Detailed results of UUR17A_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 >>>----------+
| |
| UUR17A_XRay_em_bcr3_noHs_000.rin 0.0 118 residues |
| |
+| Ramachandran plot: 85.1% core 14.9% allow 0.0% gener 0.0% disall |
| |
+| All Ramachandrans: 1 labelled residues (out of 114) |
+| Chi1-chi2 plots: 1 labelled residues (out of 89) |
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
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
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
134 -0.21
135 1.22
136 -1.12
137 -0.93
138 -1.57
139 0.37
140 -1.23
141 -0.61
142 -0.90
143 -1.26
144 -1.00
145 -3.05
146 -2.86
147 1.24
148 -0.23
149 -0.91
150 0.26
151 -0.42
152 -0.08
153 -0.77
154 -0.61
155 -1.91
156 -1.28
157 -0.67
158 -0.40
159 -0.74
160 1.22
161 -0.45
162 -1.06
163 -0.24
164 -0.20
165 0.00
166 1.19
167 1.04
168 1.01
169 0.61
170 -0.20
171 -1.19
172 -0.80
173 -0.38
174 -0.13
175 -2.67
176 0.29
177 -0.76
178 -0.14
179 -2.20
180 -0.93
181 -0.48
182 -0.34
183 -2.07
184 -0.27
185 0.13
186 -1.05
187 -0.74
188 -0.91
189 0.35
190 -0.28
191 -0.23
192 -1.93
193 -1.33
194 0.01
195 -0.51
196 0.15
197 0.42
198 0.05
199 0.91
200 -1.18
201 0.54
202 0.20
203 1.19
204 0.65
205 1.17
206 0.85
207 0.27
208 -0.83
209 0.26
210 -1.00
211 -0.67
212 -0.28
213 -1.16
217 0.42
218 -0.11
219 0.02
220 -2.57
221 0.03
222 -1.82
223 -0.20
224 0.31
225 0.60
226 0.40
227 -0.83
228 -0.04
229 -0.36
230 -0.66
231 0.08
232 -1.68
233 0.11
234 -1.08
235 -0.88
236 0.13
237 -1.38
238 -0.48
239 -0.48
240 1.14
241 -0.78
242 -0.67
243 -0.32
244 -0.20
245 0.51
246 -0.14
247 0.08
248 -1.97
249 1.11
250 -0.05
#Reported_Model_Average -0.399
#Overall_Average_Reported -0.399
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
133 -1.65
134 -0.02
135 0.91
136 0.09
137 -0.66
138 -0.73
139 -0.09
140 -1.12
141 -1.65
142 -0.14
143 -1.58
144 -0.62
145 -1.49
146 -1.39
147 0.94
148 -0.80
149 -0.73
150 -0.06
151 -0.49
152 -0.50
153 -0.77
154 -0.61
155 -0.95
156 -1.28
157 -1.27
158 0.25
159 -0.53
160 0.42
161 -0.16
162 0.06
163 0.18
164 0.08
165 0.00
166 0.58
167 1.11
168 0.96
169 0.16
170 0.55
171 -0.18
172 -1.00
173 -0.53
174 0.32
175 -2.67
176 0.56
177 -0.43
178 -0.08
179 -1.50
180 -0.15
181 -0.56
182 -0.63
183 -1.35
184 -1.48
185 -0.44
186 -0.89
187 -1.37
188 -0.62
189 0.62
190 -0.30
191 0.34
192 -1.09
193 -0.57
194 -0.28
195 0.02
196 -0.06
197 0.42
198 0.48
199 0.91
200 -2.45
201 -0.56
202 0.20
203 0.58
204 0.65
205 0.74
206 0.74
207 0.12
208 -0.83
209 0.27
210 -0.59
211 0.04
212 -0.60
213 -0.94
214 0.20
216 0.50
217 0.94
218 -0.24
219 0.60
220 -0.87
221 -0.40
222 -2.08
223 -1.21
224 0.40
225 0.71
226 0.63
227 -0.06
228 0.41
229 -0.32
230 -0.06
231 -0.50
232 -0.51
233 0.11
234 -0.13
235 -0.37
236 0.74
237 -2.04
238 -0.48
239 -0.66
240 1.14
241 -0.93
242 -0.28
243 -0.51
244 0.16
245 0.51
246 0.42
247 -0.82
248 -1.97
249 1.11
250 -0.01
251 0.88
#Reported_Model_Average -0.281
#Overall_Average_Reported -0.281
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
133 0.28
134 0.23
135 1.28
136 0.07
137 0.07
138 0.55
139 -0.09
140 0.41
141 0.51
142 0.93
143 0.24
144 1.06
145 0.47
146 0.51
147 0.55
148 0.96
149 -0.61
150 0.96
151 0.55
152 1.07
153 0.14
154 0.49
155 0.71
156 0.44
157 0.41
158 0.25
159 0.41
160 1.14
161 0.23
162 0.25
163 0.77
164 0.29
165 -0.97
166 0.47
167 0.16
168 1.11
169 0.50
170 0.66
171 -0.58
172 1.25
173 -0.43
174 0.25
175 1.10
176 1.07
177 0.41
178 1.07
179 0.10
180 -0.79
181 0.20
182 0.47
183 1.25
184 0.25
185 0.41
186 -0.59
187 1.07
188 -0.03
189 1.50
190 0.55
191 1.50
192 -0.35
193 0.00
194 0.96
195 -1.33
196 1.14
197 0.64
198 0.23
199 1.10
200 0.51
201 -0.22
202 0.63
203 -0.38
204 0.76
205 -0.48
206 0.66
207 0.32
208 1.10
209 0.55
210 1.07
211 0.35
212 1.07
213 0.49
214 1.07
216 1.07
217 0.95
218 -0.61
219 0.47
220 -0.10
221 0.51
222 0.41
223 0.25
224 0.08
225 -0.30
226 -0.30
227 0.55
228 -1.33
229 0.14
230 0.41
231 1.18
232 0.34
233 1.10
234 1.40
235 0.47
236 0.17
237 -0.26
238 0.44
239 -0.43
240 1.10
241 -0.74
242 -0.83
243 0.28
244 0.41
245 1.10
246 0.08
247 -0.94
248 0.64
249 1.10
250 -0.68
251 0.04
#Reported_Model_Average 0.386
#Overall_Average_Reported 0.386
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
133 0.28
134 0.23
135 1.28
136 0.07
137 0.07
138 0.55
139 -0.09
140 0.41
141 0.51
142 0.93
143 0.24
144 1.06
145 0.47
146 0.51
147 0.55
148 0.96
149 -0.61
150 0.96
151 0.55
152 1.07
153 0.14
154 0.49
155 0.71
156 0.44
157 0.41
158 0.25
159 0.41
160 1.14
161 0.23
162 0.25
163 0.77
164 0.29
165 -0.97
166 0.47
167 0.16
168 1.11
169 0.50
170 0.66
171 -0.58
172 1.25
173 -0.43
174 0.25
175 1.10
176 1.07
177 0.41
178 1.07
179 0.10
180 -0.79
181 0.20
182 0.47
183 1.25
184 0.25
185 0.41
186 -0.59
187 1.07
188 -0.03
189 1.50
190 0.55
191 1.50
192 -0.35
193 0.00
194 0.96
195 -1.33
196 1.14
197 0.64
198 0.23
199 1.10
200 0.51
201 -0.22
202 0.63
203 -0.38
204 0.76
205 -0.48
206 0.66
207 0.32
208 1.10
209 0.55
210 1.07
211 0.35
212 1.07
213 0.49
214 1.07
216 1.07
217 0.95
218 -0.61
219 0.47
220 -0.10
221 0.51
222 0.41
223 0.25
224 0.08
225 -0.30
226 -0.30
227 0.55
228 -1.33
229 0.14
230 0.41
231 1.18
232 0.34
233 1.10
234 1.40
235 0.47
236 0.17
237 -0.26
238 0.44
239 -0.43
240 1.10
241 -0.74
242 -0.83
243 0.28
244 0.41
245 1.10
246 0.08
247 -0.94
248 0.64
249 1.10
250 -0.68
251 0.04
#Reported_Model_Average 0.386
#Overall_Average_Reported 0.386
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
133.000 0
134.000 0
135.000 7
136.000 0
137.000 0
138.000 0
139.000 3
140.000 2
141.000 0
142.000 0
143.000 0
144.000 1
145.000 2
146.000 0
147.000 0
148.000 0
149.000 2
150.000 0
151.000 0
152.000 0
153.000 0
154.000 0
155.000 0
156.000 0
157.000 0
158.000 0
159.000 0
160.000 0
161.000 0
162.000 0
163.000 0
164.000 0
165.000 0
166.000 0
167.000 0
168.000 0
169.000 0
170.000 0
171.000 0
172.000 0
173.000 0
174.000 0
175.000 0
176.000 0
177.000 0
178.000 0
179.000 0
180.000 0
181.000 1
182.000 0
183.000 0
184.000 0
185.000 0
186.000 2
187.000 4
188.000 1
189.000 0
190.000 0
191.000 0
192.000 0
193.000 0
194.000 0
195.000 0
196.000 0
197.000 1
198.000 0
199.000 0
200.000 0
201.000 0
202.000 0
203.000 0
204.000 0
205.000 0
206.000 0
207.000 0
208.000 0
209.000 1
210.000 1
211.000 1
212.000 0
213.000 1
214.000 0
215.000 0
216.000 1
217.000 1
218.000 1
219.000 0
220.000 0
221.000 1
222.000 0
223.000 0
224.000 0
225.000 1
226.000 0
227.000 0
228.000 1
229.000 0
230.000 0
231.000 3
232.000 0
233.000 0
234.000 3
235.000 0
236.000 0
237.000 3
238.000 0
239.000 0
240.000 0
241.000 5
242.000 1
243.000 1
244.000 0
245.000 0
246.000 2
247.000 0
248.000 0
249.000 0
250.000 0
251.000 0
#Reported_Model_Average 0.454
#Overall_Average_Reported 0.454
List of bad contacts calculated by MAGE
/farm/software/bin/probe
: 1918:A 135 PHE CE2 :A 139 VAL 1HG1 : -0.842: 71
: 1918:A 139 VAL CG1 :A 135 PHE CE2 : -0.727: 71
: 1918:A 135 PHE CZ :A 139 VAL CG1 : -0.720: 70
: 1918:A 187 LEU CD1 :A 135 PHE HE1 : -0.648: 69
: 1918:A 187 LEU 3HD1 :A 135 PHE CE1 : -0.615: 69
: 1918:A 187 LEU 3HD1 :A 135 PHE HE1 : -0.588: 69
: 1918:A 187 LEU CD1 :A 135 PHE CE1 : -0.428: 69
: 1918:A 241 VAL 2HG1 :A 237 ASN 1HD2 : -0.834: 65
: 1918:A 237 ASN ND2 :A 241 VAL 2HG1 : -0.782: 65
: 1918:A 241 VAL 3HG2 :A 246 THR O : -0.510: 59
: 1918:A 241 VAL HA :A 246 THR O : -0.438: 59
: 1918:A 237 ASN ND2 :A 241 VAL CG1 : -0.425: 65
: 1918:A 211 LYS 2HE :A 197 PRO HA : -0.677: 60
: 1918:A 149 ASP OD2 :A 181 HIS HE1 : -0.672: 64
: 1918:A 145 LYS 1HB :A 144 LEU O : -0.483: 62
: 1918:A 145 LYS HA :A 149 ASP OD1 : -0.472: 62
: 1918:A 234 PHE HE2 :A 231 VAL 3HG2 : -0.650: 58
: 1918:A 231 VAL 3HG2 :A 234 PHE CE2 : -0.566: 58
: 1918:A 231 VAL CG2 :A 234 PHE HE2 : -0.524: 58
: 1918:A 213 SER HA :A 228 LEU 3HD2 : -0.618: 53
: 1918:A 221 ASN OD1 :A 218 ASP 2HB : -0.600: 73
: 1918:A 217 THR HB :A 188 ASP 2HB : -0.473: 54
: 1918:A 210 LEU N :A 209 THR 2HG2 : -0.449: 54
: 1918:A 140 ASN 2HD2 :A 140 ASN HA : -0.439: 86
: 1918:A 216 LEU N :A 225 TYR O : -0.412: 50
: 1918:A 186 GLU OE1 :A 186 GLU N : -0.400: 72
: 1918:A 243 GLU OE1 :A 242 ASP 1HB : -0.400: 50
#sum2 ::14.08 clashscore : 0.00 clashscore B<40
#summary::1918 atoms:214 atoms B<40:214132 potential dots:13380.0 A^2:27 bumps:0 bumps B<40:616.8 score
Output from PDB validation software
Summary from PDB validation
May. 11, 03:20:06 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 0.008 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 1.6 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
--------------------------------------------------------------------------------
-10.6 ILE A 191 N - CA - C 100.6 111.2
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
MSE( A 6 )
GLU( A 7 )
ASP( A 8 )
PHE( A 9 )
LYS( A 10 )
LYS( A 11 )
ILE( A 12 )
VAL( A 13 )
ASN( A 14 )
ASN( A 15 )
ILE( A 16 )
ARG( A 17 )
LEU( A 18 )
LYS( A 19 )
ASP( A 20 )
THR( A 21 )
PHE( A 22 )
ASP( A 23 )
PHE( A 24 )
LYS( A 25 )
LEU( A 26 )
ALA( A 27 )
ALA( A 28 )
PHE( A 29 )
PRO( A 30 )
ASN( A 31 )
GLN( A 32 )
ASN( A 33 )
TYR( A 34 )
ASP( A 35 )
GLN( A 36 )
LEU( A 37 )
LEU( A 38 )
PRO( A 39 )
SER( A 40 )
GLN( A 41 )
ILE( A 42 )
TYR( A 43 )
LYS( A 44 )
ASN( A 45 )
TYR( A 46 )
TYR( A 47 )
GLN( A 48 )
GLY( A 49 )
ILE( A 50 )
GLU( A 51 )
ILE( A 52 )
GLN( A 53 )
GLN( A 54 )
HIS( A 55 )
LYS( A 56 )
TYR( A 57 )
GLN( A 58 )
ASN( A 59 )
GLU( A 60 )
LEU( A 61 )
ASP( A 62 )
ILE( A 63 )
LYS( A 64 )
ILE( A 65 )
ILE( A 66 )
ASN( A 67 )
PHE( A 68 )
LEU( A 69 )
TYR( A 70 )
PRO( A 71 )
ASP( A 72 )
GLY( A 73 )
ASP( A 74 )
PHE( A 75 )
GLY( A 76 )
SER( A 77 )
ALA( A 78 )
ASN( A 79 )
LYS( A 80 )
ASN( A 81 )
GLY( A 82 )
THR( A 83 )
LEU( A 84 )
LYS( A 85 )
LEU( A 86 )
SER( A 87 )
LEU( A 88 )
MSE( A 89 )
LEU( A 90 )
THR( A 91 )
ASP( A 92 )
LYS( A 93 )
LYS( A 94 )
ASN( A 95 )
ASN( A 96 )
GLN( A 97 )
VAL( A 98 )
TYR( A 99 )
TYR( A 100 )
LYS( A 101 )
LEU( A 102 )
LEU( A 103 )
GLU( A 104 )
VAL( A 105 )
SER( A 106 )
GLY( A 107 )
PHE( A 108 )
LYS( A 109 )
SER( A 110 )
ASN( A 111 )
PRO( A 112 )
TYR( A 113 )
GLY( A 114 )
VAL( A 115 )
ASP( A 116 )
GLU( A 117 )
ASN( A 118 )
GLY( A 119 )
THR( A 120 )
ILE( A 121 )
PRO( A 122 )
GLY( A 123 )
LEU( A 124 )
GLU( A 125 )
HIS( A 126 )
HIS( A 127 )
HIS( A 128 )
HIS( A 129 )
HIS( A 130 )
HIS( A 131 )
PDB Chain_ID: A
1 15
SEQRES: MSE GLU ASP PHE LYS LYS ILE VAL ASN ASN ILE ARG LEU LYS ASP
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
16 30
SEQRES: THR PHE ASP PHE LYS LEU ALA ALA PHE PRO ASN GLN ASN TYR ASP
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
31 45
SEQRES: GLN LEU LEU PRO SER GLN ILE TYR LYS ASN TYR TYR GLN GLY ILE
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
46 60
SEQRES: GLU ILE GLN GLN HIS LYS TYR GLN ASN GLU LEU ASP ILE LYS ILE
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
61 75
SEQRES: ILE ASN PHE LEU TYR PRO ASP GLY ASP PHE GLY SER ALA ASN LYS
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
76 90
SEQRES: ASN GLY THR LEU LYS LEU SER LEU MSE LEU THR ASP LYS LYS ASN
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
91 105
SEQRES: ASN GLN VAL TYR TYR LYS LEU LEU GLU VAL SER GLY PHE LYS SER
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
106 120
SEQRES: ASN PRO TYR GLY VAL ASP GLU ASN GLY THR ILE PRO GLY LEU GLU
COORDS: ... ... ... ... ... ... ... ... ... ... ... ... ... ... ...
121 135
SEQRES: HIS HIS HIS HIS HIS HIS MSE GLU ASP PHE LYS LYS ILE VAL ASN
COORDS: ... ... ... ... ... ... MSE GLU ASP PHE LYS LYS ILE VAL ASN
132 140
136 150
SEQRES: ASN ILE ARG LEU LYS ASP THR PHE ASP PHE LYS LEU ALA ALA PHE
COORDS: ASN ILE ARG LEU LYS ASP THR PHE ASP PHE LYS LEU ALA ALA PHE
141 155
151 165
SEQRES: PRO ASN GLN ASN TYR ASP GLN LEU LEU PRO SER GLN ILE TYR LYS
COORDS: PRO ASN GLN ASN TYR ASP GLN LEU LEU PRO SER GLN ILE TYR LYS
156 170
166 180
SEQRES: ASN TYR TYR GLN GLY ILE GLU ILE GLN GLN HIS LYS TYR GLN ASN
COORDS: ASN TYR TYR GLN GLY ILE GLU ILE GLN GLN HIS LYS TYR GLN ASN
171 185
181 195
SEQRES: GLU LEU ASP ILE LYS ILE ILE ASN PHE LEU TYR PRO ASP GLY ASP
COORDS: GLU LEU ASP ILE LYS ILE ILE ASN PHE LEU TYR PRO ASP GLY ASP
186 200
196 210
SEQRES: PHE GLY SER ALA ASN LYS ASN GLY THR LEU LYS LEU SER LEU MSE
COORDS: PHE GLY SER ALA ASN LYS ASN GLY THR LEU LYS LEU SER LEU MSE
201 215
211 225
SEQRES: LEU THR ASP LYS LYS ASN ASN GLN VAL TYR TYR LYS LEU LEU GLU
COORDS: LEU THR ASP LYS LYS ASN ASN GLN VAL TYR TYR LYS LEU LEU GLU
216 230
226 240
SEQRES: VAL SER GLY PHE LYS SER ASN PRO TYR GLY VAL ASP GLU ASN GLY
COORDS: VAL SER GLY PHE LYS SER ASN PRO TYR GLY VAL ASP GLU ASN GLY
231 245
241 246
SEQRES: THR ILE PRO GLY LEU GLU
COORDS: THR ILE PRO GLY LEU GLU
246 251