data_5900
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
NMR structure of 16th module of Immune Adherence Receptor, Cr1 (Cd35)
;
_BMRB_accession_number 5900
_BMRB_flat_file_name bmr5900.str
_Entry_type original
_Submission_date 2003-08-07
_Accession_date 2003-08-07
_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 O'Leary J. M. .
2 Bromek K. . .
3 Black G. M. .
4 Uhrinova S. . .
5 Schmitz C. . .
6 Krych M. . .
7 Atkinson J. P. .
8 Uhrin D. . .
9 Barlow P. N. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 3
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 337
"15N chemical shifts" 65
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2004-07-23 original BMRB .
stop_
_Original_release_date 2003-08-07
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Backbone dynamics of complement control protein (CCP) modules reveals mobility
in binding surfaces.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15096630
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 O'Leary J. M. .
2 Bromek K. . .
3 Black G. M. .
4 Uhrinova S. . .
5 Schmitz C. . .
6 Wang X. . .
7 Krych M. . .
8 Atkinson J. P. .
9 Uhrin D. . .
10 Barlow P. N. .
stop_
_Journal_abbreviation 'Protein Sci.'
_Journal_volume 13
_Journal_issue 5
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1238
_Page_last 1250
_Year 2004
_Details .
loop_
_Keyword
CCP
Complement
Module
SCR
Structure
Sushi
stop_
save_
##################################
# Molecular system description #
##################################
save_system_Cr1_module
_Saveframe_category molecular_system
_Mol_system_name 'complement receptor type 1'
_Abbreviation_common 'complement receptor type 1'
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
'Complement receptor type 1' $Cr1_module
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_Cr1_module
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'complement receptor type 1'
_Abbreviation_common 'complement receptor type 1'
_Molecular_mass .
_Mol_thiol_state 'all disulfide bound'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 68
_Mol_residue_sequence
;
EAEAKSCKTPPDPVNGMVHV
ITDIQVGSRITYSCTTGHRL
IGHSSAECILSGNTAHWSTK
PPICQRIP
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 957 GLU 2 958 ALA 3 959 GLU 4 960 ALA 5 961 LYS
6 962 SER 7 963 CYS 8 964 LYS 9 965 THR 10 966 PRO
11 967 PRO 12 968 ASP 13 969 PRO 14 970 VAL 15 971 ASN
16 972 GLY 17 973 MET 18 974 VAL 19 975 HIS 20 976 VAL
21 977 ILE 22 978 THR 23 979 ASP 24 980 ILE 25 981 GLN
26 982 VAL 27 983 GLY 28 984 SER 29 985 ARG 30 986 ILE
31 987 THR 32 988 TYR 33 989 SER 34 990 CYS 35 991 THR
36 992 THR 37 993 GLY 38 994 HIS 39 995 ARG 40 996 LEU
41 997 ILE 42 998 GLY 43 999 HIS 44 1000 SER 45 1001 SER
46 1002 ALA 47 1003 GLU 48 1004 CYS 49 1005 ILE 50 1006 LEU
51 1007 SER 52 1008 GLY 53 1009 ASN 54 1010 THR 55 1011 ALA
56 1012 HIS 57 1013 TRP 58 1014 SER 59 1015 THR 60 1016 LYS
61 1017 PRO 62 1018 PRO 63 1019 ILE 64 1020 CYS 65 1021 GLN
66 1022 ARG 67 1023 ILE 68 1024 PRO
stop_
_Sequence_homology_query_date 2008-08-19
_Sequence_homology_query_revised_last_date 2008-08-19
loop_
_Database_name
_Database_accession_code
_Database_entry_mol_name
_Sequence_query_to_submitted_percentage
_Sequence_subject_length
_Sequence_identity
_Sequence_positive
_Sequence_homology_expectation_value
PDB 1GKG 'Structure Determination And Rational Mutagenesis Reveal Binding Surface Of Immune Adherence Receptor, Cr1 (Cd35)' 100.00 136 100.00 100.00 2.47e-32
PDB 1PPQ 'Nmr Structure Of 16th Module Of Immune Adherence Receptor, Cr1 (Cd35)' 100.00 68 100.00 100.00 2.43e-32
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$Cr1_module 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
$Cr1_module 'recombinant technology' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$Cr1_module 1 mM [U-15N]
'phosphate buffer' 25 mM .
D2O 10 % .
H2O 90 % .
stop_
save_
############################
# Computer software used #
############################
save_VNMR
_Saveframe_category software
_Name VNMR
_Version .
loop_
_Task
collection
stop_
_Details .
save_
save_AZARA
_Saveframe_category software
_Name AZARA
_Version 2.6
loop_
_Task
processing
stop_
_Details 'Boucher, W.'
save_
save_ANSIG
_Saveframe_category software
_Name ANSIG
_Version 3.3
loop_
_Task
'data analysis'
stop_
_Details 'Kraulis, P.'
save_
save_CNS
_Saveframe_category software
_Name CNS
_Version 1.0
loop_
_Task
refinement
'structure solution'
stop_
_Details Brunger
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_15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N HSQC'
_Sample_label .
save_
save_2D_NOESY_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D NOESY'
_Sample_label .
save_
save_2D_TOCSY_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D TOCSY'
_Sample_label .
save_
save_2D_RSCUBACOSY_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D RSCUBACOSY'
_Sample_label .
save_
save_3D_15N_HSQC-TOCSY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 15N HSQC-TOCSY'
_Sample_label .
save_
save_3D_15N_HSQC-NOESY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D 15N HSQC-NOESY'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 25 . mM
pH 6.0 . n/a
pressure 1 . atm
temperature 310 . 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
. H 1 . ppm . . . . . .
. N 15 . ppm . . . . . .
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_chemical_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'15N HSQC'
'2D NOESY'
'2D TOCSY'
'2D RSCUBACOSY'
'3D 15N HSQC-TOCSY'
'3D 15N HSQC-NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'Complement receptor type 1'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 4 ALA N N 111.1 0.3 1
2 . 4 ALA H H 8.29 0.03 1
3 . 4 ALA HA H 4.30 0.03 1
4 . 4 ALA HB H 1.30 0.03 1
5 . 5 LYS N N 121.3 0.3 1
6 . 5 LYS H H 8.27 0.03 1
7 . 5 LYS HA H 4.29 0.03 1
8 . 5 LYS HB2 H 1.62 0.03 1
9 . 5 LYS HG2 H 1.37 0.03 1
10 . 5 LYS HD2 H 1.66 0.03 1
11 . 5 LYS HE2 H 2.92 0.03 1
12 . 6 SER N N 114.4 0.3 1
13 . 6 SER H H 7.99 0.03 1
14 . 6 SER HA H 4.63 0.03 1
15 . 6 SER HB2 H 3.69 0.03 1
16 . 6 SER HB3 H 3.57 0.03 1
17 . 7 CYS N N 120.9 0.3 1
18 . 7 CYS H H 8.08 0.03 1
19 . 7 CYS HA H 4.07 0.03 1
20 . 7 CYS HB2 H 2.16 0.03 1
21 . 7 CYS HB3 H 2.07 0.03 1
22 . 8 LYS N N 119.7 0.3 1
23 . 8 LYS H H 8.42 0.03 1
24 . 8 LYS HA H 4.31 0.03 1
25 . 8 LYS HB2 H 1.88 0.03 1
26 . 8 LYS HB3 H 1.80 0.03 1
27 . 8 LYS HG2 H 1.53 0.03 1
28 . 8 LYS HD2 H 1.72 0.03 1
29 . 8 LYS HE2 H 3.04 0.03 1
30 . 9 THR N N 121.3 0.3 1
31 . 9 THR H H 8.41 0.03 1
32 . 9 THR HA H 4.11 0.03 1
33 . 9 THR HB H 3.94 0.03 1
34 . 9 THR HG2 H 1.16 0.03 1
35 . 10 PRO HA H 4.68 0.03 1
36 . 10 PRO HB2 H 1.66 0.03 1
37 . 10 PRO HB3 H 1.42 0.03 1
38 . 10 PRO HG2 H 1.77 0.03 1
39 . 10 PRO HG3 H 1.36 0.03 1
40 . 10 PRO HD2 H 3.56 0.03 1
41 . 11 PRO HA H 4.46 0.03 1
42 . 11 PRO HB2 H 2.13 0.03 1
43 . 11 PRO HB3 H 1.76 0.03 1
44 . 11 PRO HG2 H 1.96 0.03 1
45 . 11 PRO HG3 H 1.89 0.03 1
46 . 11 PRO HD2 H 3.75 0.03 1
47 . 11 PRO HD3 H 3.60 0.03 1
48 . 12 ASP N N 119.4 0.3 1
49 . 12 ASP H H 8.01 0.03 1
50 . 12 ASP HA H 4.63 0.03 1
51 . 12 ASP HB2 H 2.72 0.03 1
52 . 12 ASP HB3 H 2.29 0.03 1
53 . 13 PRO HA H 4.34 0.03 1
54 . 13 PRO HB2 H 2.16 0.03 1
55 . 13 PRO HB3 H 1.34 0.03 1
56 . 13 PRO HG2 H 1.64 0.03 1
57 . 13 PRO HG3 H 1.59 0.03 1
58 . 13 PRO HD2 H 3.91 0.03 1
59 . 13 PRO HD3 H 3.27 0.03 1
60 . 14 VAL N N 110.2 0.3 1
61 . 14 VAL H H 8.31 0.03 1
62 . 14 VAL HA H 3.64 0.03 1
63 . 14 VAL HB H 1.82 0.03 1
64 . 14 VAL HG1 H 1.00 0.03 1
65 . 14 VAL HG2 H 0.91 0.03 1
66 . 15 ASN N N 120.1 0.3 1
67 . 15 ASN H H 8.97 0.03 1
68 . 15 ASN HA H 4.05 0.03 1
69 . 15 ASN HB2 H 2.73 0.03 1
70 . 15 ASN HB3 H 1.55 0.03 1
71 . 15 ASN ND2 N 117.3 0.3 1
72 . 15 ASN HD21 H 7.46 0.03 1
73 . 15 ASN HD22 H 6.93 0.03 1
74 . 16 GLY N N 121.8 0.3 1
75 . 16 GLY H H 7.88 0.03 1
76 . 16 GLY HA2 H 4.45 0.03 1
77 . 16 GLY HA3 H 4.23 0.03 1
78 . 17 MET N N 116.5 0.3 1
79 . 17 MET H H 8.69 0.03 1
80 . 17 MET HA H 4.81 0.03 1
81 . 17 MET HB2 H 1.72 0.03 1
82 . 17 MET HB3 H 1.65 0.03 1
83 . 17 MET HG2 H 2.20 0.03 1
84 . 17 MET HG3 H 2.11 0.03 1
85 . 17 MET HE H 3.28 0.03 1
86 . 18 VAL N N 122.5 0.3 1
87 . 18 VAL H H 8.50 0.03 1
88 . 18 VAL HA H 4.46 0.03 1
89 . 18 VAL HB H 1.73 0.03 1
90 . 18 VAL HG1 H 0.58 0.03 1
91 . 18 VAL HG2 H 0.23 0.03 1
92 . 19 HIS N N 111.1 0.3 1
93 . 19 HIS H H 8.86 0.03 1
94 . 19 HIS HA H 4.61 0.03 1
95 . 19 HIS HB2 H 3.15 0.03 1
96 . 19 HIS HB3 H 2.77 0.03 1
97 . 19 HIS HD2 H 6.64 0.03 1
98 . 19 HIS HE1 H 7.51 0.03 1
99 . 20 VAL N N 111.3 0.3 1
100 . 20 VAL H H 8.46 0.03 1
101 . 20 VAL HA H 3.98 0.03 1
102 . 20 VAL HB H 1.92 0.03 1
103 . 20 VAL HG2 H 0.73 0.03 1
104 . 21 ILE N N 114.1 0.3 1
105 . 21 ILE H H 7.66 0.03 1
106 . 21 ILE HA H 3.89 0.03 1
107 . 21 ILE HB H 1.96 0.03 1
108 . 21 ILE HG12 H 1.50 0.03 1
109 . 21 ILE HG13 H 1.17 0.03 1
110 . 21 ILE HG2 H 0.95 0.03 1
111 . 21 ILE HD1 H 0.74 0.03 1
112 . 22 THR N N 113.1 0.3 1
113 . 22 THR H H 9.30 0.03 1
114 . 22 THR HA H 4.41 0.03 1
115 . 22 THR HB H 4.22 0.03 1
116 . 22 THR HG2 H 1.17 0.03 1
117 . 23 ASP N N 123.4 0.3 1
118 . 23 ASP H H 8.63 0.03 1
119 . 23 ASP HA H 4.59 0.03 1
120 . 23 ASP HB2 H 3.04 0.03 1
121 . 23 ASP HB3 H 2.71 0.03 1
122 . 24 ILE N N 110.7 0.3 1
123 . 24 ILE H H 7.63 0.03 1
124 . 24 ILE HA H 4.89 0.03 1
125 . 24 ILE HB H 2.34 0.03 1
126 . 24 ILE HG12 H 1.38 0.03 1
127 . 24 ILE HG13 H 1.09 0.03 1
128 . 24 ILE HG2 H 0.97 0.03 1
129 . 24 ILE HD1 H 0.90 0.03 1
130 . 25 GLN N N 118.7 0.3 1
131 . 25 GLN H H 7.88 0.03 1
132 . 25 GLN HA H 4.40 0.03 1
133 . 25 GLN HB2 H 2.05 0.03 1
134 . 25 GLN HB3 H 1.95 0.03 1
135 . 25 GLN HG2 H 2.27 0.03 1
136 . 25 GLN HG3 H 2.18 0.03 1
137 . 25 GLN NE2 N 112.2 0.3 1
138 . 25 GLN HE21 H 7.50 0.03 1
139 . 25 GLN HE22 H 6.63 0.03 1
140 . 26 VAL N N 120.0 0.3 1
141 . 26 VAL H H 7.74 0.03 1
142 . 26 VAL HA H 3.10 0.03 1
143 . 26 VAL HB H 1.77 0.03 1
144 . 26 VAL HG1 H 0.80 0.03 1
145 . 26 VAL HG2 H 0.69 0.03 1
146 . 27 GLY N N 117.7 0.3 1
147 . 27 GLY H H 9.19 0.03 1
148 . 27 GLY HA2 H 4.43 0.03 1
149 . 27 GLY HA3 H 3.80 0.03 1
150 . 28 SER N N 119.1 0.3 1
151 . 28 SER H H 8.29 0.03 1
152 . 28 SER HA H 4.59 0.03 1
153 . 28 SER HB2 H 4.08 0.03 1
154 . 29 ARG N N 120.9 0.3 1
155 . 29 ARG H H 8.54 0.03 1
156 . 29 ARG HA H 5.68 0.03 1
157 . 29 ARG HB2 H 1.83 0.03 1
158 . 29 ARG HB3 H 1.77 0.03 1
159 . 29 ARG HG2 H 1.69 0.03 1
160 . 29 ARG HG3 H 1.53 0.03 1
161 . 29 ARG HD2 H 3.15 0.03 1
162 . 30 ILE N N 117.2 0.3 1
163 . 30 ILE H H 8.81 0.03 1
164 . 30 ILE HA H 4.94 0.03 1
165 . 30 ILE HB H 1.30 0.03 1
166 . 30 ILE HG12 H 0.57 0.03 1
167 . 30 ILE HG13 H 0.43 0.03 1
168 . 30 ILE HG2 H 0.61 0.03 1
169 . 30 ILE HD1 H -0.59 0.03 1
170 . 31 THR N N 111.0 0.3 1
171 . 31 THR H H 8.00 0.03 1
172 . 31 THR HA H 5.17 0.03 1
173 . 31 THR HB H 4.27 0.03 1
174 . 31 THR HG2 H 1.10 0.03 1
175 . 32 TYR N N 118.7 0.3 1
176 . 32 TYR H H 8.47 0.03 1
177 . 32 TYR HA H 5.40 0.03 1
178 . 32 TYR HB2 H 2.62 0.03 1
179 . 32 TYR HB3 H 2.38 0.03 1
180 . 32 TYR HD1 H 6.61 0.03 1
181 . 32 TYR HE1 H 6.43 0.03 1
182 . 33 SER N N 113.6 0.3 1
183 . 33 SER H H 8.85 0.03 1
184 . 33 SER HA H 4.64 0.03 1
185 . 33 SER HB2 H 3.96 0.03 1
186 . 33 SER HB3 H 3.84 0.03 1
187 . 33 SER HG H 6.63 0.03 1
188 . 34 CYS N N 116.5 0.3 1
189 . 34 CYS H H 8.68 0.03 1
190 . 34 CYS HA H 5.41 0.03 1
191 . 34 CYS HB2 H 2.90 0.03 1
192 . 34 CYS HB3 H 2.48 0.03 1
193 . 35 THR N N 116.5 0.3 1
194 . 35 THR H H 8.48 0.03 1
195 . 35 THR HA H 4.22 0.03 1
196 . 35 THR HB H 4.07 0.03 1
197 . 35 THR HG2 H 1.10 0.03 1
198 . 35 THR HG1 H 6.61 0.03 1
199 . 36 THR N N 117.4 0.3 1
200 . 36 THR H H 8.11 0.03 1
201 . 36 THR HB H 4.06 0.03 1
202 . 36 THR HG2 H 1.25 0.03 1
203 . 36 THR HG1 H 6.64 0.03 1
204 . 37 GLY HA2 H 4.11 0.03 1
205 . 37 GLY HA3 H 3.64 0.03 1
206 . 38 HIS N N 117.4 0.3 1
207 . 38 HIS H H 7.93 0.03 1
208 . 38 HIS HA H 5.11 0.03 1
209 . 38 HIS HB2 H 3.14 0.03 1
210 . 38 HIS HB3 H 2.50 0.03 1
211 . 38 HIS HD2 H 6.51 0.03 1
212 . 39 ARG N N 122.5 0.3 1
213 . 39 ARG H H 9.42 0.03 1
214 . 39 ARG HA H 4.62 0.03 1
215 . 39 ARG HB2 H 1.72 0.03 1
216 . 39 ARG HB3 H 1.67 0.03 1
217 . 39 ARG HE H 7.81 0.03 1
218 . 39 ARG HG2 H 1.53 0.03 1
219 . 39 ARG HD2 H 3.11 0.03 1
220 . 40 LEU N N 112.9 0.3 1
221 . 40 LEU H H 8.33 0.03 1
222 . 40 LEU HA H 4.61 0.03 1
223 . 40 LEU HB2 H 1.61 0.03 1
224 . 40 LEU HB3 H 1.48 0.03 1
225 . 40 LEU HG H 1.16 0.03 1
226 . 40 LEU HD1 H 0.67 0.03 1
227 . 40 LEU HD2 H 0.42 0.03 1
228 . 41 ILE N N 115.1 0.3 1
229 . 41 ILE H H 9.36 0.03 1
230 . 41 ILE HA H 4.25 0.03 1
231 . 41 ILE HB H 1.87 0.03 1
232 . 41 ILE HG12 H 1.32 0.03 1
233 . 41 ILE HG13 H 1.15 0.03 1
234 . 41 ILE HG2 H 0.77 0.03 1
235 . 41 ILE HD1 H 0.67 0.03 1
236 . 42 GLY N N 117.2 0.3 1
237 . 42 GLY H H 8.39 0.03 1
238 . 42 GLY HA2 H 4.46 0.03 1
239 . 42 GLY HA3 H 3.49 0.03 1
240 . 43 HIS N N 120.9 0.3 1
241 . 43 HIS H H 8.80 0.03 1
242 . 43 HIS HB2 H 3.43 0.03 1
243 . 43 HIS HB3 H 3.14 0.03 1
244 . 43 HIS HD2 H 7.39 0.03 1
245 . 43 HIS HE1 H 8.29 0.03 1
246 . 44 SER N N 116.8 0.3 1
247 . 44 SER H H 9.00 0.03 1
248 . 44 SER HA H 4.30 0.03 1
249 . 44 SER HB2 H 3.90 0.03 1
250 . 45 SER N N 115.2 0.3 1
251 . 45 SER H H 7.75 0.03 1
252 . 45 SER HA H 5.30 0.03 1
253 . 45 SER HB2 H 3.92 0.03 1
254 . 45 SER HB3 H 3.87 0.03 1
255 . 46 ALA N N 121.6 0.3 1
256 . 46 ALA H H 8.33 0.03 1
257 . 46 ALA HA H 4.65 0.03 1
258 . 46 ALA HB H 1.56 0.03 1
259 . 47 GLU N N 119.8 0.3 1
260 . 47 GLU H H 8.87 0.03 1
261 . 47 GLU HA H 5.54 0.03 1
262 . 47 GLU HB2 H 1.86 0.03 1
263 . 47 GLU HG2 H 2.07 0.03 1
264 . 48 CYS N N 111.2 0.3 1
265 . 48 CYS H H 8.66 0.03 1
266 . 48 CYS HA H 4.04 0.03 1
267 . 48 CYS HB2 H 2.72 0.03 1
268 . 48 CYS HB3 H 1.67 0.03 1
269 . 49 ILE N N 114.1 0.3 1
270 . 49 ILE H H 8.86 0.03 1
271 . 49 ILE HA H 4.54 0.03 1
272 . 49 ILE HB H 1.66 0.03 1
273 . 49 ILE HG12 H 0.99 0.03 1
274 . 49 ILE HG13 H 0.85 0.03 1
275 . 49 ILE HG2 H 0.77 0.03 1
276 . 49 ILE HD1 H 0.67 0.03 1
277 . 50 LEU N N 122.5 0.3 1
278 . 50 LEU H H 8.25 0.03 1
279 . 50 LEU HA H 4.61 0.03 1
280 . 50 LEU HG H 1.31 0.03 1
281 . 50 LEU HB2 H 1.58 0.03 1
282 . 50 LEU HD1 H 0.68 0.03 1
283 . 51 SER N N 121.4 0.3 1
284 . 51 SER H H 8.51 0.03 1
285 . 51 SER HA H 4.60 0.03 1
286 . 51 SER HB2 H 3.73 0.03 1
287 . 51 SER HB3 H 3.63 0.03 1
288 . 51 SER HG H 7.00 0.03 1
289 . 52 GLY HA2 H 3.95 0.03 1
290 . 52 GLY HA3 H 3.61 0.03 1
291 . 53 ASN HA H 4.68 0.03 1
292 . 53 ASN HB2 H 2.89 0.03 1
293 . 53 ASN HB3 H 2.75 0.03 1
294 . 53 ASN ND2 N 113.0 0.3 1
295 . 53 ASN HD21 H 7.49 0.03 1
296 . 53 ASN HD22 H 6.82 0.03 1
297 . 54 THR N N 114.9 0.3 1
298 . 54 THR H H 7.80 0.03 1
299 . 54 THR HA H 4.40 0.03 1
300 . 54 THR HB H 4.06 0.03 1
301 . 54 THR HG2 H 1.09 0.03 1
302 . 55 ALA N N 114.5 0.3 1
303 . 55 ALA H H 8.41 0.03 1
304 . 55 ALA HA H 5.10 0.03 1
305 . 55 ALA HB H 0.80 0.03 1
306 . 56 HIS N N 120.9 0.3 1
307 . 56 HIS H H 9.08 0.03 1
308 . 56 HIS HA H 4.68 0.03 1
309 . 56 HIS HB2 H 3.16 0.03 1
310 . 56 HIS HB3 H 3.07 0.03 1
311 . 56 HIS HD2 H 7.00 0.03 1
312 . 56 HIS HE1 H 8.33 0.03 1
313 . 57 TRP N N 122.6 0.3 1
314 . 57 TRP H H 8.45 0.03 1
315 . 57 TRP HA H 4.98 0.03 1
316 . 57 TRP HB2 H 3.32 0.03 1
317 . 57 TRP HB3 H 3.16 0.03 1
318 . 57 TRP HD1 H 7.41 0.03 1
319 . 57 TRP NE1 N 128.7 0.3 1
320 . 57 TRP HE1 H 10.38 0.03 1
321 . 57 TRP HE3 H 7.12 0.03 1
322 . 57 TRP HZ2 H 7.17 0.03 1
323 . 57 TRP HZ3 H 6.91 0.03 1
324 . 57 TRP HH2 H 6.89 0.03 1
325 . 58 SER N N 118.4 0.3 1
326 . 58 SER H H 9.68 0.03 1
327 . 58 SER HA H 3.93 0.03 1
328 . 58 SER HB2 H 4.19 0.03 1
329 . 58 SER HB3 H 4.14 0.03 1
330 . 59 THR N N 112.0 0.3 1
331 . 59 THR H H 7.22 0.03 1
332 . 59 THR HA H 4.65 0.03 1
333 . 59 THR HB H 4.19 0.03 1
334 . 59 THR HG2 H 0.91 0.03 1
335 . 60 LYS N N 122.8 0.3 1
336 . 60 LYS H H 8.31 0.03 1
337 . 60 LYS HA H 4.53 0.03 1
338 . 60 LYS HB2 H 1.82 0.03 1
339 . 60 LYS HG2 H 1.55 0.03 1
340 . 60 LYS HD2 H 1.72 0.03 1
341 . 61 PRO HG2 H 1.97 0.03 1
342 . 61 PRO HG3 H 1.82 0.03 1
343 . 61 PRO HD2 H 3.81 0.03 1
344 . 61 PRO HD3 H 3.52 0.03 1
345 . 62 PRO HA H 4.59 0.03 1
346 . 62 PRO HB2 H 1.88 0.03 1
347 . 62 PRO HB3 H 1.50 0.03 1
348 . 63 ILE N N 112.8 0.3 1
349 . 63 ILE H H 7.86 0.03 1
350 . 63 ILE HA H 4.36 0.03 1
351 . 63 ILE HB H 1.74 0.03 1
352 . 63 ILE HG12 H 1.36 0.03 1
353 . 63 ILE HG13 H 1.12 0.03 1
354 . 63 ILE HG2 H 0.83 0.03 1
355 . 64 CYS N N 122.9 0.3 1
356 . 64 CYS H H 8.86 0.03 1
357 . 64 CYS HA H 5.32 0.03 1
358 . 64 CYS HB2 H 3.12 0.03 1
359 . 64 CYS HB3 H 2.33 0.03 1
360 . 65 GLN N N 110.9 0.3 1
361 . 65 GLN H H 9.13 0.03 1
362 . 65 GLN HA H 4.64 0.03 1
363 . 65 GLN HB2 H 2.00 0.03 1
364 . 65 GLN HB3 H 1.84 0.03 1
365 . 65 GLN NE2 N 111.9 0.3 1
366 . 65 GLN HE21 H 7.43 0.03 1
367 . 65 GLN HE22 H 6.77 0.03 1
368 . 65 GLN HG2 H 2.30 0.03 1
369 . 66 ARG N N 114.8 0.3 1
370 . 66 ARG H H 9.12 0.03 1
371 . 66 ARG HA H 3.72 0.03 1
372 . 66 ARG HG2 H 1.35 0.03 1
373 . 66 ARG HG3 H 1.23 0.03 1
374 . 66 ARG HB2 H 1.62 0.03 1
375 . 66 ARG HD2 H 2.99 0.03 1
376 . 67 ILE N N 113.8 0.3 1
377 . 67 ILE H H 7.90 0.03 1
378 . 67 ILE HA H 4.17 0.03 1
379 . 67 ILE HB H 1.58 0.03 1
380 . 67 ILE HG12 H 1.37 0.03 1
381 . 67 ILE HG13 H 0.83 0.03 1
382 . 67 ILE HG2 H 0.87 0.03 1
383 . 67 ILE HD1 H 0.68 0.03 1
384 . 68 PRO HG2 H 1.96 0.03 1
385 . 68 PRO HG3 H 1.83 0.03 1
386 . 68 PRO HD2 H 3.83 0.03 1
387 . 68 PRO HD3 H 3.58 0.03 1
stop_
save_
save_chemical_shift_set_2
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'15N HSQC'
'2D NOESY'
'2D TOCSY'
'2D RSCUBACOSY'
'3D 15N HSQC-TOCSY'
'3D 15N HSQC-NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'Complement receptor type 1'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 17 MET N N 115.7 0.3 1
2 . 17 MET H H 8.75 0.03 1
3 . 17 MET HA H 4.91 0.03 1
4 . 18 VAL N N 123.7 0.3 1
5 . 18 VAL H H 8.75 0.03 1
6 . 18 VAL HA H 4.48 0.03 1
7 . 18 VAL HB H 1.75 0.03 1
8 . 18 VAL HG1 H 0.58 0.03 1
9 . 18 VAL HG2 H 0.21 0.03 1
10 . 66 ARG N N 115.0 0.3 1
11 . 66 ARG H H 9.01 0.03 1
12 . 66 ARG HA H 3.86 0.03 1
13 . 66 ARG HB2 H 1.62 0.03 1
stop_
save_
save_chemical_shift_set_3
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
'15N HSQC'
'2D NOESY'
'2D TOCSY'
'2D RSCUBACOSY'
'3D 15N HSQC-TOCSY'
'3D 15N HSQC-NOESY'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'Complement receptor type 1'
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 17 MET N N 116.1 0.03 1
2 . 17 MET H H 8.80 0.3 1
stop_
save_