data_17347
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution NMR structure of PAP248-286 in 30% TFE
;
_BMRB_accession_number 17347
_BMRB_flat_file_name bmr17347.str
_Entry_type new
_Submission_date 2010-12-03
_Accession_date 2010-12-03
_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 NANGA 'RAVI PRAKASH REDDY' . .
2 BRENDER JEFFREY R. .
3 POPOVYCH NATALIYA . .
4 RAMAMOORTHY AYYALUSAMY . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 229
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2011-03-24 update BMRB 'update entry citation'
2011-01-27 original author 'original release'
stop_
loop_
_Related_BMRB_accession_number
_Relationship
17346 'PAP248-286 in 50% TFE'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 21262195
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Brender Jeffrey R. .
2 Nanga 'Ravi Prakash Reddy' . .
3 Popovych Nataliya . .
4 Soong Ronald . .
5 Macdonald Peter M. .
6 Ramamoorthy Ayyalusamy . .
stop_
_Journal_abbreviation 'Biochim. Biophys. Acta'
_Journal_name_full 'Biochimica et biophysica acta'
_Journal_volume 1808
_Journal_issue 4
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1161
_Page_last 1169
_Year 2011
_Details .
loop_
_Keyword
NMR
AMYLOID
SEVI
PAP248-286
stop_
save_
##################################
# Molecular system description #
##################################
save_assembly
_Saveframe_category molecular_system
_Mol_system_name PAP248-286
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
PAP248-286 $entity
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state ?
_System_paramagnetic no
_System_thiol_state .
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_entity
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common entity
_Molecular_mass 4561.504
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 39
_Mol_residue_sequence
;
GIHKQKEKSRLQGGVLVNEI
LNHMKRATQIPSYKKLIMY
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 248 GLY 2 249 ILE 3 250 HIS 4 251 LYS 5 252 GLN
6 253 LYS 7 254 GLU 8 255 LYS 9 256 SER 10 257 ARG
11 258 LEU 12 259 GLN 13 260 GLY 14 261 GLY 15 262 VAL
16 263 LEU 17 264 VAL 18 265 ASN 19 266 GLU 20 267 ILE
21 268 LEU 22 269 ASN 23 270 HIS 24 271 MET 25 272 LYS
26 273 ARG 27 274 ALA 28 275 THR 29 276 GLN 30 277 ILE
31 278 PRO 32 279 SER 33 280 TYR 34 281 LYS 35 282 LYS
36 283 LEU 37 284 ILE 38 285 MET 39 286 TYR
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-01-30
loop_
_Database_name
_Database_accession_code
_Database_entry_mol_name
_Sequence_query_to_submitted_percentage
_Sequence_subject_length
_Sequence_identity
_Sequence_positive
_Sequence_homology_expectation_value
BMRB 17193 PAP248-286 100.00 39 100.00 100.00 2.43e-18
BMRB 17346 entity 100.00 39 100.00 100.00 2.43e-18
BMRB 17924 SEVI 100.00 39 100.00 100.00 2.43e-18
BMRB 17925 SEVI 100.00 39 100.00 100.00 2.43e-18
BMRB 18287 PAP248-286 100.00 39 100.00 100.00 2.43e-18
PDB 1CVI "Crystal Structure Of Human Prostatic Acid Phosphatase" 100.00 342 100.00 100.00 2.03e-17
PDB 1ND5 "Crystal Structures Of Human Prostatic Acid Phosphatase In Complex With A Phosphate Ion And Alpha-Benzylaminobenzylphosphonic Ac" 100.00 354 100.00 100.00 1.95e-17
PDB 1ND6 "Crystal Structures Of Human Prostatic Acid Phosphatase In Complex With A Phosphate Ion And Alpha-Benzylaminobenzylphosphonic Ac" 100.00 354 100.00 100.00 1.95e-17
PDB 2HPA "Structural Origins Of L(+)-Tartrate Inhibition Of Human Prostatic Acid Phosphatase" 100.00 342 100.00 100.00 2.03e-17
PDB 2L3H "Nmr Structure In A Membrane Environment Reveals Putative Amyloidogenic Regions Of The Sevi Precursor Peptide Pap248-286" 97.44 39 100.00 100.00 2.42e-17
PDB 2L77 "Solution Nmr Structure Of Pap248-286 In 50% Tfe" 97.44 39 100.00 100.00 2.42e-17
PDB 2L79 "Solution Nmr Structure Of Pap248-286 In 30% Tfe" 97.44 39 100.00 100.00 2.42e-17
DBJ BAD89417 "Acid phosphatase prostate nirs variant 1 [Homo sapiens]" 100.00 353 100.00 100.00 3.85e-18
DBJ BAG62248 "unnamed protein product [Homo sapiens]" 100.00 353 100.00 100.00 3.85e-18
EMBL CAA36422 "unnamed protein product [Homo sapiens]" 100.00 386 100.00 100.00 3.05e-18
EMBL CAA37673 "unnamed protein product [Homo sapiens]" 100.00 386 100.00 100.00 5.55e-18
GB AAA60021 "prostatic acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17
GB AAA60022 "acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 6.90e-18
GB AAA69694 "acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17
GB AAB60640 "prostatic acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17
GB AAH07460 "ACPP protein [Homo sapiens]" 100.00 418 100.00 100.00 1.43e-17
REF NP_001090 "prostatic acid phosphatase isoform PAP precursor [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17
REF NP_001127666 "prostatic acid phosphatase isoform TM-PAP precursor [Homo sapiens]" 100.00 418 100.00 100.00 1.48e-17
REF NP_001278966 "prostatic acid phosphatase isoform 3 [Homo sapiens]" 100.00 353 100.00 100.00 3.85e-18
REF XP_001115549 "PREDICTED: prostatic acid phosphatase [Macaca mulatta]" 100.00 418 97.44 100.00 1.49e-17
REF XP_001148736 "PREDICTED: prostatic acid phosphatase [Pan troglodytes]" 100.00 418 97.44 97.44 6.83e-17
SP P15309 "RecName: Full=Prostatic acid phosphatase; Short=PAP; AltName: Full=5'-nucleotidase; Short=5'-NT; AltName: Full=Ecto-5'-nucleoti" 100.00 386 100.00 100.00 1.02e-17
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$entity 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
$entity 'obtained from a vendor' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$entity 1.2 mM 'natural abundance'
'sodium phosphate' 20 mM 'natural abundance'
D2O 10 % '[U-99% 2H]'
TFE 30 % '[U-99% 2H]'
stop_
save_
############################
# Computer software used #
############################
save_CYANA
_Saveframe_category software
_Name CYANA
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Guntert, Mumenthaler and Wuthrich' . .
stop_
loop_
_Task
'structure solution'
refinement
stop_
_Details .
save_
save_TALOS
_Saveframe_category software
_Name TALOS
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Cornilescu, Delaglio and Bax' . .
stop_
loop_
_Task
refinement
stop_
_Details .
save_
save_Molmol
_Saveframe_category software
_Name Molmol
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Koradi, Billeter and Wuthrich' . .
stop_
loop_
_Task
'structure solution'
stop_
_Details .
save_
save_SPARKY
_Saveframe_category software
_Name SPARKY
_Version .
loop_
_Vendor
_Address
_Electronic_address
Goddard . .
stop_
loop_
_Task
'chemical shift assignment'
'data analysis'
stop_
_Details .
save_
save_ProcheckNMR
_Saveframe_category software
_Name ProcheckNMR
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Laskowski and MacArthur' . .
stop_
loop_
_Task
'data analysis'
'structure solution'
stop_
_Details .
save_
save_TOPSPIN
_Saveframe_category software
_Name TOPSPIN
_Version .
loop_
_Vendor
_Address
_Electronic_address
'Bruker Biospin' . .
stop_
loop_
_Task
collection
processing
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model Avance
_Field_strength 900
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-1H_TOCSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H TOCSY'
_Sample_label $sample_1
save_
save_2D_1H-1H_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-1H NOESY'
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
temperature 298 . K
pH 7.5 . pH
pressure 1 . atm
'ionic strength' 0 . M
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_1
_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
water H 1 protons ppm 4.7 internal direct . . . 1.0
stop_
save_
###################################
# Assigned chemical shift lists #
###################################
###################################################################
# Chemical Shift Ambiguity Index Value Definitions #
# #
# The values other than 1 are used for those atoms with different #
# chemical shifts that cannot be assigned to stereospecific atoms #
# or to specific residues or chains. #
# #
# Index Value Definition #
# #
# 1 Unique (including isolated methyl protons, #
# geminal atoms, and geminal methyl #
# groups with identical chemical shifts) #
# (e.g. ILE HD11, HD12, HD13 protons) #
# 2 Ambiguity of geminal atoms or geminal methyl #
# proton groups (e.g. ASP HB2 and HB3 #
# protons, LEU CD1 and CD2 carbons, or #
# LEU HD11, HD12, HD13 and HD21, HD22, #
# HD23 methyl protons) #
# 3 Aromatic atoms on opposite sides of #
# symmetrical rings (e.g. TYR HE1 and HE2 #
# protons) #
# 4 Intraresidue ambiguities (e.g. LYS HG and #
# HD protons or TRP HZ2 and HZ3 protons) #
# 5 Interresidue ambiguities (LYS 12 vs. LYS 27) #
# 6 Intermolecular ambiguities (e.g. ASP 31 CA #
# in monomer 1 and ASP 31 CA in monomer 2 #
# of an asymmetrical homodimer, duplex #
# DNA assignments, or other assignments #
# that may apply to atoms in one or more #
# molecule in the molecular assembly) #
# 9 Ambiguous, specific ambiguity not defined #
# #
###################################################################
save_assigned_chem_shift_list_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'2D 1H-1H TOCSY'
'2D 1H-1H NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference_1
_Mol_system_component_name PAP248-286
_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
1 249 2 ILE HA H 4.111 0.02 1
2 249 2 ILE HB H 2.181 0.02 1
3 249 2 ILE HD1 H 0.852 0.02 1
4 250 3 HIS H H 8.543 0.02 1
5 250 3 HIS HA H 4.544 0.02 1
6 250 3 HIS HB2 H 3.159 0.02 2
7 250 3 HIS HB3 H 3.234 0.02 2
8 250 3 HIS HD2 H 7.134 0.02 1
9 250 3 HIS HE1 H 8.037 0.02 1
10 251 4 LYS H H 8.477 0.02 1
11 251 4 LYS HA H 4.224 0.02 1
12 252 5 GLN H H 8.474 0.02 1
13 252 5 GLN HA H 4.253 0.02 1
14 252 5 GLN HB2 H 2.179 0.02 1
15 252 5 GLN HB3 H 2.179 0.02 1
16 252 5 GLN HG2 H 2.465 0.02 1
17 252 5 GLN HG3 H 2.465 0.02 1
18 252 5 GLN HE21 H 7.553 0.02 1
19 252 5 GLN HE22 H 6.857 0.02 1
20 253 6 LYS H H 8.435 0.02 1
21 253 6 LYS HA H 4.223 0.02 1
22 253 6 LYS HB2 H 1.917 0.02 1
23 253 6 LYS HB3 H 1.917 0.02 1
24 253 6 LYS HG2 H 1.486 0.02 1
25 253 6 LYS HG3 H 1.486 0.02 1
26 253 6 LYS HD2 H 1.593 0.02 1
27 253 6 LYS HD3 H 1.736 0.02 1
28 254 7 GLU H H 8.448 0.02 1
29 254 7 GLU HA H 4.244 0.02 1
30 254 7 GLU HB2 H 2.125 0.02 1
31 254 7 GLU HB3 H 2.125 0.02 1
32 254 7 GLU HG2 H 2.367 0.02 1
33 254 7 GLU HG3 H 2.367 0.02 1
34 255 8 LYS H H 8.318 0.02 1
35 255 8 LYS HA H 4.200 0.02 1
36 255 8 LYS HB2 H 1.909 0.02 1
37 255 8 LYS HB3 H 1.945 0.02 1
38 255 8 LYS HG2 H 1.489 0.02 1
39 255 8 LYS HG3 H 1.489 0.02 1
40 255 8 LYS HD2 H 1.589 0.02 1
41 255 8 LYS HD3 H 1.740 0.02 1
42 256 9 SER H H 8.219 0.02 1
43 256 9 SER HA H 4.403 0.02 1
44 256 9 SER HB2 H 3.986 0.02 2
45 256 9 SER HB3 H 4.046 0.02 2
46 257 10 ARG H H 8.034 0.02 1
47 257 10 ARG HA H 4.229 0.02 1
48 257 10 ARG HB2 H 1.992 0.02 2
49 257 10 ARG HB3 H 2.030 0.02 2
50 257 10 ARG HG2 H 1.701 0.02 2
51 257 10 ARG HG3 H 1.829 0.02 2
52 258 11 LEU H H 8.070 0.02 1
53 258 11 LEU HA H 4.315 0.02 1
54 258 11 LEU HB2 H 1.746 0.02 2
55 258 11 LEU HB3 H 1.815 0.02 2
56 258 11 LEU HG H 1.680 0.02 1
57 258 11 LEU HD1 H 0.934 0.02 2
58 258 11 LEU HD2 H 0.978 0.02 2
59 259 12 GLN H H 8.237 0.02 1
60 259 12 GLN HA H 4.249 0.02 1
61 259 12 GLN HB2 H 2.189 0.02 2
62 259 12 GLN HB3 H 2.189 0.02 2
63 259 12 GLN HG2 H 2.424 0.02 2
64 259 12 GLN HG3 H 2.503 0.02 2
65 259 12 GLN HE21 H 7.304 0.02 1
66 259 12 GLN HE22 H 6.811 0.02 1
67 260 13 GLY H H 8.384 0.02 1
68 260 13 GLY HA2 H 3.960 0.02 1
69 260 13 GLY HA3 H 3.960 0.02 1
70 261 14 GLY H H 8.202 0.02 1
71 261 14 GLY HA2 H 3.945 0.02 2
72 261 14 GLY HA3 H 3.978 0.02 2
73 262 15 VAL H H 7.903 0.02 1
74 262 15 VAL HA H 3.877 0.02 1
75 262 15 VAL HB H 2.266 0.02 1
76 262 15 VAL HG1 H 1.058 0.02 2
77 262 15 VAL HG2 H 1.114 0.02 2
78 263 16 LEU H H 7.856 0.02 1
79 263 16 LEU HA H 4.236 0.02 1
80 263 16 LEU HB2 H 1.863 0.02 1
81 263 16 LEU HB3 H 1.863 0.02 1
82 263 16 LEU HG H 1.737 0.02 1
83 263 16 LEU HD1 H 0.933 0.02 2
84 263 16 LEU HD2 H 0.993 0.02 2
85 264 17 VAL H H 8.089 0.02 1
86 264 17 VAL HA H 3.674 0.02 1
87 264 17 VAL HB H 2.135 0.02 1
88 264 17 VAL HG1 H 0.999 0.02 2
89 264 17 VAL HG2 H 1.099 0.02 2
90 265 18 ASN H H 7.952 0.02 1
91 265 18 ASN HA H 4.428 0.02 1
92 265 18 ASN HB2 H 2.891 0.02 1
93 265 18 ASN HB3 H 2.891 0.02 1
94 265 18 ASN HD21 H 7.800 0.02 1
95 265 18 ASN HD22 H 6.822 0.02 1
96 266 19 GLU H H 8.182 0.02 1
97 266 19 GLU HA H 4.281 0.02 1
98 266 19 GLU HB2 H 2.253 0.02 2
99 266 19 GLU HB3 H 2.351 0.02 2
100 266 19 GLU HG2 H 2.394 0.02 2
101 266 19 GLU HG3 H 2.487 0.02 2
102 267 20 ILE H H 8.480 0.02 1
103 267 20 ILE HA H 3.783 0.02 1
104 267 20 ILE HB H 2.082 0.02 1
105 267 20 ILE HG12 H 1.127 0.02 1
106 267 20 ILE HG13 H 1.127 0.02 1
107 267 20 ILE HG2 H 0.994 0.02 1
108 267 20 ILE HD1 H 0.867 0.02 1
109 268 21 LEU H H 8.673 0.02 1
110 268 21 LEU HA H 4.175 0.02 1
111 268 21 LEU HB2 H 1.929 0.02 2
112 268 21 LEU HB3 H 1.983 0.02 2
113 268 21 LEU HG H 1.531 0.02 1
114 268 21 LEU HD1 H 0.928 0.02 2
115 268 21 LEU HD2 H 0.996 0.02 2
116 269 22 ASN H H 8.242 0.02 1
117 269 22 ASN HA H 4.500 0.02 1
118 269 22 ASN HB2 H 2.760 0.02 2
119 269 22 ASN HB3 H 3.056 0.02 2
120 269 22 ASN HD21 H 7.649 0.02 1
121 269 22 ASN HD22 H 6.800 0.02 1
122 270 23 HIS H H 8.289 0.02 1
123 270 23 HIS HA H 4.364 0.02 1
124 270 23 HIS HB2 H 3.360 0.02 2
125 270 23 HIS HB3 H 3.397 0.02 2
126 270 23 HIS HD2 H 7.012 0.02 1
127 270 23 HIS HE1 H 7.957 0.02 1
128 271 24 MET H H 8.688 0.02 1
129 271 24 MET HA H 4.166 0.02 1
130 271 24 MET HB2 H 2.175 0.02 2
131 271 24 MET HB3 H 2.340 0.02 2
132 271 24 MET HG2 H 2.644 0.02 2
133 271 24 MET HG3 H 2.847 0.02 2
134 272 25 LYS H H 8.453 0.02 1
135 272 25 LYS HA H 4.022 0.02 1
136 272 25 LYS HB2 H 1.958 0.02 2
137 272 25 LYS HB3 H 2.015 0.02 2
138 272 25 LYS HG2 H 1.668 0.02 2
139 272 25 LYS HG3 H 1.740 0.02 2
140 272 25 LYS HD2 H 1.672 0.02 1
141 272 25 LYS HD3 H 1.727 0.02 1
142 273 26 ARG H H 7.877 0.02 1
143 273 26 ARG HA H 4.112 0.02 1
144 273 26 ARG HB2 H 1.856 0.02 2
145 273 26 ARG HB3 H 1.943 0.02 2
146 273 26 ARG HG2 H 1.643 0.02 1
147 273 26 ARG HG3 H 1.643 0.02 1
148 274 27 ALA H H 8.245 0.02 1
149 274 27 ALA HA H 4.177 0.02 1
150 274 27 ALA HB H 1.450 0.02 1
151 275 28 THR H H 7.716 0.02 1
152 275 28 THR HA H 4.379 0.02 1
153 275 28 THR HB H 4.258 0.02 1
154 275 28 THR HG2 H 1.355 0.02 1
155 276 29 GLN H H 7.811 0.02 1
156 276 29 GLN HA H 4.405 0.02 1
157 276 29 GLN HB2 H 2.127 0.02 2
158 276 29 GLN HB3 H 2.245 0.02 2
159 276 29 GLN HG2 H 2.431 0.02 2
160 276 29 GLN HG3 H 2.497 0.02 2
161 276 29 GLN HE21 H 7.441 0.02 1
162 276 29 GLN HE22 H 6.763 0.02 1
163 277 30 ILE H H 7.850 0.02 1
164 277 30 ILE HA H 4.409 0.02 1
165 277 30 ILE HB H 2.016 0.02 1
166 277 30 ILE HG12 H 1.244 0.02 1
167 277 30 ILE HG13 H 1.244 0.02 1
168 277 30 ILE HG2 H 1.004 0.02 1
169 277 30 ILE HD1 H 0.924 0.02 1
170 278 31 PRO HA H 4.424 0.02 1
171 278 31 PRO HB2 H 2.018 0.02 2
172 278 31 PRO HB3 H 2.301 0.02 2
173 278 31 PRO HD2 H 3.700 0.02 2
174 278 31 PRO HD3 H 3.974 0.02 2
175 279 32 SER H H 8.061 0.02 1
176 279 32 SER HA H 4.345 0.02 1
177 279 32 SER HB2 H 3.938 0.02 2
178 279 32 SER HB3 H 3.973 0.02 2
179 280 33 TYR H H 7.946 0.02 1
180 280 33 TYR HA H 4.474 0.02 1
181 280 33 TYR HB2 H 3.136 0.02 1
182 280 33 TYR HB3 H 3.136 0.02 1
183 280 33 TYR HD1 H 7.135 0.02 1
184 280 33 TYR HD2 H 7.135 0.02 1
185 280 33 TYR HE1 H 6.863 0.02 1
186 280 33 TYR HE2 H 6.863 0.02 1
187 281 34 LYS H H 7.896 0.02 1
188 281 34 LYS HA H 4.132 0.02 1
189 281 34 LYS HB2 H 1.856 0.02 1
190 281 34 LYS HB3 H 1.856 0.02 1
191 281 34 LYS HG2 H 1.376 0.02 2
192 281 34 LYS HG3 H 1.417 0.02 2
193 281 34 LYS HD2 H 1.709 0.02 2
194 281 34 LYS HD3 H 1.782 0.02 2
195 282 35 LYS H H 7.797 0.02 1
196 282 35 LYS HA H 4.258 0.02 1
197 282 35 LYS HB2 H 1.857 0.02 2
198 282 35 LYS HB3 H 1.918 0.02 2
199 282 35 LYS HG2 H 1.468 0.02 2
200 282 35 LYS HG3 H 1.527 0.02 2
201 282 35 LYS HD2 H 1.747 0.02 1
202 282 35 LYS HD3 H 1.747 0.02 1
203 283 36 LEU H H 7.859 0.02 1
204 283 36 LEU HA H 4.342 0.02 1
205 283 36 LEU HB2 H 1.758 0.02 1
206 283 36 LEU HB3 H 1.758 0.02 1
207 283 36 LEU HG H 1.639 0.02 1
208 283 36 LEU HD1 H 0.891 0.02 2
209 283 36 LEU HD2 H 0.950 0.02 2
210 284 37 ILE H H 7.667 0.02 1
211 284 37 ILE HA H 4.210 0.02 1
212 284 37 ILE HB H 1.905 0.02 1
213 284 37 ILE HG12 H 1.202 0.02 2
214 284 37 ILE HG13 H 1.470 0.02 2
215 284 37 ILE HD1 H 0.859 0.02 1
216 285 38 MET H H 7.972 0.02 1
217 285 38 MET HA H 4.492 0.02 1
218 285 38 MET HB2 H 1.968 0.02 2
219 285 38 MET HB3 H 2.077 0.02 2
220 285 38 MET HG2 H 2.481 0.02 2
221 285 38 MET HG3 H 2.559 0.02 2
222 286 39 TYR H H 7.484 0.02 1
223 286 39 TYR HA H 4.434 0.02 1
224 286 39 TYR HB2 H 2.967 0.02 2
225 286 39 TYR HB3 H 3.129 0.02 2
226 286 39 TYR HD1 H 7.160 0.02 1
227 286 39 TYR HD2 H 7.160 0.02 1
228 286 39 TYR HE1 H 6.863 0.02 1
229 286 39 TYR HE2 H 6.863 0.02 1
stop_
save_