data_4874
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Sequence-specific assignment of the PAH2 domain of Sin3B free and complexed to
Mad1
;
_BMRB_accession_number 4874
_BMRB_flat_file_name bmr4874.str
_Entry_type original
_Submission_date 2000-10-23
_Accession_date 2000-10-23
_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 Spronk Christian A.E.M. .
2 Jansen Jacobus F.A. .
3 Tessari Marco . .
4 Kaan Anita M. .
5 Aelen Jan . .
6 Vermeulen Michiel . .
7 Stunnenberg Hendrik G. .
8 Vuister Geerten W. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 102
"13C chemical shifts" 296
"15N chemical shifts" 102
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-04-26 original author .
stop_
_Original_release_date 2001-04-26
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the editor:
Sequence-specific assignment of the PAH2 domain of Sin3B free and bound
to Mad1
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Spronk Christian A.E.M. .
2 Jansen Jacobus F.A. .
3 Tessari Marco . .
4 Kaan Anita M. .
5 Aelen Jan . .
6 Lasonder Edwin . .
7 Stunnenberg Hendrik G. .
8 Vuister Geerten W. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume 19
_Journal_issue 4
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 377
_Page_last 378
_Year 2001
_Details .
loop_
_Keyword
Sin3
Mad1
'transcriptional regulator'
'protein-peptide complex'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_citation_1
_Saveframe_category citation
_Citation_full
;
Delaglio, F. et al. J. Biomol. NMR 6,
277-293 (1995)
;
_Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8520220
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Delaglio F. . .
2 Grzesiek S. . .
3 Vuister 'G. W.' W. .
4 Zhu G. . .
5 Pfeifer J. . .
6 Bax A. . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 6
_Journal_issue 3
_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 277
_Page_last 293
_Year 1995
_Details
;
The NMRPipe system is a UNIX software environment of processing, graphics, and
analysis tools designed to meet current routine and research-oriented
multidimensional processing requirements, and to anticipate and accommodate
future demands and developments. The system is based on UNIX pipes, which allow
programs running simultaneously to exchange streams of data under user control.
In an NMRPipe processing scheme, a stream of spectral data flows through a
pipeline of processing programs, each of which performs one component of the
overall scheme, such as Fourier transformation or linear prediction. Complete
multidimensional processing schemes are constructed as simple UNIX shell
scripts. The processing modules themselves maintain and exploit accurate
records of data sizes, detection modes, and calibration information in all
dimensions, so that schemes can be constructed without the need to explicitly
define or anticipate data sizes or storage details of real and imaginary
channels during processing. The asynchronous pipeline scheme provides other
substantial advantages, including high flexibility, favorable processing
speeds, choice of both all-in-memory and disk-bound processing, easy adaptation
to different data formats, simpler software development and maintenance, and
the ability to distribute processing tasks on multi-CPU computers and computer
networks.
;
save_
save_citation_2
_Saveframe_category citation
_Citation_full 'Ch. Bartels, et al. J. Biomol. NMR 6, 1-10 (1995).'
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_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 .
_Page_last .
_Year .
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_mSin3B-PAH2
_Saveframe_category molecular_system
_Mol_system_name 'mSin3B-PAH2 free state'
_Abbreviation_common mSin3B-PAH2
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
PAH2 $mSin3B-PAH2
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
loop_
_Biological_function
'transcriptional regulator'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_mSin3B-PAH2
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'mSin3B-PAH2 domain'
_Abbreviation_common mSin3B-PAH2
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 105
_Mol_residue_sequence
;
ESDSVEFNNAISYVNKIKTR
FLDHPEIYRSFLEILHTYQK
EQLHTKGRPFRGMSEEEVFT
EVANLFRGQEDLLSEFGQFL
PEAKRSLFTGNGSAEMNSGQ
KNEEK
;
loop_
_Residue_seq_code
_Residue_label
1 GLU 2 SER 3 ASP 4 SER 5 VAL
6 GLU 7 PHE 8 ASN 9 ASN 10 ALA
11 ILE 12 SER 13 TYR 14 VAL 15 ASN
16 LYS 17 ILE 18 LYS 19 THR 20 ARG
21 PHE 22 LEU 23 ASP 24 HIS 25 PRO
26 GLU 27 ILE 28 TYR 29 ARG 30 SER
31 PHE 32 LEU 33 GLU 34 ILE 35 LEU
36 HIS 37 THR 38 TYR 39 GLN 40 LYS
41 GLU 42 GLN 43 LEU 44 HIS 45 THR
46 LYS 47 GLY 48 ARG 49 PRO 50 PHE
51 ARG 52 GLY 53 MET 54 SER 55 GLU
56 GLU 57 GLU 58 VAL 59 PHE 60 THR
61 GLU 62 VAL 63 ALA 64 ASN 65 LEU
66 PHE 67 ARG 68 GLY 69 GLN 70 GLU
71 ASP 72 LEU 73 LEU 74 SER 75 GLU
76 PHE 77 GLY 78 GLN 79 PHE 80 LEU
81 PRO 82 GLU 83 ALA 84 LYS 85 ARG
86 SER 87 LEU 88 PHE 89 THR 90 GLY
91 ASN 92 GLY 93 SER 94 ALA 95 GLU
96 MET 97 ASN 98 SER 99 GLY 100 GLN
101 LYS 102 ASN 103 GLU 104 GLU 105 LYS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-29
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 5457 PAH2 100.00 105 100.00 100.00 2.50e-69
BMRB 6899 PAH2 100.00 105 100.00 100.00 2.50e-69
PDB 1E91 "Structure Of The Complex Of The Mad1-Sin3b Interaction Domains" 80.95 85 100.00 100.00 3.07e-54
PDB 1PD7 "Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b" 80.95 85 100.00 100.00 3.07e-54
PDB 2F05 "Solution Structure Of Free Pah2 Domain Of Msin3b" 100.00 105 99.05 99.05 9.79e-69
GB AAH51536 "Sin3b protein, partial [Mus musculus]" 100.00 190 99.05 99.05 3.20e-68
GB EDL10815 "transcriptional regulator, SIN3B (yeast), isoform CRA_c [Mus musculus]" 100.00 893 99.05 99.05 2.94e-63
GB EDL90863 "rCG38713, isoform CRA_e [Rattus norvegicus]" 100.00 231 98.10 98.10 1.55e-66
GB EDL90864 "rCG38713, isoform CRA_f [Rattus norvegicus]" 100.00 841 98.10 98.10 1.31e-62
REF XP_006751561 "PREDICTED: paired amphipathic helix protein Sin3b-like [Leptonychotes weddellii]" 82.86 342 98.85 98.85 3.37e-52
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Gene_mnemonic
$mSin3B-PAH2 Mouse 10090 Eukaryota Metazoa Mus musculus SIN3B
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_type
_Vector_name
$mSin3B-PAH2 'recombinant technology' 'E. coli' Escherichia coli pBL21 plasmid pGEX2T
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_Typical_sample
_Saveframe_category sample
_Sample_type solution
_Details
;
Trace amounts of Sodium azide and
protease inhibitors were added for
conservation
;
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$mSin3B-PAH2 1.0 mM '[U-100% 13C; U-100% 15N]'
'Potassium Phosphate' 50 mM .
'Potassium Chloride' 100 mM .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 1.7
loop_
_Task
'Data processing'
stop_
_Details .
_Citation_label $citation_1
save_
save_XEASY
_Saveframe_category software
_Name XEASY
_Version 1.3.9
loop_
_Task
'Spectral analysis'
stop_
_Details .
_Citation_label $citation_2
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Inova
_Field_strength 500
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_HNCA_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label $Typical_sample
save_
save_HNCO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label $Typical_sample
save_
save_CBCA(CO)NNH_3
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NNH
_Sample_label $Typical_sample
save_
save_HNCACB_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label $Typical_sample
save_
#######################
# Sample conditions #
#######################
save_sample_conditions
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.5 0.1 na
temperature 293 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 . . . 1.000000000
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
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_chemical_shifts
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$Typical_sample
stop_
_Sample_conditions_label $sample_conditions
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name PAH2
_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 GLU CA C 57.582 0.200 1
2 . 1 GLU CB C 30.111 0.300 1
3 . 1 GLU C C 177.008 0.100 1
4 . 1 GLU H H 8.902 0.030 1
5 . 1 GLU N N 123.045 0.200 1
6 . 2 SER CA C 58.802 0.200 1
7 . 2 SER CB C 64.062 0.300 1
8 . 2 SER C C 174.483 0.100 1
9 . 2 SER H H 8.277 0.030 1
10 . 2 SER N N 115.643 0.200 1
11 . 3 ASP CA C 54.787 0.200 1
12 . 3 ASP CB C 41.618 0.300 1
13 . 3 ASP C C 176.495 0.100 1
14 . 3 ASP H H 8.210 0.030 1
15 . 3 ASP N N 122.305 0.200 1
16 . 4 SER CA C 58.511 0.200 1
17 . 4 SER CB C 64.403 0.300 1
18 . 4 SER C C 175.144 0.100 1
19 . 4 SER H H 8.214 0.030 1
20 . 4 SER N N 115.766 0.200 1
21 . 5 VAL CA C 63.972 0.200 1
22 . 5 VAL CB C 32.913 0.300 1
23 . 5 VAL C C 176.880 0.100 1
24 . 5 VAL H H 8.258 0.030 1
25 . 5 VAL N N 122.922 0.200 1
26 . 6 GLU CA C 58.206 0.200 1
27 . 6 GLU CB C 30.339 0.300 1
28 . 6 GLU C C 177.479 0.100 1
29 . 6 GLU H H 8.492 0.030 1
30 . 6 GLU N N 122.181 0.200 1
31 . 7 PHE CA C 59.354 0.200 1
32 . 7 PHE CB C 39.877 0.300 1
33 . 7 PHE C C 176.066 0.100 1
34 . 7 PHE H H 8.255 0.030 1
35 . 7 PHE N N 121.071 0.200 1
36 . 8 ASN CA C 54.811 0.200 1
37 . 8 ASN CB C 39.044 0.300 1
38 . 8 ASN C C 176.773 0.100 1
39 . 8 ASN H H 8.295 0.030 1
40 . 8 ASN N N 119.221 0.200 1
41 . 9 ASN CA C 54.972 0.200 1
42 . 9 ASN CB C 38.854 0.300 1
43 . 9 ASN C C 177.008 0.100 1
44 . 9 ASN H H 8.647 0.030 1
45 . 9 ASN N N 119.961 0.200 1
46 . 10 ALA CA C 55.200 0.200 1
47 . 10 ALA CB C 18.997 0.300 1
48 . 10 ALA C C 178.972 0.100 1
49 . 10 ALA H H 8.354 0.030 1
50 . 10 ALA N N 124.772 0.200 1
51 . 11 ILE CA C 63.110 0.200 1
52 . 11 ILE CB C 38.086 0.300 1
53 . 11 ILE C C 178.283 0.100 1
54 . 11 ILE H H 8.100 0.030 1
55 . 11 ILE N N 118.234 0.200 1
56 . 12 SER CA C 61.516 0.200 1
57 . 12 SER C C 176.923 0.100 1
58 . 12 SER H H 8.186 0.030 1
59 . 12 SER N N 116.753 0.200 1
60 . 13 TYR CA C 61.641 0.200 1
61 . 13 TYR CB C 41.919 0.300 1
62 . 13 TYR C C 176.976 0.100 1
63 . 13 TYR H H 8.092 0.030 1
64 . 13 TYR N N 123.785 0.200 1
65 . 14 VAL CA C 67.305 0.200 1
66 . 14 VAL CB C 30.169 0.300 1
67 . 14 VAL C C 178.018 0.100 1
68 . 14 VAL H H 8.279 0.030 1
69 . 14 VAL N N 115.520 0.200 1
70 . 15 ASN CA C 56.075 0.200 1
71 . 15 ASN CB C 38.614 0.300 1
72 . 15 ASN C C 177.718 0.100 1
73 . 15 ASN H H 8.197 0.030 1
74 . 15 ASN N N 117.370 0.200 1
75 . 16 LYS CA C 59.873 0.200 1
76 . 16 LYS CB C 32.582 0.300 1
77 . 16 LYS C C 178.831 0.100 1
78 . 16 LYS H H 8.010 0.030 1
79 . 16 LYS N N 123.785 0.200 1
80 . 17 ILE CA C 64.105 0.200 1
81 . 17 ILE CB C 37.062 0.300 1
82 . 17 ILE C C 177.259 0.100 1
83 . 17 ILE H H 7.625 0.030 1
84 . 17 ILE N N 120.207 0.200 1
85 . 18 LYS CA C 59.856 0.200 1
86 . 18 LYS CB C 32.931 0.300 1
87 . 18 LYS C C 179.449 0.100 1
88 . 18 LYS H H 8.058 0.030 1
89 . 18 LYS N N 119.714 0.200 1
90 . 19 THR CA C 65.747 0.200 1
91 . 19 THR CB C 69.508 0.300 1
92 . 19 THR C C 176.587 0.100 1
93 . 19 THR H H 7.893 0.030 1
94 . 19 THR N N 111.325 0.200 1
95 . 20 ARG CA C 56.416 0.200 1
96 . 20 ARG CB C 28.350 0.300 1
97 . 20 ARG C C 177.276 0.100 1
98 . 20 ARG H H 8.090 0.030 1
99 . 20 ARG N N 123.415 0.200 1
100 . 21 PHE CA C 57.195 0.200 1
101 . 21 PHE CB C 38.039 0.300 1
102 . 21 PHE C C 177.753 0.100 1
103 . 21 PHE H H 7.348 0.030 1
104 . 21 PHE N N 113.669 0.200 1
105 . 22 LEU CA C 58.969 0.200 1
106 . 22 LEU CB C 42.770 0.300 1
107 . 22 LEU C C 178.230 0.100 1
108 . 22 LEU H H 7.243 0.030 1
109 . 22 LEU N N 126.006 0.200 1
110 . 23 ASP CA C 54.235 0.200 1
111 . 23 ASP CB C 40.742 0.300 1
112 . 23 ASP C C 175.651 0.100 1
113 . 23 ASP H H 8.666 0.030 1
114 . 23 ASP N N 113.176 0.200 1
115 . 24 HIS CA C 54.073 0.200 1
116 . 24 HIS CB C 31.054 0.300 1
117 . 24 HIS H H 7.761 0.030 1
118 . 24 HIS N N 117.247 0.200 1
119 . 25 PRO CA C 65.276 0.200 1
120 . 25 PRO C C 177.559 0.100 1
121 . 26 GLU CA C 59.405 0.200 1
122 . 26 GLU CB C 27.531 0.300 1
123 . 26 GLU C C 178.813 0.100 1
124 . 26 GLU H H 10.290 0.030 1
125 . 26 GLU N N 121.564 0.200 1
126 . 27 ILE CA C 64.474 0.200 1
127 . 27 ILE CB C 37.319 0.300 1
128 . 27 ILE C C 177.683 0.100 1
129 . 27 ILE H H 8.150 0.030 1
130 . 27 ILE N N 123.168 0.200 1
131 . 28 TYR CA C 60.991 0.200 1
132 . 28 TYR CB C 38.836 0.300 1
133 . 28 TYR C C 176.623 0.100 1
134 . 28 TYR H H 6.806 0.030 1
135 . 28 TYR N N 119.591 0.200 1
136 . 29 ARG CA C 59.936 0.200 1
137 . 29 ARG CB C 30.287 0.300 1
138 . 29 ARG C C 179.414 0.100 1
139 . 29 ARG H H 8.401 0.030 1
140 . 29 ARG N N 117.370 0.200 1
141 . 30 SER CA C 62.674 0.200 1
142 . 30 SER CB C 63.000 0.500 1
143 . 30 SER C C 175.863 0.100 1
144 . 30 SER H H 8.176 0.030 1
145 . 30 SER N N 116.507 0.200 1
146 . 31 PHE CA C 61.408 0.200 1
147 . 31 PHE CB C 38.890 0.300 1
148 . 31 PHE C C 175.810 0.100 1
149 . 31 PHE H H 8.245 0.030 1
150 . 31 PHE N N 123.415 0.200 1
151 . 32 LEU CA C 57.651 0.200 1
152 . 32 LEU CB C 42.033 0.300 1
153 . 32 LEU C C 179.325 0.100 1
154 . 32 LEU H H 7.967 0.030 1
155 . 32 LEU N N 117.740 0.200 1
156 . 33 GLU CA C 59.616 0.200 1
157 . 33 GLU CB C 29.988 0.300 1
158 . 33 GLU C C 179.661 0.100 1
159 . 33 GLU H H 7.885 0.030 1
160 . 33 GLU N N 119.097 0.200 1
161 . 34 ILE CA C 65.149 0.200 1
162 . 34 ILE CB C 38.367 0.300 1
163 . 34 ILE C C 178.089 0.100 1
164 . 34 ILE H H 7.975 0.030 1
165 . 34 ILE N N 122.305 0.200 1
166 . 35 LEU CA C 57.700 0.200 1
167 . 35 LEU CB C 41.658 0.300 1
168 . 35 LEU C C 178.902 0.100 1
169 . 35 LEU H H 7.791 0.030 1
170 . 35 LEU N N 119.467 0.200 1
171 . 36 HIS CA C 58.695 0.200 1
172 . 36 HIS CB C 29.763 0.300 1
173 . 36 HIS C C 177.736 0.100 1
174 . 36 HIS H H 8.626 0.030 1
175 . 36 HIS N N 117.740 0.200 1
176 . 37 THR CA C 66.929 0.200 1
177 . 37 THR CB C 68.873 0.300 1
178 . 37 THR C C 175.634 0.100 1
179 . 37 THR H H 8.337 0.030 1
180 . 37 THR N N 117.370 0.200 1
181 . 38 TYR CA C 61.010 0.200 1
182 . 38 TYR CB C 39.066 0.300 1
183 . 38 TYR C C 177.188 0.100 1
184 . 38 TYR H H 8.272 0.030 1
185 . 38 TYR N N 122.181 0.200 1
186 . 39 GLN CA C 58.525 0.200 1
187 . 39 GLN CB C 29.454 0.300 1
188 . 39 GLN C C 177.930 0.100 1
189 . 39 GLN H H 8.323 0.030 1
190 . 39 GLN N N 117.370 0.200 1
191 . 40 LYS CA C 58.692 0.200 1
192 . 40 LYS CB C 32.807 0.300 1
193 . 40 LYS C C 178.336 0.100 1
194 . 40 LYS H H 7.967 0.030 1
195 . 40 LYS N N 119.467 0.200 1
196 . 41 GLU CA C 57.687 0.200 1
197 . 41 GLU CB C 30.050 0.300 1
198 . 41 GLU C C 177.559 0.100 1
199 . 41 GLU H H 8.042 0.030 1
200 . 41 GLU N N 118.974 0.200 1
201 . 42 GLN CA C 56.160 0.200 1
202 . 42 GLN CB C 29.305 0.300 1
203 . 42 GLN C C 176.605 0.100 1
204 . 42 GLN H H 7.863 0.030 1
205 . 42 GLN N N 117.740 0.200 1
206 . 43 LEU CA C 55.643 0.200 1
207 . 43 LEU CB C 42.718 0.300 1
208 . 43 LEU C C 177.276 0.100 1
209 . 43 LEU H H 7.720 0.030 1
210 . 43 LEU N N 120.207 0.200 1
211 . 44 HIS CA C 55.979 0.200 1
212 . 44 HIS CB C 30.050 0.300 1
213 . 44 HIS C C 175.351 0.100 1
214 . 44 HIS H H 8.211 0.030 1
215 . 44 HIS N N 119.221 0.200 1
216 . 45 THR CA C 62.096 0.200 1
217 . 45 THR CB C 70.587 0.300 1
218 . 45 THR C C 174.715 0.100 1
219 . 45 THR H H 8.167 0.030 1
220 . 45 THR N N 115.520 0.200 1
221 . 46 LYS CA C 57.214 0.200 1
222 . 46 LYS CB C 32.882 0.300 1
223 . 46 LYS C C 177.294 0.100 1
224 . 46 LYS H H 8.405 0.030 1
225 . 46 LYS N N 123.785 0.200 1
226 . 47 GLY CA C 45.369 0.200 1
227 . 47 GLY C C 173.849 0.100 1
228 . 47 GLY H H 8.632 0.030 1
229 . 47 GLY N N 110.585 0.200 1
230 . 48 ARG CA C 53.784 0.200 1
231 . 48 ARG CB C 30.707 0.300 1
232 . 48 ARG H H 7.916 0.030 1
233 . 48 ARG N N 120.824 0.200 1
234 . 49 PRO CA C 63.330 0.200 1
235 . 49 PRO C C 176.305 0.100 1
236 . 50 PHE CA C 57.604 0.200 1
237 . 50 PHE CB C 40.281 0.300 1
238 . 50 PHE C C 175.210 0.100 1
239 . 50 PHE H H 8.260 0.030 1
240 . 50 PHE N N 120.701 0.200 1
241 . 51 ARG CA C 55.844 0.200 1
242 . 51 ARG CB C 31.301 0.300 1
243 . 51 ARG C C 175.952 0.100 1
244 . 51 ARG H H 8.321 0.030 1
245 . 51 ARG N N 124.032 0.200 1
246 . 52 GLY CA C 44.940 0.200 1
247 . 52 GLY C C 173.408 0.100 1
248 . 52 GLY H H 7.797 0.030 1
249 . 52 GLY N N 109.845 0.200 1
250 . 53 MET CA C 56.355 0.200 1
251 . 53 MET C C 175.899 0.100 1
252 . 53 MET H H 8.796 0.030 1
253 . 53 MET N N 121.549 0.200 1
254 . 54 SER CA C 57.514 0.200 1
255 . 54 SER CB C 66.184 0.300 1
256 . 54 SER C C 175.139 0.100 1
257 . 54 SER H H 8.945 0.030 1
258 . 54 SER N N 120.454 0.200 1
259 . 55 GLU CA C 60.693 0.200 1
260 . 55 GLU CB C 29.891 0.300 1
261 . 55 GLU C C 178.266 0.100 1
262 . 55 GLU H H 9.017 0.030 1
263 . 55 GLU N N 121.318 0.200 1
264 . 56 GLU CA C 60.058 0.200 1
265 . 56 GLU CB C 29.742 0.300 1
266 . 56 GLU C C 173.885 0.100 1
267 . 56 GLU H H 8.689 0.030 1
268 . 56 GLU N N 118.480 0.200 1
269 . 57 GLU CA C 59.486 0.200 1
270 . 57 GLU CB C 30.633 0.300 1
271 . 57 GLU C C 179.096 0.100 1
272 . 57 GLU H H 7.921 0.030 1
273 . 57 GLU N N 120.948 0.200 1
274 . 58 VAL CA C 66.480 0.200 1
275 . 58 VAL CB C 31.360 0.300 1
276 . 58 VAL C C 177.206 0.100 1
277 . 58 VAL H H 8.135 0.030 1
278 . 58 VAL N N 120.454 0.200 1
279 . 59 PHE CA C 62.319 0.200 1
280 . 59 PHE CB C 39.049 0.300 1
281 . 59 PHE C C 177.789 0.100 1
282 . 59 PHE H H 8.256 0.030 1
283 . 59 PHE N N 119.467 0.200 1
284 . 60 THR CA C 66.932 0.200 1
285 . 60 THR CB C 69.284 0.300 1
286 . 60 THR C C 176.234 0.100 1
287 . 60 THR H H 8.216 0.030 1
288 . 60 THR N N 115.766 0.200 1
289 . 61 GLU CA C 59.265 0.200 1
290 . 61 GLU CB C 29.808 0.300 1
291 . 61 GLU C C 180.067 0.100 1
292 . 61 GLU H H 7.975 0.030 1
293 . 61 GLU N N 120.578 0.200 1
294 . 62 VAL CA C 66.678 0.200 1
295 . 62 VAL CB C 40.305 0.300 1
296 . 62 VAL C C 176.587 0.100 1
297 . 62 VAL H H 8.275 0.030 1
298 . 62 VAL N N 120.824 0.200 1
299 . 63 ALA CA C 55.231 0.200 1
300 . 63 ALA CB C 18.128 0.300 1
301 . 63 ALA C C 180.067 0.100 1
302 . 63 ALA H H 8.451 0.030 1
303 . 63 ALA N N 122.181 0.200 1
304 . 64 ASN CA C 55.540 0.200 1
305 . 64 ASN CB C 39.049 0.300 1
306 . 64 ASN C C 177.700 0.100 1
307 . 64 ASN H H 7.451 0.030 1
308 . 64 ASN N N 114.286 0.200 1
309 . 65 LEU CA C 57.222 0.200 1
310 . 65 LEU CB C 42.893 0.300 1
311 . 65 LEU C C 178.425 0.100 1
312 . 65 LEU H H 7.631 0.030 1
313 . 65 LEU N N 121.194 0.200 1
314 . 66 PHE CA C 53.165 0.200 1
315 . 66 PHE CB C 37.201 0.300 1
316 . 66 PHE C C 174.821 0.100 1
317 . 66 PHE H H 8.131 0.030 1
318 . 66 PHE N N 114.903 0.200 1
319 . 67 ARG CA C 58.625 0.200 1
320 . 67 ARG CB C 30.104 0.300 1
321 . 67 ARG C C 177.789 0.100 1
322 . 67 ARG H H 7.014 0.030 1
323 . 67 ARG N N 120.824 0.200 1
324 . 68 GLY CA C 45.648 0.200 1
325 . 68 GLY C C 174.326 0.100 1
326 . 68 GLY H H 9.345 0.030 1
327 . 68 GLY N N 115.150 0.200 1
328 . 69 GLN CA C 52.496 0.200 1
329 . 69 GLN CB C 26.930 0.300 1
330 . 69 GLN C C 176.164 0.100 1
331 . 69 GLN H H 8.484 0.030 1
332 . 69 GLN N N 120.454 0.200 1
333 . 70 GLU CA C 60.872 0.200 1
334 . 70 GLU CB C 29.507 0.300 1
335 . 70 GLU C C 178.478 0.100 1
336 . 70 GLU H H 8.605 0.030 1
337 . 70 GLU N N 120.578 0.200 1
338 . 71 ASP CA C 56.462 0.200 1
339 . 71 ASP CB C 38.932 0.300 1
340 . 71 ASP C C 178.372 0.100 1
341 . 71 ASP H H 8.972 0.030 1
342 . 71 ASP N N 119.221 0.200 1
343 . 72 LEU CA C 56.795 0.200 1
344 . 72 LEU CB C 42.024 0.300 1
345 . 72 LEU C C 180.421 0.100 1
346 . 72 LEU H H 7.761 0.030 1
347 . 72 LEU N N 119.591 0.200 1
348 . 73 LEU CA C 57.706 0.200 1
349 . 73 LEU CB C 42.024 0.300 1
350 . 73 LEU C C 175.916 0.100 1
351 . 73 LEU H H 8.025 0.030 1
352 . 73 LEU N N 119.961 0.200 1
353 . 74 SER CA C 61.717 0.200 1
354 . 74 SER CB C 63.152 0.300 1
355 . 74 SER C C 177.064 0.100 1
356 . 74 SER H H 8.018 0.030 1
357 . 74 SER N N 113.422 0.200 1
358 . 75 GLU CA C 57.486 0.200 1
359 . 75 GLU CB C 30.611 0.300 1
360 . 75 GLU C C 177.577 0.100 1
361 . 75 GLU H H 7.887 0.030 1
362 . 75 GLU N N 119.097 0.200 1
363 . 76 PHE CA C 62.203 0.200 1
364 . 76 PHE C C 176.711 0.100 1
365 . 76 PHE H H 7.839 0.030 1
366 . 76 PHE N N 121.441 0.200 1
367 . 77 GLY CA C 46.941 0.200 1
368 . 77 GLY C C 175.510 0.100 1
369 . 77 GLY H H 8.415 0.030 1
370 . 77 GLY N N 103.800 0.200 1
371 . 78 GLN CA C 57.012 0.200 1
372 . 78 GLN CB C 29.430 0.300 1
373 . 78 GLN C C 176.782 0.100 1
374 . 78 GLN H H 7.407 0.030 1
375 . 78 GLN N N 117.493 0.200 1
376 . 79 PHE CA C 58.789 0.200 1
377 . 79 PHE CB C 43.657 0.300 1
378 . 79 PHE C C 178.902 0.100 1
379 . 79 PHE H H 7.501 0.030 1
380 . 79 PHE N N 120.453 0.200 1
381 . 80 LEU CA C 57.616 0.200 1
382 . 80 LEU H H 8.676 0.030 1
383 . 80 LEU N N 117.740 0.200 1
384 . 81 PRO CA C 62.834 0.200 1
385 . 81 PRO C C 175.704 0.100 1
386 . 82 GLU CA C 57.931 0.200 1
387 . 82 GLU C C 178.407 0.100 1
388 . 82 GLU H H 8.566 0.030 1
389 . 82 GLU N N 122.922 0.200 1
390 . 83 ALA CA C 54.252 0.200 1
391 . 83 ALA CB C 18.198 0.300 1
392 . 83 ALA C C 178.849 0.100 1
393 . 83 ALA H H 8.138 0.030 1
394 . 83 ALA N N 122.798 0.200 1
395 . 84 LYS CA C 58.298 0.200 1
396 . 84 LYS CB C 39.364 0.300 1
397 . 84 LYS C C 175.916 0.100 1
398 . 84 LYS H H 7.960 0.030 1
399 . 84 LYS N N 116.136 0.200 1
400 . 85 ARG CA C 57.866 0.200 1
401 . 85 ARG CB C 31.382 0.300 1
402 . 85 ARG C C 177.400 0.100 1
403 . 85 ARG H H 7.567 0.030 1
404 . 85 ARG N N 119.756 0.200 1
405 . 86 SER CA C 59.589 0.200 1
406 . 86 SER CB C 64.777 0.300 1
407 . 86 SER C C 174.538 0.100 1
408 . 86 SER H H 8.066 0.030 1
409 . 86 SER N N 113.546 0.200 1
410 . 87 LEU CA C 55.688 0.200 1
411 . 87 LEU CB C 42.923 0.300 1
412 . 87 LEU C C 178.919 0.100 1
413 . 87 LEU H H 8.028 0.030 1
414 . 87 LEU N N 121.935 0.200 1
415 . 88 PHE CA C 57.414 0.200 1
416 . 88 PHE CB C 39.362 0.300 1
417 . 88 PHE C C 176.058 0.100 1
418 . 88 PHE H H 8.097 0.030 1
419 . 88 PHE N N 117.987 0.200 1
420 . 89 THR CA C 61.830 0.200 1
421 . 89 THR CB C 70.330 0.300 1
422 . 89 THR C C 175.280 0.100 1
423 . 89 THR H H 7.958 0.030 1
424 . 89 THR N N 112.682 0.200 1
425 . 90 GLY CA C 45.603 0.200 1
426 . 90 GLY C C 174.114 0.100 1
427 . 90 GLY H H 8.117 0.030 1
428 . 90 GLY N N 110.338 0.200 1
429 . 91 ASN CA C 53.382 0.200 1
430 . 91 ASN CB C 39.508 0.300 1
431 . 91 ASN C C 175.987 0.100 1
432 . 91 ASN H H 8.443 0.030 1
433 . 91 ASN N N 118.850 0.200 1
434 . 92 GLY CA C 45.681 0.200 1
435 . 92 GLY C C 174.432 0.100 1
436 . 92 GLY H H 8.527 0.030 1
437 . 92 GLY N N 109.598 0.200 1
438 . 93 SER CA C 58.497 0.200 1
439 . 93 SER CB C 64.414 0.300 1
440 . 93 SER C C 174.768 0.100 1
441 . 93 SER H H 8.200 0.030 1
442 . 93 SER N N 115.643 0.200 1
443 . 94 ALA CA C 53.097 0.200 1
444 . 94 ALA CB C 19.642 0.300 1
445 . 94 ALA C C 177.965 0.100 1
446 . 94 ALA H H 8.443 0.030 1
447 . 94 ALA N N 125.759 0.200 1
448 . 95 GLU CA C 56.911 0.200 1
449 . 95 GLU CB C 30.670 0.300 1
450 . 95 GLU C C 176.852 0.100 1
451 . 95 GLU H H 8.361 0.030 1
452 . 95 GLU N N 119.344 0.200 1
453 . 96 MET CA C 55.807 0.200 1
454 . 96 MET CB C 33.592 0.300 1
455 . 96 MET C C 176.234 0.100 1
456 . 96 MET H H 8.306 0.030 1
457 . 96 MET N N 120.701 0.200 1
458 . 97 ASN CA C 53.399 0.200 1
459 . 97 ASN CB C 39.362 0.300 1
460 . 97 ASN C C 175.369 0.100 1
461 . 97 ASN H H 8.457 0.030 1
462 . 97 ASN N N 119.714 0.200 1
463 . 98 SER CA C 58.871 0.200 1
464 . 98 SER CB C 64.127 0.300 1
465 . 98 SER C C 175.245 0.100 1
466 . 98 SER H H 8.369 0.030 1
467 . 98 SER N N 116.383 0.200 1
468 . 99 GLY CA C 45.452 0.200 1
469 . 99 GLY C C 174.273 0.100 1
470 . 99 GLY H H 8.497 0.030 1
471 . 99 GLY N N 110.708 0.200 1
472 . 100 GLN CA C 55.845 0.200 1
473 . 100 GLN CB C 30.011 0.300 1
474 . 100 GLN C C 176.005 0.100 1
475 . 100 GLN H H 8.193 0.030 1
476 . 100 GLN N N 119.961 0.200 1
477 . 101 LYS CA C 56.361 0.200 1
478 . 101 LYS CB C 33.648 0.300 1
479 . 101 LYS C C 176.252 0.100 1
480 . 101 LYS H H 8.449 0.030 1
481 . 101 LYS N N 122.798 0.200 1
482 . 102 ASN CA C 53.442 0.200 1
483 . 102 ASN CB C 39.467 0.300 1
484 . 102 ASN C C 175.157 0.100 1
485 . 102 ASN H H 8.565 0.030 1
486 . 102 ASN N N 120.578 0.200 1
487 . 103 GLU CA C 56.510 0.200 1
488 . 103 GLU CB C 30.957 0.300 1
489 . 103 GLU C C 176.234 0.100 1
490 . 103 GLU H H 8.478 0.030 1
491 . 103 GLU N N 121.441 0.200 1
492 . 104 GLU CA C 56.594 0.200 1
493 . 104 GLU CB C 30.738 0.300 1
494 . 104 GLU C C 175.492 0.100 1
495 . 104 GLU H H 8.419 0.030 1
496 . 104 GLU N N 122.675 0.200 1
497 . 105 LYS CA C 57.581 0.200 1
498 . 105 LYS CB C 34.230 0.300 1
499 . 105 LYS H H 7.969 0.030 1
500 . 105 LYS N N 127.733 0.200 1
stop_
save_