HEADER LYASE 20-OCT-10 3PB2
TITLE CHARACTERISATION OF THE FIRST MONOMERIC DIHYDRODIPICOLINATE SYNTHASE
TITLE 2 VARIANT REVEALS EVOLUTIONARY INSIGHTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDRODIPICOLINATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: DHDPS;
COMPND 5 EC: 4.2.1.52;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TIM-BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.G.PEARCE,R.C.J.DOBSON,G.B.JAMESON
REVDAT 3 20-MAR-24 3PB2 1 REMARK SEQADV
REVDAT 2 28-AUG-13 3PB2 1 JRNL
REVDAT 1 23-NOV-11 3PB2 0
JRNL AUTH F.G.PEARCE,R.C.DOBSON,G.B.JAMESON,M.A.PERUGINI,J.A.GERRARD
JRNL TITL CHARACTERIZATION OF MONOMERIC DIHYDRODIPICOLINATE SYNTHASE
JRNL TITL 2 VARIANT REVEALS THE IMPORTANCE OF SUBSTRATE BINDING IN
JRNL TITL 3 OPTIMIZING OLIGOMERIZATION.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1814 1900 2011
JRNL REFN ISSN 0006-3002
JRNL PMID 21803176
JRNL DOI 10.1016/J.BBAPAP.2011.07.016
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 141790
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 7115
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 33.2637 - 4.0912 1.00 13628 708 0.1565 0.1798
REMARK 3 2 4.0912 - 3.2482 1.00 13560 680 0.1477 0.1806
REMARK 3 3 3.2482 - 2.8378 1.00 13461 735 0.1688 0.2196
REMARK 3 4 2.8378 - 2.5785 1.00 13439 747 0.1612 0.2117
REMARK 3 5 2.5785 - 2.3937 1.00 13412 741 0.1548 0.2089
REMARK 3 6 2.3937 - 2.2526 1.00 13426 699 0.1608 0.2201
REMARK 3 7 2.2526 - 2.1398 1.00 13493 678 0.1727 0.2200
REMARK 3 8 2.1398 - 2.0467 1.00 13420 694 0.1883 0.2433
REMARK 3 9 2.0467 - 1.9679 1.00 13455 691 0.2126 0.2606
REMARK 3 10 1.9679 - 1.9000 1.00 13381 742 0.2353 0.2692
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 : 0.38
REMARK 3 B_SOL : 61.76
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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) : -0.23650
REMARK 3 B22 (A**2) : -0.16590
REMARK 3 B33 (A**2) : 0.40240
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.35800
REMARK 3 B23 (A**2) : 0.00000
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 : 0.007 14088
REMARK 3 ANGLE : 1.012 19126
REMARK 3 CHIRALITY : 0.068 2274
REMARK 3 PLANARITY : 0.005 2467
REMARK 3 DIHEDRAL : 12.903 5317
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 24
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID -5:72)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.1562 -1.5741 -1.4888
REMARK 3 T TENSOR
REMARK 3 T11: 0.1774 T22: 0.1525
REMARK 3 T33: 0.0591 T12: -0.0266
REMARK 3 T13: 0.0177 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.8645 L22: 0.8863
REMARK 3 L33: 0.3627 L12: 0.1380
REMARK 3 L13: 0.2461 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: 0.0368 S12: 0.2675 S13: 0.0917
REMARK 3 S21: -0.2784 S22: -0.0257 S23: 0.0894
REMARK 3 S31: -0.1101 S32: 0.0974 S33: -0.0222
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 73:214)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.0671 -19.2935 4.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1510 T22: 0.1215
REMARK 3 T33: 0.0499 T12: -0.0040
REMARK 3 T13: -0.0089 T23: -0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 0.8566 L22: 0.4889
REMARK 3 L33: 0.5802 L12: 0.1567
REMARK 3 L13: -0.3638 L23: -0.0247
REMARK 3 S TENSOR
REMARK 3 S11: -0.0158 S12: 0.0343 S13: -0.0249
REMARK 3 S21: -0.0943 S22: 0.0191 S23: 0.0103
REMARK 3 S31: 0.0693 S32: 0.1053 S33: -0.0076
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 215:241)
REMARK 3 ORIGIN FOR THE GROUP (A): 50.4574 -12.6504 6.4415
REMARK 3 T TENSOR
REMARK 3 T11: 0.0619 T22: 0.3690
REMARK 3 T33: 0.1158 T12: -0.0159
REMARK 3 T13: 0.0185 T23: -0.1061
REMARK 3 L TENSOR
REMARK 3 L11: 0.1286 L22: 1.6420
REMARK 3 L33: 0.9253 L12: -0.0380
REMARK 3 L13: -0.0817 L23: 0.4496
REMARK 3 S TENSOR
REMARK 3 S11: -0.0727 S12: -0.2209 S13: 0.1324
REMARK 3 S21: -0.0762 S22: 0.2890 S23: -0.4428
REMARK 3 S31: -0.0243 S32: 0.5287 S33: -0.2006
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 242:294)
REMARK 3 ORIGIN FOR THE GROUP (A): 37.0234 2.6907 15.7031
REMARK 3 T TENSOR
REMARK 3 T11: 0.1376 T22: 0.1555
REMARK 3 T33: 0.1130 T12: -0.0680
REMARK 3 T13: 0.0306 T23: -0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 0.3574 L22: 0.2225
REMARK 3 L33: 0.5004 L12: 0.0859
REMARK 3 L13: -0.3015 L23: 0.0723
REMARK 3 S TENSOR
REMARK 3 S11: 0.0990 S12: -0.1788 S13: 0.1700
REMARK 3 S21: 0.0588 S22: 0.0354 S23: 0.0589
REMARK 3 S31: -0.1101 S32: 0.1800 S33: -0.0928
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID -4:58)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8812 -15.2196 19.3656
REMARK 3 T TENSOR
REMARK 3 T11: 0.1109 T22: 0.1372
REMARK 3 T33: 0.1790 T12: 0.0036
REMARK 3 T13: -0.0447 T23: -0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 0.4515 L22: 0.7746
REMARK 3 L33: 0.5916 L12: 0.1473
REMARK 3 L13: 0.0314 L23: 0.0678
REMARK 3 S TENSOR
REMARK 3 S11: -0.0180 S12: 0.0451 S13: 0.2197
REMARK 3 S21: -0.0813 S22: 0.0408 S23: 0.1911
REMARK 3 S31: -0.0985 S32: -0.1623 S33: -0.0014
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 59:125)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9934 -2.6105 20.0007
REMARK 3 T TENSOR
REMARK 3 T11: 0.1360 T22: 0.0908
REMARK 3 T33: 0.1664 T12: 0.0121
REMARK 3 T13: -0.0048 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.7383 L22: 0.8237
REMARK 3 L33: 0.6669 L12: -0.1911
REMARK 3 L13: -0.0441 L23: -0.1628
REMARK 3 S TENSOR
REMARK 3 S11: 0.0909 S12: 0.0744 S13: 0.1463
REMARK 3 S21: -0.0933 S22: 0.0278 S23: 0.2065
REMARK 3 S31: -0.1707 S32: -0.0338 S33: -0.0799
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 126:277)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3685 -16.8818 30.7989
REMARK 3 T TENSOR
REMARK 3 T11: 0.0992 T22: 0.1038
REMARK 3 T33: 0.0913 T12: 0.0087
REMARK 3 T13: -0.0130 T23: -0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 0.6621 L22: 0.6470
REMARK 3 L33: 0.7370 L12: 0.3765
REMARK 3 L13: -0.1496 L23: -0.0655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0473 S12: -0.1020 S13: 0.0222
REMARK 3 S21: 0.0430 S22: -0.0042 S23: 0.0632
REMARK 3 S31: -0.0010 S32: 0.0229 S33: -0.0382
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 278:294)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1328 -37.3889 23.4276
REMARK 3 T TENSOR
REMARK 3 T11: 0.2755 T22: 0.0808
REMARK 3 T33: 0.2091 T12: -0.0448
REMARK 3 T13: -0.0179 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 2.9841 L22: 0.4582
REMARK 3 L33: 2.5043 L12: 0.9561
REMARK 3 L13: -1.9327 L23: -1.0532
REMARK 3 S TENSOR
REMARK 3 S11: -0.3544 S12: 0.0277 S13: -0.8814
REMARK 3 S21: -0.3650 S22: 0.0184 S23: -0.0775
REMARK 3 S31: 0.8499 S32: -0.0065 S33: 0.2481
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID -2:57)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.8685 -26.6062 61.1675
REMARK 3 T TENSOR
REMARK 3 T11: 0.2582 T22: 0.3987
REMARK 3 T33: 0.0413 T12: 0.0621
REMARK 3 T13: -0.0478 T23: 0.0140
REMARK 3 L TENSOR
REMARK 3 L11: 0.6064 L22: 0.7743
REMARK 3 L33: 0.6831 L12: -0.1313
REMARK 3 L13: -0.3614 L23: -0.0133
REMARK 3 S TENSOR
REMARK 3 S11: -0.1273 S12: -0.4016 S13: 0.0192
REMARK 3 S21: 0.3887 S22: 0.0607 S23: -0.1054
REMARK 3 S31: 0.3001 S32: 0.5872 S33: 0.0715
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 58:214)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.9023 -35.2736 49.3033
REMARK 3 T TENSOR
REMARK 3 T11: 0.2295 T22: 0.1574
REMARK 3 T33: 0.0487 T12: 0.0709
REMARK 3 T13: 0.0262 T23: 0.0153
REMARK 3 L TENSOR
REMARK 3 L11: 0.8823 L22: 0.9190
REMARK 3 L33: 1.5734 L12: -0.2668
REMARK 3 L13: -0.5834 L23: 0.0415
REMARK 3 S TENSOR
REMARK 3 S11: -0.1407 S12: -0.1124 S13: -0.1594
REMARK 3 S21: 0.1666 S22: -0.0190 S23: 0.0299
REMARK 3 S31: 0.3661 S32: 0.2443 S33: 0.1446
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 215:245)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.9954 -15.0490 54.6102
REMARK 3 T TENSOR
REMARK 3 T11: 0.3043 T22: 0.1676
REMARK 3 T33: 0.0579 T12: 0.0410
REMARK 3 T13: 0.0113 T23: -0.0141
REMARK 3 L TENSOR
REMARK 3 L11: 0.3213 L22: 0.1328
REMARK 3 L33: 0.1447 L12: 0.0091
REMARK 3 L13: 0.0701 L23: -0.1325
REMARK 3 S TENSOR
REMARK 3 S11: -0.0648 S12: 0.0690 S13: 0.1021
REMARK 3 S21: -0.0126 S22: 0.0460 S23: 0.0475
REMARK 3 S31: -0.2920 S32: -0.1420 S33: 0.0260
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 246:294)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5015 -12.1108 53.3975
REMARK 3 T TENSOR
REMARK 3 T11: 0.2608 T22: 0.3664
REMARK 3 T33: 0.1309 T12: -0.0960
REMARK 3 T13: -0.0304 T23: -0.0565
REMARK 3 L TENSOR
REMARK 3 L11: 0.2398 L22: 0.5854
REMARK 3 L33: 0.8824 L12: -0.0474
REMARK 3 L13: -0.4181 L23: -0.2224
REMARK 3 S TENSOR
REMARK 3 S11: 0.0052 S12: -0.1491 S13: 0.2038
REMARK 3 S21: 0.2693 S22: 0.1100 S23: -0.1236
REMARK 3 S31: -0.2940 S32: 0.6772 S33: -0.0785
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN D AND RESID -1:52)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.7172 21.2833 19.6572
REMARK 3 T TENSOR
REMARK 3 T11: 0.1503 T22: 0.2594
REMARK 3 T33: 0.4597 T12: -0.0337
REMARK 3 T13: 0.0205 T23: -0.1922
REMARK 3 L TENSOR
REMARK 3 L11: 1.0380 L22: 0.5736
REMARK 3 L33: 0.2616 L12: 0.4684
REMARK 3 L13: 0.3877 L23: -0.0330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0158 S12: -0.3531 S13: 0.4412
REMARK 3 S21: 0.0654 S22: -0.2153 S23: 0.2811
REMARK 3 S31: 0.1517 S32: -0.1985 S33: 0.1764
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN D AND RESID 53:76)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.5057 14.6262 16.9399
REMARK 3 T TENSOR
REMARK 3 T11: 0.1987 T22: 0.2271
REMARK 3 T33: 0.3920 T12: -0.0706
REMARK 3 T13: 0.0111 T23: -0.1134
REMARK 3 L TENSOR
REMARK 3 L11: 0.8895 L22: 0.6974
REMARK 3 L33: 0.7337 L12: 0.4522
REMARK 3 L13: 0.0955 L23: -0.5217
REMARK 3 S TENSOR
REMARK 3 S11: 0.1335 S12: -0.2699 S13: -0.1015
REMARK 3 S21: 0.0174 S22: -0.2389 S23: 0.2822
REMARK 3 S31: 0.2758 S32: -0.1864 S33: 0.1223
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN D AND RESID 77:93)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5476 15.6507 0.3822
REMARK 3 T TENSOR
REMARK 3 T11: 0.1663 T22: 0.0729
REMARK 3 T33: 0.4322 T12: -0.0137
REMARK 3 T13: -0.0223 T23: -0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 0.1526 L22: 0.0217
REMARK 3 L33: 0.1147 L12: -0.0273
REMARK 3 L13: 0.1320 L23: -0.0292
REMARK 3 S TENSOR
REMARK 3 S11: 0.1395 S12: -0.0130 S13: -0.0135
REMARK 3 S21: 0.0860 S22: -0.0841 S23: -0.2857
REMARK 3 S31: 0.1236 S32: 0.1386 S33: -0.0670
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID 94:294)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.7790 33.3411 12.3799
REMARK 3 T TENSOR
REMARK 3 T11: 0.0871 T22: 0.1143
REMARK 3 T33: 0.7965 T12: 0.0224
REMARK 3 T13: -0.0604 T23: -0.2987
REMARK 3 L TENSOR
REMARK 3 L11: 2.0698 L22: 0.6240
REMARK 3 L33: 0.8453 L12: 0.1002
REMARK 3 L13: 0.6822 L23: -0.0701
REMARK 3 S TENSOR
REMARK 3 S11: -0.1855 S12: -0.4250 S13: 1.1960
REMARK 3 S21: 0.0518 S22: -0.1569 S23: 0.1345
REMARK 3 S31: -0.1682 S32: -0.1715 S33: 0.3426
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN E AND RESID -1:61)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.4994 -46.2151 30.5238
REMARK 3 T TENSOR
REMARK 3 T11: 0.4952 T22: 0.7700
REMARK 3 T33: 0.3327 T12: 0.5323
REMARK 3 T13: 0.1138 T23: 0.0562
REMARK 3 L TENSOR
REMARK 3 L11: 0.2881 L22: 0.5554
REMARK 3 L33: 0.9661 L12: -0.0756
REMARK 3 L13: -0.0560 L23: 0.0864
REMARK 3 S TENSOR
REMARK 3 S11: -0.2515 S12: -0.3307 S13: -0.3752
REMARK 3 S21: 0.1365 S22: 0.0268 S23: -0.3642
REMARK 3 S31: 0.8387 S32: 1.0833 S33: 0.1137
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN E AND RESID 62:146)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.7680 -30.2125 37.7659
REMARK 3 T TENSOR
REMARK 3 T11: 0.1132 T22: 0.7716
REMARK 3 T33: 0.1840 T12: 0.1920
REMARK 3 T13: -0.0515 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 0.3624 L22: 0.8113
REMARK 3 L33: 1.1773 L12: -0.1728
REMARK 3 L13: -0.5246 L23: 0.3005
REMARK 3 S TENSOR
REMARK 3 S11: -0.0999 S12: -0.3544 S13: -0.0160
REMARK 3 S21: 0.1574 S22: 0.1925 S23: -0.4153
REMARK 3 S31: 0.2665 S32: 1.1691 S33: -0.0846
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN E AND RESID 147:204)
REMARK 3 ORIGIN FOR THE GROUP (A): 52.7381 -23.1650 23.7408
REMARK 3 T TENSOR
REMARK 3 T11: 0.0404 T22: 0.5728
REMARK 3 T33: 0.1467 T12: 0.0187
REMARK 3 T13: 0.0273 T23: -0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 0.2608 L22: 1.0929
REMARK 3 L33: 1.6565 L12: -0.1872
REMARK 3 L13: -0.6162 L23: -0.0237
REMARK 3 S TENSOR
REMARK 3 S11: 0.1749 S12: -0.2496 S13: 0.1266
REMARK 3 S21: -0.1141 S22: -0.0494 S23: -0.3597
REMARK 3 S31: -0.0619 S32: 1.0485 S33: -0.0696
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN E AND RESID 205:294)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.8726 -43.3465 18.3770
REMARK 3 T TENSOR
REMARK 3 T11: 0.4403 T22: 0.3275
REMARK 3 T33: 0.1212 T12: 0.2240
REMARK 3 T13: 0.0946 T23: -0.0695
REMARK 3 L TENSOR
REMARK 3 L11: 0.9450 L22: 1.3351
REMARK 3 L33: 1.2104 L12: -0.1390
REMARK 3 L13: -0.5031 L23: 0.3482
REMARK 3 S TENSOR
REMARK 3 S11: -0.2456 S12: 0.2236 S13: -0.2712
REMARK 3 S21: -0.2827 S22: 0.0057 S23: -0.0933
REMARK 3 S31: 0.7996 S32: 0.3872 S33: 0.1712
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN F AND RESID 1:77)
REMARK 3 ORIGIN FOR THE GROUP (A): 75.9124 14.1501 4.2346
REMARK 3 T TENSOR
REMARK 3 T11: 0.4228 T22: 0.1506
REMARK 3 T33: 2.4444 T12: 0.1741
REMARK 3 T13: -0.5567 T23: -0.3964
REMARK 3 L TENSOR
REMARK 3 L11: 0.5709 L22: 0.1269
REMARK 3 L33: 0.8543 L12: -0.2565
REMARK 3 L13: -0.2268 L23: 0.2198
REMARK 3 S TENSOR
REMARK 3 S11: -0.1587 S12: 0.0861 S13: 0.7243
REMARK 3 S21: -0.1982 S22: -0.2659 S23: 0.2957
REMARK 3 S31: -0.5501 S32: -0.2391 S33: 0.4617
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN F AND RESID 78:96)
REMARK 3 ORIGIN FOR THE GROUP (A): 91.6085 18.3730 10.8169
REMARK 3 T TENSOR
REMARK 3 T11: 0.6828 T22: 0.0310
REMARK 3 T33: 2.1896 T12: 0.0090
REMARK 3 T13: -0.6539 T23: -0.1882
REMARK 3 L TENSOR
REMARK 3 L11: 0.0725 L22: 0.0093
REMARK 3 L33: 0.6260 L12: -0.0139
REMARK 3 L13: 0.0609 L23: 0.0536
REMARK 3 S TENSOR
REMARK 3 S11: -0.0752 S12: 0.0434 S13: -0.1493
REMARK 3 S21: 0.3319 S22: -0.2725 S23: -0.2096
REMARK 3 S31: -0.4758 S32: -0.0499 S33: 0.3382
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN F AND RESID 97:208)
REMARK 3 ORIGIN FOR THE GROUP (A): 88.9707 0.9143 15.3887
REMARK 3 T TENSOR
REMARK 3 T11: 0.3628 T22: 0.1102
REMARK 3 T33: 1.9819 T12: 0.0596
REMARK 3 T13: -0.3688 T23: -0.3968
REMARK 3 L TENSOR
REMARK 3 L11: 0.1703 L22: 0.3151
REMARK 3 L33: 0.8246 L12: -0.1243
REMARK 3 L13: 0.2438 L23: -0.3850
REMARK 3 S TENSOR
REMARK 3 S11: -0.4819 S12: -0.1501 S13: 0.8253
REMARK 3 S21: 0.1520 S22: -0.3318 S23: 0.1650
REMARK 3 S31: -0.2810 S32: -0.1405 S33: 0.7339
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN F AND RESID 209:294)
REMARK 3 ORIGIN FOR THE GROUP (A): 72.1060 -1.5400 -1.9640
REMARK 3 T TENSOR
REMARK 3 T11: 0.2497 T22: 0.2888
REMARK 3 T33: 2.3168 T12: 0.0207
REMARK 3 T13: -0.4209 T23: -0.3925
REMARK 3 L TENSOR
REMARK 3 L11: 0.2474 L22: 0.7680
REMARK 3 L33: 2.7970 L12: -0.2765
REMARK 3 L13: -0.0857 L23: -0.4847
REMARK 3 S TENSOR
REMARK 3 S11: -0.4149 S12: 0.0633 S13: 0.7747
REMARK 3 S21: -0.1546 S22: -0.2747 S23: 0.8532
REMARK 3 S31: -0.0704 S32: -0.7995 S33: 0.7640
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PB2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-10.
REMARK 100 THE DEPOSITION ID IS D_1000062174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95661
REMARK 200 MONOCHROMATOR : YALE MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 143667
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 33.259
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% V/V PEG 300, 100MM PHOSPHATE
REMARK 280 -CITRATE BUFFER, PH 4.2, 0.02% (W/V) SODIUM AZIDE, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 96.10000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.67100
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 96.10000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 62.67100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 741 LIES ON A SPECIAL POSITION.
REMARK 375 HOH D 854 LIES ON A SPECIAL POSITION.
REMARK 375 HOH F 843 LIES ON A SPECIAL POSITION.
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 GLY B -5
REMARK 465 ILE B -4
REMARK 465 GLY C -5
REMARK 465 ILE C -4
REMARK 465 ASP C -3
REMARK 465 GLY D -5
REMARK 465 ILE D -4
REMARK 465 GLY E -5
REMARK 465 ILE E -4
REMARK 465 ASP E -3
REMARK 465 PRO E -2
REMARK 465 GLY F -5
REMARK 465 ILE F -4
REMARK 465 ASP F -3
REMARK 465 PRO F -2
REMARK 465 PHE F -1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLU B 230 CD OE1 OE2
REMARK 470 GLU B 282 CD OE1 OE2
REMARK 470 GLU C 278 CG CD OE1 OE2
REMARK 470 GLU C 290 CG CD OE1 OE2
REMARK 470 GLU D 230 CG CD OE1 OE2
REMARK 470 GLU E 278 CG CD OE1 OE2
REMARK 470 LYS F 14 CG CD CE NZ
REMARK 470 ASN F 228 CG OD1 ND2
REMARK 470 LYS F 231 CG CD CE NZ
REMARK 470 LYS F 238 CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O1 GOL A 296 O HOH B 487 2555 2.09
REMARK 500
REMARK 500 REMARK: NULL
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
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 ALA A 76 56.72 -155.15
REMARK 500 THR A 78 -167.94 -121.75
REMARK 500 TYR A 106 -46.39 77.30
REMARK 500 VAL A 134 73.94 -150.22
REMARK 500 ASN A 228 74.85 -100.24
REMARK 500 ALA B 76 50.49 -154.91
REMARK 500 TYR B 106 -39.82 76.29
REMARK 500 VAL B 134 72.37 -151.16
REMARK 500 ASN B 228 67.92 -113.20
REMARK 500 PRO B 252 30.76 -98.27
REMARK 500 ASP C 19 78.96 -111.37
REMARK 500 ALA C 76 50.26 -143.40
REMARK 500 TYR C 106 -45.82 77.77
REMARK 500 VAL C 134 68.82 -150.83
REMARK 500 ASN C 228 73.89 -108.25
REMARK 500 ASP D 67 47.31 33.33
REMARK 500 ALA D 76 42.50 -151.75
REMARK 500 TYR D 106 -42.09 75.22
REMARK 500 VAL D 134 72.23 -150.52
REMARK 500 ASP E 19 79.26 -101.17
REMARK 500 PRO E 104 120.80 -39.63
REMARK 500 TYR E 106 -45.48 76.91
REMARK 500 VAL E 134 70.90 -153.25
REMARK 500 ASN E 228 74.56 -103.90
REMARK 500 ASN E 228 73.09 -102.84
REMARK 500 MET F 1 -153.48 -74.63
REMARK 500 MET F 1 -150.04 -79.72
REMARK 500 ALA F 76 68.44 -153.73
REMARK 500 TYR F 106 -39.20 79.64
REMARK 500 SER F 210 -36.09 -38.97
REMARK 500 PRO F 214 -72.02 -48.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 299
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 295
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 296
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 297
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 298
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 295
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PB0 RELATED DB: PDB
DBREF 3PB2 A 1 294 UNP Q9X1K9 DAPA_THEMA 1 294
DBREF 3PB2 B 1 294 UNP Q9X1K9 DAPA_THEMA 1 294
DBREF 3PB2 C 1 294 UNP Q9X1K9 DAPA_THEMA 1 294
DBREF 3PB2 D 1 294 UNP Q9X1K9 DAPA_THEMA 1 294
DBREF 3PB2 E 1 294 UNP Q9X1K9 DAPA_THEMA 1 294
DBREF 3PB2 F 1 294 UNP Q9X1K9 DAPA_THEMA 1 294
SEQADV 3PB2 GLY A -5 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ILE A -4 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ASP A -3 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PRO A -2 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PHE A -1 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 THR A 0 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ALA A 233 UNP Q9X1K9 ARG 233 ENGINEERED MUTATION
SEQADV 3PB2 ALA A 237 UNP Q9X1K9 ARG 237 ENGINEERED MUTATION
SEQADV 3PB2 GLY B -5 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ILE B -4 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ASP B -3 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PRO B -2 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PHE B -1 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 THR B 0 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ALA B 233 UNP Q9X1K9 ARG 233 ENGINEERED MUTATION
SEQADV 3PB2 ALA B 237 UNP Q9X1K9 ARG 237 ENGINEERED MUTATION
SEQADV 3PB2 GLY C -5 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ILE C -4 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ASP C -3 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PRO C -2 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PHE C -1 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 THR C 0 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ALA C 233 UNP Q9X1K9 ARG 233 ENGINEERED MUTATION
SEQADV 3PB2 ALA C 237 UNP Q9X1K9 ARG 237 ENGINEERED MUTATION
SEQADV 3PB2 GLY D -5 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ILE D -4 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ASP D -3 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PRO D -2 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PHE D -1 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 THR D 0 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ALA D 233 UNP Q9X1K9 ARG 233 ENGINEERED MUTATION
SEQADV 3PB2 ALA D 237 UNP Q9X1K9 ARG 237 ENGINEERED MUTATION
SEQADV 3PB2 GLY E -5 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ILE E -4 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ASP E -3 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PRO E -2 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PHE E -1 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 THR E 0 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ALA E 233 UNP Q9X1K9 ARG 233 ENGINEERED MUTATION
SEQADV 3PB2 ALA E 237 UNP Q9X1K9 ARG 237 ENGINEERED MUTATION
SEQADV 3PB2 GLY F -5 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ILE F -4 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ASP F -3 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PRO F -2 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 PHE F -1 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 THR F 0 UNP Q9X1K9 EXPRESSION TAG
SEQADV 3PB2 ALA F 233 UNP Q9X1K9 ARG 233 ENGINEERED MUTATION
SEQADV 3PB2 ALA F 237 UNP Q9X1K9 ARG 237 ENGINEERED MUTATION
SEQRES 1 A 300 GLY ILE ASP PRO PHE THR MET PHE ARG GLY VAL GLY THR
SEQRES 2 A 300 ALA ILE VAL THR PRO PHE LYS ASN GLY GLU LEU ASP LEU
SEQRES 3 A 300 GLU SER TYR GLU ARG LEU VAL ARG TYR GLN LEU GLU ASN
SEQRES 4 A 300 GLY VAL ASN ALA LEU ILE VAL LEU GLY THR THR GLY GLU
SEQRES 5 A 300 SER PRO THR VAL ASN GLU ASP GLU ARG GLU LYS LEU VAL
SEQRES 6 A 300 SER ARG THR LEU GLU ILE VAL ASP GLY LYS ILE PRO VAL
SEQRES 7 A 300 ILE VAL GLY ALA GLY THR ASN SER THR GLU LYS THR LEU
SEQRES 8 A 300 LYS LEU VAL LYS GLN ALA GLU LYS LEU GLY ALA ASN GLY
SEQRES 9 A 300 VAL LEU VAL VAL THR PRO TYR TYR ASN LYS PRO THR GLN
SEQRES 10 A 300 GLU GLY LEU TYR GLN HIS TYR LYS TYR ILE SER GLU ARG
SEQRES 11 A 300 THR ASP LEU GLY ILE VAL VAL TYR ASN VAL PRO GLY ARG
SEQRES 12 A 300 THR GLY VAL ASN VAL LEU PRO GLU THR ALA ALA ARG ILE
SEQRES 13 A 300 ALA ALA ASP LEU LYS ASN VAL VAL GLY ILE LYS GLU ALA
SEQRES 14 A 300 ASN PRO ASP ILE ASP GLN ILE ASP ARG THR VAL SER LEU
SEQRES 15 A 300 THR LYS GLN ALA ARG SER ASP PHE MET VAL TRP SER GLY
SEQRES 16 A 300 ASN ASP ASP ARG THR PHE TYR LEU LEU CYS ALA GLY GLY
SEQRES 17 A 300 ASP GLY VAL ILE SER VAL VAL SER ASN VAL ALA PRO LYS
SEQRES 18 A 300 GLN MET VAL GLU LEU CYS ALA GLU TYR PHE SER GLY ASN
SEQRES 19 A 300 LEU GLU LYS SER ALA GLU VAL HIS ALA LYS LEU ARG PRO
SEQRES 20 A 300 LEU MET LYS ALA LEU PHE VAL GLU THR ASN PRO ILE PRO
SEQRES 21 A 300 VAL LYS ALA ALA LEU ASN LEU MET GLY PHE ILE GLU ASN
SEQRES 22 A 300 GLU LEU ARG LEU PRO LEU VAL PRO ALA SER GLU LYS THR
SEQRES 23 A 300 VAL GLU LEU LEU ARG ASN VAL LEU LYS GLU SER GLY LEU
SEQRES 24 A 300 LEU
SEQRES 1 B 300 GLY ILE ASP PRO PHE THR MET PHE ARG GLY VAL GLY THR
SEQRES 2 B 300 ALA ILE VAL THR PRO PHE LYS ASN GLY GLU LEU ASP LEU
SEQRES 3 B 300 GLU SER TYR GLU ARG LEU VAL ARG TYR GLN LEU GLU ASN
SEQRES 4 B 300 GLY VAL ASN ALA LEU ILE VAL LEU GLY THR THR GLY GLU
SEQRES 5 B 300 SER PRO THR VAL ASN GLU ASP GLU ARG GLU LYS LEU VAL
SEQRES 6 B 300 SER ARG THR LEU GLU ILE VAL ASP GLY LYS ILE PRO VAL
SEQRES 7 B 300 ILE VAL GLY ALA GLY THR ASN SER THR GLU LYS THR LEU
SEQRES 8 B 300 LYS LEU VAL LYS GLN ALA GLU LYS LEU GLY ALA ASN GLY
SEQRES 9 B 300 VAL LEU VAL VAL THR PRO TYR TYR ASN LYS PRO THR GLN
SEQRES 10 B 300 GLU GLY LEU TYR GLN HIS TYR LYS TYR ILE SER GLU ARG
SEQRES 11 B 300 THR ASP LEU GLY ILE VAL VAL TYR ASN VAL PRO GLY ARG
SEQRES 12 B 300 THR GLY VAL ASN VAL LEU PRO GLU THR ALA ALA ARG ILE
SEQRES 13 B 300 ALA ALA ASP LEU LYS ASN VAL VAL GLY ILE LYS GLU ALA
SEQRES 14 B 300 ASN PRO ASP ILE ASP GLN ILE ASP ARG THR VAL SER LEU
SEQRES 15 B 300 THR LYS GLN ALA ARG SER ASP PHE MET VAL TRP SER GLY
SEQRES 16 B 300 ASN ASP ASP ARG THR PHE TYR LEU LEU CYS ALA GLY GLY
SEQRES 17 B 300 ASP GLY VAL ILE SER VAL VAL SER ASN VAL ALA PRO LYS
SEQRES 18 B 300 GLN MET VAL GLU LEU CYS ALA GLU TYR PHE SER GLY ASN
SEQRES 19 B 300 LEU GLU LYS SER ALA GLU VAL HIS ALA LYS LEU ARG PRO
SEQRES 20 B 300 LEU MET LYS ALA LEU PHE VAL GLU THR ASN PRO ILE PRO
SEQRES 21 B 300 VAL LYS ALA ALA LEU ASN LEU MET GLY PHE ILE GLU ASN
SEQRES 22 B 300 GLU LEU ARG LEU PRO LEU VAL PRO ALA SER GLU LYS THR
SEQRES 23 B 300 VAL GLU LEU LEU ARG ASN VAL LEU LYS GLU SER GLY LEU
SEQRES 24 B 300 LEU
SEQRES 1 C 300 GLY ILE ASP PRO PHE THR MET PHE ARG GLY VAL GLY THR
SEQRES 2 C 300 ALA ILE VAL THR PRO PHE LYS ASN GLY GLU LEU ASP LEU
SEQRES 3 C 300 GLU SER TYR GLU ARG LEU VAL ARG TYR GLN LEU GLU ASN
SEQRES 4 C 300 GLY VAL ASN ALA LEU ILE VAL LEU GLY THR THR GLY GLU
SEQRES 5 C 300 SER PRO THR VAL ASN GLU ASP GLU ARG GLU LYS LEU VAL
SEQRES 6 C 300 SER ARG THR LEU GLU ILE VAL ASP GLY LYS ILE PRO VAL
SEQRES 7 C 300 ILE VAL GLY ALA GLY THR ASN SER THR GLU LYS THR LEU
SEQRES 8 C 300 LYS LEU VAL LYS GLN ALA GLU LYS LEU GLY ALA ASN GLY
SEQRES 9 C 300 VAL LEU VAL VAL THR PRO TYR TYR ASN LYS PRO THR GLN
SEQRES 10 C 300 GLU GLY LEU TYR GLN HIS TYR LYS TYR ILE SER GLU ARG
SEQRES 11 C 300 THR ASP LEU GLY ILE VAL VAL TYR ASN VAL PRO GLY ARG
SEQRES 12 C 300 THR GLY VAL ASN VAL LEU PRO GLU THR ALA ALA ARG ILE
SEQRES 13 C 300 ALA ALA ASP LEU LYS ASN VAL VAL GLY ILE LYS GLU ALA
SEQRES 14 C 300 ASN PRO ASP ILE ASP GLN ILE ASP ARG THR VAL SER LEU
SEQRES 15 C 300 THR LYS GLN ALA ARG SER ASP PHE MET VAL TRP SER GLY
SEQRES 16 C 300 ASN ASP ASP ARG THR PHE TYR LEU LEU CYS ALA GLY GLY
SEQRES 17 C 300 ASP GLY VAL ILE SER VAL VAL SER ASN VAL ALA PRO LYS
SEQRES 18 C 300 GLN MET VAL GLU LEU CYS ALA GLU TYR PHE SER GLY ASN
SEQRES 19 C 300 LEU GLU LYS SER ALA GLU VAL HIS ALA LYS LEU ARG PRO
SEQRES 20 C 300 LEU MET LYS ALA LEU PHE VAL GLU THR ASN PRO ILE PRO
SEQRES 21 C 300 VAL LYS ALA ALA LEU ASN LEU MET GLY PHE ILE GLU ASN
SEQRES 22 C 300 GLU LEU ARG LEU PRO LEU VAL PRO ALA SER GLU LYS THR
SEQRES 23 C 300 VAL GLU LEU LEU ARG ASN VAL LEU LYS GLU SER GLY LEU
SEQRES 24 C 300 LEU
SEQRES 1 D 300 GLY ILE ASP PRO PHE THR MET PHE ARG GLY VAL GLY THR
SEQRES 2 D 300 ALA ILE VAL THR PRO PHE LYS ASN GLY GLU LEU ASP LEU
SEQRES 3 D 300 GLU SER TYR GLU ARG LEU VAL ARG TYR GLN LEU GLU ASN
SEQRES 4 D 300 GLY VAL ASN ALA LEU ILE VAL LEU GLY THR THR GLY GLU
SEQRES 5 D 300 SER PRO THR VAL ASN GLU ASP GLU ARG GLU LYS LEU VAL
SEQRES 6 D 300 SER ARG THR LEU GLU ILE VAL ASP GLY LYS ILE PRO VAL
SEQRES 7 D 300 ILE VAL GLY ALA GLY THR ASN SER THR GLU LYS THR LEU
SEQRES 8 D 300 LYS LEU VAL LYS GLN ALA GLU LYS LEU GLY ALA ASN GLY
SEQRES 9 D 300 VAL LEU VAL VAL THR PRO TYR TYR ASN LYS PRO THR GLN
SEQRES 10 D 300 GLU GLY LEU TYR GLN HIS TYR LYS TYR ILE SER GLU ARG
SEQRES 11 D 300 THR ASP LEU GLY ILE VAL VAL TYR ASN VAL PRO GLY ARG
SEQRES 12 D 300 THR GLY VAL ASN VAL LEU PRO GLU THR ALA ALA ARG ILE
SEQRES 13 D 300 ALA ALA ASP LEU LYS ASN VAL VAL GLY ILE LYS GLU ALA
SEQRES 14 D 300 ASN PRO ASP ILE ASP GLN ILE ASP ARG THR VAL SER LEU
SEQRES 15 D 300 THR LYS GLN ALA ARG SER ASP PHE MET VAL TRP SER GLY
SEQRES 16 D 300 ASN ASP ASP ARG THR PHE TYR LEU LEU CYS ALA GLY GLY
SEQRES 17 D 300 ASP GLY VAL ILE SER VAL VAL SER ASN VAL ALA PRO LYS
SEQRES 18 D 300 GLN MET VAL GLU LEU CYS ALA GLU TYR PHE SER GLY ASN
SEQRES 19 D 300 LEU GLU LYS SER ALA GLU VAL HIS ALA LYS LEU ARG PRO
SEQRES 20 D 300 LEU MET LYS ALA LEU PHE VAL GLU THR ASN PRO ILE PRO
SEQRES 21 D 300 VAL LYS ALA ALA LEU ASN LEU MET GLY PHE ILE GLU ASN
SEQRES 22 D 300 GLU LEU ARG LEU PRO LEU VAL PRO ALA SER GLU LYS THR
SEQRES 23 D 300 VAL GLU LEU LEU ARG ASN VAL LEU LYS GLU SER GLY LEU
SEQRES 24 D 300 LEU
SEQRES 1 E 300 GLY ILE ASP PRO PHE THR MET PHE ARG GLY VAL GLY THR
SEQRES 2 E 300 ALA ILE VAL THR PRO PHE LYS ASN GLY GLU LEU ASP LEU
SEQRES 3 E 300 GLU SER TYR GLU ARG LEU VAL ARG TYR GLN LEU GLU ASN
SEQRES 4 E 300 GLY VAL ASN ALA LEU ILE VAL LEU GLY THR THR GLY GLU
SEQRES 5 E 300 SER PRO THR VAL ASN GLU ASP GLU ARG GLU LYS LEU VAL
SEQRES 6 E 300 SER ARG THR LEU GLU ILE VAL ASP GLY LYS ILE PRO VAL
SEQRES 7 E 300 ILE VAL GLY ALA GLY THR ASN SER THR GLU LYS THR LEU
SEQRES 8 E 300 LYS LEU VAL LYS GLN ALA GLU LYS LEU GLY ALA ASN GLY
SEQRES 9 E 300 VAL LEU VAL VAL THR PRO TYR TYR ASN LYS PRO THR GLN
SEQRES 10 E 300 GLU GLY LEU TYR GLN HIS TYR LYS TYR ILE SER GLU ARG
SEQRES 11 E 300 THR ASP LEU GLY ILE VAL VAL TYR ASN VAL PRO GLY ARG
SEQRES 12 E 300 THR GLY VAL ASN VAL LEU PRO GLU THR ALA ALA ARG ILE
SEQRES 13 E 300 ALA ALA ASP LEU LYS ASN VAL VAL GLY ILE LYS GLU ALA
SEQRES 14 E 300 ASN PRO ASP ILE ASP GLN ILE ASP ARG THR VAL SER LEU
SEQRES 15 E 300 THR LYS GLN ALA ARG SER ASP PHE MET VAL TRP SER GLY
SEQRES 16 E 300 ASN ASP ASP ARG THR PHE TYR LEU LEU CYS ALA GLY GLY
SEQRES 17 E 300 ASP GLY VAL ILE SER VAL VAL SER ASN VAL ALA PRO LYS
SEQRES 18 E 300 GLN MET VAL GLU LEU CYS ALA GLU TYR PHE SER GLY ASN
SEQRES 19 E 300 LEU GLU LYS SER ALA GLU VAL HIS ALA LYS LEU ARG PRO
SEQRES 20 E 300 LEU MET LYS ALA LEU PHE VAL GLU THR ASN PRO ILE PRO
SEQRES 21 E 300 VAL LYS ALA ALA LEU ASN LEU MET GLY PHE ILE GLU ASN
SEQRES 22 E 300 GLU LEU ARG LEU PRO LEU VAL PRO ALA SER GLU LYS THR
SEQRES 23 E 300 VAL GLU LEU LEU ARG ASN VAL LEU LYS GLU SER GLY LEU
SEQRES 24 E 300 LEU
SEQRES 1 F 300 GLY ILE ASP PRO PHE THR MET PHE ARG GLY VAL GLY THR
SEQRES 2 F 300 ALA ILE VAL THR PRO PHE LYS ASN GLY GLU LEU ASP LEU
SEQRES 3 F 300 GLU SER TYR GLU ARG LEU VAL ARG TYR GLN LEU GLU ASN
SEQRES 4 F 300 GLY VAL ASN ALA LEU ILE VAL LEU GLY THR THR GLY GLU
SEQRES 5 F 300 SER PRO THR VAL ASN GLU ASP GLU ARG GLU LYS LEU VAL
SEQRES 6 F 300 SER ARG THR LEU GLU ILE VAL ASP GLY LYS ILE PRO VAL
SEQRES 7 F 300 ILE VAL GLY ALA GLY THR ASN SER THR GLU LYS THR LEU
SEQRES 8 F 300 LYS LEU VAL LYS GLN ALA GLU LYS LEU GLY ALA ASN GLY
SEQRES 9 F 300 VAL LEU VAL VAL THR PRO TYR TYR ASN LYS PRO THR GLN
SEQRES 10 F 300 GLU GLY LEU TYR GLN HIS TYR LYS TYR ILE SER GLU ARG
SEQRES 11 F 300 THR ASP LEU GLY ILE VAL VAL TYR ASN VAL PRO GLY ARG
SEQRES 12 F 300 THR GLY VAL ASN VAL LEU PRO GLU THR ALA ALA ARG ILE
SEQRES 13 F 300 ALA ALA ASP LEU LYS ASN VAL VAL GLY ILE LYS GLU ALA
SEQRES 14 F 300 ASN PRO ASP ILE ASP GLN ILE ASP ARG THR VAL SER LEU
SEQRES 15 F 300 THR LYS GLN ALA ARG SER ASP PHE MET VAL TRP SER GLY
SEQRES 16 F 300 ASN ASP ASP ARG THR PHE TYR LEU LEU CYS ALA GLY GLY
SEQRES 17 F 300 ASP GLY VAL ILE SER VAL VAL SER ASN VAL ALA PRO LYS
SEQRES 18 F 300 GLN MET VAL GLU LEU CYS ALA GLU TYR PHE SER GLY ASN
SEQRES 19 F 300 LEU GLU LYS SER ALA GLU VAL HIS ALA LYS LEU ARG PRO
SEQRES 20 F 300 LEU MET LYS ALA LEU PHE VAL GLU THR ASN PRO ILE PRO
SEQRES 21 F 300 VAL LYS ALA ALA LEU ASN LEU MET GLY PHE ILE GLU ASN
SEQRES 22 F 300 GLU LEU ARG LEU PRO LEU VAL PRO ALA SER GLU LYS THR
SEQRES 23 F 300 VAL GLU LEU LEU ARG ASN VAL LEU LYS GLU SER GLY LEU
SEQRES 24 F 300 LEU
HET GOL A 295 6
HET GOL A 296 6
HET GOL A 297 6
HET GOL A 298 6
HET GOL A 299 6
HET GOL A 300 6
HET GOL B 295 6
HET GOL B 296 6
HET GOL B 297 6
HET GOL B 298 6
HET GOL C 295 6
HET GOL C 296 6
HET GOL C 297 6
HET GOL C 298 6
HET GOL D 295 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 15(C3 H8 O3)
FORMUL 22 HOH *1073(H2 O)
HELIX 1 1 ASP A -3 MET A 1 5 5
HELIX 2 2 ASP A 19 GLU A 32 1 14
HELIX 3 3 GLU A 46 VAL A 50 5 5
HELIX 4 4 ASN A 51 ASP A 67 1 17
HELIX 5 5 SER A 80 GLY A 95 1 16
HELIX 6 6 THR A 110 GLU A 123 1 14
HELIX 7 7 VAL A 134 GLY A 139 1 6
HELIX 8 8 LEU A 143 LEU A 154 1 12
HELIX 9 9 ASP A 166 ARG A 181 1 16
HELIX 10 10 ASN A 190 ASP A 192 5 3
HELIX 11 11 ARG A 193 ALA A 200 1 8
HELIX 12 12 VAL A 208 VAL A 212 5 5
HELIX 13 13 ALA A 213 SER A 226 1 14
HELIX 14 14 ASN A 228 LEU A 246 1 19
HELIX 15 15 PRO A 252 MET A 262 1 11
HELIX 16 16 SER A 277 SER A 291 1 15
HELIX 17 17 ASP B -3 MET B 1 5 5
HELIX 18 18 ASP B 19 ASN B 33 1 15
HELIX 19 19 GLY B 42 VAL B 50 5 9
HELIX 20 20 ASN B 51 ASP B 67 1 17
HELIX 21 21 SER B 80 GLY B 95 1 16
HELIX 22 22 THR B 110 GLU B 123 1 14
HELIX 23 23 VAL B 134 GLY B 139 1 6
HELIX 24 24 LEU B 143 LEU B 154 1 12
HELIX 25 25 ASP B 166 ARG B 181 1 16
HELIX 26 26 ASN B 190 ASP B 192 5 3
HELIX 27 27 ARG B 193 ALA B 200 1 8
HELIX 28 28 VAL B 208 VAL B 212 5 5
HELIX 29 29 ALA B 213 SER B 226 1 14
HELIX 30 30 ASN B 228 LEU B 246 1 19
HELIX 31 31 PRO B 252 MET B 262 1 11
HELIX 32 32 SER B 277 SER B 291 1 15
HELIX 33 33 ASP C 19 ASN C 33 1 15
HELIX 34 34 GLY C 42 VAL C 50 5 9
HELIX 35 35 ASN C 51 ASP C 67 1 17
HELIX 36 36 SER C 80 GLY C 95 1 16
HELIX 37 37 THR C 110 GLU C 123 1 14
HELIX 38 38 VAL C 134 GLY C 139 1 6
HELIX 39 39 LEU C 143 LEU C 154 1 12
HELIX 40 40 ASP C 166 ARG C 181 1 16
HELIX 41 41 ASN C 190 ASP C 192 5 3
HELIX 42 42 ARG C 193 GLY C 201 1 9
HELIX 43 43 VAL C 208 VAL C 212 5 5
HELIX 44 44 ALA C 213 SER C 226 1 14
HELIX 45 45 ASN C 228 LEU C 246 1 19
HELIX 46 46 PRO C 252 MET C 262 1 11
HELIX 47 47 SER C 277 SER C 291 1 15
HELIX 48 48 ASP D -3 MET D 1 5 5
HELIX 49 49 ASP D 19 ASN D 33 1 15
HELIX 50 50 GLY D 42 VAL D 50 5 9
HELIX 51 51 ASN D 51 ASP D 67 1 17
HELIX 52 52 SER D 80 GLY D 95 1 16
HELIX 53 53 THR D 110 GLU D 123 1 14
HELIX 54 54 VAL D 134 GLY D 139 1 6
HELIX 55 55 LEU D 143 LEU D 154 1 12
HELIX 56 56 ASP D 166 ARG D 181 1 16
HELIX 57 57 ASN D 190 ASP D 192 5 3
HELIX 58 58 ARG D 193 ALA D 200 1 8
HELIX 59 59 VAL D 208 VAL D 212 5 5
HELIX 60 60 ALA D 213 GLY D 227 1 15
HELIX 61 61 ASN D 228 LEU D 246 1 19
HELIX 62 62 PRO D 252 MET D 262 1 11
HELIX 63 63 SER D 277 SER D 291 1 15
HELIX 64 64 ASP E 19 ASN E 33 1 15
HELIX 65 65 GLU E 46 VAL E 50 5 5
HELIX 66 66 ASN E 51 ASP E 67 1 17
HELIX 67 67 SER E 80 GLY E 95 1 16
HELIX 68 68 THR E 110 GLU E 123 1 14
HELIX 69 69 VAL E 134 GLY E 139 1 6
HELIX 70 70 LEU E 143 LEU E 154 1 12
HELIX 71 71 ASP E 166 ARG E 181 1 16
HELIX 72 72 ASN E 190 ASP E 192 5 3
HELIX 73 73 ARG E 193 ALA E 200 1 8
HELIX 74 74 VAL E 208 VAL E 212 5 5
HELIX 75 75 ALA E 213 GLY E 227 1 15
HELIX 76 76 ASN E 228 LEU E 246 1 19
HELIX 77 77 PRO E 252 MET E 262 1 11
HELIX 78 78 SER E 277 SER E 291 1 15
HELIX 79 79 ASP F 19 ASN F 33 1 15
HELIX 80 80 GLY F 42 VAL F 50 5 9
HELIX 81 81 ASN F 51 ASP F 67 1 17
HELIX 82 82 SER F 80 LEU F 94 1 15
HELIX 83 83 THR F 110 GLU F 123 1 14
HELIX 84 84 VAL F 134 GLY F 139 1 6
HELIX 85 85 LEU F 143 LEU F 154 1 12
HELIX 86 86 ASP F 166 ARG F 181 1 16
HELIX 87 87 ASN F 190 ASP F 192 5 3
HELIX 88 88 ARG F 193 ALA F 200 1 8
HELIX 89 89 VAL F 208 VAL F 212 5 5
HELIX 90 90 ALA F 213 SER F 226 1 14
HELIX 91 91 ASN F 228 LEU F 246 1 19
HELIX 92 92 PRO F 252 MET F 262 1 11
HELIX 93 93 SER F 277 GLY F 292 1 16
SHEET 1 A 9 GLY A 4 ALA A 8 0
SHEET 2 A 9 ALA A 37 VAL A 40 1 O ILE A 39 N THR A 7
SHEET 3 A 9 VAL A 72 GLY A 75 1 O GLY A 75 N VAL A 40
SHEET 4 A 9 GLY A 98 VAL A 102 1 O GLY A 98 N VAL A 74
SHEET 5 A 9 GLY A 128 ASN A 133 1 O VAL A 130 N VAL A 99
SHEET 6 A 9 VAL A 157 GLU A 162 1 O LYS A 161 N VAL A 131
SHEET 7 A 9 MET A 185 SER A 188 1 O TRP A 187 N GLU A 162
SHEET 8 A 9 GLY A 204 SER A 207 1 O GLY A 204 N SER A 188
SHEET 9 A 9 GLY A 4 ALA A 8 1 N GLY A 6 O VAL A 205
SHEET 1 B 2 PHE A 13 LYS A 14 0
SHEET 2 B 2 GLU A 17 LEU A 18 -1 O GLU A 17 N LYS A 14
SHEET 1 C 9 GLY B 4 ALA B 8 0
SHEET 2 C 9 ALA B 37 VAL B 40 1 O ILE B 39 N THR B 7
SHEET 3 C 9 VAL B 72 GLY B 75 1 O ILE B 73 N LEU B 38
SHEET 4 C 9 GLY B 98 VAL B 102 1 O GLY B 98 N VAL B 74
SHEET 5 C 9 GLY B 128 ASN B 133 1 O VAL B 130 N VAL B 101
SHEET 6 C 9 VAL B 157 GLU B 162 1 O LYS B 161 N VAL B 131
SHEET 7 C 9 MET B 185 SER B 188 1 O TRP B 187 N GLU B 162
SHEET 8 C 9 GLY B 204 SER B 207 1 O GLY B 204 N SER B 188
SHEET 9 C 9 GLY B 4 ALA B 8 1 N GLY B 6 O VAL B 205
SHEET 1 D 2 PHE B 13 LYS B 14 0
SHEET 2 D 2 GLU B 17 LEU B 18 -1 O GLU B 17 N LYS B 14
SHEET 1 E 9 GLY C 4 ALA C 8 0
SHEET 2 E 9 ALA C 37 VAL C 40 1 O ILE C 39 N THR C 7
SHEET 3 E 9 VAL C 72 GLY C 75 1 O GLY C 75 N VAL C 40
SHEET 4 E 9 GLY C 98 VAL C 102 1 O GLY C 98 N VAL C 74
SHEET 5 E 9 GLY C 128 ASN C 133 1 O VAL C 130 N VAL C 101
SHEET 6 E 9 VAL C 157 GLU C 162 1 O LYS C 161 N VAL C 131
SHEET 7 E 9 MET C 185 SER C 188 1 O TRP C 187 N GLU C 162
SHEET 8 E 9 GLY C 204 SER C 207 1 O ILE C 206 N SER C 188
SHEET 9 E 9 GLY C 4 ALA C 8 1 N GLY C 6 O VAL C 205
SHEET 1 F 2 PHE C 13 LYS C 14 0
SHEET 2 F 2 GLU C 17 LEU C 18 -1 O GLU C 17 N LYS C 14
SHEET 1 G 9 GLY D 4 ALA D 8 0
SHEET 2 G 9 ALA D 37 VAL D 40 1 O ILE D 39 N THR D 7
SHEET 3 G 9 VAL D 72 GLY D 75 1 O ILE D 73 N LEU D 38
SHEET 4 G 9 GLY D 98 VAL D 102 1 O GLY D 98 N VAL D 74
SHEET 5 G 9 GLY D 128 ASN D 133 1 O VAL D 130 N VAL D 101
SHEET 6 G 9 VAL D 157 GLU D 162 1 O LYS D 161 N VAL D 131
SHEET 7 G 9 MET D 185 SER D 188 1 O MET D 185 N VAL D 158
SHEET 8 G 9 GLY D 204 SER D 207 1 O GLY D 204 N SER D 188
SHEET 9 G 9 GLY D 4 ALA D 8 1 N GLY D 6 O VAL D 205
SHEET 1 H 2 PHE D 13 LYS D 14 0
SHEET 2 H 2 GLU D 17 LEU D 18 -1 O GLU D 17 N LYS D 14
SHEET 1 I 9 GLY E 4 ALA E 8 0
SHEET 2 I 9 ALA E 37 VAL E 40 1 O ILE E 39 N THR E 7
SHEET 3 I 9 VAL E 72 GLY E 75 1 O GLY E 75 N VAL E 40
SHEET 4 I 9 GLY E 98 VAL E 102 1 O GLY E 98 N VAL E 74
SHEET 5 I 9 GLY E 128 ASN E 133 1 O VAL E 130 N VAL E 99
SHEET 6 I 9 VAL E 157 GLU E 162 1 O LYS E 161 N VAL E 131
SHEET 7 I 9 MET E 185 SER E 188 1 O TRP E 187 N GLU E 162
SHEET 8 I 9 GLY E 204 SER E 207 1 O ILE E 206 N SER E 188
SHEET 9 I 9 GLY E 4 ALA E 8 1 N GLY E 6 O VAL E 205
SHEET 1 J 2 PHE E 13 LYS E 14 0
SHEET 2 J 2 GLU E 17 LEU E 18 -1 O GLU E 17 N LYS E 14
SHEET 1 K 9 GLY F 4 ALA F 8 0
SHEET 2 K 9 ALA F 37 VAL F 40 1 O ILE F 39 N THR F 7
SHEET 3 K 9 VAL F 72 GLY F 75 1 O GLY F 75 N VAL F 40
SHEET 4 K 9 GLY F 98 VAL F 102 1 O GLY F 98 N VAL F 74
SHEET 5 K 9 GLY F 128 ASN F 133 1 O VAL F 130 N VAL F 99
SHEET 6 K 9 VAL F 157 GLU F 162 1 O LYS F 161 N VAL F 131
SHEET 7 K 9 MET F 185 SER F 188 1 O TRP F 187 N GLU F 162
SHEET 8 K 9 GLY F 204 SER F 207 1 O GLY F 204 N SER F 188
SHEET 9 K 9 GLY F 4 ALA F 8 1 N ALA F 8 O SER F 207
SHEET 1 L 2 PHE F 13 LYS F 14 0
SHEET 2 L 2 GLU F 17 LEU F 18 -1 O GLU F 17 N LYS F 14
CISPEP 1 ASN A 251 PRO A 252 0 5.93
CISPEP 2 LEU A 271 PRO A 272 0 9.49
CISPEP 3 ASN B 251 PRO B 252 0 7.68
CISPEP 4 LEU B 271 PRO B 272 0 9.45
CISPEP 5 ASN C 251 PRO C 252 0 6.01
CISPEP 6 LEU C 271 PRO C 272 0 11.24
CISPEP 7 ASN D 251 PRO D 252 0 10.07
CISPEP 8 LEU D 271 PRO D 272 0 13.80
CISPEP 9 ASN E 251 PRO E 252 0 6.20
CISPEP 10 LEU E 271 PRO E 272 0 14.93
CISPEP 11 ASN F 251 PRO F 252 0 7.55
CISPEP 12 LEU F 271 PRO F 272 0 7.42
SITE 1 AC1 6 TYR A 120 HOH A 383 GLU B 17 LEU B 271
SITE 2 AC1 6 HOH B 340 HOH B 487
SITE 1 AC2 8 LYS A 119 TYR A 120 GLU A 123 ARG A 124
SITE 2 AC2 8 HOH A 340 HOH A 410 LYS B 14 HOH B 487
SITE 1 AC3 7 VAL A 134 ARG A 137 GLY A 189 PHE A 247
SITE 2 AC3 7 ASN A 251 HOH A 391 HOH A 717
SITE 1 AC4 4 TYR A 224 GLY A 227 ARG C 28 GLU E 230
SITE 1 AC5 6 PRO A 135 VAL A 140 ASN A 141 HOH A 406
SITE 2 AC5 6 HOH A 485 HOH A 936
SITE 1 AC6 6 ALA A 200 HOH A 452 HOH A 461 HOH A 688
SITE 2 AC6 6 HOH A 897 HOH A1012
SITE 1 AC7 9 TYR B 132 ARG B 137 ALA B 163 GLY B 189
SITE 2 AC7 9 PHE B 247 ASN B 251 HOH B 787 HOH B1003
SITE 3 AC7 9 HOH B1063
SITE 1 AC8 3 GLU B 32 LYS B 215 GLU B 223
SITE 1 AC9 7 TYR A 106 HOH A 368 SER B 47 PRO B 48
SITE 2 AC9 7 GLY B 77 HOH B 755 HOH B 861
SITE 1 BC1 9 TYR A 120 ARG A 124 HOH A 326 HOH A 428
SITE 2 BC1 9 HOH A 745 GLU B 17 LEU B 18 LYS B 57
SITE 3 BC1 9 HOH B 604
SITE 1 BC2 3 TYR C 224 GLY C 227 LEU C 229
SITE 1 BC3 7 TYR C 132 ARG C 137 LYS C 161 GLY C 189
SITE 2 BC3 7 PHE C 247 ASN C 251 HOH C 727
SITE 1 BC4 9 GLY C 4 VAL C 5 ASN C 36 VAL C 218
SITE 2 BC4 9 CYS C 221 ALA C 222 PHE C 225 HOH C 412
SITE 3 BC4 9 HOH C 785
SITE 1 BC5 9 TYR C 29 ALA C 213 PRO C 214 LYS C 215
SITE 2 BC5 9 GLN C 216 LEU C 293 HOH C 334 HOH C 856
SITE 3 BC5 9 HOH C 860
SITE 1 BC6 5 LYS D 108 PRO D 109 THR D 110 GLN D 111
SITE 2 BC6 5 THR D 250
CRYST1 192.200 125.342 78.428 90.00 103.54 90.00 C 1 2 1 24
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 0.005203 0.000000 0.001253 0.00000
SCALE2 0.000000 0.007978 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013115 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
