 . 16 ALA HA H 4.121 0.01 1
118 . 16 ALA HB H 1.380 0.01 1
119 . 16 ALA CA C 51.467 0.15 1
120 . 17 GLY H H 8.799 0.01 1
121 . 17 GLY HA2 H 4.272 0.01 2
122 . 17 GLY HA3 H 3.675 0.01 2
123 . 17 GLY CA C 42.586 0.15 1
124 . 18 LYS H H 7.589 0.01 1
125 . 18 LYS HA H 4.288 0.01 1
126 . 18 LYS HB2 H 1.381 0.01 1
127 . 18 LYS HB3 H 1.381 0.01 1
128 . 18 LYS HG2 H 1.060 0.01 1
129 . 18 LYS HG3 H 1.060 0.01 1
130 . 18 LYS HD2 H 1.919 0.01 1
131 . 18 LYS HD3 H 1.919 0.01 1
132 . 18 LYS HE2 H 2.958 0.01 1
133 . 18 LYS HE3 H 2.958 0.01 1
134 . 18 LYS CA C 53.416 0.15 1
135 . 19 ASN H H 7.946 0.01 1
136 . 19 ASN HA H 4.958 0.01 1
137 . 19 ASN HB2 H 3.029 0.01 2
138 . 19 ASN HB3 H 2.647 0.01 2
139 . 19 ASN HD21 H 7.522 0.01 2
140 . 19 ASN HD22 H 6.986 0.01 2
141 . 19 ASN CA C 50.709 0.15 1
142 . 20 LEU H H 8.225 0.01 1
143 . 20 LEU HA H 4.852 0.01 1
144 . 20 LEU HB2 H 1.712 0.01 2
145 . 20 LEU HB3 H 1.527 0.01 2
146 . 20 LEU HG H 1.378 0.01 1
147 . 20 LEU HD1 H 0.880 0.01 2
148 . 20 LEU HD2 H 0.736 0.01 2
149 . 21 CYS H H 9.050 0.01 1
150 . 21 CYS HA H 6.133 0.01 1
151 . 21 CYS HB2 H 3.054 0.01 2
152 . 21 CYS HB3 H 2.982 0.01 2
153 . 21 CYS CA C 49.516 0.15 1
154 . 22 TYR H H 8.960 0.01 1
155 . 22 TYR HA H 6.099 0.01 1
156 . 22 TYR HB2 H 3.114 0.01 2
157 . 22 TYR HB3 H 2.947 0.01 2
158 . 22 TYR HD1 H 6.624 0.01 1
159 . 22 TYR HD2 H 6.624 0.01 1
160 . 22 TYR HE1 H 6.733 0.01 1
161 . 22 TYR HE2 H 6.733 0.01 1
162 . 22 TYR CA C 53.829 0.15 1
163 . 23 LYS H H 9.080 0.01 1
164 . 23 LYS HA H 4.948 0.01 1
165 . 23 LYS HB2 H 1.710 0.01 1
166 . 23 LYS HB3 H 1.710 0.01 1
167 . 23 LYS HG2 H 1.512 0.01 1
168 . 23 LYS HG3 H 1.512 0.01 1
169 . 23 LYS HD2 H 1.854 0.01 1
170 . 23 LYS HD3 H 1.854 0.01 1
171 . 23 LYS CA C 52.981 0.15 1
172 . 24 MET H H 8.460 0.01 1
173 . 24 MET HA H 5.229 0.01 1
174 . 24 MET HB2 H 1.798 0.01 2
175 . 24 MET HB3 H 1.621 0.01 2
176 . 24 MET HG2 H 1.346 0.01 1
177 . 24 MET HG3 H 1.346 0.01 1
178 . 24 MET CA C 51.324 0.15 1
179 . 25 PHE H H 9.095 0.01 1
180 . 25 PHE HA H 4.943 0.01 1
181 . 25 PHE HB2 H 2.902 0.01 1
182 . 25 PHE HB3 H 2.902 0.01 1
183 . 25 PHE HD1 H 6.907 0.01 1
184 . 25 PHE HD2 H 6.907 0.01 1
185 . 25 PHE HE1 H 7.108 0.01 1
186 . 25 PHE HE2 H 7.108 0.01 1
187 . 25 PHE HZ H 7.236 0.01 1
188 . 25 PHE CA C 53.575 0.15 1
189 . 26 MET H H 9.432 0.01 1
190 . 26 MET HA H 5.106 0.01 1
191 . 26 MET HB2 H 2.273 0.01 2
192 . 26 MET HB3 H 2.134 0.01 2
193 . 26 MET HG2 H 2.838 0.01 2
194 . 26 MET HG3 H 2.624 0.01 2
195 . 26 MET CA C 51.379 0.15 1
196 . 27 VAL H H 8.149 0.01 1
197 . 27 VAL HA H 3.546 0.01 1
198 . 27 VAL HB H 1.942 0.01 1
199 . 27 VAL HG1 H 0.981 0.01 2
200 . 27 VAL HG2 H 0.903 0.01 2
201 . 27 VAL CA C 63.763 0.15 1
202 . 28 ALA H H 8.470 0.01 1
203 . 28 ALA HA H 4.238 0.01 1
204 . 28 ALA HB H 1.491 0.01 1
205 . 28 ALA CA C 51.723 0.15 1
206 . 29 THR H H 7.425 0.01 1
207 . 29 THR HA H 4.824 0.01 1
208 . 29 THR HB H 4.310 0.01 1
209 . 29 THR HG2 H 1.199 0.01 1
210 . 29 THR CA C 55.557 0.15 1
211 . 30 PRO HA H 4.278 0.01 1
212 . 30 PRO HB2 H 2.043 0.01 1
213 . 30 PRO HB3 H 2.043 0.01 1
214 . 30 PRO HG2 H 1.748 0.01 1
215 . 30 PRO HG3 H 1.748 0.01 1
216 . 30 PRO HD2 H 3.580 0.01 1
217 . 30 PRO HD3 H 3.580 0.01 1
218 . 30 PRO CA C 62.313 0.15 1
219 . 31 LYS H H 8.306 0.01 1
220 . 31 LYS HA H 4.110 0.01 1
221 . 31 LYS HB2 H 1.960 0.01 2
222 . 31 LYS HB3 H 1.823 0.01 2
223 . 31 LYS HG2 H 1.638 0.01 1
224 . 31 LYS HG3 H 1.638 0.01 1
225 . 31 LYS HD2 H 1.429 0.01 2
226 . 31 LYS HD3 H 1.335 0.01 2
227 . 31 LYS CA C 55.167 0.15 1
228 . 32 VAL H H 7.565 0.01 1
229 . 32 VAL HA H 4.638 0.01 1
230 . 32 VAL HB H 2.162 0.01 1
231 . 32 VAL HG1 H 0.978 0.01 2
232 . 32 VAL HG2 H 0.920 0.01 2
233 . 32 VAL CA C 56.863 0.15 1
234 . 33 PRO HA H 4.331 0.01 1
235 . 33 PRO HB2 H 2.037 0.01 2
236 . 33 PRO HB3 H 1.795 0.01 2
237 . 33 PRO HG2 H 1.673 0.01 1
238 . 33 PRO HG3 H 1.673 0.01 1
239 . 33 PRO HD2 H 3.934 0.01 2
240 . 33 PRO HD3 H 3.836 0.01 2
241 . 33 PRO CA C 60.743 0.15 1
242 . 34 VAL H H 8.868 0.01 1
243 . 34 VAL HA H 4.309 0.01 1
244 . 34 VAL HB H 2.139 0.01 1
245 . 34 VAL HG1 H 1.050 0.01 2
246 . 34 VAL HG2 H 0.961 0.01 2
247 . 34 VAL CA C 59.892 0.15 1
248 . 35 LYS H H 7.389 0.01 1
249 . 35 LYS HA H 4.629 0.01 1
250 . 35 LYS HB2 H 1.716 0.01 2
251 . 35 LYS HB3 H 1.578 0.01 2
252 . 35 LYS HG2 H 1.853 0.01 1
253 . 35 LYS HG3 H 1.853 0.01 1
254 . 35 LYS HD2 H 2.048 0.01 1
255 . 35 LYS HD3 H 2.048 0.01 1
256 . 35 LYS HE2 H 3.090 0.01 1
257 . 35 LYS HE3 H 3.090 0.01 1
258 . 35 LYS CA C 53.902 0.15 1
259 . 36 ARG H H 8.364 0.01 1
260 . 36 ARG HA H 4.423 0.01 1
261 . 36 ARG HB2 H 1.625 0.01 2
262 . 36 ARG HB3 H 1.511 0.01 2
263 . 36 ARG HG2 H 1.054 0.01 1
264 . 36 ARG HG3 H 1.054 0.01 1
265 . 36 ARG HD2 H 3.142 0.01 2
266 . 36 ARG HD3 H 2.884 0.01 2
267 . 36 ARG HE H 8.416 0.01 1
268 . 36 ARG CA C 53.410 0.15 1
269 . 37 GLY H H 6.466 0.01 1
270 . 37 GLY HA2 H 4.364 0.01 2
271 . 37 GLY HA3 H 3.808 0.01 2
272 . 37 GLY CA C 44.044 0.15 1
273 . 38 CYS H H 9.260 0.01 1
274 . 38 CYS HA H 5.987 0.01 1
275 . 38 CYS HB2 H 3.578 0.01 2
276 . 38 CYS HB3 H 2.910 0.01 2
277 . 38 CYS CA C 53.763 0.15 1
278 . 39 ILE H H 9.937 0.01 1
279 . 39 ILE HA H 4.458 0.01 1
280 . 39 ILE HB H 1.734 0.01 1
281 . 39 ILE HG12 H 1.371 0.01 1
282 . 39 ILE HG13 H 1.371 0.01 1
283 . 39 ILE HG2 H 0.580 0.01 1
284 . 39 ILE HD1 H 0.451 0.01 1
285 . 39 ILE CA C 53.763 0.15 1
286 . 40 ASP H H 8.744 0.01 1
287 . 40 ASP HA H 4.897 0.01 1
288 . 40 ASP HB2 H 2.793 0.01 1
289 . 40 ASP HB3 H 2.793 0.01 1
290 . 40 ASP CA C 52.253 0.15 1
291 . 41 VAL H H 7.737 0.01 1
292 . 41 VAL HA H 4.018 0.01 1
293 . 41 VAL HB H 1.732 0.01 1
294 . 41 VAL HG1 H 0.765 0.01 1
295 . 41 VAL HG2 H 0.765 0.01 1
296 . 41 VAL CA C 58.018 0.15 1
297 . 42 CYS H H 8.912 0.01 1
298 . 42 CYS HA H 4.466 0.01 1
299 . 42 CYS HB2 H 3.090 0.01 2
300 . 42 CYS HB3 H 2.764 0.01 2
301 . 42 CYS CA C 52.513 0.15 1
302 . 43 PRO HA H 4.059 0.01 1
303 . 43 PRO HB2 H 1.751 0.01 2
304 . 43 PRO HB3 H 0.370 0.01 2
305 . 43 PRO HG2 H 1.247 0.01 2
306 . 43 PRO HG3 H 0.561 0.01 2
307 . 43 PRO HD2 H 3.931 0.01 2
308 . 43 PRO HD3 H 2.493 0.01 2
309 . 43 PRO CA C 59.698 0.15 1
310 . 44 LYS H H 8.029 0.01 1
311 . 44 LYS HA H 4.201 0.01 1
312 . 44 LYS HB2 H 1.727 0.01 1
313 . 44 LYS HB3 H 1.727 0.01 1
314 . 44 LYS HG2 H 1.565 0.01 1
315 . 44 LYS HG3 H 1.565 0.01 1
316 . 44 LYS HD2 H 1.834 0.01 1
317 . 44 LYS HD3 H 1.834 0.01 1
318 . 44 LYS HE2 H 3.042 0.01 1
319 . 44 LYS HE3 H 3.042 0.01 1
320 . 44 LYS CA C 54.034 0.15 1
321 . 45 SER H H 8.582 0.01 1
322 . 45 SER HA H 4.775 0.01 1
323 . 45 SER HB2 H 4.410 0.01 2
324 . 45 SER HB3 H 4.032 0.01 2
325 . 45 SER CA C 57.682 0.15 1
326 . 46 SER H H 9.436 0.01 1
327 . 46 SER HA H 5.004 0.01 1
328 . 46 SER HB2 H 4.472 0.01 2
329 . 46 SER HB3 H 3.974 0.01 2
330 . 46 SER CA C 53.928 0.15 1
331 . 47 LEU H H 8.269 0.01 1
332 . 47 LEU HA H 4.232 0.01 1
333 . 47 LEU HB2 H 1.763 0.01 1
334 . 47 LEU HB3 H 1.763 0.01 1
335 . 47 LEU HG H 1.639 0.01 1
336 . 47 LEU HD1 H 0.948 0.01 1
337 . 47 LEU HD2 H 0.948 0.01 1
338 . 47 LEU CA C 55.029 0.15 1
339 . 48 LEU H H 8.084 0.01 1
340 . 48 LEU HA H 4.545 0.01 1
341 . 48 LEU HB2 H 1.748 0.01 1
342 . 48 LEU HB3 H 1.748 0.01 1
343 . 48 LEU HG H 1.657 0.01 1
344 . 48 LEU HD1 H 0.947 0.01 2
345 . 48 LEU HD2 H 0.878 0.01 2
346 . 48 LEU CA C 53.483 0.15 1
347 . 49 VAL H H 7.538 0.01 1
348 . 49 VAL HA H 4.810 0.01 1
349 . 49 VAL HB H 1.900 0.01 1
350 . 49 VAL HG1 H 0.882 0.01 2
351 . 49 VAL HG2 H 0.763 0.01 2
352 . 49 VAL CA C 58.462 0.15 1
353 . 50 LYS H H 8.729 0.01 1
354 . 50 LYS HA H 4.813 0.01 1
355 . 50 LYS HB2 H 1.349 0.01 1
356 . 50 LYS HB3 H 1.349 0.01 1
357 . 50 LYS HG2 H 1.225 0.01 2
358 . 50 LYS HG3 H 1.148 0.01 2
359 . 50 LYS HD2 H 1.664 0.01 1
360 . 50 LYS HD3 H 1.664 0.01 1
361 . 50 LYS HE2 H 2.923 0.01 2
362 . 50 LYS HE3 H 2.842 0.01 2
363 . 50 LYS CA C 51.534 0.15 1
364 . 51 TYR H H 8.324 0.01 1
365 . 51 TYR HA H 5.293 0.01 1
366 . 51 TYR HB2 H 2.831 0.01 2
367 . 51 TYR HB3 H 2.635 0.01 2
368 . 51 TYR HD1 H 6.733 0.01 1
369 . 51 TYR HD2 H 6.733 0.01 1
370 . 51 TYR HE1 H 6.465 0.01 1
371 . 51 TYR HE2 H 6.465 0.01 1
372 . 51 TYR CA C 54.788 0.15 1
373 . 52 VAL H H 8.953 0.01 1
374 . 52 VAL HA H 4.556 0.01 1
375 . 52 VAL HB H 2.092 0.01 1
376 . 52 VAL HG1 H 1.149 0.01 2
377 . 52 VAL HG2 H 1.069 0.01 2
378 . 52 VAL CA C 59.688 0.15 1
379 . 53 CYS H H 9.471 0.01 1
380 . 53 CYS HA H 5.912 0.01 1
381 . 53 CYS HB2 H 3.803 0.01 2
382 . 53 CYS HB3 H 3.078 0.01 2
383 . 53 CYS CA C 52.609 0.15 1
384 . 54 CYS H H 9.166 0.01 1
385 . 54 CYS HA H 5.117 0.01 1
386 . 54 CYS HB2 H 3.650 0.01 2
387 . 54 CYS HB3 H 3.440 0.01 2
388 . 54 CYS CA C 52.872 0.15 1
389 . 55 ASN H H 8.595 0.01 1
390 . 55 ASN HA H 5.167 0.01 1
391 . 55 ASN HB2 H 3.402 0.01 2
392 . 55 ASN HB3 H 2.656 0.01 2
393 . 55 ASN HD21 H 6.740 0.01 2
394 . 55 ASN HD22 H 7.542 0.01 2
395 . 55 ASN CA C 50.689 0.15 1
396 . 56 THR H H 7.584 0.01 1
397 . 56 THR HA H 4.706 0.01 1
398 . 56 THR HG2 H 1.204 0.01 1
399 . 56 THR CA C 57.714 0.15 1
400 . 57 ASP H H 8.228 0.01 1
401 . 57 ASP HA H 4.856 0.01 1
402 . 57 ASP HB2 H 2.500 0.01 2
403 . 57 ASP HB3 H 2.274 0.01 2
404 . 57 ASP CA C 51.632 0.15 1
405 . 58 ARG H H 9.666 0.01 1
406 . 58 ARG HA H 3.407 0.01 1
407 . 58 ARG HB2 H 1.781 0.01 2
408 . 58 ARG HB3 H 1.372 0.01 2
409 . 58 ARG HG2 H 0.756 0.01 1
410 . 58 ARG HG3 H 0.756 0.01 1
411 . 58 ARG HD2 H 2.207 0.01 1
412 . 58 ARG HD3 H 2.207 0.01 1
413 . 58 ARG CA C 55.729 0.15 1
414 . 59 CYS H H 7.572 0.01 1
415 . 59 CYS HA H 4.473 0.01 1
416 . 59 CYS HB2 H 3.642 0.01 2
417 . 59 CYS HB3 H 3.363 0.01 2
418 . 59 CYS CA C 54.011 0.15 1
419 . 60 ASN H H 9.136 0.01 1
420 . 60 ASN HA H 4.387 0.01 1
421 . 60 ASN HB2 H 2.732 0.01 2
422 . 60 ASN HB3 H 2.357 0.01 2
423 . 60 ASN HD21 H 7.485 0.01 2
424 . 60 ASN HD22 H 7.642 0.01 2
425 . 60 ASN CA C 52.342 0.15 1
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