Detailed results of BER31_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 >>>----------+
| |
| BER31_XRay_em_bcr3_noHs_000.rin 0.0 118 residues |
| |
+| Ramachandran plot: 87.5% core 12.5% allow 0.0% gener 0.0% disall |
| |
*| All Ramachandrans: 5 labelled residues (out of 114) |
*| Chi1-chi2 plots: 2 labelled residues (out of 48) |
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
Model Secondary Structures from Procheck
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
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
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
8 -2.67
9 -0.60
10 -0.17
11 -0.37
12 -0.13
13 0.34
14 -1.29
15 0.05
16 -0.76
17 0.58
18 -0.36
19 -0.56
20 0.63
21 -0.40
22 0.31
23 -0.73
24 0.57
25 0.45
26 -1.47
27 0.38
28 -0.35
29 -0.16
30 -1.00
31 -0.55
32 -0.16
33 -1.01
34 -0.39
35 -1.68
36 -1.81
37 0.07
38 -0.69
39 -0.62
40 -1.44
41 -1.21
42 -0.72
43 0.11
44 -1.57
45 -3.26
46 -0.87
47 -3.12
48 -0.79
49 -1.52
50 0.54
51 -1.63
52 -0.09
53 0.40
54 -0.17
55 1.19
56 0.84
57 1.13
58 0.74
59 0.74
60 0.36
61 0.54
62 -3.49
63 -2.47
89 -4.51
90 -0.20
91 0.08
92 -0.48
93 -0.20
94 -0.43
95 -1.71
96 -3.27
97 -1.58
98 0.60
99 -0.72
100 -0.41
101 -0.76
102 -0.27
103 -0.08
104 -0.23
105 0.00
106 -0.27
107 -1.47
108 -1.37
109 1.01
110 -1.57
111 0.82
112 0.85
113 -0.49
114 -1.02
115 0.82
116 0.05
117 -0.83
118 0.08
119 -1.02
120 -0.83
121 -0.94
122 -0.80
123 0.84
124 0.97
125 -0.21
126 0.66
127 0.66
128 0.84
129 0.48
130 0.62
131 1.11
132 0.37
133 0.50
134 0.53
135 0.58
136 -1.69
137 -0.17
138 -0.57
139 -1.76
140 0.08
141 -0.19
142 0.04
143 -0.91
144 -0.58
145 -0.08
146 -2.24
#Reported_Model_Average -0.452
#Overall_Average_Reported -0.452
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
7 0.00
8 -2.67
9 -0.74
10 -0.17
11 -1.67
12 0.41
13 -0.27
14 -0.45
15 0.17
16 -0.76
17 -1.81
18 -0.36
19 -0.10
20 0.63
21 -0.80
22 -0.03
23 0.05
24 0.01
25 0.48
26 -0.12
27 0.07
28 0.18
29 0.20
30 -0.86
31 -0.19
32 -0.16
33 -0.58
34 -0.39
35 -0.78
36 -1.81
37 0.07
38 0.09
39 -0.62
40 -1.44
41 -0.17
42 -0.72
43 0.04
44 -1.74
45 -3.26
46 -0.45
47 -1.67
48 -0.79
49 -1.52
50 0.54
51 -2.68
52 0.23
53 -0.24
54 -0.17
55 0.24
56 0.09
57 0.21
58 0.31
59 -0.98
60 0.36
61 0.54
62 -3.49
63 -2.47
64 0.00
88 0.00
89 -4.51
90 -0.99
91 -0.50
92 -0.61
93 -0.40
94 -0.08
95 -1.71
96 -1.39
97 -1.58
98 0.47
99 -0.72
100 -1.55
101 -1.04
102 -1.03
103 0.24
104 -0.23
105 0.00
106 -0.27
107 -1.38
108 -0.70
109 0.51
110 -1.57
111 0.69
112 0.69
113 -0.49
114 -0.42
115 0.82
116 0.01
117 -0.83
118 -0.50
119 -0.20
120 -0.83
121 -0.37
122 -0.86
123 0.66
124 0.29
125 -0.21
126 0.66
127 0.66
128 0.43
129 0.68
130 0.31
131 0.60
132 0.64
133 0.20
134 0.67
135 0.58
136 -1.39
137 -0.17
138 -0.09
139 -1.76
140 -0.50
141 0.20
142 -0.52
143 -0.91
144 -1.19
145 -0.07
146 -2.24
147 0.00
#Reported_Model_Average -0.475
#Overall_Average_Reported -0.475
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
7 0.25
8 0.14
9 0.08
10 0.14
11 -0.68
12 0.51
13 0.08
14 1.18
15 0.95
16 0.14
17 1.09
18 1.75
19 0.23
20 1.10
21 1.09
22 1.50
23 -0.42
24 1.18
25 0.51
26 -0.03
27 -1.66
28 0.19
29 0.37
30 0.34
31 0.20
32 0.49
33 1.50
34 0.59
35 0.96
36 0.49
37 0.64
38 0.28
39 1.10
40 0.25
41 1.00
42 0.14
43 0.65
44 0.96
45 0.44
46 1.00
47 -0.03
48 0.00
49 0.64
50 0.14
51 0.51
52 0.93
53 0.08
54 0.76
55 0.16
56 0.16
57 1.30
58 -0.32
59 0.62
60 0.76
61 0.76
62 1.10
63 0.00
64 0.14
88 0.14
89 -0.11
90 0.28
91 0.44
92 1.07
93 1.07
94 1.18
95 1.75
96 0.55
97 1.10
98 -0.41
99 -0.41
100 0.25
101 0.20
102 -1.14
103 1.06
104 1.10
105 -0.25
106 0.00
107 0.16
108 0.30
109 0.56
110 -0.25
111 1.30
112 -0.46
113 0.14
114 -0.83
115 1.10
116 0.66
117 1.75
118 1.18
119 0.41
120 0.59
121 -0.68
122 0.51
123 0.39
124 0.62
125 -0.02
126 0.76
127 0.76
128 0.56
129 0.39
130 0.27
131 -0.58
132 -0.59
133 0.71
134 1.02
135 0.44
136 0.28
137 1.10
138 0.71
139 0.00
140 1.18
141 0.16
142 1.18
143 0.59
144 1.07
145 1.06
146 -0.11
147 0.00
#Reported_Model_Average 0.463
#Overall_Average_Reported 0.463
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
7 0.25
8 0.14
9 0.08
10 0.14
11 -0.68
12 0.51
13 0.08
14 1.18
15 0.95
16 0.14
17 1.09
18 1.75
19 0.23
20 1.10
21 1.09
22 1.50
23 -0.42
24 1.18
25 0.51
26 -0.03
27 -1.66
28 0.19
29 0.37
30 0.34
31 0.20
32 0.49
33 1.50
34 0.59
35 0.96
36 0.49
37 0.64
38 0.28
39 1.10
40 0.25
41 1.00
42 0.14
43 0.65
44 0.96
45 0.44
46 1.00
47 -0.03
48 0.00
49 0.64
50 0.14
51 0.51
52 0.93
53 0.08
54 0.76
55 0.16
56 0.16
57 1.30
58 -0.32
59 0.62
60 0.76
61 0.76
62 1.10
63 0.00
64 0.14
88 0.14
89 -0.11
90 0.28
91 0.44
92 1.07
93 1.07
94 1.18
95 1.75
96 0.55
97 1.10
98 -0.41
99 -0.41
100 0.25
101 0.20
102 -1.14
103 1.06
104 1.10
105 -0.25
106 0.00
107 0.16
108 0.30
109 0.56
110 -0.25
111 1.30
112 -0.46
113 0.14
114 -0.83
115 1.10
116 0.66
117 1.75
118 1.18
119 0.41
120 0.59
121 -0.68
122 0.51
123 0.39
124 0.62
125 -0.02
126 0.76
127 0.76
128 0.56
129 0.39
130 0.27
131 -0.58
132 -0.59
133 0.71
134 1.02
135 0.44
136 0.28
137 1.10
138 0.71
139 0.00
140 1.18
141 0.16
142 1.18
143 0.59
144 1.07
145 1.06
146 -0.11
147 0.00
#Reported_Model_Average 0.463
#Overall_Average_Reported 0.463
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
7.000 0
8.000 0
9.000 0
10.000 0
11.000 0
12.000 1
13.000 3
14.000 3
15.000 2
16.000 0
17.000 2
18.000 2
19.000 0
20.000 0
21.000 4
22.000 1
23.000 2
24.000 0
25.000 5
26.000 1
27.000 0
28.000 0
29.000 0
30.000 0
31.000 0
32.000 0
33.000 0
34.000 1
35.000 1
36.000 0
37.000 1
38.000 0
39.000 0
40.000 0
41.000 1
42.000 0
43.000 0
44.000 1
45.000 1
46.000 7
47.000 2
48.000 3
49.000 2
50.000 3
51.000 0
52.000 3
53.000 0
54.000 0
55.000 0
56.000 2
57.000 2
58.000 2
59.000 0
60.000 0
61.000 1
62.000 0
63.000 2
64.000 3
65.000 0
66.000 0
67.000 0
68.000 0
69.000 0
70.000 0
71.000 0
72.000 0
73.000 0
74.000 0
75.000 0
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 3
89.000 3
90.000 1
91.000 1
92.000 1
93.000 0
94.000 1
95.000 0
96.000 1
97.000 0
98.000 2
99.000 0
100.000 1
101.000 1
102.000 1
103.000 2
104.000 2
105.000 0
106.000 0
107.000 2
108.000 3
109.000 1
110.000 4
111.000 2
112.000 3
113.000 1
114.000 1
115.000 0
116.000 2
117.000 0
118.000 0
119.000 0
120.000 2
121.000 0
122.000 0
123.000 1
124.000 0
125.000 0
126.000 0
127.000 1
128.000 0
129.000 0
130.000 0
131.000 2
132.000 1
133.000 2
134.000 0
135.000 0
136.000 1
137.000 0
138.000 2
139.000 0
140.000 1
141.000 0
142.000 1
143.000 0
144.000 0
145.000 5
146.000 0
147.000 0
#Reported_Model_Average 0.865
#Overall_Average_Reported 0.865
List of bad contacts calculated by MAGE
/farm/software/bin/probe
: 1684:A 14 VAL H :A 131 ASN 1HD2 : -0.864: 29
: 1684:A 127 ALA 1HB :A 14 VAL 1HG1 : -0.621: 31
: 1684:A 131 ASN 1HD2 :A 14 VAL N : -0.543: 29
: 1684:A 25 ASN 1HD2 :A 13 THR H : -0.832: 29
: 1684:A 13 THR H :A 25 ASN ND2 : -0.796: 29
: 1684:A 25 ASN 1HD2 :A 12 ASN HA : -0.475: 30
: 1684:A 25 ASN 1HD2 :A 13 THR N : -0.466: 29
: 1684:A 25 ASN O :A 26 GLN 1HB : -0.424: 32
: 1684:A 96 THR HA :A 145 LEU 2HD1 : -0.807: 42
: 1684:A 145 LEU 1HD1 :A 52 ILE 1HD1 : -0.682: 42
: 1684:A 46 VAL 2HG2 :A 56 LEU 3HD1 : -0.667: 48
: 1684:A 46 VAL CG1 :A 145 LEU 1HD2 : -0.664: 49
: 1684:A 49 PRO HA :A 52 ILE 2HD1 : -0.651: 50
: 1684:A 46 VAL CG2 :A 56 LEU 3HD1 : -0.644: 48
: 1684:A 52 ILE CD1 :A 49 PRO HA : -0.605: 50
: 1684:A 145 LEU 1HD2 :A 46 VAL 2HG1 : -0.517: 49
: 1684:A 46 VAL 2HG1 :A 47 GLN N : -0.475: 55
: 1684:A 47 GLN N :A 46 VAL CG1 : -0.447: 55
: 1684:A 46 VAL 2HG1 :A 145 LEU CD2 : -0.414: 49
: 1684:A 89 PRO 2HD :A 88 ALA N : -0.792: 57
: 1684:A 89 PRO CD :A 88 ALA N : -0.649: 57
: 1684:A 64 ALA 3HB :A 63 LEU O : -0.593: 83
: 1684:A 64 ALA O :A 88 ALA 3HB : -0.572: 86
: 1684:A 108 VAL O :A 112 LEU HG : -0.555: 71
: 1684:A 116 VAL 2HG2 :A 89 PRO 1HD : -0.447: 54
: 1684:A 108 VAL O :A 108 VAL CG1 : -0.440: 64
: 1684:A 63 LEU O :A 64 ALA CB : -0.431: 83
: 1684:A 112 LEU C :A 114 MET N : -0.422: 62
: 1684:A 116 VAL O :A 112 LEU 3HD2 : -0.409: 76
: 1684:A 18 GLY 2HA :A 21 TYR CE2 : -0.759: 51
: 1684:A 18 GLY 2HA :A 21 TYR CZ : -0.679: 51
: 1684:A 21 TYR CD1 :A 21 TYR C : -0.405: 41
: 1684:A 113 ALA 3HB :A 110 PRO O : -0.746: 62
: 1684:A 58 GLN OE1 :A 110 PRO 1HB : -0.559: 71
: 1684:A 110 PRO C :A 109 ARG O : -0.465: 63
: 1684:A 58 GLN OE1 :A 110 PRO CB : -0.437: 71
: 1684:A 102 LEU 2HD1 :A 103 LEU N : -0.687: 54
: 1684:A 120 ALA 2HB :A 103 LEU CD1 : -0.434: 45
: 1684:A 120 ALA HA :A 94 VAL O : -0.432: 32
: 1684:A 61 ALA 2HB :A 92 LEU 2HD2 : -0.653: 50
: 1684:A 104 GLY N :A 107 GLN 2HG : -0.647: 65
: 1684:A 107 GLN 2HG :A 104 GLY H : -0.618: 65
: 1684:A 17 TYR N :A 17 TYR CD1 : -0.643: 76
: 1684:A 15 THR CG2 :A 23 GLU OE1 : -0.596: 51
: 1684:A 23 GLU OE1 :A 15 THR 1HG2 : -0.426: 51
: 1684:A 37 PRO 2HD :A 140 VAL O : -0.573: 43
: 1684:A 50 ALA N :A 48 ARG C : -0.569: 51
: 1684:A 48 ARG C :A 50 ALA H : -0.565: 51
: 1684:A 50 ALA N :A 48 ARG O : -0.525: 51
: 1684:A 35 PHE 2HB :A 41 VAL HA : -0.557: 36
: 1684:A 100 GLN 1HG :A 101 HIS N : -0.505: 47
: 1684:A 138 ARG 2HD :A 133 LEU 2HD2 : -0.490: 61
: 1684:A 138 ARG CD :A 133 LEU 2HD2 : -0.435: 61
: 1684:A 90 GLU 2HB :A 91 VAL 3HG2 : -0.486: 51
: 1684:A 22 ILE 1HD1 :A 123 THR 2HG2 : -0.483: 45
: 1684:A 34 ALA HA :A 142 VAL O : -0.450: 32
: 1684:A 98 ARG HE :A 98 ARG 2HB : -0.440: 54
: 1684:A 132 ILE O :A 136 GLU 1HG : -0.439: 40
: 1684:A 57 LEU 2HD1 :A 57 LEU HA : -0.431: 48
: 1684:A 44 TRP HA :A 45 PRO 2HD : -0.411: 45
: 1684:A 111 LEU 3HD2 :A 111 LEU HA : -0.403: 56
#sum2 ::36.22 clashscore : 13.98 clashscore B<40
#summary::1684 atoms:787 atoms B<40:190554 potential dots:11910.0 A^2:61 bumps:11 bumps B<40:322.5 score
Output from PDB validation software
Summary from PDB validation
May. 9, 21:28:43 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 0.009 Angstroms
The following table contains a list of the covalent bonds
greater than 6.0*RMSD.
Deviation Residue Chain Sequence AT1 - AT2 Bond Dictionary
Name ID Number Distance Value
------------------------------------------------------------------------
-0.061 VAL A 46 CA - C 1.464 1.525
*** Covalent Angle Values:
The RMS deviation for covalent angles relative to the standard
dictionary is 1.7 degrees.
All covalent bond angles lie within a 6.0*RMSD range about the
standard dictionary values.
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
MSE( A-143 )
LYS( A-142 )
LEU( A-141 )
HIS( A-140 )
THR( A-139 )
ASP( A-138 )
PRO( A-137 )
ALA( A-136 )
THR( A-135 )
ALA( A-134 )
LEU( A-133 )
ASN( A-132 )
THR( A-131 )
VAL( A-130 )
THR( A-129 )
ALA( A-128 )
TYR( A-127 )
GLY( A-126 )
ASP( A-125 )
GLY( A-124 )
TYR( A-123 )
ILE( A-122 )
GLU( A-121 )
VAL( A-120 )
ASN( A-119 )
GLN( A-118 )
VAL( A-117 )
ARG( A-116 )
PHE( A-115 )
SER( A-114 )
HIS( A-113 )
ALA( A-112 )
ILE( A-111 )
ALA( A-110 )
PHE( A-109 )
ALA( A-108 )
PRO( A-107 )
GLU( A-106 )
GLY( A-105 )
PRO( A-104 )
VAL( A-103 )
ALA( A-102 )
SER( A-101 )
TRP( A-100 )
PRO( A -99 )
VAL( A -98 )
GLN( A -97 )
ARG( A -96 )
PRO( A -95 )
ALA( A -94 )
ASP( A -93 )
ILE( A -92 )
THR( A -91 )
ALA( A -90 )
SER( A -89 )
LEU( A -88 )
LEU( A -87 )
GLN( A -86 )
GLN( A -85 )
ALA( A -84 )
ALA( A -83 )
GLY( A -82 )
LEU( A -81 )
ALA( A -80 )
GLU( A -79 )
VAL( A -78 )
VAL( A -77 )
ARG( A -76 )
ASP( A -75 )
PRO( A -74 )
LEU( A -73 )
ALA( A -72 )
PHE( A -71 )
LEU( A -70 )
ASP( A -69 )
GLU( A -68 )
PRO( A -67 )
GLU( A -66 )
ALA( A -65 )
GLY( A -64 )
ALA( A -63 )
GLY( A -62 )
ALA( A -61 )
ARG( A -60 )
PRO( A -59 )
ALA( A -58 )
ASN( A -57 )
ALA( A -56 )
PRO( A -55 )
GLU( A -54 )
VAL( A -53 )
LEU( A -52 )
LEU( A -51 )
VAL( A -50 )
GLY( A -49 )
THR( A -48 )
GLY( A -47 )
ARG( A -46 )
ARG( A -45 )
GLN( A -44 )
HIS( A -43 )
LEU( A -42 )
LEU( A -41 )
GLY( A -40 )
PRO( A -39 )
GLU( A -38 )
GLN( A -37 )
VAL( A -36 )
ARG( A -35 )
PRO( A -34 )
LEU( A -33 )
LEU( A -32 )
ALA( A -31 )
MSE( A -30 )
GLY( A -29 )
VAL( A -28 )
GLY( A -27 )
VAL( A -26 )
GLU( A -25 )
ALA( A -24 )
MSE( A -23 )
ASP( A -22 )
THR( A -21 )
GLN( A -20 )
ALA( A -19 )
ALA( A -18 )
ALA( A -17 )
ARG( A -16 )
THR( A -15 )
TYR( A -14 )
ASN( A -13 )
ILE( A -12 )
LEU( A -11 )
MSE( A -10 )
ALA( A -9 )
GLU( A -8 )
GLY( A -7 )
ARG( A -6 )
ARG( A -5 )
VAL( A -4 )
VAL( A -3 )
VAL( A -2 )
ALA( A -1 )
LEU( A 0 )
LEU( A 1 )
PRO( A 2 )
ASP( A 3 )
GLY( A 4 )
ASP( A 5 )
SER( A 6 )
SEQUENCE WARNING: Residue (A ALA 64 ) and Residue (A ALA 88 ) are not linked
Distance of C-N bond is 5.19
PDB Chain_ID: A
1 15
SEQRES: MSE LYS LEU HIS THR ASP PRO ALA THR ALA LEU ASN THR VAL THR
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
16 30
SEQRES: ALA TYR GLY ASP GLY TYR ILE GLU VAL ASN GLN VAL ARG PHE SER
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
31 45
SEQRES: HIS ALA ILE ALA PHE ALA PRO GLU GLY PRO VAL ALA SER TRP PRO
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
46 60
SEQRES: VAL GLN ARG PRO ALA ASP ILE THR ALA SER LEU LEU GLN GLN ALA
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
61 75
SEQRES: ALA GLY LEU ALA GLU VAL VAL ARG ASP PRO LEU ALA PHE LEU ASP
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
76 90
SEQRES: GLU PRO GLU ALA GLY ALA GLY ALA ARG PRO ALA ASN ALA PRO GLU
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
91 105
SEQRES: VAL LEU LEU VAL GLY THR GLY ARG ARG GLN HIS LEU LEU GLY PRO
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
106 120
SEQRES: GLU GLN VAL ARG PRO LEU LEU ALA MSE GLY VAL GLY VAL GLU ALA
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
121 135
SEQRES: MSE ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU MSE ALA
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
136 150
SEQRES: GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO ASP GLY ASP SER
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
151 165
SEQRES: PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP GLY TYR
COORDS: PRO ALA THR ALA LEU ASN THR VAL THR ALA TYR GLY ASP GLY TYR
7 21
166 180
SEQRES: ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA ILE ALA PHE ALA
COORDS: ILE GLU VAL ASN GLN VAL ARG PHE SER HIS ALA ILE ALA PHE ALA
22 36
181 195
SEQRES: PRO GLU GLY PRO VAL ALA SER TRP PRO VAL GLN ARG PRO ALA ASP
COORDS: PRO GLU GLY PRO VAL ALA SER TRP PRO VAL GLN ARG PRO ALA ASP
37 51
196 210
SEQRES: ILE THR ALA SER LEU LEU GLN GLN ALA ALA GLY LEU ALA ALA PRO
COORDS: ILE THR ALA SER LEU LEU GLN GLN ALA ALA GLY LEU ALA ALA PRO
52 89
211 225
SEQRES: GLU VAL LEU LEU VAL GLY THR GLY ARG ARG GLN HIS LEU LEU GLY
COORDS: GLU VAL LEU LEU VAL GLY THR GLY ARG ARG GLN HIS LEU LEU GLY
90 104
226 240
SEQRES: PRO GLU GLN VAL ARG PRO LEU LEU ALA MET GLY VAL GLY VAL GLU
COORDS: PRO GLU GLN VAL ARG PRO LEU LEU ALA MET GLY VAL GLY VAL GLU
105 119
241 255
SEQRES: ALA MET ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU MET
COORDS: ALA MET ASP THR GLN ALA ALA ALA ARG THR TYR ASN ILE LEU MET
120 134
256 268
SEQRES: ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO ASP
COORDS: ALA GLU GLY ARG ARG VAL VAL VAL ALA LEU LEU PRO ASP
135 147
==> The following residues have missing atoms:
RES MOD#C SEQ ATOMS
ARG( A 48) CG CD NE CZ NH1 NH2
LEU( A 63) CG CD1 CD2
GLU( A 106) CG CD OE1 OE2
MET( A 114) SD
MET( A 121) SD
MET( A 134) SD
ARG( A 139) CG CD NE CZ NH1 NH2
ASP( A 147) CG OD1 OD2
==> The following residues have extra atoms:
RES MOD#C SEQ ATOMS
MET( A 114) SE
MET( A 121) SE
MET( A 134) SE
BER31_XRay_em_bcr3.pdb: Error: Record (RES: MSE CHNID: A SSEQ: 114) in Token 'MODRES' can not be found in coordinates
BER31_XRay_em_bcr3.pdb: Error: Record (RES: MSE CHNID: A SSEQ: 121) in Token 'MODRES' can not be found in coordinates
BER31_XRay_em_bcr3.pdb: Error: Record (RES: MSE CHNID: A SSEQ: 134) in Token 'MODRES' can not be found in coordinates
BER31_XRay_em_bcr3.pdb: Error: Record (RES: MSE CHNID: A SSEQ: 121) in Token 'SHEET' can not be found in coordinates