data_5217
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution Structure and DNA Binding Properties of the C-Terminal Domain of UvrC
from E. coli
;
_BMRB_accession_number 5217
_BMRB_flat_file_name bmr5217.str
_Entry_type original
_Submission_date 2001-11-23
_Accession_date 2001-11-26
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details .
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Singh Shanteri . .
2 Folkers Gert E .
3 Bonvin Alexandre 'M. J. J.' .
4 Wechselberger Rainer . .
5 Niztayev Alidin . .
6 Boelens Rolf . .
7 Kaptein Robert . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 373
"13C chemical shifts" 261
"15N chemical shifts" 67
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2003-01-14 original author .
stop_
_Original_release_date 2003-01-14
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Solution Structure and DNA-binding Properties of the C-Terminal Domain of UvrC
from E. coli
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22313337
_PubMed_ID 12426397
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Singh Shanteri . .
2 Folkers Gert E. .
3 Bonvin Alexandre M. .
4 Boelens Rolf . .
5 Wechselberger Rainer . .
6 Niztayev Alidin . .
7 Kaptein Robert . .
stop_
_Journal_abbreviation 'EMBO J.'
_Journal_volume 21
_Journal_issue 22
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 6257
_Page_last 6266
_Year 2002
_Details .
loop_
_Keyword
'DNA binding domain'
'Helix-hairpin-helix motif'
'NER Protein'
'UvrC CTD'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_UvrC_CTD
_Saveframe_category molecular_system
_Mol_system_name 'UvrC C-terminal domain'
_Abbreviation_common 'UvrC CTD'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'UvrC CTD' $UvrC
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
loop_
_Biological_function
'Binds to bubble DNA with minimum 6 unpaired bases in the middle'
'Non-Sequence Specific DNA binding'
'Participates in the 5- incision of the DNA in Nuclear Excision Repair'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_UvrC
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'UV Repair protein C'
_Name_variant UvrC
_Abbreviation_common Exi-nuclease
_Molecular_mass 8562.82
_Mol_thiol_state 'not present'
_Details
;
HhH domain, Binds to bubble type DNA with minimum 6 unpaired bubble
Structurally resembles HhH domains of RuvA protein and DNA Ligase protein.
;
##############################
# Polymer residue sequence #
##############################
_Residue_count 78
_Mol_residue_sequence
;
MGSSHHHHHHSSGLVPRGSH
MNTSSLETIEGVGPKRRQML
LKYMGGLQGLRNASVEEIAK
VPGISQGLAEKIFWSLKH
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 GLY 3 SER 4 SER 5 HIS
6 HIS 7 HIS 8 HIS 9 HIS 10 HIS
11 SER 12 SER 13 GLY 14 LEU 15 VAL
16 PRO 17 ARG 18 GLY 19 SER 20 HIS
21 MET 22 ASN 23 THR 24 SER 25 SER
26 LEU 27 GLU 28 THR 29 ILE 30 GLU
31 GLY 32 VAL 33 GLY 34 PRO 35 LYS
36 ARG 37 ARG 38 GLN 39 MET 40 LEU
41 LEU 42 LYS 43 TYR 44 MET 45 GLY
46 GLY 47 LEU 48 GLN 49 GLY 50 LEU
51 ARG 52 ASN 53 ALA 54 SER 55 VAL
56 GLU 57 GLU 58 ILE 59 ALA 60 LYS
61 VAL 62 PRO 63 GLY 64 ILE 65 SER
66 GLN 67 GLY 68 LEU 69 ALA 70 GLU
71 LYS 72 ILE 73 PHE 74 TRP 75 SER
76 LEU 77 LYS 78 HIS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2014-10-26
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 1KFT "Solution Structure Of The C-Terminal Domain Of Uvrc From E- Coli" 100.00 78 100.00 100.00 2.67e-47
GB AHR43889 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. SA20095440]" 51.28 40 100.00 100.00 8.65e-19
GB AHS24459 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. EC20120677]" 51.28 40 100.00 100.00 8.65e-19
GB AHS50436 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. EC20121004]" 51.28 40 100.00 100.00 8.65e-19
GB AHS52317 "excinuclease ABC subunit C [Salmonella enterica subsp. enterica serovar Enteritidis str. EC20121541]" 51.28 40 100.00 100.00 8.65e-19
GB EFZ51080 "uvrABC system C domain protein [Shigella sonnei 53G]" 51.28 40 100.00 100.00 8.65e-19
REF WP_001345512 "MULTISPECIES: excinuclease ABC subunit C [Enterobacteriaceae]" 51.28 40 100.00 100.00 8.65e-19
REF WP_023252848 "excinuclease ABC subunit C [Salmonella enterica]" 64.10 50 98.00 100.00 4.51e-26
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Strain
_Plasmid
_Gene_mnemonic
_Details
$UvrC 'Escherichia coli' 562 Eubacteria . Escherichia coli K-12 DE3 UvrC 'Nuclear Excision Repair protein C.'
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
$UvrC 'recombinant technology' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details 'A complete protease inhibitor was added to the sample.'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$UvrC 1.0 mM [U-15N]
NaCl 300 mM .
'sodium phosphate buffer' 50 mM .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details 'A complete protease inhibitor was added to the sample.'
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$UvrC 1.0 mM '[U-15N; U-13C]'
NaCl 300 mM .
'sodium phosphate buffer' 50 mM .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 1.8
loop_
_Task
'NMR data processing'
stop_
_Details 'Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J., and Bax, A.'
save_
save_NmrView
_Saveframe_category software
_Name NMRView
_Version 4.1.3
loop_
_Task
'NMR data analysis'
stop_
_Details 'Bruce A. Johnson'
save_
save_ARIA
_Saveframe_category software
_Name ARIA
_Version 1.0
loop_
_Task
'ambiguous NOE assignment'
'structure calculation'
stop_
_Details 'S.,Jens Linge, Michael Nilges'
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 1.0
loop_
_Task
'structure calculation'
stop_
_Details
;
A.T.Brunger, P.D.Adams, G.M.Clore, W.L.DeLano,P.Gros, R.W.Grosse-Kunstleve,
J.-S.Jiang,J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson,
G.L.Warren.
;
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_3
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 750
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_HNCA_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label .
save_
save_HNCO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label .
save_
save_HN(CO)CA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_Sample_label .
save_
save_CBCANH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCANH
_Sample_label .
save_
save_1H-15N_TOCSY_HSQC_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N TOCSY HSQC'
_Sample_label .
save_
save_1H-15N_NOESY_HSQC_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N NOESY HSQC'
_Sample_label .
save_
save_1H-13C-H(C)CH_TOCSY_7
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C-H(C)CH TOCSY'
_Sample_label .
save_
save_1H-13C-(H)CCH_TOCSY_8
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-13C-(H)CCH TOCSY'
_Sample_label .
save_
save_1H-15N_NOESY_HSQC_9
_Saveframe_category NMR_applied_experiment
_Experiment_name '1H-15N NOESY HSQC'
_Sample_label .
save_
save_2D-NOESY_10
_Saveframe_category NMR_applied_experiment
_Experiment_name 2D-NOESY
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_Ex-cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 0.3 0.05 M
pH 6.8 0.2 na
temperature 300 1.0 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
H2O H 1 protons ppm 4.75 internal direct . internal parallel 1.000000000
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_Shift_1
_Saveframe_category assigned_chemical_shifts
_Details
;
The unassigned signals may correspond to the
residues from His-tag region.
;
loop_
_Sample_label
$sample_1
$sample_2
stop_
_Sample_conditions_label $Ex-cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'UvrC CTD'
_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 . 12 SER N N 110.537 0.5 1
2 . 12 SER CA C 58.600 0.5 1
3 . 12 SER CB C 63.800 0.5 1
4 . 13 GLY N N 110.539 0.5 1
5 . 13 GLY H H 8.368 0.04 1
6 . 13 GLY CA C 45.352 0.5 1
7 . 13 GLY HA3 H 3.936 0.04 2
8 . 14 LEU N N 121.527 0.5 1
9 . 14 LEU H H 8.018 0.04 1
10 . 14 LEU CA C 55.133 0.5 1
11 . 14 LEU HA H 4.327 0.04 1
12 . 14 LEU CB C 42.324 0.5 1
13 . 14 LEU CG C 24.614 0.5 1
14 . 14 LEU HG H 1.527 0.04 1
15 . 14 LEU CD1 C 23.372 0.5 1
16 . 14 LEU HD1 H 0.830 0.04 2
17 . 14 LEU HD2 H 0.775 0.04 2
18 . 14 LEU C C 173.844 0.5 1
19 . 15 VAL N N 122.506 0.5 1
20 . 15 VAL H H 8.045 0.04 1
21 . 15 VAL CA C 59.681 0.5 1
22 . 15 VAL HA H 4.344 0.04 1
23 . 15 VAL CB C 32.645 0.5 1
24 . 15 VAL HB H 2.028 0.04 1
25 . 15 VAL CG2 C 20.300 0.5 1
26 . 15 VAL HG2 H 0.889 0.04 2
27 . 15 VAL C C 177.077 0.5 1
28 . 16 PRO CA C 63.084 0.5 1
29 . 16 PRO CB C 31.900 0.5 1
30 . 16 PRO HB3 H 2.227 0.04 2
31 . 16 PRO HB2 H 1.784 0.04 2
32 . 16 PRO CG C 27.300 0.5 1
33 . 16 PRO CD C 50.800 0.5 1
34 . 16 PRO HD3 H 3.820 0.04 2
35 . 16 PRO HD2 H 3.620 0.04 2
36 . 17 ARG N N 122.016 0.5 1
37 . 17 ARG H H 8.440 0.04 1
38 . 17 ARG CA C 56.335 0.5 1
39 . 17 ARG HA H 4.383 0.04 1
40 . 17 ARG CB C 30.890 0.5 1
41 . 17 ARG HB3 H 1.795 0.04 2
42 . 17 ARG HB2 H 1.700 0.04 2
43 . 17 ARG CG C 26.544 0.5 1
44 . 17 ARG CD C 43.451 0.5 1
45 . 17 ARG HD3 H 3.207 0.04 2
46 . 17 ARG HD2 H 3.166 0.04 2
47 . 17 ARG C C 176.870 0.5 1
48 . 18 GLY N N 110.207 0.5 1
49 . 18 GLY H H 8.453 0.04 1
50 . 18 GLY CA C 45.500 0.5 1
51 . 18 GLY HA3 H 4.136 0.04 2
52 . 18 GLY HA2 H 3.615 0.04 2
53 . 18 GLY C C 174.983 0.5 1
54 . 19 SER N N 115.658 0.5 1
55 . 19 SER H H 8.189 0.04 1
56 . 19 SER CA C 58.300 0.5 1
57 . 19 SER HA H 4.400 0.04 1
58 . 19 SER CB C 63.900 0.5 1
59 . 19 SER HB3 H 3.777 0.04 1
60 . 19 SER HB2 H 3.777 0.04 1
61 . 21 MET CA C 55.400 0.5 1
62 . 21 MET CB C 32.800 0.5 1
63 . 22 ASN N N 120.006 0.5 1
64 . 22 ASN CA C 53.500 0.5 1
65 . 22 ASN CB C 38.900 0.5 1
66 . 22 ASN HB3 H 2.872 0.04 2
67 . 22 ASN HB2 H 2.808 0.04 2
68 . 23 THR N N 113.929 0.5 1
69 . 23 THR H H 8.230 0.04 1
70 . 23 THR CA C 62.200 0.5 1
71 . 23 THR CB C 69.400 0.5 1
72 . 23 THR HB H 4.265 0.04 1
73 . 23 THR HG2 H 1.162 0.04 1
74 . 24 SER N N 118.280 0.5 1
75 . 24 SER H H 8.391 0.04 1
76 . 24 SER CA C 59.000 0.5 1
77 . 24 SER HA H 4.274 0.04 1
78 . 24 SER CB C 63.600 0.5 1
79 . 24 SER HB3 H 4.000 0.04 2
80 . 24 SER HB2 H 4.041 0.04 2
81 . 25 SER N N 117.507 0.5 1
82 . 25 SER H H 8.306 0.04 1
83 . 25 SER CA C 59.011 0.5 1
84 . 25 SER HA H 4.400 0.04 1
85 . 25 SER CB C 63.641 0.5 1
86 . 25 SER HB3 H 3.793 0.04 1
87 . 25 SER HB2 H 3.793 0.04 1
88 . 25 SER C C 174.973 0.5 1
89 . 26 LEU N N 122.457 0.5 1
90 . 26 LEU H H 8.279 0.04 1
91 . 26 LEU CA C 56.605 0.5 1
92 . 26 LEU HA H 4.143 0.04 1
93 . 26 LEU CB C 42.216 0.5 1
94 . 26 LEU HB3 H 1.600 0.04 1
95 . 26 LEU HB2 H 1.600 0.04 1
96 . 26 LEU CG C 27.500 0.5 1
97 . 26 LEU HG H 1.625 0.04 1
98 . 26 LEU CD1 C 25.100 0.5 1
99 . 26 LEU HD1 H 0.865 0.04 2
100 . 26 LEU CD2 C 25.100 0.5 1
101 . 26 LEU HD2 H 0.805 0.04 2
102 . 26 LEU C C 175.267 0.5 1
103 . 27 GLU N N 116.497 0.5 1
104 . 27 GLU H H 8.310 0.04 1
105 . 27 GLU CA C 58.200 0.5 1
106 . 27 GLU HA H 3.865 0.04 1
107 . 27 GLU CB C 29.600 0.5 1
108 . 27 GLU HB3 H 1.981 0.04 2
109 . 27 GLU HB2 H 1.853 0.04 2
110 . 27 GLU CG C 36.900 0.5 1
111 . 27 GLU HG3 H 2.294 0.04 2
112 . 27 GLU HG2 H 2.218 0.04 2
113 . 27 GLU C C 177.537 0.5 1
114 . 28 THR N N 109.239 0.5 1
115 . 28 THR H H 7.621 0.04 1
116 . 28 THR CA C 61.838 0.5 1
117 . 28 THR HA H 4.300 0.04 1
118 . 28 THR CB C 69.134 0.5 1
119 . 28 THR HB H 4.350 0.04 1
120 . 28 THR CG2 C 21.800 0.5 1
121 . 28 THR HG2 H 1.177 0.04 1
122 . 28 THR C C 176.808 0.5 1
123 . 29 ILE N N 123.557 0.5 1
124 . 29 ILE H H 7.566 0.04 1
125 . 29 ILE CA C 61.583 0.5 1
126 . 29 ILE HA H 4.007 0.04 1
127 . 29 ILE CB C 38.182 0.5 1
128 . 29 ILE HB H 1.743 0.04 1
129 . 29 ILE CG1 C 27.300 0.5 2
130 . 29 ILE HG13 H 1.000 0.04 1
131 . 29 ILE HG12 H 1.755 0.04 1
132 . 29 ILE CD1 C 14.600 0.5 1
133 . 29 ILE HD1 H 0.845 0.04 1
134 . 29 ILE CG2 C 17.600 0.5 1
135 . 29 ILE HG2 H 0.815 0.04 1
136 . 29 ILE C C 174.498 0.5 1
137 . 30 GLU N N 130.032 0.5 1
138 . 30 GLU H H 8.686 0.04 1
139 . 30 GLU CA C 58.144 0.5 1
140 . 30 GLU HA H 4.004 0.04 1
141 . 30 GLU CB C 29.688 0.5 1
142 . 30 GLU HB3 H 1.958 0.04 1
143 . 30 GLU HB2 H 1.958 0.04 1
144 . 30 GLU CG C 36.100 0.5 1
145 . 30 GLU HG3 H 2.290 0.04 2
146 . 30 GLU HG2 H 2.225 0.04 2
147 . 30 GLU C C 175.956 0.5 1
148 . 31 GLY N N 111.124 0.5 1
149 . 31 GLY H H 8.582 0.04 1
150 . 31 GLY CA C 44.987 0.5 1
151 . 31 GLY HA3 H 4.231 0.04 2
152 . 31 GLY HA2 H 3.717 0.04 2
153 . 31 GLY C C 176.813 0.5 1
154 . 32 VAL N N 119.904 0.5 1
155 . 32 VAL H H 7.754 0.04 1
156 . 32 VAL CA C 62.451 0.5 1
157 . 32 VAL HA H 4.077 0.04 1
158 . 32 VAL CB C 30.975 0.5 1
159 . 32 VAL HB H 2.290 0.04 1
160 . 32 VAL CG2 C 22.160 0.5 1
161 . 32 VAL HG2 H 0.848 0.04 2
162 . 32 VAL CG1 C 22.400 0.5 1
163 . 32 VAL HG1 H 0.756 0.04 2
164 . 32 VAL C C 174.158 0.5 1
165 . 33 GLY N N 111.949 0.5 1
166 . 33 GLY H H 7.967 0.04 1
167 . 33 GLY CA C 44.980 0.5 1
168 . 33 GLY HA3 H 4.320 0.04 2
169 . 33 GLY HA2 H 4.187 0.04 2
170 . 33 GLY C C 175.289 0.5 1
171 . 34 PRO CA C 65.900 0.5 1
172 . 34 PRO HA H 4.411 0.04 1
173 . 34 PRO CB C 32.300 0.5 1
174 . 34 PRO HB3 H 2.375 0.04 2
175 . 34 PRO HB2 H 1.987 0.04 2
176 . 34 PRO CG C 27.400 0.5 1
177 . 34 PRO HG3 H 2.162 0.04 2
178 . 34 PRO HG2 H 2.050 0.04 2
179 . 34 PRO CD C 49.500 0.5 1
180 . 34 PRO HD3 H 3.660 0.04 2
181 . 34 PRO HD2 H 3.825 0.04 2
182 . 35 LYS N N 118.766 0.5 1
183 . 35 LYS H H 8.203 0.04 1
184 . 35 LYS CA C 59.521 0.5 1
185 . 35 LYS HA H 4.158 0.04 1
186 . 35 LYS CB C 31.817 0.5 1
187 . 35 LYS HB3 H 1.963 0.04 2
188 . 35 LYS HB2 H 1.885 0.04 2
189 . 35 LYS CG C 29.200 0.5 1
190 . 35 LYS HG3 H 1.720 0.04 1
191 . 35 LYS HG2 H 1.720 0.04 1
192 . 35 LYS CD C 25.200 0.5 1
193 . 35 LYS HD3 H 1.400 0.04 2
194 . 35 LYS HD2 H 1.510 0.04 2
195 . 35 LYS CE C 42.200 0.5 1
196 . 35 LYS HE3 H 3.000 0.04 1
197 . 35 LYS HE2 H 3.000 0.04 1
198 . 35 LYS C C 179.206 0.5 1
199 . 36 ARG N N 120.327 0.5 1
200 . 36 ARG H H 8.099 0.04 1
201 . 36 ARG CA C 59.466 0.5 1
202 . 36 ARG HA H 4.074 0.04 1
203 . 36 ARG CB C 30.269 0.5 1
204 . 36 ARG HB3 H 1.913 0.04 2
205 . 36 ARG HB2 H 1.585 0.04 2
206 . 36 ARG CG C 28.800 0.5 1
207 . 36 ARG HG3 H 1.583 0.04 2
208 . 36 ARG HG2 H 1.878 0.04 2
209 . 36 ARG CD C 43.636 0.5 1
210 . 36 ARG HD3 H 3.420 0.04 2
211 . 36 ARG HD2 H 3.050 0.04 2
212 . 36 ARG C C 179.592 0.5 1
213 . 37 ARG N N 119.188 0.5 1
214 . 37 ARG H H 8.544 0.04 1
215 . 37 ARG CA C 60.594 0.5 1
216 . 37 ARG HA H 3.671 0.04 1
217 . 37 ARG CB C 29.903 0.5 1
218 . 37 ARG HB3 H 1.889 0.04 2
219 . 37 ARG HB2 H 1.831 0.04 2
220 . 37 ARG CG C 27.700 0.5 1
221 . 37 ARG HG3 H 1.580 0.04 2
222 . 37 ARG HG2 H 1.450 0.04 2
223 . 37 ARG CD C 43.800 0.5 1
224 . 37 ARG HD3 H 3.180 0.04 2
225 . 37 ARG HD2 H 3.132 0.04 2
226 . 37 ARG C C 178.213 0.5 1
227 . 38 GLN N N 116.587 0.5 1
228 . 38 GLN H H 7.780 0.04 1
229 . 38 GLN CA C 59.000 0.5 1
230 . 38 GLN HA H 4.014 0.04 1
231 . 38 GLN CB C 28.412 0.5 1
232 . 38 GLN HB3 H 2.211 0.04 1
233 . 38 GLN HB2 H 2.211 0.04 1
234 . 38 GLN CG C 33.900 0.5 1
235 . 38 GLN HG3 H 2.570 0.04 2
236 . 38 GLN HG2 H 2.435 0.04 2
237 . 38 GLN NE2 N 111.670 0.5 1
238 . 38 GLN HE21 H 7.409 0.04 2
239 . 38 GLN HE22 H 6.847 0.04 2
240 . 38 GLN C C 177.215 0.5 1
241 . 39 MET N N 119.254 0.5 1
242 . 39 MET H H 7.902 0.04 1
243 . 39 MET CA C 59.032 0.5 1
244 . 39 MET HA H 4.284 0.04 1
245 . 39 MET CB C 32.304 0.5 1
246 . 39 MET HB3 H 2.747 0.04 2
247 . 39 MET HB2 H 2.675 0.04 2
248 . 39 MET CG C 32.304 0.5 1
249 . 39 MET HG3 H 2.225 0.04 2
250 . 39 MET HG2 H 2.090 0.04 2
251 . 39 MET C C 178.950 0.5 1
252 . 40 LEU N N 120.411 0.5 1
253 . 40 LEU H H 8.487 0.04 1
254 . 40 LEU CA C 58.605 0.5 1
255 . 40 LEU HA H 3.960 0.04 1
256 . 40 LEU CB C 42.756 0.5 1
257 . 40 LEU HB3 H 1.908 0.04 2
258 . 40 LEU HB2 H 1.593 0.04 2
259 . 40 LEU CG C 27.300 0.5 1
260 . 40 LEU HG H 1.672 0.04 1
261 . 40 LEU CD1 C 25.810 0.5 1
262 . 40 LEU HD1 H 0.860 0.04 2
263 . 40 LEU CD2 C 25.200 0.5 1
264 . 40 LEU HD2 H 0.870 0.04 2
265 . 40 LEU C C 178.302 0.5 1
266 . 41 LEU N N 116.672 0.5 1
267 . 41 LEU H H 7.994 0.04 1
268 . 41 LEU CA C 58.270 0.5 1
269 . 41 LEU HA H 3.774 0.04 1
270 . 41 LEU CB C 41.242 0.5 1
271 . 41 LEU HB3 H 1.885 0.04 2
272 . 41 LEU HB2 H 1.460 0.04 2
273 . 41 LEU CG C 27.100 0.5 1
274 . 41 LEU HG H 1.765 0.04 1
275 . 41 LEU CD1 C 25.300 0.5 1
276 . 41 LEU HD1 H 0.859 0.04 2
277 . 41 LEU CD2 C 22.500 0.5 1
278 . 41 LEU HD2 H 0.692 0.04 2
279 . 41 LEU C C 178.198 0.5 1
280 . 42 LYS N N 120.081 0.5 1
281 . 42 LYS H H 8.119 0.04 1
282 . 42 LYS CA C 59.373 0.5 1
283 . 42 LYS HA H 4.093 0.04 1
284 . 42 LYS CB C 32.600 0.5 1
285 . 42 LYS HB3 H 2.000 0.04 1
286 . 42 LYS HB2 H 2.000 0.04 1
287 . 42 LYS CG C 29.230 0.5 1
288 . 42 LYS HG3 H 1.647 0.04 1
289 . 42 LYS HG2 H 1.647 0.04 1
290 . 42 LYS CD C 24.700 0.5 1
291 . 42 LYS HD3 H 1.450 0.04 2
292 . 42 LYS HD2 H 1.274 0.04 2
293 . 42 LYS CE C 42.300 0.5 1
294 . 42 LYS HE3 H 3.000 0.04 1
295 . 42 LYS HE2 H 3.000 0.04 1
296 . 42 LYS C C 175.651 0.5 1
297 . 43 TYR N N 118.667 0.5 1
298 . 43 TYR H H 8.612 0.04 1
299 . 43 TYR CA C 61.726 0.5 1
300 . 43 TYR HA H 4.118 0.04 1
301 . 43 TYR CB C 39.203 0.5 1
302 . 43 TYR HB3 H 3.181 0.04 2
303 . 43 TYR HB2 H 3.031 0.04 2
304 . 43 TYR HD1 H 7.309 0.04 1
305 . 43 TYR HE1 H 6.876 0.04 1
306 . 43 TYR HE2 H 6.876 0.04 1
307 . 43 TYR HD2 H 7.309 0.04 1
308 . 43 TYR C C 179.482 0.5 1
309 . 44 MET N N 112.842 0.5 1
310 . 44 MET H H 7.931 0.04 1
311 . 44 MET CA C 54.370 0.5 1
312 . 44 MET HA H 4.665 0.04 1
313 . 44 MET CB C 32.583 0.5 1
314 . 44 MET HB3 H 1.970 0.04 2
315 . 44 MET HB2 H 2.110 0.04 2
316 . 44 MET CG C 33.800 0.5 1
317 . 44 MET HG3 H 2.615 0.04 2
318 . 44 MET HG2 H 2.656 0.04 2
319 . 44 MET HE H 1.981 0.04 1
320 . 44 MET C C 178.101 0.5 1
321 . 45 GLY N N 107.234 0.5 1
322 . 45 GLY H H 7.536 0.04 1
323 . 45 GLY CA C 46.381 0.5 1
324 . 45 GLY HA3 H 4.100 0.04 2
325 . 45 GLY HA2 H 3.900 0.04 2
326 . 45 GLY C C 176.266 0.5 1
327 . 46 GLY N N 108.188 0.5 1
328 . 46 GLY H H 8.526 0.04 1
329 . 46 GLY CA C 43.889 0.5 1
330 . 46 GLY HA3 H 4.533 0.04 2
331 . 46 GLY HA2 H 3.688 0.04 2
332 . 46 GLY C C 175.537 0.5 1
333 . 47 LEU N N 121.189 0.5 1
334 . 47 LEU H H 8.674 0.04 1
335 . 47 LEU CA C 58.055 0.5 1
336 . 47 LEU HA H 3.875 0.04 1
337 . 47 LEU CB C 41.770 0.5 1
338 . 47 LEU HB3 H 1.683 0.04 2
339 . 47 LEU HB2 H 1.543 0.04 2
340 . 47 LEU CG C 27.200 0.5 1
341 . 47 LEU HG H 1.540 0.04 1
342 . 47 LEU CD1 C 25.100 0.5 1
343 . 47 LEU HD1 H 0.850 0.04 2
344 . 47 LEU CD2 C 23.600 0.5 1
345 . 47 LEU HD2 H 0.920 0.04 2
346 . 47 LEU C C 173.199 0.5 1
347 . 48 GLN N N 117.348 0.5 1
348 . 48 GLN H H 8.714 0.04 1
349 . 48 GLN CA C 58.909 0.5 1
350 . 48 GLN HA H 3.906 0.04 1
351 . 48 GLN CB C 27.818 0.5 1
352 . 48 GLN HB3 H 2.005 0.04 2
353 . 48 GLN HB2 H 2.075 0.04 2
354 . 48 GLN CG C 33.800 0.5 1
355 . 48 GLN HG3 H 2.391 0.04 1
356 . 48 GLN HG2 H 2.391 0.04 1
357 . 48 GLN NE2 N 113.123 0.5 1
358 . 48 GLN HE21 H 7.475 0.04 2
359 . 48 GLN HE22 H 6.932 0.04 2
360 . 48 GLN C C 178.603 0.5 1
361 . 49 GLY N N 106.202 0.5 1
362 . 49 GLY H H 7.379 0.04 1
363 . 49 GLY CA C 46.510 0.5 1
364 . 49 GLY HA3 H 4.154 0.04 2
365 . 49 GLY HA2 H 3.837 0.04 2
366 . 49 GLY C C 178.375 0.5 1
367 . 50 LEU N N 123.135 0.5 1
368 . 50 LEU H H 7.951 0.04 1
369 . 50 LEU CA C 57.704 0.5 1
370 . 50 LEU HA H 4.100 0.04 1
371 . 50 LEU CB C 41.756 0.5 1
372 . 50 LEU HB3 H 1.960 0.04 2
373 . 50 LEU HB2 H 1.285 0.04 2
374 . 50 LEU CG C 27.100 0.5 1
375 . 50 LEU HG H 1.554 0.04 1
376 . 50 LEU CD1 C 27.100 0.5 1
377 . 50 LEU HD1 H 0.790 0.04 2
378 . 50 LEU CD2 C 24.100 0.5 1
379 . 50 LEU HD2 H 0.880 0.04 2
380 . 50 LEU C C 177.365 0.5 1
381 . 51 ARG N N 116.649 0.5 1
382 . 51 ARG H H 8.338 0.04 1
383 . 51 ARG CA C 59.316 0.5 1
384 . 51 ARG HA H 3.840 0.04 1
385 . 51 ARG CB C 30.300 0.5 1
386 . 51 ARG HB3 H 1.830 0.04 1
387 . 51 ARG HB2 H 1.830 0.04 1
388 . 51 ARG CG C 28.800 0.5 1
389 . 51 ARG HG3 H 1.830 0.04 2
390 . 51 ARG HG2 H 1.575 0.04 2
391 . 51 ARG CD C 43.800 0.5 1
392 . 51 ARG HD3 H 3.114 0.04 1
393 . 51 ARG HD2 H 3.114 0.04 1
394 . 51 ARG C C 178.322 0.5 1
395 . 52 ASN N N 114.780 0.5 1
396 . 52 ASN H H 7.331 0.04 1
397 . 52 ASN CA C 52.776 0.5 1
398 . 52 ASN HA H 4.815 0.04 1
399 . 52 ASN CB C 39.801 0.5 1
400 . 52 ASN HB3 H 3.002 0.04 2
401 . 52 ASN HB2 H 2.700 0.04 2
402 . 52 ASN ND2 N 112.640 0.5 1
403 . 52 ASN HD21 H 7.598 0.04 2
404 . 52 ASN HD22 H 6.883 0.04 2
405 . 52 ASN C C 176.524 0.5 1
406 . 53 ALA N N 124.021 0.5 1
407 . 53 ALA H H 7.290 0.04 1
408 . 53 ALA CA C 52.316 0.5 1
409 . 53 ALA HA H 4.546 0.04 1
410 . 53 ALA CB C 20.665 0.5 1
411 . 53 ALA HB H 1.596 0.04 1
412 . 53 ALA C C 174.578 0.5 1
413 . 54 SER N N 116.936 0.5 1
414 . 54 SER H H 8.568 0.04 1
415 . 54 SER CA C 56.555 0.5 1
416 . 54 SER HA H 4.620 0.04 1
417 . 54 SER CB C 65.817 0.5 1
418 . 54 SER HB3 H 4.240 0.04 2
419 . 54 SER HB2 H 3.980 0.04 2
420 . 54 SER C C 177.335 0.5 1
421 . 55 VAL N N 120.830 0.5 1
422 . 55 VAL H H 8.163 0.04 1
423 . 55 VAL CA C 67.294 0.5 1
424 . 55 VAL HA H 3.244 0.04 1
425 . 55 VAL CB C 31.345 0.5 1
426 . 55 VAL HB H 1.448 0.04 1
427 . 55 VAL CG2 C 21.500 0.5 1
428 . 55 VAL HG2 H 0.715 0.04 2
429 . 55 VAL CG1 C 22.800 0.5 1
430 . 55 VAL HG1 H 0.419 0.04 2
431 . 55 VAL C C 175.091 0.5 1
432 . 56 GLU N N 116.610 0.5 1
433 . 56 GLU H H 8.241 0.04 1
434 . 56 GLU CA C 59.605 0.5 1
435 . 56 GLU HA H 3.865 0.04 1
436 . 56 GLU CB C 29.090 0.5 1
437 . 56 GLU HB3 H 1.820 0.04 2
438 . 56 GLU HB2 H 1.950 0.04 2
439 . 56 GLU CG C 37.100 0.5 1
440 . 56 GLU HG3 H 2.295 0.04 2
441 . 56 GLU HG2 H 2.250 0.04 2
442 . 56 GLU C C 176.965 0.5 1
443 . 57 GLU N N 117.791 0.5 1
444 . 57 GLU H H 7.493 0.04 1
445 . 57 GLU CA C 59.062 0.5 1
446 . 57 GLU HA H 3.903 0.04 1
447 . 57 GLU CB C 30.092 0.5 1
448 . 57 GLU HB3 H 2.306 0.04 2
449 . 57 GLU HB2 H 2.006 0.04 2
450 . 57 GLU CG C 36.900 0.5 1
451 . 57 GLU HG3 H 2.290 0.04 2
452 . 57 GLU HG2 H 2.210 0.04 2
453 . 57 GLU C C 178.867 0.5 1
454 . 58 ILE N N 121.646 0.5 1
455 . 58 ILE H H 8.018 0.04 1
456 . 58 ILE CA C 65.555 0.5 1
457 . 58 ILE HA H 3.485 0.04 1
458 . 58 ILE CB C 38.323 0.5 1
459 . 58 ILE HB H 1.825 0.04 1
460 . 58 ILE CG1 C 29.900 0.5 2
461 . 58 ILE HG13 H 2.040 0.04 1
462 . 58 ILE HG12 H 0.634 0.04 1
463 . 58 ILE CD1 C 13.600 0.5 1
464 . 58 ILE HD1 H 0.958 0.04 1
465 . 58 ILE CG2 C 18.700 0.5 1
466 . 58 ILE HG2 H 0.880 0.04 1
467 . 58 ILE C C 179.599 0.5 1
468 . 59 ALA N N 116.806 0.5 1
469 . 59 ALA H H 7.994 0.04 1
470 . 59 ALA CA C 52.916 0.5 1
471 . 59 ALA HA H 3.886 0.04 1
472 . 59 ALA CB C 17.894 0.5 1
473 . 59 ALA HB H 1.270 0.04 1
474 . 59 ALA C C 176.571 0.5 1
475 . 60 LYS N N 115.965 0.5 1
476 . 60 LYS H H 7.037 0.04 1
477 . 60 LYS CA C 56.396 0.5 1
478 . 60 LYS HA H 4.164 0.04 1
479 . 60 LYS CB C 32.791 0.5 1
480 . 60 LYS HB3 H 1.949 0.04 2
481 . 60 LYS HB2 H 1.800 0.04 2
482 . 60 LYS CG C 29.300 0.5 1
483 . 60 LYS HG3 H 1.710 0.04 1
484 . 60 LYS HG2 H 1.710 0.04 1
485 . 60 LYS CD C 25.300 0.5 1
486 . 60 LYS HD3 H 1.515 0.04 2
487 . 60 LYS HD2 H 1.420 0.04 2
488 . 60 LYS CE C 42.300 0.5 1
489 . 60 LYS HE3 H 2.931 0.04 1
490 . 60 LYS HE2 H 2.931 0.04 1
491 . 60 LYS C C 177.126 0.5 1
492 . 61 VAL N N 124.962 0.5 1
493 . 61 VAL H H 7.544 0.04 1
494 . 61 VAL CA C 61.193 0.5 1
495 . 61 VAL HA H 3.417 0.04 1
496 . 61 VAL CB C 31.441 0.5 1
497 . 61 VAL HB H 2.053 0.04 1
498 . 61 VAL CG2 C 23.330 0.5 1
499 . 61 VAL HG2 H 0.826 0.04 2
500 . 61 VAL CG1 C 19.910 0.5 1
501 . 61 VAL HG1 H 0.600 0.04 2
502 . 61 VAL C C 177.450 0.5 1
503 . 62 PRO CA C 64.050 0.5 1
504 . 62 PRO HA H 4.400 0.04 1
505 . 62 PRO CB C 31.700 0.5 1
506 . 62 PRO HB3 H 2.220 0.04 2
507 . 62 PRO HB2 H 1.757 0.04 2
508 . 62 PRO CG C 27.800 0.5 1
509 . 62 PRO HG3 H 2.011 0.04 2
510 . 62 PRO HG2 H 1.887 0.04 2
511 . 62 PRO CD C 51.100 0.5 1
512 . 62 PRO HD3 H 3.644 0.04 2
513 . 62 PRO HD2 H 2.936 0.04 2
514 . 63 GLY N N 109.923 0.5 1
515 . 63 GLY H H 8.399 0.04 1
516 . 63 GLY CA C 45.224 0.5 1
517 . 63 GLY HA3 H 4.138 0.04 2
518 . 63 GLY HA2 H 3.648 0.04 2
519 . 63 GLY C C 176.742 0.5 1
520 . 64 ILE N N 121.746 0.5 1
521 . 64 ILE H H 7.658 0.04 1
522 . 64 ILE CA C 58.876 0.5 1
523 . 64 ILE HA H 4.168 0.04 1
524 . 64 ILE CB C 35.231 0.5 1
525 . 64 ILE HB H 2.379 0.04 1
526 . 64 ILE CG1 C 26.600 0.5 2
527 . 64 ILE HG13 H 1.215 0.04 1
528 . 64 ILE HG12 H 1.124 0.04 1
529 . 64 ILE CD1 C 9.930 0.5 1
530 . 64 ILE HD1 H 0.570 0.04 1
531 . 64 ILE CG2 C 17.300 0.5 1
532 . 64 ILE HG2 H 0.772 0.04 1
533 . 64 ILE C C 174.358 0.5 1
534 . 65 SER N N 121.391 0.5 1
535 . 65 SER H H 7.614 0.04 1
536 . 65 SER CA C 57.046 0.5 1
537 . 65 SER HA H 4.510 0.04 1
538 . 65 SER CB C 65.538 0.5 1
539 . 65 SER HB3 H 4.325 0.04 2
540 . 65 SER HB2 H 4.060 0.04 2
541 . 65 SER C C 173.958 0.5 1
542 . 66 GLN N N 121.071 0.5 1
543 . 66 GLN H H 8.924 0.04 1
544 . 66 GLN CA C 59.638 0.5 1
545 . 66 GLN HA H 3.803 0.04 1
546 . 66 GLN CB C 27.778 0.5 1
547 . 66 GLN HB3 H 2.210 0.04 1
548 . 66 GLN HB2 H 2.210 0.04 1
549 . 66 GLN CG C 32.200 0.5 1
550 . 66 GLN HG3 H 2.325 0.04 1
551 . 66 GLN HG2 H 2.325 0.04 1
552 . 66 GLN NE2 N 111.670 0.5 1
553 . 66 GLN HE21 H 7.754 0.04 2
554 . 66 GLN HE22 H 6.439 0.04 2
555 . 66 GLN C C 174.278 0.5 1
556 . 67 GLY N N 104.866 0.5 1
557 . 67 GLY H H 8.586 0.04 1
558 . 67 GLY CA C 46.765 0.5 1
559 . 67 GLY HA3 H 3.826 0.04 1
560 . 67 GLY HA2 H 3.826 0.04 1
561 . 67 GLY C C 178.092 0.5 1
562 . 68 LEU N N 124.593 0.5 1
563 . 68 LEU H H 7.810 0.04 1
564 . 68 LEU CA C 57.135 0.5 1
565 . 68 LEU HA H 4.249 0.04 1
566 . 68 LEU CB C 41.483 0.5 1
567 . 68 LEU HB3 H 1.806 0.04 2
568 . 68 LEU HB2 H 1.594 0.04 2
569 . 68 LEU CG C 26.500 0.5 1
570 . 68 LEU HG H 0.971 0.04 1
571 . 68 LEU CD1 C 23.100 0.5 1
572 . 68 LEU HD1 H 0.979 0.04 1
573 . 68 LEU CD2 C 23.100 0.5 1
574 . 68 LEU HD2 H 0.979 0.04 1
575 . 68 LEU C C 177.111 0.5 1
576 . 69 ALA N N 122.621 0.5 1
577 . 69 ALA H H 8.724 0.04 1
578 . 69 ALA CA C 55.696 0.5 1
579 . 69 ALA HA H 3.800 0.04 1
580 . 69 ALA CB C 18.667 0.5 1
581 . 69 ALA HB H 1.450 0.04 1
582 . 69 ALA C C 178.135 0.5 1
583 . 70 GLU N N 116.169 0.5 1
584 . 70 GLU H H 7.949 0.04 1
585 . 70 GLU CA C 59.919 0.5 1
586 . 70 GLU HA H 3.946 0.04 1
587 . 70 GLU CB C 29.729 0.5 1
588 . 70 GLU HB3 H 2.204 0.04 2
589 . 70 GLU HB2 H 2.180 0.04 2
590 . 70 GLU CG C 37.000 0.5 1
591 . 70 GLU HG3 H 2.586 0.04 2
592 . 70 GLU HG2 H 2.340 0.04 2
593 . 70 GLU C C 179.305 0.5 1
594 . 71 LYS N N 119.355 0.5 1
595 . 71 LYS H H 7.567 0.04 1
596 . 71 LYS CA C 59.648 0.5 1
597 . 71 LYS HA H 4.265 0.04 1
598 . 71 LYS CB C 32.672 0.5 1
599 . 71 LYS HB3 H 2.070 0.04 2
600 . 71 LYS HB2 H 2.040 0.04 2
601 . 71 LYS CG C 29.300 0.5 1
602 . 71 LYS HG3 H 1.688 0.04 2
603 . 71 LYS HG2 H 1.710 0.04 2
604 . 71 LYS CD C 24.800 0.5 1
605 . 71 LYS HD3 H 1.470 0.04 2
606 . 71 LYS HD2 H 1.656 0.04 2
607 . 71 LYS CE C 42.300 0.5 1
608 . 71 LYS HE3 H 2.983 0.04 1
609 . 71 LYS HE2 H 2.983 0.04 1
610 . 71 LYS C C 178.138 0.5 1
611 . 72 ILE N N 121.661 0.5 1
612 . 72 ILE H H 8.940 0.04 1
613 . 72 ILE CA C 65.640 0.5 1
614 . 72 ILE HA H 3.515 0.04 1
615 . 72 ILE CB C 38.370 0.5 1
616 . 72 ILE HB H 1.920 0.04 1
617 . 72 ILE CG1 C 29.500 0.5 2
618 . 72 ILE HG13 H 1.900 0.04 1
619 . 72 ILE HG12 H 0.800 0.04 1
620 . 72 ILE CD1 C 15.000 0.5 1
621 . 72 ILE HD1 H 0.720 0.04 1
622 . 72 ILE CG2 C 17.300 0.5 1
623 . 72 ILE HG2 H 0.830 0.04 1
624 . 72 ILE C C 180.448 0.5 1
625 . 73 PHE N N 119.403 0.5 1
626 . 73 PHE H H 8.515 0.04 1
627 . 73 PHE CA C 61.864 0.5 1
628 . 73 PHE HA H 3.864 0.04 1
629 . 73 PHE CB C 40.630 0.5 1
630 . 73 PHE HB3 H 3.062 0.04 2
631 . 73 PHE HB2 H 2.938 0.04 2
632 . 73 PHE HD1 H 6.493 0.04 1
633 . 73 PHE HE1 H 6.858 0.04 1
634 . 73 PHE HZ H 7.063 0.04 1
635 . 73 PHE HE2 H 6.858 0.04 1
636 . 73 PHE HD2 H 6.493 0.04 1
637 . 73 PHE C C 176.784 0.5 1
638 . 74 TRP N N 116.497 0.5 1
639 . 74 TRP H H 8.310 0.04 1
640 . 74 TRP CA C 60.100 0.5 1
641 . 74 TRP HA H 4.352 0.04 1
642 . 74 TRP CB C 29.300 0.5 1
643 . 74 TRP HB3 H 3.477 0.04 2
644 . 74 TRP HB2 H 3.357 0.04 2
645 . 74 TRP HD1 H 7.517 0.04 1
646 . 74 TRP NE1 N 129.057 0.5 1
647 . 74 TRP HE1 H 10.383 0.04 4
648 . 74 TRP HZ2 H 7.473 0.04 4
649 . 74 TRP HH2 H 7.285 0.04 1
650 . 74 TRP HZ3 H 7.181 0.04 4
651 . 74 TRP HE3 H 7.672 0.04 4
652 . 74 TRP C C 179.287 0.5 1
653 . 75 SER N N 116.497 0.5 1
654 . 75 SER H H 8.310 0.04 1
655 . 75 SER CA C 61.861 0.5 1
656 . 75 SER HA H 4.368 0.04 1
657 . 75 SER CB C 62.925 0.5 1
658 . 75 SER HB3 H 3.486 0.04 2
659 . 75 SER HB2 H 3.362 0.04 2
660 . 75 SER C C 177.553 0.5 1
661 . 76 LEU N N 119.018 0.5 1
662 . 76 LEU H H 7.382 0.04 1
663 . 76 LEU CA C 55.452 0.5 1
664 . 76 LEU HA H 4.198 0.04 1
665 . 76 LEU CB C 42.070 0.5 1
666 . 76 LEU HB3 H 1.712 0.04 2
667 . 76 LEU HB2 H 1.380 0.04 2
668 . 76 LEU CG C 26.400 0.5 1
669 . 76 LEU HG H 1.830 0.04 1
670 . 76 LEU CD1 C 22.700 0.5 1
671 . 76 LEU HD1 H 0.699 0.04 2
672 . 76 LEU CD2 C 26.600 0.5 1
673 . 76 LEU HD2 H 0.655 0.04 2
674 . 76 LEU C C 175.651 0.5 1
675 . 77 LYS N N 118.240 0.5 1
676 . 77 LYS H H 7.175 0.04 1
677 . 77 LYS CA C 55.748 0.5 1
678 . 77 LYS HA H 4.144 0.04 1
679 . 77 LYS CB C 32.718 0.5 1
680 . 77 LYS HB3 H 1.740 0.04 2
681 . 77 LYS HB2 H 1.596 0.04 2
682 . 77 LYS CG C 28.400 0.5 1
683 . 77 LYS HG3 H 1.319 0.04 1
684 . 77 LYS HG2 H 1.319 0.04 1
685 . 77 LYS CD C 24.200 0.5 1
686 . 77 LYS HD3 H 1.150 0.04 1
687 . 77 LYS HD2 H 1.150 0.04 1
688 . 77 LYS CE C 42.200 0.5 1
689 . 77 LYS HE3 H 2.610 0.04 2
690 . 77 LYS HE2 H 2.290 0.04 2
691 . 77 LYS C C 177.227 0.5 1
692 . 78 HIS N N 124.116 0.5 1
693 . 78 HIS H H 7.601 0.04 1
694 . 78 HIS CA C 57.214 0.5 1
695 . 78 HIS HA H 4.381 0.04 1
696 . 78 HIS CB C 30.397 0.5 1
697 . 78 HIS HB3 H 3.173 0.04 2
698 . 78 HIS HB2 H 2.796 0.04 2
699 . 78 HIS HD2 H 6.442 0.04 4
700 . 78 HIS HE1 H 7.762 0.04 4
701 . 78 HIS C C 175.548 0.5 1
stop_
save_