data_11050
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Structure of the N-terminal BARpeptide in SDS micelles
;
_BMRB_accession_number 11050
_BMRB_flat_file_name bmr11050.str
_Entry_type original
_Submission_date 2008-06-26
_Accession_date 2008-06-26
_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 Loew Christian . .
2 Weininger Ulrich . .
3 Balbach Jochen . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 210
"15N chemical shifts" 38
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2009-03-03 original author .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
11049 'NMR Assignment of the N-terminal BARpeptide in DPC micelles'
stop_
_Original_release_date 2009-03-03
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Structure and Dynamics of Helix-0 of the N-BAR Domain in Lipid Micelles and Bilayers'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 18658220
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Loew Christian . .
2 Weininger Ulrich . .
3 Lee Hwankyu . .
4 Schweimer Kristian . .
5 Neundorf Ines . .
6 Beck-Sickinger Annette G. .
7 Pastor Richard W. .
8 Balbach Jochen . .
stop_
_Journal_abbreviation 'Biophys. J.'
_Journal_name_full 'Biophysical Journal'
_Journal_volume 95
_Journal_issue 9
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 4315
_Page_last 4323
_Year 2008
_Details .
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name BARpeptide
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'BARpeptide (1-33)' $entity
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_entity
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'BARpeptide (1-33)'
_Molecular_mass 3714.452
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 34
_Mol_residue_sequence
;
MAEMGSKGVTAGKIASNVQK
KLTRAQEKVLQKLY
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ALA 3 GLU 4 MET 5 GLY
6 SER 7 LYS 8 GLY 9 VAL 10 THR
11 ALA 12 GLY 13 LYS 14 ILE 15 ALA
16 SER 17 ASN 18 VAL 19 GLN 20 LYS
21 LYS 22 LEU 23 THR 24 ARG 25 ALA
26 GLN 27 GLU 28 LYS 29 VAL 30 LEU
31 GLN 32 LYS 33 LEU 34 TYR
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-31
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 11049 "BARpeptide (1-33)" 100.00 34 100.00 100.00 1.60e-13
PDB 2FIC "The Crystal Structure Of The Bar Domain From Human Bin1AMPHIPHYSIN II And Its Implications For Molecular Recognition" 97.06 251 100.00 100.00 1.31e-11
PDB 2RMY "Structure Of The N-Terminal Barpeptide In Sds Micelles" 97.06 34 100.00 100.00 2.31e-12
PDB 2RND "Structure Of The N-Terminal Barpeptide In Dpc Micelles" 97.06 34 100.00 100.00 2.31e-12
DBJ BAE87346 "unnamed protein product [Macaca fascicularis]" 97.06 439 100.00 100.00 4.19e-11
DBJ BAH12028 "unnamed protein product [Homo sapiens]" 97.06 470 100.00 100.00 5.45e-11
DBJ BAJ17746 "bridging integrator 1 [synthetic construct]" 97.06 593 100.00 100.00 1.08e-09
EMBL CAA73807 "amphiphysin [Rattus norvegicus]" 97.06 588 100.00 100.00 1.58e-09
EMBL CAD28496 "hypothetical protein [Homo sapiens]" 97.06 593 100.00 100.00 1.08e-09
EMBL CAG31301 "hypothetical protein RCJMB04_4n21 [Gallus gallus]" 97.06 442 96.97 100.00 1.29e-10
EMBL CAL37828 "hypothetical protein [synthetic construct]" 97.06 593 100.00 100.00 1.08e-09
GB AAB61363 "amphiphysin II [Homo sapiens]" 97.06 482 100.00 100.00 4.11e-11
GB AAB63263 "amphiphysin II [Homo sapiens]" 97.06 593 100.00 100.00 8.96e-10
GB AAC17461 "bridging integrator protein-1 [Homo sapiens]" 97.06 454 100.00 100.00 5.00e-11
GB AAC23440 "bridging integrator protein-1 [Homo sapiens]" 97.06 497 100.00 100.00 4.40e-11
GB AAC23441 "bridging integrator protein-1 [Homo sapiens]" 88.24 494 100.00 100.00 6.06e-09
REF NP_001006524 "bridging integrator 1 [Gallus gallus]" 97.06 442 96.97 100.00 1.22e-10
REF NP_001040006 "myc box-dependent-interacting protein 1 [Bos taurus]" 97.06 433 100.00 100.00 3.72e-11
REF NP_001076803 "myc box-dependent-interacting protein 1 isoform 2 [Mus musculus]" 97.06 477 100.00 100.00 3.53e-11
REF NP_001090909 "myc box-dependent-interacting protein 1 [Sus scrofa]" 97.06 434 100.00 100.00 3.85e-11
REF NP_004296 "myc box-dependent-interacting protein 1 isoform 8 [Homo sapiens]" 97.06 454 100.00 100.00 5.00e-11
SP O00499 "RecName: Full=Myc box-dependent-interacting protein 1; AltName: Full=Amphiphysin II; AltName: Full=Amphiphysin-like protein; Al" 97.06 593 100.00 100.00 1.08e-09
SP O08539 "RecName: Full=Myc box-dependent-interacting protein 1; AltName: Full=Amphiphysin II; AltName: Full=Amphiphysin-like protein; Al" 97.06 588 100.00 100.00 1.58e-09
SP O08839 "RecName: Full=Myc box-dependent-interacting protein 1; AltName: Full=Amphiphysin II; AltName: Full=Amphiphysin-like protein; Al" 97.06 588 100.00 100.00 1.58e-09
TPG DAA32871 "TPA: bridging integrator 1 [Bos taurus]" 97.06 433 100.00 100.00 3.72e-11
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$entity Human 9606 Eukaryota Metazoa Homo sapiens
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Variant
_Vector_name
$entity 'recombinant technology' . Escherichia coli . BL21 petSUMO
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type micelle
_Details 'in SDS micelles'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$entity 1 mM '[U-100% 15N]'
stop_
save_
############################
# Computer software used #
############################
save_ARIA
_Saveframe_category software
_Name ARIA
_Version 2.1
loop_
_Vendor
_Address
_Electronic_address
'Linge, O'Donoghue and Nilges' . .
stop_
loop_
_Task
refinement
'structure solution'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model Avance
_Field_strength 700
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label $sample_1
save_
save_3D_1H-15N_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-15N NOESY'
_Sample_label $sample_1
save_
save_3D_1H-15N_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 1H-15N TOCSY'
_Sample_label $sample_1
save_
save_3D_HNHA_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNHA'
_Sample_label $sample_1
save_
save_2D_1H-1H_NOESY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H NOESY'
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 0 . M
pH 7.4 . pH
pressure 1 . atm
temperature 298 . K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_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
water H 1 protons ppm 4.700 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
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_assigned_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-15N HSQC'
'3D 1H-15N NOESY'
'3D 1H-15N TOCSY'
'2D 1H-1H NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference_1
_Mol_system_component_name 'BARpeptide (1-33)'
_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 1 MET HA H 4.095 . 1
2 1 1 MET HB2 H 2.122 . 2
3 1 1 MET HB3 H 2.123 . 2
4 1 1 MET HG2 H 2.597 . 2
5 1 1 MET HG3 H 2.598 . 2
6 2 2 ALA H H 8.341 . 1
7 2 2 ALA HA H 4.257 . 1
8 2 2 ALA HB H 1.342 . 1
9 2 2 ALA N N 128.151 . 1
10 3 3 GLU H H 8.123 . 1
11 3 3 GLU HA H 4.291 . 1
12 3 3 GLU HB2 H 1.939 . 2
13 3 3 GLU HB3 H 2.049 . 2
14 3 3 GLU HG2 H 2.407 . 2
15 3 3 GLU HG3 H 2.408 . 2
16 3 3 GLU N N 119.217 . 1
17 4 4 MET H H 8.182 . 1
18 4 4 MET HA H 4.354 . 1
19 4 4 MET HB2 H 1.998 . 2
20 4 4 MET HB3 H 1.000 . 2
21 4 4 MET HG2 H 2.469 . 2
22 4 4 MET HG3 H 2.534 . 2
23 4 4 MET N N 122.534 . 1
24 5 5 GLY H H 8.264 . 1
25 5 5 GLY HA2 H 4.008 . 2
26 5 5 GLY HA3 H 3.935 . 2
27 5 5 GLY N N 111.280 . 1
28 6 6 SER H H 8.159 . 1
29 6 6 SER HA H 4.342 . 1
30 6 6 SER HB2 H 3.829 . 2
31 6 6 SER HB3 H 3.890 . 2
32 6 6 SER N N 117.242 . 1
33 7 7 LYS H H 8.188 . 1
34 7 7 LYS HA H 4.236 . 1
35 7 7 LYS HB2 H 1.838 . 2
36 7 7 LYS HB3 H 1.839 . 2
37 7 7 LYS HD2 H 1.616 . 2
38 7 7 LYS HD3 H 1.617 . 2
39 7 7 LYS HE2 H 2.927 . 2
40 7 7 LYS HE3 H 2.927 . 2
41 7 7 LYS HG2 H 1.405 . 2
42 7 7 LYS HG3 H 1.448 . 2
43 7 7 LYS N N 123.055 . 1
44 8 8 GLY H H 8.049 . 1
45 8 8 GLY HA2 H 3.913 . 2
46 8 8 GLY HA3 H 3.806 . 2
47 8 8 GLY N N 109.733 . 1
48 9 9 VAL H H 7.768 . 1
49 9 9 VAL HA H 3.891 . 1
50 9 9 VAL HB H 2.070 . 1
51 9 9 VAL HG1 H 0.910 . 2
52 9 9 VAL HG2 H 0.871 . 2
53 9 9 VAL N N 121.474 . 1
54 10 10 THR H H 7.715 . 1
55 10 10 THR HA H 4.204 . 1
56 10 10 THR HB H 4.282 . 1
57 10 10 THR HG2 H 1.159 . 1
58 10 10 THR N N 117.703 . 1
59 11 11 ALA H H 8.389 . 1
60 11 11 ALA HA H 4.008 . 1
61 11 11 ALA HB H 1.379 . 1
62 11 11 ALA N N 125.631 . 1
63 12 12 GLY H H 8.261 . 1
64 12 12 GLY HA2 H 3.912 . 2
65 12 12 GLY HA3 H 3.809 . 2
66 12 12 GLY N N 107.084 . 1
67 13 13 LYS H H 7.878 . 1
68 13 13 LYS HA H 4.051 . 1
69 13 13 LYS HB2 H 1.874 . 2
70 13 13 LYS HB3 H 1.875 . 2
71 13 13 LYS HD2 H 1.666 . 2
72 13 13 LYS HD3 H 1.682 . 2
73 13 13 LYS HE2 H 2.912 . 2
74 13 13 LYS HE3 H 2.912 . 2
75 13 13 LYS HG2 H 1.365 . 2
76 13 13 LYS HG3 H 1.477 . 2
77 13 13 LYS N N 124.174 . 1
78 14 14 ILE H H 7.981 . 1
79 14 14 ILE HA H 3.739 . 1
80 14 14 ILE HB H 1.950 . 1
81 14 14 ILE HD1 H 0.796 . 1
82 14 14 ILE HG12 H 1.124 . 2
83 14 14 ILE HG13 H 1.125 . 2
84 14 14 ILE HG2 H 0.823 . 1
85 14 14 ILE N N 121.478 . 1
86 15 15 ALA H H 8.445 . 1
87 15 15 ALA HA H 3.846 . 1
88 15 15 ALA HB H 1.412 . 1
89 15 15 ALA N N 123.052 . 1
90 16 16 SER H H 8.011 . 1
91 16 16 SER HA H 4.185 . 1
92 16 16 SER HB2 H 3.904 . 2
93 16 16 SER HB3 H 3.905 . 2
94 16 16 SER N N 112.930 . 1
95 17 17 ASN H H 7.851 . 1
96 17 17 ASN HA H 4.489 . 1
97 17 17 ASN HB2 H 2.777 . 2
98 17 17 ASN HB3 H 2.944 . 2
99 17 17 ASN HD21 H 7.509 . 2
100 17 17 ASN HD22 H 6.857 . 2
101 17 17 ASN N N 122.427 . 1
102 17 17 ASN ND2 N 114.308 . 1
103 18 18 VAL H H 8.433 . 1
104 18 18 VAL HA H 3.564 . 1
105 18 18 VAL HB H 2.177 . 1
106 18 18 VAL HG1 H 0.992 . 2
107 18 18 VAL HG2 H 0.868 . 2
108 18 18 VAL N N 121.996 . 1
109 19 19 GLN H H 8.360 . 1
110 19 19 GLN HA H 3.842 . 1
111 19 19 GLN HB2 H 2.194 . 2
112 19 19 GLN HB3 H 2.092 . 2
113 19 19 GLN HE21 H 7.163 . 2
114 19 19 GLN HE22 H 6.611 . 2
115 19 19 GLN HG2 H 2.261 . 2
116 19 19 GLN HG3 H 2.425 . 2
117 19 19 GLN N N 121.013 . 1
118 19 19 GLN NE2 N 112.333 . 1
119 20 20 LYS H H 7.664 . 1
120 20 20 LYS HA H 4.003 . 1
121 20 20 LYS HB2 H 1.900 . 2
122 20 20 LYS HB3 H 1.905 . 2
123 20 20 LYS HD2 H 1.624 . 2
124 20 20 LYS HD3 H 1.625 . 2
125 20 20 LYS HE2 H 2.903 . 2
126 20 20 LYS HE3 H 2.903 . 2
127 20 20 LYS HG2 H 1.426 . 2
128 20 20 LYS HG3 H 1.427 . 2
129 20 20 LYS N N 119.657 . 1
130 21 21 LYS H H 7.712 . 1
131 21 21 LYS HA H 4.135 . 1
132 21 21 LYS HB2 H 1.814 . 2
133 21 21 LYS HB3 H 1.911 . 2
134 21 21 LYS HD2 H 1.577 . 2
135 21 21 LYS HD3 H 1.578 . 2
136 21 21 LYS HE2 H 2.935 . 2
137 21 21 LYS HE3 H 2.935 . 2
138 21 21 LYS HG2 H 1.484 . 2
139 21 21 LYS HG3 H 1.485 . 2
140 21 21 LYS N N 120.661 . 1
141 22 22 LEU H H 8.192 . 1
142 22 22 LEU HA H 4.182 . 1
143 22 22 LEU HB2 H 1.792 . 2
144 22 22 LEU HB3 H 1.793 . 2
145 22 22 LEU HD1 H 0.786 . 2
146 22 22 LEU HD2 H 0.785 . 2
147 22 22 LEU HG H 1.556 . 1
148 22 22 LEU N N 120.581 . 1
149 23 23 THR H H 7.990 . 1
150 23 23 THR HA H 4.045 . 1
151 23 23 THR HB H 4.195 . 1
152 23 23 THR HG2 H 1.208 . 1
153 23 23 THR N N 115.621 . 1
154 24 24 ARG H H 7.799 . 1
155 24 24 ARG HA H 4.078 . 1
156 24 24 ARG HB2 H 1.906 . 2
157 24 24 ARG HB3 H 1.907 . 2
158 24 24 ARG HD2 H 3.168 . 2
159 24 24 ARG HD3 H 3.169 . 2
160 24 24 ARG HE H 7.085 . 1
161 24 24 ARG HG2 H 1.608 . 2
162 24 24 ARG HG3 H 1.716 . 2
163 24 24 ARG N N 123.192 . 1
164 24 24 ARG NE N 109.031 . 1
165 25 25 ALA H H 8.080 . 1
166 25 25 ALA HA H 4.023 . 1
167 25 25 ALA HB H 1.426 . 1
168 25 25 ALA N N 123.717 . 1
169 26 26 GLN H H 8.317 . 1
170 26 26 GLN HA H 3.841 . 1
171 26 26 GLN HB2 H 2.086 . 2
172 26 26 GLN HB3 H 2.217 . 2
173 26 26 GLN HE21 H 6.876 . 2
174 26 26 GLN HE22 H 6.666 . 2
175 26 26 GLN HG2 H 2.217 . 2
176 26 26 GLN HG3 H 2.324 . 2
177 26 26 GLN N N 118.677 . 1
178 26 26 GLN NE2 N 111.262 . 1
179 27 27 GLU H H 7.913 . 1
180 27 27 GLU HA H 4.004 . 1
181 27 27 GLU HB2 H 2.079 . 2
182 27 27 GLU HB3 H 2.153 . 2
183 27 27 GLU HG2 H 2.455 . 2
184 27 27 GLU HG3 H 2.576 . 2
185 27 27 GLU N N 118.496 . 1
186 28 28 LYS H H 7.857 . 1
187 28 28 LYS HA H 4.068 . 1
188 28 28 LYS HB2 H 1.839 . 2
189 28 28 LYS HB3 H 1.895 . 2
190 28 28 LYS HD2 H 1.642 . 2
191 28 28 LYS HD3 H 1.643 . 2
192 28 28 LYS HE2 H 2.896 . 2
193 28 28 LYS HE3 H 2.896 . 2
194 28 28 LYS HG2 H 1.433 . 2
195 28 28 LYS HG3 H 1.434 . 2
196 28 28 LYS N N 120.774 . 1
197 29 29 VAL H H 8.035 . 1
198 29 29 VAL HA H 3.597 . 1
199 29 29 VAL HB H 2.138 . 1
200 29 29 VAL HG1 H 0.986 . 2
201 29 29 VAL HG2 H 0.880 . 2
202 29 29 VAL N N 120.353 . 1
203 30 30 LEU H H 8.105 . 1
204 30 30 LEU HA H 4.011 . 1
205 30 30 LEU HB2 H 1.794 . 2
206 30 30 LEU HB3 H 1.795 . 2
207 30 30 LEU HD1 H 0.875 . 2
208 30 30 LEU HD2 H 0.845 . 2
209 30 30 LEU HG H 1.522 . 1
210 30 30 LEU N N 120.674 . 1
211 31 31 GLN H H 7.741 . 1
212 31 31 GLN HA H 4.007 . 1
213 31 31 GLN HB2 H 2.089 . 2
214 31 31 GLN HB3 H 2.090 . 2
215 31 31 GLN HE21 H 7.381 . 2
216 31 31 GLN HE22 H 6.764 . 2
217 31 31 GLN HG2 H 2.358 . 2
218 31 31 GLN HG3 H 2.472 . 2
219 31 31 GLN N N 117.642 . 1
220 31 31 GLN NE2 N 113.425 . 1
221 32 32 LYS H H 7.581 . 1
222 32 32 LYS HA H 4.176 . 1
223 32 32 LYS HB2 H 1.863 . 2
224 32 32 LYS HB3 H 1.864 . 2
225 32 32 LYS HD2 H 1.641 . 2
226 32 32 LYS HD3 H 1.642 . 2
227 32 32 LYS HE2 H 2.895 . 2
228 32 32 LYS HE3 H 2.895 . 2
229 32 32 LYS HG2 H 1.407 . 2
230 32 32 LYS HG3 H 1.408 . 2
231 32 32 LYS N N 119.328 . 1
232 33 33 LEU H H 7.780 . 1
233 33 33 LEU HA H 4.112 . 1
234 33 33 LEU HB2 H 1.541 . 2
235 33 33 LEU HB3 H 1.560 . 2
236 33 33 LEU HD1 H 0.779 . 2
237 33 33 LEU HD2 H 0.741 . 2
238 33 33 LEU HG H 1.264 . 1
239 33 33 LEU N N 119.522 . 1
240 34 34 TYR H H 7.600 . 1
241 34 34 TYR HA H 4.581 . 1
242 34 34 TYR HB2 H 2.881 . 2
243 34 34 TYR HB3 H 3.068 . 2
244 34 34 TYR HD1 H 7.048 . 3
245 34 34 TYR HD2 H 7.048 . 3
246 34 34 TYR HE1 H 6.705 . 3
247 34 34 TYR HE2 H 6.705 . 3
248 34 34 TYR N N 119.400 . 1
stop_
save_