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HEADER TRANSFERASE 31-JUL-08 2VZ9
TITLE CRYSTAL STRUCTURE OF MAMMALIAN FATTY ACID SYNTHASE IN
TITLE 2 COMPLEX WITH NADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FATTY ACID SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.3.1.85;
COMPND 5 OTHER_DETAILS: PURIFIED FROM NATIVE SOURCE IN
COMPND 6 ENZYMATICALLY ACTIVE FORM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: MAMMARY GLAND;
SOURCE 6 OTHER_DETAILS: LACTATING MAMMARY GLAND
KEYWDS TRANSFERASE, PHOSPHOPANTETHEINE, FATTY ACID SYNTHASE,
KEYWDS 2 MULTIENZYME, MEGASYNTHASE, FATTY ACID SYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR T.MAIER,M.LEIBUNDGUT,N.BAN
REVDAT 3 24-FEB-09 2VZ9 1 VERSN
REVDAT 2 16-SEP-08 2VZ9 1 JRNL
REVDAT 1 09-SEP-08 2VZ9 0
JRNL AUTH T.MAIER,M.LEIBUNDGUT,N.BAN
JRNL TITL THE CRYSTAL STRUCTURE OF A MAMMALIAN FATTY ACID
JRNL TITL 2 SYNTHASE.
JRNL REF SCIENCE V. 321 1315 2008
JRNL REFN ISSN 0036-8075
JRNL PMID 18772430
JRNL DOI 10.1126/SCIENCE.1161269
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.MAIER,S.JENNI,N.BAN
REMARK 1 TITL ARCHITECTURE OF MAMMALIAN FATTY ACID SYNTHASE AT
REMARK 1 TITL 2 4. 5A RESOLUTION.
REMARK 1 REF SCIENCE V. 311 1258 2006
REMARK 1 REFN ISSN 0036-8075
REMARK 1 PMID 16513975
REMARK 1 DOI 10.1126/SCIENCE.1123248
REMARK 2
REMARK 2 RESOLUTION. 3.3 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.3
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 84.09
REMARK 3 NUMBER OF REFLECTIONS : 147640
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.1930
REMARK 3 FREE R VALUE : 0.2442
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 7420
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.9700 - 10.2351 0.87 4886 227 0.1842 0.2062
REMARK 3 2 10.2351 - 8.1783 0.93 5174 265 0.1098 0.1749
REMARK 3 3 8.1783 - 7.1606 0.94 5202 275 0.1317 0.1879
REMARK 3 4 7.1606 - 6.5132 0.93 5156 302 0.1519 0.2089
REMARK 3 5 6.5132 - 6.0505 0.93 5207 277 0.1664 0.2304
REMARK 3 6 6.0505 - 5.6963 0.94 5163 263 0.1645 0.2273
REMARK 3 7 5.6963 - 5.4128 0.94 5275 243 0.1641 0.2406
REMARK 3 8 5.4128 - 5.1784 0.93 5198 268 0.1708 0.2661
REMARK 3 9 5.1784 - 4.9800 0.93 5128 309 0.1675 0.2345
REMARK 3 10 4.9800 - 4.8089 0.93 5144 257 0.1623 0.2180
REMARK 3 11 4.8089 - 4.6591 0.93 5189 290 0.1643 0.2344
REMARK 3 12 4.6591 - 4.5264 0.93 5178 288 0.1717 0.2180
REMARK 3 13 4.5264 - 4.4076 0.93 5170 298 0.1817 0.2438
REMARK 3 14 4.4076 - 4.3004 0.93 5141 298 0.1917 0.2427
REMARK 3 15 4.3004 - 4.2029 0.93 5166 284 0.2155 0.2831
REMARK 3 16 4.2029 - 4.1137 0.93 5202 263 0.2250 0.2583
REMARK 3 17 4.1137 - 4.0316 0.93 5168 274 0.2309 0.2762
REMARK 3 18 4.0316 - 3.9557 0.93 5198 283 0.2335 0.2552
REMARK 3 19 3.9557 - 3.8852 0.93 5146 276 0.2509 0.2581
REMARK 3 20 3.8852 - 3.8194 0.93 5112 260 0.2560 0.2822
REMARK 3 21 3.8194 - 3.7580 0.82 4581 248 0.2506 0.3113
REMARK 3 22 3.7580 - 3.7002 0.78 4310 232 0.2624 0.2828
REMARK 3 23 3.7002 - 3.6459 0.79 4454 228 0.2758 0.3346
REMARK 3 24 3.6459 - 3.5947 0.76 4264 210 0.2897 0.3294
REMARK 3 25 3.5947 - 3.5462 0.77 4212 233 0.3020 0.3313
REMARK 3 26 3.5462 - 3.5002 0.76 4217 235 0.3020 0.3188
REMARK 3 27 3.5002 - 3.4565 0.76 4249 191 0.3276 0.3608
REMARK 3 28 3.4565 - 3.4149 0.54 3020 166 0.3413 0.3455
REMARK 3 29 3.4149 - 3.3752 0.40 2257 107 0.3396 0.3672
REMARK 3 30 3.3752 - 3.3374 0.26 1453 70 0.3572 0.3806
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.290
REMARK 3 B_SOL : 78.380
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.37
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.38
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 32647
REMARK 3 ANGLE : 1.280 44406
REMARK 3 CHIRALITY : 0.079 5031
REMARK 3 PLANARITY : 0.006 5776
REMARK 3 DIHEDRAL : 19.474 11898
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 30
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 1:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 34.7713 73.9885 50.2140
REMARK 3 T TENSOR
REMARK 3 T11: 0.7668 T22: 0.4957
REMARK 3 T33: 1.5055 T12: 0.0118
REMARK 3 T13: 0.2057 T23: -0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 3.2878 L22: 2.2110
REMARK 3 L33: 2.3754 L12: 0.5462
REMARK 3 L13: 1.4200 L23: -0.2930
REMARK 3 S TENSOR
REMARK 3 S11: -0.4188 S12: -0.0227 S13: 0.7764
REMARK 3 S21: -0.0214 S22: -0.2199 S23: 0.1412
REMARK 3 S31: -0.1800 S32: -0.2854 S33: 0.0004
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 316:325)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.3972 57.6968 57.8677
REMARK 3 T TENSOR
REMARK 3 T11: 1.2647 T22: 0.8195
REMARK 3 T33: 1.6318 T12: -0.0615
REMARK 3 T13: 0.1757 T23: -0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.2333 L22: 0.2802
REMARK 3 L33: -0.1809 L12: -0.0998
REMARK 3 L13: -0.0203 L23: -0.0175
REMARK 3 S TENSOR
REMARK 3 S11: -0.2069 S12: 0.1351 S13: -0.3624
REMARK 3 S21: 0.8673 S22: -0.0376 S23: -0.1130
REMARK 3 S31: 1.3727 S32: -0.9443 S33: -0.0012
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 326:419)
REMARK 3 ORIGIN FOR THE GROUP (A): 25.9985 62.9952 58.2595
REMARK 3 T TENSOR
REMARK 3 T11: 0.8806 T22: 0.7545
REMARK 3 T33: 1.4078 T12: -0.0766
REMARK 3 T13: 0.3127 T23: -0.0383
REMARK 3 L TENSOR
REMARK 3 L11: 1.8354 L22: 2.6162
REMARK 3 L33: 2.6965 L12: 2.0094
REMARK 3 L13: -1.6542 L23: 1.8463
REMARK 3 S TENSOR
REMARK 3 S11: -0.1930 S12: -0.9112 S13: 0.4730
REMARK 3 S21: 0.4236 S22: -0.0213 S23: 0.4001
REMARK 3 S31: 0.7150 S32: -0.8655 S33: -0.0002
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND RESID 420:488)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.9582 62.2827 68.2223
REMARK 3 T TENSOR
REMARK 3 T11: 0.8062 T22: 0.8305
REMARK 3 T33: 1.4385 T12: 0.2002
REMARK 3 T13: 0.1250 T23: 0.0898
REMARK 3 L TENSOR
REMARK 3 L11: 1.5937 L22: 1.4576
REMARK 3 L33: 1.1288 L12: -0.4991
REMARK 3 L13: 1.1256 L23: 1.4877
REMARK 3 S TENSOR
REMARK 3 S11: -0.2810 S12: -0.5119 S13: -0.0271
REMARK 3 S21: -0.3336 S22: 0.0532 S23: -0.5900
REMARK 3 S31: -0.4155 S32: -0.0074 S33: -0.0001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND RESID 489:611)
REMARK 3 ORIGIN FOR THE GROUP (A): 79.2714 40.3263 66.3610
REMARK 3 T TENSOR
REMARK 3 T11: 0.4990 T22: 0.5621
REMARK 3 T33: 0.7312 T12: -0.0529
REMARK 3 T13: 0.0443 T23: 0.1097
REMARK 3 L TENSOR
REMARK 3 L11: 0.6277 L22: 1.9222
REMARK 3 L33: 1.7033 L12: -2.4045
REMARK 3 L13: -0.2749 L23: -1.6015
REMARK 3 S TENSOR
REMARK 3 S11: -0.0517 S12: 0.5136 S13: 0.7149
REMARK 3 S21: -0.1022 S22: 0.2205 S23: 0.0502
REMARK 3 S31: -0.3857 S32: -0.4782 S33: -0.0004
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND RESID 612:672)
REMARK 3 ORIGIN FOR THE GROUP (A): 100.8584 51.4876 78.7963
REMARK 3 T TENSOR
REMARK 3 T11: 0.8420 T22: 0.8087
REMARK 3 T33: 1.4274 T12: -0.0830
REMARK 3 T13: -0.0130 T23: -0.3031
REMARK 3 L TENSOR
REMARK 3 L11: 1.3410 L22: 0.9037
REMARK 3 L33: 2.0755 L12: -0.2485
REMARK 3 L13: 0.6961 L23: -0.6584
REMARK 3 S TENSOR
REMARK 3 S11: -0.2100 S12: -0.9625 S13: 1.0003
REMARK 3 S21: -0.1731 S22: 0.4422 S23: -0.2465
REMARK 3 S31: -0.1476 S32: -0.3162 S33: 0.0006
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN A AND RESID 673:851)
REMARK 3 ORIGIN FOR THE GROUP (A): 78.1660 53.8955 63.6483
REMARK 3 T TENSOR
REMARK 3 T11: 0.7444 T22: 0.7122
REMARK 3 T33: 1.0314 T12: 0.0017
REMARK 3 T13: 0.1203 T23: 0.1539
REMARK 3 L TENSOR
REMARK 3 L11: 2.1301 L22: 3.2198
REMARK 3 L33: -0.0827 L12: -2.2145
REMARK 3 L13: 0.4269 L23: -0.1778
REMARK 3 S TENSOR
REMARK 3 S11: 0.1622 S12: -0.1077 S13: 0.8788
REMARK 3 S21: -0.2638 S22: 0.0067 S23: -0.1764
REMARK 3 S31: -0.1209 S32: -0.1301 S33: 0.0003
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN A AND RESID 858:981)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.1338 118.0756 50.4356
REMARK 3 T TENSOR
REMARK 3 T11: 0.6802 T22: 0.5207
REMARK 3 T33: 0.9092 T12: 0.1127
REMARK 3 T13: 0.0705 T23: -0.2414
REMARK 3 L TENSOR
REMARK 3 L11: 4.1625 L22: 3.9110
REMARK 3 L33: 5.6650 L12: -0.6421
REMARK 3 L13: 2.1031 L23: -0.4202
REMARK 3 S TENSOR
REMARK 3 S11: 0.1394 S12: 0.1078 S13: -0.9272
REMARK 3 S21: -0.1474 S22: -0.0590 S23: -0.6429
REMARK 3 S31: 0.3471 S32: 0.0251 S33: -0.0021
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN A AND RESID 982:1105)
REMARK 3 ORIGIN FOR THE GROUP (A): 66.2281 125.5033 52.7652
REMARK 3 T TENSOR
REMARK 3 T11: 0.7735 T22: 0.7170
REMARK 3 T33: 0.5380 T12: 0.1147
REMARK 3 T13: 0.2004 T23: -0.0725
REMARK 3 L TENSOR
REMARK 3 L11: 3.0696 L22: 4.4242
REMARK 3 L33: 2.9958 L12: 1.1424
REMARK 3 L13: 3.4895 L23: -0.2012
REMARK 3 S TENSOR
REMARK 3 S11: 0.3308 S12: 0.4104 S13: -0.3465
REMARK 3 S21: -0.1763 S22: 0.0632 S23: -0.6508
REMARK 3 S31: 0.2032 S32: 0.5345 S33: -0.0014
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN A AND RESID 1106:1192)
REMARK 3 ORIGIN FOR THE GROUP (A): 65.4027 112.0573 109.0744
REMARK 3 T TENSOR
REMARK 3 T11: 2.4126 T22: 1.5480
REMARK 3 T33: 1.6833 T12: 0.0472
REMARK 3 T13: 0.1629 T23: 0.0886
REMARK 3 L TENSOR
REMARK 3 L11: 0.0320 L22: 0.5178
REMARK 3 L33: 0.8054 L12: -0.6493
REMARK 3 L13: 0.1078 L23: 0.4030
REMARK 3 S TENSOR
REMARK 3 S11: -0.7956 S12: -0.5331 S13: -0.1412
REMARK 3 S21: 0.7905 S22: -0.3889 S23: 0.5875
REMARK 3 S31: 1.0300 S32: -0.4876 S33: -0.0008
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN A AND RESID 1193:1418)
REMARK 3 ORIGIN FOR THE GROUP (A): 73.6291 95.9115 108.1573
REMARK 3 T TENSOR
REMARK 3 T11: 2.4840 T22: 1.7726
REMARK 3 T33: 1.6518 T12: 0.1120
REMARK 3 T13: -0.2447 T23: 0.6204
REMARK 3 L TENSOR
REMARK 3 L11: 0.7668 L22: 0.8811
REMARK 3 L33: 2.0706 L12: 1.2043
REMARK 3 L13: 0.1883 L23: 0.4718
REMARK 3 S TENSOR
REMARK 3 S11: 0.0625 S12: -1.0262 S13: -1.0142
REMARK 3 S21: 0.4539 S22: -0.4419 S23: -0.0522
REMARK 3 S31: 1.0227 S32: -0.0794 S33: 0.0006
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN A AND RESID 1419:1505)
REMARK 3 ORIGIN FOR THE GROUP (A): 98.6315 108.2773 95.7624
REMARK 3 T TENSOR
REMARK 3 T11: 2.0361 T22: 2.0067
REMARK 3 T33: 1.5638 T12: 0.5088
REMARK 3 T13: -0.6489 T23: 0.2305
REMARK 3 L TENSOR
REMARK 3 L11: 1.8705 L22: 0.4612
REMARK 3 L33: 1.4541 L12: -0.0120
REMARK 3 L13: -0.7474 L23: -0.6295
REMARK 3 S TENSOR
REMARK 3 S11: 0.0490 S12: 0.0406 S13: -1.1744
REMARK 3 S21: 1.6777 S22: -0.1093 S23: -1.3601
REMARK 3 S31: 0.4774 S32: 0.7196 S33: 0.0009
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN A AND RESID 1506:1856)
REMARK 3 ORIGIN FOR THE GROUP (A): 44.5259 144.6223 80.7299
REMARK 3 T TENSOR
REMARK 3 T11: 0.8265 T22: 1.0005
REMARK 3 T33: 0.4171 T12: -0.0950
REMARK 3 T13: 0.1393 T23: -0.1845
REMARK 3 L TENSOR
REMARK 3 L11: 4.7849 L22: 0.6465
REMARK 3 L33: 2.8566 L12: -0.4066
REMARK 3 L13: 2.9451 L23: -0.2020
REMARK 3 S TENSOR
REMARK 3 S11: -0.0951 S12: -1.0616 S13: -0.0532
REMARK 3 S21: 0.3427 S22: -0.1214 S23: -0.0371
REMARK 3 S31: 0.3395 S32: -0.2366 S33: 0.0002
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN A AND RESID 1857:2043)
REMARK 3 ORIGIN FOR THE GROUP (A): 83.7512 132.0790 82.0134
REMARK 3 T TENSOR
REMARK 3 T11: 0.8789 T22: 0.9209
REMARK 3 T33: 0.7278 T12: 0.0417
REMARK 3 T13: -0.1874 T23: 0.1199
REMARK 3 L TENSOR
REMARK 3 L11: 2.9689 L22: 1.8223
REMARK 3 L33: 4.0322 L12: 0.0382
REMARK 3 L13: 0.4126 L23: -0.6807
REMARK 3 S TENSOR
REMARK 3 S11: -0.1371 S12: -0.4746 S13: -0.4558
REMARK 3 S21: 0.2370 S22: 0.0052 S23: -0.3655
REMARK 3 S31: 0.3834 S32: 0.6756 S33: -0.0009
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN A AND RESID 2044:2113)
REMARK 3 ORIGIN FOR THE GROUP (A): 77.9168 120.0860 84.0901
REMARK 3 T TENSOR
REMARK 3 T11: 1.2458 T22: 1.0503
REMARK 3 T33: 0.9466 T12: 0.1343
REMARK 3 T13: -0.0882 T23: 0.2021
REMARK 3 L TENSOR
REMARK 3 L11: 1.1273 L22: 1.4341
REMARK 3 L33: 1.1667 L12: 0.1519
REMARK 3 L13: -1.5285 L23: -1.4430
REMARK 3 S TENSOR
REMARK 3 S11: -0.1704 S12: 0.3378 S13: -0.6111
REMARK 3 S21: 0.7188 S22: 0.3600 S23: -0.9354
REMARK 3 S31: 1.2605 S32: 1.0127 S33: -0.0019
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN B AND RESID 1:315)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.0175 80.9895 25.6071
REMARK 3 T TENSOR
REMARK 3 T11: 1.1970 T22: 1.0101
REMARK 3 T33: 1.7497 T12: 0.2027
REMARK 3 T13: 0.1697 T23: 0.6890
REMARK 3 L TENSOR
REMARK 3 L11: 4.0577 L22: 1.5391
REMARK 3 L33: 2.1656 L12: -0.7825
REMARK 3 L13: 0.7057 L23: 0.1327
REMARK 3 S TENSOR
REMARK 3 S11: 0.1662 S12: 1.2302 S13: 1.1966
REMARK 3 S21: -0.6620 S22: -0.6237 S23: -0.2037
REMARK 3 S31: -0.3143 S32: 0.5174 S33: 0.0003
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN B AND RESID 316:325)
REMARK 3 ORIGIN FOR THE GROUP (A): 56.5628 71.2184 10.6567
REMARK 3 T TENSOR
REMARK 3 T11: 1.4947 T22: 2.1622
REMARK 3 T33: 1.9252 T12: 0.1599
REMARK 3 T13: 0.0387 T23: 1.0794
REMARK 3 L TENSOR
REMARK 3 L11: 0.0587 L22: 0.2758
REMARK 3 L33: -0.0996 L12: -0.0418
REMARK 3 L13: -0.4206 L23: 0.3249
REMARK 3 S TENSOR
REMARK 3 S11: -0.2246 S12: 1.1414 S13: -0.0714
REMARK 3 S21: -0.8522 S22: -0.4060 S23: 0.5364
REMARK 3 S31: 1.0126 S32: 1.0390 S33: -0.0038
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN B AND RESID 326:419)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8876 75.9082 13.0321
REMARK 3 T TENSOR
REMARK 3 T11: 1.5435 T22: 1.8476
REMARK 3 T33: 1.7094 T12: 0.3472
REMARK 3 T13: 0.3102 T23: 0.7307
REMARK 3 L TENSOR
REMARK 3 L11: 0.7441 L22: 1.7976
REMARK 3 L33: 0.3192 L12: 0.2509
REMARK 3 L13: -1.1169 L23: -0.2548
REMARK 3 S TENSOR
REMARK 3 S11: -0.0016 S12: 1.4340 S13: 0.4063
REMARK 3 S21: -0.9748 S22: -0.3611 S23: 0.4902
REMARK 3 S31: -0.2264 S32: 0.9884 S33: -0.0004
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN B AND RESID 420:488)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.8476 80.2863 3.9779
REMARK 3 T TENSOR
REMARK 3 T11: 1.8867 T22: 1.6441
REMARK 3 T33: 1.7379 T12: 0.3987
REMARK 3 T13: -0.0278 T23: 0.2112
REMARK 3 L TENSOR
REMARK 3 L11: 0.4962 L22: -0.1750
REMARK 3 L33: -0.1889 L12: 0.6567
REMARK 3 L13: -0.0022 L23: 0.6646
REMARK 3 S TENSOR
REMARK 3 S11: -0.2078 S12: 1.3140 S13: -0.0999
REMARK 3 S21: -0.0005 S22: -0.4543 S23: 1.0622
REMARK 3 S31: 0.3701 S32: -0.3073 S33: -0.0012
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN B AND RESID 489:611)
REMARK 3 ORIGIN FOR THE GROUP (A): -4.1920 59.2212 -4.8436
REMARK 3 T TENSOR
REMARK 3 T11: 1.9280 T22: 1.7940
REMARK 3 T33: 1.2739 T12: 0.3589
REMARK 3 T13: -0.2348 T23: -0.1207
REMARK 3 L TENSOR
REMARK 3 L11: 1.4656 L22: 1.1185
REMARK 3 L33: 0.1041 L12: 0.6340
REMARK 3 L13: 0.7582 L23: -0.3475
REMARK 3 S TENSOR
REMARK 3 S11: 0.0320 S12: 0.6408 S13: -0.0726
REMARK 3 S21: -0.6711 S22: -0.1614 S23: 0.2359
REMARK 3 S31: -0.0251 S32: -0.1387 S33: 0.0001
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN B AND RESID 612:672)
REMARK 3 ORIGIN FOR THE GROUP (A): -29.3340 72.0452 -9.7053
REMARK 3 T TENSOR
REMARK 3 T11: 2.6213 T22: 2.2476
REMARK 3 T33: 1.6630 T12: 0.2388
REMARK 3 T13: -0.6188 T23: -0.0369
REMARK 3 L TENSOR
REMARK 3 L11: -0.5661 L22: -0.3892
REMARK 3 L33: -0.1900 L12: -0.0395
REMARK 3 L13: -0.5008 L23: 0.6315
REMARK 3 S TENSOR
REMARK 3 S11: -1.1437 S12: 0.4606 S13: 1.0526
REMARK 3 S21: -0.7964 S22: -0.5639 S23: 1.5425
REMARK 3 S31: -0.9940 S32: 0.3280 S33: -0.0083
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN B AND RESID 673:851)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8488 69.6080 4.1242
REMARK 3 T TENSOR
REMARK 3 T11: 1.7935 T22: 1.6742
REMARK 3 T33: 1.4512 T12: 0.3537
REMARK 3 T13: -0.1299 T23: 0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 0.7710 L22: 0.2145
REMARK 3 L33: 1.8289 L12: 0.0491
REMARK 3 L13: 0.9538 L23: 0.3046
REMARK 3 S TENSOR
REMARK 3 S11: 0.1472 S12: 0.2317 S13: 0.0668
REMARK 3 S21: -0.5152 S22: -0.3760 S23: -0.0046
REMARK 3 S31: 0.1182 S32: -0.2071 S33: -0.0001
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN B AND RESID 858:981)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1847 122.2808 48.6516
REMARK 3 T TENSOR
REMARK 3 T11: 0.6580 T22: 0.6400
REMARK 3 T33: 0.9776 T12: -0.1781
REMARK 3 T13: -0.0136 T23: -0.2687
REMARK 3 L TENSOR
REMARK 3 L11: 5.4710 L22: 4.2286
REMARK 3 L33: 2.7144 L12: -0.8879
REMARK 3 L13: 1.8780 L23: 0.2786
REMARK 3 S TENSOR
REMARK 3 S11: 0.2886 S12: 0.1298 S13: -1.1509
REMARK 3 S21: -0.2271 S22: -0.2654 S23: 0.3297
REMARK 3 S31: 0.5509 S32: 0.2285 S33: -0.0001
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN B AND RESID 982:1105)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9143 132.4228 51.7424
REMARK 3 T TENSOR
REMARK 3 T11: 0.7053 T22: 0.8395
REMARK 3 T33: 0.5878 T12: -0.1342
REMARK 3 T13: 0.0239 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 3.1737 L22: 3.1704
REMARK 3 L33: 2.1886 L12: -1.5331
REMARK 3 L13: 2.3942 L23: -0.2560
REMARK 3 S TENSOR
REMARK 3 S11: 0.0714 S12: -0.1605 S13: -0.3992
REMARK 3 S21: -0.0122 S22: 0.0644 S23: 0.5592
REMARK 3 S31: -0.0029 S32: -0.3739 S33: -0.0001
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN B AND RESID 1106:1192)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.1889 152.0391 -3.8463
REMARK 3 T TENSOR
REMARK 3 T11: 1.7529 T22: 1.6026
REMARK 3 T33: 1.0935 T12: -0.2805
REMARK 3 T13: -0.1550 T23: -0.1111
REMARK 3 L TENSOR
REMARK 3 L11: 0.6758 L22: 0.6306
REMARK 3 L33: 0.4797 L12: -0.2328
REMARK 3 L13: 0.4514 L23: 0.2475
REMARK 3 S TENSOR
REMARK 3 S11: -0.0939 S12: 0.4329 S13: 0.0606
REMARK 3 S21: -0.6486 S22: 0.0772 S23: -0.3970
REMARK 3 S31: 0.5545 S32: -0.6185 S33: -0.0003
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN B AND RESID 1193:1418)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4418 139.9657 -10.3078
REMARK 3 T TENSOR
REMARK 3 T11: 2.1877 T22: 2.1260
REMARK 3 T33: 0.9957 T12: -0.4000
REMARK 3 T13: -0.4602 T23: -0.2678
REMARK 3 L TENSOR
REMARK 3 L11: 2.2237 L22: 0.8562
REMARK 3 L33: 1.5497 L12: 0.7333
REMARK 3 L13: -0.2803 L23: -0.2820
REMARK 3 S TENSOR
REMARK 3 S11: -0.3157 S12: 1.1860 S13: -0.5436
REMARK 3 S21: -0.6730 S22: 0.0676 S23: -0.2775
REMARK 3 S31: 0.2676 S32: -0.7597 S33: -0.0005
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN B AND RESID 1419:1505)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.8176 149.2897 8.5479
REMARK 3 T TENSOR
REMARK 3 T11: 1.5987 T22: 2.6337
REMARK 3 T33: 1.2768 T12: -0.3956
REMARK 3 T13: -0.8771 T23: 0.1209
REMARK 3 L TENSOR
REMARK 3 L11: 1.1278 L22: 0.2358
REMARK 3 L33: 1.3833 L12: 0.6918
REMARK 3 L13: -1.1108 L23: -0.5079
REMARK 3 S TENSOR
REMARK 3 S11: -0.4636 S12: 1.1938 S13: -0.2621
REMARK 3 S21: -1.5764 S22: 0.1550 S23: 1.6484
REMARK 3 S31: 0.0740 S32: -1.0239 S33: -0.0004
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN B AND RESID 1506:1856)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.6379 158.7576 38.1652
REMARK 3 T TENSOR
REMARK 3 T11: 0.8803 T22: 0.9419
REMARK 3 T33: 0.5708 T12: 0.0727
REMARK 3 T13: -0.0217 T23: 0.0542
REMARK 3 L TENSOR
REMARK 3 L11: 3.7815 L22: 0.5681
REMARK 3 L33: 1.9449 L12: -0.6338
REMARK 3 L13: 2.0286 L23: -0.8449
REMARK 3 S TENSOR
REMARK 3 S11: -0.2227 S12: 0.9083 S13: 0.4646
REMARK 3 S21: -0.4889 S22: -0.1242 S23: -0.0040
REMARK 3 S31: -0.0775 S32: -0.3372 S33: 0.0004
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN B AND RESID 1857:2043)
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8786 157.4477 32.0220
REMARK 3 T TENSOR
REMARK 3 T11: 0.6090 T22: 0.9394
REMARK 3 T33: 0.7051 T12: -0.0226
REMARK 3 T13: -0.2653 T23: -0.0805
REMARK 3 L TENSOR
REMARK 3 L11: 2.1907 L22: 2.2873
REMARK 3 L33: 3.9778 L12: -0.0014
REMARK 3 L13: -0.6496 L23: -0.9738
REMARK 3 S TENSOR
REMARK 3 S11: -0.0243 S12: 0.8676 S13: 0.1528
REMARK 3 S21: -0.4062 S22: -0.0026 S23: 0.4210
REMARK 3 S31: 0.1260 S32: -0.2816 S33: -0.0006
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN B AND RESID 2044:2113)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6028 147.5093 23.2997
REMARK 3 T TENSOR
REMARK 3 T11: 0.8762 T22: 1.3124
REMARK 3 T33: 0.4702 T12: -0.1396
REMARK 3 T13: -0.2732 T23: -0.3115
REMARK 3 L TENSOR
REMARK 3 L11: 1.9158 L22: 0.5380
REMARK 3 L33: 1.9867 L12: 0.0756
REMARK 3 L13: -0.6255 L23: 1.3112
REMARK 3 S TENSOR
REMARK 3 S11: -0.4442 S12: 0.6141 S13: -0.5148
REMARK 3 S21: 0.0123 S22: 0.7275 S23: 0.3485
REMARK 3 S31: 0.7217 S32: -0.2524 S33: -0.0008
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 26
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1:116 OR RESSEQ
REMARK 3 118:120 OR RESSEQ 129:205 OR RESSEQ
REMARK 3 207:211 OR RESSEQ 220:235 OR RESSEQ
REMARK 3 237:287 OR RESSEQ 289:320 OR RESSEQ
REMARK 3 325:351 OR RESSEQ 355:368 OR RESSEQ
REMARK 3 370:473))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 1:116 OR RESSEQ
REMARK 3 118:120 OR RESSEQ 129:205 OR RESSEQ
REMARK 3 207:211 OR RESSEQ 220:235 OR RESSEQ
REMARK 3 237:287 OR RESSEQ 289:320 OR RESSEQ
REMARK 3 325:351 OR RESSEQ 355:368 OR RESSEQ
REMARK 3 370:473))
REMARK 3 ATOM PAIRS NUMBER : 3329
REMARK 3 RMSD : 0.034
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 474:479 OR RESSEQ
REMARK 3 485:489))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 474:479 OR RESSEQ
REMARK 3 485:489))
REMARK 3 ATOM PAIRS NUMBER : 65
REMARK 3 RMSD : 0.043
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 490:499 OR RESSEQ
REMARK 3 500:503 OR RESSEQ 505:538 OR RESSEQ
REMARK 3 548:579 OR RESSEQ 585:594 OR RESSEQ
REMARK 3 598:610))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 490:499 OR RESSEQ
REMARK 3 500:503 OR RESSEQ 505:538 OR RESSEQ
REMARK 3 548:579 OR RESSEQ 585:594 OR RESSEQ
REMARK 3 598:610))
REMARK 3 ATOM PAIRS NUMBER : 785
REMARK 3 RMSD : 0.037
REMARK 3 NCS GROUP : 4
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 626:633)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 626:633)
REMARK 3 ATOM PAIRS NUMBER : 73
REMARK 3 RMSD : 0.037
REMARK 3 NCS GROUP : 5
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 637:642)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 637:642)
REMARK 3 ATOM PAIRS NUMBER : 37
REMARK 3 RMSD : 0.047
REMARK 3 NCS GROUP : 6
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 648:652)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 648:652)
REMARK 3 ATOM PAIRS NUMBER : 35
REMARK 3 RMSD : 0.035
REMARK 3 NCS GROUP : 7
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 683:702)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 683:702)
REMARK 3 ATOM PAIRS NUMBER : 168
REMARK 3 RMSD : 0.034
REMARK 3 NCS GROUP : 8
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 706:722 OR RESSEQ
REMARK 3 724:732 OR RESSEQ 734:750 OR RESSEQ
REMARK 3 752:755))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 706:722 OR RESSEQ
REMARK 3 724:732 OR RESSEQ 734:750 OR RESSEQ
REMARK 3 752:755))
REMARK 3 ATOM PAIRS NUMBER : 373
REMARK 3 RMSD : 0.032
REMARK 3 NCS GROUP : 9
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 756:817)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 756:817)
REMARK 3 ATOM PAIRS NUMBER : 476
REMARK 3 RMSD : 0.034
REMARK 3 NCS GROUP : 10
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 822:843)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 822:843)
REMARK 3 ATOM PAIRS NUMBER : 178
REMARK 3 RMSD : 0.028
REMARK 3 NCS GROUP : 11
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 859:970)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 859:970)
REMARK 3 ATOM PAIRS NUMBER : 884
REMARK 3 RMSD : 0.038
REMARK 3 NCS GROUP : 12
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 985:1052 OR RESSEQ
REMARK 3 1054:1104))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 985:1052 OR RESSEQ
REMARK 3 1054:1104))
REMARK 3 ATOM PAIRS NUMBER : 942
REMARK 3 RMSD : 0.041
REMARK 3 NCS GROUP : 13
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1105:1111)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1105:1111)
REMARK 3 ATOM PAIRS NUMBER : 64
REMARK 3 RMSD : 0.029
REMARK 3 NCS GROUP : 14
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1113:1135)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1113:1135)
REMARK 3 ATOM PAIRS NUMBER : 171
REMARK 3 RMSD : 0.114
REMARK 3 NCS GROUP : 15
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1216:1275 OR
REMARK 3 RESSEQ 1277:1281 OR RESSEQ 1283:1289 OR
REMARK 3 RESSEQ 1294:1300))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 1216:1275 OR
REMARK 3 RESSEQ 1277:1281 OR RESSEQ 1283:1289 OR
REMARK 3 RESSEQ 1294:1300))
REMARK 3 ATOM PAIRS NUMBER : 589
REMARK 3 RMSD : 0.181
REMARK 3 NCS GROUP : 16
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1312:1320)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1312:1320)
REMARK 3 ATOM PAIRS NUMBER : 61
REMARK 3 RMSD : 0.255
REMARK 3 NCS GROUP : 17
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1327:1349)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1327:1349)
REMARK 3 ATOM PAIRS NUMBER : 162
REMARK 3 RMSD : 0.131
REMARK 3 NCS GROUP : 18
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1376:1385)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1376:1385)
REMARK 3 ATOM PAIRS NUMBER : 79
REMARK 3 RMSD : 0.162
REMARK 3 NCS GROUP : 19
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1387:1406)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1387:1406)
REMARK 3 ATOM PAIRS NUMBER : 165
REMARK 3 RMSD : 0.155
REMARK 3 NCS GROUP : 20
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1414:1433)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1414:1433)
REMARK 3 ATOM PAIRS NUMBER : 167
REMARK 3 RMSD : 0.143
REMARK 3 NCS GROUP : 21
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1438:1470)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1438:1470)
REMARK 3 ATOM PAIRS NUMBER : 245
REMARK 3 RMSD : 0.160
REMARK 3 NCS GROUP : 22
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1471:1482)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1471:1482)
REMARK 3 ATOM PAIRS NUMBER : 82
REMARK 3 RMSD : 0.357
REMARK 3 NCS GROUP : 23
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1492:1512)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1492:1512)
REMARK 3 ATOM PAIRS NUMBER : 167
REMARK 3 RMSD : 0.145
REMARK 3 NCS GROUP : 24
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND RESSEQ 1513:1526)
REMARK 3 SELECTION : CHAIN B AND RESSEQ 1513:1526)
REMARK 3 ATOM PAIRS NUMBER : 125
REMARK 3 RMSD : 0.221
REMARK 3 NCS GROUP : 25
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1563:1594 OR
REMARK 3 RESSEQ 1696:1798 OR RESSEQ 1803:1846 OR
REMARK 3 RESSEQ 1848:1850 OR RESSEQ 1852:1855))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 1563:1594 OR
REMARK 3 RESSEQ 1696:1798 OR RESSEQ 1803:1846 OR
REMARK 3 RESSEQ 1848:1850 OR RESSEQ 1852:1855))
REMARK 3 ATOM PAIRS NUMBER : 1445
REMARK 3 RMSD : 0.041
REMARK 3 NCS GROUP : 26
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 1872:1974 OR
REMARK 3 RESSEQ 1991:2071 OR RESSEQ 2076:2110))
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 1872:1974 OR
REMARK 3 RESSEQ 1991:2071 OR RESSEQ 2076:2110))
REMARK 3 ATOM PAIRS NUMBER : 1649
REMARK 3 RMSD : 0.038
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: UNBIASED ELECTRON DENSITY MAPS FOR
REMARK 3 THE LINKERS (RESIDUES 852-857) IN THE REGION OF THE CENTRAL
REMARK 3 CONNECTION ARE NOT CONTIGUOUS FOR ONE OR TWO AMINO ACIDS SUCH
REMARK 3 THAT THE POSSIBILITY OF ALTERNATIVE CONNECTIVITY OR MULTIPLE
REMARK 3 CONFORMATIONS FOR THIS REGION CAN NOT BE EXCLUDED.
REMARK 4
REMARK 4 2VZ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-08.
REMARK 100 THE PDBE ID CODE IS EBI-37081.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 8
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9992
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 80129
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.20
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NONE
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.4
REMARK 200 DATA REDUNDANCY : 5.7
REMARK 200 R MERGE (I) : 0.16
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 68.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.1
REMARK 200 R MERGE FOR SHELL (I) : 0.93
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 2CF2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 122.44500
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 156690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 THR A 1152
REMARK 465 LYS A 1153
REMARK 465 VAL A 1154
REMARK 465 ALA A 1155
REMARK 465 GLN A 1156
REMARK 465 GLN A 1157
REMARK 465 GLY A 1158
REMARK 465 LEU A 1159
REMARK 465 LYS A 1160
REMARK 465 MET A 1161
REMARK 465 VAL A 1162
REMARK 465 VAL A 1163
REMARK 465 PRO A 1164
REMARK 465 GLY A 1165
REMARK 465 LEU A 1166
REMARK 465 ASP A 1167
REMARK 465 GLY A 1168
REMARK 465 ALA A 1169
REMARK 465 GLN A 1170
REMARK 465 ALA A 1171
REMARK 465 PRO A 1172
REMARK 465 ARG A 1173
REMARK 465 GLU A 1174
REMARK 465 ALA A 1175
REMARK 465 PRO A 1176
REMARK 465 GLN A 1177
REMARK 465 GLN A 1178
REMARK 465 SER A 1179
REMARK 465 LEU A 1196
REMARK 465 GLN A 1197
REMARK 465 LEU A 1198
REMARK 465 GLU A 1199
REMARK 465 LYS A 2114
REMARK 465 LYS A 2115
REMARK 465 ALA A 2116
REMARK 465 ALA A 2117
REMARK 465 ALA A 2118
REMARK 465 PRO A 2119
REMARK 465 ARG A 2120
REMARK 465 ASP A 2121
REMARK 465 GLY A 2122
REMARK 465 SER A 2123
REMARK 465 SER A 2124
REMARK 465 GLN A 2125
REMARK 465 LYS A 2126
REMARK 465 ASP A 2127
REMARK 465 LEU A 2128
REMARK 465 VAL A 2129
REMARK 465 LYS A 2130
REMARK 465 ALA A 2131
REMARK 465 VAL A 2132
REMARK 465 ALA A 2133
REMARK 465 HIS A 2134
REMARK 465 ILE A 2135
REMARK 465 LEU A 2136
REMARK 465 GLY A 2137
REMARK 465 ILE A 2138
REMARK 465 ARG A 2139
REMARK 465 ASP A 2140
REMARK 465 VAL A 2141
REMARK 465 ALA A 2142
REMARK 465 SER A 2143
REMARK 465 ILE A 2144
REMARK 465 ASN A 2145
REMARK 465 PRO A 2146
REMARK 465 ASP A 2147
REMARK 465 SER A 2148
REMARK 465 THR A 2149
REMARK 465 LEU A 2150
REMARK 465 VAL A 2151
REMARK 465 ASP A 2152
REMARK 465 LEU A 2153
REMARK 465 GLY A 2154
REMARK 465 LEU A 2155
REMARK 465 ASP A 2156
REMARK 465 SER A 2157
REMARK 465 LEU A 2158
REMARK 465 MET A 2159
REMARK 465 GLY A 2160
REMARK 465 VAL A 2161
REMARK 465 GLU A 2162
REMARK 465 VAL A 2163
REMARK 465 ARG A 2164
REMARK 465 GLN A 2165
REMARK 465 ILE A 2166
REMARK 465 LEU A 2167
REMARK 465 GLU A 2168
REMARK 465 ARG A 2169
REMARK 465 GLU A 2170
REMARK 465 HIS A 2171
REMARK 465 ASP A 2172
REMARK 465 LEU A 2173
REMARK 465 VAL A 2174
REMARK 465 LEU A 2175
REMARK 465 SER A 2176
REMARK 465 MET A 2177
REMARK 465 ARG A 2178
REMARK 465 GLU A 2179
REMARK 465 VAL A 2180
REMARK 465 ARG A 2181
REMARK 465 GLN A 2182
REMARK 465 LEU A 2183
REMARK 465 SER A 2184
REMARK 465 LEU A 2185
REMARK 465 ARG A 2186
REMARK 465 LYS A 2187
REMARK 465 LEU A 2188
REMARK 465 GLN A 2189
REMARK 465 GLU A 2190
REMARK 465 LEU A 2191
REMARK 465 SER A 2192
REMARK 465 SER A 2193
REMARK 465 LYS A 2194
REMARK 465 THR A 2195
REMARK 465 SER A 2196
REMARK 465 THR A 2197
REMARK 465 ASP A 2198
REMARK 465 ALA A 2199
REMARK 465 ASP A 2200
REMARK 465 PRO A 2201
REMARK 465 ALA A 2202
REMARK 465 THR A 2203
REMARK 465 PRO A 2204
REMARK 465 THR A 2205
REMARK 465 SER A 2206
REMARK 465 HIS A 2207
REMARK 465 GLU A 2208
REMARK 465 ASP A 2209
REMARK 465 SER A 2210
REMARK 465 PRO A 2211
REMARK 465 VAL A 2212
REMARK 465 ARG A 2213
REMARK 465 GLN A 2214
REMARK 465 GLN A 2215
REMARK 465 ALA A 2216
REMARK 465 THR A 2217
REMARK 465 LEU A 2218
REMARK 465 ASN A 2219
REMARK 465 LEU A 2220
REMARK 465 SER A 2221
REMARK 465 THR A 2222
REMARK 465 LEU A 2223
REMARK 465 LEU A 2224
REMARK 465 VAL A 2225
REMARK 465 ASN A 2226
REMARK 465 PRO A 2227
REMARK 465 GLU A 2228
REMARK 465 GLY A 2229
REMARK 465 PRO A 2230
REMARK 465 THR A 2231
REMARK 465 LEU A 2232
REMARK 465 THR A 2233
REMARK 465 ARG A 2234
REMARK 465 LEU A 2235
REMARK 465 ASN A 2236
REMARK 465 SER A 2237
REMARK 465 VAL A 2238
REMARK 465 GLN A 2239
REMARK 465 SER A 2240
REMARK 465 ALA A 2241
REMARK 465 GLU A 2242
REMARK 465 ARG A 2243
REMARK 465 PRO A 2244
REMARK 465 LEU A 2245
REMARK 465 PHE A 2246
REMARK 465 LEU A 2247
REMARK 465 VAL A 2248
REMARK 465 HIS A 2249
REMARK 465 PRO A 2250
REMARK 465 ILE A 2251
REMARK 465 GLU A 2252
REMARK 465 GLY A 2253
REMARK 465 SER A 2254
REMARK 465 ILE A 2255
REMARK 465 THR A 2256
REMARK 465 VAL A 2257
REMARK 465 PHE A 2258
REMARK 465 HIS A 2259
REMARK 465 GLY A 2260
REMARK 465 LEU A 2261
REMARK 465 ALA A 2262
REMARK 465 ALA A 2263
REMARK 465 LYS A 2264
REMARK 465 LEU A 2265
REMARK 465 SER A 2266
REMARK 465 ILE A 2267
REMARK 465 PRO A 2268
REMARK 465 THR A 2269
REMARK 465 TYR A 2270
REMARK 465 GLY A 2271
REMARK 465 LEU A 2272
REMARK 465 GLN A 2273
REMARK 465 CYS A 2274
REMARK 465 THR A 2275
REMARK 465 GLY A 2276
REMARK 465 ALA A 2277
REMARK 465 ALA A 2278
REMARK 465 PRO A 2279
REMARK 465 LEU A 2280
REMARK 465 ASP A 2281
REMARK 465 SER A 2282
REMARK 465 ILE A 2283
REMARK 465 GLN A 2284
REMARK 465 SER A 2285
REMARK 465 LEU A 2286
REMARK 465 ALA A 2287
REMARK 465 SER A 2288
REMARK 465 TYR A 2289
REMARK 465 TYR A 2290
REMARK 465 ILE A 2291
REMARK 465 GLU A 2292
REMARK 465 CYS A 2293
REMARK 465 ILE A 2294
REMARK 465 ARG A 2295
REMARK 465 GLN A 2296
REMARK 465 VAL A 2297
REMARK 465 GLN A 2298
REMARK 465 PRO A 2299
REMARK 465 GLU A 2300
REMARK 465 GLY A 2301
REMARK 465 PRO A 2302
REMARK 465 TYR A 2303
REMARK 465 ARG A 2304
REMARK 465 ILE A 2305
REMARK 465 ALA A 2306
REMARK 465 GLY A 2307
REMARK 465 TYR A 2308
REMARK 465 SER A 2309
REMARK 465 TYR A 2310
REMARK 465 GLY A 2311
REMARK 465 ALA A 2312
REMARK 465 CYS A 2313
REMARK 465 VAL A 2314
REMARK 465 ALA A 2315
REMARK 465 PHE A 2316
REMARK 465 GLU A 2317
REMARK 465 MET A 2318
REMARK 465 CYS A 2319
REMARK 465 SER A 2320
REMARK 465 GLN A 2321
REMARK 465 LEU A 2322
REMARK 465 GLN A 2323
REMARK 465 ALA A 2324
REMARK 465 GLN A 2325
REMARK 465 GLN A 2326
REMARK 465 SER A 2327
REMARK 465 ALA A 2328
REMARK 465 THR A 2329
REMARK 465 PRO A 2330
REMARK 465 GLY A 2331
REMARK 465 ASN A 2332
REMARK 465 HIS A 2333
REMARK 465 SER A 2334
REMARK 465 LEU A 2335
REMARK 465 PHE A 2336
REMARK 465 LEU A 2337
REMARK 465 PHE A 2338
REMARK 465 ASP A 2339
REMARK 465 GLY A 2340
REMARK 465 SER A 2341
REMARK 465 HIS A 2342
REMARK 465 THR A 2343
REMARK 465 PHE A 2344
REMARK 465 VAL A 2345
REMARK 465 LEU A 2346
REMARK 465 ALA A 2347
REMARK 465 TYR A 2348
REMARK 465 THR A 2349
REMARK 465 GLN A 2350
REMARK 465 SER A 2351
REMARK 465 VAL A 2352
REMARK 465 ARG A 2353
REMARK 465 ALA A 2354
REMARK 465 LYS A 2355
REMARK 465 MET A 2356
REMARK 465 THR A 2357
REMARK 465 PRO A 2358
REMARK 465 GLY A 2359
REMARK 465 CYS A 2360
REMARK 465 GLU A 2361
REMARK 465 ALA A 2362
REMARK 465 GLU A 2363
REMARK 465 ALA A 2364
REMARK 465 GLU A 2365
REMARK 465 ALA A 2366
REMARK 465 LYS A 2367
REMARK 465 ALA A 2368
REMARK 465 MET A 2369
REMARK 465 TYR A 2370
REMARK 465 PHE A 2371
REMARK 465 PHE A 2372
REMARK 465 VAL A 2373
REMARK 465 GLN A 2374
REMARK 465 GLN A 2375
REMARK 465 PHE A 2376
REMARK 465 THR A 2377
REMARK 465 ASP A 2378
REMARK 465 MET A 2379
REMARK 465 GLU A 2380
REMARK 465 GLN A 2381
REMARK 465 GLY A 2382
REMARK 465 LYS A 2383
REMARK 465 VAL A 2384
REMARK 465 LEU A 2385
REMARK 465 GLU A 2386
REMARK 465 ALA A 2387
REMARK 465 LEU A 2388
REMARK 465 ILE A 2389
REMARK 465 PRO A 2390
REMARK 465 LEU A 2391
REMARK 465 GLN A 2392
REMARK 465 GLY A 2393
REMARK 465 LEU A 2394
REMARK 465 GLU A 2395
REMARK 465 ALA A 2396
REMARK 465 ARG A 2397
REMARK 465 VAL A 2398
REMARK 465 ALA A 2399
REMARK 465 ALA A 2400
REMARK 465 THR A 2401
REMARK 465 VAL A 2402
REMARK 465 ASP A 2403
REMARK 465 LEU A 2404
REMARK 465 ILE A 2405
REMARK 465 THR A 2406
REMARK 465 GLN A 2407
REMARK 465 SER A 2408
REMARK 465 HIS A 2409
REMARK 465 ALA A 2410
REMARK 465 GLY A 2411
REMARK 465 LEU A 2412
REMARK 465 ASP A 2413
REMARK 465 ARG A 2414
REMARK 465 HIS A 2415
REMARK 465 ALA A 2416
REMARK 465 LEU A 2417
REMARK 465 SER A 2418
REMARK 465 PHE A 2419
REMARK 465 ALA A 2420
REMARK 465 ALA A 2421
REMARK 465 ARG A 2422
REMARK 465 SER A 2423
REMARK 465 PHE A 2424
REMARK 465 TYR A 2425
REMARK 465 GLN A 2426
REMARK 465 LYS A 2427
REMARK 465 LEU A 2428
REMARK 465 ARG A 2429
REMARK 465 ALA A 2430
REMARK 465 ALA A 2431
REMARK 465 GLU A 2432
REMARK 465 ASN A 2433
REMARK 465 TYR A 2434
REMARK 465 TRP A 2435
REMARK 465 PRO A 2436
REMARK 465 GLN A 2437
REMARK 465 ALA A 2438
REMARK 465 THR A 2439
REMARK 465 TYR A 2440
REMARK 465 HIS A 2441
REMARK 465 GLY A 2442
REMARK 465 ASN A 2443
REMARK 465 VAL A 2444
REMARK 465 THR A 2445
REMARK 465 LEU A 2446
REMARK 465 LEU A 2447
REMARK 465 ARG A 2448
REMARK 465 ALA A 2449
REMARK 465 LYS A 2450
REMARK 465 THR A 2451
REMARK 465 GLY A 2452
REMARK 465 GLY A 2453
REMARK 465 ALA A 2454
REMARK 465 TYR A 2455
REMARK 465 GLY A 2456
REMARK 465 GLU A 2457
REMARK 465 ASP A 2458
REMARK 465 LEU A 2459
REMARK 465 GLY A 2460
REMARK 465 ALA A 2461
REMARK 465 ASP A 2462
REMARK 465 TYR A 2463
REMARK 465 ASN A 2464
REMARK 465 LEU A 2465
REMARK 465 SER A 2466
REMARK 465 GLN A 2467
REMARK 465 VAL A 2468
REMARK 465 CYS A 2469
REMARK 465 ASP A 2470
REMARK 465 GLY A 2471
REMARK 465 LYS A 2472
REMARK 465 VAL A 2473
REMARK 465 SER A 2474
REMARK 465 VAL A 2475
REMARK 465 HIS A 2476
REMARK 465 VAL A 2477
REMARK 465 ILE A 2478
REMARK 465 GLU A 2479
REMARK 465 GLY A 2480
REMARK 465 ASP A 2481
REMARK 465 HIS A 2482
REMARK 465 ARG A 2483
REMARK 465 THR A 2484
REMARK 465 LEU A 2485
REMARK 465 LEU A 2486
REMARK 465 GLU A 2487
REMARK 465 GLY A 2488
REMARK 465 SER A 2489
REMARK 465 GLY A 2490
REMARK 465 LEU A 2491
REMARK 465 GLU A 2492
REMARK 465 SER A 2493
REMARK 465 ILE A 2494
REMARK 465 LEU A 2495
REMARK 465 SER A 2496
REMARK 465 ILE A 2497
REMARK 465 ILE A 2498
REMARK 465 HIS A 2499
REMARK 465 SER A 2500
REMARK 465 CYS A 2501
REMARK 465 LEU A 2502
REMARK 465 ALA A 2503
REMARK 465 GLU A 2504
REMARK 465 PRO A 2505
REMARK 465 ARG A 2506
REMARK 465 VAL A 2507
REMARK 465 SER A 2508
REMARK 465 VAL A 2509
REMARK 465 ARG A 2510
REMARK 465 GLU A 2511
REMARK 465 GLY A 2512
REMARK 465 ALA B 1155
REMARK 465 GLN B 1156
REMARK 465 GLN B 1157
REMARK 465 GLY B 1158
REMARK 465 LEU B 1159
REMARK 465 LYS B 1160
REMARK 465 MET B 1161
REMARK 465 VAL B 1162
REMARK 465 VAL B 1163
REMARK 465 PRO B 1164
REMARK 465 GLY B 1165
REMARK 465 LEU B 1166
REMARK 465 ASP B 1167
REMARK 465 GLY B 1168
REMARK 465 ALA B 1169
REMARK 465 GLN B 1170
REMARK 465 ALA B 1171
REMARK 465 PRO B 1172
REMARK 465 ARG B 1173
REMARK 465 GLU B 1174
REMARK 465 ALA B 1175
REMARK 465 PRO B 1176
REMARK 465 GLN B 1177
REMARK 465 GLN B 1178
REMARK 465 SER B 1179
REMARK 465 LEU B 1196
REMARK 465 GLN B 1197
REMARK 465 LEU B 1198
REMARK 465 LYS B 2115
REMARK 465 ALA B 2116
REMARK 465 ALA B 2117
REMARK 465 ALA B 2118
REMARK 465 PRO B 2119
REMARK 465 ARG B 2120
REMARK 465 ASP B 2121
REMARK 465 GLY B 2122
REMARK 465 SER B 2123
REMARK 465 SER B 2124
REMARK 465 GLN B 2125
REMARK 465 LYS B 2126
REMARK 465 ASP B 2127
REMARK 465 LEU B 2128
REMARK 465 VAL B 2129
REMARK 465 LYS B 2130
REMARK 465 ALA B 2131
REMARK 465 VAL B 2132
REMARK 465 ALA B 2133
REMARK 465 HIS B 2134
REMARK 465 ILE B 2135
REMARK 465 LEU B 2136
REMARK 465 GLY B 2137
REMARK 465 ILE B 2138
REMARK 465 ARG B 2139
REMARK 465 ASP B 2140
REMARK 465 VAL B 2141
REMARK 465 ALA B 2142
REMARK 465 SER B 2143
REMARK 465 ILE B 2144
REMARK 465 ASN B 2145
REMARK 465 PRO B 2146
REMARK 465 ASP B 2147
REMARK 465 SER B 2148
REMARK 465 THR B 2149
REMARK 465 LEU B 2150
REMARK 465 VAL B 2151
REMARK 465 ASP B 2152
REMARK 465 LEU B 2153
REMARK 465 GLY B 2154
REMARK 465 LEU B 2155
REMARK 465 ASP B 2156
REMARK 465 SER B 2157
REMARK 465 LEU B 2158
REMARK 465 MET B 2159
REMARK 465 GLY B 2160
REMARK 465 VAL B 2161
REMARK 465 GLU B 2162
REMARK 465 VAL B 2163
REMARK 465 ARG B 2164
REMARK 465 GLN B 2165
REMARK 465 ILE B 2166
REMARK 465 LEU B 2167
REMARK 465 GLU B 2168
REMARK 465 ARG B 2169
REMARK 465 GLU B 2170
REMARK 465 HIS B 2171
REMARK 465 ASP B 2172
REMARK 465 LEU B 2173
REMARK 465 VAL B 2174
REMARK 465 LEU B 2175
REMARK 465 SER B 2176
REMARK 465 MET B 2177
REMARK 465 ARG B 2178
REMARK 465 GLU B 2179
REMARK 465 VAL B 2180
REMARK 465 ARG B 2181
REMARK 465 GLN B 2182
REMARK 465 LEU B 2183
REMARK 465 SER B 2184
REMARK 465 LEU B 2185
REMARK 465 ARG B 2186
REMARK 465 LYS B 2187
REMARK 465 LEU B 2188
REMARK 465 GLN B 2189
REMARK 465 GLU B 2190
REMARK 465 LEU B 2191
REMARK 465 SER B 2192
REMARK 465 SER B 2193
REMARK 465 LYS B 2194
REMARK 465 THR B 2195
REMARK 465 SER B 2196
REMARK 465 THR B 2197
REMARK 465 ASP B 2198
REMARK 465 ALA B 2199
REMARK 465 ASP B 2200
REMARK 465 PRO B 2201
REMARK 465 ALA B 2202
REMARK 465 THR B 2203
REMARK 465 PRO B 2204
REMARK 465 THR B 2205
REMARK 465 SER B 2206
REMARK 465 HIS B 2207
REMARK 465 GLU B 2208
REMARK 465 ASP B 2209
REMARK 465 SER B 2210
REMARK 465 PRO B 2211
REMARK 465 VAL B 2212
REMARK 465 ARG B 2213
REMARK 465 GLN B 2214
REMARK 465 GLN B 2215
REMARK 465 ALA B 2216
REMARK 465 THR B 2217
REMARK 465 LEU B 2218
REMARK 465 ASN B 2219
REMARK 465 LEU B 2220
REMARK 465 SER B 2221
REMARK 465 THR B 2222
REMARK 465 LEU B 2223
REMARK 465 LEU B 2224
REMARK 465 VAL B 2225
REMARK 465 ASN B 2226
REMARK 465 PRO B 2227
REMARK 465 GLU B 2228
REMARK 465 GLY B 2229
REMARK 465 PRO B 2230
REMARK 465 THR B 2231
REMARK 465 LEU B 2232
REMARK 465 THR B 2233
REMARK 465 ARG B 2234
REMARK 465 LEU B 2235
REMARK 465 ASN B 2236
REMARK 465 SER B 2237
REMARK 465 VAL B 2238
REMARK 465 GLN B 2239
REMARK 465 SER B 2240
REMARK 465 ALA B 2241
REMARK 465 GLU B 2242
REMARK 465 ARG B 2243
REMARK 465 PRO B 2244
REMARK 465 LEU B 2245
REMARK 465 PHE B 2246
REMARK 465 LEU B 2247
REMARK 465 VAL B 2248
REMARK 465 HIS B 2249
REMARK 465 PRO B 2250
REMARK 465 ILE B 2251
REMARK 465 GLU B 2252
REMARK 465 GLY B 2253
REMARK 465 SER B 2254
REMARK 465 ILE B 2255
REMARK 465 THR B 2256
REMARK 465 VAL B 2257
REMARK 465 PHE B 2258
REMARK 465 HIS B 2259
REMARK 465 GLY B 2260
REMARK 465 LEU B 2261
REMARK 465 ALA B 2262
REMARK 465 ALA B 2263
REMARK 465 LYS B 2264
REMARK 465 LEU B 2265
REMARK 465 SER B 2266
REMARK 465 ILE B 2267
REMARK 465 PRO B 2268
REMARK 465 THR B 2269
REMARK 465 TYR B 2270
REMARK 465 GLY B 2271
REMARK 465 LEU B 2272
REMARK 465 GLN B 2273
REMARK 465 CYS B 2274
REMARK 465 THR B 2275
REMARK 465 GLY B 2276
REMARK 465 ALA B 2277
REMARK 465 ALA B 2278
REMARK 465 PRO B 2279
REMARK 465 LEU B 2280
REMARK 465 ASP B 2281
REMARK 465 SER B 2282
REMARK 465 ILE B 2283
REMARK 465 GLN B 2284
REMARK 465 SER B 2285
REMARK 465 LEU B 2286
REMARK 465 ALA B 2287
REMARK 465 SER B 2288
REMARK 465 TYR B 2289
REMARK 465 TYR B 2290
REMARK 465 ILE B 2291
REMARK 465 GLU B 2292
REMARK 465 CYS B 2293
REMARK 465 ILE B 2294
REMARK 465 ARG B 2295
REMARK 465 GLN B 2296
REMARK 465 VAL B 2297
REMARK 465 GLN B 2298
REMARK 465 PRO B 2299
REMARK 465 GLU B 2300
REMARK 465 GLY B 2301
REMARK 465 PRO B 2302
REMARK 465 TYR B 2303
REMARK 465 ARG B 2304
REMARK 465 ILE B 2305
REMARK 465 ALA B 2306
REMARK 465 GLY B 2307
REMARK 465 TYR B 2308
REMARK 465 SER B 2309
REMARK 465 TYR B 2310
REMARK 465 GLY B 2311
REMARK 465 ALA B 2312
REMARK 465 CYS B 2313
REMARK 465 VAL B 2314
REMARK 465 ALA B 2315
REMARK 465 PHE B 2316
REMARK 465 GLU B 2317
REMARK 465 MET B 2318
REMARK 465 CYS B 2319
REMARK 465 SER B 2320
REMARK 465 GLN B 2321
REMARK 465 LEU B 2322
REMARK 465 GLN B 2323
REMARK 465 ALA B 2324
REMARK 465 GLN B 2325
REMARK 465 GLN B 2326
REMARK 465 SER B 2327
REMARK 465 ALA B 2328
REMARK 465 THR B 2329
REMARK 465 PRO B 2330
REMARK 465 GLY B 2331
REMARK 465 ASN B 2332
REMARK 465 HIS B 2333
REMARK 465 SER B 2334
REMARK 465 LEU B 2335
REMARK 465 PHE B 2336
REMARK 465 LEU B 2337
REMARK 465 PHE B 2338
REMARK 465 ASP B 2339
REMARK 465 GLY B 2340
REMARK 465 SER B 2341
REMARK 465 HIS B 2342
REMARK 465 THR B 2343
REMARK 465 PHE B 2344
REMARK 465 VAL B 2345
REMARK 465 LEU B 2346
REMARK 465 ALA B 2347
REMARK 465 TYR B 2348
REMARK 465 THR B 2349
REMARK 465 GLN B 2350
REMARK 465 SER B 2351
REMARK 465 VAL B 2352
REMARK 465 ARG B 2353
REMARK 465 ALA B 2354
REMARK 465 LYS B 2355
REMARK 465 MET B 2356
REMARK 465 THR B 2357
REMARK 465 PRO B 2358
REMARK 465 GLY B 2359
REMARK 465 CYS B 2360
REMARK 465 GLU B 2361
REMARK 465 ALA B 2362
REMARK 465 GLU B 2363
REMARK 465 ALA B 2364
REMARK 465 GLU B 2365
REMARK 465 ALA B 2366
REMARK 465 LYS B 2367
REMARK 465 ALA B 2368
REMARK 465 MET B 2369
REMARK 465 TYR B 2370
REMARK 465 PHE B 2371
REMARK 465 PHE B 2372
REMARK 465 VAL B 2373
REMARK 465 GLN B 2374
REMARK 465 GLN B 2375
REMARK 465 PHE B 2376
REMARK 465 THR B 2377
REMARK 465 ASP B 2378
REMARK 465 MET B 2379
REMARK 465 GLU B 2380
REMARK 465 GLN B 2381
REMARK 465 GLY B 2382
REMARK 465 LYS B 2383
REMARK 465 VAL B 2384
REMARK 465 LEU B 2385
REMARK 465 GLU B 2386
REMARK 465 ALA B 2387
REMARK 465 LEU B 2388
REMARK 465 ILE B 2389
REMARK 465 PRO B 2390
REMARK 465 LEU B 2391
REMARK 465 GLN B 2392
REMARK 465 GLY B 2393
REMARK 465 LEU B 2394
REMARK 465 GLU B 2395
REMARK 465 ALA B 2396
REMARK 465 ARG B 2397
REMARK 465 VAL B 2398
REMARK 465 ALA B 2399
REMARK 465 ALA B 2400
REMARK 465 THR B 2401
REMARK 465 VAL B 2402
REMARK 465 ASP B 2403
REMARK 465 LEU B 2404
REMARK 465 ILE B 2405
REMARK 465 THR B 2406
REMARK 465 GLN B 2407
REMARK 465 SER B 2408
REMARK 465 HIS B 2409
REMARK 465 ALA B 2410
REMARK 465 GLY B 2411
REMARK 465 LEU B 2412
REMARK 465 ASP B 2413
REMARK 465 ARG B 2414
REMARK 465 HIS B 2415
REMARK 465 ALA B 2416
REMARK 465 LEU B 2417
REMARK 465 SER B 2418
REMARK 465 PHE B 2419
REMARK 465 ALA B 2420
REMARK 465 ALA B 2421
REMARK 465 ARG B 2422
REMARK 465 SER B 2423
REMARK 465 PHE B 2424
REMARK 465 TYR B 2425
REMARK 465 GLN B 2426
REMARK 465 LYS B 2427
REMARK 465 LEU B 2428
REMARK 465 ARG B 2429
REMARK 465 ALA B 2430
REMARK 465 ALA B 2431
REMARK 465 GLU B 2432
REMARK 465 ASN B 2433
REMARK 465 TYR B 2434
REMARK 465 TRP B 2435
REMARK 465 PRO B 2436
REMARK 465 GLN B 2437
REMARK 465 ALA B 2438
REMARK 465 THR B 2439
REMARK 465 TYR B 2440
REMARK 465 HIS B 2441
REMARK 465 GLY B 2442
REMARK 465 ASN B 2443
REMARK 465 VAL B 2444
REMARK 465 THR B 2445
REMARK 465 LEU B 2446
REMARK 465 LEU B 2447
REMARK 465 ARG B 2448
REMARK 465 ALA B 2449
REMARK 465 LYS B 2450
REMARK 465 THR B 2451
REMARK 465 GLY B 2452
REMARK 465 GLY B 2453
REMARK 465 ALA B 2454
REMARK 465 TYR B 2455
REMARK 465 GLY B 2456
REMARK 465 GLU B 2457
REMARK 465 ASP B 2458
REMARK 465 LEU B 2459
REMARK 465 GLY B 2460
REMARK 465 ALA B 2461
REMARK 465 ASP B 2462
REMARK 465 TYR B 2463
REMARK 465 ASN B 2464
REMARK 465 LEU B 2465
REMARK 465 SER B 2466
REMARK 465 GLN B 2467
REMARK 465 VAL B 2468
REMARK 465 CYS B 2469
REMARK 465 ASP B 2470
REMARK 465 GLY B 2471
REMARK 465 LYS B 2472
REMARK 465 VAL B 2473
REMARK 465 SER B 2474
REMARK 465 VAL B 2475
REMARK 465 HIS B 2476
REMARK 465 VAL B 2477
REMARK 465 ILE B 2478
REMARK 465 GLU B 2479
REMARK 465 GLY B 2480
REMARK 465 ASP B 2481
REMARK 465 HIS B 2482
REMARK 465 ARG B 2483
REMARK 465 THR B 2484
REMARK 465 LEU B 2485
REMARK 465 LEU B 2486
REMARK 465 GLU B 2487
REMARK 465 GLY B 2488
REMARK 465 SER B 2489
REMARK 465 GLY B 2490
REMARK 465 LEU B 2491
REMARK 465 GLU B 2492
REMARK 465 SER B 2493
REMARK 465 ILE B 2494
REMARK 465 LEU B 2495
REMARK 465 SER B 2496
REMARK 465 ILE B 2497
REMARK 465 ILE B 2498
REMARK 465 HIS B 2499
REMARK 465 SER B 2500
REMARK 465 CYS B 2501
REMARK 465 LEU B 2502
REMARK 465 ALA B 2503
REMARK 465 GLU B 2504
REMARK 465 PRO B 2505
REMARK 465 ARG B 2506
REMARK 465 VAL B 2507
REMARK 465 SER B 2508
REMARK 465 VAL B 2509
REMARK 465 ARG B 2510
REMARK 465 GLU B 2511
REMARK 465 GLY B 2512
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O PRO A 1649 - OG1 THR A 1653 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 868 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 PRO A 887 C - N - CA ANGL. DEV. = 12.2 DEGREES
REMARK 500 PRO A1224 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 PRO A1327 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO B 868 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO B 887 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO B1224 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500 PRO B1301 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO B1327 C - N - CA ANGL. DEV. = 9.9 DEGREES
REMARK 500 PRO B1413 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 14 121.03 -36.08
REMARK 500 ASP A 31 105.32 -53.43
REMARK 500 ASP A 37 33.45 -79.69
REMARK 500 TRP A 40 -143.64 -132.26
REMARK 500 LEU A 47 152.37 -46.29
REMARK 500 PHE A 60 144.60 173.80
REMARK 500 SER A 114 54.70 -110.41
REMARK 500 LEU A 120 41.66 -96.06
REMARK 500 SER A 121 30.72 -149.84
REMARK 500 CYS A 135 -36.77 -147.59
REMARK 500 ASP A 149 34.77 73.47
REMARK 500 PRO A 153 134.01 -33.25
REMARK 500 ALA A 160 -147.06 75.30
REMARK 500 SER A 162 -74.36 -83.76
REMARK 500 SER A 163 -94.22 38.52
REMARK 500 ASN A 189 111.75 -167.75
REMARK 500 LEU A 192 -51.42 -125.34
REMARK 500 LYS A 202 3.88 -68.92
REMARK 500 CYS A 212 48.83 -107.89
REMARK 500 ARG A 213 102.61 -43.93
REMARK 500 PHE A 215 -54.14 73.94
REMARK 500 ASP A 216 152.57 -38.19
REMARK 500 ALA A 227 137.68 176.24
REMARK 500 SER A 237 40.07 -64.84
REMARK 500 LEU A 238 -2.55 -169.83
REMARK 500 ASN A 252 -166.59 -129.37
REMARK 500 TYR A 277 -140.67 -113.12
REMARK 500 ALA A 278 -98.46 5.38
REMARK 500 PRO A 282 -178.35 -58.22
REMARK 500 ALA A 292 -178.96 -69.95
REMARK 500 ASN A 310 7.08 -68.47
REMARK 500 ALA A 314 77.67 -119.33
REMARK 500 THR A 315 136.70 -170.11
REMARK 500 ARG A 316 -167.44 -79.56
REMARK 500 ARG A 317 159.12 48.53
REMARK 500 GLU A 318 91.12 -61.71
REMARK 500 PRO A 319 -72.96 -47.26
REMARK 500 SER A 324 106.26 -164.77
REMARK 500 THR A 325 -37.12 -39.88
REMARK 500 PRO A 332 16.75 -68.71
REMARK 500 GLU A 333 -114.72 43.20
REMARK 500 HIS A 360 -74.43 -99.40
REMARK 500 PRO A 367 -148.05 -72.70
REMARK 500 ALA A 368 -29.97 70.54
REMARK 500 GLN A 370 -3.58 -154.80
REMARK 500 ARG A 373 -80.44 -63.43
REMARK 500 PRO A 380 87.58 -63.03
REMARK 500 ASN A 387 94.42 -161.85
REMARK 500 ARG A 409 125.95 175.88
REMARK 500 PRO A 412 -179.43 -63.74
REMARK 500 PRO A 414 -165.24 -69.64
REMARK 500 HIS A 417 1.29 -66.50
REMARK 500 SER A 461 131.85 -34.88
REMARK 500 GLU A 476 30.78 -66.05
REMARK 500 SER A 488 -176.11 50.47
REMARK 500 TRP A 503 141.25 173.26
REMARK 500 THR A 541 134.87 -23.25
REMARK 500 SER A 581 -129.35 78.55
REMARK 500 ASN A 614 23.82 36.06
REMARK 500 VAL A 615 153.04 -35.04
REMARK 500 ALA A 619 133.61 177.96
REMARK 500 PRO A 635 153.03 -43.33
REMARK 500 ASN A 644 -70.93 -88.04
REMARK 500 ASP A 647 24.61 -142.12
REMARK 500 ARG A 667 21.91 -70.65
REMARK 500 GLU A 668 19.96 -145.67
REMARK 500 ALA A 691 -51.16 -29.28
REMARK 500 ILE A 702 75.23 -106.39
REMARK 500 GLN A 721 40.15 -94.38
REMARK 500 PRO A 753 -174.79 -57.04
REMARK 500 ASP A 791 85.19 -159.97
REMARK 500 PRO A 828 135.75 -36.80
REMARK 500 PRO A 845 129.86 -30.46
REMARK 500 SER A 854 -157.42 163.52
REMARK 500 CYS A 856 85.48 -151.78
REMARK 500 SER A 857 -3.54 -57.69
REMARK 500 PRO A 868 -16.08 -44.19
REMARK 500 VAL A 884 78.07 -102.93
REMARK 500 SER A 904 -9.58 71.43
REMARK 500 THR A 910 72.96 -118.05
REMARK 500 PRO A 965 99.64 -68.38
REMARK 500 PHE A 970 58.19 -112.70
REMARK 500 VAL A 976 -169.89 177.49
REMARK 500 ALA A 979 47.67 -85.48
REMARK 500 THR A 982 -22.84 86.46
REMARK 500 ALA A 983 -118.56 -107.70
REMARK 500 GLU A 984 -101.20 76.39
REMARK 500 PHE A 985 94.62 109.33
REMARK 500 ASP A1002 48.31 -89.20
REMARK 500 ASP A1014 152.37 -38.32
REMARK 500 THR A1052 -42.14 -146.33
REMARK 500 SER A1056 97.55 -178.67
REMARK 500 THR A1074 -5.09 87.42
REMARK 500 ARG A1084 -19.38 -49.84
REMARK 500 GLU A1110 28.40 -77.49
REMARK 500 PHE A1119 64.21 -113.54
REMARK 500 VAL A1125 74.68 -104.21
REMARK 500 LEU A1130 -143.46 67.13
REMARK 500 GLN A1141 -19.13 -140.80
REMARK 500 ALA A1149 54.39 -96.29
REMARK 500 LEU A1150 -14.54 -179.30
REMARK 500 LEU A1210 26.90 -141.01
REMARK 500 ASP A1213 38.29 -82.76
REMARK 500 PRO A1215 57.73 -59.19
REMARK 500 LEU A1221 68.05 -103.84
REMARK 500 PRO A1224 -48.75 -0.85
REMARK 500 PRO A1240 38.80 -61.94
REMARK 500 VAL A1267 75.80 -112.26
REMARK 500 HIS A1293 81.39 62.36
REMARK 500 PRO A1301 63.28 -51.34
REMARK 500 ASN A1303 -48.81 103.49
REMARK 500 PRO A1304 99.79 -61.30
REMARK 500 SER A1308 22.35 -69.85
REMARK 500 LYS A1311 126.72 72.68
REMARK 500 ALA A1312 -152.55 -111.63
REMARK 500 ASP A1313 -37.88 -136.73
REMARK 500 CYS A1317 115.01 -165.71
REMARK 500 ALA A1322 69.57 -69.65
REMARK 500 THR A1323 129.65 -31.56
REMARK 500 LEU A1362 -90.29 -68.50
REMARK 500 ARG A1370 27.22 -76.12
REMARK 500 LEU A1373 179.00 -59.86
REMARK 500 SER A1386 27.99 82.02
REMARK 500 LEU A1389 106.57 -53.47
REMARK 500 PRO A1409 145.42 -30.95
REMARK 500 ASP A1411 -120.36 -97.20
REMARK 500 PHE A1423 35.59 87.00
REMARK 500 TRP A1425 -17.85 -42.00
REMARK 500 ALA A1436 -101.36 -42.57
REMARK 500 SER A1438 84.15 -40.26
REMARK 500 THR A1450 47.79 -142.61
REMARK 500 ARG A1461 -10.01 -49.05
REMARK 500 LYS A1462 14.94 -143.03
REMARK 500 HIS A1467 -78.26 -32.09
REMARK 500 GLU A1485 62.56 161.50
REMARK 500 SER A1489 -24.10 77.84
REMARK 500 SER A1490 -133.43 -100.98
REMARK 500 ASP A1500 -18.94 69.03
REMARK 500 LEU A1501 137.49 -34.47
REMARK 500 GLN A1521 -59.57 66.54
REMARK 500 SER A1537 98.98 -161.75
REMARK 500 ALA A1554 136.33 -174.39
REMARK 500 ALA A1557 -53.76 -16.91
REMARK 500 SER A1558 -75.94 -35.11
REMARK 500 ASP A1561 12.74 -69.90
REMARK 500 MET A1577 -19.59 -47.34
REMARK 500 ALA A1579 -3.77 -58.00
REMARK 500 PRO A1585 2.63 -64.21
REMARK 500 SER A1587 26.44 -69.57
REMARK 500 ASP A1596 -82.58 -56.18
REMARK 500 MET A1598 22.99 -158.17
REMARK 500 ARG A1611 -177.48 -50.36
REMARK 500 ALA A1619 174.47 171.38
REMARK 500 LEU A1622 85.79 -61.04
REMARK 500 LEU A1628 110.98 -39.30
REMARK 500 ALA A1632 48.72 -147.32
REMARK 500 PRO A1649 -75.55 -28.14
REMARK 500 ARG A1664 57.64 34.94
REMARK 500 GLN A1714 8.38 -69.07
REMARK 500 SER A1723 -14.89 -141.89
REMARK 500 ARG A1734 -77.42 -64.13
REMARK 500 HIS A1735 29.35 -67.73
REMARK 500 LEU A1745 73.36 -110.58
REMARK 500 GLU A1750 -106.73 2.06
REMARK 500 LEU A1799 -120.79 -97.70
REMARK 500 PHE A1800 -112.04 58.99
REMARK 500 LYS A1835 31.88 -81.13
REMARK 500 LYS A1847 30.08 -92.40
REMARK 500 ALA A1864 105.67 -45.03
REMARK 500 ILE A1871 109.63 -59.63
REMARK 500 MET A1973 129.36 -174.89
REMARK 500 ARG A1976 65.43 -151.28
REMARK 500 ALA A1978 130.34 176.22
REMARK 500 PRO A1985 2.11 -63.67
REMARK 500 ALA A2009 63.45 -170.92
REMARK 500 CYS A2010 55.75 -142.31
REMARK 500 PRO A2011 1.35 -64.71
REMARK 500 ASP A2065 -30.12 25.30
REMARK 500 THR A2072 -85.85 -97.77
REMARK 500 SER A2100 53.57 -94.02
REMARK 500 HIS A2103 160.40 -47.43
REMARK 500 SER A2108 114.56 -166.97
REMARK 500 ALA A2112 -95.02 -78.33
REMARK 500 PRO B 14 120.52 -35.25
REMARK 500 ASP B 31 105.13 -53.46
REMARK 500 ASP B 37 33.84 -79.70
REMARK 500 TRP B 40 -142.35 -132.80
REMARK 500 LEU B 47 151.82 -46.93
REMARK 500 PHE B 60 145.04 172.07
REMARK 500 SER B 114 55.97 -110.91
REMARK 500 LEU B 120 37.81 -96.53
REMARK 500 SER B 121 -3.22 -141.57
REMARK 500 ARG B 122 -70.68 -63.92
REMARK 500 CYS B 135 -38.83 -148.11
REMARK 500 ASP B 149 34.58 75.56
REMARK 500 PRO B 153 133.70 -34.06
REMARK 500 ALA B 160 -149.24 72.72
REMARK 500 SER B 162 -74.31 -84.39
REMARK 500 SER B 163 -94.57 35.62
REMARK 500 ASN B 189 112.46 -168.68
REMARK 500 LEU B 192 -51.28 -126.60
REMARK 500 SER B 196 -64.46 -29.65
REMARK 500 LYS B 202 3.12 -65.19
REMARK 500 ARG B 213 81.62 -69.40
REMARK 500 PHE B 215 18.67 -146.20
REMARK 500 ALA B 227 137.56 175.81
REMARK 500 SER B 237 41.56 -69.66
REMARK 500 LEU B 238 -4.41 -169.95
REMARK 500 ASN B 252 -164.66 -128.76
REMARK 500 TYR B 277 -139.20 -113.48
REMARK 500 ALA B 278 -97.72 3.43
REMARK 500 PRO B 282 -178.30 -58.16
REMARK 500 PRO B 284 -9.96 -56.81
REMARK 500 ASN B 310 5.54 -67.39
REMARK 500 ALA B 314 77.69 -118.93
REMARK 500 ARG B 317 159.66 49.83
REMARK 500 GLU B 318 91.29 -61.91
REMARK 500 PRO B 319 -72.87 -47.90
REMARK 500 SER B 324 139.47 -173.64
REMARK 500 PRO B 332 14.78 -68.47
REMARK 500 GLU B 333 -114.72 45.90
REMARK 500 VAL B 352 117.02 -164.28
REMARK 500 HIS B 360 -74.92 -98.47
REMARK 500 PRO B 367 -148.23 -74.44
REMARK 500 ALA B 368 -24.79 70.04
REMARK 500 GLN B 370 -4.77 176.55
REMARK 500 ARG B 373 -79.64 -63.83
REMARK 500 PRO B 380 88.60 -62.53
REMARK 500 ASN B 387 95.05 -162.86
REMARK 500 SER B 392 115.70 -160.23
REMARK 500 ARG B 409 125.41 175.47
REMARK 500 PRO B 414 -164.84 -70.07
REMARK 500 HIS B 417 1.38 -66.90
REMARK 500 SER B 461 132.16 -33.86
REMARK 500 GLU B 476 31.09 -66.54
REMARK 500 SER B 488 -176.71 49.66
REMARK 500 TRP B 503 131.78 173.38
REMARK 500 SER B 581 -104.34 46.60
REMARK 500 ASN B 614 93.01 51.49
REMARK 500 LEU B 616 151.45 -42.67
REMARK 500 ASN B 644 -71.66 -72.75
REMARK 500 PRO B 654 -157.97 -70.96
REMARK 500 ASP B 669 9.53 155.60
REMARK 500 ALA B 681 76.78 -107.25
REMARK 500 ASP B 704 72.64 55.86
REMARK 500 GLN B 721 41.25 -94.65
REMARK 500 PRO B 753 -175.14 -55.92
REMARK 500 ASP B 791 87.54 -160.00
REMARK 500 GLU B 820 86.72 -36.06
REMARK 500 PRO B 828 135.99 -36.67
REMARK 500 PRO B 845 97.96 -43.23
REMARK 500 PRO B 868 -15.82 -45.39
REMARK 500 ASP B 872 30.25 -94.62
REMARK 500 HIS B 878 58.96 -93.52
REMARK 500 VAL B 884 77.46 -103.46
REMARK 500 SER B 904 -9.99 71.51
REMARK 500 THR B 910 73.34 -116.86
REMARK 500 PHE B 970 60.43 -106.61
REMARK 500 ARG B 973 -104.40 -66.44
REMARK 500 ALA B 974 125.55 80.13
REMARK 500 ASP B 977 113.93 -14.00
REMARK 500 PRO B 978 -160.70 -61.64
REMARK 500 ASP B 980 -106.09 -30.56
REMARK 500 THR B 982 -61.45 -106.09
REMARK 500 ALA B 983 32.02 -60.11
REMARK 500 GLU B 984 71.15 -57.57
REMARK 500 ASP B1002 51.32 -91.13
REMARK 500 ASP B1014 152.93 -40.31
REMARK 500 THR B1052 -45.88 -144.92
REMARK 500 SER B1056 97.71 -176.29
REMARK 500 LEU B1071 172.82 -59.05
REMARK 500 THR B1074 -6.62 87.14
REMARK 500 ASP B1083 75.35 -118.84
REMARK 500 GLU B1110 28.28 -76.78
REMARK 500 LEU B1112 34.11 -144.53
REMARK 500 PHE B1119 67.97 -111.02
REMARK 500 VAL B1125 76.23 -103.10
REMARK 500 LEU B1130 -139.13 67.53
REMARK 500 LYS B1153 -66.95 -90.12
REMARK 500 PRO B1181 -71.77 -38.22
REMARK 500 ARG B1182 -164.52 -63.37
REMARK 500 ALA B1205 -16.20 -49.18
REMARK 500 LEU B1210 11.38 -158.63
REMARK 500 LEU B1221 65.12 -103.94
REMARK 500 PRO B1224 -58.29 -0.64
REMARK 500 ALA B1225 -57.20 -26.41
REMARK 500 PRO B1240 37.33 -61.59
REMARK 500 LEU B1282 34.07 -94.45
REMARK 500 HIS B1293 81.82 43.09
REMARK 500 PRO B1301 58.72 -51.68
REMARK 500 ALA B1302 -132.99 -83.27
REMARK 500 PRO B1304 98.05 -53.42
REMARK 500 ALA B1312 157.32 166.14
REMARK 500 LEU B1321 -14.42 -169.59
REMARK 500 ALA B1322 26.75 49.05
REMARK 500 PRO B1354 -83.46 -30.35
REMARK 500 MET B1358 -72.92 -39.27
REMARK 500 LEU B1362 -24.19 -141.87
REMARK 500 HIS B1371 115.52 168.34
REMARK 500 LEU B1372 99.63 -161.04
REMARK 500 LEU B1389 104.74 -57.26
REMARK 500 GLN B1406 73.39 -112.38
REMARK 500 PHE B1423 42.12 81.79
REMARK 500 TRP B1425 -11.95 -46.87
REMARK 500 ILE B1432 23.73 -71.74
REMARK 500 SER B1437 27.35 -65.70
REMARK 500 MET B1444 108.14 -163.11
REMARK 500 THR B1450 44.98 -141.56
REMARK 500 ARG B1461 -9.26 -43.14
REMARK 500 LYS B1462 18.07 -141.21
REMARK 500 HIS B1467 -77.24 -37.60
REMARK 500 PRO B1482 43.51 -75.90
REMARK 500 PRO B1488 37.60 -76.09
REMARK 500 SER B1489 -35.67 -132.79
REMARK 500 SER B1491 -108.14 50.25
REMARK 500 ASP B1500 -16.57 77.84
REMARK 500 LEU B1501 133.84 -38.37
REMARK 500 GLU B1520 38.85 -82.51
REMARK 500 GLN B1521 -29.48 8.39
REMARK 500 LEU B1541 4.91 -64.89
REMARK 500 CYS B1548 108.91 -52.01
REMARK 500 ALA B1554 112.97 -166.20
REMARK 500 LEU B1555 78.76 -104.60
REMARK 500 ALA B1557 -7.51 -49.35
REMARK 500 MET B1577 -18.49 -49.09
REMARK 500 ALA B1579 -3.31 -56.57
REMARK 500 PRO B1585 2.56 -66.08
REMARK 500 SER B1587 26.07 -69.65
REMARK 500 ASP B1596 -104.43 -54.08
REMARK 500 CYS B1597 109.93 -43.02
REMARK 500 MET B1598 53.41 -157.72
REMARK 500 THR B1633 107.57 -163.58
REMARK 500 PRO B1637 150.77 -41.82
REMARK 500 ALA B1646 -19.13 -47.46
REMARK 500 PRO B1649 -75.00 -58.98
REMARK 500 GLU B1669 157.16 -48.16
REMARK 500 GLN B1714 7.01 -68.04
REMARK 500 SER B1723 -14.45 -142.22
REMARK 500 ARG B1734 -77.77 -63.02
REMARK 500 HIS B1735 29.15 -66.75
REMARK 500 LEU B1745 75.46 -112.70
REMARK 500 GLU B1750 -105.82 0.43
REMARK 500 LYS B1771 -12.57 -141.25
REMARK 500 LEU B1799 -65.01 -94.67
REMARK 500 PHE B1800 -59.33 -2.71
REMARK 500 LYS B1835 31.35 -80.28
REMARK 500 GLU B1858 158.53 -46.78
REMARK 500 PRO B1863 99.88 -42.20
REMARK 500 ALA B1864 83.03 -54.93
REMARK 500 MET B1973 129.77 -176.11
REMARK 500 ARG B1976 78.28 -104.32
REMARK 500 ALA B1978 149.21 -174.55
REMARK 500 VAL B1979 168.91 -47.81
REMARK 500 ALA B2009 64.70 -169.82
REMARK 500 CYS B2010 55.98 -142.04
REMARK 500 PRO B2011 0.63 -64.31
REMARK 500 SER B2020 -163.47 -101.43
REMARK 500 ASP B2065 -31.76 28.23
REMARK 500 THR B2072 -81.45 -104.75
REMARK 500 ASN B2076 7.95 -68.38
REMARK 500 SER B2100 54.52 -93.40
REMARK 500 HIS B2103 160.50 -46.75
REMARK 500 SER B2108 113.02 -168.41
REMARK 500 GLU B2113 74.77 -110.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A2065 24.8 L L OUTSIDE RANGE
REMARK 500 GLN B1521 22.7 L L OUTSIDE RANGE
REMARK 500 ASP B2065 24.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B3002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2VZ8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MAMMALIAN FATTY ACID
REMARK 900 SYNTHASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SEQUENCE CONTAINS A SINGLE X BASED ON TRANSLATION FROM
REMARK 999 NUCLEIC ACID SEQUENCE CONTAINING A K. THIS POSITION WAS
REMARK 999 ASSIGNED BASED ON FURTHER EST SEQUENCES.
DBREF 2VZ9 A 1 2512 UNP A5YV76 A5YV76_PIG 1 2512
DBREF 2VZ9 B 1 2512 UNP A5YV76 A5YV76_PIG 1 2512
SEQADV 2VZ9 ILE A 834 UNP A5YV76 UNK 834 CONFLICT SEE REMARK 999
SEQADV 2VZ9 ILE B 834 UNP A5YV76 UNK 834 CONFLICT SEE REMARK 999
SEQRES 1 A 2512 MET GLU GLU VAL VAL ILE ALA GLY MET SER GLY LYS LEU
SEQRES 2 A 2512 PRO GLU SER GLU ASN LEU GLU GLU PHE TRP ALA ASN LEU
SEQRES 3 A 2512 ILE GLY GLY VAL ASP MET VAL THR ALA ASP ASP ARG ARG
SEQRES 4 A 2512 TRP LYS ALA GLY LEU TYR GLY LEU PRO ARG ARG MET GLY
SEQRES 5 A 2512 LYS LEU LYS ASP LEU SER ARG PHE ASP ALA SER PHE PHE
SEQRES 6 A 2512 GLY VAL HIS SER LYS GLN ALA ASN THR MET ASP PRO GLN
SEQRES 7 A 2512 LEU ARG MET LEU LEU GLU VAL THR TYR GLU ALA ILE VAL
SEQRES 8 A 2512 ASP GLY GLY ILE ASN PRO ALA SER LEU ARG GLY THR SER
SEQRES 9 A 2512 THR GLY VAL TRP VAL GLY VAL SER SER SER ASP ALA SER
SEQRES 10 A 2512 GLU ALA LEU SER ARG ASP PRO GLU THR LEU VAL GLY TYR
SEQRES 11 A 2512 SER MET ILE GLY CYS GLN ARG ALA MET MET ALA ASN ARG
SEQRES 12 A 2512 LEU SER PHE PHE PHE ASP PHE LYS GLY PRO SER ILE THR
SEQRES 13 A 2512 ILE ASP THR ALA CYS SER SER SER LEU LEU ALA LEU GLN
SEQRES 14 A 2512 SER ALA TYR GLN ALA ILE ARG GLY GLY GLU CYS SER ALA
SEQRES 15 A 2512 ALA VAL VAL GLY GLY LEU ASN VAL LEU LEU LYS PRO ASN
SEQRES 16 A 2512 SER SER LEU GLN PHE MET LYS LEU GLY MET LEU SER GLN
SEQRES 17 A 2512 ASP GLY THR CYS ARG SER PHE ASP ALA GLU GLY THR GLY
SEQRES 18 A 2512 TYR CYS ARG ALA GLU ALA VAL VAL ALA VAL LEU LEU THR
SEQRES 19 A 2512 LYS LYS SER LEU ALA ARG ARG VAL TYR ALA THR ILE LEU
SEQRES 20 A 2512 ASN ALA GLY THR ASN THR ASP GLY SER LYS GLU GLN GLY
SEQRES 21 A 2512 VAL THR PHE PRO SER GLY ASP VAL GLN GLU GLN LEU ILE
SEQRES 22 A 2512 ARG SER LEU TYR ALA PRO ALA GLY PRO ASP PRO GLU SER
SEQRES 23 A 2512 LEU GLU TYR ILE GLU ALA HIS GLY THR GLY THR LYS VAL
SEQRES 24 A 2512 GLY ASP PRO GLN GLU LEU ASN GLY ILE VAL ASN ALA LEU
SEQRES 25 A 2512 CYS ALA THR ARG ARG GLU PRO LEU LEU ILE GLY SER THR
SEQRES 26 A 2512 LYS SER ASN MET GLY HIS PRO GLU PRO ALA SER GLY VAL
SEQRES 27 A 2512 ALA ALA LEU ILE LYS VAL LEU LEU SER LEU GLU HIS GLY
SEQRES 28 A 2512 VAL TRP ALA PRO ASN LEU HIS TYR HIS THR PRO ASN PRO
SEQRES 29 A 2512 GLU ILE PRO ALA LEU GLN ASP GLY ARG LEU GLN VAL VAL
SEQRES 30 A 2512 ASP ARG PRO LEU PRO ILE ARG GLY GLY ASN VAL GLY ILE
SEQRES 31 A 2512 ASN SER PHE GLY PHE GLY GLY SER ASN VAL HIS VAL ILE
SEQRES 32 A 2512 LEU GLN PRO ASN SER ARG PRO ALA PRO PRO PRO ALA GLN
SEQRES 33 A 2512 HIS ALA ALA LEU PRO ARG LEU LEU GLN ALA SER GLY ARG
SEQRES 34 A 2512 THR LEU GLU ALA VAL GLN THR LEU LEU GLU GLN GLY LEU
SEQRES 35 A 2512 ARG HIS SER ARG ASP LEU ALA PHE VAL GLY MET LEU ASN
SEQRES 36 A 2512 GLU ILE ALA ALA VAL SER PRO VAL ALA MET PRO PHE ARG
SEQRES 37 A 2512 GLY TYR ALA VAL LEU GLY GLY GLU ALA GLY SER GLN GLU
SEQRES 38 A 2512 VAL GLN GLN VAL PRO GLY SER LYS ARG PRO VAL TRP PHE
SEQRES 39 A 2512 ILE CYS SER GLY MET GLY ALA GLN TRP GLN GLY MET GLY
SEQRES 40 A 2512 LEU SER LEU MET ARG LEU ASP ARG PHE ARG ASP SER ILE
SEQRES 41 A 2512 LEU ARG SER ASP GLN ALA LEU LYS PRO LEU GLY LEU ARG
SEQRES 42 A 2512 VAL SER ASP LEU LEU LEU SER THR ASP GLU ALA VAL LEU
SEQRES 43 A 2512 ASP ASP ILE VAL SER SER PHE VAL SER LEU THR SER ILE
SEQRES 44 A 2512 GLN ILE ALA LEU ILE ASP LEU LEU THR SER LEU GLY LEU
SEQRES 45 A 2512 GLN PRO ASP GLY ILE ILE GLY HIS SER LEU GLY GLU VAL
SEQRES 46 A 2512 ALA CYS GLY TYR ALA ASP GLY CYS LEU THR GLN GLU GLU
SEQRES 47 A 2512 ALA VAL LEU SER SER TYR TRP ARG GLY TYR CYS ILE LYS
SEQRES 48 A 2512 GLU ALA ASN VAL LEU PRO GLY ALA MET ALA ALA VAL GLY
SEQRES 49 A 2512 LEU SER TRP GLU GLU CYS LYS GLN ARG CYS PRO PRO GLY
SEQRES 50 A 2512 ILE VAL PRO ALA CYS HIS ASN SER LYS ASP THR VAL THR
SEQRES 51 A 2512 ILE SER GLY PRO GLN ALA ALA MET SER GLU PHE LEU GLN
SEQRES 52 A 2512 GLN LEU LYS ARG GLU ASP VAL PHE VAL LYS GLU VAL ARG
SEQRES 53 A 2512 THR GLY GLY ILE ALA PHE HIS SER TYR PHE MET GLU SER
SEQRES 54 A 2512 ILE ALA PRO THR LEU LEU ARG GLN LEU ARG LYS VAL ILE
SEQRES 55 A 2512 LEU ASP PRO LYS PRO ARG SER LYS ARG TRP LEU SER THR
SEQRES 56 A 2512 SER ILE PRO GLU ALA GLN TRP GLN GLY SER LEU ALA ARG
SEQRES 57 A 2512 THR PHE SER ALA GLU TYR SER VAL ASN ASN LEU VAL SER
SEQRES 58 A 2512 PRO VAL LEU PHE GLN GLU ALA LEU GLN HIS VAL PRO ALA
SEQRES 59 A 2512 HIS ALA VAL VAL VAL GLU ILE ALA PRO HIS ALA LEU LEU
SEQRES 60 A 2512 GLN ALA VAL LEU LYS ARG SER LEU GLU SER SER CYS THR
SEQRES 61 A 2512 ILE ILE PRO LEU MET LYS LYS ASP HIS ARG ASP ASN LEU
SEQRES 62 A 2512 GLU PHE PHE LEU SER ASN VAL GLY ARG LEU HIS LEU ALA
SEQRES 63 A 2512 GLY VAL SER VAL ASN PRO ASN GLY LEU PHE PRO PRO VAL
SEQRES 64 A 2512 GLU PHE PRO ALA PRO ARG GLY THR PRO LEU ILE SER PRO
SEQRES 65 A 2512 HIS ILE LYS TRP ASP HIS SER GLN ALA TRP ASP VAL PRO
SEQRES 66 A 2512 SER ALA ALA ASP PHE PRO SER GLY SER SER CYS SER SER
SEQRES 67 A 2512 VAL ALA VAL TYR LYS PHE ASP VAL SER PRO GLU SER PRO
SEQRES 68 A 2512 ASP HIS TYR LEU VAL ASP HIS CYS ILE ASP GLY ARG VAL
SEQRES 69 A 2512 LEU PHE PRO GLY THR GLY TYR LEU TRP LEU THR TRP LYS
SEQRES 70 A 2512 THR LEU ALA ARG ALA LEU SER GLN ASN LEU GLU GLU THR
SEQRES 71 A 2512 PRO VAL VAL PHE GLU ASP VAL THR LEU HIS GLN ALA THR
SEQRES 72 A 2512 ILE LEU PRO LYS THR GLY THR VAL SER LEU GLU VAL ARG
SEQRES 73 A 2512 LEU LEU GLU ALA SER HIS ALA PHE GLU VAL SER ASP SER
SEQRES 74 A 2512 ASN GLY SER LEU ILE ALA SER GLY LYS VAL TYR GLN TRP
SEQRES 75 A 2512 GLU SER PRO ASP PRO LYS LEU PHE ASP THR ARG ALA ALA
SEQRES 76 A 2512 VAL ASP PRO ALA ASP SER THR ALA GLU PHE ARG LEU SER
SEQRES 77 A 2512 GLN GLY ASP VAL TYR LYS ASP LEU ARG LEU ARG GLY TYR
SEQRES 78 A 2512 ASP TYR GLY PRO PHE PHE GLN LEU VAL LEU GLU SER ASP
SEQRES 79 A 2512 LEU GLU GLY ASN ARG GLY ARG LEU GLN TRP ASN ASP SER
SEQRES 80 A 2512 TRP VAL SER PHE LEU ASP ALA MET LEU HIS MET SER ILE
SEQRES 81 A 2512 LEU ALA PRO GLY GLN LEU GLY LEU TYR LEU PRO THR ARG
SEQRES 82 A 2512 PHE THR SER ILE ARG ILE ASP PRO VAL THR HIS ARG GLN
SEQRES 83 A 2512 LYS LEU TYR THR LEU GLN ASP THR THR GLN ALA ALA ASP
SEQRES 84 A 2512 VAL VAL VAL ASP ARG ASN LEU ASN THR VAL VAL ALA GLY
SEQRES 85 A 2512 GLY ALA LEU PHE LEU GLY ALA HIS SER SER VAL ALA PRO
SEQRES 86 A 2512 ARG ARG PRO GLN GLU HIS LEU LYS PRO ILE LEU GLU LYS
SEQRES 87 A 2512 PHE CYS PHE THR PRO HIS VAL GLU SER GLY CYS LEU ALA
SEQRES 88 A 2512 GLY ASN THR ALA LEU GLN GLU GLU LEU GLN LEU CYS ARG
SEQRES 89 A 2512 GLY LEU ALA GLN ALA LEU GLN THR LYS VAL ALA GLN GLN
SEQRES 90 A 2512 GLY LEU LYS MET VAL VAL PRO GLY LEU ASP GLY ALA GLN
SEQRES 91 A 2512 ALA PRO ARG GLU ALA PRO GLN GLN SER LEU PRO ARG LEU
SEQRES 92 A 2512 LEU ALA ALA ALA CYS GLN LEU GLN LEU ASN GLY ASN LEU
SEQRES 93 A 2512 GLN LEU GLU LEU GLY GLN VAL LEU ALA GLN GLU ARG PRO
SEQRES 94 A 2512 LEU LEU CYS ASP ASP PRO LEU LEU SER GLY LEU LEU ASP
SEQRES 95 A 2512 ALA PRO ALA LEU LYS ALA CYS VAL ASP THR ALA LEU GLU
SEQRES 96 A 2512 ASN MET ALA SER PRO LYS MET LYS VAL VAL GLU VAL LEU
SEQRES 97 A 2512 ALA GLY ASP GLY GLN LEU TYR SER ARG ILE PRO ALA LEU
SEQRES 98 A 2512 LEU ASN THR GLN PRO VAL MET ASP LEU ASP TYR THR ALA
SEQRES 99 A 2512 THR ASP ARG ASN PRO GLN ALA LEU GLU ALA ALA GLN ALA
SEQRES 100 A 2512 LYS LEU GLU GLN LEU HIS VAL THR GLN GLY GLN TRP ASP
SEQRES 101 A 2512 PRO ALA ASN PRO ALA PRO GLY SER LEU GLY LYS ALA ASP
SEQRES 102 A 2512 LEU LEU VAL CYS ASN CYS ALA LEU ALA THR LEU GLY ASP
SEQRES 103 A 2512 PRO ALA VAL ALA VAL GLY ASN MET ALA ALA THR LEU LYS
SEQRES 104 A 2512 GLU GLY GLY PHE LEU LEU LEU HIS THR LEU LEU ALA GLY
SEQRES 105 A 2512 HIS PRO LEU GLY GLU MET VAL GLY PHE LEU THR SER PRO
SEQRES 106 A 2512 GLU GLN GLY GLY ARG HIS LEU LEU SER GLN ASP GLN TRP
SEQRES 107 A 2512 GLU SER LEU PHE ALA GLY ALA SER LEU HIS LEU VAL ALA
SEQRES 108 A 2512 LEU LYS ARG SER PHE TYR GLY SER VAL LEU PHE LEU CYS
SEQRES 109 A 2512 ARG GLN GLN THR PRO GLN ASP SER PRO VAL PHE LEU SER
SEQRES 110 A 2512 VAL GLU ASP THR SER PHE ARG TRP VAL ASP SER LEU LYS
SEQRES 111 A 2512 ASP ILE LEU ALA ASP ALA SER SER ARG PRO VAL TRP LEU
SEQRES 112 A 2512 MET ALA VAL GLY CYS SER THR SER GLY VAL VAL GLY MET
SEQRES 113 A 2512 VAL ASN CYS LEU ARG LYS GLU PRO GLY GLY HIS ARG ILE
SEQRES 114 A 2512 ARG CYS VAL LEU VAL SER ASN LEU SER SER THR SER PRO
SEQRES 115 A 2512 ALA PRO GLU MET HIS PRO SER SER SER GLU LEU GLN LYS
SEQRES 116 A 2512 VAL LEU GLN GLY ASP LEU VAL MET ASN VAL TYR ARG ASP
SEQRES 117 A 2512 GLY ALA TRP GLY ALA PHE ARG HIS PHE PRO LEU GLU GLN
SEQRES 118 A 2512 ASP ARG PRO GLU LYS GLN THR GLU HIS ALA PHE VAL ASN
SEQRES 119 A 2512 VAL LEU SER ARG GLY ASP LEU SER SER ILE ARG TRP VAL
SEQRES 120 A 2512 CYS SER PRO LEU HIS TYR ALA LEU PRO ALA SER CYS GLN
SEQRES 121 A 2512 ASP ARG LEU CYS SER VAL TYR TYR THR SER LEU ASN PHE
SEQRES 122 A 2512 ARG ASP VAL MET LEU ALA THR GLY LYS LEU SER PRO ASP
SEQRES 123 A 2512 SER ILE PRO GLY LYS TRP LEU THR ARG ASP CYS MET LEU
SEQRES 124 A 2512 GLY MET GLU PHE SER GLY ARG ASP ALA SER GLY ARG ARG
SEQRES 125 A 2512 VAL MET GLY MET VAL PRO ALA GLU GLY LEU ALA THR SER
SEQRES 126 A 2512 VAL LEU LEU LEU GLN HIS ALA THR TRP GLU VAL PRO SER
SEQRES 127 A 2512 THR TRP THR LEU GLU GLU ALA ALA SER VAL PRO ILE VAL
SEQRES 128 A 2512 TYR THR THR ALA TYR TYR SER LEU VAL VAL ARG GLY ARG
SEQRES 129 A 2512 MET GLN PRO GLY GLU SER VAL LEU ILE HIS SER GLY SER
SEQRES 130 A 2512 GLY GLY VAL GLY GLN ALA ALA ILE ALA ILE ALA LEU SER
SEQRES 131 A 2512 ARG GLY CYS ARG VAL PHE THR THR VAL GLY SER ALA GLU
SEQRES 132 A 2512 LYS ARG ALA TYR LEU GLN ALA ARG PHE PRO GLN LEU ASP
SEQRES 133 A 2512 GLU THR CYS PHE ALA ASN SER ARG ASP THR SER PHE GLU
SEQRES 134 A 2512 GLN HIS VAL LEU ARG HIS THR ALA GLY LYS GLY VAL ASP
SEQRES 135 A 2512 LEU VAL LEU ASN SER LEU ALA GLU GLU LYS LEU GLN ALA
SEQRES 136 A 2512 SER VAL ARG CYS LEU ALA GLN HIS GLY ARG PHE LEU GLU
SEQRES 137 A 2512 ILE GLY LYS PHE ASP LEU SER ASN ASN HIS ALA LEU GLY
SEQRES 138 A 2512 MET ALA VAL PHE LEU LYS ASN VAL THR PHE HIS GLY ILE
SEQRES 139 A 2512 LEU LEU ASP SER LEU PHE GLU GLU GLY GLY ALA THR TRP
SEQRES 140 A 2512 GLN GLU VAL SER GLU LEU LEU LYS ALA GLY ILE GLN GLU
SEQRES 141 A 2512 GLY VAL VAL GLN PRO LEU LYS CYS THR VAL PHE PRO ARG
SEQRES 142 A 2512 THR LYS VAL GLU ALA ALA PHE ARG TYR MET ALA GLN GLY
SEQRES 143 A 2512 LYS HIS ILE GLY LYS VAL VAL ILE GLN VAL ARG GLU GLU
SEQRES 144 A 2512 GLU GLN GLY PRO ALA PRO ARG GLY LEU PRO PRO ILE ALA
SEQRES 145 A 2512 LEU THR GLY LEU SER LYS THR PHE CYS PRO PRO HIS LYS
SEQRES 146 A 2512 SER TYR VAL ILE THR GLY GLY LEU GLY GLY PHE GLY LEU
SEQRES 147 A 2512 GLN LEU ALA GLN TRP LEU ARG LEU ARG GLY ALA GLN LYS
SEQRES 148 A 2512 LEU VAL LEU THR SER ARG SER GLY ILE ARG THR GLY TYR
SEQRES 149 A 2512 GLN ALA ARG GLN VAL ARG GLU TRP ARG ARG GLN GLY VAL
SEQRES 150 A 2512 GLN VAL LEU VAL SER THR SER ASN ALA SER SER LEU ASP
SEQRES 151 A 2512 GLY ALA ARG SER LEU ILE THR GLU ALA THR GLN LEU GLY
SEQRES 152 A 2512 PRO VAL GLY GLY VAL PHE ASN LEU ALA MET VAL LEU ARG
SEQRES 153 A 2512 ASP ALA VAL LEU GLU ASN GLN THR PRO GLU PHE PHE GLN
SEQRES 154 A 2512 ASP VAL SER LYS PRO LYS TYR SER GLY THR ALA ASN LEU
SEQRES 155 A 2512 ASP ARG VAL THR ARG GLU ALA CYS PRO GLU LEU ASP TYR
SEQRES 156 A 2512 PHE VAL ILE PHE SER SER VAL SER CYS GLY ARG GLY ASN
SEQRES 157 A 2512 ALA GLY GLN ALA ASN TYR GLY PHE ALA ASN SER ALA MET
SEQRES 158 A 2512 GLU ARG ILE CYS GLU LYS ARG ARG HIS ASP GLY LEU PRO
SEQRES 159 A 2512 GLY LEU ALA VAL GLN TRP GLY ALA ILE GLY ASP VAL GLY
SEQRES 160 A 2512 VAL VAL LEU GLU THR MET GLY THR ASN ASP THR VAL ILE
SEQRES 161 A 2512 GLY GLY THR LEU PRO GLN ARG ILE ALA SER CYS LEU GLU
SEQRES 162 A 2512 VAL LEU ASP LEU PHE LEU SER GLN PRO HIS PRO VAL LEU
SEQRES 163 A 2512 SER SER PHE VAL LEU ALA GLU LYS LYS ALA ALA ALA PRO
SEQRES 164 A 2512 ARG ASP GLY SER SER GLN LYS ASP LEU VAL LYS ALA VAL
SEQRES 165 A 2512 ALA HIS ILE LEU GLY ILE ARG ASP VAL ALA SER ILE ASN
SEQRES 166 A 2512 PRO ASP SER THR LEU VAL ASP LEU GLY LEU ASP SER LEU
SEQRES 167 A 2512 MET GLY VAL GLU VAL ARG GLN ILE LEU GLU ARG GLU HIS
SEQRES 168 A 2512 ASP LEU VAL LEU SER MET ARG GLU VAL ARG GLN LEU SER
SEQRES 169 A 2512 LEU ARG LYS LEU GLN GLU LEU SER SER LYS THR SER THR
SEQRES 170 A 2512 ASP ALA ASP PRO ALA THR PRO THR SER HIS GLU ASP SER
SEQRES 171 A 2512 PRO VAL ARG GLN GLN ALA THR LEU ASN LEU SER THR LEU
SEQRES 172 A 2512 LEU VAL ASN PRO GLU GLY PRO THR LEU THR ARG LEU ASN
SEQRES 173 A 2512 SER VAL GLN SER ALA GLU ARG PRO LEU PHE LEU VAL HIS
SEQRES 174 A 2512 PRO ILE GLU GLY SER ILE THR VAL PHE HIS GLY LEU ALA
SEQRES 175 A 2512 ALA LYS LEU SER ILE PRO THR TYR GLY LEU GLN CYS THR
SEQRES 176 A 2512 GLY ALA ALA PRO LEU ASP SER ILE GLN SER LEU ALA SER
SEQRES 177 A 2512 TYR TYR ILE GLU CYS ILE ARG GLN VAL GLN PRO GLU GLY
SEQRES 178 A 2512 PRO TYR ARG ILE ALA GLY TYR SER TYR GLY ALA CYS VAL
SEQRES 179 A 2512 ALA PHE GLU MET CYS SER GLN LEU GLN ALA GLN GLN SER
SEQRES 180 A 2512 ALA THR PRO GLY ASN HIS SER LEU PHE LEU PHE ASP GLY
SEQRES 181 A 2512 SER HIS THR PHE VAL LEU ALA TYR THR GLN SER VAL ARG
SEQRES 182 A 2512 ALA LYS MET THR PRO GLY CYS GLU ALA GLU ALA GLU ALA
SEQRES 183 A 2512 LYS ALA MET TYR PHE PHE VAL GLN GLN PHE THR ASP MET
SEQRES 184 A 2512 GLU GLN GLY LYS VAL LEU GLU ALA LEU ILE PRO LEU GLN
SEQRES 185 A 2512 GLY LEU GLU ALA ARG VAL ALA ALA THR VAL ASP LEU ILE
SEQRES 186 A 2512 THR GLN SER HIS ALA GLY LEU ASP ARG HIS ALA LEU SER
SEQRES 187 A 2512 PHE ALA ALA ARG SER PHE TYR GLN LYS LEU ARG ALA ALA
SEQRES 188 A 2512 GLU ASN TYR TRP PRO GLN ALA THR TYR HIS GLY ASN VAL
SEQRES 189 A 2512 THR LEU LEU ARG ALA LYS THR GLY GLY ALA TYR GLY GLU
SEQRES 190 A 2512 ASP LEU GLY ALA ASP TYR ASN LEU SER GLN VAL CYS ASP
SEQRES 191 A 2512 GLY LYS VAL SER VAL HIS VAL ILE GLU GLY ASP HIS ARG
SEQRES 192 A 2512 THR LEU LEU GLU GLY SER GLY LEU GLU SER ILE LEU SER
SEQRES 193 A 2512 ILE ILE HIS SER CYS LEU ALA GLU PRO ARG VAL SER VAL
SEQRES 194 A 2512 ARG GLU GLY
SEQRES 1 B 2512 MET GLU GLU VAL VAL ILE ALA GLY MET SER GLY LYS LEU
SEQRES 2 B 2512 PRO GLU SER GLU ASN LEU GLU GLU PHE TRP ALA ASN LEU
SEQRES 3 B 2512 ILE GLY GLY VAL ASP MET VAL THR ALA ASP ASP ARG ARG
SEQRES 4 B 2512 TRP LYS ALA GLY LEU TYR GLY LEU PRO ARG ARG MET GLY
SEQRES 5 B 2512 LYS LEU LYS ASP LEU SER ARG PHE ASP ALA SER PHE PHE
SEQRES 6 B 2512 GLY VAL HIS SER LYS GLN ALA ASN THR MET ASP PRO GLN
SEQRES 7 B 2512 LEU ARG MET LEU LEU GLU VAL THR TYR GLU ALA ILE VAL
SEQRES 8 B 2512 ASP GLY GLY ILE ASN PRO ALA SER LEU ARG GLY THR SER
SEQRES 9 B 2512 THR GLY VAL TRP VAL GLY VAL SER SER SER ASP ALA SER
SEQRES 10 B 2512 GLU ALA LEU SER ARG ASP PRO GLU THR LEU VAL GLY TYR
SEQRES 11 B 2512 SER MET ILE GLY CYS GLN ARG ALA MET MET ALA ASN ARG
SEQRES 12 B 2512 LEU SER PHE PHE PHE ASP PHE LYS GLY PRO SER ILE THR
SEQRES 13 B 2512 ILE ASP THR ALA CYS SER SER SER LEU LEU ALA LEU GLN
SEQRES 14 B 2512 SER ALA TYR GLN ALA ILE ARG GLY GLY GLU CYS SER ALA
SEQRES 15 B 2512 ALA VAL VAL GLY GLY LEU ASN VAL LEU LEU LYS PRO ASN
SEQRES 16 B 2512 SER SER LEU GLN PHE MET LYS LEU GLY MET LEU SER GLN
SEQRES 17 B 2512 ASP GLY THR CYS ARG SER PHE ASP ALA GLU GLY THR GLY
SEQRES 18 B 2512 TYR CYS ARG ALA GLU ALA VAL VAL ALA VAL LEU LEU THR
SEQRES 19 B 2512 LYS LYS SER LEU ALA ARG ARG VAL TYR ALA THR ILE LEU
SEQRES 20 B 2512 ASN ALA GLY THR ASN THR ASP GLY SER LYS GLU GLN GLY
SEQRES 21 B 2512 VAL THR PHE PRO SER GLY ASP VAL GLN GLU GLN LEU ILE
SEQRES 22 B 2512 ARG SER LEU TYR ALA PRO ALA GLY PRO ASP PRO GLU SER
SEQRES 23 B 2512 LEU GLU TYR ILE GLU ALA HIS GLY THR GLY THR LYS VAL
SEQRES 24 B 2512 GLY ASP PRO GLN GLU LEU ASN GLY ILE VAL ASN ALA LEU
SEQRES 25 B 2512 CYS ALA THR ARG ARG GLU PRO LEU LEU ILE GLY SER THR
SEQRES 26 B 2512 LYS SER ASN MET GLY HIS PRO GLU PRO ALA SER GLY VAL
SEQRES 27 B 2512 ALA ALA LEU ILE LYS VAL LEU LEU SER LEU GLU HIS GLY
SEQRES 28 B 2512 VAL TRP ALA PRO ASN LEU HIS TYR HIS THR PRO ASN PRO
SEQRES 29 B 2512 GLU ILE PRO ALA LEU GLN ASP GLY ARG LEU GLN VAL VAL
SEQRES 30 B 2512 ASP ARG PRO LEU PRO ILE ARG GLY GLY ASN VAL GLY ILE
SEQRES 31 B 2512 ASN SER PHE GLY PHE GLY GLY SER ASN VAL HIS VAL ILE
SEQRES 32 B 2512 LEU GLN PRO ASN SER ARG PRO ALA PRO PRO PRO ALA GLN
SEQRES 33 B 2512 HIS ALA ALA LEU PRO ARG LEU LEU GLN ALA SER GLY ARG
SEQRES 34 B 2512 THR LEU GLU ALA VAL GLN THR LEU LEU GLU GLN GLY LEU
SEQRES 35 B 2512 ARG HIS SER ARG ASP LEU ALA PHE VAL GLY MET LEU ASN
SEQRES 36 B 2512 GLU ILE ALA ALA VAL SER PRO VAL ALA MET PRO PHE ARG
SEQRES 37 B 2512 GLY TYR ALA VAL LEU GLY GLY GLU ALA GLY SER GLN GLU
SEQRES 38 B 2512 VAL GLN GLN VAL PRO GLY SER LYS ARG PRO VAL TRP PHE
SEQRES 39 B 2512 ILE CYS SER GLY MET GLY ALA GLN TRP GLN GLY MET GLY
SEQRES 40 B 2512 LEU SER LEU MET ARG LEU ASP ARG PHE ARG ASP SER ILE
SEQRES 41 B 2512 LEU ARG SER ASP GLN ALA LEU LYS PRO LEU GLY LEU ARG
SEQRES 42 B 2512 VAL SER ASP LEU LEU LEU SER THR ASP GLU ALA VAL LEU
SEQRES 43 B 2512 ASP ASP ILE VAL SER SER PHE VAL SER LEU THR SER ILE
SEQRES 44 B 2512 GLN ILE ALA LEU ILE ASP LEU LEU THR SER LEU GLY LEU
SEQRES 45 B 2512 GLN PRO ASP GLY ILE ILE GLY HIS SER LEU GLY GLU VAL
SEQRES 46 B 2512 ALA CYS GLY TYR ALA ASP GLY CYS LEU THR GLN GLU GLU
SEQRES 47 B 2512 ALA VAL LEU SER SER TYR TRP ARG GLY TYR CYS ILE LYS
SEQRES 48 B 2512 GLU ALA ASN VAL LEU PRO GLY ALA MET ALA ALA VAL GLY
SEQRES 49 B 2512 LEU SER TRP GLU GLU CYS LYS GLN ARG CYS PRO PRO GLY
SEQRES 50 B 2512 ILE VAL PRO ALA CYS HIS ASN SER LYS ASP THR VAL THR
SEQRES 51 B 2512 ILE SER GLY PRO GLN ALA ALA MET SER GLU PHE LEU GLN
SEQRES 52 B 2512 GLN LEU LYS ARG GLU ASP VAL PHE VAL LYS GLU VAL ARG
SEQRES 53 B 2512 THR GLY GLY ILE ALA PHE HIS SER TYR PHE MET GLU SER
SEQRES 54 B 2512 ILE ALA PRO THR LEU LEU ARG GLN LEU ARG LYS VAL ILE
SEQRES 55 B 2512 LEU ASP PRO LYS PRO ARG SER LYS ARG TRP LEU SER THR
SEQRES 56 B 2512 SER ILE PRO GLU ALA GLN TRP GLN GLY SER LEU ALA ARG
SEQRES 57 B 2512 THR PHE SER ALA GLU TYR SER VAL ASN ASN LEU VAL SER
SEQRES 58 B 2512 PRO VAL LEU PHE GLN GLU ALA LEU GLN HIS VAL PRO ALA
SEQRES 59 B 2512 HIS ALA VAL VAL VAL GLU ILE ALA PRO HIS ALA LEU LEU
SEQRES 60 B 2512 GLN ALA VAL LEU LYS ARG SER LEU GLU SER SER CYS THR
SEQRES 61 B 2512 ILE ILE PRO LEU MET LYS LYS ASP HIS ARG ASP ASN LEU
SEQRES 62 B 2512 GLU PHE PHE LEU SER ASN VAL GLY ARG LEU HIS LEU ALA
SEQRES 63 B 2512 GLY VAL SER VAL ASN PRO ASN GLY LEU PHE PRO PRO VAL
SEQRES 64 B 2512 GLU PHE PRO ALA PRO ARG GLY THR PRO LEU ILE SER PRO
SEQRES 65 B 2512 HIS ILE LYS TRP ASP HIS SER GLN ALA TRP ASP VAL PRO
SEQRES 66 B 2512 SER ALA ALA ASP PHE PRO SER GLY SER SER CYS SER SER
SEQRES 67 B 2512 VAL ALA VAL TYR LYS PHE ASP VAL SER PRO GLU SER PRO
SEQRES 68 B 2512 ASP HIS TYR LEU VAL ASP HIS CYS ILE ASP GLY ARG VAL
SEQRES 69 B 2512 LEU PHE PRO GLY THR GLY TYR LEU TRP LEU THR TRP LYS
SEQRES 70 B 2512 THR LEU ALA ARG ALA LEU SER GLN ASN LEU GLU GLU THR
SEQRES 71 B 2512 PRO VAL VAL PHE GLU ASP VAL THR LEU HIS GLN ALA THR
SEQRES 72 B 2512 ILE LEU PRO LYS THR GLY THR VAL SER LEU GLU VAL ARG
SEQRES 73 B 2512 LEU LEU GLU ALA SER HIS ALA PHE GLU VAL SER ASP SER
SEQRES 74 B 2512 ASN GLY SER LEU ILE ALA SER GLY LYS VAL TYR GLN TRP
SEQRES 75 B 2512 GLU SER PRO ASP PRO LYS LEU PHE ASP THR ARG ALA ALA
SEQRES 76 B 2512 VAL ASP PRO ALA ASP SER THR ALA GLU PHE ARG LEU SER
SEQRES 77 B 2512 GLN GLY ASP VAL TYR LYS ASP LEU ARG LEU ARG GLY TYR
SEQRES 78 B 2512 ASP TYR GLY PRO PHE PHE GLN LEU VAL LEU GLU SER ASP
SEQRES 79 B 2512 LEU GLU GLY ASN ARG GLY ARG LEU GLN TRP ASN ASP SER
SEQRES 80 B 2512 TRP VAL SER PHE LEU ASP ALA MET LEU HIS MET SER ILE
SEQRES 81 B 2512 LEU ALA PRO GLY GLN LEU GLY LEU TYR LEU PRO THR ARG
SEQRES 82 B 2512 PHE THR SER ILE ARG ILE ASP PRO VAL THR HIS ARG GLN
SEQRES 83 B 2512 LYS LEU TYR THR LEU GLN ASP THR THR GLN ALA ALA ASP
SEQRES 84 B 2512 VAL VAL VAL ASP ARG ASN LEU ASN THR VAL VAL ALA GLY
SEQRES 85 B 2512 GLY ALA LEU PHE LEU GLY ALA HIS SER SER VAL ALA PRO
SEQRES 86 B 2512 ARG ARG PRO GLN GLU HIS LEU LYS PRO ILE LEU GLU LYS
SEQRES 87 B 2512 PHE CYS PHE THR PRO HIS VAL GLU SER GLY CYS LEU ALA
SEQRES 88 B 2512 GLY ASN THR ALA LEU GLN GLU GLU LEU GLN LEU CYS ARG
SEQRES 89 B 2512 GLY LEU ALA GLN ALA LEU GLN THR LYS VAL ALA GLN GLN
SEQRES 90 B 2512 GLY LEU LYS MET VAL VAL PRO GLY LEU ASP GLY ALA GLN
SEQRES 91 B 2512 ALA PRO ARG GLU ALA PRO GLN GLN SER LEU PRO ARG LEU
SEQRES 92 B 2512 LEU ALA ALA ALA CYS GLN LEU GLN LEU ASN GLY ASN LEU
SEQRES 93 B 2512 GLN LEU GLU LEU GLY GLN VAL LEU ALA GLN GLU ARG PRO
SEQRES 94 B 2512 LEU LEU CYS ASP ASP PRO LEU LEU SER GLY LEU LEU ASP
SEQRES 95 B 2512 ALA PRO ALA LEU LYS ALA CYS VAL ASP THR ALA LEU GLU
SEQRES 96 B 2512 ASN MET ALA SER PRO LYS MET LYS VAL VAL GLU VAL LEU
SEQRES 97 B 2512 ALA GLY ASP GLY GLN LEU TYR SER ARG ILE PRO ALA LEU
SEQRES 98 B 2512 LEU ASN THR GLN PRO VAL MET ASP LEU ASP TYR THR ALA
SEQRES 99 B 2512 THR ASP ARG ASN PRO GLN ALA LEU GLU ALA ALA GLN ALA
SEQRES 100 B 2512 LYS LEU GLU GLN LEU HIS VAL THR GLN GLY GLN TRP ASP
SEQRES 101 B 2512 PRO ALA ASN PRO ALA PRO GLY SER LEU GLY LYS ALA ASP
SEQRES 102 B 2512 LEU LEU VAL CYS ASN CYS ALA LEU ALA THR LEU GLY ASP
SEQRES 103 B 2512 PRO ALA VAL ALA VAL GLY ASN MET ALA ALA THR LEU LYS
SEQRES 104 B 2512 GLU GLY GLY PHE LEU LEU LEU HIS THR LEU LEU ALA GLY
SEQRES 105 B 2512 HIS PRO LEU GLY GLU MET VAL GLY PHE LEU THR SER PRO
SEQRES 106 B 2512 GLU GLN GLY GLY ARG HIS LEU LEU SER GLN ASP GLN TRP
SEQRES 107 B 2512 GLU SER LEU PHE ALA GLY ALA SER LEU HIS LEU VAL ALA
SEQRES 108 B 2512 LEU LYS ARG SER PHE TYR GLY SER VAL LEU PHE LEU CYS
SEQRES 109 B 2512 ARG GLN GLN THR PRO GLN ASP SER PRO VAL PHE LEU SER
SEQRES 110 B 2512 VAL GLU ASP THR SER PHE ARG TRP VAL ASP SER LEU LYS
SEQRES 111 B 2512 ASP ILE LEU ALA ASP ALA SER SER ARG PRO VAL TRP LEU
SEQRES 112 B 2512 MET ALA VAL GLY CYS SER THR SER GLY VAL VAL GLY MET
SEQRES 113 B 2512 VAL ASN CYS LEU ARG LYS GLU PRO GLY GLY HIS ARG ILE
SEQRES 114 B 2512 ARG CYS VAL LEU VAL SER ASN LEU SER SER THR SER PRO
SEQRES 115 B 2512 ALA PRO GLU MET HIS PRO SER SER SER GLU LEU GLN LYS
SEQRES 116 B 2512 VAL LEU GLN GLY ASP LEU VAL MET ASN VAL TYR ARG ASP
SEQRES 117 B 2512 GLY ALA TRP GLY ALA PHE ARG HIS PHE PRO LEU GLU GLN
SEQRES 118 B 2512 ASP ARG PRO GLU LYS GLN THR GLU HIS ALA PHE VAL ASN
SEQRES 119 B 2512 VAL LEU SER ARG GLY ASP LEU SER SER ILE ARG TRP VAL
SEQRES 120 B 2512 CYS SER PRO LEU HIS TYR ALA LEU PRO ALA SER CYS GLN
SEQRES 121 B 2512 ASP ARG LEU CYS SER VAL TYR TYR THR SER LEU ASN PHE
SEQRES 122 B 2512 ARG ASP VAL MET LEU ALA THR GLY LYS LEU SER PRO ASP
SEQRES 123 B 2512 SER ILE PRO GLY LYS TRP LEU THR ARG ASP CYS MET LEU
SEQRES 124 B 2512 GLY MET GLU PHE SER GLY ARG ASP ALA SER GLY ARG ARG
SEQRES 125 B 2512 VAL MET GLY MET VAL PRO ALA GLU GLY LEU ALA THR SER
SEQRES 126 B 2512 VAL LEU LEU LEU GLN HIS ALA THR TRP GLU VAL PRO SER
SEQRES 127 B 2512 THR TRP THR LEU GLU GLU ALA ALA SER VAL PRO ILE VAL
SEQRES 128 B 2512 TYR THR THR ALA TYR TYR SER LEU VAL VAL ARG GLY ARG
SEQRES 129 B 2512 MET GLN PRO GLY GLU SER VAL LEU ILE HIS SER GLY SER
SEQRES 130 B 2512 GLY GLY VAL GLY GLN ALA ALA ILE ALA ILE ALA LEU SER
SEQRES 131 B 2512 ARG GLY CYS ARG VAL PHE THR THR VAL GLY SER ALA GLU
SEQRES 132 B 2512 LYS ARG ALA TYR LEU GLN ALA ARG PHE PRO GLN LEU ASP
SEQRES 133 B 2512 GLU THR CYS PHE ALA ASN SER ARG ASP THR SER PHE GLU
SEQRES 134 B 2512 GLN HIS VAL LEU ARG HIS THR ALA GLY LYS GLY VAL ASP
SEQRES 135 B 2512 LEU VAL LEU ASN SER LEU ALA GLU GLU LYS LEU GLN ALA
SEQRES 136 B 2512 SER VAL ARG CYS LEU ALA GLN HIS GLY ARG PHE LEU GLU
SEQRES 137 B 2512 ILE GLY LYS PHE ASP LEU SER ASN ASN HIS ALA LEU GLY
SEQRES 138 B 2512 MET ALA VAL PHE LEU LYS ASN VAL THR PHE HIS GLY ILE
SEQRES 139 B 2512 LEU LEU ASP SER LEU PHE GLU GLU GLY GLY ALA THR TRP
SEQRES 140 B 2512 GLN GLU VAL SER GLU LEU LEU LYS ALA GLY ILE GLN GLU
SEQRES 141 B 2512 GLY VAL VAL GLN PRO LEU LYS CYS THR VAL PHE PRO ARG
SEQRES 142 B 2512 THR LYS VAL GLU ALA ALA PHE ARG TYR MET ALA GLN GLY
SEQRES 143 B 2512 LYS HIS ILE GLY LYS VAL VAL ILE GLN VAL ARG GLU GLU
SEQRES 144 B 2512 GLU GLN GLY PRO ALA PRO ARG GLY LEU PRO PRO ILE ALA
SEQRES 145 B 2512 LEU THR GLY LEU SER LYS THR PHE CYS PRO PRO HIS LYS
SEQRES 146 B 2512 SER TYR VAL ILE THR GLY GLY LEU GLY GLY PHE GLY LEU
SEQRES 147 B 2512 GLN LEU ALA GLN TRP LEU ARG LEU ARG GLY ALA GLN LYS
SEQRES 148 B 2512 LEU VAL LEU THR SER ARG SER GLY ILE ARG THR GLY TYR
SEQRES 149 B 2512 GLN ALA ARG GLN VAL ARG GLU TRP ARG ARG GLN GLY VAL
SEQRES 150 B 2512 GLN VAL LEU VAL SER THR SER ASN ALA SER SER LEU ASP
SEQRES 151 B 2512 GLY ALA ARG SER LEU ILE THR GLU ALA THR GLN LEU GLY
SEQRES 152 B 2512 PRO VAL GLY GLY VAL PHE ASN LEU ALA MET VAL LEU ARG
SEQRES 153 B 2512 ASP ALA VAL LEU GLU ASN GLN THR PRO GLU PHE PHE GLN
SEQRES 154 B 2512 ASP VAL SER LYS PRO LYS TYR SER GLY THR ALA ASN LEU
SEQRES 155 B 2512 ASP ARG VAL THR ARG GLU ALA CYS PRO GLU LEU ASP TYR
SEQRES 156 B 2512 PHE VAL ILE PHE SER SER VAL SER CYS GLY ARG GLY ASN
SEQRES 157 B 2512 ALA GLY GLN ALA ASN TYR GLY PHE ALA ASN SER ALA MET
SEQRES 158 B 2512 GLU ARG ILE CYS GLU LYS ARG ARG HIS ASP GLY LEU PRO
SEQRES 159 B 2512 GLY LEU ALA VAL GLN TRP GLY ALA ILE GLY ASP VAL GLY
SEQRES 160 B 2512 VAL VAL LEU GLU THR MET GLY THR ASN ASP THR VAL ILE
SEQRES 161 B 2512 GLY GLY THR LEU PRO GLN ARG ILE ALA SER CYS LEU GLU
SEQRES 162 B 2512 VAL LEU ASP LEU PHE LEU SER GLN PRO HIS PRO VAL LEU
SEQRES 163 B 2512 SER SER PHE VAL LEU ALA GLU LYS LYS ALA ALA ALA PRO
SEQRES 164 B 2512 ARG ASP GLY SER SER GLN LYS ASP LEU VAL LYS ALA VAL
SEQRES 165 B 2512 ALA HIS ILE LEU GLY ILE ARG ASP VAL ALA SER ILE ASN
SEQRES 166 B 2512 PRO ASP SER THR LEU VAL ASP LEU GLY LEU ASP SER LEU
SEQRES 167 B 2512 MET GLY VAL GLU VAL ARG GLN ILE LEU GLU ARG GLU HIS
SEQRES 168 B 2512 ASP LEU VAL LEU SER MET ARG GLU VAL ARG GLN LEU SER
SEQRES 169 B 2512 LEU ARG LYS LEU GLN GLU LEU SER SER LYS THR SER THR
SEQRES 170 B 2512 ASP ALA ASP PRO ALA THR PRO THR SER HIS GLU ASP SER
SEQRES 171 B 2512 PRO VAL ARG GLN GLN ALA THR LEU ASN LEU SER THR LEU
SEQRES 172 B 2512 LEU VAL ASN PRO GLU GLY PRO THR LEU THR ARG LEU ASN
SEQRES 173 B 2512 SER VAL GLN SER ALA GLU ARG PRO LEU PHE LEU VAL HIS
SEQRES 174 B 2512 PRO ILE GLU GLY SER ILE THR VAL PHE HIS GLY LEU ALA
SEQRES 175 B 2512 ALA LYS LEU SER ILE PRO THR TYR GLY LEU GLN CYS THR
SEQRES 176 B 2512 GLY ALA ALA PRO LEU ASP SER ILE GLN SER LEU ALA SER
SEQRES 177 B 2512 TYR TYR ILE GLU CYS ILE ARG GLN VAL GLN PRO GLU GLY
SEQRES 178 B 2512 PRO TYR ARG ILE ALA GLY TYR SER TYR GLY ALA CYS VAL
SEQRES 179 B 2512 ALA PHE GLU MET CYS SER GLN LEU GLN ALA GLN GLN SER
SEQRES 180 B 2512 ALA THR PRO GLY ASN HIS SER LEU PHE LEU PHE ASP GLY
SEQRES 181 B 2512 SER HIS THR PHE VAL LEU ALA TYR THR GLN SER VAL ARG
SEQRES 182 B 2512 ALA LYS MET THR PRO GLY CYS GLU ALA GLU ALA GLU ALA
SEQRES 183 B 2512 LYS ALA MET TYR PHE PHE VAL GLN GLN PHE THR ASP MET
SEQRES 184 B 2512 GLU GLN GLY LYS VAL LEU GLU ALA LEU ILE PRO LEU GLN
SEQRES 185 B 2512 GLY LEU GLU ALA ARG VAL ALA ALA THR VAL ASP LEU ILE
SEQRES 186 B 2512 THR GLN SER HIS ALA GLY LEU ASP ARG HIS ALA LEU SER
SEQRES 187 B 2512 PHE ALA ALA ARG SER PHE TYR GLN LYS LEU ARG ALA ALA
SEQRES 188 B 2512 GLU ASN TYR TRP PRO GLN ALA THR TYR HIS GLY ASN VAL
SEQRES 189 B 2512 THR LEU LEU ARG ALA LYS THR GLY GLY ALA TYR GLY GLU
SEQRES 190 B 2512 ASP LEU GLY ALA ASP TYR ASN LEU SER GLN VAL CYS ASP
SEQRES 191 B 2512 GLY LYS VAL SER VAL HIS VAL ILE GLU GLY ASP HIS ARG
SEQRES 192 B 2512 THR LEU LEU GLU GLY SER GLY LEU GLU SER ILE LEU SER
SEQRES 193 B 2512 ILE ILE HIS SER CYS LEU ALA GLU PRO ARG VAL SER VAL
SEQRES 194 B 2512 ARG GLU GLY
HET NAP A3001 48
HET NAP A3002 48
HET NAP B3001 48
HET NAP B3002 48
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM 2 NAP PHOSPHATE
FORMUL 3 NAP 4(C21 H28 N7 O17 P3)
HELIX 1 1 LEU A 19 GLY A 28 1 10
HELIX 2 2 GLY A 43 LEU A 47 5 5
HELIX 3 3 HIS A 68 THR A 74 1 7
HELIX 4 4 ASP A 76 ASP A 92 1 17
HELIX 5 5 ASN A 96 LEU A 100 5 5
HELIX 6 6 SER A 114 SER A 121 1 8
HELIX 7 7 GLY A 129 CYS A 135 5 7
HELIX 8 8 ARG A 137 ASP A 149 1 13
HELIX 9 9 SER A 163 GLY A 177 1 15
HELIX 10 10 LYS A 193 LEU A 203 1 11
HELIX 11 11 GLY A 266 SER A 275 1 10
HELIX 12 12 TYR A 277 GLY A 281 5 5
HELIX 13 13 VAL A 299 CYS A 313 1 15
HELIX 14 14 THR A 325 GLY A 330 1 6
HELIX 15 15 PRO A 332 PRO A 334 5 3
HELIX 16 16 SER A 336 HIS A 350 1 15
HELIX 17 17 THR A 430 HIS A 444 1 15
HELIX 18 18 ASP A 447 ALA A 459 1 13
HELIX 19 19 LEU A 513 LEU A 527 1 15
HELIX 20 20 PRO A 529 GLY A 531 5 3
HELIX 21 21 ARG A 533 SER A 540 1 8
HELIX 22 22 ASP A 542 ASP A 547 1 6
HELIX 23 23 ILE A 549 LEU A 570 1 22
HELIX 24 24 LEU A 582 ASP A 591 1 10
HELIX 25 25 THR A 595 ALA A 613 1 19
HELIX 26 26 SER A 626 CYS A 634 1 9
HELIX 27 27 GLN A 655 GLU A 668 1 14
HELIX 28 28 TYR A 685 GLU A 688 5 4
HELIX 29 29 ILE A 690 ILE A 702 1 13
HELIX 30 30 PRO A 718 GLY A 724 5 7
HELIX 31 31 SER A 731 SER A 741 1 11
HELIX 32 32 PHE A 745 HIS A 751 1 7
HELIX 33 33 LEU A 767 SER A 774 1 8
HELIX 34 34 ASP A 791 GLY A 807 1 17
HELIX 35 35 PRO A 812 LEU A 815 5 4
HELIX 36 36 ILE A 830 ILE A 834 5 5
HELIX 37 37 PRO A 871 VAL A 876 5 6
HELIX 38 38 PRO A 887 LEU A 903 1 17
HELIX 39 39 ASN A 906 THR A 910 5 5
HELIX 30 30 ASP A 966 PHE A 970 5 5
HELIX 41 41 GLN A 989 ARG A 999 1 11
HELIX 42 42 PRO A 1005 GLN A 1008 5 4
HELIX 43 43 SER A 1027 LEU A 1041 1 15
HELIX 44 44 ASP A 1060 LEU A 1068 1 9
HELIX 45 45 THR A 1134 GLN A 1151 1 18
HELIX 46 46 ARG A 1182 ASN A 1195 1 14
HELIX 47 47 LEU A 1200 LEU A 1211 1 12
HELIX 48 48 PRO A 1224 ASN A 1236 1 13
HELIX 49 49 LEU A 1254 THR A 1264 1 11
HELIX 50 50 PRO A 1279 LEU A 1282 1 4
HELIX 51 51 ALA A 1284 LEU A 1292 1 9
HELIX 52 52 PRO A 1306 GLY A 1310 5 5
HELIX 53 53 PRO A 1327 ALA A 1336 1 10
HELIX 54 54 PRO A 1354 LEU A 1362 1 9
HELIX 55 55 SER A 1374 ALA A 1385 1 12
HELIX 56 56 ARG A 1424 ILE A 1432 1 9
HELIX 57 57 GLY A 1452 ARG A 1461 1 10
HELIX 58 58 PRO A 1464 ARG A 1468 5 5
HELIX 59 59 SER A 1491 ASP A 1500 1 10
HELIX 60 60 SER A 1549 ALA A 1554 1 6
HELIX 61 61 ALA A 1557 ARG A 1562 1 6
HELIX 62 62 ASN A 1572 GLY A 1581 1 10
HELIX 63 63 SER A 1584 ILE A 1588 5 5
HELIX 64 64 LEU A 1629 HIS A 1631 5 3
HELIX 65 65 THR A 1641 SER A 1647 1 7
HELIX 66 66 PRO A 1649 VAL A 1660 1 12
HELIX 67 67 GLY A 1678 ARG A 1691 1 14
HELIX 68 68 SER A 1701 PHE A 1712 1 12
HELIX 69 69 ASP A 1716 THR A 1718 5 3
HELIX 70 70 THR A 1726 HIS A 1735 1 10
HELIX 71 71 GLU A 1750 CYS A 1759 1 10
HELIX 72 72 LYS A 1771 ASN A 1776 1 6
HELIX 73 73 ALA A 1783 LYS A 1787 5 5
HELIX 74 74 LEU A 1795 LEU A 1799 5 5
HELIX 75 75 GLY A 1804 GLU A 1820 1 17
HELIX 76 76 LYS A 1835 GLN A 1845 1 11
HELIX 77 77 GLY A 1894 ARG A 1907 1 14
HELIX 78 78 THR A 1922 GLN A 1935 1 14
HELIX 79 79 SER A 1948 LEU A 1962 1 15
HELIX 80 80 THR A 1984 LYS A 1993 1 10
HELIX 81 81 LYS A 1995 ALA A 2009 1 15
HELIX 82 82 VAL A 2022 ARG A 2026 1 5
HELIX 83 83 GLN A 2031 ASP A 2051 1 21
HELIX 84 84 GLY A 2067 THR A 2072 1 6
HELIX 85 85 ARG A 2087 SER A 2100 1 14
HELIX 86 86 LEU B 19 GLY B 28 1 10
HELIX 87 87 GLY B 43 LEU B 47 5 5
HELIX 88 88 HIS B 68 THR B 74 1 7
HELIX 89 89 ASP B 76 ASP B 92 1 17
HELIX 90 90 ASN B 96 LEU B 100 5 5
HELIX 91 91 SER B 114 SER B 121 1 8
HELIX 92 92 GLY B 129 CYS B 135 5 7
HELIX 93 93 ARG B 137 ASP B 149 1 13
HELIX 94 94 SER B 163 GLY B 177 1 15
HELIX 95 95 LYS B 193 LEU B 203 1 11
HELIX 96 96 GLY B 266 SER B 275 1 10
HELIX 97 97 TYR B 277 GLY B 281 5 5
HELIX 98 98 VAL B 299 CYS B 313 1 15
HELIX 99 99 THR B 325 GLY B 330 1 6
HELIX 100 100 PRO B 332 PRO B 334 5 3
HELIX 101 101 SER B 336 HIS B 350 1 15
HELIX 102 102 THR B 430 HIS B 444 1 15
HELIX 103 103 ASP B 447 ALA B 459 1 13
HELIX 104 104 LEU B 513 LEU B 527 1 15
HELIX 105 105 PRO B 529 GLY B 531 5 3
HELIX 106 106 ARG B 533 SER B 540 1 8
HELIX 107 107 ASP B 542 ASP B 547 1 6
HELIX 108 108 ILE B 549 LEU B 570 1 22
HELIX 109 109 LEU B 582 ASP B 591 1 10
HELIX 110 110 THR B 595 ALA B 613 1 19
HELIX 111 111 SER B 626 CYS B 634 1 9
HELIX 112 112 GLN B 655 GLU B 668 1 14
HELIX 113 113 TYR B 685 GLU B 688 5 4
HELIX 114 114 ILE B 690 ILE B 702 1 13
HELIX 115 115 PRO B 718 GLY B 724 5 7
HELIX 116 116 SER B 731 SER B 741 1 11
HELIX 117 117 PHE B 745 HIS B 751 1 7
HELIX 118 118 LEU B 767 SER B 774 1 8
HELIX 119 119 ASP B 791 GLY B 807 1 17
HELIX 120 120 PRO B 812 LEU B 815 5 4
HELIX 121 121 ILE B 830 ILE B 834 5 5
HELIX 122 122 PRO B 871 VAL B 876 5 6
HELIX 123 123 PRO B 887 LEU B 903 1 17
HELIX 124 124 ASN B 906 THR B 910 5 5
HELIX 125 125 ASP B 966 PHE B 970 5 5
HELIX 126 126 GLN B 989 ARG B 999 1 11
HELIX 127 127 PRO B 1005 GLN B 1008 5 4
HELIX 128 128 SER B 1027 LEU B 1041 1 15
HELIX 129 129 ASP B 1060 LEU B 1068 1 9
HELIX 130 130 THR B 1134 VAL B 1154 1 21
HELIX 131 131 ARG B 1182 ASN B 1195 1 14
HELIX 132 132 GLU B 1199 LEU B 1211 1 13
HELIX 133 133 PRO B 1224 ASN B 1236 1 13
HELIX 134 134 LEU B 1254 THR B 1264 1 11
HELIX 135 135 PRO B 1279 LEU B 1282 1 4
HELIX 136 136 ALA B 1284 LEU B 1292 1 9
HELIX 137 137 PRO B 1306 GLY B 1310 5 5
HELIX 138 138 PRO B 1327 ALA B 1336 1 10
HELIX 139 139 PRO B 1354 LEU B 1362 1 9
HELIX 140 140 SER B 1364 GLY B 1368 1 5
HELIX 141 141 SER B 1374 ALA B 1385 1 12
HELIX 142 142 ARG B 1424 ILE B 1432 1 9
HELIX 143 143 GLY B 1452 ARG B 1461 1 10
HELIX 144 144 PRO B 1464 ARG B 1468 5 5
HELIX 145 145 SER B 1491 ASP B 1500 1 10
HELIX 146 146 SER B 1549 ALA B 1554 1 6
HELIX 147 147 ALA B 1557 ARG B 1562 1 6
HELIX 148 148 ASN B 1572 GLY B 1581 1 10
HELIX 149 149 SER B 1584 ILE B 1588 5 5
HELIX 150 150 LEU B 1629 HIS B 1631 5 3
HELIX 151 151 THR B 1641 SER B 1647 1 7
HELIX 152 152 PRO B 1649 VAL B 1660 1 12
HELIX 153 153 GLY B 1678 ARG B 1691 1 14
HELIX 154 154 SER B 1701 PHE B 1712 1 12
HELIX 155 155 ASP B 1716 THR B 1718 5 3
HELIX 156 156 THR B 1726 HIS B 1735 1 10
HELIX 157 157 GLU B 1750 CYS B 1759 1 10
HELIX 158 158 LYS B 1771 ASN B 1776 1 6
HELIX 159 159 ALA B 1783 LYS B 1787 5 5
HELIX 160 160 LEU B 1795 LEU B 1799 5 5
HELIX 161 161 GLY B 1804 GLU B 1820 1 17
HELIX 162 162 LYS B 1835 GLN B 1845 1 11
HELIX 163 163 GLY B 1894 ARG B 1907 1 14
HELIX 164 164 THR B 1922 GLN B 1935 1 14
HELIX 165 165 SER B 1948 LEU B 1962 1 15
HELIX 166 166 THR B 1984 LYS B 1993 1 10
HELIX 167 167 LYS B 1995 ALA B 2009 1 15
HELIX 168 168 VAL B 2022 ARG B 2026 1 5
HELIX 169 169 GLN B 2031 ASP B 2051 1 21
HELIX 170 170 GLY B 2067 THR B 2072 1 6
HELIX 171 171 ARG B 2087 SER B 2100 1 14
SHEET 1 AA22 LEU A 374 VAL A 377 0
SHEET 2 AA22 LEU A 320 SER A 324 1 O ILE A 322 N VAL A 377
SHEET 3 AA22 GLU A 288 ALA A 292 1 O GLU A 288 N LEU A 321
SHEET 4 AA22 ASN A 387 GLY A 394 1 O GLY A 389 N GLU A 291
SHEET 5 AA22 SER A 398 PRO A 406 -1 O SER A 398 N GLY A 394
SHEET 6 AA22 ALA A 244 THR A 253 -1 O THR A 245 N GLN A 405
SHEET 7 AA22 VAL A 4 LEU A 13 -1 O VAL A 4 N ILE A 246
SHEET 8 AA22 ARG A 224 LYS A 235 -1 O VAL A 228 N LYS A 12
SHEET 9 AA22 SER A 181 VAL A 190 -1 O ALA A 183 N LEU A 233
SHEET 10 AA22 THR A 105 VAL A 111 1 O GLY A 106 N VAL A 184
SHEET 11 AA22 PRO A 153 ASP A 158 1 O ILE A 155 N VAL A 109
SHEET 12 AA22 PRO B 153 ASP B 158 -1 O THR B 156 N ASP A 158
SHEET 13 AA22 THR B 105 VAL B 111 1 O VAL B 107 N ILE B 155
SHEET 14 AA22 SER B 181 VAL B 190 1 O VAL B 184 N TRP B 108
SHEET 15 AA22 ARG B 224 LYS B 235 -1 O ALA B 227 N ASN B 189
SHEET 16 AA22 VAL B 4 LEU B 13 -1 O VAL B 5 N THR B 234
SHEET 17 AA22 ALA B 244 THR B 253 -1 O ILE B 246 N VAL B 4
SHEET 18 AA22 SER B 398 PRO B 406 -1 N ASN B 399 O ASN B 252
SHEET 19 AA22 ASN B 387 GLY B 394 -1 O VAL B 388 N LEU B 404
SHEET 20 AA22 GLU B 288 ALA B 292 1 O GLU B 291 N ASN B 391
SHEET 21 AA22 LEU B 320 SER B 324 1 N LEU B 321 O GLU B 288
SHEET 22 AA22 LEU B 374 VAL B 377 1 N GLN B 375 O LEU B 320
SHEET 1 AB 3 VAL A 33 ALA A 35 0
SHEET 2 AB 3 ARG A 50 LYS A 53 -1 O MET A 51 N THR A 34
SHEET 3 AB 3 ARG A 224 LYS A 235 1 N GLU A 226 O GLY A 52
SHEET 1 AC 3 ARG A 422 GLY A 428 0
SHEET 2 AC 3 PHE A 467 LEU A 473 -1 O PHE A 467 N GLY A 428
SHEET 3 AC 3 SER A 479 GLN A 484 -1 O GLU A 481 N TYR A 470
SHEET 1 AD 5 ARG A 711 LEU A 713 0
SHEET 2 AD 5 GLY A 576 GLY A 579 1 O ILE A 577 N LEU A 713
SHEET 3 AD 5 PRO A 491 CYS A 496 1 O VAL A 492 N GLY A 576
SHEET 4 AD 5 ALA A 756 ILE A 761 1 O VAL A 757 N TRP A 493
SHEET 5 AD 5 CYS A 779 PRO A 783 1 O THR A 780 N VAL A 758
SHEET 1 AE 5 PHE A 671 VAL A 675 0
SHEET 2 AE 5 GLY A 618 GLY A 624 -1 O MET A 620 N VAL A 675
SHEET 3 AE 5 THR A 648 PRO A 654 -1 O VAL A 649 N VAL A 623
SHEET 4 AE 5 VAL A 639 SER A 645 -1 O VAL A 639 N SER A 652
SHEET 5 AE 5 VAL A 743 LEU A 744 1 O VAL A 743 N HIS A 643
SHEET 1 AF 2 LYS A 706 PRO A 707 0
SHEET 2 AF 2 THR A 729 PHE A 730 -1 N PHE A 730 O LYS A 706
SHEET 1 AG12 SER A 858 ASP A 865 0
SHEET 2 AG12 THR A 930 LEU A 938 -1 O VAL A 931 N PHE A 864
SHEET 3 AG12 ALA A 943 SER A 949 -1 O ALA A 943 N LEU A 938
SHEET 4 AG12 SER A 952 GLN A 961 -1 N ILE A 954 O VAL A 946
SHEET 5 AG12 PRO A 911 HIS A 920 -1 O VAL A 913 N TYR A 960
SHEET 6 AG12 TYR A1049 ASP A1060 -1 O ILE A1059 N VAL A 912
SHEET 7 AG12 GLY A1093 VAL A1103 -1 O LEU A1095 N ARG A1058
SHEET 8 AG12 ASN A1087 ALA A1091 -1 O ALA A1091 N ALA A1094
SHEET 9 AG12 THR A1075 ASP A1083 -1 O VAL A1081 N VAL A1090
SHEET 10 AG12 ASN A1018 TRP A1024 -1 O GLY A1020 N VAL A1080
SHEET 11 AG12 LEU A1009 ASP A1014 -1 N LEU A1011 O ARG A1021
SHEET 12 AG12 ARG A 986 SER A 988 -1 O LEU A 987 N SER A1013
SHEET 1 AH 4 THR A 923 LEU A 925 0
SHEET 2 AH 4 ARG A 883 PHE A 886 -1 O VAL A 884 N LEU A 925
SHEET 3 AH 4 ASP A 877 ASP A 881 -1 O ILE A 880 N ARG A 883
SHEET 4 AH 4 GLY A1000 GLY A1004 -1 N ASP A1002 O CYS A 879
SHEET 1 AI 2 TYR A1069 LEU A1071 0
SHEET 2 AI 2 THR A1075 ASP A1083 -1 N ALA A1077 O TYR A1069
SHEET 1 AJ13 PRO A1413 VAL A1418 0
SHEET 2 AJ13 PRO A1440 ALA A1445 1 O TRP A1442 N LEU A1416
SHEET 3 AJ13 CYS A1471 ASN A1476 1 O VAL A1472 N LEU A1443
SHEET 4 AJ13 VAL A1502 ARG A1507 1 O ASN A1504 N SER A1475
SHEET 5 AJ13 ALA A1510 PRO A1518 -1 O GLY A1512 N VAL A1505
SHEET 6 AJ13 ILE A1115 PRO A1123 -1 O LYS A1118 N PHE A1517
SHEET 7 AJ13 PRO A2104 LEU A2111 -1 N SER A2107 O GLU A1117
SHEET 8 AJ13 GLY A2055 GLY A2061 1 O ALA A2057 N LEU A2106
SHEET 9 AJ13 ASP A2014 SER A2021 1 O PHE A2016 N LEU A2056
SHEET 10 AJ13 VAL A1965 LEU A1971 1 O VAL A1968 N VAL A2017
SHEET 11 AJ13 SER A1886 GLY A1891 1 O SER A1886 N GLY A1966
SHEET 12 AJ13 GLN A1910 SER A1916 1 O LYS A1911 N TYR A1887
SHEET 13 AJ13 VAL A1937 THR A1943 1 O GLN A1938 N LEU A1912
SHEET 1 AK 8 VAL A1125 CYS A1129 0
SHEET 2 AK 8 LEU A1387 SER A1395 1 O LEU A1392 N GLU A1126
SHEET 3 AK 8 SER A1399 GLN A1406 -1 O SER A1399 N SER A1395
SHEET 4 AK 8 GLY A1342 LEU A1349 -1 O LEU A1344 N CYS A1404
SHEET 5 AK 8 ASP A1313 CYS A1319 1 O LEU A1315 N LEU A1345
SHEET 6 AK 8 LYS A1241 VAL A1247 1 O LYS A1243 N LEU A1314
SHEET 7 AK 8 ASP A1269 ASP A1276 1 O ASP A1271 N VAL A1244
SHEET 8 AK 8 VAL A1294 GLN A1298 1 O THR A1295 N ALA A1274
SHEET 1 AL 2 GLU A1525 GLU A1529 0
SHEET 2 AL 2 ALA A1872 LEU A1876 -1 O LEU A1873 N THR A1528
SHEET 1 AM 2 ALA A1531 VAL A1535 0
SHEET 2 AM 2 ILE A1544 CYS A1548 -1 O VAL A1547 N PHE A1532
SHEET 1 AN 6 LYS A1827 PRO A1832 0
SHEET 2 AN 6 GLY A1850 VAL A1856 1 O VAL A1853 N PHE A1831
SHEET 3 AN 6 LEU A1563 LEU A1571 -1 O THR A1569 N ILE A1854
SHEET 4 AN 6 MET A1601 ALA A1608 -1 O GLU A1602 N SER A1570
SHEET 5 AN 6 ARG A1611 VAL A1617 -1 O VAL A1613 N GLY A1605
SHEET 6 AN 6 ALA A1632 GLU A1635 -1 O TRP A1634 N MET A1614
SHEET 1 AO 2 LEU A1563 LEU A1571 0
SHEET 2 AO 2 THR A1624 LEU A1627 -1 N VAL A1626 O CYS A1564
SHEET 1 AP12 CYS A1719 ASN A1722 0
SHEET 2 AP12 ARG A1694 VAL A1699 1 O THR A1697 N ALA A1721
SHEET 3 AP12 SER A1670 SER A1675 1 O VAL A1671 N PHE A1696
SHEET 4 AP12 ASP A1742 SER A1747 1 N LEU A1743 O SER A1670
SHEET 5 AP12 GLY A1764 ILE A1769 1 N ARG A1765 O ASP A1742
SHEET 6 AP12 VAL A1789 GLY A1793 1 O THR A1790 N PHE A1766
SHEET 7 AP12 VAL B1789 GLY B1793 -1 O PHE B1791 N PHE A1791
SHEET 8 AP12 GLY B1764 ILE B1769 1 O GLY B1764 N THR B1790
SHEET 9 AP12 ASP B1742 SER B1747 1 O ASP B1742 N ARG B1765
SHEET 10 AP12 SER B1670 SER B1675 1 O SER B1670 N LEU B1743
SHEET 11 AP12 ARG B1694 VAL B1699 1 O ARG B1694 N VAL B1671
SHEET 12 AP12 CYS B1719 ASN B1722 1 N ALA B1721 O THR B1697
SHEET 1 AQ 2 HIS A1778 MET A1782 0
SHEET 2 AQ 2 HIS B1778 MET B1782 -1 N LEU B1780 O LEU A1780
SHEET 1 AR 2 PRO A2104 LEU A2111 0
SHEET 2 AR 2 THR A2083 LEU A2084 -1 N LEU A2084 O VAL A2110
SHEET 1 BA 3 VAL B 33 ALA B 35 0
SHEET 2 BA 3 ARG B 50 LYS B 53 -1 O MET B 51 N THR B 34
SHEET 3 BA 3 ARG B 224 LYS B 235 1 N GLU B 226 O GLY B 52
SHEET 1 BB 3 ARG B 422 GLY B 428 0
SHEET 2 BB 3 PHE B 467 LEU B 473 -1 O PHE B 467 N GLY B 428
SHEET 3 BB 3 SER B 479 GLN B 484 -1 N GLN B 483 O ARG B 468
SHEET 1 BC 5 ARG B 711 LEU B 713 0
SHEET 2 BC 5 GLY B 576 GLY B 579 1 O ILE B 577 N LEU B 713
SHEET 3 BC 5 PRO B 491 CYS B 496 1 O VAL B 492 N GLY B 576
SHEET 4 BC 5 ALA B 756 ILE B 761 1 O VAL B 757 N TRP B 493
SHEET 5 BC 5 CYS B 779 PRO B 783 1 O THR B 780 N VAL B 758
SHEET 1 BD 5 PHE B 671 VAL B 675 0
SHEET 2 BD 5 ALA B 619 GLY B 624 -1 O MET B 620 N VAL B 675
SHEET 3 BD 5 THR B 648 PRO B 654 -1 O VAL B 649 N VAL B 623
SHEET 4 BD 5 VAL B 639 SER B 645 -1 O VAL B 639 N SER B 652
SHEET 5 BD 5 VAL B 743 LEU B 744 1 O VAL B 743 N HIS B 643
SHEET 1 BE 2 LYS B 706 PRO B 707 0
SHEET 2 BE 2 THR B 729 PHE B 730 -1 N PHE B 730 O LYS B 706
SHEET 1 BF12 SER B 858 ASP B 865 0
SHEET 2 BF12 THR B 930 LEU B 938 -1 O VAL B 931 N PHE B 864
SHEET 3 BF12 ALA B 943 SER B 949 -1 O ALA B 943 N LEU B 938
SHEET 4 BF12 SER B 952 GLN B 961 -1 N ILE B 954 O VAL B 946
SHEET 5 BF12 PRO B 911 HIS B 920 -1 O VAL B 913 N TYR B 960
SHEET 6 BF12 TYR B1049 ASP B1060 -1 O ILE B1059 N VAL B 912
SHEET 7 BF12 GLY B1093 VAL B1103 -1 O LEU B1095 N ARG B1058
SHEET 8 BF12 ASN B1087 ALA B1091 -1 O ALA B1091 N ALA B1094
SHEET 9 BF12 THR B1075 ASP B1083 -1 O VAL B1081 N VAL B1090
SHEET 10 BF12 ASN B1018 TRP B1024 -1 O GLY B1020 N VAL B1080
SHEET 11 BF12 LEU B1009 ASP B1014 -1 N LEU B1011 O ARG B1021
SHEET 12 BF12 ARG B 986 SER B 988 -1 O LEU B 987 N SER B1013
SHEET 1 BG 4 THR B 923 LEU B 925 0
SHEET 2 BG 4 ARG B 883 PHE B 886 -1 O VAL B 884 N LEU B 925
SHEET 3 BG 4 ASP B 877 ASP B 881 -1 O ILE B 880 N ARG B 883
SHEET 4 BG 4 GLY B1000 GLY B1004 -1 N ASP B1002 O CYS B 879
SHEET 1 BH 2 TYR B1069 LEU B1071 0
SHEET 2 BH 2 THR B1075 ASP B1083 -1 N ALA B1077 O TYR B1069
SHEET 1 BI13 PRO B1413 VAL B1418 0
SHEET 2 BI13 PRO B1440 ALA B1445 1 O TRP B1442 N LEU B1416
SHEET 3 BI13 CYS B1471 ASN B1476 1 O VAL B1472 N LEU B1443
SHEET 4 BI13 VAL B1502 ARG B1507 1 O ASN B1504 N SER B1475
SHEET 5 BI13 ALA B1510 PRO B1518 -1 O GLY B1512 N VAL B1505
SHEET 6 BI13 ILE B1115 PRO B1123 -1 O LYS B1118 N PHE B1517
SHEET 7 BI13 PRO B2104 LEU B2111 -1 O SER B2107 N GLU B1117
SHEET 8 BI13 GLY B2055 GLY B2061 1 O ALA B2057 N LEU B2106
SHEET 9 BI13 ASP B2014 SER B2021 1 O PHE B2016 N LEU B2056
SHEET 10 BI13 VAL B1965 LEU B1971 1 O VAL B1968 N VAL B2017
SHEET 11 BI13 SER B1886 GLY B1891 1 O SER B1886 N GLY B1966
SHEET 12 BI13 GLN B1910 SER B1916 1 O LYS B1911 N TYR B1887
SHEET 13 BI13 VAL B1937 THR B1943 1 O GLN B1938 N LEU B1912
SHEET 1 BJ 8 VAL B1125 CYS B1129 0
SHEET 2 BJ 8 LEU B1387 SER B1395 1 O LEU B1392 N GLU B1126
SHEET 3 BJ 8 SER B1399 GLN B1406 -1 O SER B1399 N SER B1395
SHEET 4 BJ 8 GLY B1342 LEU B1349 -1 O LEU B1344 N CYS B1404
SHEET 5 BJ 8 ASP B1313 CYS B1319 1 O LEU B1315 N LEU B1345
SHEET 6 BJ 8 LYS B1241 VAL B1247 1 O VAL B1245 N VAL B1316
SHEET 7 BJ 8 ASP B1269 ASP B1276 1 O ASP B1269 N MET B1242
SHEET 8 BJ 8 VAL B1294 GLN B1298 1 O THR B1295 N ALA B1274
SHEET 1 BK 2 GLU B1525 GLU B1529 0
SHEET 2 BK 2 ALA B1872 LEU B1876 -1 O GLY B1875 N LYS B1526
SHEET 1 BL 2 ALA B1531 VAL B1535 0
SHEET 2 BL 2 ILE B1544 CYS B1548 -1 O ARG B1545 N ASN B1534
SHEET 1 BM 6 LYS B1827 PRO B1832 0
SHEET 2 BM 6 GLY B1850 VAL B1856 1 O VAL B1853 N PHE B1831
SHEET 3 BM 6 LEU B1563 LEU B1571 -1 O THR B1569 N ILE B1854
SHEET 4 BM 6 MET B1601 ALA B1608 -1 O GLU B1602 N SER B1570
SHEET 5 BM 6 ARG B1611 VAL B1617 -1 O VAL B1613 N GLY B1605
SHEET 6 BM 6 ALA B1632 GLU B1635 -1 O TRP B1634 N MET B1614
SHEET 1 BN 2 LEU B1563 LEU B1571 0
SHEET 2 BN 2 THR B1624 LEU B1627 -1 N VAL B1626 O CYS B1564
SHEET 1 BO 2 PRO B2104 LEU B2111 0
SHEET 2 BO 2 THR B2083 LEU B2084 -1 N LEU B2084 O VAL B2110
CISPEP 1 LEU A 703 ASP A 704 0 -4.66
CISPEP 2 PHE A 821 PRO A 822 0 4.93
CISPEP 3 PHE B 821 PRO B 822 0 4.34
SITE 1 AC1 19 PHE A1573 THR A1654 SER A1675 SER A1677
SITE 2 AC1 19 GLY A1678 GLY A1679 VAL A1680 VAL A1699
SITE 3 AC1 19 GLY A1700 LYS A1704 SER A1723 ARG A1724
SITE 4 AC1 19 ILE A1769 ILE A1794 LEU A1796 MET A1843
SITE 5 AC1 19 ALA A1844 GLY A1846 HIS A1848
SITE 1 AC2 22 GLY A1891 GLY A1894 PHE A1896 THR A1915
SITE 2 AC2 22 SER A1916 ARG A1917 SER A1918 ARG A1921
SITE 3 AC2 22 ASN A1945 LEU A1971 ALA A1972 MET A1973
SITE 4 AC2 22 LYS A1995 PHE A2019 SER A2020 SER A2021
SITE 5 AC2 22 TYR A2034 GLY A2061 ILE A2063 GLY A2067
SITE 6 AC2 22 VAL A2068 VAL A2069
SITE 1 AC3 19 PHE B1573 THR B1654 SER B1675 SER B1677
SITE 2 AC3 19 GLY B1678 GLY B1679 VAL B1680 VAL B1699
SITE 3 AC3 19 GLY B1700 LYS B1704 SER B1723 ARG B1724
SITE 4 AC3 19 ILE B1769 LYS B1771 ILE B1794 LEU B1796
SITE 5 AC3 19 ALA B1844 GLY B1846 HIS B1848
SITE 1 AC4 20 GLY B1894 PHE B1896 THR B1915 SER B1916
SITE 2 AC4 20 ARG B1917 SER B1918 ASN B1945 LEU B1971
SITE 3 AC4 20 ALA B1972 MET B1973 LYS B1995 PHE B2019
SITE 4 AC4 20 SER B2020 SER B2021 TYR B2034 GLY B2061
SITE 5 AC4 20 ILE B2063 GLY B2067 VAL B2068 VAL B2069
CRYST1 96.150 244.890 135.370 90.00 101.84 90.00 P 1 21 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 0.010400 0.000000 0.002180 0.00000
SCALE2 0.000000 0.004083 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007548 0.00000
TER 15859 GLU A2113
TER 31759 LYS B2114
MASTER 2197 0 4 171 178 0 21 631949 2 192 388
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