data_5956
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR solution structure of Max in absence of DNA: Insight into the mechanism of
DNA recognition by B-HLH-LZ transcription factors
;
_BMRB_accession_number 5956
_BMRB_flat_file_name bmr5956.str
_Entry_type original
_Submission_date 2003-09-19
_Accession_date 2003-09-19
_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 Sauve Simon . .
2 Tremblay Luc . .
3 Lavigne Pierre . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 318
"13C chemical shifts" 239
"15N chemical shifts" 75
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2005-05-03 original BMRB .
stop_
_Original_release_date 2003-09-19
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA:
insights into the specific and reversible DNA binding mechanism of dimeric
transcription factors.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15342239
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Sauve S. . .
2 Tremblay L. . .
3 Lavigne P. . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_volume 342
_Journal_issue 3
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 813
_Page_last 832
_Year 2004
_Details .
save_
#######################################
# Cited references within the entry #
#######################################
save_references
_Saveframe_category citation
_Citation_full
;
Jean-Francois N, Frederic G, Raymund W, Benoit C, Lavigne P.
Improving the thermodynamic stability of the leucine zipper of max increases
the stability of its b-HLH-LZ:E-box complex.
J Mol Biol. 2003 Mar 7;326(5):1577-95.
;
_Citation_title
;
Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12595267
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Jean-Francois Naud . .
2 Frederic Gagnon . .
3 Raymund Wellinger . .
4 Benoit Chabot . .
5 Lavigne Pierre . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of molecular biology'
_Journal_volume 326
_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 1577
_Page_last 1595
_Year 2003
_Details
;
Max is a member of the b-HLH-LZ (basic region-helix1-loop-helix2-leucine zipper)
family of eukaryotic transcription factors. It is the obligate partner of the
related b-HLH-LZ proteins, c-Myc and Mad1, with which it forms heterodimers on
target DNA. While c-Myc and Mad1 require Max for DNA-binding, Max itself can
form a homodimer that recognizes E-box DNA sequences (CACGTG) in gene promoters
that are targeted by c-Myc. Evidence suggests that this mode of binding by Max
may repress c-Myc transcriptional activity, and this may have applications in
the control of the aberrant activity of c-Myc during certain oncogenic
transformations. To enhance this repressive potential of Max, we sought to
stabilize Max homodimers. We have designed a double mutant (N78V/H81L) located
in the coiled-coil interface of the leucine zipper domain and we demonstrate
that these mutations do indeed increase the stability of the protein. The
mutations also improve the stability of the complex with cognate DNA. Thermal
denaturations monitored by circular dichroism reveal two transitions that are
due to intermediate folding states for both the wild-type and mutant proteins;
this is supported by detailed thermodynamic analyses. A formalism to
characterize the temperature-dependence of the unfolding, including the effect
of intermediates, is presented.
;
save_
##################################
# Molecular system description #
##################################
save_system_Max_VL
_Saveframe_category molecular_system
_Mol_system_name 'Max*VL homodimer'
_Abbreviation_common Max*VL
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Max*VL subunit 1' $Max_VL_monomer
'Max*VL subunit 2' $Max_VL_monomer
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state dimer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
loop_
_Biological_function
'Transcription factor'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_Max_VL_monomer
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Max
_Name_variant 'N58V H61L'
_Abbreviation_common Max*VL
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 87
_Mol_residue_sequence
;
MADKRAHHNALERKRRDHIK
DSFHSLRDSVPSLQGEKASR
AQILDKATEYIQYMRRKVHT
LQQDIDDLKRQNALLEQQVR
ALEGSGC
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ALA 3 ASP 4 LYS 5 ARG
6 ALA 7 HIS 8 HIS 9 ASN 10 ALA
11 LEU 12 GLU 13 ARG 14 LYS 15 ARG
16 ARG 17 ASP 18 HIS 19 ILE 20 LYS
21 ASP 22 SER 23 PHE 24 HIS 25 SER
26 LEU 27 ARG 28 ASP 29 SER 30 VAL
31 PRO 32 SER 33 LEU 34 GLN 35 GLY
36 GLU 37 LYS 38 ALA 39 SER 40 ARG
41 ALA 42 GLN 43 ILE 44 LEU 45 ASP
46 LYS 47 ALA 48 THR 49 GLU 50 TYR
51 ILE 52 GLN 53 TYR 54 MET 55 ARG
56 ARG 57 LYS 58 VAL 59 HIS 60 THR
61 LEU 62 GLN 63 GLN 64 ASP 65 ILE
66 ASP 67 ASP 68 LEU 69 LYS 70 ARG
71 GLN 72 ASN 73 ALA 74 LEU 75 LEU
76 GLU 77 GLN 78 GLN 79 VAL 80 ARG
81 ALA 82 LEU 83 GLU 84 GLY 85 SER
86 GLY 87 CYS
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 1R05 'Solution Structure Of Max B-Hlh-Lz' 100.00 87 100.00 100.00 2.88e-43
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$Max_VL_monomer 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_type
_Vector_name
_Details
$Max_VL_monomer 'recombinant technology' 'E. coli' Escherichia coli BL21 pLysS plasmid pEt3a
;
For more information on the construction, please refer to
Jean-Francois, N. et al. J. Mol. Biol. (2003) 326, 1577-1595.
;
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
$Max_VL_monomer 30 mM [U-15N]
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$Max_VL_monomer 30 mM '[U-13C; U-15N]'
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UNITY-INOVA
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N HSQC'
_Sample_label .
save_
save_13C_HSQC_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C HSQC'
_Sample_label .
save_
save_15N_NOESY_HSQC_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N NOESY HSQC'
_Sample_label .
save_
save_13C_NOESY_HSQC_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C NOESY HSQC'
_Sample_label .
save_
save_13C_aromatic_NOESY_HSQC_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C aromatic NOESY HSQC'
_Sample_label .
save_
save_HNCA_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label .
save_
save_HN(CO)CA_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_Sample_label .
save_
save_HNCACB_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label .
save_
save_CBCA(CO)NH_9
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label .
save_
save_HCCH_TOCSY_10
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH TOCSY'
_Sample_label .
save_
save_HCCH_COSY_11
_Saveframe_category NMR_applied_experiment
_Experiment_name 'HCCH COSY'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_Expt_condition_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.8 . n/a
temperature 308 . 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 0.00 external indirect . . . .
DSS H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel 1.0
DSS N 15 'methyl protons' ppm 0.00 external indirect . . . .
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_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'15N HSQC'
'13C HSQC'
'15N NOESY HSQC'
'13C NOESY HSQC'
'13C aromatic NOESY HSQC'
HNCA
HN(CO)CA
HNCACB
CBCA(CO)NH
'HCCH TOCSY'
'HCCH COSY'
stop_
_Sample_conditions_label $Expt_condition_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'Max*VL subunit 1'
_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 . 2 ALA CA C 53.048 . 1
2 . 2 ALA CB C 19.232 . 1
3 . 2 ALA HB H 1.434 . 1
4 . 2 ALA C C 177.459 . 1
5 . 3 ASP N N 120.250 . 1
6 . 3 ASP H H 8.034 . 1
7 . 7 HIS N N 123.480 . 1
8 . 7 HIS H H 7.852 . 1
9 . 10 ALA CA C 52.608 . 1
10 . 10 ALA CB C 19.419 . 1
11 . 10 ALA C C 177.281 . 1
12 . 11 LEU N N 121.297 . 1
13 . 11 LEU H H 8.100 . 1
14 . 11 LEU CA C 56.755 . 1
15 . 11 LEU C C 176.366 . 1
16 . 15 ARG CA C 56.632 . 1
17 . 15 ARG CB C 33.031 . 1
18 . 15 ARG C C 179.023 . 1
19 . 16 ARG N N 121.514 . 1
20 . 16 ARG H H 8.309 . 1
21 . 17 ASP HA H 4.350 . 1
22 . 18 HIS CA C 63.015 . 1
23 . 18 HIS HA H 4.341 . 1
24 . 18 HIS HB3 H 3.280 . 2
25 . 18 HIS HB2 H 3.062 . 2
26 . 19 ILE N N 123.210 . 1
27 . 19 ILE H H 8.688 . 1
28 . 19 ILE CA C 63.714 . 1
29 . 19 ILE HA H 4.124 . 1
30 . 19 ILE CB C 39.057 . 1
31 . 19 ILE HG13 H 1.090 . 1
32 . 19 ILE C C 178.529 . 1
33 . 20 LYS N N 118.903 . 1
34 . 20 LYS H H 8.140 . 1
35 . 20 LYS CA C 59.172 . 1
36 . 20 LYS HA H 4.124 . 1
37 . 20 LYS CB C 29.918 . 1
38 . 20 LYS HB2 H 1.886 . 2
39 . 20 LYS HE2 H 3.061 . 2
40 . 20 LYS C C 177.234 . 1
41 . 21 ASP N N 115.353 . 1
42 . 21 ASP H H 8.330 . 1
43 . 21 ASP CA C 62.025 . 1
44 . 21 ASP HA H 4.302 . 1
45 . 22 SER CA C 59.740 . 1
46 . 22 SER C C 178.087 . 1
47 . 23 PHE N N 119.629 . 1
48 . 23 PHE H H 8.135 . 1
49 . 23 PHE CA C 56.988 . 1
50 . 23 PHE HA H 4.230 . 1
51 . 23 PHE CB C 42.177 . 1
52 . 23 PHE HB3 H 3.145 . 2
53 . 23 PHE CD1 C 132.000 . 3
54 . 23 PHE HD1 H 7.288 . 3
55 . 23 PHE CE1 C 129.500 . 3
56 . 23 PHE HE1 H 6.934 . 3
57 . 24 HIS N N 120.817 . 1
58 . 24 HIS H H 8.110 . 1
59 . 24 HIS CA C 57.299 . 1
60 . 24 HIS HA H 4.227 . 1
61 . 24 HIS CB C 30.600 . 1
62 . 25 SER H H 8.340 . 1
63 . 25 SER HA H 4.319 . 1
64 . 25 SER HB3 H 4.114 . 2
65 . 25 SER HB2 H 3.947 . 2
66 . 26 LEU N N 123.511 . 1
67 . 26 LEU H H 7.861 . 1
68 . 26 LEU CA C 58.620 . 1
69 . 26 LEU HA H 4.120 . 1
70 . 26 LEU CB C 41.260 . 1
71 . 26 LEU HB3 H 2.000 . 2
72 . 26 LEU HG H 1.335 . 1
73 . 26 LEU CD1 C 27.800 . 1
74 . 26 LEU HD1 H 0.913 . 2
75 . 26 LEU HD2 H 0.717 . 2
76 . 26 LEU C C 178.845 . 1
77 . 27 ARG N N 119.829 . 1
78 . 27 ARG H H 8.466 . 1
79 . 27 ARG CA C 59.797 . 1
80 . 27 ARG HA H 4.364 . 1
81 . 27 ARG CB C 29.886 . 1
82 . 27 ARG HB3 H 2.278 . 2
83 . 27 ARG HG3 H 1.248 . 2
84 . 27 ARG HG2 H 1.606 . 2
85 . 27 ARG C C 177.740 . 1
86 . 28 ASP N N 114.161 . 1
87 . 28 ASP H H 7.948 . 1
88 . 28 ASP CA C 56.093 . 1
89 . 28 ASP HA H 4.463 . 1
90 . 28 ASP CB C 40.129 . 1
91 . 28 ASP HB3 H 2.681 . 2
92 . 28 ASP HB2 H 2.823 . 2
93 . 28 ASP C C 176.989 . 1
94 . 29 SER N N 115.420 . 1
95 . 29 SER H H 7.912 . 1
96 . 29 SER CA C 59.890 . 1
97 . 29 SER HA H 4.286 . 1
98 . 29 SER CB C 64.420 . 1
99 . 29 SER C C 172.450 . 1
100 . 30 VAL N N 122.523 . 1
101 . 30 VAL H H 7.308 . 1
102 . 30 VAL CA C 59.382 . 1
103 . 30 VAL HA H 4.095 . 1
104 . 30 VAL CB C 33.020 . 1
105 . 30 VAL HB H 2.166 . 1
106 . 30 VAL CG2 C 21.250 . 1
107 . 30 VAL HG2 H 0.562 . 2
108 . 30 VAL HG1 H 0.939 . 2
109 . 31 PRO CA C 63.868 . 1
110 . 31 PRO HB3 H 1.888 . 2
111 . 32 SER N N 122.466 . 1
112 . 32 SER H H 8.044 . 1
113 . 32 SER CA C 59.754 . 1
114 . 32 SER HA H 4.100 . 1
115 . 32 SER CB C 62.544 . 1
116 . 32 SER HB3 H 3.530 . 2
117 . 32 SER C C 174.914 . 1
118 . 33 LEU N N 120.369 . 1
119 . 33 LEU H H 7.646 . 1
120 . 33 LEU CA C 54.361 . 1
121 . 33 LEU HA H 4.388 . 1
122 . 33 LEU CB C 43.533 . 1
123 . 33 LEU HB3 H 2.188 . 2
124 . 33 LEU HB2 H 2.029 . 2
125 . 33 LEU HG H 1.504 . 1
126 . 33 LEU HD1 H 0.943 . 2
127 . 33 LEU HD2 H 0.744 . 2
128 . 33 LEU C C 176.895 . 1
129 . 34 GLN N N 120.081 . 1
130 . 34 GLN H H 7.423 . 1
131 . 34 GLN CA C 57.818 . 1
132 . 34 GLN HA H 4.144 . 1
133 . 34 GLN CB C 28.243 . 1
134 . 34 GLN HB3 H 2.037 . 2
135 . 34 GLN HG3 H 2.396 . 2
136 . 35 GLY N N 112.512 . 1
137 . 35 GLY H H 8.725 . 1
138 . 35 GLY CA C 45.854 . 1
139 . 35 GLY HA3 H 3.767 . 2
140 . 35 GLY HA2 H 4.079 . 2
141 . 35 GLY C C 173.991 . 1
142 . 36 GLU N N 119.602 . 1
143 . 36 GLU H H 7.830 . 1
144 . 36 GLU CA C 55.449 . 1
145 . 36 GLU HA H 4.430 . 1
146 . 36 GLU CB C 31.375 . 1
147 . 36 GLU HB3 H 2.025 . 2
148 . 36 GLU HB2 H 1.831 . 2
149 . 36 GLU CG C 36.700 . 1
150 . 36 GLU HG3 H 2.244 . 2
151 . 36 GLU C C 176.530 . 1
152 . 37 LYS N N 123.347 . 1
153 . 37 LYS H H 8.498 . 1
154 . 37 LYS CA C 56.037 . 1
155 . 37 LYS HA H 4.341 . 1
156 . 37 LYS CB C 31.323 . 1
157 . 37 LYS C C 175.759 . 1
158 . 38 ALA N N 125.549 . 1
159 . 38 ALA H H 7.740 . 1
160 . 38 ALA CA C 51.429 . 1
161 . 38 ALA HA H 4.340 . 1
162 . 38 ALA CB C 21.620 . 1
163 . 38 ALA HB H 1.250 . 1
164 . 38 ALA C C 176.676 . 1
165 . 39 SER N N 118.235 . 1
166 . 39 SER H H 8.514 . 1
167 . 39 SER CA C 56.967 . 1
168 . 39 SER HA H 4.224 . 1
169 . 39 SER CB C 65.310 . 1
170 . 39 SER HB3 H 3.830 . 2
171 . 40 ARG CA C 60.897 . 1
172 . 40 ARG CB C 30.100 . 1
173 . 40 ARG HG3 H 1.596 . 2
174 . 40 ARG C C 177.751 . 1
175 . 41 ALA N N 118.857 . 1
176 . 41 ALA H H 8.283 . 1
177 . 41 ALA CA C 55.737 . 1
178 . 41 ALA HA H 3.798 . 1
179 . 41 ALA CB C 18.039 . 1
180 . 41 ALA HB H 1.212 . 1
181 . 41 ALA C C 178.777 . 1
182 . 42 GLN N N 116.075 . 1
183 . 42 GLN H H 7.386 . 1
184 . 42 GLN CA C 58.938 . 1
185 . 42 GLN HA H 4.110 . 1
186 . 42 GLN CB C 28.900 . 1
187 . 42 GLN HB3 H 1.950 . 2
188 . 42 GLN HB2 H 1.970 . 2
189 . 42 GLN CG C 34.050 . 1
190 . 42 GLN HG3 H 2.310 . 2
191 . 42 GLN HG2 H 2.414 . 2
192 . 42 GLN NE2 N 109.200 . 1
193 . 42 GLN HE21 H 7.020 . 2
194 . 42 GLN HE22 H 6.667 . 2
195 . 42 GLN C C 178.678 . 1
196 . 43 ILE N N 119.552 . 1
197 . 43 ILE H H 8.298 . 1
198 . 43 ILE CA C 65.834 . 1
199 . 43 ILE HA H 3.556 . 1
200 . 43 ILE CB C 38.750 . 1
201 . 43 ILE HB H 1.810 . 1
202 . 43 ILE CG1 C 27.500 . 2
203 . 43 ILE HG13 H 1.330 . 1
204 . 43 ILE CD1 C 12.810 . 1
205 . 43 ILE HD1 H 0.835 . 1
206 . 43 ILE CG2 C 17.810 . 1
207 . 43 ILE HG2 H 1.078 . 1
208 . 43 ILE C C 177.254 . 1
209 . 44 LEU N N 116.700 . 1
210 . 44 LEU H H 7.857 . 1
211 . 44 LEU CA C 58.505 . 1
212 . 44 LEU HA H 3.788 . 1
213 . 44 LEU CB C 42.385 . 1
214 . 44 LEU HB3 H 1.913 . 2
215 . 44 LEU HB2 H 1.554 . 2
216 . 44 LEU CG C 26.250 . 1
217 . 44 LEU CD1 C 23.750 . 1
218 . 44 LEU HD1 H 0.200 . 2
219 . 44 LEU CD2 C 26.400 . 1
220 . 44 LEU HD2 H 0.217 . 2
221 . 44 LEU C C 179.263 . 1
222 . 45 ASP N N 120.116 . 1
223 . 45 ASP H H 8.500 . 1
224 . 45 ASP CA C 57.881 . 1
225 . 45 ASP HA H 4.440 . 1
226 . 45 ASP CB C 40.402 . 1
227 . 45 ASP HB3 H 2.742 . 2
228 . 45 ASP C C 179.787 . 1
229 . 46 LYS N N 119.724 . 1
230 . 46 LYS H H 8.837 . 1
231 . 46 LYS CA C 58.113 . 1
232 . 46 LYS HA H 4.241 . 1
233 . 46 LYS CB C 31.101 . 1
234 . 46 LYS HB3 H 1.577 . 2
235 . 46 LYS HB2 H 2.119 . 2
236 . 46 LYS C C 180.182 . 1
237 . 47 ALA N N 124.062 . 1
238 . 47 ALA H H 8.711 . 1
239 . 47 ALA CA C 56.201 . 1
240 . 47 ALA HA H 4.240 . 1
241 . 47 ALA CB C 18.683 . 1
242 . 47 ALA HB H 1.540 . 1
243 . 47 ALA C C 178.767 . 1
244 . 48 THR N N 116.736 . 1
245 . 48 THR H H 8.191 . 1
246 . 48 THR CA C 68.138 . 1
247 . 48 THR HA H 4.380 . 1
248 . 48 THR CB C 68.193 . 1
249 . 48 THR HB H 3.770 . 1
250 . 48 THR CG2 C 22.190 . 1
251 . 48 THR HG2 H 1.160 . 1
252 . 48 THR C C 176.508 . 1
253 . 49 GLU N N 120.524 . 1
254 . 49 GLU H H 7.877 . 1
255 . 49 GLU CA C 59.686 . 1
256 . 49 GLU HA H 4.074 . 1
257 . 49 GLU CB C 30.537 . 1
258 . 49 GLU HB3 H 2.010 . 2
259 . 49 GLU CG C 36.250 . 1
260 . 49 GLU HG3 H 2.200 . 2
261 . 49 GLU HG2 H 2.478 . 2
262 . 49 GLU C C 179.005 . 1
263 . 50 TYR N N 121.976 . 1
264 . 50 TYR H H 8.517 . 1
265 . 50 TYR CA C 60.858 . 1
266 . 50 TYR HA H 4.410 . 1
267 . 50 TYR CB C 39.400 . 1
268 . 50 TYR HB3 H 3.372 . 2
269 . 50 TYR HB2 H 3.114 . 2
270 . 50 TYR CE1 C 118.300 . 3
271 . 50 TYR HE1 H 6.940 . 3
272 . 50 TYR CD1 C 132.630 . 3
273 . 50 TYR HD1 H 7.170 . 3
274 . 50 TYR C C 177.857 . 1
275 . 51 ILE N N 120.056 . 1
276 . 51 ILE H H 8.754 . 1
277 . 51 ILE CA C 67.320 . 1
278 . 51 ILE HA H 3.415 . 1
279 . 51 ILE CB C 37.833 . 1
280 . 51 ILE HB H 2.030 . 1
281 . 51 ILE CD1 C 14.370 . 1
282 . 51 ILE HD1 H 0.967 . 1
283 . 51 ILE CG2 C 18.440 . 1
284 . 51 ILE HG2 H 1.185 . 1
285 . 51 ILE C C 177.910 . 1
286 . 52 GLN N N 117.829 . 1
287 . 52 GLN H H 8.120 . 1
288 . 52 GLN CA C 59.594 . 1
289 . 52 GLN HA H 4.090 . 1
290 . 52 GLN CB C 27.569 . 1
291 . 52 GLN HB3 H 2.192 . 2
292 . 52 GLN HB2 H 1.865 . 2
293 . 52 GLN HG3 H 2.707 . 2
294 . 52 GLN HG2 H 2.571 . 2
295 . 52 GLN NE2 N 110.610 . 1
296 . 52 GLN HE21 H 7.240 . 2
297 . 52 GLN HE22 H 6.820 . 2
298 . 52 GLN C C 179.020 . 1
299 . 53 TYR N N 121.466 . 1
300 . 53 TYR H H 8.300 . 1
301 . 53 TYR CA C 61.215 . 1
302 . 53 TYR HA H 4.260 . 1
303 . 53 TYR CB C 38.353 . 1
304 . 53 TYR HB3 H 3.374 . 2
305 . 53 TYR CE1 C 118.300 . 3
306 . 53 TYR HE1 H 6.952 . 3
307 . 53 TYR CD1 C 133.880 . 3
308 . 53 TYR HD1 H 7.110 . 3
309 . 53 TYR C C 177.810 . 1
310 . 54 MET N N 120.370 . 1
311 . 54 MET H H 8.740 . 1
312 . 54 MET CA C 57.947 . 1
313 . 54 MET HA H 3.920 . 1
314 . 54 MET CB C 32.800 . 1
315 . 54 MET HB3 H 2.020 . 2
316 . 54 MET CE C 18.380 . 1
317 . 54 MET HE H 1.840 . 1
318 . 54 MET C C 178.104 . 1
319 . 55 ARG N N 119.752 . 1
320 . 55 ARG H H 8.677 . 1
321 . 55 ARG CA C 60.411 . 1
322 . 55 ARG HA H 3.880 . 1
323 . 55 ARG CB C 30.509 . 1
324 . 55 ARG HB3 H 2.030 . 2
325 . 55 ARG CG C 28.120 . 1
326 . 55 ARG HG3 H 1.860 . 2
327 . 55 ARG HG2 H 1.616 . 2
328 . 55 ARG C C 179.628 . 1
329 . 56 ARG N N 119.607 . 1
330 . 56 ARG H H 7.618 . 1
331 . 56 ARG CA C 59.365 . 1
332 . 56 ARG HA H 4.148 . 1
333 . 56 ARG CB C 29.963 . 1
334 . 56 ARG HB2 H 1.949 . 2
335 . 56 ARG HG3 H 1.653 . 2
336 . 56 ARG HG2 H 1.313 . 2
337 . 56 ARG HD3 H 3.285 . 2
338 . 56 ARG C C 178.595 . 1
339 . 57 LYS N N 122.937 . 1
340 . 57 LYS H H 8.249 . 1
341 . 57 LYS CA C 59.205 . 1
342 . 57 LYS HA H 3.960 . 1
343 . 57 LYS CB C 31.873 . 1
344 . 57 LYS HB2 H 1.855 . 2
345 . 57 LYS HG3 H 1.482 . 2
346 . 57 LYS HG2 H 1.860 . 2
347 . 57 LYS HD2 H 1.312 . 2
348 . 57 LYS HE2 H 3.294 . 2
349 . 57 LYS C C 178.445 . 1
350 . 58 VAL N N 118.280 . 1
351 . 58 VAL H H 8.505 . 1
352 . 58 VAL CA C 67.537 . 1
353 . 58 VAL HA H 3.432 . 1
354 . 58 VAL CB C 31.654 . 1
355 . 58 VAL HB H 2.078 . 1
356 . 58 VAL CG2 C 24.690 . 1
357 . 58 VAL HG2 H 0.722 . 2
358 . 58 VAL HG1 H 0.951 . 2
359 . 58 VAL C C 177.148 . 1
360 . 59 HIS N N 117.810 . 1
361 . 59 HIS H H 7.559 . 1
362 . 59 HIS CA C 60.113 . 1
363 . 59 HIS HA H 4.389 . 1
364 . 59 HIS CB C 30.511 . 1
365 . 59 HIS HB3 H 3.298 . 2
366 . 59 HIS HB2 H 2.307 . 2
367 . 59 HIS C C 178.277 . 1
368 . 60 THR N N 115.741 . 1
369 . 60 THR H H 8.379 . 1
370 . 60 THR CA C 66.699 . 1
371 . 60 THR HA H 3.947 . 1
372 . 60 THR CB C 69.185 . 1
373 . 60 THR HB H 4.350 . 1
374 . 60 THR CG2 C 21.870 . 1
375 . 60 THR HG2 H 1.325 . 1
376 . 60 THR C C 176.505 . 1
377 . 61 LEU N N 122.310 . 1
378 . 61 LEU H H 8.552 . 1
379 . 61 LEU CA C 58.187 . 1
380 . 61 LEU HA H 4.205 . 1
381 . 61 LEU CB C 42.422 . 1
382 . 61 LEU HB2 H 1.995 . 2
383 . 61 LEU CG C 24.500 . 1
384 . 61 LEU HG H 1.317 . 1
385 . 61 LEU HD1 H 0.912 . 2
386 . 61 LEU C C 179.210 . 1
387 . 62 GLN N N 117.403 . 1
388 . 62 GLN H H 8.411 . 1
389 . 62 GLN CA C 59.217 . 1
390 . 62 GLN HA H 3.976 . 1
391 . 62 GLN CB C 28.324 . 1
392 . 62 GLN HB3 H 2.053 . 2
393 . 62 GLN CG C 34.300 . 1
394 . 62 GLN HG3 H 2.558 . 2
395 . 62 GLN HG2 H 2.312 . 2
396 . 62 GLN NE2 N 112.185 . 1
397 . 62 GLN HE21 H 7.356 . 2
398 . 62 GLN HE22 H 6.800 . 2
399 . 62 GLN C C 178.550 . 1
400 . 63 GLN N N 119.400 . 1
401 . 63 GLN H H 7.745 . 1
402 . 63 GLN CA C 59.046 . 1
403 . 63 GLN HA H 4.119 . 1
404 . 63 GLN CB C 28.257 . 1
405 . 63 GLN HB3 H 2.076 . 2
406 . 63 GLN HB2 H 2.241 . 2
407 . 63 GLN NE2 N 113.200 . 1
408 . 63 GLN HE21 H 7.310 . 2
409 . 63 GLN HE22 H 6.823 . 2
410 . 63 GLN C C 178.484 . 1
411 . 64 ASP N N 121.785 . 1
412 . 64 ASP H H 8.180 . 1
413 . 64 ASP CA C 57.924 . 1
414 . 64 ASP HA H 4.470 . 1
415 . 64 ASP CB C 40.800 . 1
416 . 64 ASP HB3 H 3.030 . 2
417 . 64 ASP C C 179.604 . 1
418 . 65 ILE N N 121.700 . 1
419 . 65 ILE H H 8.401 . 1
420 . 65 ILE CA C 66.021 . 1
421 . 65 ILE HA H 3.601 . 1
422 . 65 ILE CB C 37.988 . 1
423 . 65 ILE HB H 1.857 . 1
424 . 65 ILE HG13 H 1.334 . 1
425 . 65 ILE CD1 C 16.870 . 1
426 . 65 ILE HD1 H 0.916 . 1
427 . 65 ILE CG2 C 15.500 . 1
428 . 65 ILE HG2 H 1.000 . 1
429 . 65 ILE C C 177.149 . 1
430 . 66 ASP N N 121.300 . 1
431 . 66 ASP H H 8.050 . 1
432 . 66 ASP CA C 58.154 . 1
433 . 66 ASP HA H 4.383 . 1
434 . 66 ASP CB C 40.453 . 1
435 . 66 ASP HB3 H 2.721 . 2
436 . 66 ASP C C 179.531 . 1
437 . 67 ASP N N 120.268 . 1
438 . 67 ASP H H 8.163 . 1
439 . 67 ASP CA C 57.947 . 1
440 . 67 ASP HA H 4.490 . 1
441 . 67 ASP CB C 41.325 . 1
442 . 67 ASP HB3 H 2.760 . 2
443 . 67 ASP HB2 H 2.902 . 2
444 . 67 ASP C C 179.087 . 1
445 . 68 LEU N N 122.026 . 1
446 . 68 LEU H H 8.406 . 1
447 . 68 LEU CA C 58.409 . 1
448 . 68 LEU HA H 4.000 . 1
449 . 68 LEU CB C 43.644 . 1
450 . 68 LEU HB3 H 1.315 . 2
451 . 68 LEU HB2 H 2.070 . 2
452 . 68 LEU HG H 1.840 . 1
453 . 68 LEU CD1 C 23.530 . 1
454 . 68 LEU HD1 H 0.930 . 2
455 . 68 LEU CD2 C 24.050 . 1
456 . 68 LEU HD2 H 0.910 . 2
457 . 68 LEU C C 179.939 . 1
458 . 69 LYS N N 120.455 . 1
459 . 69 LYS H H 9.019 . 1
460 . 69 LYS CA C 60.619 . 1
461 . 69 LYS HA H 3.983 . 1
462 . 69 LYS CB C 32.448 . 1
463 . 69 LYS HB2 H 1.650 . 2
464 . 69 LYS HG3 H 1.425 . 2
465 . 69 LYS HG2 H 1.384 . 2
466 . 69 LYS C C 180.041 . 1
467 . 70 ARG N N 121.500 . 1
468 . 70 ARG H H 7.871 . 1
469 . 70 ARG CA C 59.836 . 1
470 . 70 ARG HA H 4.144 . 1
471 . 70 ARG CB C 29.948 . 1
472 . 70 ARG HB3 H 1.876 . 2
473 . 70 ARG HB2 H 2.077 . 2
474 . 70 ARG CG C 28.100 . 1
475 . 70 ARG HG3 H 1.578 . 2
476 . 70 ARG HD3 H 2.749 . 2
477 . 70 ARG HD2 H 3.291 . 2
478 . 70 ARG C C 179.190 . 1
479 . 71 GLN N N 119.398 . 1
480 . 71 GLN H H 8.247 . 1
481 . 71 GLN CA C 59.119 . 1
482 . 71 GLN HA H 4.096 . 1
483 . 71 GLN CB C 28.718 . 1
484 . 71 GLN HB3 H 2.100 . 2
485 . 71 GLN HG3 H 2.440 . 2
486 . 71 GLN HG2 H 2.503 . 2
487 . 71 GLN NE2 N 111.290 . 1
488 . 71 GLN HE21 H 6.760 . 2
489 . 71 GLN HE22 H 7.270 . 2
490 . 71 GLN C C 178.476 . 1
491 . 72 ASN N N 119.924 . 1
492 . 72 ASN H H 8.764 . 1
493 . 72 ASN CA C 57.232 . 1
494 . 72 ASN HA H 4.296 . 1
495 . 72 ASN CB C 38.711 . 1
496 . 72 ASN HB3 H 2.731 . 2
497 . 72 ASN HB2 H 3.205 . 2
498 . 72 ASN ND2 N 106.339 . 1
499 . 72 ASN HD21 H 6.611 . 2
500 . 72 ASN HD22 H 7.641 . 2
501 . 72 ASN C C 176.765 . 1
502 . 73 ALA N N 121.453 . 1
503 . 73 ALA H H 7.908 . 1
504 . 73 ALA CA C 55.225 . 1
505 . 73 ALA HA H 4.179 . 1
506 . 73 ALA CB C 18.050 . 1
507 . 73 ALA HB H 1.564 . 1
508 . 73 ALA C C 181.010 . 1
509 . 74 LEU N N 119.748 . 1
510 . 74 LEU H H 7.718 . 1
511 . 74 LEU CA C 58.200 . 1
512 . 74 LEU HA H 4.122 . 1
513 . 74 LEU CB C 41.912 . 1
514 . 74 LEU HB3 H 1.845 . 2
515 . 74 LEU HB2 H 1.582 . 2
516 . 74 LEU HG H 1.323 . 1
517 . 74 LEU HD1 H 0.919 . 2
518 . 74 LEU C C 180.335 . 1
519 . 75 LEU N N 121.460 . 1
520 . 75 LEU H H 8.250 . 1
521 . 75 LEU CA C 58.222 . 1
522 . 75 LEU HA H 4.116 . 1
523 . 75 LEU CB C 43.752 . 1
524 . 75 LEU HB3 H 2.190 . 2
525 . 75 LEU HG H 1.644 . 1
526 . 75 LEU HD1 H 0.969 . 2
527 . 75 LEU HD2 H 0.898 . 2
528 . 75 LEU C C 178.973 . 1
529 . 76 GLU N N 119.469 . 1
530 . 76 GLU H H 8.659 . 1
531 . 76 GLU CA C 60.400 . 1
532 . 76 GLU HA H 3.904 . 1
533 . 76 GLU CB C 29.554 . 1
534 . 76 GLU HB3 H 2.142 . 2
535 . 76 GLU HB2 H 2.077 . 2
536 . 76 GLU CG C 37.200 . 1
537 . 76 GLU HG3 H 2.434 . 2
538 . 76 GLU HG2 H 2.200 . 2
539 . 76 GLU C C 179.362 . 1
540 . 77 GLN N N 117.636 . 1
541 . 77 GLN H H 7.763 . 1
542 . 77 GLN CA C 59.008 . 1
543 . 77 GLN HA H 4.000 . 1
544 . 77 GLN CB C 28.299 . 1
545 . 77 GLN HB3 H 1.882 . 2
546 . 77 GLN HG3 H 2.562 . 2
547 . 77 GLN HG2 H 2.256 . 2
548 . 77 GLN C C 178.733 . 1
549 . 78 GLN N N 121.481 . 1
550 . 78 GLN H H 8.031 . 1
551 . 78 GLN CA C 59.232 . 1
552 . 78 GLN HA H 4.151 . 1
553 . 78 GLN CB C 28.734 . 1
554 . 78 GLN HB2 H 2.171 . 2
555 . 78 GLN CG C 34.430 . 1
556 . 78 GLN HG3 H 2.336 . 2
557 . 78 GLN HG2 H 2.569 . 2
558 . 78 GLN C C 178.526 . 1
559 . 79 VAL N N 119.675 . 1
560 . 79 VAL H H 8.404 . 1
561 . 79 VAL CA C 67.490 . 1
562 . 79 VAL HA H 3.458 . 1
563 . 79 VAL CB C 31.805 . 1
564 . 79 VAL HB H 2.160 . 1
565 . 79 VAL CG2 C 21.500 . 1
566 . 79 VAL HG2 H 0.878 . 2
567 . 79 VAL CG1 C 24.110 . 1
568 . 79 VAL HG1 H 1.010 . 2
569 . 79 VAL C C 177.896 . 1
570 . 80 ARG N N 117.434 . 1
571 . 80 ARG H H 7.829 . 1
572 . 80 ARG CA C 59.040 . 1
573 . 80 ARG HA H 4.100 . 1
574 . 80 ARG CB C 30.221 . 1
575 . 80 ARG HB3 H 1.906 . 2
576 . 80 ARG HB2 H 2.150 . 2
577 . 80 ARG HG3 H 1.533 . 2
578 . 80 ARG HD2 H 3.236 . 2
579 . 80 ARG C C 179.464 . 1
580 . 81 ALA N N 121.568 . 1
581 . 81 ALA H H 7.995 . 1
582 . 81 ALA CA C 54.619 . 1
583 . 81 ALA HA H 4.181 . 1
584 . 81 ALA CB C 18.307 . 1
585 . 81 ALA HB H 1.534 . 1
586 . 81 ALA C C 180.228 . 1
587 . 82 LEU N N 119.358 . 1
588 . 82 LEU H H 8.020 . 1
589 . 82 LEU CA C 56.882 . 1
590 . 82 LEU HA H 4.120 . 1
591 . 82 LEU CB C 43.556 . 1
592 . 82 LEU HB3 H 1.904 . 2
593 . 82 LEU HG H 1.519 . 1
594 . 82 LEU HD1 H 0.940 . 2
595 . 82 LEU CD2 C 24.390 . 1
596 . 82 LEU C C 179.294 . 1
597 . 83 GLU N N 120.282 . 1
598 . 83 GLU H H 8.366 . 1
599 . 83 GLU CA C 58.848 . 1
600 . 83 GLU HA H 4.132 . 1
601 . 83 GLU CB C 29.979 . 1
602 . 83 GLU HB3 H 2.010 . 2
603 . 83 GLU HB2 H 2.180 . 2
604 . 83 GLU CG C 36.560 . 1
605 . 83 GLU HG3 H 2.481 . 2
606 . 83 GLU C C 178.396 . 1
607 . 84 GLY N N 107.735 . 1
608 . 84 GLY H H 8.103 . 1
609 . 84 GLY CA C 45.954 . 1
610 . 84 GLY HA3 H 3.950 . 2
611 . 84 GLY C C 174.810 . 1
612 . 85 SER N N 115.624 . 1
613 . 85 SER H H 7.822 . 1
614 . 85 SER CA C 59.024 . 1
615 . 85 SER HA H 4.520 . 1
616 . 85 SER CB C 64.227 . 1
617 . 85 SER HB3 H 4.069 . 2
618 . 85 SER HB2 H 4.050 . 2
619 . 85 SER C C 174.779 . 1
620 . 86 GLY N N 110.396 . 1
621 . 86 GLY H H 8.232 . 1
622 . 86 GLY CA C 45.688 . 1
623 . 86 GLY HA3 H 3.970 . 2
624 . 86 GLY HA2 H 4.064 . 2
625 . 86 GLY C C 173.489 . 1
626 . 87 CYS N N 123.760 . 1
627 . 87 CYS H H 7.944 . 1
628 . 87 CYS CA C 57.645 . 1
629 . 87 CYS HA H 4.475 . 1
630 . 87 CYS CB C 43.300 . 1
631 . 87 CYS HB3 H 3.278 . 2
632 . 87 CYS HB2 H 3.008 . 2
stop_
save_