data_5264
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution Structure of Human beta-Defensin 3
;
_BMRB_accession_number 5264
_BMRB_flat_file_name bmr5264.str
_Entry_type original
_Submission_date 2002-01-23
_Accession_date 2002-01-24
_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 Schibli D. J. .
2 Hunter H. N. .
3 Aseyev V. . .
4 Starner T. D. .
5 Wiencek J. M. .
6 McCray P. M. Jr.
7 Tack B. F. .
8 Vogel H. J. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 241
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2002-06-13 original BMRB .
stop_
_Original_release_date 2002-01-24
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
The Solution Structures of the Human beta-Defensins lead to a Better
Understanding of the Potent Bactericidal Activity of HBD3 against Staphylococcus
aureus
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 21864161
_PubMed_ID 11741980
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Schibli D. J. .
2 Hunter H. N. .
3 Aseyev V. . .
4 Starner T. D. .
5 Wiencek J. M. .
6 McCray P. M. Jr.
7 Tack B. F. .
8 Vogel H. J. .
stop_
_Journal_abbreviation 'J. Biol. Chem.'
_Journal_volume 277
_Journal_issue 10
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 8279
_Page_last 8289
_Year 2002
_Details .
loop_
_Keyword
HBD3
'antimicrobial protein'
beta-defensin
defensin
'human beta-defensin 3'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_HBD-3
_Saveframe_category molecular_system
_Mol_system_name 'Human Beta-defensin 3'
_Abbreviation_common HBD-3
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Beta-defensin 3' $HBD-3
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state dimer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
loop_
_Biological_function
'antimicrobial protein'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_HBD-3
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Human beta-defensin 3'
_Abbreviation_common HBD-3
_Molecular_mass 5168.9
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 45
_Mol_residue_sequence
;
GIINTLQKYYCRVRGGRCAV
LSCLPKEEQIGKCSTRGRKC
CRRKK
;
loop_
_Residue_seq_code
_Residue_label
1 GLY 2 ILE 3 ILE 4 ASN 5 THR
6 LEU 7 GLN 8 LYS 9 TYR 10 TYR
11 CYS 12 ARG 13 VAL 14 ARG 15 GLY
16 GLY 17 ARG 18 CYS 19 ALA 20 VAL
21 LEU 22 SER 23 CYS 24 LEU 25 PRO
26 LYS 27 GLU 28 GLU 29 GLN 30 ILE
31 GLY 32 LYS 33 CYS 34 SER 35 THR
36 ARG 37 GLY 38 ARG 39 LYS 40 CYS
41 CYS 42 ARG 43 ARG 44 LYS 45 LYS
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 1KJ6 'Solution Structure Of Human Beta-Defensin 3' 100.00 45 100.00 100.00 1.68e-16
DBJ BAB40572 'defensin like protein [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17
EMBL CAC03097 'beta-defensin-3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17
EMBL CAL68919 'beta defensin 103 [Gorilla gorilla]' 100.00 67 100.00 100.00 5.45e-17
EMBL CAL68920 'beta defensin 103 [Pongo pygmaeus]' 100.00 67 100.00 100.00 5.09e-17
GenBank AAF73853 'beta defensin-3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17
GenBank AAG02237 'beta-defensin 3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17
GenBank AAG22030 'beta-defensin 3 [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17
GenBank AAI11597 'DEFB103A protein [synthetic construct]' 100.00 67 100.00 100.00 5.09e-17
GenBank AAI48675 'Defensin, beta 103B [synthetic construct]' 100.00 67 100.00 100.00 5.09e-17
REF NP_001075020 'beta-defensin 103B precursor [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17
REF NP_061131 'defensin, beta 103A precursor [Homo sapiens]' 100.00 67 100.00 100.00 5.09e-17
REF XP_001083420 'PREDICTED: defensin, beta 103A [Macaca mulatta]' 100.00 67 100.00 100.00 5.09e-17
SWISS-PROT A4H1Z9 'Beta-defensin 103A precursor (Defensin, beta 103A) (Defensin, beta 103)' 100.00 67 100.00 100.00 5.45e-17
SWISS-PROT A4H200 'Beta-defensin 103A precursor (Defensin, beta 103A) (Defensin, beta 103)' 100.00 67 100.00 100.00 5.09e-17
SWISS-PROT P81534 'Beta-defensin 103 precursor (Defensin, beta 103) (Beta-defensin 3) (BD-3) (hBD-3) (HBD3) (DEFB-3) (Defensin-like protein)' 100.00 67 100.00 100.00 5.09e-17
tpg|DAA01350.1| DAA01350 'TPA: TPA_exp: DEFB103-like protein [Papio anubis]' 100.00 67 100.00 100.00 4.61e-17
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
_Tissue
$HBD-3 Human 9606 Eukaryota Metazoa Homo sapiens heart 'skeletal muscle; placenta; esophagus; trachea; oral mucosa; skin tissues'
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
$HBD-3 'recombinant technology' . . . . . 'Produced by Peprotech (Rocky Hill, NJ).'
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
$HBD-3 0.36 mM .
D2O 10 % .
H2O 90 % .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$HBD-3 0.36 mM .
D2O 100 % .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name XWINNMR
_Version 2.6
loop_
_Task
collection
stop_
_Details Bruker
save_
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 1.8
loop_
_Task
processing
stop_
_Details 'Delaglio, G., Grzejiek, S., Vuister, G., Zhu, G., Pfeifer, J., Bax, A.'
save_
save_NMRView
_Saveframe_category software
_Name NMRView
_Version 4.1.3
loop_
_Task
'data analysis'
stop_
_Details 'Johnson, B.A., Blevins, R.A.'
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 1.0
loop_
_Task
refinement
stop_
_Details
;
A.T.Brunger, P.D.Adams, G.M.Clore, W.L.Delano, P.Gros, R.W.Grosse-Kunstleve, J.-S.Jiang,
J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson, G.L.Warren.
;
save_
save_Aria
_Saveframe_category software
_Name Aria
_Version 1.0
loop_
_Task
refinement
stop_
_Details "J.Linge, S.O'Donoghue, M.Nilges."
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AVANCE
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label .
save_
save_2D_TOCSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label .
save_
save_2D_DQF-COSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D DQF-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
pH 4.00 0.1 n/a
pressure 1 . atm
temperature 298 0.1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS 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_chemical_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D NOESY'
'2D TOCSY'
'2D DQF-COSY'
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 'Beta-defensin 3'
_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 GLY HA3 H 3.873 . 2
2 . 2 ILE H H 8.530 . 1
3 . 2 ILE HA H 4.231 . 1
4 . 2 ILE HB H 1.839 . 1
5 . 2 ILE HG13 H 1.466 . 9
6 . 2 ILE HG12 H 1.199 . 9
7 . 2 ILE HD1 H 0.882 . 1
8 . 2 ILE HG2 H 0.908 . 4
9 . 3 ILE H H 8.364 . 1
10 . 3 ILE HA H 4.183 . 1
11 . 3 ILE HB H 1.868 . 1
12 . 3 ILE HG13 H 1.506 . 9
13 . 3 ILE HG12 H 1.215 . 9
14 . 3 ILE HD1 H 0.859 . 1
15 . 3 ILE HG2 H 0.854 . 4
16 . 4 ASN H H 8.595 . 1
17 . 4 ASN HA H 4.766 . 1
18 . 4 ASN HB3 H 2.834 . 2
19 . 4 ASN HD21 H 6.918 . 2
20 . 4 ASN HD22 H 7.641 . 2
21 . 5 THR H H 8.172 . 1
22 . 5 THR HA H 4.230 . 1
23 . 5 THR HB H 4.285 . 1
24 . 5 THR HG2 H 1.207 . 1
25 . 6 LEU H H 8.195 . 1
26 . 6 LEU HA H 4.329 . 1
27 . 6 LEU HB3 H 1.715 . 2
28 . 6 LEU HG H 1.622 . 1
29 . 6 LEU HD1 H 0.916 . 2
30 . 6 LEU HD2 H 0.848 . 2
31 . 7 GLN H H 8.166 . 1
32 . 7 GLN HA H 4.130 . 1
33 . 7 GLN HB3 H 2.082 . 2
34 . 7 GLN HB2 H 1.939 . 2
35 . 7 GLN HG3 H 2.335 . 2
36 . 7 GLN HE21 H 6.740 . 2
37 . 7 GLN HE22 H 7.442 . 2
38 . 8 LYS H H 8.160 . 1
39 . 8 LYS HA H 4.045 . 1
40 . 8 LYS HB3 H 1.707 . 2
41 . 8 LYS HG3 H 1.292 . 2
42 . 8 LYS HG2 H 1.187 . 2
43 . 8 LYS HD2 H 1.615 . 2
44 . 8 LYS HE2 H 2.924 . 2
45 . 9 TYR H H 7.994 . 1
46 . 9 TYR HA H 4.532 . 1
47 . 9 TYR HB3 H 2.986 . 2
48 . 9 TYR HB2 H 3.157 . 2
49 . 9 TYR HD1 H 6.981 . 2
50 . 9 TYR HE1 H 6.762 . 2
51 . 10 TYR H H 8.070 . 1
52 . 10 TYR HA H 4.291 . 1
53 . 10 TYR HB3 H 3.077 . 2
54 . 10 TYR HD1 H 7.099 . 2
55 . 10 TYR HE1 H 6.823 . 2
56 . 11 CYS H H 8.343 . 1
57 . 11 CYS HA H 4.255 . 1
58 . 11 CYS HB3 H 3.088 . 2
59 . 11 CYS HB2 H 2.971 . 2
60 . 12 ARG H H 7.958 . 1
61 . 12 ARG HA H 4.270 . 1
62 . 12 ARG HB3 H 1.949 . 2
63 . 12 ARG HG3 H 1.693 . 2
64 . 12 ARG HD3 H 3.210 . 2
65 . 12 ARG HE H 7.208 . 1
66 . 13 VAL H H 8.298 . 1
67 . 13 VAL HA H 3.904 . 1
68 . 13 VAL HB H 2.127 . 1
69 . 13 VAL HG2 H 0.919 . 2
70 . 13 VAL HG1 H 0.953 . 2
71 . 14 ARG H H 7.312 . 1
72 . 14 ARG HA H 4.303 . 1
73 . 14 ARG HB3 H 2.123 . 2
74 . 14 ARG HB2 H 1.936 . 2
75 . 14 ARG HG3 H 1.638 . 2
76 . 14 ARG HG2 H 1.531 . 2
77 . 14 ARG HD3 H 2.978 . 2
78 . 14 ARG HE H 6.879 . 1
79 . 15 GLY H H 8.009 . 1
80 . 15 GLY HA3 H 3.850 . 2
81 . 15 GLY HA2 H 4.217 . 2
82 . 16 GLY H H 8.176 . 1
83 . 16 GLY HA3 H 4.572 . 2
84 . 16 GLY HA2 H 3.306 . 2
85 . 17 ARG H H 8.843 . 1
86 . 17 ARG HA H 4.685 . 1
87 . 17 ARG HB3 H 1.741 . 2
88 . 17 ARG HB2 H 1.680 . 2
89 . 17 ARG HG3 H 1.535 . 2
90 . 17 ARG HG2 H 1.259 . 2
91 . 17 ARG HD3 H 3.184 . 2
92 . 17 ARG HD2 H 2.999 . 2
93 . 17 ARG HE H 9.220 . 1
94 . 17 ARG HH21 H 6.847 . 9
95 . 18 CYS H H 8.924 . 1
96 . 18 CYS HA H 5.362 . 1
97 . 18 CYS HB3 H 2.935 . 2
98 . 18 CYS HB2 H 2.720 . 2
99 . 19 ALA H H 9.365 . 1
100 . 19 ALA HA H 4.537 . 1
101 . 19 ALA HB H 1.323 . 1
102 . 20 VAL H H 8.640 . 1
103 . 20 VAL HA H 3.845 . 1
104 . 20 VAL HB H 2.034 . 1
105 . 20 VAL HG2 H 0.975 . 2
106 . 20 VAL HG1 H 1.012 . 2
107 . 21 LEU H H 8.345 . 1
108 . 21 LEU HA H 4.408 . 1
109 . 21 LEU HB3 H 1.718 . 2
110 . 21 LEU HG H 1.556 . 1
111 . 21 LEU HD1 H 0.951 . 2
112 . 21 LEU HD2 H 0.930 . 2
113 . 22 SER H H 8.189 . 1
114 . 22 SER HA H 4.484 . 1
115 . 22 SER HB3 H 3.795 . 2
116 . 22 SER HB2 H 3.881 . 2
117 . 23 CYS H H 8.581 . 1
118 . 23 CYS HA H 4.784 . 1
119 . 23 CYS HB3 H 3.399 . 2
120 . 23 CYS HB2 H 2.659 . 2
121 . 24 LEU H H 9.244 . 1
122 . 24 LEU HA H 4.500 . 1
123 . 24 LEU HB3 H 1.766 . 2
124 . 24 LEU HB2 H 1.305 . 2
125 . 24 LEU HG H 1.632 . 1
126 . 24 LEU HD1 H 0.958 . 4
127 . 24 LEU HD2 H 0.868 . 4
128 . 25 PRO HA H 4.354 . 1
129 . 25 PRO HB3 H 1.873 . 2
130 . 25 PRO HB2 H 2.431 . 2
131 . 25 PRO HG3 H 2.160 . 2
132 . 25 PRO HG2 H 2.056 . 2
133 . 25 PRO HD3 H 3.753 . 2
134 . 25 PRO HD2 H 3.819 . 2
135 . 26 LYS H H 7.828 . 1
136 . 26 LYS HA H 4.348 . 1
137 . 26 LYS HB3 H 1.868 . 2
138 . 26 LYS HB2 H 2.110 . 2
139 . 26 LYS HG3 H 1.419 . 2
140 . 26 LYS HD2 H 1.769 . 2
141 . 26 LYS HE2 H 2.982 . 2
142 . 27 GLU H H 8.122 . 1
143 . 27 GLU HA H 4.863 . 1
144 . 27 GLU HB3 H 1.821 . 2
145 . 27 GLU HB2 H 1.651 . 2
146 . 27 GLU HG3 H 2.520 . 2
147 . 27 GLU HG2 H 2.120 . 2
148 . 28 GLU H H 9.032 . 1
149 . 28 GLU HA H 4.755 . 1
150 . 28 GLU HB3 H 1.974 . 2
151 . 28 GLU HB2 H 1.869 . 2
152 . 28 GLU HG3 H 2.189 . 2
153 . 28 GLU HG2 H 2.123 . 2
154 . 29 GLN H H 9.027 . 1
155 . 29 GLN HA H 4.987 . 1
156 . 29 GLN HB3 H 2.088 . 2
157 . 29 GLN HG3 H 2.482 . 2
158 . 29 GLN HE21 H 7.099 . 2
159 . 29 GLN HE22 H 7.187 . 2
160 . 30 ILE H H 8.744 . 1
161 . 30 ILE HA H 4.717 . 1
162 . 30 ILE HB H 2.103 . 1
163 . 30 ILE HG13 H 0.966 . 1
164 . 30 ILE HD1 H 0.674 . 1
165 . 30 ILE HG2 H 0.824 . 4
166 . 31 GLY H H 7.629 . 1
167 . 31 GLY HA3 H 4.339 . 2
168 . 31 GLY HA2 H 4.055 . 2
169 . 32 LYS H H 8.947 . 1
170 . 32 LYS HA H 4.930 . 1
171 . 32 LYS HB3 H 1.966 . 2
172 . 32 LYS HG3 H 1.376 . 2
173 . 32 LYS HD2 H 1.665 . 2
174 . 32 LYS HE2 H 2.948 . 2
175 . 33 CYS H H 8.424 . 1
176 . 33 CYS HA H 4.840 . 1
177 . 33 CYS HB3 H 3.285 . 2
178 . 34 SER H H 8.202 . 1
179 . 34 SER HA H 4.364 . 1
180 . 34 SER HB3 H 3.895 . 2
181 . 34 SER HB2 H 4.076 . 2
182 . 35 THR H H 8.036 . 1
183 . 35 THR HA H 4.270 . 1
184 . 35 THR HB H 4.151 . 1
185 . 35 THR HG2 H 1.270 . 1
186 . 36 ARG H H 8.461 . 1
187 . 36 ARG HA H 4.213 . 1
188 . 36 ARG HB3 H 1.766 . 2
189 . 36 ARG HB2 H 1.987 . 2
190 . 36 ARG HG3 H 1.654 . 2
191 . 36 ARG HD3 H 3.208 . 2
192 . 37 GLY H H 8.166 . 1
193 . 37 GLY HA3 H 4.106 . 2
194 . 37 GLY HA2 H 3.780 . 2
195 . 38 ARG H H 7.625 . 1
196 . 38 ARG HA H 4.570 . 1
197 . 38 ARG HB3 H 1.756 . 2
198 . 38 ARG HG3 H 1.603 . 2
199 . 38 ARG HD3 H 3.024 . 2
200 . 38 ARG HE H 7.123 . 1
201 . 39 LYS H H 8.974 . 1
202 . 39 LYS HA H 4.317 . 1
203 . 39 LYS HB3 H 1.558 . 2
204 . 39 LYS HG3 H 1.350 . 2
205 . 39 LYS HD2 H 1.548 . 2
206 . 39 LYS HE2 H 3.039 . 2
207 . 40 CYS H H 8.311 . 1
208 . 40 CYS HA H 5.226 . 1
209 . 40 CYS HB3 H 2.494 . 2
210 . 40 CYS HB2 H 2.546 . 2
211 . 41 CYS H H 9.448 . 1
212 . 41 CYS HA H 5.468 . 1
213 . 41 CYS HB3 H 2.843 . 2
214 . 41 CYS HB2 H 2.553 . 2
215 . 42 ARG H H 9.430 . 1
216 . 42 ARG HA H 4.922 . 1
217 . 42 ARG HB3 H 1.922 . 2
218 . 42 ARG HB2 H 1.385 . 2
219 . 42 ARG HG3 H 1.801 . 2
220 . 42 ARG HD3 H 3.375 . 2
221 . 42 ARG HD2 H 2.939 . 2
222 . 42 ARG HE H 7.662 . 1
223 . 43 ARG H H 8.986 . 1
224 . 43 ARG HA H 4.235 . 1
225 . 43 ARG HB3 H 1.895 . 2
226 . 43 ARG HG3 H 1.736 . 2
227 . 43 ARG HD3 H 3.246 . 2
228 . 43 ARG HE H 7.346 . 1
229 . 44 LYS H H 8.604 . 1
230 . 44 LYS HA H 4.204 . 1
231 . 44 LYS HB3 H 1.829 . 2
232 . 44 LYS HG3 H 1.366 . 2
233 . 44 LYS HG2 H 1.309 . 2
234 . 44 LYS HD2 H 1.608 . 2
235 . 44 LYS HE2 H 2.933 . 2
236 . 45 LYS H H 8.243 . 1
237 . 45 LYS HA H 4.099 . 1
238 . 45 LYS HB3 H 1.783 . 2
239 . 45 LYS HG3 H 1.434 . 2
240 . 45 LYS HD2 H 1.713 . 2
241 . 45 LYS HE2 H 3.013 . 2
stop_
save_