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1 HEADER EXTRACELLULAR MATRIX 22-JAN-98 1A3I
2 TITLE X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A COLLAGEN-LIKE
3 TITLE 2 PEPTIDE WITH THE REPEATING SEQUENCE (PRO-PRO-GLY)
4 COMPND MOL_ID: 1;
5 COMPND 2 MOLECULE: COLLAGEN-LIKE PEPTIDE;
6 COMPND 3 CHAIN: A, B, C;
7 COMPND 4 ENGINEERED: YES
8 SOURCE MOL_ID: 1;
9 SOURCE 2 SYNTHETIC: YES
10 KEYWDS COLLAGEN, EXTRACELLULAR MATRIX
11 EXPDTA X-RAY DIFFRACTION
12 AUTHOR R.Z.KRAMER,L.VITAGLIANO,J.BELLA,R.BERISIO,L.MAZZARELLA,
13 AUTHOR 2 B.BRODSKY,A.ZAGARI,H.M.BERMAN
14 REVDAT 2 23-JUN-99 1A3I 1 JRNL
15 REVDAT 1 06-MAY-98 1A3I 0
16 JRNL AUTH R.Z.KRAMER,L.VITAGLIANO,J.BELLA,R.BERISIO,
17 JRNL AUTH 2 L.MAZZARELLA,B.BRODSKY,A.ZAGARI,H.M.BERMAN
18 JRNL TITL X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A
19 JRNL TITL 2 COLLAGEN-LIKE PEPTIDE WITH THE REPEATING SEQUENCE
20 JRNL TITL 3 (PRO-PRO-GLY)
21 JRNL REF J.MOL.BIOL. V. 280 623 1998
22 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 0070
23 REMARK 1
24 REMARK 2
25 REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
26 REMARK 3
27 REMARK 3 REFINEMENT.
28 REMARK 3 PROGRAM : X-PLOR 3.1
29 REMARK 3 AUTHORS : BRUNGER
30 REMARK 3
31 REMARK 3 DATA USED IN REFINEMENT.
32 REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
33 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.
34 REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.
35 REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1000000.
36 REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.1
37 REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 76.7
38 REMARK 3 NUMBER OF REFLECTIONS : 861
39 REMARK 3
40 REMARK 3 FIT TO DATA USED IN REFINEMENT.
41 REMARK 3 CROSS-VALIDATION METHOD : NULL
42 REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
43 REMARK 3 R VALUE (WORKING SET) : 0.181
44 REMARK 3 FREE R VALUE : NULL
45 REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
46 REMARK 3 FREE R VALUE TEST SET COUNT : NULL
47 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
48 REMARK 3
49 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
50 REMARK 3 TOTAL NUMBER OF BINS USED : 10
51 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.97
52 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.04
53 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 63.3
54 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 69.
55 REMARK 3 BIN R VALUE (WORKING SET) : 0.22
56 REMARK 3 BIN FREE R VALUE : NULL
57 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
58 REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
59 REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
60 REMARK 3
61 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
62 REMARK 3 PROTEIN ATOMS : 126
63 REMARK 3 NUCLEIC ACID ATOMS : 0
64 REMARK 3 HETEROGEN ATOMS : 0
65 REMARK 3 SOLVENT ATOMS : 45
66 REMARK 3
67 REMARK 3 B VALUES.
68 REMARK 3 FROM WILSON PLOT (A**2) : NULL
69 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.9
70 REMARK 3 OVERALL ANISOTROPIC B VALUE.
71 REMARK 3 B11 (A**2) : NULL
72 REMARK 3 B22 (A**2) : NULL
73 REMARK 3 B33 (A**2) : NULL
74 REMARK 3 B12 (A**2) : NULL
75 REMARK 3 B13 (A**2) : NULL
76 REMARK 3 B23 (A**2) : NULL
77 REMARK 3
78 REMARK 3 ESTIMATED COORDINATE ERROR.
79 REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
80 REMARK 3 ESD FROM SIGMAA (A) : NULL
81 REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
82 REMARK 3
83 REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
84 REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
85 REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
86 REMARK 3
87 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
88 REMARK 3 BOND LENGTHS (A) : 0.01
89 REMARK 3 BOND ANGLES (DEGREES) : 2.07
90 REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
91 REMARK 3 IMPROPER ANGLES (DEGREES) : 2.11
92 REMARK 3
93 REMARK 3 ISOTROPIC THERMAL MODEL : GROUP
94 REMARK 3
95 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
96 REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
97 REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
98 REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
99 REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
100 REMARK 3
101 REMARK 3 NCS MODEL : NONE
102 REMARK 3
103 REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
104 REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
105 REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
106 REMARK 3
107 REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
108 REMARK 3 PARAMETER FILE 2 : NULL
109 REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
110 REMARK 3 TOPOLOGY FILE 2 : NULL
111 REMARK 3
112 REMARK 3 OTHER REFINEMENT REMARKS: DUE TO THE QUASI-INFINITE,
113 REMARK 3 AVERAGED NATURE OF THE TRIPLE HELIX, DURING REFINEMENT
114 REMARK 3 COVALENT BONDS ARE NECESSARY TO JOIN THE MOLECULE WITH
115 REMARK 3 ITS SYMMETRY MATES BOTH ABOVE IT AND BELOW IT ALONG THE
116 REMARK 3 HELICAL AXIS AND TIGHT REFINEMENT CONSTRAINTS WERE
117 REMARK 3 MAINTAINED.
118 REMARK 4
119 REMARK 4 1A3I COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996
120 REMARK 6
121 REMARK 6 THE 21 RESIDUE ASYMMETRIC UNIT CORRESPONDS TO ONE
122 REMARK 6 TRIPLE-HELICAL REPEAT AND IS SMALLER THAN THE ENTIRE 90
123 REMARK 6 RESIDUE PEPTIDE DUE TO TRANSLATIONAL DISORDER ALONG THE
124 REMARK 6 HELICAL AXIS. THE RESULT IS A POLYMER-LIKE STRUCTURE WITH
125 REMARK 6 NO DEFINED ENDS.
126 REMARK 7
127 REMARK 7 THE POLYMER STRUCTURE IS FORMED BY CONTINUATION OF THE
128 REMARK 7 CHAINS USING THE SYMMETRY-RELATED MOLECULES ALONG THE
129 REMARK 7 HELICAL AXIS. THE TVECT RECORD BELOW PRESENTS THE
130 REMARK 7 TRANSLATION THAT WILL GENERATE THE POLYMER. NOTE:
131 REMARK 7 THEREFORE, CLOSE CONTACTS BETWEEN SYMMETRY-RELATED
132 REMARK 7 MOLECULES ARE INTENTIONAL AND NECESSARY. INTERCHAIN
133 REMARK 7 HYDROGEN BONDING AT THE END OF CHAINS ALSO UTILIZES
134 REMARK 7 SYMMETRY-RELATED MOLECULES.
135 REMARK 8
136 REMARK 8 THE ENTIRE 30 RESIDUE LONG PEPTIDE CAN BE GENERATED FROM
137 REMARK 8 THE SUBMITTED ASYMMETRIC UNIT BY APPLYING THE FOLLOWING
138 REMARK 8 TRANSLATIONS (USING FRACTIONAL COORDINATES):
139 REMARK 8 CHAIN A: TRANSLATE RESIDUES 1 - 9 BY (0 0 1), (0 0 2), AND
140 REMARK 8 (0 0 3) AND RESIDUES 7 - 9 BY (0 0 4).
141 REMARK 8 CHAIN B: TRANSLATE RESIDUES 31 - 36 BY (0 0 1), (0 0 2),
142 REMARK 8 AND (0 0 3).
143 REMARK 8 CHAIN C: TRANSLATE RESIDUES 61 - 66 BY (0 0 1), (0 0 2),
144 REMARK 8 AND (0 0 3) AND RESIDUES 64 - 66 BY (004).
145 REMARK 8 THIS WILL RESULT IN A MOLECULE WITH A TOTAL OF 90 RESIDUES,
146 REMARK 8 30 IN EACH CHAIN.
147 REMARK 9
148 REMARK 9 HYDROGEN BONDS BETWEEN PEPTIDE CHAINS FOLLOW THE RICH AND
149 REMARK 9 CRICK MODEL II FOR COLLAGEN.
150 REMARK 10
151 REMARK 10 THE UNIT CELL AXES WERE CHOSEN TO COINCIDE WITH A
152 REMARK 10 PREVIOUS STRUCTURE DETERMINATION (OKUYAMA 1981) OF THIS
153 REMARK 10 PEPTIDE.
154 REMARK 11
155 REMARK 11 FOR EACH CHAIN, RESIDUE NUMBERING CORRESPONDS TO THE ENTIRE
156 REMARK 11 MOLECULE RATHER THAN THE SHORTER ASYMMETRIC UNIT.
157 REMARK 200
158 REMARK 200 EXPERIMENTAL DETAILS
159 REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
160 REMARK 200 DATE OF DATA COLLECTION : OCT-1991
161 REMARK 200 TEMPERATURE (KELVIN) : 259.0
162 REMARK 200 PH : NULL
163 REMARK 200 NUMBER OF CRYSTALS USED : 1
164 REMARK 200
165 REMARK 200 SYNCHROTRON (Y/N) : N
166 REMARK 200 RADIATION SOURCE : NULL
167 REMARK 200 BEAMLINE : NULL
168 REMARK 200 X-RAY GENERATOR MODEL : NULL
169 REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
170 REMARK 200 WAVELENGTH OR RANGE (A) : 1.542
171 REMARK 200 MONOCHROMATOR : NULL
172 REMARK 200 OPTICS : NULL
173 REMARK 200
174 REMARK 200 DETECTOR TYPE : CAD4 DIFFRACTOMETER
175 REMARK 200 DETECTOR MANUFACTURER : ENRAF-NONIUS
176 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOLEN
177 REMARK 200 DATA SCALING SOFTWARE : NULL
178 REMARK 200
179 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 1136
180 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.97
181 REMARK 200 RESOLUTION RANGE LOW (A) : INFINITY
182 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.
183 REMARK 200
184 REMARK 200 OVERALL.
185 REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
186 REMARK 200 DATA REDUNDANCY : NULL
187 REMARK 200 R MERGE (I) : NULL
188 REMARK 200 R SYM (I) : NULL
189 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
190 REMARK 200
191 REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
192 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
193 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.2
194 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.
195 REMARK 200 DATA REDUNDANCY IN SHELL : NULL
196 REMARK 200 R MERGE FOR SHELL (I) : NULL
197 REMARK 200 R SYM FOR SHELL (I) : NULL
198 REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
199 REMARK 200
200 REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR
201 REMARK 200 REPLACEMENT
202 REMARK 200 SOFTWARE USED: LALS
203 REMARK 200 STARTING MODEL: IDEALIZED SEVEN-FOLD TRIPLE-HELIX
204 REMARK 200
205 REMARK 200 REMARK: NULL
206 REMARK 280
207 REMARK 280 CRYSTAL
208 REMARK 280 SOLVENT CONTENT, VS (%): NULL
209 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL
210 REMARK 280
211 REMARK 280 CRYSTALLIZATION CONDITIONS: PEPTIDE WAS CRYSTALLIZED FROM
212 REMARK 280 4.0 MG/ML PEPTIDE IN 10% ACETIC ACID, 0.1% SODIUM AZIDE,
213 REMARK 280 AND 3.0% PEG400.
214 REMARK 290
215 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
216 REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
217 REMARK 290
218 REMARK 290 SYMOP SYMMETRY
219 REMARK 290 NNNMMM OPERATOR
220 REMARK 290 1555 X,Y,Z
221 REMARK 290 2555 1/2-X,-Y,1/2+Z
222 REMARK 290 3555 -X,1/2+Y,1/2-Z
223 REMARK 290 4555 1/2+X,1/2-Y,-Z
224 REMARK 290
225 REMARK 290 WHERE NNN -> OPERATOR NUMBER
226 REMARK 290 MMM -> TRANSLATION VECTOR
227 REMARK 290
228 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
229 REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
230 REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
231 REMARK 290 RELATED MOLECULES.
232 REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
233 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
234 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
235 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 13.40986
236 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
237 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 10.09000
238 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
239 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 13.14510
240 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 10.09000
241 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 13.40986
242 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 13.14510
243 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
244 REMARK 290
245 REMARK 290 REMARK: NULL
246 REMARK 900
247 REMARK 900 RELATED ENTRIES
248 REMARK 900 THIS ENTRY IS RELATED TO PDB ENTRY 1A3J.
249 DBREF 1A3I A 1 9 PDB 1A3I 1A3I 1 9
250 DBREF 1A3I B 31 36 PDB 1A3I 1A3I 31 36
251 DBREF 1A3I C 61 66 PDB 1A3I 1A3I 61 66
252 SEQRES 1 A 9 PRO PRO GLY PRO PRO GLY PRO PRO GLY
253 SEQRES 1 B 6 PRO PRO GLY PRO PRO GLY
254 SEQRES 1 C 6 PRO PRO GLY PRO PRO GLY
255 HET ACY 401 4
256 HET ACY 402 4
257 HETNAM ACY ACETIC ACID
258 FORMUL 4 ACY 2(C2 H4 O2)
259 FORMUL 5 HOH *37(H2 O1)
260 LINK N PRO C 61 C GLY A 9 1556
261 LINK N PRO A 1 C GLY B 36 1556
262 LINK N PRO B 31 C GLY C 66 1556
263 CRYST1 26.820 26.290 20.180 90.00 90.00 90.00 P 21 21 21 4
264 ORIGX1 1.000000 0.000000 0.000000 0.00000
265 ORIGX2 0.000000 1.000000 0.000000 0.00000
266 ORIGX3 0.000000 0.000000 1.000000 0.00000
267 SCALE1 0.037286 0.000000 0.000000 0.00000
268 SCALE2 0.000000 0.038037 0.000000 0.00000
269 SCALE3 0.000000 0.000000 0.049554 0.00000
270 TVECT 1 0.00000 0.00000 20.18000
271 ATOM 1 N PRO A 1 8.316 21.206 21.530 1.00 17.44 N
272 ATOM 2 CA PRO A 1 7.608 20.729 20.336 1.00 17.44 C
273 ATOM 3 C PRO A 1 8.487 20.707 19.092 1.00 17.44 C
274 ATOM 4 O PRO A 1 9.466 21.457 19.005 1.00 17.44 O
275 ATOM 5 CB PRO A 1 6.460 21.723 20.211 1.00 22.26 C
276 ATOM 6 CG PRO A 1 7.110 23.002 20.661 1.00 22.26 C
277 ATOM 7 CD PRO A 1 7.873 22.569 21.889 1.00 22.26 C
278 ATOM 8 N PRO A 2 8.177 19.849 18.107 1.00 13.49 N
279 ATOM 9 CA PRO A 2 9.057 19.896 16.936 1.00 13.49 C
280 ATOM 10 C PRO A 2 9.087 21.308 16.377 1.00 13.49 C
281 ATOM 11 O PRO A 2 8.318 22.186 16.816 1.00 13.49 O
282 ATOM 12 CB PRO A 2 8.426 18.899 15.970 1.00 18.26 C
283 ATOM 13 CG PRO A 2 7.776 17.914 16.886 1.00 18.26 C
284 ATOM 14 CD PRO A 2 7.166 18.797 17.954 1.00 18.26 C
285 ATOM 15 N GLY A 3 9.981 21.517 15.426 1.00 12.07 N
286 ATOM 16 CA GLY A 3 10.060 22.799 14.777 1.00 12.07 C
287 ATOM 17 C GLY A 3 9.119 22.720 13.589 1.00 12.07 C
288 ATOM 18 O GLY A 3 8.531 21.655 13.334 1.00 12.07 O
289 ATOM 19 N PRO A 4 8.954 23.832 12.847 1.00 14.22 N
290 ATOM 20 CA PRO A 4 8.095 23.907 11.675 1.00 14.22 C
291 ATOM 21 C PRO A 4 8.733 23.310 10.437 1.00 14.22 C
292 ATOM 22 O PRO A 4 9.963 23.078 10.402 1.00 14.22 O
293 ATOM 23 CB PRO A 4 7.863 25.403 11.527 1.00 8.61 C
294 ATOM 24 CG PRO A 4 9.218 25.934 11.895 1.00 8.61 C
295 ATOM 25 CD PRO A 4 9.530 25.158 13.143 1.00 8.61 C
296 ATOM 26 N PRO A 5 7.918 23.027 9.412 1.00 14.03 N
297 ATOM 27 CA PRO A 5 8.416 22.493 8.135 1.00 14.03 C
298 ATOM 28 C PRO A 5 9.621 23.306 7.672 1.00 14.03 C
299 ATOM 29 O PRO A 5 9.876 24.379 8.181 1.00 14.03 O
300 ATOM 30 CB PRO A 5 7.229 22.641 7.193 1.00 10.90 C
301 ATOM 31 CG PRO A 5 6.082 22.382 8.123 1.00 10.90 C
302 ATOM 32 CD PRO A 5 6.452 23.069 9.415 1.00 10.90 C
303 ATOM 33 N GLY A 6 10.369 22.765 6.725 1.00 10.80 N
304 ATOM 34 CA GLY A 6 11.517 23.464 6.204 1.00 10.80 C
305 ATOM 35 C GLY A 6 11.139 24.138 4.928 1.00 10.80 C
306 ATOM 36 O GLY A 6 10.028 23.948 4.418 1.00 10.80 O
307 ATOM 37 N PRO A 7 12.050 24.922 4.355 1.00 11.55 N
308 ATOM 38 CA PRO A 7 11.797 25.641 3.111 1.00 11.55 C
309 ATOM 39 C PRO A 7 11.484 24.709 1.970 1.00 11.55 C
310 ATOM 40 O PRO A 7 11.783 23.500 2.038 1.00 11.55 O
311 ATOM 41 CB PRO A 7 13.091 26.440 2.901 1.00 10.61 C
312 ATOM 42 CG PRO A 7 14.119 25.540 3.516 1.00 10.61 C
313 ATOM 43 CD PRO A 7 13.456 25.102 4.796 1.00 10.61 C
314 ATOM 44 N PRO A 8 10.853 25.225 0.900 1.00 14.31 N
315 ATOM 45 CA PRO A 8 10.571 24.322 -0.220 1.00 14.31 C
316 ATOM 46 C PRO A 8 11.897 23.973 -0.901 1.00 14.31 C
317 ATOM 47 O PRO A 8 12.973 24.425 -0.473 1.00 14.31 O
318 ATOM 48 CB PRO A 8 9.623 25.131 -1.124 1.00 16.14 C
319 ATOM 49 CG PRO A 8 9.080 26.188 -0.206 1.00 16.14 C
320 ATOM 50 CD PRO A 8 10.279 26.556 0.633 1.00 16.14 C
321 ATOM 51 N GLY A 9 11.816 23.125 -1.918 1.00 11.65 N
322 ATOM 52 CA GLY A 9 12.996 22.720 -2.639 1.00 11.65 C
323 ATOM 53 C GLY A 9 13.234 23.577 -3.852 1.00 11.65 C
324 ATOM 54 O GLY A 9 12.433 24.459 -4.180 1.00 11.65 O
325 TER 55 GLY A 9
326 ATOM 56 N PRO B 31 12.731 18.403 18.599 1.00 8.71 N
327 ATOM 57 CA PRO B 31 13.374 17.891 17.389 1.00 8.71 C
328 ATOM 58 C PRO B 31 13.142 18.745 16.166 1.00 8.71 C
329 ATOM 59 O PRO B 31 12.207 19.526 16.121 1.00 8.71 O
330 ATOM 60 CB PRO B 31 12.784 16.471 17.255 1.00 15.38 C
331 ATOM 61 CG PRO B 31 11.434 16.598 17.873 1.00 15.38 C
332 ATOM 62 CD PRO B 31 11.660 17.490 19.065 1.00 15.38 C
333 ATOM 63 N PRO B 32 14.011 18.647 15.178 1.00 13.67 N
334 ATOM 64 CA PRO B 32 13.833 19.426 13.967 1.00 13.67 C
335 ATOM 65 C PRO B 32 12.523 19.099 13.336 1.00 13.67 C
336 ATOM 66 O PRO B 32 12.038 17.968 13.473 1.00 13.67 O
337 ATOM 67 CB PRO B 32 15.025 19.023 13.125 1.00 9.03 C
338 ATOM 68 CG PRO B 32 16.077 18.799 14.163 1.00 9.03 C
339 ATOM 69 CD PRO B 32 15.320 17.975 15.152 1.00 9.03 C
340 ATOM 70 N GLY B 33 11.928 20.070 12.640 1.00 14.26 N
341 ATOM 71 CA GLY B 33 10.661 19.801 12.008 1.00 14.26 C
342 ATOM 72 C GLY B 33 10.802 18.911 10.797 1.00 14.26 C
343 ATOM 73 O GLY B 33 11.882 18.368 10.516 1.00 14.26 O
344 ATOM 74 N PRO B 34 9.708 18.736 10.046 1.00 11.50 N
345 ATOM 75 CA PRO B 34 9.665 17.922 8.836 1.00 11.50 C
346 ATOM 76 C PRO B 34 10.227 18.620 7.654 1.00 11.50 C
347 ATOM 77 O PRO B 34 10.284 19.836 7.639 1.00 11.50 O
348 ATOM 78 CB PRO B 34 8.192 17.649 8.657 1.00 9.66 C
349 ATOM 79 CG PRO B 34 7.586 18.930 9.132 1.00 9.66 C
350 ATOM 80 CD PRO B 34 8.350 19.245 10.373 1.00 9.66 C
351 ATOM 81 N PRO B 35 10.677 17.860 6.651 1.00 16.25 N
352 ATOM 82 CA PRO B 35 11.228 18.392 5.413 1.00 16.25 C
353 ATOM 83 C PRO B 35 10.219 19.317 4.794 1.00 16.25 C
354 ATOM 84 O PRO B 35 9.010 19.249 5.127 1.00 16.25 O
355 ATOM 85 CB PRO B 35 11.468 17.160 4.542 1.00 10.89 C
356 ATOM 86 CG PRO B 35 11.668 16.066 5.531 1.00 10.89 C
357 ATOM 87 CD PRO B 35 10.798 16.385 6.703 1.00 10.89 C
358 ATOM 88 N GLY B 36 10.709 20.223 3.948 1.00 19.34 N
359 ATOM 89 CA GLY B 36 9.836 21.154 3.260 1.00 19.34 C
360 ATOM 90 C GLY B 36 9.207 20.491 2.050 1.00 19.34 C
361 ATOM 91 O GLY B 36 9.565 19.355 1.710 1.00 19.34 O
362 TER 92 GLY B 36
363 ATOM 93 N PRO C 61 14.309 23.332 15.622 1.00 10.63 N
364 ATOM 94 CA PRO C 61 14.643 24.095 14.422 1.00 10.63 C
365 ATOM 95 C PRO C 61 13.859 23.751 13.161 1.00 10.63 C
366 ATOM 96 O PRO C 61 13.189 22.726 13.091 1.00 10.63 O
367 ATOM 97 CB PRO C 61 16.144 23.846 14.270 1.00 19.41 C
368 ATOM 98 CG PRO C 61 16.308 22.475 14.820 1.00 19.41 C
369 ATOM 99 CD PRO C 61 15.451 22.510 16.056 1.00 19.41 C
370 ATOM 100 N PRO C 62 13.910 24.631 12.163 1.00 15.75 N
371 ATOM 101 CA PRO C 62 13.234 24.402 10.876 1.00 15.75 C
372 ATOM 102 C PRO C 62 13.686 23.039 10.262 1.00 15.75 C
373 ATOM 103 O PRO C 62 14.874 22.653 10.369 1.00 15.75 O
374 ATOM 104 CB PRO C 62 13.668 25.600 10.024 1.00 9.87 C
375 ATOM 105 CG PRO C 62 13.859 26.675 11.052 1.00 9.87 C
376 ATOM 106 CD PRO C 62 14.515 25.976 12.213 1.00 9.87 C
377 ATOM 107 N GLY C 63 12.761 22.316 9.639 1.00 16.50 N
378 ATOM 108 CA GLY C 63 13.167 21.066 9.028 1.00 16.50 C
379 ATOM 109 C GLY C 63 14.105 21.312 7.849 1.00 16.50 C
380 ATOM 110 O GLY C 63 14.435 22.472 7.518 1.00 16.50 O
381 ATOM 111 N PRO C 64 14.571 20.246 7.184 1.00 15.53 N
382 ATOM 112 CA PRO C 64 15.458 20.417 6.037 1.00 15.53 C
383 ATOM 113 C PRO C 64 14.684 20.927 4.823 1.00 15.53 C
384 ATOM 114 O PRO C 64 13.463 20.829 4.772 1.00 15.53 O
385 ATOM 115 CB PRO C 64 16.001 19.018 5.816 1.00 5.63 C
386 ATOM 116 CG PRO C 64 14.806 18.201 6.163 1.00 5.63 C
387 ATOM 117 CD PRO C 64 14.354 18.810 7.450 1.00 5.63 C
388 ATOM 118 N PRO C 65 15.378 21.485 3.840 1.00 10.50 N
389 ATOM 119 CA PRO C 65 14.622 21.927 2.689 1.00 10.50 C
390 ATOM 120 C PRO C 65 14.079 20.706 1.955 1.00 10.50 C
391 ATOM 121 O PRO C 65 14.505 19.531 2.221 1.00 10.50 O
392 ATOM 122 CB PRO C 65 15.615 22.734 1.892 1.00 11.55 C
393 ATOM 123 CG PRO C 65 16.951 22.189 2.279 1.00 11.55 C
394 ATOM 124 CD PRO C 65 16.808 21.850 3.742 1.00 11.55 C
395 ATOM 125 N GLY C 66 13.102 20.952 1.076 1.00 9.96 N
396 ATOM 126 CA GLY C 66 12.479 19.874 0.334 1.00 9.96 C
397 ATOM 127 C GLY C 66 13.226 19.430 -0.900 1.00 9.96 C
398 ATOM 128 O GLY C 66 14.206 20.054 -1.286 1.00 9.96 O
399 TER 129 GLY C 66
400 HETATM 130 C ACY 401 3.682 22.541 11.236 1.00 21.19 C
401 HETATM 131 O ACY 401 2.807 23.097 10.553 1.00 21.19 O
402 HETATM 132 OXT ACY 401 4.306 23.101 12.291 1.00 21.19 O
403 HETATM 133 CH3 ACY 401 4.134 21.141 10.915 1.00 21.19 C
404 HETATM 134 C ACY 402 19.091 22.160 7.837 1.00 38.32 C
405 HETATM 135 O ACY 402 19.334 21.755 6.694 1.00 38.32 O
406 HETATM 136 OXT ACY 402 18.633 21.338 8.768 1.00 38.32 O
407 HETATM 137 CH3 ACY 402 19.293 23.618 8.266 1.00 38.32 C
408 HETATM 138 O HOH 101 5.594 21.889 15.805 1.00 28.97 O
409 HETATM 139 O HOH 102 7.355 25.253 16.293 1.00 22.47 O
410 HETATM 140 O HOH 103 6.457 20.993 12.327 1.00 29.02 O
411 HETATM 141 O HOH 104 7.423 26.270 8.119 1.00 30.44 O
412 HETATM 142 O HOH 105 11.373 26.588 6.950 1.00 23.32 O
413 HETATM 143 O HOH 106 7.408 25.371 4.091 1.00 5.05 O
414 HETATM 144 O HOH 107 13.153 27.296 -0.172 1.00 21.02 O
415 HETATM 145 O HOH 108 15.664 24.810 -1.390 1.00 11.17 O
416 HETATM 146 O HOH 109 12.152 26.921 -4.540 1.00 9.23 O
417 HETATM 147 O HOH 111 13.443 15.615 12.881 1.00 13.59 O
418 HETATM 148 O HOH 112 9.758 16.818 12.994 1.00 27.99 O
419 HETATM 149 O HOH 113 12.963 16.325 9.228 1.00 23.25 O
420 HETATM 150 O HOH 115 5.878 20.610 4.485 1.00 24.12 O
421 HETATM 151 O HOH 116 8.848 16.145 2.532 1.00 47.48 O
422 HETATM 152 O HOH 121 18.638 24.296 11.397 1.00 27.03 O
423 HETATM 153 O HOH 122 16.444 20.463 10.447 1.00 25.94 O
424 HETATM 154 O HOH 123 16.295 24.230 6.930 1.00 19.70 O
425 HETATM 155 O HOH 124 17.331 17.619 2.413 1.00 31.73 O
426 HETATM 156 O HOH 125 13.985 16.977 0.817 1.00 53.43 O
427 HETATM 157 O HOH 126 16.914 19.363 -0.910 1.00 9.43 O
428 HETATM 158 O HOH 201 5.473 23.666 4.098 1.00 14.40 O
429 HETATM 159 O HOH 202 21.595 24.992 9.644 1.00 17.29 O
430 HETATM 160 O HOH 204 4.187 25.027 5.974 1.00 7.43 O
431 HETATM 161 O HOH 205 13.466 14.688 2.583 1.00 7.90 O
432 HETATM 162 O HOH 208 16.622 16.376 -0.560 1.00 22.05 O
433 HETATM 163 O HOH 209 17.417 23.063 -0.970 1.00 23.97 O
434 HETATM 164 O HOH 210 17.034 27.356 9.718 1.00 20.07 O
435 HETATM 165 O HOH 218 3.280 23.836 8.294 1.00 17.32 O
436 HETATM 166 O HOH 220 16.159 26.500 -3.605 1.00 26.00 O
437 HETATM 167 O HOH 241 17.060 26.756 1.465 1.00 16.81 O
438 HETATM 168 O HOH 242 6.144 15.504 5.728 1.00 23.11 O
439 HETATM 169 O HOH 243 18.532 26.812 12.585 1.00 13.40 O
440 HETATM 170 O HOH 244 9.783 28.384 5.130 1.00 21.62 O
441 HETATM 171 O HOH 245 10.552 28.648 13.053 1.00 23.05 O
442 HETATM 172 O HOH 246 9.269 14.976 15.672 1.00 28.60 O
443 HETATM 173 O HOH 247 6.015 15.569 15.283 1.00 26.87 O
444 HETATM 174 O HOH 248 20.598 27.021 8.450 1.00 22.69 O
445 CONECT 130 131 132 133
446 CONECT 131 130
447 CONECT 132 130
448 CONECT 133 130
449 CONECT 134 135 136 137
450 CONECT 135 134
451 CONECT 136 134
452 CONECT 137 134
453 MASTER 226 0 2 0 0 0 0 6 171 3 8 3
454 END