Detailed results of HR1958_XRay_em_bcr3 by PSVS
Output from PDBStat
Output from PROCHECK
Ramachandran Plot for all models
Text summary of Ramachandran Plot
+----------<<< P R O C H E C K S U M M A R Y >>>----------+
| |
| HR1958_XRay_em_bcr3_noHs_000.rin 0.0 136 residues |
| |
+| Ramachandran plot: 85.4% core 13.8% allow 0.8% gener 0.0% disall |
| |
+| All Ramachandrans: 3 labelled residues (out of 134) |
+| Chi1-chi2 plots: 1 labelled residues (out of 81) |
JPEG image for all model Ramachandran Plot
Residue Properties for all models
JPEG for all model Residue Properties - page $num_n
JPEG for all model Residue Properties - page $num_n
JPEG for all model Residue Properties - page $num_n
Model Secondary Structures from Procheck
JPEG for Model Secondary Structures - page $num_n
JPEG for Model Secondary Structures - page $num_n
JPEG for Model Secondary Structures - page $num_n
Ramachandran Plots for each residue
JPEG for residue Ramachandran Plots - page $num_n
JPEG for residue Ramachandran Plots - page $num_n
JPEG for residue Ramachandran Plots - page $num_n
JPEG for residue Ramachandran Plots - page $num_n
JPEG for residue Ramachandran Plots - page $num_n
JPEG for residue Ramachandran Plots - page $num_n
JPEG for residue Ramachandran Plots - page $num_n
Ramachandran analysis for each residue from Molprobity
Chi1-Chi2 Plots for each residue
JPEG for residue Chi1-Chi2 Plots - page $num_n
JPEG for residue Chi1-Chi2 Plots - page $num_n
JPEG for residue Chi1-Chi2 Plots - page $num_n
JPEG for residue Chi1-Chi2 Plots - page $num_n
JPEG for residue Chi1-Chi2 Plots - page $num_n
Procheck G-factors for phi-psi for each residue
JPEG image for residue phi-psi G-factors
Table of Procheck G-factors for phi-psi for ordered residues
#phipsi_gfactor
#Residue\Model average
5 -3.34
6 0.50
7 0.30
8 -0.65
9 0.88
10 0.70
11 -0.56
12 0.45
13 0.25
14 -0.87
15 0.05
16 -1.01
17 -2.47
18 -0.39
19 -0.44
20 0.20
21 -2.72
22 -0.14
23 0.61
24 -0.10
25 -1.28
26 0.13
27 0.42
28 0.14
29 0.25
30 -0.39
31 -3.37
32 0.05
33 0.57
34 -0.43
35 0.45
36 -0.56
37 -0.65
38 -0.06
39 -0.33
40 0.40
41 -0.47
42 -0.60
43 -1.19
44 -2.67
45 -0.51
46 0.42
47 -0.90
48 -1.49
49 -0.12
50 0.31
51 0.16
52 0.14
53 -0.10
54 -0.98
55 -2.30
56 -0.55
57 -0.06
58 -0.86
59 -0.67
60 -1.40
61 -1.60
62 -0.46
63 0.38
64 0.29
65 -0.68
66 -1.03
67 -0.50
68 -3.08
69 -0.48
70 -2.39
71 0.49
72 -0.10
73 -0.21
74 0.52
75 -0.79
76 -0.23
77 0.29
78 -0.65
79 0.01
80 0.95
81 -0.86
82 -2.24
83 -0.35
84 -0.87
85 -0.34
86 -0.36
87 -0.50
88 -2.78
89 -0.14
90 -1.27
91 -0.25
92 -0.03
93 -0.62
94 -0.97
95 -0.81
96 0.17
97 -1.25
98 0.82
99 -0.35
100 -0.94
101 -0.27
102 -0.76
103 -0.74
104 -0.46
105 -0.56
106 -2.15
107 -0.68
108 -0.29
110 -1.94
111 -0.14
112 -0.83
113 -0.66
114 0.10
115 -0.36
116 -0.52
117 -0.23
118 0.35
119 -1.57
120 0.73
121 0.03
122 -0.74
123 -0.42
124 -1.91
125 0.06
126 -0.06
127 -0.55
128 0.29
129 -0.14
130 0.20
131 -0.42
132 -0.40
133 -0.09
134 -1.12
135 -0.43
136 -0.66
137 0.40
138 -0.37
139 0.34
#Reported_Model_Average -0.503
#Overall_Average_Reported -0.503
Procheck G-factors for all dihedral angles for each residue
JPEG image for residue all dihedral G-factors
Table of Procheck G-factors for all dihedrals for ordered residues
#alldih_gfactor
#Residue\Model average
4 -1.50
5 -2.25
6 0.71
7 0.22
8 0.13
9 0.77
10 1.02
11 -0.07
12 0.45
13 0.73
14 -0.44
15 0.01
16 -0.58
17 -0.96
18 -0.39
19 -0.36
20 0.08
21 -1.38
22 -0.25
23 0.64
24 0.20
25 -0.05
26 0.13
27 0.42
28 -0.06
29 -0.02
30 0.25
31 -1.76
32 0.09
33 0.57
34 -0.23
35 0.45
36 -0.56
37 -0.08
38 0.03
39 -0.38
40 -0.24
41 -0.38
42 -0.15
43 -1.19
44 -0.93
45 -0.22
46 0.42
47 -0.76
48 -1.03
49 -0.37
50 0.61
51 0.39
52 0.13
53 0.24
54 -0.58
55 -1.13
56 0.13
57 -0.31
58 -1.48
59 0.08
60 -0.31
61 -0.58
62 0.21
63 0.72
64 0.39
65 -0.22
66 -0.08
67 -0.63
68 -2.18
69 0.16
70 -0.88
71 0.48
72 -1.20
73 0.33
74 0.40
75 -0.38
76 -0.02
77 -0.21
78 -0.76
79 -0.01
80 0.49
81 -0.30
82 -2.24
83 -0.30
84 -0.19
85 -0.36
86 -0.32
87 0.06
88 -1.97
89 -0.09
90 -0.24
91 -1.21
92 -1.61
93 -1.06
94 -1.02
95 -0.09
96 0.58
97 -0.44
98 0.82
99 0.08
100 -0.03
101 0.13
102 -1.11
103 -0.89
104 -0.02
105 0.16
106 -1.09
107 -0.68
108 -0.35
110 -1.94
111 0.60
112 -0.83
113 -0.77
114 0.26
115 0.08
116 -0.04
117 -0.03
118 0.39
119 -0.47
120 0.66
121 0.20
122 -0.74
123 -0.19
124 -2.05
125 0.23
126 -0.67
127 -0.55
128 -0.21
129 0.39
130 -0.31
131 0.12
132 -0.74
133 -0.06
134 -1.12
135 0.19
136 -0.66
137 0.34
138 0.19
139 0.15
140 1.06
#Reported_Model_Average -0.263
#Overall_Average_Reported -0.263
Output from Verify3D
Verify3D Score over a window of $winsize_s residues
JPEG image for Verify3D Score
Table of Verify3D scores for ordered residues across all models
#verify3d
#Residue\Model only_model
4 -0.94
5 0.51
6 0.77
7 1.29
8 0.29
9 0.17
10 0.34
11 0.28
12 1.10
13 0.59
14 0.41
15 1.18
16 0.09
17 -0.68
18 0.49
19 0.08
20 0.17
21 0.34
22 0.34
23 0.04
24 0.47
25 0.54
26 0.44
27 0.64
28 0.28
29 -0.26
30 0.93
31 0.81
32 0.51
33 1.10
34 0.51
35 0.44
36 0.04
37 0.08
38 0.71
39 0.83
40 0.95
41 0.55
42 0.08
43 1.10
44 -1.30
45 0.71
46 0.44
47 0.52
48 -0.42
49 0.96
50 1.50
51 1.50
52 1.28
53 0.96
54 -0.49
55 0.35
56 -0.49
57 1.18
58 0.19
59 1.50
60 0.41
61 0.84
62 1.07
63 0.08
64 1.50
65 0.52
66 0.49
67 1.09
68 0.71
69 1.18
70 0.10
71 0.79
72 1.07
73 0.35
74 1.50
75 -0.20
76 0.35
77 0.49
78 0.08
79 0.17
80 -0.10
81 0.28
82 0.64
83 -0.74
84 0.23
85 1.04
86 0.41
87 0.10
88 0.92
89 1.07
90 0.41
91 0.55
92 -0.30
93 0.77
94 -0.80
95 1.04
96 0.08
97 0.04
98 1.10
99 0.25
100 -0.68
101 0.52
102 0.00
103 0.41
104 0.41
105 1.50
106 -0.80
107 0.49
108 0.20
110 1.75
111 0.49
112 0.59
113 0.79
114 1.30
115 1.07
116 0.84
117 0.96
118 1.07
119 1.50
120 0.44
121 0.49
122 0.59
123 0.71
124 0.51
125 -0.41
126 -0.84
127 0.49
128 0.49
129 1.18
130 -2.26
131 0.49
132 1.18
133 0.49
134 0.59
135 0.41
136 1.75
137 -0.17
138 0.44
139 0.08
140 0.34
#Reported_Model_Average 0.478
#Overall_Average_Reported 0.478
Output from ProsaII
ProsaII Score over a window of $winsize_s residues
JPEG image for ProsaII Score
Table of Verify3D scores for ordered residues across all models
#verify3d
#Residue\Model only_model
4 -0.94
5 0.51
6 0.77
7 1.29
8 0.29
9 0.17
10 0.34
11 0.28
12 1.10
13 0.59
14 0.41
15 1.18
16 0.09
17 -0.68
18 0.49
19 0.08
20 0.17
21 0.34
22 0.34
23 0.04
24 0.47
25 0.54
26 0.44
27 0.64
28 0.28
29 -0.26
30 0.93
31 0.81
32 0.51
33 1.10
34 0.51
35 0.44
36 0.04
37 0.08
38 0.71
39 0.83
40 0.95
41 0.55
42 0.08
43 1.10
44 -1.30
45 0.71
46 0.44
47 0.52
48 -0.42
49 0.96
50 1.50
51 1.50
52 1.28
53 0.96
54 -0.49
55 0.35
56 -0.49
57 1.18
58 0.19
59 1.50
60 0.41
61 0.84
62 1.07
63 0.08
64 1.50
65 0.52
66 0.49
67 1.09
68 0.71
69 1.18
70 0.10
71 0.79
72 1.07
73 0.35
74 1.50
75 -0.20
76 0.35
77 0.49
78 0.08
79 0.17
80 -0.10
81 0.28
82 0.64
83 -0.74
84 0.23
85 1.04
86 0.41
87 0.10
88 0.92
89 1.07
90 0.41
91 0.55
92 -0.30
93 0.77
94 -0.80
95 1.04
96 0.08
97 0.04
98 1.10
99 0.25
100 -0.68
101 0.52
102 0.00
103 0.41
104 0.41
105 1.50
106 -0.80
107 0.49
108 0.20
110 1.75
111 0.49
112 0.59
113 0.79
114 1.30
115 1.07
116 0.84
117 0.96
118 1.07
119 1.50
120 0.44
121 0.49
122 0.59
123 0.71
124 0.51
125 -0.41
126 -0.84
127 0.49
128 0.49
129 1.18
130 -2.26
131 0.49
132 1.18
133 0.49
134 0.59
135 0.41
136 1.75
137 -0.17
138 0.44
139 0.08
140 0.34
#Reported_Model_Average 0.478
#Overall_Average_Reported 0.478
Output from MolProbity
VdW violations from MAGE
JPEG image for MAGE VdW violation
Table of MAGE VdW violations for ordered residues across all models
#mage_clash
#Residue\Model only_model
4.000 12
5.000 4
6.000 0
7.000 0
8.000 5
9.000 0
10.000 0
11.000 0
12.000 0
13.000 0
14.000 1
15.000 0
16.000 1
17.000 0
18.000 0
19.000 0
20.000 0
21.000 0
22.000 1
23.000 0
24.000 1
25.000 1
26.000 0
27.000 0
28.000 0
29.000 0
30.000 0
31.000 0
32.000 0
33.000 0
34.000 0
35.000 1
36.000 0
37.000 0
38.000 1
39.000 0
40.000 0
41.000 0
42.000 0
43.000 0
44.000 0
45.000 1
46.000 1
47.000 0
48.000 0
49.000 0
50.000 0
51.000 0
52.000 0
53.000 1
54.000 0
55.000 2
56.000 0
57.000 0
58.000 0
59.000 1
60.000 0
61.000 2
62.000 0
63.000 1
64.000 0
65.000 1
66.000 0
67.000 0
68.000 0
69.000 2
70.000 0
71.000 0
72.000 0
73.000 1
74.000 0
75.000 1
76.000 0
77.000 0
78.000 0
79.000 0
80.000 0
81.000 0
82.000 0
83.000 0
84.000 0
85.000 0
86.000 0
87.000 0
88.000 0
89.000 0
90.000 0
91.000 0
92.000 0
93.000 2
94.000 1
95.000 1
96.000 0
97.000 0
98.000 0
99.000 0
100.000 0
101.000 3
102.000 0
103.000 0
104.000 1
105.000 0
106.000 0
107.000 0
108.000 1
109.000 0
110.000 0
111.000 0
112.000 0
113.000 0
114.000 0
115.000 0
116.000 1
117.000 0
118.000 1
119.000 0
120.000 0
121.000 0
122.000 0
123.000 0
124.000 0
125.000 0
126.000 0
127.000 0
128.000 0
129.000 0
130.000 1
131.000 0
132.000 0
133.000 6
134.000 1
135.000 2
136.000 0
137.000 0
138.000 1
139.000 0
140.000 0
#Reported_Model_Average 0.467
#Overall_Average_Reported 0.467
List of bad contacts calculated by MAGE
/farm/software/bin/probe
: 2122:A 133 SER HG :A 4 ILE N : -1.063: 27
: 2122:A 133 SER 1HB :A 4 ILE 2HG2 : -0.784: 28
: 2122:A 133 SER CB :A 4 ILE 2HG2 : -0.716: 28
: 2122:A 5 ASP 2HB :A 134 ALA O : -0.654: 26
: 2122:A 5 ASP H :A 4 ILE 1HG1 : -0.643: 28
: 2122:A 4 ILE N :A 133 SER OG : -0.624: 27
: 2122:A 8 LEU HG :A 4 ILE HA : -0.557: 23
: 2122:A 4 ILE 3HG2 :A 5 ASP N : -0.521: 28
: 2122:A 8 LEU CD2 :A 4 ILE HA : -0.513: 23
: 2122:A 63 VAL HB :A 133 SER 2HB : -0.480: 14
: 2122:A 61 ARG 2HB :A 135 GLU 2HB : -0.473: 17
: 2122:A 8 LEU CG :A 4 ILE HA : -0.463: 23
: 2122:A 135 GLU HA :A 5 ASP OD1 : -0.456: 33
: 2122:A 4 ILE 2HG1 :A 8 LEU 1HD2 : -0.443: 28
: 2122:A 133 SER HA :A 4 ILE N : -0.422: 27
: 2122:A 4 ILE CA :A 8 LEU HG : -0.418: 23
: 2122:A 104 GLU CD :A 61 ARG HE : -0.416: 28
: 2122:A 35 PRO O :A 130 HIS HD2 : -0.659: 12
: 2122:A 101 GLN 1HE2 :A 69 VAL H : -0.631: 7
: 2122:A 69 VAL H :A 101 GLN NE2 : -0.417: 7
: 2122:A 101 GLN O :A 65 GLN HA : -0.406: 10
: 2122:A 108 HIS HA :A 59 ILE O : -0.570: 19
: 2122:A 46 PRO HA :A 45 PHE 2HB : -0.534: 7
: 2122:A 118 ILE HB :A 73 LYS 2HB : -0.528: 13
: 2122:A 93 LEU 2HD1 :A 93 LEU N : -0.507: 22
: 2122:A 138 VAL 2HG2 :A 55 LYS 1HD : -0.462: 24
: 2122:A 53 PHE O :A 55 LYS 1HG : -0.431: 22
: 2122:A 14 GLU 1HG :A 16 ILE 3HG2 : -0.456: 15
: 2122:A 25 HIS 2HB :A 38 PHE O : -0.439: 16
: 2122:A 116 ARG 2HB :A 75 GLU 1HB : -0.427: 10
: 2122:A 22 ASP OD2 :A 24 LYS 1HB : -0.425: 29
: 2122:A 95 HIS N :A 94 VAL 2HG2 : -0.410: 25
#sum2 ::15.08 clashscore : 15.08 clashscore B<40
#summary::2122 atoms:2122 atoms B<40:238962 potential dots:14940.0 A^2:32 bumps:32 bumps B<40:696.7 score
Output from PDB validation software
Summary from PDB validation
May. 10, 05:27:00 2013
Greetings,
[ Text modified to reflect that this was run under PSVS - Aneerban Bhattacharya: Dec 2005 ]
The following checks were made on :
-----------------------------------------
DISTANCES AND ANGLES
We have checked your intra and intermolecular distances and angles with the
procedures currently in place at PDB:
==> The following solvent molecules are further away than 3.5 Angstroms from
macromolecule atoms which are available for hydrogen bonding in the
asymmetric unit.
none
The coordinates for water molecules which could be translated back into
the asymmetric unit are listed. If you do not indicate otherwise we will
replace the solvent coordinates in the entry with the ones below:
none
==> Close contacts in same asymmetric unit. Distances smaller than 2.2
Angstroms are considered as close contacts.
none
==> Close contacts based on crystal symmetry. Distances smaller than 2.2
Angstroms are considered as close contacts.
none
==> Bond and angle checks are performed by first computing the average rms
error for all bonds and angles relative to standard values for nucleotide
units [L. Clowney et al., Geometric Parameters in Nucleic Acids: Nitrogenous
Bases, J.Am.Chem.Soc. 1996, 118, 509-518; A. Gelbin et al., Geometric
Parameters in Nucleic Acids: Sugar and Phosphate Constituents, J.Am.Chem.Soc.
1996, 118, 519-529] and amino acid units [R.A. Engh and R. Huber, Accurate
Bond and Angle Parameters for X-ray protein structure refinement, Acta
Crystallogr. 1991, A47, 392-400]. Any bond or angle which deviates from the
dictionary values by more than six times this computed rms error is
identified as an outlier.
*** Covalent Bond Lengths:
The RMS deviation for covalent bonds relative to the standard
dictionary is 0.005 Angstroms
All covalent bonds lie within a 6.0*RMSD range about the
standard dictionary values.
*** Covalent Angle Values:
The RMS deviation for covalent angles relative to the standard
dictionary is 1.3 degrees.
The following table contains a list of the covalent bond angles
greater than 6.0*RMSD.
Deviation Residue Chain Sequence AT1 - AT2 - AT3 Bond Dictionary
Name ID Number Angle Value
--------------------------------------------------------------------------------
-8.9 TRP A 39 N - CA - C 102.3 111.2
-9.1 ILE A 119 N - CA - C 102.1 111.2
TORSION ANGLES
The torsion angle distributions have been checked. The postscript file of the
conformation rings showing the torsion angle distributions will be sent in a
separate E-mail message.
CHIRALITY
The chirality has been checked and there are no incorrect carbon chiral centers.
Some of O1P and O2P atoms do not follow the convention defined in the standard
IUBMB nomenclature (Liebecq, C. Compendium of Biochemical Nomenclature and Related
Documents, 2nd ed.; Portland Press: London and Chapel Hill, 1992). If you do not
indicate otherwise, we will switch the labels of O1P and O2P as shown below.
OTHER IMPORTANT ISSUES
==> Please check carefully REMARKS 3 and 200 and fill in the parameters as
appropriate.
==> The following residues are missing:
(Note: The SEQ number starts from 1 for each chain according to SEQRES
sequence record.)
RES MOD#C SEQ
MET( A-149 )
GLY( A-148 )
HIS( A-147 )
HIS( A-146 )
HIS( A-145 )
HIS( A-144 )
HIS( A-143 )
HIS( A-142 )
SER( A-141 )
HIS( A-140 )
MET( A-139 )
ARG( A-138 )
LYS( A-137 )
ILE( A-136 )
ASP( A-135 )
LEU( A-134 )
CYS( A-133 )
LEU( A-132 )
SER( A-131 )
SER( A-130 )
GLU( A-129 )
GLY( A-128 )
SER( A-127 )
GLU( A-126 )
VAL( A-125 )
ILE( A-124 )
LEU( A-123 )
ALA( A-122 )
THR( A-121 )
SER( A-120 )
SER( A-119 )
ASP( A-118 )
GLU( A-117 )
LYS( A-116 )
HIS( A-115 )
PRO( A-114 )
PRO( A-113 )
GLU( A-112 )
ASN( A-111 )
ILE( A-110 )
ILE( A-109 )
ASP( A-108 )
GLY( A-107 )
ASN( A-106 )
PRO( A-105 )
GLU( A-104 )
THR( A-103 )
PHE( A-102 )
TRP( A-101 )
THR( A-100 )
THR( A -99 )
THR( A -98 )
GLY( A -97 )
MET( A -96 )
PHE( A -95 )
PRO( A -94 )
GLN( A -93 )
GLU( A -92 )
PHE( A -91 )
ILE( A -90 )
ILE( A -89 )
CYS( A -88 )
PHE( A -87 )
HIS( A -86 )
LYS( A -85 )
HIS( A -84 )
VAL( A -83 )
ARG( A -82 )
ILE( A -81 )
GLU( A -80 )
ARG( A -79 )
LEU( A -78 )
VAL( A -77 )
ILE( A -76 )
GLN( A -75 )
SER( A -74 )
TYR( A -73 )
PHE( A -72 )
VAL( A -71 )
GLN( A -70 )
THR( A -69 )
LEU( A -68 )
LYS( A -67 )
ILE( A -66 )
GLU( A -65 )
LYS( A -64 )
SER( A -63 )
THR( A -62 )
SER( A -61 )
LYS( A -60 )
GLU( A -59 )
PRO( A -58 )
VAL( A -57 )
ASP( A -56 )
PHE( A -55 )
GLU( A -54 )
GLN( A -53 )
TRP( A -52 )
ILE( A -51 )
GLU( A -50 )
LYS( A -49 )
ASP( A -48 )
LEU( A -47 )
VAL( A -46 )
HIS( A -45 )
THR( A -44 )
GLU( A -43 )
GLY( A -42 )
GLN( A -41 )
LEU( A -40 )
GLN( A -39 )
ASN( A -38 )
GLU( A -37 )
GLU( A -36 )
ILE( A -35 )
VAL( A -34 )
ALA( A -33 )
HIS( A -32 )
GLY( A -31 )
SER( A -30 )
ALA( A -29 )
THR( A -28 )
TYR( A -27 )
LEU( A -26 )
ARG( A -25 )
PHE( A -24 )
ILE( A -23 )
ILE( A -22 )
VAL( A -21 )
SER( A -20 )
ALA( A -19 )
PHE( A -18 )
ASP( A -17 )
HIS( A -16 )
PHE( A -15 )
ALA( A -14 )
SER( A -13 )
VAL( A -12 )
HIS( A -11 )
SER( A -10 )
VAL( A -9 )
SER( A -8 )
ALA( A -7 )
GLU( A -6 )
GLY( A -5 )
THR( A -4 )
VAL( A -3 )
VAL( A -2 )
SER( A -1 )
ASN( A 0 )
LEU( A 1 )
SER( A 2 )
SER( A 3 )
PDB Chain_ID: A
1 15
SEQRES: MET GLY HIS HIS HIS HIS HIS HIS SER HIS MET ARG LYS ILE ASP
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
16 30
SEQRES: LEU CYS LEU SER SER GLU GLY SER GLU VAL ILE LEU ALA THR SER
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
31 45
SEQRES: SER ASP GLU LYS HIS PRO PRO GLU ASN ILE ILE ASP GLY ASN PRO
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
46 60
SEQRES: GLU THR PHE TRP THR THR THR GLY MET PHE PRO GLN GLU PHE ILE
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
61 75
SEQRES: ILE CYS PHE HIS LYS HIS VAL ARG ILE GLU ARG LEU VAL ILE GLN
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
76 90
SEQRES: SER TYR PHE VAL GLN THR LEU LYS ILE GLU LYS SER THR SER LYS
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
91 105
SEQRES: GLU PRO VAL ASP PHE GLU GLN TRP ILE GLU LYS ASP LEU VAL HIS
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
106 120
SEQRES: THR GLU GLY GLN LEU GLN ASN GLU GLU ILE VAL ALA HIS GLY SER
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
121 135
SEQRES: ALA THR TYR LEU ARG PHE ILE ILE VAL SER ALA PHE ASP HIS PHE
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
136 150
SEQRES: ALA SER VAL HIS SER VAL SER ALA GLU GLY THR VAL VAL SER ASN
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
151 165
SEQRES: LEU SER SER ILE ASP LEU CYS LEU SER SER GLU GLY SER GLU VAL
COORDS: ... ... ... ILE ASP LEU CYS LEU SER SER GLU GLY SER GLU VAL
4 15
166 180
SEQRES: ILE LEU ALA THR SER SER ASP GLU LYS HIS PRO PRO GLU ASN ILE
COORDS: ILE LEU ALA THR SER SER ASP GLU LYS HIS PRO PRO GLU ASN ILE
16 30
181 195
SEQRES: ILE ASP GLY ASN PRO GLU THR PHE TRP THR THR THR GLY MET PHE
COORDS: ILE ASP GLY ASN PRO GLU THR PHE TRP THR THR THR GLY MET PHE
31 45
196 210
SEQRES: PRO GLN GLU PHE ILE ILE CYS PHE HIS LYS HIS VAL ARG ILE GLU
COORDS: PRO GLN GLU PHE ILE ILE CYS PHE HIS LYS HIS VAL ARG ILE GLU
46 60
211 225
SEQRES: ARG LEU VAL ILE GLN SER TYR PHE VAL GLN THR LEU LYS ILE GLU
COORDS: ARG LEU VAL ILE GLN SER TYR PHE VAL GLN THR LEU LYS ILE GLU
61 75
226 240
SEQRES: LYS SER THR SER LYS GLU PRO VAL ASP PHE GLU GLN TRP ILE GLU
COORDS: LYS SER THR SER LYS GLU PRO VAL ASP PHE GLU GLN TRP ILE GLU
76 90
241 255
SEQRES: LYS ASP LEU VAL HIS THR GLU GLY GLN LEU GLN ASN GLU GLU ILE
COORDS: LYS ASP LEU VAL HIS THR GLU GLY GLN LEU GLN ASN GLU GLU ILE
91 105
256 270
SEQRES: VAL ALA HIS GLY SER ALA THR TYR LEU ARG PHE ILE ILE VAL SER
COORDS: VAL ALA HIS GLY SER ALA THR TYR LEU ARG PHE ILE ILE VAL SER
106 121
271 285
SEQRES: ALA PHE ASP HIS PHE ALA SER VAL HIS SER VAL SER ALA GLU GLY
COORDS: ALA PHE ASP HIS PHE ALA SER VAL HIS SER VAL SER ALA GLU GLY
122 136
286 289
SEQRES: THR VAL VAL SER
COORDS: THR VAL VAL SER
137 140
HR1958_XRay_em_bcr3.pdb: Error: Record (RES: HOH CHNID: A SSEQ: 334) in Token 'SITE' can not be found in coordinates