data_5214
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Y2 selective analogue-I of neuropeptide Y
;
_BMRB_accession_number 5214
_BMRB_flat_file_name bmr5214.str
_Entry_type original
_Submission_date 2001-11-21
_Accession_date 2001-11-26
_Entry_origination author
_NMR_STAR_version 2.1.1
_Experimental_method NMR
_Details .
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Yao Shenggen . .
2 Smith-white Margaret A .
3 Potter Erica K .
4 Norton Raymond S .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 3
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 301
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2008-07-17 update BMRB 'Updating non-standard residue'
stop_
loop_
_Related_BMRB_accession_number
_Relationship
4398 'neuropeptide Y'
5215 'Y2 selective analogue-II of neuropeptide Y'
5216 'Y2 selective analogue-III of neuropeptide Y'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Stabilization of the helical structural of Y2-selective analogues of
neuropeptide Y by lactam bridges
;
_Citation_status 'in preparation'
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Yao Shenggen . .
2 Smith-white Margaret A .
3 Potter Erica K .
4 Norton Raymond S .
stop_
_Journal_abbreviation .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first .
_Page_last .
_Year .
_Details .
loop_
_Keyword
'neuropeptide Y'
'Y2 agonist'
'lactam bridge'
helix
NMR
stop_
save_
##################################
# Molecular system description #
##################################
save_system_NPY
_Saveframe_category molecular_system
_Mol_system_name 'Y2 selective analogue I of neuropeptide Y'
_Abbreviation_common NPY
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'analogue I of neuropeptide Y' $NPY
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_NPY
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'neuropeptide Y'
_Name_variant 'analog-I, L24A, I28K, I31L, T32E'
_Abbreviation_common NPY
_Molecular_mass .
_Mol_thiol_state 'not present'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 15
_Mol_residue_sequence XARHYKNLLERQRYX
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 24 ACE 2 24 ALA 3 25 ARG 4 26 HIS 5 27 TYR
6 28 LYS 7 29 ASN 8 30 LEU 9 31 LEU 10 32 GLU
11 33 ARG 12 34 GLN 13 35 ARG 14 36 TYR 15 36 NH2
stop_
_Sequence_homology_query_date 2005-11-24
_Sequence_homology_query_revised_last_date 2002-02-09
save_
######################
# Polymer residues #
######################
save_chem_comp_ACE
_Saveframe_category polymer_residue
_Mol_type NON-POLYMER
_Name_common 'ACETYL GROUP'
_BMRB_code ACE
_PDB_code ACE
_Standard_residue_derivative .
_Molecular_mass 44.053
_Mol_paramagnetic .
_Details .
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
C C C . 0 . ?
CH3 CH3 C . 0 . ?
H H H . 0 . ?
H1 H1 H . 0 . ?
H2 H2 H . 0 . ?
H3 H3 H . 0 . ?
O O O . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
DOUB C O ? ?
SING C CH3 ? ?
SING C H ? ?
SING CH3 H1 ? ?
SING CH3 H2 ? ?
SING CH3 H3 ? ?
stop_
save_
save_chem_comp_NH2
_Saveframe_category polymer_residue
_Mol_type non-polymer
_Name_common 'AMINO GROUP'
_BMRB_code .
_PDB_code NH2
_Standard_residue_derivative .
_Molecular_mass 16.023
_Mol_paramagnetic .
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jul 21 10:41:13 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
N N N . 0 . ?
HN1 HN1 H . 0 . ?
HN2 HN2 H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
SING N HN1 ? ?
SING N HN2 ? ?
stop_
save_
########################################
# Molecular bond linkage definitions #
########################################
save_crosslink_bonds
_Saveframe_category crosslink_bonds
loop_
_Bond_order
_Bond_type
_Atom_one_mol_system_component_name
_Atom_one_residue_seq_code
_Atom_one_residue_label
_Atom_one_atom_name
_Atom_two_mol_system_component_name
_Atom_two_residue_seq_code
_Atom_two_residue_label
_Atom_two_atom_name
single lactam 'analogue I of neuropeptide Y' 6 LYS NZ 'analogue I of neuropeptide Y' 10 GLU CD
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$NPY 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
$NPY 'chemical synthesis' . . . . .
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
$NPY 3.0 mM .
TFE 40 % .
H2O 60 % .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$NPY 3.0 mM .
TFE 30 % .
H2O 70 % .
stop_
save_
save_sample_3
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$NPY 3.0 mM .
H2O 100 % .
stop_
save_
############################
# Computer software used #
############################
save_xwinnmr
_Saveframe_category software
_Name xwinnmr
_Version 2.6
loop_
_Task
process
stop_
_Details 'Bruker AG, Karlsruhe, Germany'
save_
save_XEASY
_Saveframe_category software
_Name XEASY
_Version 1.3
loop_
_Task
analysis
stop_
_Details 'C. Bartels et. al., J. Biomol. NMR 1995, 6, 1-10'
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_DQFCOSY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name DQFCOSY
_Sample_label .
save_
save_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_Sample_label .
save_
save_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TOCSY
_Sample_label .
save_
save_NMR_applied_experiment
_Saveframe_category NMR_applied_experiment
_Experiment_name .
_BMRB_pulse_sequence_accession_number .
_Details
;
Standard Bruker pulse sequences were used.
Water suppression was achieved using water-gate segment.
;
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name DQFCOSY
_BMRB_pulse_sequence_accession_number .
_Details
;
Standard Bruker pulse sequences were used.
Water suppression was achieved using water-gate segment.
;
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_BMRB_pulse_sequence_accession_number .
_Details
;
Standard Bruker pulse sequences were used.
Water suppression was achieved using water-gate segment.
;
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TOCSY
_BMRB_pulse_sequence_accession_number .
_Details
;
Standard Bruker pulse sequences were used.
Water suppression was achieved using water-gate segment.
;
save_
#######################
# Sample conditions #
#######################
save_condition_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 5.0 0.2 n/a
temperature 298 1 K
stop_
save_
save_condition_2
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 5.0 0.2 n/a
temperature 308 1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS H 1 'methyl protons' ppm 0.0 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_analog-I_cs_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $condition_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'analogue I of neuropeptide Y'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 1 ACE H1 H 2.06 0.01 1
2 . 1 ACE H2 H 2.06 0.01 1
3 . 1 ACE H3 H 2.06 0.01 1
4 . 2 ALA H H 8.15 0.01 1
5 . 2 ALA HA H 4.21 0.01 1
6 . 2 ALA HB H 1.37 0.01 1
7 . 3 ARG H H 8.19 0.01 1
8 . 3 ARG HA H 4.14 0.01 1
9 . 3 ARG HB2 H 1.70 0.01 1
10 . 3 ARG HB3 H 1.70 0.01 1
11 . 3 ARG HG2 H 1.56 0.01 1
12 . 3 ARG HG3 H 1.56 0.01 1
13 . 3 ARG HD2 H 3.15 0.01 1
14 . 3 ARG HD3 H 3.15 0.01 1
15 . 3 ARG HE H 7.15 0.01 1
16 . 4 HIS H H 8.10 0.01 1
17 . 4 HIS HA H 4.55 0.01 1
18 . 4 HIS HB2 H 3.14 0.01 1
19 . 4 HIS HB3 H 3.14 0.01 1
20 . 4 HIS HD2 H 7.03 0.01 1
21 . 4 HIS HE1 H 8.42 0.01 1
22 . 5 TYR H H 7.95 0.01 1
23 . 5 TYR HA H 4.49 0.01 1
24 . 5 TYR HB2 H 3.12 0.01 2
25 . 5 TYR HB3 H 2.91 0.01 2
26 . 5 TYR HD1 H 7.10 0.01 1
27 . 5 TYR HD2 H 7.10 0.01 1
28 . 5 TYR HE1 H 6.79 0.01 1
29 . 5 TYR HE2 H 6.79 0.01 1
30 . 6 LYS H H 8.26 0.01 1
31 . 6 LYS HA H 4.04 0.01 1
32 . 6 LYS HB2 H 1.99 0.01 2
33 . 6 LYS HB3 H 1.71 0.01 2
34 . 6 LYS HG2 H 1.44 0.01 2
35 . 6 LYS HG3 H 1.34 0.01 2
36 . 6 LYS HD2 H 1.55 0.01 2
37 . 6 LYS HD3 H 1.48 0.01 2
38 . 6 LYS HE2 H 3.40 0.01 2
39 . 6 LYS HE3 H 2.98 0.01 2
40 . 6 LYS HZ H 7.49 0.01 1
41 . 7 ASN H H 7.92 0.01 1
42 . 7 ASN HA H 4.48 0.01 1
43 . 7 ASN HB2 H 2.97 0.01 1
44 . 7 ASN HB3 H 2.97 0.01 1
45 . 7 ASN HD21 H 7.61 0.01 2
46 . 7 ASN HD22 H 6.70 0.01 2
47 . 8 LEU H H 8.04 0.01 1
48 . 8 LEU HA H 4.07 0.01 1
49 . 8 LEU HB2 H 1.75 0.01 1
50 . 8 LEU HB3 H 1.75 0.01 1
51 . 8 LEU HG H 1.65 0.01 1
52 . 8 LEU HD1 H 0.91 0.01 2
53 . 8 LEU HD2 H 0.88 0.01 2
54 . 9 LEU H H 7.97 0.01 1
55 . 9 LEU HA H 4.12 0.01 1
56 . 9 LEU HB2 H 1.75 0.01 1
57 . 9 LEU HB3 H 1.75 0.01 1
58 . 9 LEU HG H 1.59 0.01 1
59 . 9 LEU HD1 H 0.87 0.01 2
60 . 9 LEU HD2 H 0.55 0.01 2
61 . 10 GLU H H 7.95 0.01 1
62 . 10 GLU HA H 4.07 0.01 1
63 . 10 GLU HB2 H 2.21 0.01 1
64 . 10 GLU HB3 H 2.21 0.01 1
65 . 10 GLU HG2 H 2.48 0.01 1
66 . 10 GLU HG3 H 2.48 0.01 1
67 . 11 ARG H H 7.84 0.01 1
68 . 11 ARG HA H 3.85 0.01 1
69 . 11 ARG HB2 H 1.93 0.01 2
70 . 11 ARG HB3 H 1.76 0.01 2
71 . 11 ARG HG2 H 1.61 0.01 1
72 . 11 ARG HG3 H 1.61 0.01 1
73 . 11 ARG HD2 H 3.12 0.01 1
74 . 11 ARG HD3 H 3.12 0.01 1
75 . 11 ARG HE H 7.23 0.01 1
76 . 12 GLN H H 8.08 0.01 1
77 . 12 GLN HA H 4.12 0.01 1
78 . 12 GLN HB2 H 2.12 0.01 1
79 . 12 GLN HB3 H 2.12 0.01 1
80 . 12 GLN HG2 H 2.42 0.01 2
81 . 12 GLN HG3 H 2.37 0.01 2
82 . 12 GLN HE21 H 7.48 0.01 2
83 . 12 GLN HE22 H 6.71 0.01 2
84 . 13 ARG H H 7.96 0.01 1
85 . 13 ARG HA H 4.12 0.01 1
86 . 13 ARG HB2 H 1.69 0.01 2
87 . 13 ARG HB3 H 1.60 0.01 2
88 . 13 ARG HG2 H 1.38 0.01 1
89 . 13 ARG HG3 H 1.38 0.01 1
90 . 13 ARG HD2 H 3.04 0.01 1
91 . 13 ARG HD3 H 3.04 0.01 1
92 . 13 ARG HE H 7.08 0.01 1
93 . 14 TYR H H 7.91 0.01 1
94 . 14 TYR HA H 4.61 0.01 1
95 . 14 TYR HB2 H 3.22 0.01 2
96 . 14 TYR HB3 H 2.90 0.01 2
97 . 14 TYR HD1 H 7.20 0.01 1
98 . 14 TYR HD2 H 7.20 0.01 1
99 . 14 TYR HE1 H 6.82 0.01 1
100 . 14 TYR HE2 H 6.82 0.01 1
stop_
save_
save_analog-I_cs_set_2
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $condition_2
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'analogue I of neuropeptide Y'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 1 ACE H1 H 2.06 0.01 1
2 . 1 ACE H2 H 2.06 0.01 1
3 . 1 ACE H3 H 2.06 0.01 1
4 . 2 ALA H H 8.12 0.01 1
5 . 2 ALA HA H 4.22 0.01 1
6 . 2 ALA HB H 1.38 0.01 1
7 . 3 ARG H H 8.18 0.01 1
8 . 3 ARG HA H 4.16 0.01 1
9 . 3 ARG HB2 H 1.71 0.01 1
10 . 3 ARG HB3 H 1.71 0.01 1
11 . 3 ARG HG2 H 1.57 0.01 1
12 . 3 ARG HG3 H 1.57 0.01 1
13 . 3 ARG HD2 H 3.16 0.01 1
14 . 3 ARG HD3 H 3.16 0.01 1
15 . 3 ARG HE H 7.15 0.01 1
16 . 4 HIS H H 8.02 0.01 1
17 . 4 HIS HA H 4.55 0.01 1
18 . 4 HIS HB2 H 3.10 0.01 1
19 . 4 HIS HB3 H 3.10 0.01 1
20 . 4 HIS HD1 H 6.96 0.01 1
21 . 4 HIS HD2 H 8.18 0.01 1
22 . 4 HIS HE1 H 8.18 0.01 1
23 . 5 TYR H H 7.87 0.01 1
24 . 5 TYR HA H 4.46 0.01 1
25 . 5 TYR HB2 H 2.94 0.01 2
26 . 5 TYR HB3 H 3.10 0.01 2
27 . 5 TYR HD1 H 7.09 0.01 1
28 . 5 TYR HD2 H 7.09 0.01 1
29 . 5 TYR HE1 H 6.81 0.01 1
30 . 5 TYR HE2 H 6.81 0.01 1
31 . 6 LYS H H 8.18 0.01 1
32 . 6 LYS HA H 4.02 0.01 1
33 . 6 LYS HB2 H 1.73 0.01 2
34 . 6 LYS HB3 H 1.97 0.01 2
35 . 6 LYS HG2 H 1.39 0.01 2
36 . 6 LYS HG3 H 1.46 0.01 2
37 . 6 LYS HD2 H 1.54 0.01 1
38 . 6 LYS HD3 H 1.54 0.01 1
39 . 6 LYS HE2 H 3.00 0.01 2
40 . 6 LYS HE3 H 3.36 0.01 2
41 . 6 LYS HZ H 7.45 0.01 1
42 . 7 ASN H H 7.95 0.01 1
43 . 7 ASN HA H 4.48 0.01 1
44 . 7 ASN HB2 H 2.94 0.01 1
45 . 7 ASN HB3 H 2.94 0.01 1
46 . 7 ASN HD21 H 6.71 0.01 2
47 . 7 ASN HD22 H 7.60 0.01 2
48 . 8 LEU H H 8.00 0.01 1
49 . 8 LEU HA H 4.08 0.01 1
50 . 8 LEU HB2 H 1.76 0.01 1
51 . 8 LEU HB3 H 1.76 0.01 1
52 . 8 LEU HG H 1.66 0.01 1
53 . 8 LEU HD1 H 0.88 0.01 2
54 . 8 LEU HD2 H 0.90 0.01 2
55 . 9 LEU H H 7.99 0.01 1
56 . 9 LEU HA H 4.13 0.01 1
57 . 9 LEU HB2 H 1.76 0.01 1
58 . 9 LEU HB3 H 1.76 0.01 1
59 . 9 LEU HG H 1.60 0.01 1
60 . 9 LEU HD1 H 0.84 0.01 2
61 . 9 LEU HD2 H 0.86 0.01 2
62 . 10 GLU H H 7.89 0.01 1
63 . 10 GLU HA H 4.10 0.01 1
64 . 10 GLU HB2 H 2.21 0.01 1
65 . 10 GLU HB3 H 2.21 0.01 1
66 . 10 GLU HG2 H 2.44 0.01 2
67 . 10 GLU HG3 H 2.50 0.01 2
68 . 11 ARG H H 7.86 0.01 1
69 . 11 ARG HA H 3.96 0.01 1
70 . 11 ARG HB2 H 1.79 0.01 2
71 . 11 ARG HB3 H 1.95 0.01 2
72 . 11 ARG HG2 H 1.64 0.01 1
73 . 11 ARG HG3 H 1.64 0.01 1
74 . 11 ARG HD2 H 3.15 0.01 1
75 . 11 ARG HD3 H 3.15 0.01 1
76 . 11 ARG HE H 7.21 0.01 1
77 . 12 GLN H H 8.06 0.01 1
78 . 12 GLN HA H 4.14 0.01 1
79 . 12 GLN HB2 H 2.12 0.01 1
80 . 12 GLN HB3 H 2.12 0.01 1
81 . 12 GLN HG2 H 2.38 0.01 2
82 . 12 GLN HG3 H 2.44 0.01 2
83 . 12 GLN HE21 H 6.61 0.01 2
84 . 12 GLN HE22 H 7.19 0.01 2
85 . 13 ARG H H 7.94 0.01 1
86 . 13 ARG HA H 4.15 0.01 1
87 . 13 ARG HB2 H 1.64 0.01 2
88 . 13 ARG HB3 H 1.69 0.01 2
89 . 13 ARG HG2 H 1.40 0.01 2
90 . 13 ARG HG3 H 1.43 0.01 2
91 . 13 ARG HD2 H 3.07 0.01 1
92 . 13 ARG HD3 H 3.07 0.01 1
93 . 13 ARG HE H 7.08 0.01 1
94 . 14 TYR H H 7.89 0.01 1
95 . 14 TYR HA H 4.59 0.01 1
96 . 14 TYR HB2 H 2.92 0.01 2
97 . 14 TYR HB3 H 3.22 0.01 2
98 . 14 TYR HD1 H 7.19 0.01 1
99 . 14 TYR HD2 H 7.19 0.01 1
100 . 14 TYR HE1 H 6.83 0.01 1
101 . 14 TYR HE2 H 6.83 0.01 1
stop_
save_
save_analog-I_cs_set_3
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_2
stop_
_Sample_conditions_label $condition_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'analogue I of neuropeptide Y'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 1 ACE H1 H 1.96 0.01 1
2 . 1 ACE H2 H 1.96 0.01 1
3 . 1 ACE H3 H 1.96 0.01 1
4 . 2 ALA H H 8.21 0.01 1
5 . 2 ALA HA H 4.16 0.01 1
6 . 2 ALA HB H 1.27 0.01 1
7 . 3 ARG H H 8.25 0.01 1
8 . 3 ARG HA H 4.16 0.01 1
9 . 3 ARG HB2 H 1.59 0.01 2
10 . 3 ARG HB3 H 1.49 0.01 2
11 . 3 ARG HG2 H 1.42 0.01 1
12 . 3 ARG HG3 H 1.42 0.01 1
13 . 3 ARG HD2 H 3.08 0.01 1
14 . 3 ARG HD3 H 3.08 0.01 1
15 . 3 ARG HE H 7.05 0.01 1
16 . 4 HIS H H 8.40 0.01 1
17 . 4 HIS HA H 4.61 0.01 1
18 . 4 HIS HB2 H 3.11 0.01 2
19 . 4 HIS HB3 H 3.03 0.01 2
20 . 4 HIS HD2 H 7.13 0.01 1
21 . 4 HIS HE1 H 8.47 0.01 1
22 . 5 TYR H H 8.27 0.01 1
23 . 5 TYR HA H 4.55 0.01 1
24 . 5 TYR HB2 H 2.98 0.01 2
25 . 5 TYR HB3 H 2.83 0.01 2
26 . 5 TYR HD1 H 7.05 0.01 1
27 . 5 TYR HD2 H 7.05 0.01 1
28 . 5 TYR HE1 H 6.74 0.01 1
29 . 5 TYR HE2 H 6.74 0.01 1
30 . 6 LYS H H 8.20 0.01 1
31 . 6 LYS HA H 4.13 0.01 1
32 . 6 LYS HB2 H 1.73 0.01 2
33 . 6 LYS HB3 H 1.64 0.01 2
34 . 6 LYS HG2 H 1.27 0.01 1
35 . 6 LYS HG3 H 1.27 0.01 1
36 . 6 LYS HD2 H 1.52 0.01 2
37 . 6 LYS HD3 H 1.42 0.01 2
38 . 6 LYS HE2 H 3.20 0.01 1
39 . 6 LYS HE3 H 3.20 0.01 1
40 . 6 LYS HZ H 7.86 0.01 1
41 . 7 ASN H H 8.18 0.01 1
42 . 7 ASN HA H 4.48 0.01 1
43 . 7 ASN HB2 H 2.89 0.01 1
44 . 7 ASN HB3 H 2.89 0.01 1
45 . 7 ASN HD21 H 7.65 0.01 2
46 . 7 ASN HD22 H 6.89 0.01 2
47 . 8 LEU H H 8.26 0.01 1
48 . 8 LEU HA H 4.16 0.01 1
49 . 8 LEU HB2 H 1.65 0.01 1
50 . 8 LEU HB3 H 1.65 0.01 1
51 . 8 LEU HG H 1.59 0.01 1
52 . 8 LEU HD1 H 0.90 0.01 2
53 . 8 LEU HD2 H 0.84 0.01 2
54 . 9 LEU H H 8.09 0.01 1
55 . 9 LEU HA H 4.24 0.01 1
56 . 9 LEU HB2 H 1.62 0.01 1
57 . 9 LEU HB3 H 1.62 0.01 1
58 . 9 LEU HG H 1.57 0.01 1
59 . 9 LEU HD1 H 0.88 0.01 2
60 . 9 LEU HD2 H 0.81 0.01 2
61 . 10 GLU H H 7.91 0.01 1
62 . 10 GLU HA H 4.13 0.01 1
63 . 10 GLU HB2 H 2.14 0.01 2
64 . 10 GLU HB3 H 2.03 0.01 2
65 . 10 GLU HG2 H 2.31 0.01 1
66 . 10 GLU HG3 H 2.31 0.01 1
67 . 11 ARG H H 8.07 0.01 1
68 . 11 ARG HA H 3.96 0.01 1
69 . 11 ARG HB2 H 1.81 0.01 2
70 . 11 ARG HB3 H 1.65 0.01 2
71 . 11 ARG HG2 H 1.51 0.01 1
72 . 11 ARG HG3 H 1.51 0.01 1
73 . 11 ARG HD2 H 3.11 0.01 1
74 . 11 ARG HD3 H 3.11 0.01 1
75 . 11 ARG HE H 7.16 0.01 1
76 . 12 GLN H H 8.26 0.01 1
77 . 12 GLN HA H 4.12 0.01 1
78 . 12 GLN HB2 H 1.97 0.01 1
79 . 12 GLN HB3 H 1.97 0.01 1
80 . 12 GLN HG2 H 2.29 0.01 1
81 . 12 GLN HG3 H 2.29 0.01 1
82 . 12 GLN HE21 H 7.42 0.01 2
83 . 12 GLN HE22 H 6.80 0.01 2
84 . 13 ARG H H 8.17 0.01 1
85 . 13 ARG HA H 4.14 0.01 1
86 . 13 ARG HB2 H 1.62 0.01 2
87 . 13 ARG HB3 H 1.43 0.01 2
88 . 13 ARG HG2 H 1.35 0.01 1
89 . 13 ARG HG3 H 1.35 0.01 1
90 . 13 ARG HD2 H 3.06 0.01 1
91 . 13 ARG HD3 H 3.06 0.01 1
92 . 13 ARG HE H 7.08 0.01 1
93 . 14 TYR H H 8.07 0.01 1
94 . 14 TYR HA H 4.54 0.01 1
95 . 14 TYR HB2 H 3.11 0.01 2
96 . 14 TYR HB3 H 2.86 0.01 2
97 . 14 TYR HD1 H 7.13 0.01 1
98 . 14 TYR HD2 H 7.13 0.01 1
99 . 14 TYR HE1 H 6.79 0.01 1
100 . 14 TYR HE2 H 6.79 0.01 1
stop_
save_