data_5808
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Chemical shift assignments and relaxation parameters for the PAH2 domain of
mSin3B bound to an extended SID of Mad1
;
_BMRB_accession_number 5808
_BMRB_flat_file_name bmr5808.str
_Entry_type original
_Submission_date 2003-05-22
_Accession_date 2003-05-22
_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 'van Ingen' Hugo . .
2 Jansen Jaap F.A. .
3 Spronk Chris A.E.M. .
4 Vuister Geerten W. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
S2_parameters 1
T1_relaxation 1
heteronucl_NOE 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 472
"13C chemical shifts" 269
"15N chemical shifts" 90
"T1 relaxation values" 78
"order parameters" 77
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2004-02-12 original author .
stop_
loop_
_Related_BMRB_accession_number
_Relationship
5457 'chemical shift assignment of SID24'
4841 'chemical shift assignment of PAH2:SID13 complex'
stop_
_Original_release_date 2004-02-12
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Extension of the binding motif of the Sin3 Interacting Domain of the mad family
proteins
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 14705930
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 'van Ingen' Hugo . .
2 Lasonder Edwin . .
3 Jansen Jaap F.A. .
4 Kaan Anita M. .
5 Spronk Chris A.E.M. .
6 Stunnenberg Henk G. .
7 Vuister Geerten W. .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 43
_Journal_issue 1
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 46
_Page_last 54
_Year 2004
_Details .
loop_
_Keyword
MAD
Sin
'Interacting Domain'
PAH
Sin3
stop_
save_
##################################
# Molecular system description #
##################################
save_system_PAH2_SID
_Saveframe_category molecular_system
_Mol_system_name 'PAH2-SID24 complex'
_Abbreviation_common 'PAH2, SID24'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'PAH2 domain of mSin3B' $PAH2
'SID domain of Mad1' $SID24
stop_
_System_molecular_weight 15300
_System_physical_state native
_System_oligomer_state complex
_System_paramagnetic no
_System_thiol_state 'not present'
loop_
_Biological_function
'regulation of gene transcription'
stop_
_Database_query_date .
_Details '1:1 complex between PAH2 domain of mSin3B and extended SID domain of Mad1.'
save_
########################
# Monomeric polymers #
########################
save_PAH2
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'PAH2 domain'
_Abbreviation_common 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 2015-01-28
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 1G1E "Nmr Structure Of The Human Mad1 Transrepression Domain Sid In Complex With Mammalian Sin3a Pah2 Domain" 66.67 16 100.00 100.00 7.14e-01
PDB 1PD7 "Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b" 100.00 24 100.00 100.00 2.58e-06
PDB 1S5Q "Solution Structure Of Mad1 Sid-Msin3a Pah2 Complex" 66.67 16 100.00 100.00 7.14e-01
DBJ BAG35605 "unnamed protein product [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
DBJ BAG73371 "MAX dimerization protein 1 [synthetic construct]" 100.00 221 100.00 100.00 2.55e-06
DBJ BAH13406 "unnamed protein product [Homo sapiens]" 100.00 105 100.00 100.00 1.73e-06
EMBL CAG38734 "MAD [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
EMBL CAG46493 "MAD [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
GB AAA36194 "antagonizer of myc transcriptional activity [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
GB AAH69377 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
GB AAH69433 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
GB AAH98396 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
GB AAI13532 "MAX dimerization protein 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
REF NP_001179309 "max dimerization protein 1 [Bos taurus]" 100.00 222 100.00 100.00 2.46e-06
REF NP_001189442 "max dimerization protein 1 isoform 2 [Homo sapiens]" 100.00 220 100.00 100.00 2.39e-06
REF NP_001189443 "max dimerization protein 1 isoform 3 [Homo sapiens]" 100.00 211 100.00 100.00 2.19e-06
REF NP_001247787 "max dimerization protein 1 [Macaca mulatta]" 100.00 221 100.00 100.00 2.64e-06
REF NP_002348 "max dimerization protein 1 isoform 1 [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
SP Q05195 "RecName: Full=Max dimerization protein 1; Short=Max dimerizer 1; AltName: Full=Protein MAD [Homo sapiens]" 100.00 221 100.00 100.00 2.55e-06
TPG DAA24557 "TPA: MAX dimerization protein 1-like [Bos taurus]" 100.00 222 100.00 100.00 2.46e-06
stop_
save_
save_SID24
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common Mad1
_Name_variant 'SID domain of Hs. Mad1'
_Abbreviation_common SID
_Molecular_mass 2973
_Mol_thiol_state 'not present'
_Details .
_Residue_count 24
_Mol_residue_sequence
;
VRMNIQMLLEAADYLERRER
EAEH
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 5 VAL 2 6 ARG 3 7 MET 4 8 ASN 5 9 ILE
6 10 GLN 7 11 MET 8 12 LEU 9 13 LEU 10 14 GLU
11 15 ALA 12 16 ALA 13 17 ASP 14 18 TYR 15 19 LEU
16 20 GLU 17 21 ARG 18 22 ARG 19 23 GLU 20 24 ARG
21 25 GLU 22 26 ALA 23 27 GLU 24 28 HIS
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
SWISS-PROT Q05195 'MAD protein (MAX dimerizer) (MAX dimerization protein 1)' 100.00 221 100.00 100.00 5.63e-05
REF XP_592508 'PREDICTED: similar to MAX dimerization protein 1 isoform 2 [Bos taurus]' 100.00 222 100.00 100.00 5.40e-05
REF XP_525776 'PREDICTED: MAX dimerization protein 1 isoform 2 [Pan troglodytes]' 100.00 221 100.00 100.00 5.63e-05
REF XP_001493078 'PREDICTED: similar to MAX dimerization protein 1 [Equus caballus]' 100.00 221 100.00 100.00 5.87e-05
REF XP_001098088 'PREDICTED: similar to MAX dimerization protein 1 [Macaca mulatta]' 100.00 221 100.00 100.00 5.77e-05
REF NP_002348 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
GenBank AAI13532 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
GenBank AAH98396 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
GenBank AAH69433 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
GenBank AAH69377 'MAX dimerization protein 1 [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
GenBank AAA36194 'antagonizer of myc transcriptional activity' 100.00 221 100.00 100.00 5.63e-05
EMBL CAG46493 'MAD [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
EMBL CAG38734 'MAD [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
DBJ BAG35605 'unnamed protein product [Homo sapiens]' 100.00 221 100.00 100.00 5.63e-05
PDB 1PD7 'Extended Sid Of Mad1 Bound To The Pah2 Domain Of Msin3b' 100.00 24 100.00 100.00 2.57e-04
BMRB 5457 Mad1 100.00 24 100.00 100.00 2.57e-04
BMRB 4635 'MAD1 SID domain' 66.67 16 100.00 100.00 5.40e+00
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$PAH2 'house mouse' 10090 Eukaryota Metazoa Mus musculus
$SID24 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
_Vector_name
$PAH2 'recombinant technology' . . . . .
$SID24 'solid phase synthesis' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details 'The sample also contained trace amounts of sodium azide and Pefabloc.'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$SID24 1.3 mM .
$PAH2 1.3 mM '[U-13C; U-15N]'
'K2HPO4/KH2PO4 buffer' 50 mM .
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityInova
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityInova
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_3
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityInova
_Field_strength 750
_Details .
save_
save_NMR_spectrometer_4
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityInova
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_HNCA_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label $sample_1
save_
save_HNCACB_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label $sample_1
save_
save_CBCACONH_3
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCACONH
_Sample_label $sample_1
save_
save_(H)CCH-TOCSY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name (H)CCH-TOCSY
_Sample_label $sample_1
save_
save_15N_NOESY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N NOESY'
_Sample_label $sample_1
save_
save_13C_NOESY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C NOESY'
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCACONH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name (H)CCH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_Ex-cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.3 . n/a
temperature 293 . 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_citation_label
_Correction_value_citation_label
DSS H 1 'methyl protons' ppm . . . . . . $entry_citation $entry_citation
DSS C 13 'methyl protons' ppm . . . . . . $entry_citation $entry_citation
DSS N 15 'methyl protons' ppm . . . . . . $entry_citation $entry_citation
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $Ex-cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'PAH2 domain of mSin3B'
_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 N N 123.132 0.02 1
2 . 1 GLU H H 8.900 0.003 1
3 . 1 GLU CA C 57.659 0.02 1
4 . 1 GLU HA H 4.199 0.002 1
5 . 1 GLU HB2 H 1.908 0.007 1
6 . 1 GLU HB3 H 2.019 0.002 1
7 . 1 GLU CG C 36.331 0.02 1
8 . 1 GLU HG2 H 2.233 0.003 1
9 . 2 SER N N 115.424 0.02 1
10 . 2 SER H H 8.166 0.006 1
11 . 2 SER CA C 58.821 0.02 1
12 . 2 SER HA H 4.206 0.004 1
13 . 2 SER CB C 63.449 0.02 1
14 . 2 SER HB2 H 3.674 0.005 1
15 . 2 SER HB3 H 3.791 0.002 1
16 . 2 SER HG H 4.789 0.002 1
17 . 3 ASP N N 121.939 0.02 1
18 . 3 ASP H H 8.108 0.006 1
19 . 3 ASP CA C 54.472 0.02 1
20 . 3 ASP HA H 4.664 0.003 1
21 . 3 ASP CB C 41.035 0.02 1
22 . 3 ASP HB2 H 2.680 0.003 1
23 . 4 SER N N 115.481 0.02 1
24 . 4 SER H H 8.028 0.002 1
25 . 4 SER CA C 58.132 0.02 1
26 . 4 SER HA H 4.535 0.002 1
27 . 4 SER CB C 64.304 0.02 1
28 . 4 SER HB2 H 4.020 0.003 1
29 . 4 SER HB3 H 4.162 0.004 1
30 . 5 VAL N N 125.145 0.02 1
31 . 5 VAL H H 8.610 0.002 1
32 . 5 VAL CA C 65.669 0.02 1
33 . 5 VAL HA H 3.798 0.005 1
34 . 5 VAL CB C 31.909 0.02 1
35 . 5 VAL HB H 2.042 0.002 1
36 . 5 VAL HG1 H 0.926 0.003 1
37 . 5 VAL HG2 H 1.039 0.003 1
38 . 5 VAL CG1 C 20.883 0.027 1
39 . 5 VAL CG2 C 22.015 0.02 1
40 . 6 GLU N N 120.288 0.02 1
41 . 6 GLU H H 9.015 0.006 1
42 . 6 GLU CA C 60.768 0.017 1
43 . 6 GLU HA H 4.023 0.003 1
44 . 6 GLU CB C 28.885 0.02 1
45 . 6 GLU HB2 H 1.852 0.005 1
46 . 6 GLU CG C 36.882 0.02 1
47 . 6 GLU HG2 H 2.289 0.006 1
48 . 6 GLU HG3 H 2.289 0.003 1
49 . 7 PHE N N 120.563 0.02 1
50 . 7 PHE H H 8.342 0.003 1
51 . 7 PHE CA C 60.969 0.035 1
52 . 7 PHE HA H 4.521 0.004 1
53 . 7 PHE CB C 39.130 0.02 1
54 . 7 PHE HB2 H 3.004 0.005 1
55 . 7 PHE HB3 H 3.188 0.003 1
56 . 7 PHE HD1 H 7.179 0.003 1
57 . 7 PHE HE1 H 7.179 0.003 1
58 . 7 PHE CD1 C 131.836 0.02 1
59 . 8 ASN N N 117.075 0.02 1
60 . 8 ASN H H 8.225 0.004 1
61 . 8 ASN CA C 56.551 0.02 1
62 . 8 ASN HA H 4.313 0.004 1
63 . 8 ASN CB C 38.120 0.02 1
64 . 8 ASN HB2 H 2.755 0.005 1
65 . 8 ASN HB3 H 2.937 0.004 1
66 . 8 ASN ND2 N 112.855 0.02 1
67 . 8 ASN HD21 H 7.006 0.002 1
68 . 8 ASN HD22 H 7.503 0.002 1
69 . 9 ASN N N 120.838 0.02 1
70 . 9 ASN H H 8.463 0.004 1
71 . 9 ASN CA C 55.807 0.02 1
72 . 9 ASN HA H 4.558 0.003 1
73 . 9 ASN CB C 37.735 0.02 1
74 . 9 ASN HB2 H 2.899 0.005 1
75 . 9 ASN HB3 H 3.166 0.003 1
76 . 9 ASN ND2 N 111.725 0.02 1
77 . 9 ASN HD21 H 6.967 0.006 1
78 . 9 ASN HD22 H 7.355 0.003 1
79 . 10 ALA N N 125.701 0.02 1
80 . 10 ALA H H 8.293 0.001 1
81 . 10 ALA CA C 55.878 0.052 1
82 . 10 ALA HA H 4.242 0.004 1
83 . 10 ALA HB H 1.503 0.004 1
84 . 10 ALA CB C 18.552 0.061 1
85 . 11 ILE N N 118.430 0.02 1
86 . 11 ILE H H 8.341 0.006 1
87 . 11 ILE CA C 65.692 0.006 1
88 . 11 ILE HA H 3.406 0.002 1
89 . 11 ILE CB C 38.120 0.02 1
90 . 11 ILE HB H 1.759 0.003 1
91 . 11 ILE HG2 H 0.863 0.005 1
92 . 11 ILE CG2 C 17.680 0.004 1
93 . 11 ILE CG1 C 28.813 0.035 1
94 . 11 ILE HG12 H 0.511 0.003 1
95 . 11 ILE HG13 H 1.133 0.004 1
96 . 11 ILE HD1 H 0.313 0.003 1
97 . 11 ILE CD1 C 13.953 0.014 1
98 . 12 SER N N 113.837 0.02 1
99 . 12 SER H H 8.061 0.005 1
100 . 12 SER CA C 61.695 0.02 1
101 . 12 SER HA H 4.166 0.004 1
102 . 13 TYR N N 122.654 0.02 1
103 . 13 TYR H H 8.080 0.005 1
104 . 13 TYR CA C 60.954 0.02 1
105 . 13 TYR HA H 4.445 0.003 1
106 . 13 TYR CB C 38.409 0.02 1
107 . 13 TYR HB2 H 2.918 0.008 1
108 . 13 TYR HB3 H 3.441 0.004 1
109 . 13 TYR HD1 H 6.958 0.005 1
110 . 13 TYR HE1 H 6.742 0.003 1
111 . 13 TYR CD1 C 133.083 0.02 1
112 . 13 TYR CE1 C 117.697 0.02 1
113 . 14 VAL N N 118.046 0.02 1
114 . 14 VAL H H 8.530 0.003 1
115 . 14 VAL CA C 67.463 0.02 1
116 . 14 VAL HA H 3.388 0.006 1
117 . 14 VAL CB C 31.145 0.038 1
118 . 14 VAL HB H 2.088 0.003 1
119 . 14 VAL HG1 H 1.157 0.003 1
120 . 14 VAL HG2 H 1.211 0.008 1
121 . 14 VAL CG1 C 23.957 0.02 1
122 . 14 VAL CG2 C 24.329 0.02 1
123 . 15 ASN N N 117.050 0.02 1
124 . 15 ASN H H 8.603 0.003 1
125 . 15 ASN CA C 56.279 0.02 1
126 . 15 ASN HA H 4.338 0.003 1
127 . 15 ASN CB C 39.086 0.02 1
128 . 15 ASN HB2 H 2.756 0.003 1
129 . 15 ASN ND2 N 112.579 0.02 1
130 . 15 ASN HD21 H 6.730 0.003 1
131 . 15 ASN HD22 H 7.490 0.002 1
132 . 16 LYS N N 123.601 0.02 1
133 . 16 LYS H H 7.983 0.006 1
134 . 16 LYS CA C 60.275 0.02 1
135 . 16 LYS HA H 3.838 0.003 1
136 . 16 LYS CB C 32.183 0.02 1
137 . 16 LYS HB2 H 1.952 0.003 1
138 . 16 LYS CG C 25.297 0.02 1
139 . 16 LYS HG2 H 1.108 0.005 1
140 . 16 LYS HG3 H 1.508 0.004 1
141 . 16 LYS CD C 30.365 0.02 1
142 . 16 LYS HD2 H 1.639 0.003 1
143 . 16 LYS CE C 41.633 0.02 1
144 . 16 LYS HE2 H 2.788 0.003 1
145 . 16 LYS HE3 H 2.861 0.003 1
146 . 17 ILE N N 120.163 0.02 1
147 . 17 ILE H H 7.640 0.004 1
148 . 17 ILE CA C 65.165 0.02 1
149 . 17 ILE HA H 3.104 0.003 1
150 . 17 ILE CB C 38.321 0.02 1
151 . 17 ILE HB H 1.798 0.005 1
152 . 17 ILE HG2 H 0.750 0.003 1
153 . 17 ILE CG2 C 18.421 0.02 1
154 . 17 ILE CG1 C 28.430 0.02 1
155 . 17 ILE HG12 H 0.309 0.003 1
156 . 17 ILE HG13 H 1.058 0.005 1
157 . 17 ILE HD1 H 0.030 0.005 1
158 . 17 ILE CD1 C 14.278 0.023 1
159 . 18 LYS N N 119.278 0.02 1
160 . 18 LYS H H 8.334 0.003 1
161 . 18 LYS CA C 59.885 0.02 1
162 . 18 LYS HA H 3.121 0.003 1
163 . 18 LYS CB C 32.604 0.009 1
164 . 18 LYS HB2 H 1.211 0.003 1
165 . 18 LYS HB3 H 1.568 0.002 1
166 . 18 LYS CG C 24.832 0.02 1
167 . 18 LYS HG2 H 0.502 0.002 1
168 . 18 LYS HG3 H 0.713 0.003 1
169 . 18 LYS CD C 29.533 0.022 1
170 . 18 LYS HD2 H 1.314 0.001 1
171 . 18 LYS HD3 H 1.410 0.002 1
172 . 18 LYS CE C 42.077 0.035 1
173 . 18 LYS HE2 H 2.762 0.003 1
174 . 19 THR N N 111.471 0.02 1
175 . 19 THR H H 8.100 0.008 1
176 . 19 THR CA C 65.689 0.02 1
177 . 19 THR HA H 3.732 0.004 1
178 . 19 THR CB C 68.828 0.02 1
179 . 19 THR HB H 4.052 0.003 1
180 . 19 THR HG2 H 1.131 0.006 1
181 . 19 THR CG2 C 21.250 0.02 1
182 . 20 ARG N N 124.572 0.02 1
183 . 20 ARG H H 7.947 0.005 1
184 . 20 ARG CA C 56.055 0.02 1
185 . 20 ARG HA H 3.773 0.005 1
186 . 20 ARG CB C 27.378 0.02 1
187 . 20 ARG HB2 H 1.085 0.003 1
188 . 20 ARG HB3 H 1.584 0.003 1
189 . 20 ARG CG C 24.350 0.02 1
190 . 20 ARG HG2 H 0.448 0.004 1
191 . 20 ARG HG3 H 0.867 0.005 1
192 . 20 ARG CD C 39.800 0.02 1
193 . 20 ARG HD2 H 2.988 0.011 1
194 . 21 PHE N N 113.130 0.02 1
195 . 21 PHE H H 7.162 0.002 1
196 . 21 PHE HA H 4.980 0.007 1
197 . 21 PHE CB C 38.159 0.02 1
198 . 21 PHE HB2 H 2.422 0.006 1
199 . 21 PHE HB3 H 3.900 0.005 1
200 . 21 PHE HD1 H 7.243 0.011 1
201 . 21 PHE HE1 H 6.823 0.003 1
202 . 21 PHE CD1 C 132.303 0.02 1
203 . 21 PHE CE1 C 131.016 0.02 1
204 . 21 PHE CZ C 129.541 0.02 1
205 . 21 PHE HZ H 7.125 0.002 1
206 . 22 LEU N N 126.344 0.02 1
207 . 22 LEU H H 7.212 0.002 1
208 . 22 LEU CA C 59.008 0.02 1
209 . 22 LEU HA H 3.990 0.004 1
210 . 22 LEU CB C 42.266 0.02 1
211 . 22 LEU HB2 H 1.561 0.003 1
212 . 22 LEU HB3 H 1.787 0.004 1
213 . 22 LEU CG C 26.533 0.02 1
214 . 22 LEU HG H 1.877 0.004 1
215 . 22 LEU HD1 H 0.892 0.003 1
216 . 22 LEU HD2 H 0.843 0.003 1
217 . 22 LEU CD1 C 24.568 0.02 1
218 . 22 LEU CD2 C 24.237 0.02 1
219 . 23 ASP N N 113.038 0.02 1
220 . 23 ASP H H 8.642 0.006 1
221 . 23 ASP CA C 54.151 0.02 1
222 . 23 ASP HA H 4.518 0.005 1
223 . 23 ASP CB C 40.135 0.02 1
224 . 23 ASP HB2 H 2.513 0.002 1
225 . 23 ASP HB3 H 2.548 0.002 1
226 . 24 HIS N N 117.175 0.02 1
227 . 24 HIS H H 7.703 0.004 1
228 . 24 HIS CA C 54.092 0.02 1
229 . 24 HIS HA H 5.173 0.003 1
230 . 24 HIS CB C 30.292 0.02 1
231 . 24 HIS HB2 H 2.959 0.006 1
232 . 24 HIS HB3 H 3.407 0.004 1
233 . 24 HIS CD2 C 120.166 0.02 1
234 . 24 HIS CE1 C 136.59 0.02 1
235 . 24 HIS HD2 H 7.350 0.002 1
236 . 24 HIS HE1 H 8.542 0.001 1
237 . 25 PRO CD C 50.414 0.02 1
238 . 25 PRO CA C 65.218 0.02 1
239 . 25 PRO HA H 4.427 0.004 1
240 . 25 PRO CB C 31.564 0.02 1
241 . 25 PRO HB2 H 2.162 0.002 1
242 . 25 PRO HB3 H 2.418 0.003 1
243 . 25 PRO CG C 27.637 0.02 1
244 . 25 PRO HG2 H 2.073 0.002 1
245 . 25 PRO HG3 H 2.147 0.002 1
246 . 25 PRO HD2 H 3.493 0.006 1
247 . 25 PRO HD3 H 3.702 0.004 1
248 . 26 GLU N N 121.633 0.02 1
249 . 26 GLU H H 10.308 0.001 1
250 . 26 GLU CA C 59.291 0.02 1
251 . 26 GLU HA H 4.195 0.004 1
252 . 26 GLU CB C 27.285 0.02 1
253 . 26 GLU HB2 H 2.024 0.006 1
254 . 26 GLU HB3 H 2.155 0.004 1
255 . 26 GLU CG C 35.353 0.02 1
256 . 26 GLU HG2 H 2.306 0.004 1
257 . 26 GLU HG3 H 2.529 0.006 1
258 . 27 ILE N N 123.675 0.02 1
259 . 27 ILE H H 8.209 0.005 1
260 . 27 ILE CA C 64.540 0.02 1
261 . 27 ILE HA H 3.646 0.003 1
262 . 27 ILE CB C 36.801 0.02 1
263 . 27 ILE HB H 1.508 0.004 1
264 . 27 ILE HG2 H -0.063 0.001 1
265 . 27 ILE CG2 C 15.457 0.02 1
266 . 27 ILE CG1 C 28.727 0.02 1
267 . 27 ILE HG12 H 1.124 0.004 1
268 . 27 ILE HG13 H 1.520 0.002 1
269 . 27 ILE HD1 H 0.714 0.006 1
270 . 27 ILE CD1 C 11.764 0.02 1
271 . 28 TYR N N 119.737 0.02 1
272 . 28 TYR H H 6.767 0.003 1
273 . 28 TYR CA C 61.181 0.02 1
274 . 28 TYR HA H 4.161 0.003 1
275 . 28 TYR CB C 39.017 0.02 1
276 . 28 TYR HB2 H 3.110 0.005 1
277 . 28 TYR HB3 H 3.216 0.004 1
278 . 28 TYR HD1 H 7.018 0.004 1
279 . 28 TYR HE1 H 6.720 0.005 1
280 . 28 TYR CD1 C 132.453 0.02 1
281 . 28 TYR CE1 C 118.008 0.02 1
282 . 29 ARG N N 116.129 0.02 1
283 . 29 ARG H H 8.171 0.005 1
284 . 29 ARG CA C 59.524 0.02 1
285 . 29 ARG HA H 3.747 0.003 1
286 . 29 ARG CB C 29.770 0.02 1
287 . 29 ARG HB2 H 1.867 0.002 1
288 . 29 ARG HB3 H 1.928 0.002 1
289 . 29 ARG CG C 27.404 0.02 1
290 . 29 ARG HG2 H 1.628 0.003 1
291 . 29 ARG HG3 H 1.856 0.002 1
292 . 29 ARG CD C 43.126 0.02 1
293 . 29 ARG HD2 H 3.152 0.002 1
294 . 29 ARG HD3 H 3.249 0.002 1
295 . 30 SER N N 116.988 0.02 1
296 . 30 SER H H 8.264 0.004 1
297 . 30 SER CA C 62.731 0.02 1
298 . 30 SER HA H 4.144 0.009 1
299 . 30 SER CB C 63.006 0.02 1
300 . 30 SER HB2 H 3.857 0.006 1
301 . 31 PHE N N 123.825 0.02 1
302 . 31 PHE H H 8.110 0.007 1
303 . 31 PHE CA C 60.902 0.02 1
304 . 31 PHE HA H 3.850 0.005 1
305 . 31 PHE CB C 38.278 0.001 1
306 . 31 PHE HB2 H 2.986 0.003 1
307 . 31 PHE HB3 H 3.451 0.007 1
308 . 31 PHE HD1 H 6.782 0.005 1
309 . 31 PHE HE1 H 6.782 0.005 1
310 . 31 PHE CD1 C 132.139 0.02 1
311 . 32 LEU N N 116.527 0.02 1
312 . 32 LEU H H 7.608 0.004 1
313 . 32 LEU CA C 57.482 0.023 1
314 . 32 LEU HA H 3.419 0.005 1
315 . 32 LEU CB C 40.958 0.02 1
316 . 32 LEU HB2 H 1.107 0.007 1
317 . 32 LEU HB3 H 1.737 0.003 1
318 . 32 LEU CG C 26.225 0.02 1
319 . 32 LEU HG H 1.344 0.003 1
320 . 32 LEU HD1 H 0.611 0.002 1
321 . 32 LEU HD2 H 0.560 0.002 1
322 . 32 LEU CD1 C 25.566 0.013 1
323 . 32 LEU CD2 C 21.615 0.02 1
324 . 33 GLU N N 119.591 0.02 1
325 . 33 GLU H H 8.038 0.002 1
326 . 33 GLU CA C 59.646 0.02 1
327 . 33 GLU HA H 4.068 0.002 1
328 . 33 GLU HB2 H 2.104 0.002 1
329 . 33 GLU HG2 H 2.274 0.002 1
330 . 34 ILE N N 122.447 0.02 1
331 . 34 ILE H H 8.011 0.003 1
332 . 34 ILE CA C 65.057 0.02 1
333 . 34 ILE HA H 3.689 0.003 1
334 . 34 ILE CB C 38.120 0.02 1
335 . 34 ILE HB H 1.762 0.006 1
336 . 34 ILE HG2 H 0.736 0.007 1
337 . 34 ILE CG2 C 17.827 0.02 1
338 . 34 ILE CG1 C 28.814 0.02 1
339 . 34 ILE HG12 H 1.024 0.004 1
340 . 34 ILE HG13 H 1.716 0.002 1
341 . 34 ILE HD1 H 0.681 0.001 1
342 . 34 ILE CD1 C 14.827 0.02 1
343 . 35 LEU N N 117.698 0.02 1
344 . 35 LEU H H 7.306 0.003 1
345 . 35 LEU CA C 58.085 0.001 1
346 . 35 LEU HA H 3.830 0.004 1
347 . 35 LEU CB C 40.120 0.047 1
348 . 35 LEU HB2 H 1.113 0.007 1
349 . 35 LEU HB3 H 1.683 0.006 1
350 . 35 LEU CG C 25.932 0.009 1
351 . 35 LEU HG H 1.349 0.008 1
352 . 35 LEU HD1 H 0.350 0.006 1
353 . 35 LEU HD2 H 0.513 0.005 1
354 . 35 LEU CD1 C 25.698 0.070 1
355 . 35 LEU CD2 C 21.393 0.067 1
356 . 36 HIS N N 117.224 0.02 1
357 . 36 HIS H H 8.754 0.004 1
358 . 36 HIS CA C 59.952 0.02 1
359 . 36 HIS HA H 4.208 0.006 1
360 . 36 HIS CB C 29.244 0.02 1
361 . 36 HIS HB2 H 3.150 0.004 1
362 . 36 HIS HB3 H 3.271 0.004 1
363 . 36 HIS CD2 C 120.493 0.02 1
364 . 36 HIS CE1 C 137.14 0.02 1
365 . 36 HIS HD2 H 7.064 0.005 1
366 . 36 HIS HE1 H 8.314 0.002 1
367 . 37 THR N N 119.094 0.02 1
368 . 37 THR H H 8.528 0.006 1
369 . 37 THR CA C 67.171 0.02 1
370 . 37 THR HA H 3.829 0.003 1
371 . 37 THR CB C 68.353 0.02 1
372 . 37 THR HB H 4.416 0.003 1
373 . 37 THR HG2 H 1.241 0.004 1
374 . 37 THR CG2 C 21.891 0.02 1
375 . 38 TYR N N 122.081 0.02 1
376 . 38 TYR H H 8.164 0.005 1
377 . 38 TYR CA C 61.841 0.02 1
378 . 38 TYR HA H 4.097 0.008 1
379 . 38 TYR CB C 38.230 0.02 1
380 . 38 TYR HB2 H 3.104 0.003 1
381 . 38 TYR HB3 H 3.182 0.004 1
382 . 38 TYR HD1 H 6.935 0.015 1
383 . 38 TYR HE1 H 6.711 0.003 1
384 . 38 TYR CD1 C 133.419 0.02 1
385 . 38 TYR CE1 C 118.420 0.02 1
386 . 39 GLN N N 118.544 0.02 1
387 . 39 GLN H H 8.352 0.005 1
388 . 39 GLN CA C 58.281 0.02 1
389 . 39 GLN HA H 3.840 0.004 1
390 . 39 GLN CB C 29.494 0.02 1
391 . 39 GLN HB2 H 2.085 0.002 1
392 . 39 GLN HB3 H 2.131 0.002 1
393 . 39 GLN CG C 33.906 0.031 1
394 . 39 GLN HG2 H 2.320 0.004 1
395 . 39 GLN HG3 H 2.376 0.001 1
396 . 39 GLN NE2 N 109.693 0.02 1
397 . 39 GLN HE21 H 6.794 0.002 1
398 . 39 GLN HE22 H 7.345 0.007 1
399 . 40 LYS N N 119.737 0.02 1
400 . 40 LYS H H 8.152 0.005 1
401 . 40 LYS CA C 59.152 0.02 1
402 . 40 LYS HA H 4.051 0.003 1
403 . 40 LYS CB C 32.378 0.02 1
404 . 40 LYS HB2 H 1.905 0.006 1
405 . 40 LYS HG2 H 1.483 0.002 1
406 . 40 LYS CD C 29.373 0.02 1
407 . 40 LYS HD2 H 1.630 0.003 1
408 . 40 LYS CE C 42.079 0.02 1
409 . 40 LYS HE2 H 2.904 0.003 1
410 . 41 GLU N N 117.626 0.02 1
411 . 41 GLU H H 7.827 0.001 1
412 . 41 GLU CA C 57.555 0.02 1
413 . 41 GLU HA H 4.195 0.004 1
414 . 41 GLU HB2 H 2.045 0.002 1
415 . 41 GLU HG2 H 2.309 0.002 1
416 . 42 GLN N N 116.984 0.02 1
417 . 42 GLN H H 7.621 0.003 1
418 . 42 GLN CA C 56.143 0.02 1
419 . 42 GLN HA H 4.062 0.004 1
420 . 42 GLN CB C 28.735 0.02 1
421 . 42 GLN HB2 H 1.877 0.004 1
422 . 42 GLN HB3 H 2.057 0.005 1
423 . 42 GLN CG C 33.249 0.02 1
424 . 42 GLN HG2 H 2.146 0.003 1
425 . 42 GLN NE2 N 115.149 0.02 1
426 . 42 GLN HE21 H 6.769 0.007 1
427 . 42 GLN HE22 H 6.992 0.001 1
428 . 43 LEU N N 119.553 0.02 1
429 . 43 LEU H H 7.488 0.001 1
430 . 43 LEU CA C 55.432 0.02 1
431 . 43 LEU HA H 4.236 0.004 1
432 . 43 LEU CB C 42.232 0.02 1
433 . 43 LEU HB2 H 1.454 0.002 1
434 . 43 LEU HB3 H 1.646 0.001 1
435 . 43 LEU CG C 26.722 0.02 1
436 . 43 LEU HG H 1.598 0.002 1
437 . 43 LEU HD1 H 0.874 0.002 1
438 . 43 LEU HD2 H 0.811 0.003 1
439 . 43 LEU CD1 C 25.138 0.02 1
440 . 43 LEU CD2 C 23.243 0.02 1
441 . 44 HIS N N 119.370 0.02 1
442 . 44 HIS H H 8.007 0.002 1
443 . 44 HIS CA C 55.661 0.02 1
444 . 44 HIS HA H 4.660 0.006 1
445 . 44 HIS HB2 H 3.054 0.002 1
446 . 44 HIS HB3 H 3.148 0.002 1
447 . 44 HIS CD2 C 120.028 0.02 1
448 . 44 HIS CE1 C 137.16 0.02 1
449 . 44 HIS HD2 H 7.052 0.002 1
450 . 44 HIS HE1 H 8.035 0.002 1
451 . 45 THR N N 114.687 0.02 1
452 . 45 THR H H 8.017 0.002 1
453 . 45 THR CA C 61.985 0.02 1
454 . 45 THR HA H 4.270 0.010 1
455 . 45 THR CB C 69.943 0.02 1
456 . 45 THR HB H 4.128 0.003 1
457 . 45 THR HG2 H 1.138 0.002 1
458 . 45 THR CG2 C 21.810 0.02 1
459 . 46 LYS N N 124.325 0.02 1
460 . 46 LYS H H 8.382 0.002 1
461 . 46 LYS CA C 57.408 0.02 1
462 . 46 LYS HA H 4.164 0.003 1
463 . 46 LYS CB C 32.461 0.02 1
464 . 46 LYS HB2 H 1.799 0.002 1
465 . 46 LYS CG C 24.751 0.02 1
466 . 46 LYS HG2 H 1.393 0.003 1
467 . 46 LYS CD C 29.146 0.02 1
468 . 46 LYS HD2 H 1.643 0.002 1
469 . 46 LYS CE C 42.481 0.02 1
470 . 46 LYS HE2 H 2.914 0.003 1
471 . 47 GLY N N 110.928 0.02 1
472 . 47 GLY H H 8.680 0.002 1
473 . 47 GLY CA C 45.449 0.02 1
474 . 47 GLY HA2 H 3.784 0.003 1
475 . 47 GLY HA3 H 4.049 0.002 1
476 . 48 ARG N N 120.761 0.02 1
477 . 48 ARG H H 7.847 0.005 1
478 . 48 ARG CA C 53.350 0.02 1
479 . 48 ARG HA H 4.676 0.001 1
480 . 48 ARG CB C 30.667 0.02 1
481 . 48 ARG HB2 H 1.673 0.001 1
482 . 48 ARG HB3 H 1.798 0.001 1
483 . 48 ARG CG C 26.722 0.02 1
484 . 48 ARG HG2 H 1.536 0.002 1
485 . 48 ARG HG3 H 1.581 0.003 1
486 . 48 ARG CD C 43.649 0.02 1
487 . 48 ARG HD2 H 3.130 0.004 1
488 . 49 PRO CD C 50.499 0.02 1
489 . 49 PRO CA C 63.263 0.02 1
490 . 49 PRO HA H 4.384 0.003 1
491 . 49 PRO CB C 31.662 0.02 1
492 . 49 PRO HB2 H 1.761 0.003 1
493 . 49 PRO HB3 H 2.160 0.003 1
494 . 49 PRO CG C 27.350 0.02 1
495 . 49 PRO HG2 H 1.936 0.003 1
496 . 49 PRO HD2 H 3.570 0.005 1
497 . 49 PRO HD3 H 3.736 0.003 1
498 . 50 PHE N N 120.563 0.02 1
499 . 50 PHE H H 8.178 0.003 1
500 . 50 PHE CA C 57.437 0.02 1
501 . 50 PHE HA H 4.588 0.003 1
502 . 50 PHE CB C 40.121 0.02 1
503 . 50 PHE HB2 H 3.006 0.004 1
504 . 50 PHE HD1 H 7.028 0.002 1
505 . 50 PHE HE1 H 7.230 0.002 1
506 . 50 PHE HD2 H 7.131 0.006 1
507 . 50 PHE HE2 H 7.131 0.006 1
508 . 50 PHE CD1 C 131.759 0.02 1
509 . 51 ARG N N 124.233 0.02 1
510 . 51 ARG H H 8.317 0.002 1
511 . 51 ARG CA C 55.861 0.02 1
512 . 51 ARG HA H 4.279 0.004 1
513 . 51 ARG CB C 31.219 0.02 1
514 . 51 ARG HB2 H 1.639 0.002 1
515 . 51 ARG HB3 H 1.780 0.004 1
516 . 51 ARG CG C 26.839 0.02 1
517 . 51 ARG HG2 H 1.529 0.004 1
518 . 51 ARG CD C 43.335 0.02 1
519 . 51 ARG HD2 H 3.090 0.003 1
520 . 52 GLY N N 109.722 0.02 1
521 . 52 GLY H H 7.714 0.005 1
522 . 52 GLY CA C 44.931 0.02 1
523 . 52 GLY HA2 H 3.748 0.003 1
524 . 52 GLY HA3 H 3.955 0.003 1
525 . 53 MET N N 121.085 0.02 1
526 . 53 MET H H 8.396 0.006 1
527 . 53 MET CA C 56.536 0.02 1
528 . 53 MET HA H 4.470 0.002 1
529 . 53 MET CB C 35.025 0.02 1
530 . 53 MET HB2 H 1.916 0.003 1
531 . 53 MET HB3 H 2.015 0.004 1
532 . 53 MET CG C 32.284 0.02 1
533 . 53 MET HG2 H 2.630 0.002 1
534 . 53 MET HG3 H 2.700 0.003 1
535 . 53 MET HE H 2.043 0.005 1
536 . 53 MET CE C 17.278 0.02 1
537 . 54 SER N N 120.930 0.02 1
538 . 54 SER H H 8.950 0.001 1
539 . 54 SER HA H 4.790 0.006 1
540 . 54 SER CB C 65.931 0.02 1
541 . 54 SER HB2 H 4.073 0.007 1
542 . 54 SER HB3 H 4.473 0.002 1
543 . 55 GLU N N 120.689 0.02 1
544 . 55 GLU H H 9.088 0.001 1
545 . 55 GLU CA C 60.831 0.02 1
546 . 55 GLU HA H 3.819 0.002 1
547 . 55 GLU CB C 29.425 0.02 1
548 . 55 GLU HB2 H 1.957 0.006 1
549 . 55 GLU HB3 H 2.101 0.002 1
550 . 55 GLU CG C 38.048 0.02 1
551 . 55 GLU HG2 H 2.303 0.007 1
552 . 55 GLU HG3 H 2.428 0.004 1
553 . 56 GLU N N 118.819 0.02 1
554 . 56 GLU H H 8.717 0.002 1
555 . 56 GLU CA C 60.192 0.02 1
556 . 56 GLU HA H 4.034 0.003 1
557 . 56 GLU HB2 H 2.065 0.002 1
558 . 56 GLU CG C 36.882 0.02 1
559 . 56 GLU HG2 H 2.347 0.007 1
560 . 57 GLU N N 121.010 0.02 1
561 . 57 GLU H H 7.905 0.004 1
562 . 57 GLU HA H 4.054 0.002 1
563 . 57 GLU HB2 H 2.073 0.002 1
564 . 57 GLU CG C 37.410 0.02 1
565 . 57 GLU HG2 H 2.359 0.003 1
566 . 58 VAL N N 120.163 0.02 1
567 . 58 VAL H H 8.034 0.003 1
568 . 58 VAL CA C 66.350 0.02 1
569 . 58 VAL HA H 3.556 0.004 1
570 . 58 VAL CB C 31.564 0.02 1
571 . 58 VAL HB H 2.108 0.003 1
572 . 58 VAL HG1 H 0.752 0.004 1
573 . 58 VAL HG2 H 0.802 0.003 1
574 . 58 VAL CG1 C 21.270 0.010 1
575 . 58 VAL CG2 C 23.740 0.02 1
576 . 59 PHE N N 120.196 0.02 1
577 . 59 PHE H H 8.306 0.003 1
578 . 59 PHE CA C 62.680 0.02 1
579 . 59 PHE HA H 3.954 0.004 1
580 . 59 PHE CB C 38.890 0.02 1
581 . 59 PHE HB2 H 3.064 0.004 1
582 . 59 PHE HB3 H 3.295 0.001 1
583 . 60 THR N N 114.930 0.02 1
584 . 60 THR H H 8.305 0.006 1
585 . 60 THR CA C 66.873 0.02 1
586 . 60 THR HA H 3.751 0.002 1
587 . 60 THR CB C 68.854 0.02 1
588 . 60 THR HB H 4.310 0.001 1
589 . 60 THR HG2 H 1.219 0.006 1
590 . 60 THR CG2 C 21.752 0.02 1
591 . 61 GLU N N 120.587 0.02 1
592 . 61 GLU H H 7.955 0.005 1
593 . 61 GLU HA H 4.048 0.002 1
594 . 61 GLU HB2 H 2.002 0.003 1
595 . 61 GLU HG2 H 2.334 0.002 1
596 . 62 VAL N N 122.214 0.02 1
597 . 62 VAL H H 8.306 0.004 1
598 . 62 VAL CA C 66.836 0.02 1
599 . 62 VAL HA H 2.936 0.005 1
600 . 62 VAL CB C 30.817 0.02 1
601 . 62 VAL HB H 1.466 0.003 1
602 . 62 VAL HG1 H -0.357 0.004 1
603 . 62 VAL HG2 H 0.509 0.003 1
604 . 62 VAL CG1 C 21.018 0.02 1
605 . 62 VAL CG2 C 23.150 0.02 1
606 . 63 ALA N N 122.306 0.02 1
607 . 63 ALA H H 8.724 0.009 1
608 . 63 ALA CA C 55.266 0.02 1
609 . 63 ALA HA H 3.719 0.003 1
610 . 63 ALA HB H 1.147 0.003 1
611 . 63 ALA CB C 17.592 0.02 1
612 . 64 ASN N N 114.582 0.02 1
613 . 64 ASN H H 7.507 0.005 1
614 . 64 ASN CA C 55.673 0.02 1
615 . 64 ASN HA H 4.416 0.002 1
616 . 64 ASN CB C 38.431 0.02 1
617 . 64 ASN HB2 H 2.783 0.005 1
618 . 64 ASN ND2 N 113.497 0.02 1
619 . 64 ASN HD21 H 6.890 0.002 1
620 . 64 ASN HD22 H 7.660 0.002 1
621 . 65 LEU N N 121.359 0.02 1
622 . 65 LEU H H 7.495 0.003 1
623 . 65 LEU CA C 57.161 0.02 1
624 . 65 LEU HA H 4.019 0.005 1
625 . 65 LEU CB C 42.294 0.02 1
626 . 65 LEU HB2 H 1.345 0.002 1
627 . 65 LEU HB3 H 1.459 0.002 1
628 . 65 LEU CG C 26.225 0.02 1
629 . 65 LEU HG H 1.581 0.003 1
630 . 65 LEU HD1 H 0.787 0.001 1
631 . 65 LEU HD2 H 0.756 0.003 1
632 . 65 LEU CD1 C 24.402 0.02 1
633 . 65 LEU CD2 C 24.237 0.02 1
634 . 66 PHE N N 115.332 0.02 1
635 . 66 PHE H H 8.224 0.007 1
636 . 66 PHE HA H 4.827 0.002 1
637 . 66 PHE CB C 36.133 0.02 1
638 . 66 PHE HB2 H 2.881 0.004 1
639 . 66 PHE HB3 H 3.664 0.009 1
640 . 66 PHE HD1 H 6.546 0.005 1
641 . 66 PHE HE1 H 6.596 0.005 1
642 . 66 PHE HD2 H 6.564 0.002 1
643 . 66 PHE HE2 H 6.564 0.002 1
644 . 66 PHE CD1 C 129.065 0.02 1
645 . 66 PHE CE1 C 130.429 0.02 1
646 . 66 PHE CZ C 129.086 0.02 1
647 . 66 PHE HZ H 5.881 0.007 1
648 . 67 ARG N N 121.384 0.02 1
649 . 67 ARG H H 6.952 0.005 1
650 . 67 ARG CA C 58.684 0.02 1
651 . 67 ARG HA H 4.098 0.004 1
652 . 67 ARG CB C 29.770 0.02 1
653 . 67 ARG HB2 H 1.825 0.012 1
654 . 67 ARG HB3 H 1.973 0.003 1
655 . 67 ARG CG C 26.839 0.02 1
656 . 67 ARG HG2 H 1.695 0.003 1
657 . 67 ARG HG3 H 1.800 0.002 1
658 . 67 ARG CD C 43.393 0.02 1
659 . 67 ARG HD2 H 3.247 0.002 1
660 . 67 ARG HD3 H 3.276 0.002 1
661 . 68 GLY N N 115.883 0.02 1
662 . 68 GLY H H 9.396 0.009 1
663 . 68 GLY CA C 45.447 0.02 1
664 . 68 GLY HA2 H 3.863 0.005 1
665 . 68 GLY HA3 H 4.313 0.003 1
666 . 69 GLN N N 120.471 0.02 1
667 . 69 GLN H H 8.488 0.004 1
668 . 69 GLN HA H 4.817 0.002 1
669 . 69 GLN HB2 H 1.836 0.002 1
670 . 69 GLN HG2 H 2.232 0.002 1
671 . 69 GLN NE2 N 111.081 0.02 1
672 . 69 GLN HE21 H 6.758 0.002 1
673 . 69 GLN HE22 H 7.498 0.001 1
674 . 70 GLU N N 120.413 0.02 1
675 . 70 GLU H H 8.580 0.006 1
676 . 70 GLU CA C 61.033 0.02 1
677 . 70 GLU HA H 3.898 0.003 1
678 . 70 GLU CB C 28.942 0.02 1
679 . 70 GLU HB2 H 2.111 0.003 1
680 . 70 GLU CG C 37.304 0.02 1
681 . 70 GLU HG2 H 2.358 0.003 1
682 . 70 GLU HG3 H 2.515 0.003 1
683 . 71 ASP N N 119.342 0.02 1
684 . 71 ASP H H 8.971 0.001 1
685 . 71 ASP CA C 56.467 0.02 1
686 . 71 ASP HA H 4.387 0.003 1
687 . 71 ASP CB C 38.317 0.02 1
688 . 71 ASP HB2 H 2.658 0.003 1
689 . 71 ASP HB3 H 2.822 0.003 1
690 . 72 LEU N N 119.491 0.02 1
691 . 72 LEU H H 7.772 0.004 1
692 . 72 LEU CA C 56.887 0.02 1
693 . 72 LEU HA H 4.298 0.003 1
694 . 72 LEU CB C 41.798 0.02 1
695 . 72 LEU HB2 H 1.014 0.004 1
696 . 72 LEU HB3 H 1.647 0.002 1
697 . 72 LEU CG C 26.317 0.02 1
698 . 72 LEU HG H 1.537 0.006 1
699 . 72 LEU HD1 H 0.153 0.003 1
700 . 72 LEU HD2 H 0.486 0.001 1
701 . 72 LEU CD1 C 26.095 0.02 1
702 . 72 LEU CD2 C 21.970 0.02 1
703 . 73 LEU N N 120.781 0.02 1
704 . 73 LEU H H 7.885 0.007 1
705 . 73 LEU CA C 57.538 0.02 1
706 . 73 LEU HA H 4.369 0.002 1
707 . 73 LEU CB C 42.053 0.02 1
708 . 73 LEU HB2 H 1.813 0.003 1
709 . 73 LEU HB3 H 2.018 0.003 1
710 . 73 LEU CG C 27.090 0.02 1
711 . 73 LEU HG H 1.840 0.002 1
712 . 73 LEU HD1 H 0.774 0.005 1
713 . 73 LEU HD2 H 0.848 0.004 1
714 . 73 LEU CD1 C 24.071 0.02 1
715 . 73 LEU CD2 C 24.568 0.02 1
716 . 74 SER N N 115.079 0.02 1
717 . 74 SER H H 8.311 0.005 1
718 . 74 SER CA C 61.695 0.02 1
719 . 74 SER HA H 4.297 0.009 1
720 . 74 SER CB C 68.897 0.02 1
721 . 74 SER HB2 H 4.045 0.003 1
722 . 75 GLU N N 120.114 0.02 1
723 . 75 GLU H H 7.889 0.007 1
724 . 75 GLU CA C 58.637 0.02 1
725 . 75 GLU HA H 4.053 0.005 1
726 . 75 GLU CB C 30.805 0.02 1
727 . 75 GLU HB2 H 1.802 0.003 1
728 . 75 GLU HB3 H 2.022 0.002 1
729 . 75 GLU CG C 36.995 0.02 1
730 . 75 GLU HG2 H 1.936 0.003 1
731 . 75 GLU HG3 H 2.288 0.004 1
732 . 76 PHE N N 119.553 0.02 1
733 . 76 PHE H H 7.650 0.003 1
734 . 76 PHE CA C 60.837 0.02 1
735 . 76 PHE HA H 4.379 0.007 1
736 . 76 PHE CB C 38.936 0.02 1
737 . 76 PHE HB2 H 3.277 0.003 1
738 . 76 PHE HB3 H 4.057 0.005 1
739 . 76 PHE HD1 H 7.337 0.003 1
740 . 76 PHE HE1 H 7.039 0.003 1
741 . 76 PHE CD1 C 131.541 0.02 1
742 . 76 PHE CE1 C 130.351 0.02 1
743 . 76 PHE CZ C 128.698 0.02 1
744 . 76 PHE HZ H 6.798 0.006 1
745 . 77 GLY N N 124.600 0.02 1
746 . 77 GLY H H 7.795 0.003 1
747 . 77 GLY CA C 46.814 0.02 1
748 . 77 GLY HA2 H 3.511 0.002 1
749 . 77 GLY HA3 H 3.869 0.003 1
750 . 78 GLN N N 117.167 0.02 1
751 . 78 GLN H H 7.387 0.004 1
752 . 78 GLN CA C 57.142 0.02 1
753 . 78 GLN HA H 3.884 0.005 1
754 . 78 GLN CB C 28.597 0.02 1
755 . 78 GLN HB2 H 1.643 0.012 1
756 . 78 GLN CG C 33.833 0.028 1
757 . 78 GLN HG2 H 1.872 0.004 1
758 . 78 GLN HG3 H 2.078 0.005 1
759 . 78 GLN NE2 N 111.725 0.02 1
760 . 78 GLN HE21 H 6.942 0.004 1
761 . 78 GLN HE22 H 7.340 0.002 1
762 . 79 PHE N N 115.057 0.02 1
763 . 79 PHE H H 7.665 0.006 1
764 . 79 PHE CA C 58.328 0.02 1
765 . 79 PHE HA H 4.055 0.002 1
766 . 79 PHE CB C 38.606 0.02 1
767 . 79 PHE HB2 H 2.505 0.001 1
768 . 79 PHE HB3 H 2.883 0.002 1
769 . 79 PHE HD1 H 7.236 0.003 1
770 . 79 PHE HE1 H 7.236 0.003 1
771 . 79 PHE CD1 C 132.458 0.02 1
772 . 80 LEU N N 118.370 0.02 1
773 . 80 LEU H H 6.893 0.005 1
774 . 80 LEU CA C 51.948 0.02 1
775 . 80 LEU HA H 4.650 0.001 1
776 . 80 LEU CB C 42.536 0.02 1
777 . 80 LEU HB2 H 1.429 0.004 1
778 . 80 LEU CG C 26.292 0.02 1
779 . 80 LEU HG H 1.249 0.004 1
780 . 80 LEU HD1 H 0.702 0.003 1
781 . 80 LEU HD2 H 0.654 0.004 1
782 . 80 LEU CD1 C 26.291 0.004 1
783 . 80 LEU CD2 C 23.852 0.035 1
784 . 81 PRO CD C 50.580 0.02 1
785 . 81 PRO CA C 63.941 0.02 1
786 . 81 PRO HA H 4.326 0.004 1
787 . 81 PRO CB C 32.185 0.02 1
788 . 81 PRO HB2 H 1.889 0.003 1
789 . 81 PRO HB3 H 2.318 0.003 1
790 . 81 PRO CG C 27.716 0.02 1
791 . 81 PRO HG2 H 2.053 0.003 1
792 . 81 PRO HD2 H 3.685 0.004 1
793 . 82 GLU N N 120.563 0.02 1
794 . 82 GLU H H 9.056 0.006 1
795 . 82 GLU CA C 57.583 0.02 1
796 . 82 GLU HA H 4.100 0.002 1
797 . 82 GLU CB C 29.597 0.02 1
798 . 82 GLU HB2 H 1.909 0.004 1
799 . 82 GLU HB3 H 2.033 0.003 1
800 . 82 GLU HG2 H 2.274 0.002 1
801 . 83 ALA N N 123.499 0.02 1
802 . 83 ALA H H 8.147 0.001 1
803 . 83 ALA CA C 52.879 0.02 1
804 . 83 ALA HA H 4.200 0.007 1
805 . 83 ALA HB H 1.319 0.003 1
806 . 83 ALA CB C 19.141 0.02 1
807 . 84 LYS N N 119.186 0.02 1
808 . 84 LYS H H 8.223 0.008 1
809 . 84 LYS CA C 56.369 0.02 1
810 . 84 LYS HA H 4.205 0.003 1
811 . 84 LYS CB C 32.668 0.02 1
812 . 84 LYS HB2 H 1.713 0.002 1
813 . 84 LYS HB3 H 1.826 0.003 1
814 . 84 LYS CG C 24.996 0.02 1
815 . 84 LYS HG2 H 1.367 0.002 1
816 . 84 LYS CD C 29.060 0.02 1
817 . 84 LYS HD2 H 1.628 0.003 1
818 . 84 LYS CE C 42.071 0.02 1
819 . 84 LYS HE2 H 2.911 0.002 1
820 . 85 ARG N N 120.746 0.02 1
821 . 85 ARG H H 8.065 0.010 1
822 . 85 ARG CA C 56.886 0.02 1
823 . 85 ARG HA H 4.152 0.004 1
824 . 85 ARG CB C 30.563 0.02 1
825 . 85 ARG HB2 H 1.702 0.002 1
826 . 85 ARG HB3 H 1.794 0.007 1
827 . 85 ARG CG C 27.109 0.02 1
828 . 85 ARG HG2 H 1.557 0.003 1
829 . 85 ARG HG3 H 1.611 0.002 1
830 . 85 ARG CD C 43.427 0.02 1
831 . 85 ARG HD2 H 3.064 0.002 1
stop_
save_
save_15N_T1_Set_1
_Saveframe_category T1_relaxation
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $Ex-cond_1
_Spectrometer_frequency_1H 600
_T1_coherence_type Nz
_T1_value_units ms
_Mol_system_component_name 'PAH2 domain of mSin3B'
_Text_data_format .
_Text_data .
loop_
_T1_ID
_Residue_seq_code
_Residue_label
_Atom_name
_T1_value
_T1_value_error
1 1 GLU N 0.708 0.028
2 2 SER N 0.602 0.024
3 3 ASP N 0.565 0.023
4 4 SER N 0.604 0.024
5 5 VAL N 0.666 0.027
6 7 PHE N 0.646 0.026
7 8 ASN N 0.663 0.026
8 9 ASN N 0.666 0.027
9 10 ALA N 0.657 0.026
10 12 SER N 0.660 0.027
11 13 TYR N 0.668 0.027
12 14 VAL N 0.657 0.026
13 15 ASN N 0.661 0.027
14 16 LYS N 0.689 0.028
15 17 ILE N 0.672 0.027
16 18 LYS N 0.650 0.026
17 19 THR N 0.727 0.029
18 20 ARG N 0.690 0.028
19 21 PHE N 0.697 0.028
20 22 LEU N 0.684 0.028
21 23 ASP N 0.707 0.028
22 24 HIS N 0.710 0.028
23 26 GLU N 0.683 0.028
24 27 ILE N 0.698 0.028
25 28 TYR N 0.746 0.032
26 29 ARG N 0.683 0.027
27 30 SER N 0.717 0.029
28 31 PHE N 0.707 0.029
29 32 LEU N 0.710 0.028
30 33 GLU N 0.670 0.027
31 34 ILE N 0.706 0.028
32 35 LEU N 0.690 0.028
33 36 HIS N 0.690 0.028
34 37 THR N 0.683 0.027
35 38 TYR N 0.712 0.028
36 41 GLU N 0.670 0.027
37 42 GLN N 0.677 0.027
38 43 LEU N 0.646 0.026
39 44 HIS N 0.573 0.023
40 46 LYS N 0.606 0.028
41 47 GLY N 0.678 0.122
42 50 PHE N 0.623 0.025
43 51 ARG N 0.590 0.024
44 52 GLY N 0.618 0.025
45 53 MET N 0.644 0.026
46 54 SER N 0.643 0.039
47 56 GLU N 0.748 0.035
48 58 VAL N 0.691 0.028
49 59 PHE N 0.693 0.028
50 61 GLU N 0.671 0.027
51 62 VAL N 0.699 0.028
52 63 ALA N 0.690 0.028
53 64 ASN N 0.715 0.029
54 65 LEU N 0.688 0.027
55 66 PHE N 0.743 0.030
56 67 ARG N 0.699 0.028
57 68 GLY N 0.713 0.043
58 69 GLN N 0.692 0.028
59 70 GLU N 0.685 0.027
60 71 ASP N 0.682 0.027
61 72 LEU N 0.669 0.027
62 75 GLU N 0.683 0.028
63 76 PHE N 0.659 0.026
64 77 GLY N 0.684 0.028
65 78 GLN N 0.661 0.027
66 79 PHE N 0.667 0.027
67 80 LEU N 0.701 0.028
68 83 ALA N 0.634 0.025
69 85 ARG N 0.602 0.024
70 94 ALA N 0.651 0.026
71 96 MET N 0.636 0.025
72 97 ASN N 0.611 0.025
73 99 GLY N 0.664 0.026
74 101 LYS N 0.694 0.028
75 102 ASN N 0.703 0.028
76 103 GLU N 0.741 0.030
77 104 GLU N 0.780 0.031
78 105 LYS N 1.016 0.040
stop_
save_
save_heteronuclear_NOE_1
_Saveframe_category heteronuclear_NOE
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $Ex-cond_1
_Spectrometer_frequency_1H 600
_Mol_system_component_name 'PAH2 domain of mSin3B'
_Atom_one_atom_name N
_Atom_two_atom_name H
_Heteronuclear_NOE_value_type .
_NOE_reference_value .
_NOE_reference_description .
_Text_data_format .
_Text_data .
loop_
_Residue_seq_code
_Residue_label
_Heteronuclear_NOE_value
_Heteronuclear_NOE_value_error
1 GLU -0.266 0.082
2 SER 0.014 0.100
3 ASP 0.168 0.071
4 SER 0.275 0.048
5 VAL 0.599 0.025
7 PHE 0.755 0.030
8 ASN 0.733 0.029
9 ASN 0.818 0.033
10 ALA 0.796 0.032
12 SER 0.735 0.029
13 TYR 0.794 0.032
14 VAL 0.775 0.031
15 ASN 0.771 0.031
16 LYS 0.875 0.035
17 ILE 0.779 0.031
18 LYS 0.894 0.036
19 THR 0.761 0.030
20 ARG 0.816 0.033
21 PHE 0.778 0.031
22 LEU 0.728 0.029
23 ASP 0.752 0.030
24 HIS 0.712 0.028
26 GLU 0.747 0.030
27 ILE 0.757 0.030
28 TYR 0.733 0.029
29 ARG 0.788 0.032
30 SER 0.783 0.031
31 PHE 0.792 0.032
32 LEU 0.848 0.034
33 GLU 0.686 0.027
34 ILE 0.766 0.031
35 LEU 0.743 0.030
36 HIS 0.755 0.030
37 THR 0.796 0.032
38 TYR 0.735 0.029
41 GLU 0.701 0.028
42 GLN 0.689 0.028
43 LEU 0.567 0.030
44 HIS 0.167 0.148
46 LYS 0.369 0.059
47 GLY 0.363 0.107
50 PHE 0.379 0.050
51 ARG 0.391 0.053
52 GLY 0.358 0.084
53 MET 0.483 0.040
54 SER 0.706 0.031
56 GLU 0.756 0.030
58 VAL 0.719 0.029
59 PHE 0.772 0.031
61 GLU 0.722 0.029
62 VAL 0.763 0.031
63 ALA 0.744 0.030
64 ASN 0.782 0.031
65 LEU 0.810 0.032
66 PHE 0.750 0.030
67 ARG 0.706 0.028
68 GLY 0.690 0.028
69 GLN 0.836 0.033
70 GLU 0.629 0.025
71 ASP 0.773 0.031
72 LEU 0.688 0.028
75 GLU 0.688 0.028
76 PHE 0.711 0.028
77 GLY 0.729 0.029
78 GLN 0.746 0.030
79 PHE 0.765 0.031
80 LEU 0.671 0.027
83 ALA 0.516 0.054
85 ARG 0.400 0.060
94 ALA -0.316 0.079
96 MET -0.340 0.134
97 ASN -0.426 0.073
99 GLY -0.419 0.056
101 LYS -0.705 0.030
102 ASN -0.735 0.040
103 GLU -0.812 0.032
104 GLU -1.137 0.045
105 LYS -1.499 0.060
stop_
save_
save_S2_parameters_label
_Saveframe_category S2_parameters
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $Ex-cond_1
_Mol_system_component_name 'PAH2 domain of mSin3B'
_Tau_e_value_units .
_Text_data_format .
_Text_data .
loop_
_Residue_seq_code
_Residue_label
_Atom_name
_Model_fit
_S2_value
_S2_value_fit_error
_Tau_e_value
_Tau_e_value_fit_error
_S2f_value
_S2f_value_fit_error
_S2s_value
_S2s_value_fit_error
_Tau_s_value
_Tau_s_value_fit_error
_S2H_value
_S2H_value_fit_error
_S2N_value
_S2N_value_fit_error
1 GLU N . 0.136 . . . . . . . . . . . . .
2 SER N . 0.212 . . . . . . . . . . . . .
3 ASP N . 0.261 . . . . . . . . . . . . .
4 SER N . 0.363 . . . . . . . . . . . . .
5 VAL N . 0.841 . . . . . . . . . . . . .
7 PHE N . 0.900 . . . . . . . . . . . . .
8 ASN N . 0.879 . . . . . . . . . . . . .
9 ASN N . 0.940 . . . . . . . . . . . . .
10 ALA N . 0.939 . . . . . . . . . . . . .
12 SER N . 0.903 . . . . . . . . . . . . .
13 TYR N . 0.922 . . . . . . . . . . . . .
14 VAL N . 0.932 . . . . . . . . . . . . .
15 ASN N . 0.927 . . . . . . . . . . . . .
16 LYS N . 0.976 . . . . . . . . . . . . .
17 ILE N . 0.905 . . . . . . . . . . . . .
18 LYS N . 1.000 . . . . . . . . . . . . .
19 THR N . 0.886 . . . . . . . . . . . . .
20 ARG N . 0.933 . . . . . . . . . . . . .
21 PHE N . 0.863 . . . . . . . . . . . . .
22 LEU N . 0.894 . . . . . . . . . . . . .
23 ASP N . 0.881 . . . . . . . . . . . . .
24 HIS N . 0.827 . . . . . . . . . . . . .
26 GLU N . 0.891 . . . . . . . . . . . . .
27 ILE N . 0.940 . . . . . . . . . . . . .
28 TYR N . 0.876 . . . . . . . . . . . . .
29 ARG N . 0.934 . . . . . . . . . . . . .
30 SER N . 0.900 . . . . . . . . . . . . .
31 PHE N . 0.885 . . . . . . . . . . . . .
32 LEU N . 0.918 . . . . . . . . . . . . .
33 GLU N . 0.881 . . . . . . . . . . . . .
34 ILE N . 0.925 . . . . . . . . . . . . .
35 LEU N . 0.937 . . . . . . . . . . . . .
36 HIS N . 0.929 . . . . . . . . . . . . .
37 THR N . 0.935 . . . . . . . . . . . . .
38 TYR N . 0.875 . . . . . . . . . . . . .
41 GLU N . 0.898 . . . . . . . . . . . . .
42 GLN N . 0.900 . . . . . . . . . . . . .
43 LEU N . 0.687 . . . . . . . . . . . . .
44 HIS N . 0.324 . . . . . . . . . . . . .
46 LYS N . 0.521 . . . . . . . . . . . . .
47 GLY N . 0.330 . . . . . . . . . . . . .
50 PHE N . 0.497 . . . . . . . . . . . . .
51 ARG N . 0.518 . . . . . . . . . . . . .
52 GLY N . 0.551 . . . . . . . . . . . . .
53 MET N . 0.583 . . . . . . . . . . . . .
56 GLU N . 0.873 . . . . . . . . . . . . .
58 VAL N . 0.899 . . . . . . . . . . . . .
59 PHE N . 0.937 . . . . . . . . . . . . .
61 GLU N . 0.922 . . . . . . . . . . . . .
62 VAL N . 0.911 . . . . . . . . . . . . .
63 ALA N . 0.930 . . . . . . . . . . . . .
64 ASN N . 0.891 . . . . . . . . . . . . .
65 LEU N . 0.901 . . . . . . . . . . . . .
66 PHE N . 0.883 . . . . . . . . . . . . .
67 ARG N . 0.858 . . . . . . . . . . . . .
68 GLY N . 0.853 . . . . . . . . . . . . .
69 GLN N . 0.864 . . . . . . . . . . . . .
70 GLU N . 0.833 . . . . . . . . . . . . .
71 ASP N . 0.921 . . . . . . . . . . . . .
72 LEU N . 0.777 . . . . . . . . . . . . .
75 GLU N . 0.873 . . . . . . . . . . . . .
76 PHE N . 0.892 . . . . . . . . . . . . .
77 GLY N . 0.862 . . . . . . . . . . . . .
78 GLN N . 0.918 . . . . . . . . . . . . .
79 PHE N . 0.915 . . . . . . . . . . . . .
80 LEU N . 0.865 . . . . . . . . . . . . .
83 ALA N . 0.714 . . . . . . . . . . . . .
85 ARG N . 0.478 . . . . . . . . . . . . .
94 ALA N . 0.065 . . . . . . . . . . . . .
96 MET N . 0.070 . . . . . . . . . . . . .
97 ASN N . 0.055 . . . . . . . . . . . . .
99 GLY N . 0.054 . . . . . . . . . . . . .
101 LYS N . 0.035 . . . . . . . . . . . . .
102 ASN N . 0.063 . . . . . . . . . . . . .
103 GLU N . 0.024 . . . . . . . . . . . . .
104 GLU N . 0.021 . . . . . . . . . . . . .
105 LYS N . 0.024 . . . . . . . . . . . . .
stop_
_Tau_s_value_units .
save_