data_5599
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
The Tertiary Structure and Backbone Dynamics of Human Prolactin: Evidence for
Reversible Oligomerization in Solution
;
_BMRB_accession_number 5599
_BMRB_flat_file_name bmr5599.str
_Entry_type original
_Submission_date 2002-11-25
_Accession_date 2002-11-26
_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 Keeler Camille . .
2 Dannies Priscilla S. .
3 Hodsdon Michael E. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 676
"13C chemical shifts" 668
"15N chemical shifts" 170
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2003-05-14 original author .
stop_
_Original_release_date 2003-05-14
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'The Tertiary Structure and Backbone Dynamics of Human Prolactin'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 22616165
_PubMed_ID 12729745
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Keeler Camille . .
2 Dannies Priscilla S. .
3 Hodsdon Michael E. .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_volume 328
_Journal_issue 5
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1105
_Page_last 1121
_Year 2003
_Details .
save_
#######################################
# Cited references within the entry #
#######################################
save_reference_1
_Saveframe_category citation
_Citation_full
;
F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax:
NMRPipe: a multidimensional spectral processing system based on UNIX pipes.
J.Biomol. NMR. 6, 277-293 (1995)
;
_Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8520220
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Delaglio F. . .
2 Grzesiek S. . .
3 Vuister 'G. W.' W. .
4 Zhu G. . .
5 Pfeifer J. . .
6 Bax A. . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 6
_Journal_issue 3
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 277
_Page_last 293
_Year 1995
_Details
;
The NMRPipe system is a UNIX software environment of processing, graphics, and
analysis tools designed to meet current routine and research-oriented
multidimensional processing requirements, and to anticipate and accommodate
future demands and developments. The system is based on UNIX pipes, which allow
programs running simultaneously to exchange streams of data under user control.
In an NMRPipe processing scheme, a stream of spectral data flows through a
pipeline of processing programs, each of which performs one component of the
overall scheme, such as Fourier transformation or linear prediction. Complete
multidimensional processing schemes are constructed as simple UNIX shell
scripts. The processing modules themselves maintain and exploit accurate
records of data sizes, detection modes, and calibration information in all
dimensions, so that schemes can be constructed without the need to explicitly
define or anticipate data sizes or storage details of real and imaginary
channels during processing. The asynchronous pipeline scheme provides other
substantial advantages, including high flexibility, favorable processing
speeds, choice of both all-in-memory and disk-bound processing, easy adaptation
to different data formats, simpler software development and maintenance, and
the ability to distribute processing tasks on multi-CPU computers and computer
networks.
;
save_
save_reference_2
_Saveframe_category citation
_Citation_full
;
J. Vavanagh, W. J. Fairbrother, A. G. Palmer, N. J. Skelton;
Protein NMR spectroscopy : principles and practice. Academic Press, New York
(1996) pp 175-176
;
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first .
_Page_last .
_Year .
_Details .
save_
save_reference_3
_Saveframe_category citation
_Citation_full
;
T. D. Goddard and D. G. Kneller, SPARKY 3,
University of California, San Francisco
;
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first .
_Page_last .
_Year .
_Details .
save_
save_reference_4
_Saveframe_category citation
_Citation_full
;
NMRView: A computer program for the visualization and analysis of NMR data
(1994) B. A. Johnson and R. A. Blevins, J. Biomol. NMR 4:603-614
;
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first .
_Page_last .
_Year .
_Details .
save_
save_reference_5
_Saveframe_category citation
_Citation_full
;
Protein NMR Structure Determination with Automated NOE Assignment using
the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA.
Herrmann T., Guntert P. & Wuthrich K.
J. Mol. Biol. 2002 May 24; 319(1): 209-227.
;
_Citation_title 'Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 12051947
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Herrmann Torsten . .
2 Guntert Peter . .
3 Wuthrich Kurt . .
stop_
_Journal_abbreviation 'J. Mol. Biol.'
_Journal_name_full 'Journal of molecular biology'
_Journal_volume 319
_Journal_issue 1
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 209
_Page_last 227
_Year 2002
_Details
;
Combined automated NOE assignment and structure determination module (CANDID) is
a new software for efficient NMR structure determination of proteins by
automated assignment of the NOESY spectra. CANDID uses an iterative approach
with multiple cycles of NOE cross-peak assignment and protein structure
calculation using the fast DYANA torsion angle dynamics algorithm, so that the
result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE
cross-peak assignments in all available spectra and a three-dimensional protein
structure represented by a bundle of conformers. The input for the first CANDID
cycle consists of the amino acid sequence, the chemical shift list from the
sequence-specific resonance assignment, and listings of the cross-peak
positions and volumes in one or several two, three or four-dimensional NOESY
spectra. The input for the second and subsequent CANDID cycles contains the
three-dimensional protein structure from the previous cycle, in addition to the
complete input used for the first cycle. CANDID includes two new elements that
make it robust with respect to the presence of artifacts in the input data,
i.e. network-anchoring and constraint-combination, which have a key role in de
novo protein structure determinations for the successful generation of the
correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use
of the fact that any network of correct NOE cross-peak assignments forms a
self-consistent set; the initial, chemical shift-based assignments for each
individual NOE cross-peak are therefore weighted by the extent to which they
can be embedded into the network formed by all other NOE cross-peak
assignments. Constraint-combination reduces the deleterious impact of artifact
NOE upper distance constraints in the input for a protein structure calculation
by combining the assignments for two or several peaks into a single upper limit
distance constraint, which lowers the probability that the presence of an
artifact peak will influence the outcome of the structure calculation. CANDID
test calculations were performed with NMR data sets of four proteins for which
high-quality structures had previously been solved by interactive protocols,
and they yielded comparable results to these reference structure determinations
with regard to both the residual constraint violations, and the precision and
accuracy of the atomic coordinates. The CANDID approach has further been
validated by de novo NMR structure determinations of four additional proteins.
The experience gained in these calculations shows that once nearly complete
sequence-specific resonance assignments are available, the automated CANDID
approach results in greatly enhanced efficiency of the NOESY spectral analysis.
The fact that the correct fold is obtained in cycle 1 of a de novo structure
calculation is the single most important advance achieved with CANDID, when
compared with previously proposed automated NOESY assignment methods that do
not use network-anchoring and constraint-combination.
;
save_
##################################
# Molecular system description #
##################################
save_system_hPrl
_Saveframe_category molecular_system
_Mol_system_name 'Human Prolactin'
_Abbreviation_common hPrl
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
prolactin $hPrl
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disulfide bound'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_hPrl
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Human Prolactin'
_Abbreviation_common hPrl
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 199
_Mol_residue_sequence
;
LPICPGGAARCQVTLRDLFD
RAVVLSHYIHNLSSEMFSEF
DKRYTHGRGFITKAINSCHT
SSLATPEDKEQAQQMNQKDF
LSLIVSILRSWNEPLYHLVT
EVRGMQEAPEAILSKAVEIE
EQTKRLLEGMELIVSQVHPE
TKENEIYPVWSGLPSLQMAD
EESRLSAYYNLLHCLRRDSH
KIDNYLKLLKCRIIHNNNC
;
loop_
_Residue_seq_code
_Residue_label
1 LEU 2 PRO 3 ILE 4 CYS 5 PRO
6 GLY 7 GLY 8 ALA 9 ALA 10 ARG
11 CYS 12 GLN 13 VAL 14 THR 15 LEU
16 ARG 17 ASP 18 LEU 19 PHE 20 ASP
21 ARG 22 ALA 23 VAL 24 VAL 25 LEU
26 SER 27 HIS 28 TYR 29 ILE 30 HIS
31 ASN 32 LEU 33 SER 34 SER 35 GLU
36 MET 37 PHE 38 SER 39 GLU 40 PHE
41 ASP 42 LYS 43 ARG 44 TYR 45 THR
46 HIS 47 GLY 48 ARG 49 GLY 50 PHE
51 ILE 52 THR 53 LYS 54 ALA 55 ILE
56 ASN 57 SER 58 CYS 59 HIS 60 THR
61 SER 62 SER 63 LEU 64 ALA 65 THR
66 PRO 67 GLU 68 ASP 69 LYS 70 GLU
71 GLN 72 ALA 73 GLN 74 GLN 75 MET
76 ASN 77 GLN 78 LYS 79 ASP 80 PHE
81 LEU 82 SER 83 LEU 84 ILE 85 VAL
86 SER 87 ILE 88 LEU 89 ARG 90 SER
91 TRP 92 ASN 93 GLU 94 PRO 95 LEU
96 TYR 97 HIS 98 LEU 99 VAL 100 THR
101 GLU 102 VAL 103 ARG 104 GLY 105 MET
106 GLN 107 GLU 108 ALA 109 PRO 110 GLU
111 ALA 112 ILE 113 LEU 114 SER 115 LYS
116 ALA 117 VAL 118 GLU 119 ILE 120 GLU
121 GLU 122 GLN 123 THR 124 LYS 125 ARG
126 LEU 127 LEU 128 GLU 129 GLY 130 MET
131 GLU 132 LEU 133 ILE 134 VAL 135 SER
136 GLN 137 VAL 138 HIS 139 PRO 140 GLU
141 THR 142 LYS 143 GLU 144 ASN 145 GLU
146 ILE 147 TYR 148 PRO 149 VAL 150 TRP
151 SER 152 GLY 153 LEU 154 PRO 155 SER
156 LEU 157 GLN 158 MET 159 ALA 160 ASP
161 GLU 162 GLU 163 SER 164 ARG 165 LEU
166 SER 167 ALA 168 TYR 169 TYR 170 ASN
171 LEU 172 LEU 173 HIS 174 CYS 175 LEU
176 ARG 177 ARG 178 ASP 179 SER 180 HIS
181 LYS 182 ILE 183 ASP 184 ASN 185 TYR
186 LEU 187 LYS 188 LEU 189 LEU 190 LYS
191 CYS 192 ARG 193 ILE 194 ILE 195 HIS
196 ASN 197 ASN 198 ASN 199 CYS
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
BMRB 15773 hPrl 100.00 199 100.00 100.00 1.02e-145
BMRB 6643 hPRL 100.00 199 100.00 100.00 1.02e-145
PDB 1RW5 "Solution Structure Of Human Prolactin" 100.00 199 100.00 100.00 1.02e-145
PDB 2Q98 "X-Ray Structure Of A Prolactin Antagonist" 95.48 191 98.95 98.95 2.21e-135
PDB 3D48 "Crystal Structure Of A Prolactin Receptor Antagonist Bound To The Extracellular Domain Of The Prolactin Receptor" 93.97 188 99.47 99.47 9.03e-134
PDB 3MZG "Crystal Structure Of A Human Prolactin Receptor Antagonist In Complex With The Extracellular Domain Of The Human Prolactin Rece" 92.96 186 99.46 99.46 4.31e-132
PDB 3N06 "A Mutant Human Prolactin Receptor Antagonist H27a In Complex With The Extracellular Domain Of The Human Prolactin Receptor" 92.96 186 98.92 98.92 5.45e-131
PDB 3N0P "A Mutant Human Prolactin Receptor Antagonist H30a In Complex With The Extracellular Domain Of The Human Prolactin Receptor" 92.96 186 98.92 98.92 5.45e-131
PDB 3NCB "A Mutant Human Prolactin Receptor Antagonist H180a In Complex With The Extracellular Domain Of The Human Prolactin Receptor" 92.96 186 98.92 98.92 5.45e-131
PDB 3NCC "A Human Prolactin Receptor Antagonist In Complex With The Mutant Extracellular Domain H188a Of The Human Prolactin Receptor" 92.96 186 99.46 99.46 4.31e-132
PDB 3NCE "A Mutant Human Prolactin Receptor Antagonist H27a In Complex With The Mutant Extracellular Domain H188a Of The Human Prolactin " 92.96 186 98.92 98.92 5.45e-131
PDB 3NCF "A Mutant Human Prolactin Receptor Antagonist H30a In Complex With The Mutant Extracellular Domain H188a Of The Human Prolactin " 92.96 186 98.92 98.92 5.45e-131
PDB 3NPZ "Prolactin Receptor (Prlr) Complexed With The Natural Hormone (Prl)" 100.00 199 100.00 100.00 1.02e-145
DBJ BAA00312 "prolactin PRL precursor [Homo sapiens]" 100.00 217 98.99 99.50 5.01e-144
DBJ BAI46568 "prolactin [synthetic construct]" 100.00 227 100.00 100.00 3.23e-145
EMBL CAA23829 "prolactin [Homo sapiens]" 100.00 227 100.00 100.00 3.23e-145
EMBL CAA25214 "prolactin [Homo sapiens]" 100.00 217 100.00 100.00 1.01e-145
EMBL CAA38264 "prolactin [Homo sapiens]" 100.00 220 100.00 100.00 1.11e-145
GB AAA18471 "prolactin [Macaca mulatta]" 100.00 227 97.99 99.50 1.12e-142
GB AAA60173 "prolactin, partial [Homo sapiens]" 100.00 217 99.50 99.50 1.66e-144
GB AAB70858 "preprolactin, partial [Homo sapiens]" 86.93 191 98.84 98.84 2.01e-122
GB AAH15850 "Prolactin [Homo sapiens]" 100.00 227 100.00 100.00 3.23e-145
GB AAH88370 "Prolactin [Homo sapiens]" 100.00 228 100.00 100.00 2.44e-145
PRF 1005222A prolactin 100.00 217 100.00 100.00 1.01e-145
REF NP_000939 "prolactin precursor [Homo sapiens]" 100.00 227 100.00 100.00 3.23e-145
REF NP_001040593 "prolactin precursor [Macaca mulatta]" 100.00 227 97.99 99.50 1.12e-142
REF NP_001157030 "prolactin precursor [Homo sapiens]" 100.00 227 100.00 100.00 3.23e-145
REF XP_002816520 "PREDICTED: prolactin [Pongo abelii]" 100.00 227 98.99 99.50 2.35e-143
REF XP_003263607 "PREDICTED: prolactin [Nomascus leucogenys]" 100.00 227 99.50 100.00 2.12e-144
SP P01236 "RecName: Full=Prolactin; Short=PRL; Flags: Precursor [Homo sapiens]" 100.00 227 100.00 100.00 3.23e-145
SP P55151 "RecName: Full=Prolactin; Short=PRL; Flags: Precursor [Macaca mulatta]" 100.00 227 97.99 99.50 1.12e-142
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$hPrl 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_type
_Vector_name
$hPrl 'recombinant technology' 'E. Coli' Escherichia coli 'BL21 DE3' plasmid pT7L-hPrl
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
$hPrl 1.0 mM '[U-13C; U-15N]'
'phosphate buffer' 20 mM .
NaCl 100 mM .
stop_
save_
############################
# Computer software used #
############################
save_nmrView
_Saveframe_category software
_Name nmrView
_Version 5.0.4
loop_
_Task
'4D data analysis'
stop_
_Details .
_Citation_label $reference_4
save_
save_Sparky
_Saveframe_category software
_Name Sparky
_Version 3.106
loop_
_Task
'3D data analysis'
stop_
_Details .
_Citation_label $reference_3
save_
save_CYANA
_Saveframe_category software
_Name CYANA
_Version 1.0.5
loop_
_Task
'structure solution'
stop_
_Details .
_Citation_label $reference_5
save_
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 1.0
loop_
_Task
'processing varian format data'
stop_
_Details .
_Citation_label $reference_1
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model INOVA
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_HNCO_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label $sample_1
save_
save_HNCA_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label $sample_1
save_
save_HNCACA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACA
_Sample_label $sample_1
save_
save_HN(CO)CA_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_Sample_label $sample_1
save_
save_CBCA(CO)NH_5
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label $sample_1
save_
save_H(CA)CO(CA)NH_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(CA)CO(CA)NH
_Sample_label $sample_1
save_
save_C(CO)NH_7
_Saveframe_category NMR_applied_experiment
_Experiment_name C(CO)NH
_Sample_label $sample_1
save_
save_H(CCO)NH_8
_Saveframe_category NMR_applied_experiment
_Experiment_name H(CCO)NH
_Sample_label $sample_1
save_
save_HCCH-TOCSY_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_Sample_label $sample_1
save_
save_(4D)_13C_15N_HMQC-NOESY-HSQC_10
_Saveframe_category NMR_applied_experiment
_Experiment_name '(4D) 13C 15N HMQC-NOESY-HSQC'
_Sample_label $sample_1
save_
save_(3D)_15N_HSQC-NOESY_11
_Saveframe_category NMR_applied_experiment
_Experiment_name '(3D) 15N HSQC-NOESY'
_Sample_label $sample_1
save_
save_(3D)_13C_NOESY-HSQC_12
_Saveframe_category NMR_applied_experiment
_Experiment_name '(3D) 13C NOESY-HSQC'
_Sample_label $sample_1
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CO)CA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name H(CA)CO(CA)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_7
_Saveframe_category NMR_applied_experiment
_Experiment_name C(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_8
_Saveframe_category NMR_applied_experiment
_Experiment_name H(CCO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_10
_Saveframe_category NMR_applied_experiment
_Experiment_name '(4D) 13C 15N HMQC-NOESY-HSQC'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_11
_Saveframe_category NMR_applied_experiment
_Experiment_name '(3D) 15N HSQC-NOESY'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_12
_Saveframe_category NMR_applied_experiment
_Experiment_name '(3D) 13C NOESY-HSQC'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_conditions_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.8 0.2 n/a
temperature 298 1 K
'ionic strength' 0.2 0.02 M
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
_Reference_correction_type
_Correction_value
DSS H 1 methyl ppm 0.00 external direct cylindrical external_to_the_sample parallel_to_Bo 1 temperature 0.052
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 $conditions_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name prolactin
_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 . 2 PRO CA C 63.383 0.075 1
2 . 2 PRO HA H 4.524 0.0090 1
3 . 2 PRO C C 176.431 0.0 1
4 . 2 PRO CB C 32.497 0.045 1
5 . 2 PRO HB2 H 2.31 0.0060 1
6 . 2 PRO HB3 H 1.96 0.0060 1
7 . 2 PRO CG C 28.019 0.02 1
8 . 2 PRO HG2 H 2.08 0.0030 1
9 . 2 PRO CD C 51.109 0.019 1
10 . 2 PRO HD2 H 3.892 0.011 1
11 . 2 PRO HD3 H 3.698 0.0050 1
12 . 3 ILE H H 8.153 0.0040 1
13 . 3 ILE N N 121.425 0.253 1
14 . 3 ILE CA C 62.191 0.091 1
15 . 3 ILE HA H 4.13 0.0060 1
16 . 3 ILE C C 176.045 0.039 1
17 . 3 ILE CB C 39.259 0.068 1
18 . 3 ILE HB H 1.871 0.012 1
19 . 3 ILE CG2 C 20.729 4.205 1
20 . 3 ILE CG1 C 28.07 0.055 1
21 . 3 ILE HG12 H 1.226 0.0060 1
22 . 3 ILE HG13 H 0.949 0.0020 1
23 . 3 ILE CD1 C 13.599 0.01 1
24 . 3 ILE HD1 H 0.894 0.0050 1
25 . 4 CYS H H 8.354 0.0080 1
26 . 4 CYS N N 122.716 0.06 1
27 . 4 CYS CA C 53.58 0.023 1
28 . 4 CYS HA H 5.072 0.01 1
29 . 4 CYS C C 172.856 0.0 1
30 . 4 CYS CB C 41.401 0.0010 1
31 . 4 CYS HB2 H 3.053 0.0090 1
32 . 4 CYS HB3 H 3.163 0.0090 1
33 . 5 PRO C C 175.329 0.0 1
34 . 6 GLY H H 8.055 0.0 1
35 . 6 GLY N N 108.957 0.013 1
36 . 6 GLY CA C 46.123 0.149 1
37 . 6 GLY HA2 H 4.028 0.0080 1
38 . 6 GLY C C 175.083 0.0 1
39 . 7 GLY H H 8.173 0.0010 1
40 . 7 GLY N N 109.772 0.0080 1
41 . 7 GLY CA C 45.892 0.075 1
42 . 7 GLY HA2 H 3.857 0.0050 1
43 . 7 GLY HA3 H 4.185 0.0090 1
44 . 7 GLY C C 174.222 0.0 1
45 . 8 ALA H H 7.701 0.0050 1
46 . 8 ALA N N 123.839 0.03 1
47 . 8 ALA CA C 53.7 0.065 1
48 . 8 ALA HA H 4.267 0.0040 1
49 . 8 ALA C C 177.866 0.0 1
50 . 8 ALA CB C 19.769 0.061 1
51 . 8 ALA HB H 1.49 0.0040 1
52 . 9 ALA H H 8.296 0.011 1
53 . 9 ALA N N 122.683 0.126 1
54 . 9 ALA CA C 54.373 0.074 1
55 . 9 ALA HA H 4.248 0.0070 1
56 . 9 ALA C C 178.503 0.0 1
57 . 9 ALA CB C 19.573 0.15 1
58 . 9 ALA HB H 1.484 0.0070 1
59 . 10 ARG H H 7.867 0.0020 1
60 . 10 ARG N N 116.776 0.023 1
61 . 10 ARG CA C 56.277 0.046 1
62 . 10 ARG HA H 4.46 0.018 1
63 . 10 ARG C C 175.798 0.0010 1
64 . 10 ARG CB C 31.379 0.103 1
65 . 10 ARG HB2 H 1.933 0.0080 1
66 . 10 ARG HB3 H 1.821 0.0030 1
67 . 10 ARG CG C 27.615 0.027 1
68 . 10 ARG HG2 H 1.645 0.0090 1
69 . 10 ARG CD C 43.926 0.054 1
70 . 10 ARG HD2 H 3.252 0.01 1
71 . 11 CYS H H 8.069 0.0040 1
72 . 11 CYS N N 118.635 0.068 1
73 . 11 CYS CA C 56.457 0.013 1
74 . 11 CYS C C 174.049 0.0 1
75 . 11 CYS CB C 41.239 0.0 1
76 . 12 GLN CA C 56.962 0.06 1
77 . 12 GLN HA H 4.427 0.012 1
78 . 12 GLN C C 175.603 0.022 1
79 . 12 GLN CB C 29.841 0.07 1
80 . 12 GLN HB2 H 2.139 0.025 1
81 . 12 GLN CG C 34.3 0.0 1
82 . 12 GLN HG2 H 2.417 0.0020 1
83 . 13 VAL H H 7.942 0.0040 1
84 . 13 VAL N N 122.278 0.097 1
85 . 13 VAL CA C 62.637 0.052 1
86 . 13 VAL HA H 4.36 0.0080 1
87 . 13 VAL C C 176.051 0.0 1
88 . 13 VAL CB C 33.829 0.069 1
89 . 13 VAL HB H 2.122 0.0020 1
90 . 13 VAL CG1 C 21.702 0.099 1
91 . 13 VAL HG1 H 1.016 0.0040 1
92 . 14 THR H H 8.502 0.0020 1
93 . 14 THR N N 117.474 0.042 1
94 . 14 THR CA C 62.18 0.14 1
95 . 14 THR HA H 4.571 0.015 1
96 . 14 THR C C 175.542 0.0 1
97 . 14 THR CB C 71.749 0.0 1
98 . 14 THR HB H 4.615 0.0 1
99 . 14 THR CG2 C 22.43 0.0 1
100 . 14 THR HG2 H 1.372 0.0050 1
101 . 15 LEU H H 8.57 0.0060 1
102 . 15 LEU N N 123.251 0.031 1
103 . 15 LEU CA C 58.814 0.102 1
104 . 15 LEU HA H 4.113 0.0090 1
105 . 15 LEU C C 178.876 0.0 1
106 . 15 LEU CB C 42.265 0.105 1
107 . 15 LEU HB2 H 1.811 0.012 1
108 . 15 LEU CD1 C 25.861 0.293 1
109 . 15 LEU HD1 H 1.016 0.018 1
110 . 16 ARG H H 8.315 0.0040 1
111 . 16 ARG N N 119.124 0.032 1
112 . 16 ARG CA C 60.733 0.085 1
113 . 16 ARG HA H 3.957 0.017 1
114 . 16 ARG C C 177.788 0.0 1
115 . 16 ARG CB C 30.304 0.09 1
116 . 16 ARG HB2 H 1.931 0.01 1
117 . 16 ARG CG C 27.308 0.0 1
118 . 16 ARG HG2 H 1.699 0.011 1
119 . 16 ARG CD C 43.854 0.118 1
120 . 16 ARG HD2 H 3.244 0.0060 1
121 . 17 ASP H H 7.598 0.015 1
122 . 17 ASP N N 120.099 0.065 1
123 . 17 ASP CA C 58.188 0.072 1
124 . 17 ASP HA H 4.492 0.0080 1
125 . 17 ASP C C 179.234 0.0 1
126 . 17 ASP CB C 41.33 0.202 1
127 . 17 ASP HB2 H 2.994 0.0070 1
128 . 17 ASP HB3 H 2.728 0.0060 1
129 . 18 LEU H H 8.116 0.0060 1
130 . 18 LEU N N 120.485 0.073 1
131 . 18 LEU CA C 58.651 0.098 1
132 . 18 LEU HA H 3.963 0.0 1
133 . 18 LEU C C 180.331 0.0 1
134 . 18 LEU CB C 42.391 0.147 1
135 . 18 LEU HB2 H 1.951 0.0 1
136 . 18 LEU CD1 C 24.041 0.129 1
137 . 18 LEU HD1 H 0.809 0.018 1
138 . 19 PHE H H 8.534 0.0040 1
139 . 19 PHE N N 120.208 0.041 1
140 . 19 PHE CA C 63.859 0.087 1
141 . 19 PHE HA H 4.125 0.0090 1
142 . 19 PHE C C 177.943 0.0 1
143 . 19 PHE CB C 39.916 0.038 1
144 . 19 PHE HB2 H 2.934 0.012 1
145 . 19 PHE HB3 H 3.14 0.017 1
146 . 20 ASP H H 8.436 0.0040 1
147 . 20 ASP N N 120.96 0.053 1
148 . 20 ASP CA C 58.352 0.087 1
149 . 20 ASP HA H 4.54 0.0050 1
150 . 20 ASP C C 179.184 0.0 1
151 . 20 ASP CB C 40.751 0.139 1
152 . 20 ASP HB2 H 2.75 0.0060 1
153 . 20 ASP HB3 H 2.974 0.0030 1
154 . 21 ARG H H 7.822 0.0040 1
155 . 21 ARG N N 119.095 0.064 1
156 . 21 ARG CA C 59.261 0.077 1
157 . 21 ARG HA H 4.105 0.014 1
158 . 21 ARG C C 178.627 0.021 1
159 . 21 ARG CB C 30.871 0.077 1
160 . 21 ARG HB2 H 1.97 0.0060 1
161 . 21 ARG CG C 27.944 0.041 1
162 . 21 ARG HG2 H 1.766 0.01 1
163 . 21 ARG CD C 44.512 0.0 1
164 . 21 ARG HD2 H 3.173 0.0070 1
165 . 22 ALA H H 8.036 0.0080 1
166 . 22 ALA N N 123.182 0.033 1
167 . 22 ALA CA C 56.067 0.103 1
168 . 22 ALA HA H 4.064 0.0070 1
169 . 22 ALA C C 178.802 0.0 1
170 . 22 ALA CB C 18.728 0.159 1
171 . 22 ALA HB H 1.445 0.0010 1
172 . 23 VAL H H 8.064 0.0070 1
173 . 23 VAL N N 115.493 0.093 1
174 . 23 VAL CA C 65.17 0.091 1
175 . 23 VAL HA H 4.507 0.012 1
176 . 23 VAL C C 179.225 0.0 1
177 . 23 VAL CB C 32.136 0.137 1
178 . 23 VAL HB H 2.378 0.0020 1
179 . 23 VAL CG1 C 22.547 0.147 1
180 . 23 VAL HG1 H 1.206 0.0030 1
181 . 23 VAL CG2 C 22.947 0.135 1
182 . 23 VAL HG2 H 1.094 0.0020 1
183 . 24 VAL H H 7.432 0.0050 1
184 . 24 VAL N N 122.998 0.023 1
185 . 24 VAL CA C 67.309 0.134 1
186 . 24 VAL HA H 3.851 0.0070 1
187 . 24 VAL C C 179.398 0.0 1
188 . 24 VAL CB C 32.288 0.088 1
189 . 24 VAL HB H 2.252 0.0060 1
190 . 24 VAL CG1 C 22.245 0.02 1
191 . 24 VAL HG1 H 1.002 0.011 1
192 . 24 VAL CG2 C 23.876 0.06 1
193 . 24 VAL HG2 H 1.153 0.0070 1
194 . 25 LEU H H 7.819 0.013 1
195 . 25 LEU N N 121.376 0.084 1
196 . 25 LEU CA C 58.679 0.049 1
197 . 25 LEU HA H 4.331 0.014 1
198 . 25 LEU C C 179.013 0.0 1
199 . 25 LEU CB C 43.634 0.082 1
200 . 25 LEU HB2 H 2.099 0.021 1
201 . 25 LEU CG C 24.737 0.0 1
202 . 25 LEU CD1 C 25.121 0.0 1
203 . 25 LEU HD1 H 1.029 0.013 1
204 . 25 LEU HG H 1.572 0.0 1
205 . 26 SER H H 9.325 0.0050 1
206 . 26 SER N N 117.16 0.018 1
207 . 26 SER CA C 63.21 0.0040 1
208 . 26 SER C C 178.197 0.0 1
209 . 27 HIS H H 8.031 0.0050 1
210 . 27 HIS N N 126.443 0.02 1
211 . 27 HIS CA C 60.383 0.069 1
212 . 27 HIS HA H 4.389 0.016 1
213 . 27 HIS C C 177.279 0.0 1
214 . 27 HIS CB C 30.312 0.046 1
215 . 27 HIS HB2 H 3.664 0.02 1
216 . 27 HIS HB3 H 3.423 0.0060 1
217 . 28 TYR H H 7.898 0.0060 1
218 . 28 TYR N N 122.007 0.012 1
219 . 28 TYR CA C 60.821 0.112 1
220 . 28 TYR HA H 4.462 0.014 1
221 . 28 TYR C C 177.955 0.0 1
222 . 28 TYR CB C 39.143 0.043 1
223 . 28 TYR HB2 H 3.453 0.0030 1
224 . 28 TYR HB3 H 3.367 0.017 1
225 . 29 ILE H H 8.846 0.0050 1
226 . 29 ILE N N 119.921 0.048 1
227 . 29 ILE CA C 66.773 0.052 1
228 . 29 ILE HA H 3.366 0.0090 1
229 . 29 ILE C C 178.391 0.0 1
230 . 29 ILE CB C 39.029 0.08 1
231 . 29 ILE HB H 1.809 0.0080 1
232 . 29 ILE CG2 C 17.59 0.01 1
233 . 29 ILE HG13 H 0.796 0.0040 1
234 . 30 HIS H H 8.199 0.014 1
235 . 30 HIS N N 121.412 0.019 1
236 . 30 HIS CA C 59.437 0.111 1
237 . 30 HIS HA H 4.525 0.0040 1
238 . 30 HIS C C 177.83 0.0 1
239 . 30 HIS CB C 29.082 0.077 1
240 . 30 HIS HB2 H 3.0 0.025 1
241 . 30 HIS HB3 H 3.257 0.013 1
242 . 31 ASN H H 8.123 0.0040 1
243 . 31 ASN N N 121.928 0.026 1
244 . 31 ASN CA C 57.536 0.032 1
245 . 31 ASN HA H 4.13 0.0070 1
246 . 31 ASN C C 177.558 0.0 1
247 . 31 ASN CB C 38.471 0.098 1
248 . 31 ASN HB2 H 2.764 0.0070 1
249 . 32 LEU H H 8.488 0.01 1
250 . 32 LEU N N 121.422 0.038 1
251 . 32 LEU CA C 58.688 0.12 1
252 . 32 LEU HA H 3.961 0.012 1
253 . 32 LEU C C 179.547 0.0 1
254 . 32 LEU CB C 43.779 0.107 1
255 . 32 LEU HB2 H 1.695 0.0040 1
256 . 32 LEU HB3 H 1.152 0.0050 1
257 . 32 LEU CG C 27.4 0.0 1
258 . 32 LEU CD1 C 23.933 0.024 1
259 . 32 LEU HD1 H 0.45 0.0020 1
260 . 32 LEU CD2 C 25.991 0.103 1
261 . 32 LEU HD2 H 0.787 0.0020 1
262 . 32 LEU HG H 1.369 0.0070 1
263 . 33 SER H H 8.552 0.0030 1
264 . 33 SER N N 117.083 0.019 1
265 . 33 SER CA C 63.128 0.053 1
266 . 33 SER C C 177.657 0.0 1
267 . 34 SER H H 8.058 0.0030 1
268 . 34 SER N N 121.92 0.066 1
269 . 34 SER CA C 62.915 0.068 1
270 . 34 SER C C 176.844 0.0 1
271 . 35 GLU H H 8.278 0.0050 1
272 . 35 GLU N N 124.095 0.032 1
273 . 35 GLU CA C 59.911 0.112 1
274 . 35 GLU HA H 4.176 0.0070 1
275 . 35 GLU C C 179.098 0.0 1
276 . 35 GLU CB C 30.367 0.122 1
277 . 35 GLU HB2 H 2.266 0.0090 1
278 . 35 GLU CG C 36.853 0.112 1
279 . 35 GLU HG2 H 2.517 0.0050 1
280 . 36 MET H H 8.826 0.0040 1
281 . 36 MET N N 120.392 0.043 1
282 . 36 MET CA C 60.712 0.097 1
283 . 36 MET HA H 3.965 0.0 1
284 . 36 MET C C 177.317 0.0 1
285 . 36 MET CB C 34.143 0.0080 1
286 . 36 MET HB2 H 2.536 0.0 1
287 . 37 PHE H H 7.955 0.0040 1
288 . 37 PHE N N 118.707 0.047 1
289 . 37 PHE CA C 62.871 0.042 1
290 . 37 PHE HA H 4.145 0.0060 1
291 . 37 PHE C C 176.432 0.0 1
292 . 37 PHE CB C 39.543 0.037 1
293 . 37 PHE HB2 H 3.174 0.0010 1
294 . 38 SER H H 8.167 0.0030 1
295 . 38 SER N N 115.126 0.024 1
296 . 38 SER CA C 62.686 0.047 1
297 . 38 SER C C 177.147 0.0 1
298 . 38 SER CB C 63.344 0.0 1
299 . 39 GLU H H 8.368 0.0030 1
300 . 39 GLU N N 121.772 0.018 1
301 . 39 GLU CA C 59.64 0.086 1
302 . 39 GLU HA H 4.458 0.01 1
303 . 39 GLU C C 178.789 0.0 1
304 . 39 GLU CB C 30.068 0.054 1
305 . 39 GLU HB2 H 2.405 0.012 1
306 . 39 GLU CG C 36.5 0.0 1
307 . 39 GLU HG2 H 2.25 0.0 1
308 . 40 PHE H H 8.349 0.0030 1
309 . 40 PHE N N 122.015 0.013 1
310 . 40 PHE CA C 62.929 0.091 1
311 . 40 PHE HA H 4.08 0.01 1
312 . 40 PHE C C 176.888 0.0 1
313 . 40 PHE CB C 41.103 0.208 1
314 . 40 PHE HB2 H 3.282 0.0030 1
315 . 40 PHE HB3 H 3.054 0.0010 1
316 . 41 ASP H H 8.651 0.0080 1
317 . 41 ASP N N 120.625 0.104 1
318 . 41 ASP CA C 56.533 0.058 1
319 . 41 ASP HA H 4.984 0.0080 1
320 . 41 ASP C C 178.853 0.0 1
321 . 41 ASP CB C 42.607 0.245 1
322 . 41 ASP HB2 H 2.632 0.011 1
323 . 41 ASP HB3 H 2.349 0.017 1
324 . 42 LYS H H 8.046 0.0050 1
325 . 42 LYS N N 117.947 0.044 1
326 . 42 LYS CA C 59.826 0.162 1
327 . 42 LYS HA H 3.89 0.0060 1
328 . 42 LYS C C 178.106 0.0 1
329 . 42 LYS CB C 32.984 0.094 1
330 . 42 LYS HB2 H 1.897 0.02 1
331 . 42 LYS CG C 25.477 0.041 1
332 . 42 LYS HG2 H 1.427 0.0070 1
333 . 42 LYS HG3 H 1.53 0.0020 1
334 . 42 LYS CD C 29.899 0.0060 1
335 . 42 LYS HD2 H 1.647 0.0020 1
336 . 42 LYS CE C 42.51 0.029 1
337 . 42 LYS HE2 H 2.924 0.0070 1
338 . 43 ARG H H 7.285 0.0040 1
339 . 43 ARG N N 116.819 0.013 1
340 . 43 ARG CA C 57.957 0.059 1
341 . 43 ARG HA H 4.091 0.0050 1
342 . 43 ARG C C 177.482 0.0 1
343 . 43 ARG CB C 31.355 0.09 1
344 . 43 ARG HB2 H 1.468 0.0050 1
345 . 43 ARG HB3 H 1.18 0.0070 1
346 . 43 ARG CG C 27.982 0.031 1
347 . 43 ARG HG2 H 0.931 0.01 1
348 . 43 ARG CD C 43.09 0.017 1
349 . 43 ARG HD2 H 2.972 0.0030 1
350 . 44 TYR H H 8.07 0.0090 1
351 . 44 TYR N N 115.218 0.037 1
352 . 44 TYR CA C 60.441 0.047 1
353 . 44 TYR HA H 4.741 0.0 1
354 . 44 TYR C C 176.584 0.0 1
355 . 44 TYR CB C 41.257 0.137 1
356 . 44 TYR HB2 H 2.907 0.0 1
357 . 45 THR H H 7.65 0.0040 1
358 . 45 THR N N 109.159 0.018 1
359 . 45 THR CA C 63.393 0.126 1
360 . 45 THR HA H 4.393 0.0060 1
361 . 45 THR C C 175.731 0.0 1
362 . 45 THR CB C 69.914 0.071 1
363 . 45 THR HB H 4.344 0.01 1
364 . 45 THR CG2 C 24.06 0.0 1
365 . 45 THR HG2 H 1.231 0.0010 1
366 . 46 HIS H H 8.575 0.0040 1
367 . 46 HIS N N 124.846 0.09 1
368 . 46 HIS CA C 58.63 0.043 1
369 . 46 HIS HA H 4.37 0.0070 1
370 . 46 HIS C C 176.712 0.0 1
371 . 46 HIS CB C 29.639 0.072 1
372 . 46 HIS HB2 H 3.125 0.0020 1
373 . 48 ARG C C 177.527 0.0 1
374 . 49 GLY H H 8.067 0.221 1
375 . 49 GLY N N 114.491 2.958 1
376 . 49 GLY CA C 46.681 0.1 1
377 . 49 GLY HA2 H 3.818 0.0050 1
378 . 49 GLY C C 174.954 0.0 1
379 . 50 PHE H H 7.675 0.01 1
380 . 50 PHE N N 118.795 0.043 1
381 . 50 PHE CA C 58.127 0.107 1
382 . 50 PHE HA H 4.604 0.0030 1
383 . 50 PHE C C 176.331 0.0 1
384 . 50 PHE CB C 38.64 0.072 1
385 . 50 PHE HB2 H 2.953 0.0010 1
386 . 50 PHE HB3 H 3.103 0.0040 1
387 . 51 ILE H H 7.582 0.0030 1
388 . 51 ILE N N 122.094 0.03 1
389 . 51 ILE CA C 61.926 0.068 1
390 . 51 ILE HA H 4.124 0.01 1
391 . 51 ILE C C 176.471 0.0 1
392 . 51 ILE CB C 38.625 0.033 1
393 . 51 ILE HB H 1.818 0.011 1
394 . 51 ILE CG2 C 18.117 0.034 1
395 . 51 ILE HG2 H 0.795 0.0030 1
396 . 51 ILE CG1 C 27.9 0.0 1
397 . 51 ILE HG12 H 1.071 0.0050 1
398 . 51 ILE HG13 H 1.297 0.0060 1
399 . 51 ILE CD1 C 13.5 0.0 1
400 . 51 ILE HD1 H 0.752 0.0070 1
401 . 52 THR H H 7.791 0.0030 1
402 . 52 THR N N 116.84 0.031 1
403 . 52 THR CA C 63.195 0.077 1
404 . 52 THR HA H 4.235 0.0050 1
405 . 52 THR C C 174.987 0.0 1
406 . 52 THR CB C 69.647 0.054 1
407 . 52 THR HB H 4.216 0.0 1
408 . 52 THR CG2 C 21.9 0.0 1
409 . 52 THR HG2 H 1.205 0.0040 1
410 . 53 LYS H H 7.853 0.0090 1
411 . 53 LYS N N 122.686 0.03 1
412 . 53 LYS CA C 56.834 0.081 1
413 . 53 LYS HA H 4.381 0.015 1
414 . 53 LYS C C 176.459 0.0 1
415 . 53 LYS CB C 33.419 0.058 1
416 . 53 LYS HB2 H 1.809 0.0080 1
417 . 53 LYS HB3 H 1.922 0.0070 1
418 . 53 LYS CG C 25.427 0.039 1
419 . 53 LYS HG2 H 1.466 0.017 1
420 . 53 LYS CD C 29.695 0.051 1
421 . 53 LYS HD2 H 1.717 0.024 1
422 . 53 LYS CE C 42.701 0.0010 1
423 . 53 LYS HE2 H 3.003 0.0050 1
424 . 54 ALA H H 7.893 0.0090 1
425 . 54 ALA N N 125.176 0.069 1
426 . 54 ALA CA C 53.282 0.101 1
427 . 54 ALA HA H 4.413 0.0050 1
428 . 54 ALA C C 177.585 0.0 1
429 . 54 ALA CB C 19.944 0.072 1
430 . 54 ALA HB H 1.442 0.0010 1
431 . 55 ILE H H 7.896 0.0040 1
432 . 55 ILE N N 119.771 0.042 1
433 . 55 ILE CA C 61.956 0.077 1
434 . 55 ILE HA H 4.215 0.0070 1
435 . 55 ILE C C 176.043 0.0 1
436 . 55 ILE CB C 39.186 0.085 1
437 . 55 ILE HB H 1.885 0.0060 1
438 . 55 ILE CG2 C 18.035 0.144 1
439 . 55 ILE HG2 H 1.231 0.0090 1
440 . 55 ILE CG1 C 27.726 0.159 1
441 . 55 ILE HG12 H 1.501 0.016 1
442 . 55 ILE HG13 H 0.948 0.0040 1
443 . 55 ILE CD1 C 13.545 0.063 1
444 . 55 ILE HD1 H 0.896 0.0070 1
445 . 56 ASN H H 8.165 0.0080 1
446 . 56 ASN N N 124.086 0.029 1
447 . 56 ASN CA C 55.072 0.093 1
448 . 56 ASN HA H 4.598 0.0040 1
449 . 56 ASN C C 176.283 0.0 1
450 . 56 ASN CB C 41.885 0.041 1
451 . 56 ASN HB2 H 2.672 0.015 1
452 . 57 SER H H 8.141 0.013 1
453 . 57 SER N N 116.671 0.082 1
454 . 57 SER CA C 58.718 0.03 1
455 . 57 SER C C 174.794 0.0 1
456 . 57 SER CB C 64.327 0.0 1
457 . 59 HIS CA C 60.482 0.088 1
458 . 59 HIS C C 176.42 0.0 1
459 . 60 THR H H 7.41 0.0030 1
460 . 60 THR N N 109.131 0.047 1
461 . 60 THR CA C 62.583 0.034 1
462 . 60 THR C C 176.933 0.0 1
463 . 60 THR CB C 68.721 0.147 1
464 . 61 SER H H 7.846 0.0030 1
465 . 61 SER N N 119.049 0.052 1
466 . 61 SER CA C 62.059 0.09 1
467 . 61 SER C C 173.661 0.0 1
468 . 61 SER CB C 63.626 0.0 1
469 . 62 SER CA C 59.7 0.1 1
470 . 62 SER HA H 4.382 0.0080 1
471 . 62 SER C C 175.031 0.0 1
472 . 62 SER CB C 63.459 0.187 1
473 . 62 SER HB2 H 4.028 0.0060 1
474 . 63 LEU H H 7.461 0.0030 1
475 . 63 LEU N N 123.912 0.023 1
476 . 63 LEU CA C 54.987 0.146 1
477 . 63 LEU HA H 4.388 0.017 1
478 . 63 LEU C C 176.302 0.0 1
479 . 63 LEU CB C 43.05 0.236 1
480 . 63 LEU HB2 H 1.902 0.011 1
481 . 63 LEU CG C 26.7 0.0 1
482 . 63 LEU CD1 C 23.767 0.0 1
483 . 63 LEU HD1 H 0.939 0.0070 1
484 . 63 LEU HG H 1.412 0.014 1
485 . 64 ALA H H 8.354 0.0060 1
486 . 64 ALA N N 127.783 0.048 1
487 . 64 ALA CA C 52.523 0.086 1
488 . 64 ALA HA H 4.485 0.0090 1
489 . 64 ALA C C 176.9 0.032 1
490 . 64 ALA CB C 18.181 0.079 1
491 . 64 ALA HB H 1.368 0.0 1
492 . 65 THR H H 7.989 0.0030 1
493 . 65 THR N N 113.97 0.026 1
494 . 65 THR CA C 58.611 0.044 1
495 . 65 THR HA H 4.581 0.0090 1
496 . 65 THR C C 173.206 0.0 1
497 . 65 THR CB C 69.168 0.105 1
498 . 65 THR HB H 4.656 0.0080 1
499 . 65 THR CG2 C 23.307 0.0 1
500 . 65 THR HG2 H 1.323 0.0010 1
501 . 66 PRO CA C 63.226 0.09 1
502 . 66 PRO HA H 4.528 0.0070 1
503 . 66 PRO C C 178.17 0.0 1
504 . 66 PRO CB C 31.748 0.158 1
505 . 66 PRO HB2 H 1.877 0.0060 1
506 . 66 PRO CG C 28.334 0.168 1
507 . 66 PRO HG2 H 1.865 0.0050 1
508 . 66 PRO HG3 H 1.631 0.0090 1
509 . 66 PRO CD C 50.614 0.176 1
510 . 66 PRO HD2 H 3.387 0.016 1
511 . 66 PRO HD3 H 3.518 0.012 1
512 . 67 GLU H H 8.744 0.0030 1
513 . 67 GLU N N 124.791 0.031 1
514 . 67 GLU CA C 57.69 0.087 1
515 . 67 GLU HA H 4.377 0.011 1
516 . 67 GLU C C 175.747 0.0 1
517 . 67 GLU CB C 31.27 0.112 1
518 . 67 GLU HB2 H 2.221 0.014 1
519 . 67 GLU HB3 H 1.932 0.012 1
520 . 67 GLU CG C 36.595 0.01 1
521 . 67 GLU HG2 H 2.42 0.013 1
522 . 68 ASP H H 7.503 0.0010 1
523 . 68 ASP N N 117.092 0.02 1
524 . 68 ASP CA C 53.484 0.181 1
525 . 68 ASP HA H 4.739 0.0080 1
526 . 68 ASP C C 176.391 0.0 1
527 . 68 ASP CB C 43.167 0.119 1
528 . 68 ASP HB2 H 3.046 0.011 1
529 . 68 ASP HB3 H 2.862 0.014 1
530 . 69 LYS H H 8.461 0.0090 1
531 . 69 LYS N N 121.637 0.049 1
532 . 69 LYS CA C 59.825 0.087 1
533 . 69 LYS HA H 4.078 0.013 1
534 . 69 LYS C C 177.934 0.0 1
535 . 69 LYS CB C 33.317 0.271 1
536 . 69 LYS HB2 H 1.929 0.019 1
537 . 69 LYS CG C 25.248 0.174 1
538 . 69 LYS HG2 H 1.509 0.013 1
539 . 69 LYS CD C 29.819 0.13 1
540 . 69 LYS HD2 H 1.742 0.011 1
541 . 69 LYS CE C 42.561 0.147 1
542 . 69 LYS HE2 H 3.043 0.0070 1
543 . 70 GLU H H 8.255 0.0030 1
544 . 70 GLU N N 121.764 0.037 1
545 . 70 GLU CA C 60.268 0.038 1
546 . 70 GLU HA H 4.096 0.0090 1
547 . 70 GLU C C 179.306 0.0 1
548 . 70 GLU CB C 29.333 0.172 1
549 . 70 GLU HB2 H 2.148 0.01 1
550 . 70 GLU CG C 37.194 0.169 1
551 . 70 GLU HG2 H 2.318 0.0050 1
552 . 71 GLN H H 8.572 0.0030 1
553 . 71 GLN N N 119.473 0.039 1
554 . 71 GLN CA C 59.091 0.181 1
555 . 71 GLN HA H 4.06 0.01 1
556 . 71 GLN C C 179.381 0.0 1
557 . 71 GLN CB C 29.499 0.063 1
558 . 71 GLN HB2 H 2.057 0.018 1
559 . 71 GLN CG C 34.679 0.088 1
560 . 71 GLN HG2 H 2.8 0.0070 1
561 . 71 GLN HG3 H 2.439 0.012 1
562 . 72 ALA H H 7.885 0.0020 1
563 . 72 ALA N N 122.737 0.033 1
564 . 72 ALA CA C 55.382 0.03 1
565 . 72 ALA HA H 3.79 0.0080 1
566 . 72 ALA C C 178.841 0.0 1
567 . 72 ALA CB C 18.934 0.112 1
568 . 72 ALA HB H 1.475 0.0020 1
569 . 73 GLN H H 8.039 0.0060 1
570 . 73 GLN N N 116.732 0.05 1
571 . 73 GLN CA C 58.529 0.086 1
572 . 73 GLN HA H 4.079 0.013 1
573 . 73 GLN C C 176.965 0.0 1
574 . 73 GLN CB C 29.367 0.09 1
575 . 73 GLN HB2 H 2.136 0.063 1
576 . 73 GLN CG C 34.665 0.035 1
577 . 73 GLN HG2 H 2.539 0.031 1
578 . 74 GLN H H 7.292 0.0020 1
579 . 74 GLN N N 115.682 0.032 1
580 . 74 GLN CA C 56.381 0.064 1
581 . 74 GLN HA H 4.259 0.0040 1
582 . 74 GLN C C 176.31 0.0 1
583 . 74 GLN CB C 29.583 0.254 1
584 . 74 GLN HB2 H 2.183 0.011 1
585 . 74 GLN HB3 H 2.03 0.022 1
586 . 74 GLN CG C 34.307 0.082 1
587 . 74 GLN HG2 H 2.553 0.0030 1
588 . 74 GLN HG3 H 2.496 0.0050 1
589 . 75 MET H H 7.207 0.0010 1
590 . 75 MET N N 121.303 0.021 1
591 . 75 MET CA C 56.555 0.035 1
592 . 75 MET C C 175.9 0.019 1
593 . 75 MET CB C 33.724 0.193 1
594 . 76 ASN H H 8.979 0.0040 1
595 . 76 ASN N N 125.152 0.048 1
596 . 76 ASN CA C 54.04 0.056 1
597 . 76 ASN HA H 4.662 0.015 1
598 . 76 ASN C C 173.213 0.0 1
599 . 76 ASN CB C 39.935 0.0060 1
600 . 76 ASN HB2 H 3.115 0.0080 1
601 . 77 GLN CA C 60.829 0.07 1
602 . 77 GLN C C 176.898 0.0 1
603 . 77 GLN CB C 32.383 0.0 1
604 . 77 GLN HB2 H 1.974 0.0 1
605 . 77 GLN HB3 H 2.076 0.0 1
606 . 77 GLN HG2 H 2.308 0.0 1
607 . 77 GLN HG3 H 2.308 0.0 1
608 . 78 LYS H H 8.146 0.0020 1
609 . 78 LYS N N 121.246 0.046 1
610 . 78 LYS CA C 60.668 0.069 1
611 . 78 LYS HA H 3.794 0.0060 1
612 . 78 LYS C C 178.658 0.0 1
613 . 78 LYS CB C 32.296 0.149 1
614 . 78 LYS HB2 H 1.41 0.0090 1
615 . 78 LYS HB3 H 1.625 0.011 1
616 . 78 LYS CG C 25.301 0.081 1
617 . 78 LYS HG2 H 1.176 0.0030 1
618 . 78 LYS CD C 29.712 0.108 1
619 . 78 LYS HD2 H 1.506 0.0090 1
620 . 78 LYS CE C 42.582 0.037 1
621 . 78 LYS HE2 H 2.901 0.0050 1
622 . 79 ASP H H 7.941 0.0030 1
623 . 79 ASP N N 120.905 0.032 1
624 . 79 ASP CA C 57.422 0.024 1
625 . 79 ASP C C 178.979 0.0 1
626 . 79 ASP CB C 40.614 0.042 1
627 . 80 PHE H H 8.302 0.0070 1
628 . 80 PHE N N 122.903 0.012 1
629 . 80 PHE CA C 60.199 0.037 1
630 . 80 PHE HA H 4.485 0.01 1
631 . 80 PHE C C 178.233 0.0 1
632 . 80 PHE CB C 40.022 0.143 1
633 . 80 PHE HB2 H 3.205 0.0040 1
634 . 81 LEU H H 8.348 0.0050 1
635 . 81 LEU N N 119.514 0.018 1
636 . 81 LEU CA C 59.281 0.103 1
637 . 81 LEU HA H 4.01 0.012 1
638 . 81 LEU C C 178.467 0.0 1
639 . 81 LEU CB C 42.24 0.224 1
640 . 81 LEU HB2 H 2.114 0.017 1
641 . 81 LEU CD1 C 24.465 0.11 1
642 . 81 LEU HD1 H 1.027 0.0080 1
643 . 81 LEU HD2 H 0.9 0.0010 1
644 . 81 LEU HG H 1.556 0.0 1
645 . 82 SER H H 8.075 0.0030 1
646 . 82 SER N N 113.965 0.04 1
647 . 82 SER CA C 62.521 0.18 1
648 . 82 SER C C 176.845 0.0 1
649 . 83 LEU H H 7.89 0.0030 1
650 . 83 LEU N N 124.617 0.027 1
651 . 83 LEU CA C 58.846 0.102 1
652 . 83 LEU C C 178.252 0.0 1
653 . 83 LEU CB C 42.834 0.0 1
654 . 84 ILE H H 7.87 0.0020 1
655 . 84 ILE N N 119.332 0.016 1
656 . 84 ILE CA C 66.856 0.139 1
657 . 84 ILE HA H 3.624 0.0060 1
658 . 84 ILE C C 177.557 0.0 1
659 . 84 ILE CB C 38.972 0.191 1
660 . 84 ILE HB H 2.112 0.017 1
661 . 84 ILE CG2 C 18.487 0.0 1
662 . 84 ILE HG12 H 1.001 0.0040 1
663 . 84 ILE HG13 H 1.077 0.0080 1
664 . 84 ILE CD1 C 15.221 0.0090 1
665 . 84 ILE HD1 H 0.859 0.0070 1
666 . 85 VAL H H 7.841 0.0030 1
667 . 85 VAL N N 118.48 0.03 1
668 . 85 VAL CA C 68.33 0.078 1
669 . 85 VAL HA H 3.494 0.01 1
670 . 85 VAL C C 177.314 0.0 1
671 . 85 VAL CB C 32.23 0.198 1
672 . 85 VAL HB H 2.266 0.0060 1
673 . 85 VAL HG1 H 1.152 0.0030 1
674 . 85 VAL CG2 C 22.104 0.0 1
675 . 85 VAL HG2 H 1.04 0.015 1
676 . 86 SER H H 8.426 0.0030 1
677 . 86 SER N N 116.95 0.015 1
678 . 86 SER CA C 63.53 0.062 1
679 . 86 SER C C 176.71 0.0 1
680 . 87 ILE H H 8.37 0.0050 1
681 . 87 ILE N N 122.215 0.041 1
682 . 87 ILE CA C 66.984 0.176 1
683 . 87 ILE C C 179.024 0.0 1
684 . 87 ILE CB C 41.684 0.097 1
685 . 88 LEU H H 8.097 0.0080 1
686 . 88 LEU N N 120.312 0.033 1
687 . 88 LEU CA C 59.453 0.034 1
688 . 88 LEU HA H 4.156 0.015 1
689 . 88 LEU C C 179.822 0.0 1
690 . 88 LEU CB C 44.023 0.044 1
691 . 88 LEU HB2 H 1.397 0.0090 1
692 . 88 LEU HB3 H 2.174 0.0020 1
693 . 88 LEU HD1 H 0.972 0.0010 1
694 . 88 LEU HD2 H 0.84 0.0010 1
695 . 89 ARG H H 8.93 0.0060 1
696 . 89 ARG N N 118.996 0.017 1
697 . 89 ARG CA C 60.008 0.149 1
698 . 89 ARG HA H 3.877 0.016 1
699 . 89 ARG C C 179.728 0.0 1
700 . 89 ARG CB C 30.042 0.351 1
701 . 89 ARG HB2 H 1.819 0.012 1
702 . 89 ARG CG C 29.9 0.0 1
703 . 89 ARG HG2 H 1.492 0.011 1
704 . 89 ARG HG3 H 1.094 0.0040 1
705 . 89 ARG CD C 44.057 0.085 1
706 . 89 ARG HD2 H 3.082 0.011 1
707 . 90 SER H H 7.838 0.0020 1
708 . 90 SER N N 115.092 0.031 1
709 . 90 SER CA C 61.525 0.114 1
710 . 90 SER HA H 4.348 0.01 1
711 . 90 SER C C 175.723 0.0 1
712 . 90 SER CB C 63.933 0.056 1
713 . 90 SER HB2 H 4.033 0.0020 1
714 . 91 TRP H H 7.7 0.0040 1
715 . 91 TRP N N 122.566 0.042 1
716 . 91 TRP CA C 60.007 0.13 1
717 . 91 TRP HA H 4.612 0.0090 1
718 . 91 TRP C C 176.493 0.0 1
719 . 91 TRP CB C 30.519 0.108 1
720 . 91 TRP HB2 H 3.151 0.0090 1
721 . 91 TRP HB3 H 3.558 0.0080 1
722 . 92 ASN H H 7.249 0.0010 1
723 . 92 ASN N N 120.59 0.038 1
724 . 92 ASN CA C 58.401 0.081 1
725 . 92 ASN HA H 4.59 0.0070 1
726 . 92 ASN C C 177.225 0.0 1
727 . 92 ASN CB C 39.466 0.104 1
728 . 92 ASN HB2 H 2.968 0.0020 1
729 . 93 GLU H H 9.208 0.0040 1
730 . 93 GLU N N 120.386 0.028 1
731 . 93 GLU CA C 61.681 0.02 1
732 . 93 GLU C C 175.682 0.0 1
733 . 93 GLU CB C 27.977 0.0 1
734 . 94 PRO CA C 66.547 0.097 1
735 . 94 PRO C C 178.201 0.0 1
736 . 94 PRO CB C 29.583 0.0 1
737 . 95 LEU H H 7.74 0.0020 1
738 . 95 LEU N N 114.717 0.026 1
739 . 95 LEU CA C 58.905 0.103 1
740 . 95 LEU C C 178.178 0.0 1
741 . 95 LEU CB C 42.043 0.173 1
742 . 96 TYR H H 7.742 0.0040 1
743 . 96 TYR N N 120.997 0.019 1
744 . 96 TYR CA C 61.762 0.067 1
745 . 96 TYR HA H 4.295 0.0070 1
746 . 96 TYR C C 179.405 0.0 1
747 . 96 TYR CB C 38.358 0.039 1
748 . 96 TYR HB2 H 3.253 0.019 1
749 . 97 HIS H H 8.145 0.0030 1
750 . 97 HIS N N 120.525 0.029 1
751 . 97 HIS CA C 60.707 0.08 1
752 . 97 HIS HA H 4.243 0.0010 1
753 . 97 HIS C C 176.791 0.0 1
754 . 97 HIS CB C 31.321 0.041 1
755 . 97 HIS HB2 H 3.233 0.0090 1
756 . 97 HIS HB3 H 3.134 0.02 1
757 . 98 LEU H H 8.833 0.0030 1
758 . 98 LEU N N 123.094 0.089 1
759 . 98 LEU CA C 59.479 0.033 1
760 . 98 LEU C C 177.51 0.0 1
761 . 98 LEU CB C 42.608 0.0 1
762 . 99 VAL H H 7.68 0.0030 1
763 . 99 VAL N N 117.339 0.0070 1
764 . 99 VAL CA C 67.999 0.065 1
765 . 99 VAL HA H 3.274 0.0050 1
766 . 99 VAL C C 177.316 0.0 1
767 . 99 VAL CB C 32.571 0.08 1
768 . 99 VAL HB H 2.089 0.0070 1
769 . 99 VAL CG1 C 24.063 0.018 1
770 . 99 VAL HG1 H 1.034 0.01 1
771 . 99 VAL CG2 C 22.526 0.025 1
772 . 99 VAL HG2 H 0.894 0.0030 1
773 . 100 THR H H 7.555 0.0080 1
774 . 100 THR N N 114.507 0.046 1
775 . 100 THR CA C 67.547 0.066 1
776 . 100 THR HA H 3.649 0.0080 1
777 . 100 THR C C 177.702 0.0 1
778 . 100 THR CB C 69.322 0.19 1
779 . 100 THR HB H 4.15 0.011 1
780 . 100 THR HG2 H 1.142 0.0010 1
781 . 101 GLU H H 8.949 0.0030 1
782 . 101 GLU N N 122.095 0.012 1
783 . 101 GLU CA C 59.354 0.046 1
784 . 101 GLU HA H 4.056 0.0010 1
785 . 101 GLU C C 180.416 0.0 1
786 . 101 GLU CB C 30.484 0.048 1
787 . 101 GLU HB2 H 2.156 0.0040 1
788 . 101 GLU CG C 36.831 0.197 1
789 . 101 GLU HG2 H 2.406 0.0070 1
790 . 102 VAL H H 8.466 0.0040 1
791 . 102 VAL N N 121.276 0.022 1
792 . 102 VAL CA C 66.762 0.077 1
793 . 102 VAL HA H 3.934 0.0090 1
794 . 102 VAL C C 178.596 0.0 1
795 . 102 VAL CB C 31.452 0.256 1
796 . 102 VAL HB H 2.249 0.0020 1
797 . 102 VAL CG1 C 23.683 0.188 1
798 . 102 VAL HG1 H 1.131 0.0070 1
799 . 102 VAL CG2 C 23.017 0.034 1
800 . 102 VAL HG2 H 1.012 0.053 1
801 . 103 ARG H H 8.275 0.0020 1
802 . 103 ARG N N 120.061 0.088 1
803 . 103 ARG CA C 60.056 0.038 1
804 . 103 ARG HA H 3.977 0.0030 1
805 . 103 ARG C C 177.707 0.0 1
806 . 103 ARG CB C 31.005 0.239 1
807 . 103 ARG HB2 H 1.915 0.028 1
808 . 103 ARG HG2 H 1.84 0.0020 1
809 . 103 ARG CD C 44.2 0.0 1
810 . 103 ARG HD2 H 3.248 0.0070 1
811 . 104 GLY H H 7.364 0.0020 1
812 . 104 GLY N N 104.273 0.019 1
813 . 104 GLY CA C 45.573 0.064 1
814 . 104 GLY HA2 H 4.252 0.014 1
815 . 104 GLY HA3 H 3.832 0.0080 1
816 . 104 GLY C C 174.396 0.0 1
817 . 105 MET H H 7.463 0.0030 1
818 . 105 MET N N 122.592 0.056 1
819 . 105 MET CA C 56.929 0.021 1
820 . 105 MET HA H 4.392 0.0 1
821 . 105 MET C C 176.358 0.0 1
822 . 105 MET CB C 33.836 0.162 1
823 . 106 GLN H H 8.612 0.0030 1
824 . 106 GLN N N 124.6 0.018 1
825 . 106 GLN CA C 58.525 0.062 1
826 . 106 GLN HA H 4.179 0.0 1
827 . 106 GLN C C 176.805 0.0 1
828 . 106 GLN CB C 29.29 0.15 1
829 . 106 GLN HB2 H 2.164 0.0050 1
830 . 106 GLN CG C 34.665 0.035 1
831 . 106 GLN HG2 H 2.516 0.0020 1
832 . 107 GLU H H 8.66 0.0030 1
833 . 107 GLU N N 119.985 0.049 1
834 . 107 GLU CA C 56.496 0.082 1
835 . 107 GLU HA H 4.258 0.0060 1
836 . 107 GLU C C 175.607 0.0070 1
837 . 107 GLU CB C 29.213 0.081 1
838 . 107 GLU HB2 H 2.179 0.01 1
839 . 107 GLU CG C 37.099 0.0020 1
840 . 107 GLU HG2 H 2.288 0.0060 1
841 . 108 ALA H H 7.772 0.0020 1
842 . 108 ALA N N 125.481 0.022 1
843 . 108 ALA CA C 51.569 0.016 1
844 . 108 ALA HA H 4.518 0.013 1
845 . 108 ALA C C 176.308 0.0 1
846 . 108 ALA CB C 19.06 0.0 1
847 . 108 ALA HB H 1.454 0.0020 1
848 . 109 PRO CA C 56.481 0.041 1
849 . 109 PRO C C 176.207 0.0 1
850 . 109 PRO CB C 33.888 0.0 1
851 . 110 GLU H H 8.427 0.0060 1
852 . 110 GLU N N 123.885 0.06 1
853 . 110 GLU CA C 56.929 0.13 1
854 . 110 GLU HA H 4.369 0.014 1
855 . 110 GLU C C 175.552 0.0 1
856 . 110 GLU CB C 29.9 0.0 1
857 . 110 GLU HB2 H 2.122 0.0080 1
858 . 110 GLU CG C 36.861 0.039 1
859 . 110 GLU HG2 H 2.317 0.0070 1
860 . 111 ALA H H 8.092 0.0030 1
861 . 111 ALA N N 125.292 0.033 1
862 . 111 ALA CA C 55.332 0.095 1
863 . 111 ALA HA H 4.285 0.023 1
864 . 111 ALA C C 179.729 0.0 1
865 . 111 ALA CB C 19.315 0.015 1
866 . 111 ALA HB H 1.452 0.0030 1
867 . 112 ILE H H 7.201 0.0020 1
868 . 112 ILE N N 115.256 0.045 1
869 . 112 ILE CA C 64.66 0.058 1
870 . 112 ILE HA H 3.935 0.0070 1
871 . 112 ILE C C 176.461 0.0 1
872 . 112 ILE CB C 38.439 0.049 1
873 . 112 ILE HB H 2.065 0.0050 1
874 . 112 ILE CG2 C 17.458 0.117 1
875 . 112 ILE HG13 H 1.081 0.01 1
876 . 112 ILE CD1 C 13.6 0.213 1
877 . 112 ILE HD1 H 1.082 0.011 1
878 . 113 LEU H H 7.831 0.0040 1
879 . 113 LEU N N 121.303 0.054 1
880 . 113 LEU CA C 59.108 0.067 1
881 . 113 LEU HA H 4.057 0.0 1
882 . 113 LEU C C 177.603 0.0 1
883 . 113 LEU CB C 42.116 0.202 1
884 . 113 LEU HB2 H 1.926 0.0020 1
885 . 113 LEU HD1 H 0.991 0.0 1
886 . 114 SER H H 8.462 0.0050 1
887 . 114 SER N N 112.097 0.023 1
888 . 114 SER CA C 62.167 0.048 1
889 . 114 SER HA H 4.163 0.0060 1
890 . 114 SER C C 178.041 0.0 1
891 . 114 SER CB C 63.2 0.265 1
892 . 114 SER HB2 H 4.021 0.0080 1
893 . 115 LYS H H 7.154 0.0040 1
894 . 115 LYS N N 121.925 0.052 1
895 . 115 LYS CA C 60.077 0.047 1
896 . 115 LYS C C 176.941 0.0 1
897 . 115 LYS CB C 33.55 0.072 1
898 . 116 ALA H H 8.296 0.0080 1
899 . 116 ALA N N 124.335 0.039 1
900 . 116 ALA CA C 56.442 0.056 1
901 . 116 ALA HA H 3.874 0.0060 1
902 . 116 ALA C C 178.75 0.0 1
903 . 116 ALA CB C 18.349 0.363 1
904 . 116 ALA HB H 1.524 0.0040 1
905 . 117 VAL H H 8.281 0.0040 1
906 . 117 VAL N N 118.087 0.028 1
907 . 117 VAL CA C 66.603 0.094 1
908 . 117 VAL HA H 3.746 0.0050 1
909 . 117 VAL C C 179.046 0.0 1
910 . 117 VAL CB C 33.108 0.03 1
911 . 117 VAL HB H 2.198 0.0050 1
912 . 117 VAL CG1 C 21.501 0.143 1
913 . 117 VAL HG1 H 1.061 0.0040 1
914 . 117 VAL CG2 C 23.865 0.092 1
915 . 117 VAL HG2 H 1.175 0.0040 1
916 . 118 GLU H H 7.472 0.0020 1
917 . 118 GLU N N 121.525 0.027 1
918 . 118 GLU CA C 59.664 0.074 1
919 . 118 GLU HA H 4.455 0.015 1
920 . 118 GLU C C 178.879 0.0 1
921 . 118 GLU CB C 30.716 0.032 1
922 . 118 GLU HB2 H 2.149 0.012 1
923 . 118 GLU HB3 H 2.248 0.013 1
924 . 118 GLU CG C 36.6 0.0 1
925 . 118 GLU HG2 H 2.403 0.012 1
926 . 119 ILE H H 8.944 0.0040 1
927 . 119 ILE N N 121.369 0.098 1
928 . 119 ILE CA C 67.122 0.084 1
929 . 119 ILE HA H 3.497 0.01 1
930 . 119 ILE C C 178.711 0.0 1
931 . 119 ILE CB C 38.428 0.096 1
932 . 119 ILE HB H 1.821 0.013 1
933 . 119 ILE CG2 C 18.771 0.101 1
934 . 119 ILE HG13 H 0.908 0.0020 1
935 . 119 ILE CD1 C 14.916 0.044 1
936 . 119 ILE HD1 H 0.709 0.0030 1
937 . 120 GLU H H 8.439 0.0060 1
938 . 120 GLU N N 125.252 0.028 1
939 . 120 GLU CA C 61.503 0.032 1
940 . 120 GLU HA H 3.933 0.0090 1
941 . 120 GLU C C 177.981 0.0 1
942 . 120 GLU CB C 29.794 0.073 1
943 . 120 GLU HB2 H 2.243 0.0030 1
944 . 120 GLU CG C 35.732 0.074 1
945 . 120 GLU HG2 H 2.405 0.0060 1
946 . 121 GLU H H 7.675 0.0030 1
947 . 121 GLU N N 119.01 0.025 1
948 . 121 GLU CA C 59.814 0.062 1
949 . 121 GLU HA H 4.169 0.013 1
950 . 121 GLU C C 179.584 0.0010 1
951 . 121 GLU CB C 30.133 0.08 1
952 . 121 GLU HB2 H 2.163 0.0060 1
953 . 121 GLU CG C 36.142 0.042 1
954 . 121 GLU HG2 H 2.407 0.017 1
955 . 122 GLN H H 9.011 0.0020 1
956 . 122 GLN N N 117.308 0.017 1
957 . 122 GLN CA C 58.514 0.026 1
958 . 122 GLN C C 179.105 0.0 1
959 . 122 GLN CB C 30.514 0.0 1
960 . 123 THR H H 8.493 0.0060 1
961 . 123 THR N N 117.583 0.071 1
962 . 123 THR CA C 68.656 0.136 1
963 . 123 THR HA H 4.509 0.012 1
964 . 123 THR C C 176.819 0.0 1
965 . 123 THR CB C 62.639 0.273 1
966 . 123 THR HB H 4.037 0.0070 1
967 . 123 THR CG2 C 22.399 0.026 1
968 . 123 THR HG2 H 0.677 0.0040 1
969 . 124 LYS H H 7.144 0.0030 1
970 . 124 LYS N N 122.29 0.017 1
971 . 124 LYS CA C 61.013 0.065 1
972 . 124 LYS HA H 3.961 0.0060 1
973 . 124 LYS C C 179.774 0.0 1
974 . 124 LYS CB C 32.72 0.02 1
975 . 124 LYS HB2 H 1.925 0.0090 1
976 . 124 LYS CD C 27.6 0.0 1
977 . 124 LYS HD2 H 1.702 0.0090 1
978 . 124 LYS CE C 43.477 0.0 1
979 . 124 LYS HE2 H 3.253 0.013 1
980 . 125 ARG H H 7.644 0.0030 1
981 . 125 ARG N N 120.087 0.02 1
982 . 125 ARG CA C 59.283 0.184 1
983 . 125 ARG HA H 4.255 0.0020 1
984 . 125 ARG C C 179.875 0.0 1
985 . 125 ARG CB C 30.79 0.095 1
986 . 125 ARG HB2 H 1.935 0.0 1
987 . 125 ARG CG C 27.624 0.0 1
988 . 125 ARG HG2 H 1.45 0.0 1
989 . 125 ARG CD C 44.039 0.0 1
990 . 125 ARG HD2 H 3.262 0.0030 1
991 . 126 LEU H H 8.796 0.0050 1
992 . 126 LEU N N 124.479 0.054 1
993 . 126 LEU CA C 58.312 0.04 1
994 . 126 LEU C C 178.24 0.0 1
995 . 126 LEU CB C 41.115 0.156 1
996 . 127 LEU H H 8.468 0.0040 1
997 . 127 LEU N N 122.273 0.026 1
998 . 127 LEU CA C 59.359 0.107 1
999 . 127 LEU C C 177.861 0.0 1
1000 . 127 LEU CB C 41.561 0.107 1
1001 . 128 GLU H H 7.932 0.0090 1
1002 . 128 GLU N N 119.552 0.14 1
1003 . 128 GLU CA C 60.055 0.073 1
1004 . 128 GLU HA H 4.174 0.0090 1
1005 . 128 GLU C C 180.083 0.0 1
1006 . 128 GLU CB C 30.401 0.013 1
1007 . 128 GLU HB2 H 2.266 0.012 1
1008 . 128 GLU CG C 36.93 0.029 1
1009 . 128 GLU HG2 H 2.518 0.0050 1
1010 . 129 GLY H H 7.976 0.0040 1
1011 . 129 GLY N N 107.798 0.024 1
1012 . 129 GLY CA C 47.765 0.127 1
1013 . 129 GLY HA2 H 3.883 0.0040 1
1014 . 129 GLY C C 176.051 0.0 1
1015 . 130 MET H H 8.753 0.0050 1
1016 . 130 MET N N 120.983 0.015 1
1017 . 130 MET CA C 56.1 0.067 1
1018 . 130 MET C C 179.136 0.0 1
1019 . 130 MET CB C 29.793 0.016 1
1020 . 131 GLU H H 8.673 0.0040 1
1021 . 131 GLU N N 121.032 0.027 1
1022 . 131 GLU CA C 60.702 0.085 1
1023 . 131 GLU HA H 4.037 0.017 1
1024 . 131 GLU C C 180.165 0.0 1
1025 . 131 GLU CB C 29.879 0.115 1
1026 . 131 GLU HB2 H 2.287 0.032 1
1027 . 131 GLU HB3 H 2.045 0.0090 1
1028 . 131 GLU CG C 37.772 0.139 1
1029 . 131 GLU HG2 H 2.648 0.0090 1
1030 . 131 GLU HG3 H 2.175 0.0060 1
1031 . 132 LEU H H 7.598 0.0040 1
1032 . 132 LEU N N 121.986 0.045 1
1033 . 132 LEU CA C 58.482 0.087 1
1034 . 132 LEU HA H 3.313 0.0080 1
1035 . 132 LEU C C 180.014 0.0 1
1036 . 132 LEU CB C 41.587 0.496 1
1037 . 132 LEU HB2 H 1.006 0.0050 1
1038 . 132 LEU HB3 H 1.712 0.0060 1
1039 . 132 LEU CG C 27.011 0.166 1
1040 . 132 LEU CD1 C 19.983 0.014 1
1041 . 132 LEU HD1 H -0.291 0.0030 1
1042 . 132 LEU CD2 C 26.458 0.064 1
1043 . 132 LEU HD2 H 0.646 0.0030 1
1044 . 132 LEU HG H 1.131 0.0060 1
1045 . 133 ILE H H 7.865 0.0080 1
1046 . 133 ILE N N 122.087 0.078 1
1047 . 133 ILE CA C 67.324 0.076 1
1048 . 133 ILE HA H 3.397 0.012 1
1049 . 133 ILE C C 178.137 0.0 1
1050 . 133 ILE CB C 38.733 0.143 1
1051 . 133 ILE HB H 2.017 0.011 1
1052 . 133 ILE CG2 C 18.362 0.34 1
1053 . 133 ILE HG2 H 0.454 0.0070 1
1054 . 133 ILE CG1 C 31.616 0.051 1
1055 . 133 ILE HG12 H 1.811 0.0070 1
1056 . 133 ILE HG13 H 0.711 0.0080 1
1057 . 133 ILE CD1 C 12.182 0.078 1
1058 . 133 ILE HD1 H 0.093 0.0060 1
1059 . 134 VAL H H 8.703 0.0020 1
1060 . 134 VAL N N 120.681 0.021 1
1061 . 134 VAL CA C 68.41 0.085 1
1062 . 134 VAL HA H 3.48 0.018 1
1063 . 134 VAL C C 177.658 0.0 1
1064 . 134 VAL CB C 32.144 0.079 1
1065 . 134 VAL HB H 2.241 0.012 1
1066 . 134 VAL CG1 C 24.409 0.0 1
1067 . 134 VAL HG1 H 1.145 0.011 1
1068 . 134 VAL CG2 C 22.2 0.0 1
1069 . 134 VAL HG2 H 1.054 0.0070 1
1070 . 135 SER H H 7.788 0.0040 1
1071 . 135 SER N N 113.688 0.032 1
1072 . 135 SER CA C 62.06 0.064 1
1073 . 135 SER HA H 4.206 0.0 1
1074 . 135 SER C C 174.943 0.0 1
1075 . 135 SER CB C 63.578 0.137 1
1076 . 135 SER HB2 H 4.089 0.0010 1
1077 . 136 GLN H H 7.42 0.0030 1
1078 . 136 GLN N N 118.181 0.03 1
1079 . 136 GLN CA C 57.983 0.075 1
1080 . 136 GLN HA H 4.346 0.0070 1
1081 . 136 GLN C C 177.353 0.0 1
1082 . 136 GLN CB C 30.238 0.056 1
1083 . 136 GLN HB2 H 2.158 0.0080 1
1084 . 136 GLN CG C 34.4 0.0 1
1085 . 136 GLN HG2 H 2.416 0.0060 1
1086 . 137 VAL H H 7.98 0.0040 1
1087 . 137 VAL N N 117.211 0.035 1
1088 . 137 VAL CA C 64.526 0.059 1
1089 . 137 VAL HA H 4.088 0.014 1
1090 . 137 VAL C C 175.549 0.022 1
1091 . 137 VAL CB C 34.027 0.082 1
1092 . 137 VAL HB H 1.898 0.013 1
1093 . 137 VAL CG1 C 22.83 0.071 1
1094 . 137 VAL HG1 H 1.049 0.012 1
1095 . 137 VAL CG2 C 22.585 0.086 1
1096 . 137 VAL HG2 H 0.832 0.0090 1
1097 . 138 HIS H H 8.577 0.0060 1
1098 . 138 HIS N N 118.963 0.033 1
1099 . 138 HIS CA C 54.563 0.047 1
1100 . 138 HIS HA H 5.205 0.018 1
1101 . 138 HIS C C 172.261 0.0 1
1102 . 138 HIS CB C 31.044 0.064 1
1103 . 138 HIS HB2 H 3.212 0.016 1
1104 . 138 HIS HB3 H 2.943 0.0060 1
1105 . 139 PRO CA C 65.077 0.06 1
1106 . 139 PRO HA H 4.486 0.015 1
1107 . 139 PRO C C 177.457 0.0 1
1108 . 139 PRO CB C 32.488 0.087 1
1109 . 139 PRO HB2 H 2.533 0.015 1
1110 . 139 PRO CG C 27.766 0.168 1
1111 . 139 PRO HG2 H 2.063 0.017 1
1112 . 139 PRO CD C 50.952 0.021 1
1113 . 139 PRO HD2 H 3.349 0.0020 1
1114 . 139 PRO HD3 H 3.709 0.012 1
1115 . 140 GLU H H 9.137 0.0040 1
1116 . 140 GLU N N 120.455 0.037 1
1117 . 140 GLU CA C 57.638 0.064 1
1118 . 140 GLU HA H 4.368 0.0050 1
1119 . 140 GLU C C 176.657 0.0 1
1120 . 140 GLU CB C 29.506 0.032 1
1121 . 140 GLU HB2 H 2.066 0.0060 1
1122 . 140 GLU HB3 H 2.164 0.0060 1
1123 . 140 GLU CG C 36.3 0.0 1
1124 . 140 GLU HG2 H 2.434 0.01 1
1125 . 140 GLU HG3 H 2.392 0.0080 1
1126 . 141 THR H H 7.922 0.0020 1
1127 . 141 THR N N 118.229 0.048 1
1128 . 141 THR CA C 63.717 0.102 1
1129 . 141 THR HA H 4.216 0.0070 1
1130 . 141 THR C C 174.368 0.0 1
1131 . 141 THR CB C 70.131 0.108 1
1132 . 141 THR HB H 4.156 0.013 1
1133 . 141 THR CG2 C 22.242 0.0 1
1134 . 141 THR HG2 H 1.254 0.0090 1
1135 . 142 LYS H H 8.307 0.0040 1
1136 . 142 LYS N N 126.442 0.067 1
1137 . 142 LYS CA C 56.512 0.122 1
1138 . 142 LYS HA H 4.435 0.014 1
1139 . 142 LYS C C 176.41 0.0 1
1140 . 142 LYS CB C 33.636 0.082 1
1141 . 142 LYS HB2 H 1.913 0.01 1
1142 . 142 LYS HB3 H 1.815 0.011 1
1143 . 142 LYS CG C 25.056 0.058 1
1144 . 142 LYS HG2 H 1.498 0.013 1
1145 . 142 LYS CD C 29.3 0.0 1
1146 . 142 LYS HD2 H 1.729 0.016 1
1147 . 142 LYS CE C 42.469 0.098 1
1148 . 142 LYS HE2 H 3.047 0.01 1
1149 . 143 GLU H H 8.387 0.0060 1
1150 . 143 GLU N N 122.59 0.024 1
1151 . 143 GLU CA C 57.282 0.074 1
1152 . 143 GLU HA H 4.321 0.0040 1
1153 . 143 GLU C C 176.201 0.0 1
1154 . 143 GLU CB C 30.808 0.033 1
1155 . 143 GLU HB2 H 2.095 0.042 1
1156 . 143 GLU HB3 H 1.994 0.0040 1
1157 . 143 GLU CG C 36.784 0.036 1
1158 . 143 GLU HG2 H 2.313 0.015 1
1159 . 144 ASN H H 8.369 0.0040 1
1160 . 144 ASN N N 120.505 0.025 1
1161 . 144 ASN CA C 53.772 0.082 1
1162 . 144 ASN HA H 4.739 0.015 1
1163 . 144 ASN C C 175.021 0.0 1
1164 . 144 ASN CB C 39.292 0.113 1
1165 . 144 ASN HB2 H 2.87 0.0080 1
1166 . 144 ASN HB3 H 2.807 0.011 1
1167 . 145 GLU H H 8.332 0.0030 1
1168 . 145 GLU N N 122.918 0.019 1
1169 . 145 GLU CA C 57.249 0.164 1
1170 . 145 GLU HA H 4.382 0.011 1
1171 . 145 GLU C C 176.191 0.0 1
1172 . 145 GLU CB C 31.077 0.169 1
1173 . 145 GLU HB2 H 2.128 0.014 1
1174 . 145 GLU HB3 H 1.957 0.018 1
1175 . 145 GLU CG C 36.8 0.0 1
1176 . 145 GLU HG2 H 2.376 0.0040 1
1177 . 145 GLU HG3 H 2.275 0.0050 1
1178 . 146 ILE H H 8.021 0.0030 1
1179 . 146 ILE N N 122.692 0.023 1
1180 . 146 ILE CA C 61.433 0.08 1
1181 . 146 ILE HA H 4.161 0.016 1
1182 . 146 ILE C C 174.933 0.0050 1
1183 . 146 ILE CB C 39.298 0.079 1
1184 . 146 ILE HB H 1.845 0.011 1
1185 . 146 ILE CG2 C 17.981 0.04 1
1186 . 146 ILE HG2 H 1.176 0.01 1
1187 . 146 ILE CG1 C 27.561 0.051 1
1188 . 146 ILE HG12 H 1.441 0.011 1
1189 . 146 ILE HG13 H 0.847 0.0060 1
1190 . 146 ILE CD1 C 13.208 0.05 1
1191 . 146 ILE HD1 H 0.846 0.0070 1
1192 . 147 TYR H H 7.379 0.0040 1
1193 . 147 TYR N N 123.706 0.03 1
1194 . 147 TYR CA C 55.243 0.0010 1
1195 . 147 TYR HA H 4.997 0.025 1
1196 . 147 TYR C C 172.838 0.0 1
1197 . 147 TYR CB C 38.627 0.12 1
1198 . 147 TYR HB2 H 3.147 0.014 1
1199 . 148 PRO CA C 62.963 0.107 1
1200 . 148 PRO HA H 4.615 0.0090 1
1201 . 148 PRO C C 177.675 0.0 1
1202 . 148 PRO CB C 31.91 0.101 1
1203 . 148 PRO HB2 H 2.406 0.0090 1
1204 . 148 PRO HB3 H 2.046 0.0060 1
1205 . 148 PRO CG C 28.497 0.055 1
1206 . 148 PRO HG2 H 2.171 0.0070 1
1207 . 148 PRO CD C 51.196 0.092 1
1208 . 148 PRO HD2 H 4.072 0.0090 1
1209 . 148 PRO HD3 H 3.642 0.01 1
1210 . 149 VAL H H 8.875 0.0040 1
1211 . 149 VAL N N 129.582 0.045 1
1212 . 149 VAL CA C 60.499 0.044 1
1213 . 149 VAL HA H 4.383 0.0 1
1214 . 149 VAL C C 178.047 0.0 1
1215 . 149 VAL CB C 30.014 0.0 1
1216 . 151 SER C C 177.37 0.0 1
1217 . 152 GLY H H 7.886 0.0050 1
1218 . 152 GLY N N 116.451 0.049 1
1219 . 152 GLY CA C 46.597 0.047 1
1220 . 152 GLY C C 174.651 0.0 1
1221 . 153 LEU H H 7.651 0.0050 1
1222 . 153 LEU N N 119.109 0.078 1
1223 . 153 LEU CA C 57.867 0.049 1
1224 . 153 LEU C C 175.985 0.0 1
1225 . 153 LEU CB C 39.01 0.0 1
1226 . 156 LEU CA C 56.983 0.0080 1
1227 . 156 LEU C C 177.897 0.0 1
1228 . 157 GLN H H 7.238 0.015 1
1229 . 157 GLN N N 115.104 0.0060 1
1230 . 157 GLN CA C 55.704 0.064 1
1231 . 157 GLN HA H 4.334 0.0010 1
1232 . 157 GLN C C 176.019 0.0 1
1233 . 157 GLN HB2 H 2.255 0.0 1
1234 . 157 GLN HB3 H 2.218 0.0 1
1235 . 157 GLN HG2 H 2.411 0.0 1
1236 . 158 MET H H 6.96 0.0070 1
1237 . 158 MET N N 120.517 0.053 1
1238 . 158 MET CA C 56.649 0.093 1
1239 . 158 MET HA H 4.346 0.017 1
1240 . 158 MET C C 175.688 0.0 1
1241 . 158 MET CB C 33.868 0.086 1
1242 . 158 MET HB2 H 2.188 0.01 1
1243 . 158 MET HB3 H 2.042 0.013 1
1244 . 158 MET CG C 32.9 0.0 1
1245 . 158 MET HG2 H 2.851 0.01 1
1246 . 158 MET HG3 H 2.788 0.012 1
1247 . 159 ALA H H 8.294 0.0060 1
1248 . 159 ALA N N 124.553 0.077 1
1249 . 159 ALA CA C 54.409 0.081 1
1250 . 159 ALA HA H 4.209 0.013 1
1251 . 159 ALA C C 178.393 0.0 1
1252 . 159 ALA CB C 19.534 0.166 1
1253 . 159 ALA HB H 1.515 0.0050 1
1254 . 160 ASP H H 7.826 0.0020 1
1255 . 160 ASP N N 118.458 0.022 1
1256 . 160 ASP CA C 54.487 0.087 1
1257 . 160 ASP HA H 4.658 0.0060 1
1258 . 160 ASP C C 175.649 0.0 1
1259 . 160 ASP CB C 42.836 0.09 1
1260 . 160 ASP HB2 H 2.853 0.01 1
1261 . 160 ASP HB3 H 2.686 0.0080 1
1262 . 161 GLU H H 8.751 0.0080 1
1263 . 161 GLU N N 128.136 0.012 1
1264 . 161 GLU CA C 61.105 0.06 1
1265 . 161 GLU C C 177.685 0.0 1
1266 . 161 GLU CB C 32.529 1.493 1
1267 . 162 GLU H H 8.569 0.0040 1
1268 . 162 GLU N N 119.219 0.023 1
1269 . 162 GLU CA C 60.849 0.131 1
1270 . 162 GLU HA H 3.824 0.011 1
1271 . 162 GLU C C 179.513 0.012 1
1272 . 162 GLU CB C 29.784 0.075 1
1273 . 162 GLU HB2 H 1.954 0.011 1
1274 . 162 GLU CG C 37.0 0.0 1
1275 . 162 GLU HG2 H 2.11 0.01 1
1276 . 162 GLU HG3 H 2.265 0.013 1
1277 . 163 SER H H 8.015 0.0040 1
1278 . 163 SER N N 117.133 0.072 1
1279 . 163 SER CA C 62.618 0.192 1
1280 . 163 SER HA H 4.245 0.0040 1
1281 . 163 SER C C 176.982 0.0 1
1282 . 163 SER CB C 62.318 1.792 1
1283 . 163 SER HB2 H 4.068 0.0070 1
1284 . 164 ARG H H 8.332 0.0030 1
1285 . 164 ARG N N 125.556 0.012 1
1286 . 164 ARG CA C 60.409 0.082 1
1287 . 164 ARG HA H 4.328 0.0030 1
1288 . 164 ARG C C 178.528 0.0 1
1289 . 164 ARG CB C 31.267 0.044 1
1290 . 164 ARG HB2 H 2.126 0.0070 1
1291 . 164 ARG HB3 H 1.96 0.0090 1
1292 . 164 ARG CG C 28.862 0.059 1
1293 . 164 ARG HG2 H 1.608 0.0030 1
1294 . 164 ARG CD C 44.342 0.075 1
1295 . 164 ARG HD2 H 3.541 0.026 1
1296 . 164 ARG HD3 H 3.49 0.01 1
1297 . 165 LEU H H 8.817 0.0070 1
1298 . 165 LEU N N 118.904 0.0090 1
1299 . 165 LEU CA C 59.08 0.082 1
1300 . 165 LEU HA H 4.348 0.034 1
1301 . 165 LEU C C 179.926 0.0 1
1302 . 165 LEU CB C 42.182 0.125 1
1303 . 165 LEU HB2 H 2.161 0.0090 1
1304 . 165 LEU HB3 H 1.47 0.0050 1
1305 . 165 LEU CG C 27.556 0.069 1
1306 . 165 LEU CD1 C 26.59 0.178 1
1307 . 165 LEU HD1 H 1.024 0.014 1
1308 . 165 LEU CD2 C 22.764 0.065 1
1309 . 165 LEU HD2 H 0.755 0.016 1
1310 . 165 LEU HG H 2.048 0.018 1
1311 . 166 SER H H 7.998 0.0060 1
1312 . 166 SER N N 115.023 0.099 1
1313 . 166 SER CA C 62.45 0.102 1
1314 . 166 SER HA H 4.156 0.012 1
1315 . 166 SER C C 176.226 0.0 1
1316 . 166 SER CB C 63.489 0.049 1
1317 . 166 SER HB2 H 4.038 0.0020 1
1318 . 167 ALA H H 7.845 0.0040 1
1319 . 167 ALA N N 126.235 0.016 1
1320 . 167 ALA CA C 55.957 0.083 1
1321 . 167 ALA HA H 4.371 0.011 1
1322 . 167 ALA C C 181.847 0.0 1
1323 . 167 ALA CB C 19.04 0.118 1
1324 . 167 ALA HB H 1.601 0.0090 1
1325 . 168 TYR H H 8.468 0.0030 1
1326 . 168 TYR N N 120.995 0.015 1
1327 . 168 TYR CA C 63.669 0.084 1
1328 . 168 TYR HA H 3.933 0.012 1
1329 . 168 TYR C C 177.225 0.0 1
1330 . 168 TYR CB C 40.477 0.093 1
1331 . 168 TYR HB2 H 3.115 0.014 1
1332 . 168 TYR HB3 H 2.343 0.014 1
1333 . 169 TYR H H 8.718 0.0050 1
1334 . 169 TYR N N 121.218 0.048 1
1335 . 169 TYR CA C 63.299 0.109 1
1336 . 169 TYR HA H 3.819 0.0050 1
1337 . 169 TYR C C 177.312 0.0 1
1338 . 169 TYR CB C 39.672 0.138 1
1339 . 169 TYR HB2 H 3.511 0.013 1
1340 . 169 TYR HB3 H 3.304 0.0050 1
1341 . 170 ASN H H 8.489 0.0050 1
1342 . 170 ASN N N 117.092 0.024 1
1343 . 170 ASN CA C 57.539 0.114 1
1344 . 170 ASN HA H 4.583 0.0080 1
1345 . 170 ASN C C 177.299 0.0 1
1346 . 170 ASN CB C 39.729 0.079 1
1347 . 170 ASN HB2 H 3.105 0.0070 1
1348 . 170 ASN HB3 H 2.918 0.0070 1
1349 . 171 LEU H H 8.039 0.0040 1
1350 . 171 LEU N N 122.801 0.0020 1
1351 . 171 LEU CA C 59.685 0.02 1
1352 . 171 LEU HA H 4.402 0.0070 1
1353 . 171 LEU C C 178.853 0.0 1
1354 . 171 LEU CB C 43.347 0.058 1
1355 . 171 LEU HB2 H 1.901 0.0080 1
1356 . 171 LEU CG C 28.125 0.0 1
1357 . 171 LEU CD1 C 26.8 0.0 1
1358 . 171 LEU HD1 H 0.935 0.011 1
1359 . 171 LEU CD2 C 26.358 0.0 1
1360 . 171 LEU HD2 H 1.024 0.015 1
1361 . 171 LEU HG H 1.872 0.0 1
1362 . 172 LEU H H 8.51 0.01 1
1363 . 172 LEU N N 118.945 0.05 1
1364 . 172 LEU CA C 58.454 0.02 1
1365 . 172 LEU HA H 4.123 0.0020 1
1366 . 172 LEU C C 180.046 0.0 1
1367 . 172 LEU CB C 42.046 0.099 1
1368 . 172 LEU HB2 H 1.809 0.0090 1
1369 . 172 LEU HB3 H 1.589 0.0090 1
1370 . 172 LEU CG C 27.164 0.078 1
1371 . 172 LEU CD1 C 21.793 0.03 1
1372 . 172 LEU HD1 H 0.328 0.0060 1
1373 . 172 LEU CD2 C 24.94 0.068 1
1374 . 172 LEU HD2 H 0.801 0.012 1
1375 . 172 LEU HG H 1.761 0.016 1
1376 . 173 HIS H H 8.943 0.0060 1
1377 . 173 HIS N N 124.309 0.016 1
1378 . 173 HIS CA C 61.085 0.08 1
1379 . 173 HIS HA H 3.568 0.011 1
1380 . 173 HIS C C 178.639 0.0 1
1381 . 173 HIS CB C 30.954 0.076 1
1382 . 173 HIS HB2 H 3.353 0.03 1
1383 . 173 HIS HB3 H 2.945 0.017 1
1384 . 174 CYS H H 8.599 0.0020 1
1385 . 174 CYS N N 120.977 0.025 1
1386 . 174 CYS CA C 59.842 0.098 1
1387 . 174 CYS HA H 4.311 0.0050 1
1388 . 174 CYS C C 175.883 0.0 1
1389 . 174 CYS CB C 39.814 0.17 1
1390 . 174 CYS HB2 H 3.725 0.015 1
1391 . 174 CYS HB3 H 3.476 0.0080 1
1392 . 175 LEU H H 8.634 0.01 1
1393 . 175 LEU N N 124.88 0.011 1
1394 . 175 LEU CA C 58.411 0.016 1
1395 . 175 LEU C C 179.119 0.0 1
1396 . 175 LEU CB C 40.852 0.06 1
1397 . 176 ARG H H 7.834 0.0050 1
1398 . 176 ARG N N 123.217 0.026 1
1399 . 176 ARG CA C 60.315 0.028 1
1400 . 176 ARG C C 177.548 0.0 1
1401 . 177 ARG H H 7.805 0.0090 1
1402 . 177 ARG N N 120.484 0.037 1
1403 . 177 ARG CA C 59.674 0.065 1
1404 . 177 ARG HA H 4.025 0.0010 1
1405 . 177 ARG C C 179.601 0.0 1
1406 . 177 ARG CB C 30.962 0.013 1
1407 . 177 ARG HB2 H 1.838 0.0 1
1408 . 177 ARG CG C 27.235 0.022 1
1409 . 177 ARG HG2 H 1.455 0.0090 1
1410 . 177 ARG CD C 44.0 0.0 1
1411 . 177 ARG HD2 H 3.325 0.01 1
1412 . 178 ASP H H 8.95 0.0060 1
1413 . 178 ASP N N 122.86 0.073 1
1414 . 178 ASP CA C 58.145 0.093 1
1415 . 178 ASP HA H 4.57 0.011 1
1416 . 178 ASP C C 178.592 0.0 1
1417 . 178 ASP CB C 39.319 0.088 1
1418 . 178 ASP HB2 H 2.96 0.0060 1
1419 . 179 SER H H 8.59 0.0040 1
1420 . 179 SER N N 116.899 0.0010 1
1421 . 179 SER CA C 62.837 0.144 1
1422 . 179 SER HA H 3.977 0.013 1
1423 . 179 SER C C 177.408 0.0 1
1424 . 179 SER CB C 62.7 0.0 1
1425 . 179 SER HB2 H 3.697 0.0060 1
1426 . 180 HIS H H 7.7 0.0040 1
1427 . 180 HIS N N 126.442 0.0090 1
1428 . 180 HIS CA C 59.56 0.075 1
1429 . 180 HIS HA H 3.517 0.015 1
1430 . 180 HIS C C 176.87 0.0 1
1431 . 180 HIS CB C 30.663 0.09 1
1432 . 180 HIS HB2 H 2.959 0.0040 1
1433 . 180 HIS HB3 H 3.318 0.016 1
1434 . 181 LYS H H 7.658 0.0060 1
1435 . 181 LYS N N 119.729 0.016 1
1436 . 181 LYS CA C 60.411 0.079 1
1437 . 181 LYS HA H 3.47 0.014 1
1438 . 181 LYS C C 177.039 0.0 1
1439 . 181 LYS CB C 32.577 0.136 1
1440 . 181 LYS HB2 H 1.448 0.0090 1
1441 . 181 LYS HB3 H 1.905 0.0090 1
1442 . 181 LYS CG C 25.91 0.067 1
1443 . 181 LYS HG2 H 1.305 0.013 1
1444 . 181 LYS HG3 H 1.582 0.0080 1
1445 . 181 LYS HD2 H 1.495 0.0 1
1446 . 181 LYS HE2 H 2.977 0.0020 1
1447 . 182 ILE H H 8.034 0.0040 1
1448 . 182 ILE N N 116.555 0.057 1
1449 . 182 ILE CA C 65.879 0.158 1
1450 . 182 ILE HA H 3.438 0.015 1
1451 . 182 ILE C C 176.783 0.0 1
1452 . 182 ILE CB C 37.708 0.322 1
1453 . 182 ILE HB H 1.923 0.02 1
1454 . 182 ILE CG2 C 18.564 0.103 1
1455 . 182 ILE CG1 C 28.655 0.0 1
1456 . 182 ILE HG12 H 1.79 0.0050 1
1457 . 182 ILE HG13 H 0.995 0.0070 1
1458 . 182 ILE HD1 H 0.894 0.0020 1
1459 . 183 ASP H H 7.292 0.0060 1
1460 . 183 ASP N N 119.482 0.03 1
1461 . 183 ASP CA C 58.115 0.085 1
1462 . 183 ASP HA H 4.46 0.0060 1
1463 . 183 ASP C C 177.502 0.0 1
1464 . 183 ASP CB C 42.855 0.126 1
1465 . 183 ASP HB2 H 2.636 0.0090 1
1466 . 183 ASP HB3 H 2.697 0.0070 1
1467 . 184 ASN H H 7.798 0.0060 1
1468 . 184 ASN N N 117.096 0.023 1
1469 . 184 ASN CA C 56.802 0.039 1
1470 . 184 ASN HA H 4.299 0.016 1
1471 . 184 ASN C C 179.012 0.0 1
1472 . 184 ASN CB C 38.703 0.067 1
1473 . 184 ASN HB2 H 2.616 0.014 1
1474 . 184 ASN HB3 H 2.683 0.0060 1
1475 . 185 TYR H H 9.028 0.0030 1
1476 . 185 TYR N N 120.928 0.047 1
1477 . 185 TYR CA C 57.7 0.145 1
1478 . 185 TYR HA H 4.531 0.02 1
1479 . 185 TYR C C 178.393 0.0 1
1480 . 185 TYR CB C 37.754 0.061 1
1481 . 185 TYR HB2 H 3.008 0.0070 1
1482 . 185 TYR HB3 H 3.214 0.019 1
1483 . 186 LEU H H 8.827 0.0040 1
1484 . 186 LEU N N 121.806 0.061 1
1485 . 186 LEU CA C 58.94 0.07 1
1486 . 186 LEU C C 179.122 0.0 1
1487 . 186 LEU CB C 42.332 0.073 1
1488 . 187 LYS N N 119.998 0.078 1
1489 . 187 LYS CA C 61.288 0.058 1
1490 . 187 LYS C C 179.855 0.0 1
1491 . 187 LYS CB C 32.99 0.037 1
1492 . 188 LEU H H 7.674 0.0070 1
1493 . 188 LEU N N 122.2 0.0 1
1494 . 188 LEU CA C 58.466 0.086 1
1495 . 188 LEU HA H 4.078 0.0020 1
1496 . 188 LEU C C 179.689 0.0 1
1497 . 188 LEU CB C 42.499 0.0 1
1498 . 188 LEU HB2 H 1.95 0.0010 1
1499 . 188 LEU CG C 28.375 0.248 1
1500 . 188 LEU CD1 C 23.997 0.068 1
1501 . 188 LEU HD1 H 0.82 0.01 1
1502 . 188 LEU CD2 C 25.86 0.016 1
1503 . 188 LEU HD2 H 0.534 0.0070 1
1504 . 188 LEU HG H 1.924 0.0050 1
1505 . 189 LEU H H 8.612 0.0050 1
1506 . 189 LEU N N 121.909 0.031 1
1507 . 189 LEU CA C 58.486 0.061 1
1508 . 189 LEU C C 178.168 0.0 1
1509 . 189 LEU CB C 42.859 0.0 1
1510 . 190 LYS H H 8.511 0.0060 1
1511 . 190 LYS N N 121.41 0.024 1
1512 . 190 LYS CA C 60.603 0.033 1
1513 . 190 LYS C C 179.536 0.0 1
1514 . 190 LYS CB C 32.991 0.0 1
stop_
save_