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* OPEN_CA_1OMP *

B-factor analysis for ID 2604231333361693976

Overall B-factor prediction

Correlation= 0.570 for 370 C-alpha atoms.

B-factors for all residues

Residue-by-residue B-factor prediction for CA atoms

B-factors are computed based on the first 100 normal modes (B-PREDICT) and are scaled to match the overall B-factors in the submitted model (B-SCALED). A high correlation with the observations is an indicator that the normal modes capture well the overall flexibility features of the model. Comparison of the observed (B-OBS, blue) and the computed (B-SCALED, red) B-factors for all C-alpha atoms is presented below. Differences between B-factors from normal mode analysis and from X-ray crystallographic data may for example indicate regions where the protein flexibility is modified due to external factors such as tight crystall-packing.

ATOM TYP RES RESID B-PREDICT B-SCALED B-OBS	B-SCALED	B-OBS
1 CA LYS 1 13.5776 54.1846 57.0200
2 CA ILE 2 6.7780 31.2022 52.1700
3 CA GLU 3 4.4335 23.2781 47.0100
4 CA GLU 4 4.9989 25.1888 38.7800
5 CA GLY 5 6.2441 29.3976 33.1100
6 CA LYS 6 3.9330 21.5863 26.5500
7 CA LEU 7 2.5513 16.9160 22.2900
8 CA VAL 8 2.4238 16.4853 20.4800
9 CA ILE 9 1.9610 14.9208 17.1100
10 CA TRP 10 2.2605 15.9333 17.3200
11 CA ILE 11 2.4174 16.4635 15.5200
12 CA ASN 12 3.8001 21.1371 19.9200
13 CA GLY 13 6.0427 28.7171 23.7800
14 CA ASP 14 8.8212 38.1084 26.7400
15 CA LYS 15 4.7294 24.2779 25.0900
16 CA GLY 16 4.3763 23.0847 22.4200
17 CA TYR 17 3.9244 21.5571 23.1600
18 CA ASN 18 4.7389 24.3101 22.1600
19 CA GLY 19 3.6070 20.4843 20.6600
20 CA LEU 20 2.7235 17.4981 21.3000
21 CA ALA 21 3.6533 20.6408 22.7300
22 CA GLU 22 4.1101 22.1849 26.3200
23 CA VAL 23 3.5404 20.2592 22.0200
24 CA GLY 24 3.4203 19.8534 24.8300
25 CA LYS 25 4.9212 24.9262 29.3100
26 CA LYS 26 6.2914 29.5576 29.8800
27 CA PHE 27 5.0596 25.3941 28.5000
28 CA GLU 28 4.8006 24.5188 32.4100
29 CA LYS 29 10.4135 43.4901 38.6200
30 CA ASP 30 14.1423 56.0935 37.1500
31 CA THR 31 11.5679 47.3920 34.4500
32 CA GLY 32 10.1893 42.7323 32.4600
33 CA ILE 33 6.3342 29.7023 32.2600
34 CA LYS 34 4.8000 24.5167 32.1400
35 CA VAL 35 2.9838 18.3780 28.4900
36 CA THR 36 3.3320 19.5547 27.7600
37 CA VAL 37 2.8053 17.7748 24.4800
38 CA GLU 38 3.4272 19.8768 26.8500
39 CA HIS 39 3.9311 21.5797 28.4000
40 CA PRO 40 5.4734 26.7928 31.7700
41 CA ASP 41 8.8000 38.0364 38.0900
42 CA LYS 42 8.0441 35.4816 35.8800
43 CA LEU 43 5.4563 26.7351 29.5900
44 CA GLU 44 6.6210 30.6717 25.3000
45 CA GLU 45 7.4390 33.4364 26.4400
46 CA LYS 46 7.2434 32.7753 24.7400
47 CA PHE 47 6.0281 28.6676 21.6200
48 CA PRO 48 6.1627 29.1226 23.8500
49 CA GLN 49 7.3644 33.1843 26.4300
50 CA VAL 50 6.0923 28.8847 21.9800
51 CA ALA 51 4.5822 23.7805 21.8300
52 CA ALA 52 6.6044 30.6156 25.4400
53 CA THR 53 8.1920 35.9816 27.9100
54 CA GLY 54 6.2137 29.2950 27.3200
55 CA ASP 55 5.5435 27.0299 28.0800
56 CA GLY 56 4.2323 22.5978 24.6600
57 CA PRO 57 2.2361 15.8509 16.4100
58 CA ASP 58 1.5685 13.5944 13.3800
59 CA ILE 59 1.2353 12.4682 15.1000
60 CA ILE 60 1.6300 13.8022 13.4900
61 CA PHE 61 1.4799 13.2949 11.2200
62 CA TRP 62 1.4273 13.1170 10.3800
63 CA ALA 63 1.4152 13.0763 11.1600
64 CA HIS 64 1.2577 12.5438 12.9600
65 CA ASP 65 1.6222 13.7759 18.3300
66 CA ARG 66 1.8771 14.6375 20.6600
67 CA PHE 67 1.5614 13.5703 18.3400
68 CA GLY 68 1.6957 14.0241 20.8600
69 CA GLY 69 3.0763 18.6908 20.7400
70 CA TYR 70 2.5283 16.8383 19.6300
71 CA ALA 71 2.5425 16.8863 19.3100
72 CA GLN 72 4.3012 22.8308 23.2600
73 CA SER 73 5.7507 27.7299 17.5900
74 CA GLY 74 4.4903 23.4701 16.7600
75 CA LEU 75 3.1116 18.8098 15.0000
76 CA LEU 76 2.0754 15.3078 15.3700
77 CA ALA 77 2.2972 16.0573 15.5400
78 CA GLU 78 2.1456 15.5450 20.5400
79 CA ILE 79 3.3116 19.4860 19.9600
80 CA THR 80 6.9000 31.6147 28.1000
81 CA PRO 81 14.4078 56.9908 29.6300
82 CA ASP 82 11.7346 47.9554 34.0200
83 CA LYS 83 11.3905 46.7922 31.8600
84 CA ALA 84 8.7117 37.7380 27.8900
85 CA PHE 85 5.2386 25.9992 21.7100
86 CA GLN 86 5.0396 25.3264 23.2600
87 CA ASP 87 5.8689 28.1295 26.4100
88 CA LYS 88 5.6123 27.2623 23.0500
89 CA LEU 89 2.9463 18.2513 19.7200
90 CA TYR 90 3.3524 19.6240 20.0300
91 CA PRO 91 3.3049 19.4632 19.8500
92 CA PHE 92 2.8239 17.8374 15.9700
93 CA THR 93 1.4444 13.1748 13.9300
94 CA TRP 94 1.3642 12.9039 14.6000
95 CA ASP 95 1.6448 13.8521 15.8500
96 CA ALA 96 1.4550 13.2108 13.7600
97 CA VAL 97 1.3762 12.9442 15.5200
98 CA ARG 98 1.5268 13.4534 23.9700
99 CA TYR 99 1.9365 14.8381 31.2100
100 CA ASN 100 2.9951 18.4161 39.4300
101 CA GLY 101 3.9368 21.5993 37.9400
102 CA LYS 102 2.6838 17.3639 31.2400
103 CA LEU 103 1.8852 14.6648 20.2400
104 CA ILE 104 1.4348 13.1425 12.6100
105 CA ALA 105 1.5620 13.5725 11.6800
106 CA TYR 106 1.1631 12.2242 11.2500
107 CA PRO 107 0.9090 11.3651 11.7400
108 CA ILE 108 1.0030 11.6830 12.6900
109 CA ALA 109 1.2717 12.5910 13.4700
110 CA VAL 110 1.0909 11.9800 14.8700
111 CA GLU 111 1.1307 12.1147 14.9800
112 CA ALA 112 1.2321 12.4572 9.9100
113 CA LEU 113 1.1094 12.0424 8.6200
114 CA SER 114 0.9859 11.6250 7.6500
115 CA LEU 115 1.1402 12.1467 8.4500
116 CA ILE 116 1.4608 13.2304 9.6300
117 CA TYR 117 2.2129 15.7723 10.4100
118 CA ASN 118 2.9254 18.1806 12.0400
119 CA LYS 119 4.6403 23.9770 16.8500
120 CA ASP 120 6.8830 31.5572 19.9200
121 CA LEU 121 6.9079 31.6415 18.1500
122 CA LEU 122 5.6712 27.4612 22.9900
123 CA PRO 123 10.2362 42.8910 31.2600
124 CA ASN 124 10.8998 45.1338 31.4100
125 CA PRO 125 7.0884 32.2513 23.8000
126 CA PRO 126 4.8617 24.7253 16.7900
127 CA LYS 127 3.3448 19.5982 15.4200
128 CA THR 128 3.3792 19.7145 14.1200
129 CA TRP 129 3.2642 19.3258 11.3600
130 CA GLU 130 5.5199 26.9501 14.0000
131 CA GLU 131 4.8216 24.5897 17.2600
132 CA ILE 132 3.2964 19.4345 16.0000
133 CA PRO 133 3.6295 20.5605 18.5500
134 CA ALA 134 4.7206 24.2482 17.0600
135 CA LEU 135 3.8966 21.4631 18.6600
136 CA ASP 136 2.7316 17.5254 16.7400
137 CA LYS 137 5.5078 26.9090 22.3100
138 CA GLU 138 7.2879 32.9257 21.1900
139 CA LEU 139 5.3701 26.4437 17.1600
140 CA LYS 140 5.9548 28.4197 17.1300
141 CA ALA 141 13.3220 53.3209 19.9900
142 CA LYS 142 13.4810 53.8584 22.3500
143 CA GLY 143 10.1212 42.5024 20.2800
144 CA LYS 144 6.4493 30.0912 19.0400
145 CA SER 145 2.5622 16.9529 15.9400
146 CA ALA 146 1.9500 14.8837 11.5800
147 CA LEU 147 1.4054 13.0431 12.6800
148 CA MET 148 1.5783 13.6275 13.6600
149 CA PHE 149 1.8467 14.5348 14.0300
150 CA ASN 150 1.8314 14.4828 14.3400
151 CA LEU 151 1.8479 14.5388 15.7300
152 CA GLN 152 2.6226 17.1572 17.7000
153 CA GLU 153 2.2939 16.0461 18.5200
154 CA PRO 154 1.8079 14.4033 13.2700
155 CA TYR 155 1.9740 14.9650 11.5800
156 CA PHE 156 1.3014 12.6916 10.4000
157 CA THR 157 1.2162 12.4036 9.9400
158 CA TRP 158 1.0130 11.7169 11.3600
159 CA PRO 159 0.9697 11.5705 8.7700
160 CA LEU 160 0.9963 11.6604 10.8100
161 CA ILE 161 1.0941 11.9909 13.2100
162 CA ALA 162 1.1415 12.1512 11.9900
163 CA ALA 163 1.1816 12.2867 13.2400
164 CA ASP 164 1.4841 13.3091 15.3100
165 CA GLY 165 1.8257 14.4636 16.7500
166 CA GLY 166 1.2311 12.4538 16.2100
167 CA TYR 167 1.5125 13.4049 17.7100
168 CA ALA 168 1.9765 14.9734 17.8000
169 CA PHE 169 2.2890 16.0295 21.2900
170 CA LYS 170 2.8866 18.0494 26.9700
171 CA TYR 171 3.8105 21.1723 36.0400
172 CA GLU 172 6.5463 30.4190 49.2100
173 CA ASN 173 5.1382 25.6597 50.4000
174 CA GLY 174 2.7720 17.6622 44.5500
175 CA LYS 175 2.2923 16.0409 37.5100
176 CA TYR 176 2.5497 16.9106 32.6200
177 CA ASP 177 3.5639 20.3387 32.6500
178 CA ILE 178 4.0103 21.8475 34.1300
179 CA LYS 179 5.1263 25.6194 33.8300
180 CA ASP 180 3.7137 20.8449 29.6100
181 CA VAL 181 2.4232 16.4831 26.7900
182 CA GLY 182 1.7431 14.1845 24.2300
183 CA VAL 183 1.5107 13.3990 27.1600
184 CA ASP 184 1.7845 14.3243 30.7600
185 CA ASN 185 2.2764 15.9869 26.7900
186 CA ALA 186 2.7063 17.4400 24.5400
187 CA GLY 187 1.8922 14.6885 21.4700
188 CA ALA 188 1.2751 12.6026 17.3900
189 CA LYS 189 1.8007 14.3790 20.8400
190 CA ALA 190 1.9697 14.9503 19.1900
191 CA GLY 191 1.4743 13.2761 15.6100
192 CA LEU 192 1.6426 13.8447 15.5500
193 CA THR 193 2.6818 17.3573 18.9900
194 CA PHE 194 3.8729 21.3831 18.9600
195 CA LEU 195 3.8361 21.2586 17.4400
196 CA VAL 196 3.3462 19.6030 18.0000
197 CA ASP 197 4.2754 22.7434 23.2000
198 CA LEU 198 3.2933 19.4239 23.9400
199 CA ILE 199 3.3262 19.5352 25.0300
200 CA LYS 200 5.7480 27.7210 30.1200
201 CA ASN 201 5.9740 28.4848 27.9100
202 CA LYS 202 4.6702 24.0780 26.7500
203 CA HIS 203 4.4069 23.1879 24.0800
204 CA MET 204 3.8413 21.2763 26.9300
205 CA ASN 205 3.7980 21.1298 28.5400
206 CA ALA 206 3.9374 21.6012 27.1300
207 CA ASP 207 4.0544 21.9967 26.5000
208 CA THR 208 2.7522 17.5952 21.0800
209 CA ASP 209 3.6329 20.5721 18.7100
210 CA TYR 210 4.8910 24.8243 15.7800
211 CA SER 211 6.9580 31.8108 19.7500
212 CA ILE 212 4.9258 24.9419 20.4000
213 CA ALA 213 2.9733 18.3423 16.0400
214 CA GLU 214 4.3095 22.8588 17.9000
215 CA ALA 215 5.5318 26.9900 17.7000
216 CA ALA 216 3.7891 21.0998 15.2500
217 CA PHE 217 2.7631 17.6321 13.1700
218 CA ASN 218 4.2348 22.6062 15.1300
219 CA LYS 219 4.9626 25.0663 17.5200
220 CA GLY 220 3.7588 20.9974 18.8900
221 CA GLU 221 3.7133 20.8435 17.3700
222 CA THR 222 2.2685 15.9603 12.3200
223 CA ALA 223 2.0246 15.1358 11.9300
224 CA MET 224 1.5401 13.4985 10.3600
225 CA THR 225 1.4297 13.1252 9.8700
226 CA ILE 226 1.1203 12.0793 9.4000
227 CA ASN 227 1.4183 13.0868 7.7300
228 CA GLY 228 1.9262 14.8032 10.7000
229 CA PRO 229 4.4043 23.1793 12.7600
230 CA TRP 230 6.9072 31.6390 14.0500
231 CA ALA 231 5.3627 26.4186 16.4100
232 CA TRP 232 6.2484 29.4123 16.3500
233 CA SER 233 10.5842 44.0671 25.3500
234 CA ASN 234 7.8880 34.9541 26.3900
235 CA ILE 235 5.3451 26.3590 22.4400
236 CA ASP 236 9.1960 39.3749 26.9200
237 CA THR 237 9.8423 41.5596 29.7500
238 CA SER 238 6.8173 31.3352 31.8300
239 CA LYS 239 7.5932 33.9577 34.3300
240 CA VAL 240 5.3811 26.4807 25.4600
241 CA ASN 241 5.7999 27.8965 21.9400
242 CA TYR 242 3.4245 19.8677 14.7200
243 CA GLY 243 2.6680 17.3105 11.0800
244 CA VAL 244 2.5496 16.9104 12.0200
245 CA THR 245 1.4459 13.1799 10.1300
246 CA VAL 246 1.4330 13.1363 12.5100
247 CA LEU 247 1.4666 13.2500 11.5200
248 CA PRO 248 2.3630 16.2797 11.7000
249 CA THR 249 1.5903 13.6679 13.8700
250 CA PHE 250 1.6441 13.8499 16.0200
251 CA LYS 251 3.6034 20.4723 18.6500
252 CA GLY 252 3.9218 21.5485 18.6700
253 CA GLN 253 2.1289 15.4886 14.9400
254 CA PRO 254 1.5325 13.4728 12.9000
255 CA SER 255 0.9360 11.4565 13.3200
256 CA LYS 256 1.1933 12.3262 14.2700
257 CA PRO 257 0.9568 11.5268 11.4000
258 CA PHE 258 1.1170 12.0683 13.0600
259 CA VAL 259 1.4104 13.0600 12.1600
260 CA GLY 260 1.9865 15.0072 10.3100
261 CA VAL 261 1.0431 11.8186 10.8300
262 CA LEU 262 1.0018 11.6788 9.4600
263 CA SER 263 0.7909 10.9661 8.5700
264 CA ALA 264 0.9619 11.5442 8.0200
265 CA GLY 265 1.5920 13.6739 9.5300
266 CA ILE 266 1.4337 13.1386 10.4000
267 CA ASN 267 1.7829 14.3191 11.5900
268 CA ALA 268 2.3830 16.3472 13.5900
269 CA ALA 269 3.1728 19.0169 17.1800
270 CA SER 270 2.4232 16.4831 18.8100
271 CA PRO 271 3.7562 20.9886 19.4100
272 CA ASN 272 3.2882 19.4068 17.5300
273 CA LYS 273 3.5541 20.3057 15.6100
274 CA GLU 274 5.1868 25.8239 15.4000
275 CA LEU 275 3.9892 21.7762 14.1600
276 CA ALA 276 2.3364 16.1896 13.9200
277 CA LYS 277 4.6366 23.9643 16.4200
278 CA GLU 278 4.9681 25.0850 19.9800
279 CA PHE 279 3.8626 21.3483 17.2600
280 CA LEU 280 3.7678 21.0280 15.3600
281 CA GLU 281 4.5541 23.6856 16.9400
282 CA ASN 282 4.6782 24.1051 19.6700
283 CA TYR 283 3.5387 20.2537 20.5300
284 CA LEU 284 2.9160 18.1488 17.4300
285 CA LEU 285 2.9113 18.1330 13.8700
286 CA THR 286 3.4526 19.9627 16.2300
287 CA ASP 287 4.2275 22.5818 21.2600
288 CA GLU 288 4.5364 23.6256 22.4400
289 CA GLY 289 3.2785 19.3742 19.1400
290 CA LEU 290 3.3434 19.5933 17.8600
291 CA GLU 291 4.3973 23.1557 24.2300
292 CA ALA 292 4.0722 22.0569 21.5100
293 CA VAL 293 2.9305 18.1979 20.4600
294 CA ASN 294 3.4596 19.9863 23.2800
295 CA LYS 295 5.3978 26.5374 27.9200
296 CA ASP 296 5.2204 25.9378 27.6300
297 CA LYS 297 4.4366 23.2885 25.8800
298 CA PRO 298 2.7222 17.4938 23.5600
299 CA LEU 299 2.1569 15.5830 18.8600
300 CA GLY 300 2.1535 15.5715 15.1100
301 CA ALA 301 1.7316 14.1455 13.3100
302 CA VAL 302 1.3376 12.8137 12.3800
303 CA ALA 303 1.5354 13.4825 10.2800
304 CA LEU 304 1.7527 14.2170 9.8200
305 CA LYS 305 2.9832 18.3758 14.1500
306 CA SER 306 3.1221 18.8454 17.3900
307 CA TYR 307 2.3889 16.3671 16.7900
308 CA GLU 308 2.2283 15.8245 18.2800
309 CA GLU 309 4.2209 22.5593 25.2800
310 CA GLU 310 4.9673 25.0821 23.3100
311 CA LEU 311 3.4661 20.0080 17.2300
312 CA ALA 312 3.5077 20.1487 14.2400
313 CA LYS 313 7.1539 32.4728 15.6100
314 CA ASP 314 5.5083 26.9109 13.6200
315 CA PRO 315 3.7465 20.9560 13.0600
316 CA ARG 316 2.8368 17.8811 9.2700
317 CA ILE 317 2.0281 15.1476 10.5200
318 CA ALA 318 1.9486 14.8789 9.0000
319 CA ALA 319 1.4749 13.2781 11.0000
320 CA THR 320 1.3552 12.8735 13.2100
321 CA MET 321 1.4905 13.3307 11.3100
322 CA GLU 322 1.4203 13.0934 12.2600
323 CA ASN 323 1.0703 11.9103 9.9000
324 CA ALA 324 1.2297 12.4491 11.7200
325 CA GLN 325 1.8075 14.4021 14.5000
326 CA LYS 326 1.4869 13.3185 16.1300
327 CA GLY 327 1.1614 12.2184 12.0900
328 CA GLU 328 1.5465 13.5201 12.6300
329 CA ILE 329 1.9218 14.7883 12.0200
330 CA MET 330 1.5574 13.5567 14.7200
331 CA PRO 331 1.5547 13.5478 16.3500
332 CA ASN 332 1.5093 13.3943 19.6000
333 CA ILE 333 1.9270 14.8061 23.7300
334 CA PRO 334 2.7959 17.7430 27.0900
335 CA GLN 335 3.6020 20.4674 27.6400
336 CA MET 336 2.5681 16.9728 25.4300
337 CA SER 337 3.8321 21.2451 25.7200
338 CA ALA 338 2.9683 18.3255 22.5000
339 CA PHE 339 2.4372 16.5305 17.8400
340 CA TRP 340 3.4236 19.8645 20.0300
341 CA TYR 341 3.2316 19.2156 24.8100
342 CA ALA 342 2.4873 16.6998 19.7900
343 CA VAL 343 1.9698 14.9508 20.4100
344 CA ARG 344 2.3795 16.3356 22.5800
345 CA THR 345 2.8995 18.0931 22.2600
346 CA ALA 346 2.3108 16.1031 19.6500
347 CA VAL 347 2.2475 15.8893 22.4600
348 CA ILE 348 2.9727 18.3406 24.5200
349 CA ASN 349 3.3889 19.7473 23.4200
350 CA ALA 350 2.8301 17.8584 24.9100
351 CA ALA 351 3.6758 20.7170 31.6700
352 CA SER 352 5.0431 25.3383 36.0300
353 CA GLY 353 6.8842 31.5612 37.5400
354 CA ARG 354 7.4595 33.5056 39.6700
355 CA GLN 355 5.0793 25.4607 33.6700
356 CA THR 356 4.6714 24.0819 30.0300
357 CA VAL 357 2.8007 17.7590 27.3500
358 CA ASP 358 3.1333 18.8834 32.4200
359 CA GLU 359 3.1731 19.0177 31.0700
360 CA ALA 360 2.5246 16.8257 25.0300
361 CA LEU 361 1.9191 14.7793 22.4100
362 CA LYS 362 2.6548 17.2661 26.6400
363 CA ASP 363 2.7999 17.7564 26.5000
364 CA ALA 364 2.1208 15.4611 24.1700
365 CA GLN 365 2.0681 15.2830 26.1800
366 CA THR 366 3.0024 18.4408 29.2100
367 CA ARG 367 3.2020 19.1155 32.3100
368 CA ILE 368 2.7646 17.6369 33.3200
369 CA THR 369 3.5673 20.3503 36.7100
370 CA LYS 370 5.1272 25.6227 44.2600

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.