forked from project-gemmi/gemmi
-
Notifications
You must be signed in to change notification settings - Fork 0
/
Copy path5wkd.pdb
328 lines (328 loc) · 25.9 KB
/
5wkd.pdb
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30
31
32
33
34
35
36
37
38
39
40
41
42
43
44
45
46
47
48
49
50
51
52
53
54
55
56
57
58
59
60
61
62
63
64
65
66
67
68
69
70
71
72
73
74
75
76
77
78
79
80
81
82
83
84
85
86
87
88
89
90
91
92
93
94
95
96
97
98
99
100
101
102
103
104
105
106
107
108
109
110
111
112
113
114
115
116
117
118
119
120
121
122
123
124
125
126
127
128
129
130
131
132
133
134
135
136
137
138
139
140
141
142
143
144
145
146
147
148
149
150
151
152
153
154
155
156
157
158
159
160
161
162
163
164
165
166
167
168
169
170
171
172
173
174
175
176
177
178
179
180
181
182
183
184
185
186
187
188
189
190
191
192
193
194
195
196
197
198
199
200
201
202
203
204
205
206
207
208
209
210
211
212
213
214
215
216
217
218
219
220
221
222
223
224
225
226
227
228
229
230
231
232
233
234
235
236
237
238
239
240
241
242
243
244
245
246
247
248
249
250
251
252
253
254
255
256
257
258
259
260
261
262
263
264
265
266
267
268
269
270
271
272
273
274
275
276
277
278
279
280
281
282
283
284
285
286
287
288
289
290
291
292
293
294
295
296
297
298
299
300
301
302
303
304
305
306
307
308
309
310
311
312
313
314
315
316
317
318
319
320
321
322
323
324
325
326
327
328
HEADER PROTEIN FIBRIL 25-JUL-17 5WKD
TITLE CRYSTAL STRUCTURE OF THE SEGMENT, GNNQGSN, FROM THE LOW COMPLEXITY
TITLE 2 DOMAIN OF TDP-43, RESIDUES 300-306
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TAR DNA-BINDING PROTEIN 43;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 300-306;
COMPND 5 SYNONYM: TDP-43;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606
KEYWDS TDP-43, AMYLOID, LOW COMPLEXITY DOMAIN, PROTEIN FIBRIL
EXPDTA X-RAY DIFFRACTION
AUTHOR E.L.GUENTHER,H.TRINH,M.R.SAWAYA,D.CASCIO,D.S.EISENBERG
REVDAT 6 18-DEC-19 5WKD 1 REMARK
REVDAT 5 20-FEB-19 5WKD 1 REMARK
REVDAT 4 20-JUN-18 5WKD 1 JRNL
REVDAT 3 06-JUN-18 5WKD 1 JRNL
REVDAT 2 30-MAY-18 5WKD 1 JRNL
REVDAT 1 18-APR-18 5WKD 0
JRNL AUTH E.L.GUENTHER,Q.CAO,H.TRINH,J.LU,M.R.SAWAYA,D.CASCIO,
JRNL AUTH 2 D.R.BOYER,J.A.RODRIGUEZ,M.P.HUGHES,D.S.EISENBERG
JRNL TITL ATOMIC STRUCTURES OF TDP-43 LCD SEGMENTS AND INSIGHTS INTO
JRNL TITL 2 REVERSIBLE OR PATHOGENIC AGGREGATION.
JRNL REF NAT. STRUCT. MOL. BIOL. V. 25 463 2018
JRNL REFN ESSN 1545-9985
JRNL PMID 29786080
JRNL DOI 10.1038/S41594-018-0064-2
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 3 NUMBER OF REFLECTIONS : 345
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 6.000
REMARK 3 FREE R VALUE TEST SET COUNT : 22
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 48
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 2
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : -0.24000
REMARK 3 B33 (A**2) : 0.32000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.14000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.205
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.114
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5WKD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229073.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9791
REMARK 200 MONOCHROMATOR : SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 373
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.6
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.15800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : 0.25000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: IDEALIZED BETA STRAND
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 2.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS PROPANE, PH 7.5, 200 MM
REMARK 280 SODIUM SULFATE, 20% PEG3350, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 25.17350
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 2.38850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 25.17350
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 2.38850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 4.77700
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 9.55400
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 1.000000 0.000000 -4.77700
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 -9.55400
REMARK 350 BIOMT3 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 6 -1.000000 0.000000 0.000000 25.17350
REMARK 350 BIOMT2 6 0.000000 1.000000 0.000000 2.38850
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 7 -1.000000 0.000000 0.000000 25.17350
REMARK 350 BIOMT2 7 0.000000 1.000000 0.000000 7.16550
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 8 -1.000000 0.000000 0.000000 25.17350
REMARK 350 BIOMT2 8 0.000000 1.000000 0.000000 11.94250
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 9 -1.000000 0.000000 0.000000 25.17350
REMARK 350 BIOMT2 9 0.000000 1.000000 0.000000 -2.38850
REMARK 350 BIOMT3 9 0.000000 0.000000 -1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 10 -1.000000 0.000000 0.000000 25.17350
REMARK 350 BIOMT2 10 0.000000 1.000000 0.000000 -7.16550
REMARK 350 BIOMT3 10 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 401 LIES ON A SPECIAL POSITION.
DBREF 5WKD A 300 306 UNP Q13148 TADBP_HUMAN 300 306
SEQRES 1 A 7 GLY ASN ASN GLN GLY SER ASN
FORMUL 2 HOH *2(H2 O)
CRYST1 50.347 4.777 14.746 90.00 101.73 90.00 C 1 2 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019862 0.000000 0.004125 0.00000
SCALE2 0.000000 0.209336 0.000000 0.00000
SCALE3 0.000000 0.000000 0.069262 0.00000
ATOM 1 N GLY A 300 0.958 0.885 3.506 1.00 13.41 N
ATOM 2 CA GLY A 300 2.189 0.130 3.261 1.00 11.45 C
ATOM 3 C GLY A 300 3.414 0.816 3.766 1.00 10.36 C
ATOM 4 O GLY A 300 3.427 2.050 3.946 1.00 9.06 O
ATOM 5 N ASN A 301 4.441 -0.005 3.969 1.00 8.48 N
ATOM 6 CA ASN A 301 5.752 0.443 4.412 1.00 10.23 C
ATOM 7 C ASN A 301 6.828 -0.143 3.505 1.00 8.85 C
ATOM 8 O ASN A 301 6.776 -1.337 3.163 1.00 7.98 O
ATOM 9 CB ASN A 301 6.006 -0.049 5.828 1.00 11.40 C
ATOM 10 CG ASN A 301 5.126 0.629 6.880 1.00 16.85 C
ATOM 11 OD1 ASN A 301 4.735 -0.040 7.857 1.00 24.53 O
ATOM 12 ND2 ASN A 301 4.822 1.937 6.717 1.00 15.59 N
ATOM 13 N ASN A 302 7.781 0.706 3.092 1.00 7.99 N
ATOM 14 CA ASN A 302 8.977 0.318 2.342 1.00 6.37 C
ATOM 15 C ASN A 302 10.144 0.930 3.095 1.00 5.74 C
ATOM 16 O ASN A 302 10.139 2.121 3.335 1.00 4.44 O
ATOM 17 CB ASN A 302 8.907 0.767 0.863 1.00 7.61 C
ATOM 18 CG ASN A 302 7.687 0.222 0.186 1.00 6.18 C
ATOM 19 OD1 ASN A 302 7.544 -0.988 0.138 1.00 6.49 O
ATOM 20 ND2 ASN A 302 6.752 1.071 -0.209 1.00 6.54 N
ATOM 21 N GLN A 303 11.123 0.091 3.421 1.00 5.85 N
ATOM 22 CA GLN A 303 12.339 0.491 4.084 1.00 6.53 C
ATOM 23 C GLN A 303 13.553 -0.176 3.442 1.00 7.08 C
ATOM 24 O GLN A 303 13.543 -1.391 3.298 1.00 7.14 O
ATOM 25 CB GLN A 303 12.238 0.037 5.494 1.00 7.41 C
ATOM 26 CG GLN A 303 13.445 0.409 6.333 1.00 9.08 C
ATOM 27 CD GLN A 303 13.208 0.022 7.714 1.00 9.34 C
ATOM 28 OE1 GLN A 303 13.186 -1.168 8.041 1.00 11.92 O
ATOM 29 NE2 GLN A 303 12.938 0.994 8.522 1.00 8.56 N
ATOM 30 N GLY A 304 14.611 0.578 3.107 1.00 6.92 N
ATOM 31 CA GLY A 304 15.837 -0.029 2.607 1.00 7.01 C
ATOM 32 C GLY A 304 17.086 0.682 3.069 1.00 8.20 C
ATOM 33 O GLY A 304 17.093 1.900 3.287 1.00 9.03 O
ATOM 34 N SER A 305 18.183 -0.053 3.159 1.00 8.14 N
ATOM 35 CA SER A 305 19.433 0.516 3.537 1.00 7.93 C
ATOM 36 C SER A 305 20.546 -0.109 2.760 1.00 7.64 C
ATOM 37 O SER A 305 20.581 -1.341 2.608 1.00 5.66 O
ATOM 38 CB SER A 305 19.664 0.285 5.045 1.00 10.87 C
ATOM 39 OG SER A 305 19.910 -1.065 5.271 1.00 12.12 O
ATOM 40 N ASN A 306 21.497 0.739 2.326 1.00 7.94 N
ATOM 41 CA ASN A 306 22.687 0.282 1.614 1.00 9.04 C
ATOM 42 C ASN A 306 23.906 0.883 2.357 1.00 15.55 C
ATOM 43 O ASN A 306 23.769 1.630 3.382 1.00 18.57 O
ATOM 44 CB ASN A 306 22.679 0.726 0.136 1.00 9.12 C
ATOM 45 CG ASN A 306 21.520 0.146 -0.601 1.00 10.74 C
ATOM 46 OD1 ASN A 306 21.411 -1.102 -0.709 1.00 15.42 O
ATOM 47 ND2 ASN A 306 20.643 1.001 -1.125 1.00 10.39 N
ATOM 48 OXT ASN A 306 25.061 0.620 1.925 1.00 21.94 O
TER 49 ASN A 306
HETATM 50 O HOH A 401 25.165 2.934 0.008 0.50 23.31 O
HETATM 51 O HOH A 402 12.554 -2.226 0.065 1.00 13.65 O
MASTER 234 0 0 0 0 0 0 6 50 1 0 1
END