data_4925
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Structural Basis for the Functional switch of the E. Coli Ada Protein
;
_BMRB_accession_number 4925
_BMRB_flat_file_name bmr4925.str
_Entry_type original
_Submission_date 2000-05-07
_Accession_date 2000-12-13
_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 Lin Yingxi . .
2 Dotsch Volker . .
3 Wintner T. . .
4 Peariso Katrina . .
5 Myers Lawrence C. .
6 Penner-Hahn James E. .
7 Verdine Gregory L. .
8 Wagner Gerhard . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 478
"13C chemical shifts" 85
"15N chemical shifts" 90
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2001-09-12 original author .
stop_
_Original_release_date 2001-09-12
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Structural Basis for the Functional switch of the E. Coli Ada Protein'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 21181598
_PubMed_ID 11284682
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Lin Yingxi . .
2 Dotsch Volker . .
3 Wintner T. . .
4 Peariso Katrina . .
5 Myers Lawrence C. .
6 Penner-Hahn James E. .
7 Verdine Gregory L. .
8 Wagner Gerhard . .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 40
_Journal_issue 14
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 4261
_Page_last 4271
_Year 2001
_Details .
loop_
_Keyword
ADA
'DNA Repair'
N-Ada10
NMR
Structure
stop_
save_
##################################
# Molecular system description #
##################################
save_system_N-Ada10
_Saveframe_category molecular_system
_Mol_system_name N-Ada10
_Abbreviation_common N-Ada10
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'N-Ada10 subunit 1' $N-Ada10
Zn2+ $ZN
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'other bound and free'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_N-Ada10
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common N-Ada10
_Abbreviation_common N-Ada10
_Molecular_mass .
_Mol_thiol_state 'not reported'
_Details
;
Cys 6 and Cys 91 are free, Cys 38, 42, 69, and 72 are bound to the Zinc
atom.
;
##############################
# Polymer residue sequence #
##############################
_Residue_count 92
_Mol_residue_sequence
;
MKKATCLTDDQRWQSVLARD
PNADGEFVFAVRTTGIFCRP
SCRARHALRENVSFYANASE
ALAAGFRPCKRCQPDKANPR
QHRLDKITHACR
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 LYS 3 LYS 4 ALA 5 THR
6 CYS 7 LEU 8 THR 9 ASP 10 ASP
11 GLN 12 ARG 13 TRP 14 GLN 15 SER
16 VAL 17 LEU 18 ALA 19 ARG 20 ASP
21 PRO 22 ASN 23 ALA 24 ASP 25 GLY
26 GLU 27 PHE 28 VAL 29 PHE 30 ALA
31 VAL 32 ARG 33 THR 34 THR 35 GLY
36 ILE 37 PHE 38 CYS 39 ARG 40 PRO
41 SER 42 CYS 43 ARG 44 ALA 45 ARG
46 HIS 47 ALA 48 LEU 49 ARG 50 GLU
51 ASN 52 VAL 53 SER 54 PHE 55 TYR
56 ALA 57 ASN 58 ALA 59 SER 60 GLU
61 ALA 62 LEU 63 ALA 64 ALA 65 GLY
66 PHE 67 ARG 68 PRO 69 CYS 70 LYS
71 ARG 72 CYS 73 GLN 74 PRO 75 ASP
76 LYS 77 ALA 78 ASN 79 PRO 80 ARG
81 GLN 82 HIS 83 ARG 84 LEU 85 ASP
86 LYS 87 ILE 88 THR 89 HIS 90 ALA
91 CYS 92 ARG
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
REF YP_670153 'ADA regulatory protein [Escherichia coli 536]' 100.00 354 98.91 98.91 2.16e-48
REF YP_408500 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella boydii Sb227]' 100.00 354 98.91 98.91 2.11e-48
REF YP_311153 'O6-methylguanine-DNA methyltransferase [Shigella sonnei Ss046]' 100.00 354 98.91 98.91 2.11e-48
REF NP_837823 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 2457T]' 100.00 354 98.91 98.91 2.11e-48
REF NP_708108 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 301]' 100.00 354 98.91 98.91 2.11e-48
GenBank ABB66672 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella boydii Sb227]' 100.00 354 98.91 98.91 2.11e-48
GenBank AAZ88918 'O6-methylguanine-DNA methyltransferase [Shigella sonnei Ss046]' 100.00 354 98.91 98.91 2.11e-48
GenBank AAP17632 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 2457T]' 100.00 354 98.91 98.91 2.11e-48
GenBank AAN43815 'O6-methylguanine-DNA methyltransferase; transcription activator/repressor [Shigella flexneri 2a str. 301]' 100.00 354 98.91 98.91 2.11e-48
GenBank AAA23413 'Ada polyprotein' 100.00 354 100.00 100.00 5.37e-49
PDB 1ZGW 'Nmr Structure Of E. Coli Ada Protein In Complex With Dna' 100.00 139 98.91 98.91 3.42e-47
PDB 1U8B 'Crystal Structure Of The Methylated N-AdaDNA COMPLEX' 91.30 133 98.81 98.81 2.46e-42
PDB 1EYF 'Refined Structure Of The Dna Methyl Phosphotriester Repair Domain Of E. Coli Ada' 98.91 92 100.00 100.00 4.82e-47
PDB 1ADN 'Solution Structure Of The Dna Methylphosphotriester Repair Domain Of Escherichia Coli Ada' 100.00 92 100.00 100.00 1.82e-47
BMRB 6605 Ada 100.00 139 98.91 98.91 3.54e-47
stop_
save_
#############
# Ligands #
#############
save_ZN
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "ZN (ZINC ION)"
_BMRB_code .
_PDB_code ZN
_Molecular_mass 65.409
_Mol_charge 2
_Mol_paramagnetic .
_Mol_aromatic no
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Wed Jun 15 12:20:01 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
ZN ZN ZN . 2 . ?
stop_
_Mol_thiol_state .
_Sequence_homology_query_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$N-Ada10 'E. coli' 562 Bacteria . Escherichia coli
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
$N-Ada10 'recombinant technology' . . . . .
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
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$N-Ada10 . mM 2 3 '[U-15N; U-13C]'
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer1
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Unity-plus
_Field_strength 750
_Details .
save_
save_NMR_spectrometer2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Unity-plus
_Field_strength 450
_Details .
save_
save_NMR_spectrometer3
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer4
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_1H-15N_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N NOESY'
_Sample_label $sample_1
save_
save_1H-15N_TOCSY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N TOCSY'
_Sample_label $sample_1
save_
save_2D_NOESY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label $sample_1
save_
save_HCCH-TOCSY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N TOCSY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_Ex-cond1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.4 0.1 n/a
temperature 298 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
_Indirect_shift_ratio_citation_label
_Correction_value_citation_label
DSS H 1 'methyl protons' ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo 1.0 $entry_citation $entry_citation
DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $entry_citation $entry_citation
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $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_
_Experiment_label
'1H-15N NOESY'
'1H-15N TOCSY'
'2D NOESY'
HCCH-TOCSY
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $Ex-cond1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'N-Ada10 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 . 4 ALA H H 8.453 0.02 1
2 . 4 ALA HA H 4.361 0.02 1
3 . 4 ALA HB H 1.401 0.02 1
4 . 4 ALA CA C 52.3 0.02 1
5 . 4 ALA N N 126.854 0.02 1
6 . 5 THR H H 8.453 0.02 1
7 . 5 THR HA H 4.316 0.02 1
8 . 5 THR HB H 4.198 0.02 1
9 . 5 THR HG2 H 1.2 0.02 1
10 . 5 THR CA C 62.24 0.02 1
11 . 5 THR N N 114.521 0.02 1
12 . 6 CYS H H 8.74 0.02 1
13 . 6 CYS HA H 4.493 0.02 1
14 . 6 CYS HB2 H 2.9 0.02 2
15 . 6 CYS HB3 H 2.702 0.02 2
16 . 6 CYS CA C 58.33 0.02 1
17 . 6 CYS N N 122.768 0.02 1
18 . 7 LEU H H 8.382 0.02 1
19 . 7 LEU HA H 4.444 0.02 1
20 . 7 LEU HB2 H 1.62 0.02 2
21 . 7 LEU HB3 H 1.503 0.02 2
22 . 7 LEU HD1 H 0.9 0.02 1
23 . 7 LEU HD2 H 0.8 0.02 1
24 . 7 LEU CA C 55.38 0.02 1
25 . 7 LEU N N 123.771 0.02 1
26 . 8 THR H H 7.943 0.02 1
27 . 8 THR HA H 4.48 0.02 1
28 . 8 THR HB H 4.534 0.02 1
29 . 8 THR HG2 H 1.191 0.02 1
30 . 8 THR CA C 60.03 0.02 1
31 . 8 THR N N 110.41 0.02 1
32 . 9 ASP H H 8.941 0.02 1
33 . 9 ASP HA H 3.8 0.02 1
34 . 9 ASP HB2 H 2.571 0.02 1
35 . 9 ASP HB3 H 2.571 0.02 1
36 . 9 ASP CA C 57.23 0.02 1
37 . 9 ASP N N 122.768 0.02 1
38 . 10 ASP H H 8.153 0.02 1
39 . 10 ASP HA H 4.467 0.02 1
40 . 10 ASP HB2 H 2.575 0.02 2
41 . 10 ASP HB3 H 2.694 0.02 2
42 . 10 ASP CA C 57.51 0.02 1
43 . 10 ASP N N 119.146 0.02 1
44 . 11 GLN H H 7.609 0.02 1
45 . 11 GLN HA H 4.001 0.02 1
46 . 11 GLN HB2 H 2.191 0.02 2
47 . 11 GLN HB3 H 2.049 0.02 2
48 . 11 GLN HG2 H 2.41 0.02 1
49 . 11 GLN HG3 H 2.41 0.02 1
50 . 11 GLN HE21 H 7.489 0.02 1
51 . 11 GLN HE22 H 6.778 0.02 1
52 . 11 GLN CA C 58.83 0.02 1
53 . 11 GLN N N 120.571 0.02 1
54 . 11 GLN NE2 N 111.5 0.02 1
55 . 12 ARG H H 8.042 0.02 1
56 . 12 ARG HA H 3.352 0.02 1
57 . 12 ARG HB2 H 0.531 0.02 2
58 . 12 ARG HB3 H -0.197 0.02 2
59 . 12 ARG HG2 H 1.126 0.02 2
60 . 12 ARG HG3 H 0.048 0.02 2
61 . 12 ARG HD2 H 2.07 0.02 2
62 . 12 ARG HD3 H 1.7 0.02 2
63 . 12 ARG CA C 59.13 0.02 1
64 . 12 ARG N N 120.7 0.02 1
65 . 13 TRP H H 8.372 0.02 1
66 . 13 TRP HA H 4.659 0.02 1
67 . 13 TRP HB2 H 3.319 0.02 1
68 . 13 TRP HB3 H 3.385 0.02 1
69 . 13 TRP HD1 H 7.238 0.02 1
70 . 13 TRP HE1 H 10.375 0.02 1
71 . 13 TRP HE3 H 7.334 0.02 1
72 . 13 TRP HZ2 H 7.468 0.02 1
73 . 13 TRP HZ3 H 6.447 0.02 1
74 . 13 TRP HH2 H 7.080 0.02 1
75 . 13 TRP CA C 58.95 0.02 1
76 . 13 TRP N N 119.146 0.02 1
77 . 13 TRP NE1 N 129.3 0.02 1
78 . 14 GLN H H 7.782 0.02 1
79 . 14 GLN HA H 3.71 0.02 1
80 . 14 GLN HB2 H 2.172 0.02 1
81 . 14 GLN HB3 H 2.172 0.02 1
82 . 14 GLN HG2 H 2.534 0.02 1
83 . 14 GLN HG3 H 2.534 0.02 1
84 . 14 GLN HE21 H 7.620 0.02 1
85 . 14 GLN HE22 H 6.884 0.02 1
86 . 14 GLN CA C 59.05 0.02 1
87 . 14 GLN N N 116.078 0.02 1
88 . 14 GLN NE2 N 113.0 0.02 1
89 . 15 SER H H 7.84 0.02 1
90 . 15 SER HA H 4.338 0.02 1
91 . 15 SER HB2 H 3.855 0.02 1
92 . 15 SER HB3 H 3.855 0.02 1
93 . 15 SER CA C 63.82 0.02 1
94 . 15 SER N N 117.089 0.02 1
95 . 16 VAL H H 7.707 0.02 1
96 . 16 VAL HA H 3.718 0.02 1
97 . 16 VAL HB H 1.852 0.02 1
98 . 16 VAL HG1 H 1.14 0.02 1
99 . 16 VAL HG2 H -0.202 0.02 1
100 . 16 VAL CA C 66.36 0.02 1
101 . 16 VAL N N 123.262 0.02 1
102 . 17 LEU H H 8.066 0.02 1
103 . 17 LEU HA H 3.309 0.02 1
104 . 17 LEU HB2 H 1.07 0.02 1
105 . 17 LEU HB3 H 1.434 0.02 1
106 . 17 LEU HG H 0.358 0.02 1
107 . 17 LEU HD1 H 0.555 0.02 1
108 . 17 LEU HD2 H 0.23 0.02 1
109 . 17 LEU CA C 57.51 0.02 1
110 . 17 LEU N N 110.143 0.02 1
111 . 18 ALA H H 7.387 0.02 1
112 . 18 ALA HA H 4.165 0.02 1
113 . 18 ALA HB H 1.405 0.02 1
114 . 18 ALA CA C 51.9 0.02 1
115 . 18 ALA N N 117.604 0.02 1
116 . 19 ARG H H 8.101 0.02 1
117 . 19 ARG HA H 4.255 0.02 1
118 . 19 ARG HB2 H 1.93 0.02 2
119 . 19 ARG HB3 H 1.545 0.02 2
120 . 19 ARG CA C 56 0.02 1
121 . 19 ARG N N 121.149 0.02 1
122 . 20 ASP H H 7.617 0.02 1
123 . 20 ASP HA H 4.578 0.02 1
124 . 20 ASP HB2 H 2.829 0.02 1
125 . 20 ASP HB3 H 2.556 0.02 1
126 . 20 ASP CA C 51.51 0.02 1
127 . 20 ASP N N 117.09 0.02 1
128 . 21 PRO HA H 4.371 0.02 1
129 . 21 PRO HB2 H 2.305 0.02 2
130 . 21 PRO HB3 H 2.009 0.02 2
131 . 21 PRO HG2 H 2.02 0.02 1
132 . 21 PRO HG3 H 2.02 0.02 1
133 . 21 PRO HD2 H 4.426 0.02 2
134 . 21 PRO HD3 H 4.014 0.02 2
135 . 21 PRO CA C 64 0.02 1
136 . 22 ASN H H 8.519 0.02 1
137 . 22 ASN HA H 4.515 0.02 1
138 . 22 ASN HB2 H 2.95 0.02 1
139 . 22 ASN HB3 H 2.752 0.02 1
140 . 22 ASN HD21 H 7.045 0.02 1
141 . 22 ASN HD22 H 8.130 0.02 1
142 . 22 ASN CA C 55.05 0.02 1
143 . 22 ASN N N 117.09 0.02 1
144 . 22 ASN ND2 N 115.7 0.02 1
145 . 23 ALA H H 7.755 0.02 1
146 . 23 ALA HA H 4.394 0.02 1
147 . 23 ALA HB H 1.472 0.02 1
148 . 23 ALA CA C 51.67 0.02 1
149 . 23 ALA N N 120.701 0.02 1
150 . 24 ASP H H 7.213 0.02 1
151 . 24 ASP HA H 4.4 0.02 1
152 . 24 ASP HB2 H 2.515 0.02 1
153 . 24 ASP HB3 H 2.943 0.02 1
154 . 24 ASP CA C 56.49 0.02 1
155 . 24 ASP N N 120.687 0.02 1
156 . 25 GLY H H 9.673 0.02 1
157 . 25 GLY HA2 H 4.291 0.02 2
158 . 25 GLY HA3 H 3.723 0.02 2
159 . 25 GLY CA C 45.11 0.02 1
160 . 25 GLY N N 111.951 0.02 1
161 . 26 GLU H H 8.376 0.02 1
162 . 26 GLU HA H 4.421 0.02 1
163 . 26 GLU HB2 H 2.397 0.02 2
164 . 26 GLU HB3 H 2.443 0.02 2
165 . 26 GLU HG2 H 2.505 0.02 2
166 . 26 GLU HG3 H 2.245 0.02 2
167 . 26 GLU CA C 57.89 0.02 1
168 . 26 GLU N N 121.241 0.02 1
169 . 27 PHE H H 7.295 0.02 1
170 . 27 PHE HA H 5.1 0.02 1
171 . 27 PHE HB2 H 3.582 0.02 1
172 . 27 PHE HB3 H 3.426 0.02 1
173 . 27 PHE HD1 H 7.247 0.02 1
174 . 27 PHE HD2 H 7.247 0.02 1
175 . 27 PHE HE1 H 7.325 0.02 1
176 . 27 PHE HE2 H 7.325 0.02 1
177 . 27 PHE HZ H 7.473 0.02 1
178 . 27 PHE CA C 56.17 0.02 1
179 . 27 PHE N N 110.431 0.02 1
180 . 28 VAL H H 9.038 0.02 1
181 . 28 VAL HA H 5.035 0.02 1
182 . 28 VAL HB H 2.358 0.02 1
183 . 28 VAL HG1 H 0.414 0.02 1
184 . 28 VAL HG2 H 0.856 0.02 1
185 . 28 VAL CA C 59.66 0.02 1
186 . 28 VAL N N 109.901 0.02 1
187 . 29 PHE H H 9.14 0.02 1
188 . 29 PHE HA H 5.962 0.02 1
189 . 29 PHE HB2 H 2.92 0.02 1
190 . 29 PHE HB3 H 3.085 0.02 1
191 . 29 PHE HD1 H 6.875 0.02 1
192 . 29 PHE HD2 H 6.875 0.02 1
193 . 29 PHE HE1 H 7.466 0.02 1
194 . 29 PHE HE2 H 7.466 0.02 1
195 . 29 PHE HZ H 7.636 0.02 1
196 . 29 PHE CA C 54.67 0.02 1
197 . 29 PHE N N 120.174 0.02 1
198 . 30 ALA H H 9.432 0.02 1
199 . 30 ALA HA H 4.826 0.02 1
200 . 30 ALA HB H 0.141 0.02 1
201 . 30 ALA CA C 49.71 0.02 1
202 . 30 ALA N N 125.826 0.02 1
203 . 31 VAL H H 8.167 0.02 1
204 . 31 VAL HA H 4.72 0.02 1
205 . 31 VAL HB H 2.411 0.02 1
206 . 31 VAL HG1 H 1.173 0.02 1
207 . 31 VAL HG2 H 1.207 0.02 1
208 . 31 VAL CA C 61.87 0.02 1
209 . 31 VAL N N 122.237 0.02 1
210 . 32 ARG H H 9.225 0.02 1
211 . 32 ARG HA H 4.279 0.02 1
212 . 32 ARG HB2 H 2.079 0.02 1
213 . 32 ARG HB3 H 2.079 0.02 1
214 . 32 ARG HG2 H 1.781 0.02 1
215 . 32 ARG HG3 H 1.781 0.02 1
216 . 32 ARG HD2 H 3.361 0.02 2
217 . 32 ARG HD3 H 3.324 0.02 2
218 . 32 ARG CA C 60.02 0.02 1
219 . 32 ARG N N 127.914 0.02 1
220 . 33 THR H H 7.508 0.02 1
221 . 33 THR HA H 4.32 0.02 1
222 . 33 THR HB H 4.21 0.02 1
223 . 33 THR HG2 H 1.277 0.02 1
224 . 33 THR CA C 63.46 0.02 1
225 . 33 THR N N 105.785 0.02 1
226 . 34 THR H H 7.153 0.02 1
227 . 34 THR HA H 4.57 0.02 1
228 . 34 THR HB H 4.348 0.02 1
229 . 34 THR HG2 H 1.228 0.02 1
230 . 34 THR CA C 61.54 0.02 1
231 . 34 THR N N 108.372 0.02 1
232 . 35 GLY H H 8.521 0.02 1
233 . 35 GLY HA2 H 4.314 0.02 2
234 . 35 GLY HA3 H 3.942 0.02 2
235 . 35 GLY CA C 46.48 0.02 1
236 . 35 GLY N N 109.896 0.02 1
237 . 36 ILE H H 7.683 0.02 1
238 . 36 ILE HA H 5.504 0.02 1
239 . 36 ILE HB H 1.786 0.02 1
240 . 36 ILE HG12 H 1.114 0.02 1
241 . 36 ILE HG13 H 1.476 0.02 1
242 . 36 ILE HG2 H 0.875 0.02 1
243 . 36 ILE HD1 H 0.821 0.02 1
244 . 36 ILE CA C 59.02 0.02 1
245 . 36 ILE N N 122.75 0.02 1
246 . 37 PHE H H 8.782 0.02 1
247 . 37 PHE HA H 5.816 0.02 1
248 . 37 PHE HB2 H 2.741 0.02 1
249 . 37 PHE HB3 H 2.251 0.02 1
250 . 37 PHE HD1 H 6.747 0.02 1
251 . 37 PHE HD2 H 6.747 0.02 1
252 . 37 PHE HE1 H 6.889 0.02 1
253 . 37 PHE HE2 H 6.889 0.02 1
254 . 37 PHE HZ H 7.011 0.02 1
255 . 37 PHE CA C 54.57 0.02 1
256 . 37 PHE N N 124.46 0.02 1
257 . 38 CYS H H 8.428 0.02 1
258 . 38 CYS HA H 4.208 0.02 1
259 . 38 CYS HB2 H 2.958 0.02 1
260 . 38 CYS HB3 H 0.82 0.02 1
261 . 38 CYS CA C 61.24 0.02 1
262 . 38 CYS N N 118.632 0.02 1
263 . 39 ARG H H 9.348 0.02 1
264 . 39 ARG HA H 4.897 0.02 1
265 . 39 ARG HB2 H 1.793 0.02 2
266 . 39 ARG HB3 H 1.896 0.02 2
267 . 39 ARG HG2 H 1.593 0.02 2
268 . 39 ARG HG3 H 1.563 0.02 2
269 . 39 ARG HD2 H 3.212 0.02 2
270 . 39 ARG HD3 H 3.165 0.02 2
271 . 39 ARG CA C 63.44 0.02 1
272 . 39 ARG N N 121.201 0.02 1
273 . 40 PRO HA H 4.436 0.02 1
274 . 40 PRO HB2 H 1.859 0.02 1
275 . 40 PRO HB3 H 1.859 0.02 1
276 . 40 PRO HG2 H 1.588 0.02 2
277 . 40 PRO HG3 H 0.945 0.02 2
278 . 40 PRO HD2 H 3.65 0.02 2
279 . 40 PRO HD3 H 4.066 0.02 2
280 . 40 PRO CA C 66.08 0.02 1
281 . 41 SER H H 8.604 0.02 1
282 . 41 SER HA H 3.72 0.02 1
283 . 41 SER HB2 H 4.003 0.02 2
284 . 41 SER HB3 H 3.411 0.02 2
285 . 41 SER CA C 58.59 0.02 1
286 . 41 SER N N 108.354 0.02 1
287 . 42 CYS H H 8.095 0.02 1
288 . 42 CYS HA H 3.942 0.02 1
289 . 42 CYS HB2 H 3.517 0.02 1
290 . 42 CYS HB3 H 3.215 0.02 1
291 . 42 CYS CA C 62.77 0.02 1
292 . 42 CYS N N 125.826 0.02 1
293 . 43 ARG H H 8.596 0.02 1
294 . 43 ARG HA H 3.992 0.02 1
295 . 43 ARG HB2 H 1.746 0.02 1
296 . 43 ARG HB3 H 2.066 0.02 1
297 . 43 ARG HG2 H 1.898 0.02 1
298 . 43 ARG HG3 H 1.898 0.02 1
299 . 43 ARG HD2 H 3.244 0.02 1
300 . 43 ARG HD3 H 3.244 0.02 1
301 . 43 ARG CA C 57.21 0.02 1
302 . 43 ARG N N 126.84 0.02 1
303 . 44 ALA H H 8.758 0.02 1
304 . 44 ALA HA H 4.187 0.02 1
305 . 44 ALA HB H 1.516 0.02 1
306 . 44 ALA CA C 53.13 0.02 1
307 . 44 ALA N N 125.52 0.02 1
308 . 45 ARG H H 8.464 0.02 1
309 . 45 ARG HA H 3.941 0.02 1
310 . 45 ARG HB2 H 1.827 0.02 2
311 . 45 ARG HB3 H 1.766 0.02 2
312 . 45 ARG HG2 H 1.73 0.02 1
313 . 45 ARG HG3 H 1.73 0.02 1
314 . 45 ARG HD2 H 3.238 0.02 1
315 . 45 ARG HD3 H 3.238 0.02 1
316 . 45 ARG CA C 56.52 0.02 1
317 . 45 ARG N N 121.201 0.02 1
318 . 46 HIS H H 8.842 0.02 1
319 . 46 HIS HA H 4.789 0.02 1
320 . 46 HIS HB2 H 3.267 0.02 2
321 . 46 HIS HB3 H 3.1 0.02 2
322 . 46 HIS HD2 H 7.19 0.02 1
323 . 46 HIS HE1 H 8.129 0.02 1
324 . 46 HIS N N 123.13 0.02 1
325 . 47 ALA H H 8.248 0.02 1
326 . 47 ALA HA H 4.562 0.02 1
327 . 47 ALA HB H 1.557 0.02 1
328 . 47 ALA CA C 50.53 0.02 1
329 . 47 ALA N N 125.312 0.02 1
330 . 48 LEU H H 8.131 0.02 1
331 . 48 LEU HA H 4.426 0.02 1
332 . 48 LEU HB2 H 1.602 0.02 2
333 . 48 LEU HB3 H 1.688 0.02 2
334 . 48 LEU HG H 1.808 0.02 1
335 . 48 LEU HD1 H 0.985 0.02 1
336 . 48 LEU HD2 H 0.95 0.02 1
337 . 48 LEU CA C 54.53 0.02 1
338 . 48 LEU N N 118.118 0.02 1
339 . 49 ARG H H 8.545 0.02 1
340 . 49 ARG HA H 2.62 0.02 1
341 . 49 ARG HB2 H 1.059 0.02 1
342 . 49 ARG HB3 H 1.374 0.02 1
343 . 49 ARG HG2 H 1.21 0.02 2
344 . 49 ARG HG3 H 0.6 0.02 2
345 . 49 ARG HD2 H 1.92 0.02 2
346 . 49 ARG HD3 H 1.6 0.02 2
347 . 49 ARG CA C 58.33 0.02 1
348 . 49 ARG N N 123.257 0.02 1
349 . 50 GLU H H 9.066 0.02 1
350 . 50 GLU HA H 4.094 0.02 1
351 . 50 GLU HB2 H 2.104 0.02 2
352 . 50 GLU HB3 H 1.97 0.02 2
353 . 50 GLU HG2 H 2.014 0.02 1
354 . 50 GLU HG3 H 2.014 0.02 1
355 . 50 GLU CA C 58.17 0.02 1
356 . 50 GLU N N 115.035 0.02 1
357 . 51 ASN H H 8.014 0.02 1
358 . 51 ASN HA H 5.08 0.02 1
359 . 51 ASN HB2 H 3.181 0.02 1
360 . 51 ASN HB3 H 2.807 0.02 1
361 . 51 ASN HD21 H 7.760 0.02 1
362 . 51 ASN HD22 H 7.427 0.02 1
363 . 51 ASN CA C 52.6 0.02 1
364 . 51 ASN N N 116.576 0.02 1
365 . 51 ASN ND2 N 124.1 0.02 1
366 . 52 VAL H H 7.591 0.02 1
367 . 52 VAL HA H 5.089 0.02 1
368 . 52 VAL HB H 1.662 0.02 1
369 . 52 VAL HG1 H 0.873 0.02 1
370 . 52 VAL HG2 H 0.585 0.02 1
371 . 52 VAL CA C 61.67 0.02 1
372 . 52 VAL N N 121.22 0.02 1
373 . 53 SER H H 8.852 0.02 1
374 . 53 SER HA H 4.45 0.02 1
375 . 53 SER HB2 H 3.665 0.02 1
376 . 53 SER HB3 H 3.427 0.02 1
377 . 53 SER CA C 56.4 0.02 1
378 . 53 SER N N 121.712 0.02 1
379 . 54 PHE H H 8.562 0.02 1
380 . 54 PHE HA H 5.375 0.02 1
381 . 54 PHE HB2 H 2.724 0.02 1
382 . 54 PHE HB3 H 2.823 0.02 1
383 . 54 PHE HD1 H 7.183 0.02 1
384 . 54 PHE HD2 H 7.183 0.02 1
385 . 54 PHE HE1 H 7.122 0.02 1
386 . 54 PHE HE2 H 7.122 0.02 1
387 . 54 PHE HZ H 7.159 0.02 1
388 . 54 PHE CA C 57.1 0.02 1
389 . 54 PHE N N 119.329 0.02 1
390 . 55 TYR H H 8.636 0.02 1
391 . 55 TYR HA H 4.729 0.02 1
392 . 55 TYR HB2 H 3.161 0.02 1
393 . 55 TYR HB3 H 2.212 0.02 1
394 . 55 TYR HD1 H 6.727 0.02 1
395 . 55 TYR HD2 H 6.727 0.02 1
396 . 55 TYR HE1 H 6.457 0.02 1
397 . 55 TYR HE2 H 6.457 0.02 1
398 . 55 TYR CA C 57.16 0.02 1
399 . 55 TYR N N 117.616 0.02 1
400 . 56 ALA H H 9.134 0.02 1
401 . 56 ALA HA H 4.3 0.02 1
402 . 56 ALA HB H 1.529 0.02 1
403 . 56 ALA CA C 54.59 0.02 1
404 . 56 ALA N N 122.77 0.02 1
405 . 57 ASN H H 7.197 0.02 1
406 . 57 ASN HA H 4.509 0.02 1
407 . 57 ASN HB2 H 3.024 0.02 1
408 . 57 ASN HB3 H 3.194 0.02 1
409 . 57 ASN HD21 H 7.053 0.02 1
410 . 57 ASN HD22 H 7.666 0.02 1
411 . 57 ASN N N 104.243 0.02 1
412 . 57 ASN ND2 N 115.7 0.02 1
413 . 58 ALA H H 8.93 0.02 1
414 . 58 ALA HA H 3.577 0.02 1
415 . 58 ALA HB H 1.534 0.02 1
416 . 58 ALA CA C 54.55 0.02 1
417 . 58 ALA N N 120.682 0.02 1
418 . 59 SER H H 8.31 0.02 1
419 . 59 SER HA H 4.073 0.02 1
420 . 59 SER HB2 H 3.9 0.02 1
421 . 59 SER HB3 H 3.9 0.02 1
422 . 59 SER CA C 62.38 0.02 1
423 . 59 SER N N 113.493 0.02 1
424 . 60 GLU H H 8.162 0.02 1
425 . 60 GLU HA H 3.986 0.02 1
426 . 60 GLU HB2 H 2.241 0.02 2
427 . 60 GLU HB3 H 2.047 0.02 2
428 . 60 GLU HG2 H 2.609 0.02 2
429 . 60 GLU HG3 H 2.361 0.02 2
430 . 60 GLU CA C 59.11 0.02 1
431 . 60 GLU N N 122.545 0.02 1
432 . 61 ALA H H 6.886 0.02 1
433 . 61 ALA HA H 2.674 0.02 1
434 . 61 ALA HB H -0.09 0.02 1
435 . 61 ALA CA C 54.35 0.02 1
436 . 61 ALA N N 122.229 0.02 1
437 . 62 LEU H H 8.222 0.02 1
438 . 62 LEU HA H 4.473 0.02 1
439 . 62 LEU HB2 H 1.834 0.02 2
440 . 62 LEU HB3 H 1.543 0.02 2
441 . 62 LEU HG H 1.776 0.02 1
442 . 62 LEU HD1 H 1.226 0.02 1
443 . 62 LEU HD2 H 1.005 0.02 1
444 . 62 LEU CA C 57.26 0.02 1
445 . 62 LEU N N 120.155 0.02 1
446 . 63 ALA H H 7.817 0.02 1
447 . 63 ALA HA H 4.087 0.02 1
448 . 63 ALA HB H 1.463 0.02 1
449 . 63 ALA CA C 54.37 0.02 1
450 . 63 ALA N N 122.743 0.02 1
451 . 64 ALA H H 7.141 0.02 1
452 . 64 ALA HA H 4.338 0.02 1
453 . 64 ALA HB H 1.446 0.02 1
454 . 64 ALA CA C 51.73 0.02 1
455 . 64 ALA N N 118.632 0.02 1
456 . 65 GLY H H 7.707 0.02 1
457 . 65 GLY HA2 H 4.041 0.02 2
458 . 65 GLY HA3 H 3.612 0.02 2
459 . 65 GLY CA C 44.75 0.02 1
460 . 65 GLY N N 105.302 0.02 1
461 . 66 PHE H H 7.701 0.02 1
462 . 66 PHE HA H 4.635 0.02 1
463 . 66 PHE HB2 H 2.521 0.02 1
464 . 66 PHE HB3 H 2.992 0.02 1
465 . 66 PHE HD1 H 6.956 0.02 1
466 . 66 PHE HD2 H 6.956 0.02 1
467 . 66 PHE HE1 H 7.278 0.02 1
468 . 66 PHE HE2 H 7.278 0.02 1
469 . 66 PHE HZ H 7.342 0.02 1
470 . 66 PHE CA C 58.03 0.02 1
471 . 66 PHE N N 119.148 0.02 1
472 . 67 ARG H H 9.158 0.02 1
473 . 67 ARG HA H 5.073 0.02 1
474 . 67 ARG HB2 H 1.845 0.02 1
475 . 67 ARG HB3 H 1.845 0.02 1
476 . 67 ARG HG2 H 1.75 0.02 1
477 . 67 ARG HG3 H 1.75 0.02 1
478 . 67 ARG HD2 H 3.208 0.02 1
479 . 67 ARG HD3 H 3.208 0.02 1
480 . 67 ARG CA C 52.37 0.02 1
481 . 67 ARG N N 120.174 0.02 1
482 . 68 PRO HA H 2.791 0.02 1
483 . 68 PRO HB2 H 1.637 0.02 2
484 . 68 PRO HB3 H 1.457 0.02 2
485 . 68 PRO HG2 H 1.96 0.02 2
486 . 68 PRO HG3 H 2.214 0.02 2
487 . 68 PRO HD2 H 3.704 0.02 1
488 . 68 PRO HD3 H 3.704 0.02 1
489 . 68 PRO CA C 62.07 0.02 1
490 . 69 CYS H H 7.946 0.02 1
491 . 69 CYS HA H 3.915 0.02 1
492 . 69 CYS HB2 H 3.233 0.02 1
493 . 69 CYS HB3 H 3.28 0.02 1
494 . 69 CYS CA C 60 0.02 1
495 . 69 CYS N N 127.368 0.02 1
496 . 70 LYS H H 8.908 0.02 1
497 . 70 LYS HA H 4.174 0.02 1
498 . 70 LYS HB2 H 1.935 0.02 2
499 . 70 LYS HB3 H 1.826 0.02 2
500 . 70 LYS CA C 57.79 0.02 1
501 . 70 LYS N N 127.882 0.02 1
502 . 71 ARG H H 9.698 0.02 1
503 . 71 ARG HA H 4.319 0.02 1
504 . 71 ARG HB2 H 1.862 0.02 2
505 . 71 ARG HB3 H 1.962 0.02 2
506 . 71 ARG HG2 H 1.676 0.02 2
507 . 71 ARG HG3 H 1.642 0.02 2
508 . 71 ARG HD2 H 3.167 0.02 2
509 . 71 ARG HD3 H 3.068 0.02 2
510 . 71 ARG CA C 58.07 0.02 1
511 . 71 ARG N N 122.745 0.02 1
512 . 72 CYS H H 8.538 0.02 1
513 . 72 CYS HA H 4.859 0.02 1
514 . 72 CYS HB2 H 3.11 0.02 1
515 . 72 CYS HB3 H 3.035 0.02 1
516 . 72 CYS CA C 59.19 0.02 1
517 . 72 CYS N N 118.118 0.02 1
518 . 73 GLN H H 7.542 0.02 1
519 . 73 GLN HA H 4.24 0.02 1
520 . 73 GLN HB2 H 2.17 0.02 2
521 . 73 GLN HB3 H 1.95 0.02 2
522 . 73 GLN HG2 H 2.27 0.02 2
523 . 73 GLN HG3 H 2.11 0.02 2
524 . 73 GLN HE21 H 7.39 0.02 1
525 . 73 GLN HE22 H 6.69 0.02 1
526 . 73 GLN CA C 56.23 0.02 1
527 . 73 GLN N N 117.64 0.02 1
528 . 73 GLN NE2 N 112.0 0.02 1
529 . 74 PRO HA H 4.27 0.02 1
530 . 74 PRO HB2 H 2.324 0.02 2
531 . 74 PRO HB3 H 1.91 0.02 2
532 . 74 PRO HG2 H 2.173 0.02 1
533 . 74 PRO HG3 H 2.173 0.02 1
534 . 74 PRO HD2 H 3.69 0.02 1
535 . 74 PRO HD3 H 3.69 0.02 1
536 . 74 PRO CA C 64.54 0.02 1
537 . 75 ASP H H 9.72 0.02 1
538 . 75 ASP HA H 4.372 0.02 1
539 . 75 ASP HB2 H 2.292 0.02 2
540 . 75 ASP HB3 H 2.843 0.02 2
541 . 75 ASP CA C 53.6 0.02 1
542 . 75 ASP N N 117.09 0.02 1
543 . 76 LYS H H 7.507 0.02 1
544 . 76 LYS HA H 4.425 0.02 1
545 . 76 LYS HB2 H 1.847 0.02 2
546 . 76 LYS HB3 H 1.738 0.02 2
547 . 76 LYS HG2 H 1.42 0.02 2
548 . 76 LYS HG3 H 1.33 0.02 2
549 . 76 LYS HD2 H 1.627 0.02 1
550 . 76 LYS HD3 H 1.627 0.02 1
551 . 76 LYS CA C 55 0.02 1
552 . 76 LYS N N 120.758 0.02 1
553 . 77 ALA H H 7.98 0.02 1
554 . 77 ALA HA H 4.279 0.02 1
555 . 77 ALA HB H 1.357 0.02 1
556 . 77 ALA CA C 52.39 0.02 1
557 . 77 ALA N N 124.982 0.02 1
558 . 78 ASN H H 8.38 0.02 1
559 . 78 ASN HA H 4.976 0.02 1
560 . 78 ASN HB2 H 2.84 0.02 2
561 . 78 ASN HB3 H 2.68 0.02 2
562 . 78 ASN HD21 H 7.674 0.02 1
563 . 78 ASN HD22 H 6.962 0.02 1
564 . 78 ASN CA C 51.19 0.02 1
565 . 78 ASN N N 119.366 0.02 1
566 . 78 ASN ND2 N 113.2 0.02 1
567 . 79 PRO HA H 4.436 0.02 1
568 . 79 PRO HB2 H 2.29 0.02 2
569 . 79 PRO HB3 H 1.94 0.02 2
570 . 79 PRO HG2 H 2.027 0.02 1
571 . 79 PRO HG3 H 2.027 0.02 1
572 . 79 PRO HD2 H 3.756 0.02 1
573 . 79 PRO HD3 H 3.756 0.02 1
574 . 79 PRO CA C 63.44 0.02 1
575 . 80 ARG H H 8.377 0.02 1
576 . 80 ARG HA H 4.274 0.02 1
577 . 80 ARG HB2 H 1.858 0.02 2
578 . 80 ARG HB3 H 1.753 0.02 2
579 . 80 ARG HG2 H 1.65 0.02 1
580 . 80 ARG HG3 H 1.65 0.02 1
581 . 80 ARG HD2 H 3.24 0.02 1
582 . 80 ARG HD3 H 3.24 0.02 1
583 . 80 ARG CA C 56.24 0.02 1
584 . 80 ARG N N 120.783 0.02 1
585 . 81 GLN H H 8.263 0.02 1
586 . 81 GLN HA H 4.261 0.02 1
587 . 81 GLN HB2 H 2.025 0.02 2
588 . 81 GLN HB3 H 1.974 0.02 2
589 . 81 GLN HG2 H 2.324 0.02 1
590 . 81 GLN HG3 H 2.324 0.02 1
591 . 81 GLN HE21 H 7.570 0.02 1
592 . 81 GLN HE22 H 6.906 0.02 1
593 . 81 GLN CA C 55.9 0.02 1
594 . 81 GLN N N 121.201 0.02 1
595 . 81 GLN NE2 N 112.7 0.02 1
596 . 82 HIS H H 8.43 0.02 1
597 . 82 HIS HA H 4.688 0.02 1
598 . 82 HIS HB2 H 3.2 0.02 2
599 . 82 HIS HB3 H 3.12 0.02 2
600 . 82 HIS CA C 55.56 0.02 1
601 . 82 HIS N N 120.82 0.02 1
602 . 83 ARG H H 8.357 0.02 1
603 . 83 ARG HA H 4.33 0.02 1
604 . 83 ARG HB2 H 1.84 0.02 2
605 . 83 ARG HB3 H 1.77 0.02 2
606 . 83 ARG HG2 H 1.457 0.02 1
607 . 83 ARG HG3 H 1.457 0.02 1
608 . 83 ARG HD2 H 3.02 0.02 1
609 . 83 ARG HD3 H 3.02 0.02 1
610 . 83 ARG CA C 56.26 0.02 1
611 . 83 ARG N N 124.771 0.02 1
612 . 84 LEU H H 8.468 0.02 1
613 . 84 LEU HA H 4.38 0.02 1
614 . 84 LEU HB2 H 1.631 0.02 1
615 . 84 LEU HB3 H 1.631 0.02 1
616 . 84 LEU HD1 H 0.95 0.02 1
617 . 84 LEU HD2 H 0.89 0.02 1
618 . 84 LEU CA C 55.05 0.02 1
619 . 84 LEU N N 123.257 0.02 1
620 . 85 ASP H H 8.326 0.02 1
621 . 85 ASP HA H 4.594 0.02 1
622 . 85 ASP HB2 H 2.679 0.02 2
623 . 85 ASP HB3 H 2.65 0.02 2
624 . 85 ASP CA C 54.26 0.02 1
625 . 85 ASP N N 120.687 0.02 1
626 . 86 LYS H H 8.153 0.02 1
627 . 86 LYS HA H 4.34 0.02 1
628 . 86 LYS HB2 H 1.88 0.02 2
629 . 86 LYS HB3 H 1.75 0.02 2
630 . 86 LYS CA C 56.12 0.02 1
631 . 86 LYS N N 121.307 0.02 1
632 . 87 ILE H H 8.17 0.02 1
633 . 87 ILE HA H 4.23 0.02 1
634 . 87 ILE HB H 1.86 0.02 1
635 . 87 ILE HG12 H 1.46 0.02 2
636 . 87 ILE HG13 H 1.20 0.02 2
637 . 87 ILE HG2 H 0.85 0.02 1
638 . 87 ILE HD1 H 0.65 0.02 1
639 . 87 ILE CA C 61.11 0.02 1
640 . 87 ILE N N 122.539 0.02 1
641 . 88 THR H H 8.22 0.02 1
642 . 88 THR HA H 4.35 0.02 1
643 . 88 THR HB H 4.21 0.02 1
644 . 88 THR HG2 H 1.19 0.02 1
645 . 88 THR CA C 61.73 0.02 1
646 . 88 THR N N 118.503 0.02 1
647 . 89 HIS H H 8.078 0.02 1
648 . 89 HIS HA H 4.48 0.02 1
649 . 89 HIS HB2 H 3.25 0.02 2
650 . 89 HIS HB3 H 3.11 0.02 2
651 . 89 HIS CA C 57 0.02 1
652 . 89 HIS N N 126.34 0.02 1
653 . 90 ALA CA C 54.72 0.02 1
stop_
save_