HEADER CELL CYCLE/LIGASE/SIGNALING PROTEIN 11-MAY-12 4F52
TITLE STRUCTURE OF A GLOMULIN-RBX1-CUL1 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CULLIN-1;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN, DELTA WHB DOMAIN, UNP RESIDUES 411-690;
COMPND 5 SYNONYM: CUL-1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RBX1;
COMPND 10 CHAIN: B, D;
COMPND 11 FRAGMENT: UNP RESIDUES 5-108;
COMPND 12 SYNONYM: PROTEIN ZYP, RING FINGER PROTEIN 75, RING-BOX PROTEIN 1,
COMPND 13 RBX1, REGULATOR OF CULLINS 1;
COMPND 14 EC: 6.3.2.-;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: GLOMULIN;
COMPND 18 CHAIN: E, F;
COMPND 19 SYNONYM: FK506-BINDING PROTEIN-ASSOCIATED PROTEIN, FAP, FKBP-
COMPND 20 ASSOCIATED PROTEIN;
COMPND 21 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CUL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: RBX1, RNF75, ROC1;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 GENE: GLMN, FAP48, FAP68, VMGLOM;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CULLIN-RING E3 LIGASE, INHIBITOR, CELL CYCLE-LIGASE-SIGNALING PROTEIN
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.M.DUDA,J.L.OLSZEWSKI,B.A.SCHULMAN
REVDAT 2 28-FEB-24 4F52 1 REMARK SEQADV LINK
REVDAT 1 19-SEP-12 4F52 0
JRNL AUTH D.M.DUDA,J.L.OLSZEWSKI,A.E.TRON,M.HAMMEL,L.J.LAMBERT,
JRNL AUTH 2 M.B.WADDELL,T.MITTAG,J.A.DECAPRIO,B.A.SCHULMAN
JRNL TITL STRUCTURE OF A GLOMULIN-RBX1-CUL1 COMPLEX: INHIBITION OF A
JRNL TITL 2 RING E3 LIGASE THROUGH MASKING OF ITS E2-BINDING SURFACE.
JRNL REF MOL.CELL V. 47 371 2012
JRNL REFN ISSN 1097-2765
JRNL PMID 22748924
JRNL DOI 10.1016/J.MOLCEL.2012.05.044
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 56192
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2831
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 37.3860 - 8.1198 0.96 2612 169 0.1897 0.2449
REMARK 3 2 8.1198 - 6.4557 0.98 2668 134 0.2120 0.2623
REMARK 3 3 6.4557 - 5.6428 0.99 2711 137 0.2434 0.2990
REMARK 3 4 5.6428 - 5.1283 0.99 2683 128 0.2296 0.2771
REMARK 3 5 5.1283 - 4.7615 0.99 2699 135 0.1794 0.2771
REMARK 3 6 4.7615 - 4.4813 1.00 2638 164 0.1682 0.2167
REMARK 3 7 4.4813 - 4.2572 0.99 2712 142 0.1792 0.2783
REMARK 3 8 4.2572 - 4.0721 0.99 2655 133 0.2009 0.2965
REMARK 3 9 4.0721 - 3.9155 0.99 2723 141 0.2101 0.2938
REMARK 3 10 3.9155 - 3.7805 0.99 2635 146 0.2190 0.2795
REMARK 3 11 3.7805 - 3.6624 0.99 2695 136 0.2272 0.3013
REMARK 3 12 3.6624 - 3.5578 1.00 2683 126 0.2335 0.3125
REMARK 3 13 3.5578 - 3.4642 0.99 2710 134 0.2306 0.3222
REMARK 3 14 3.4642 - 3.3797 1.00 2656 148 0.2459 0.3425
REMARK 3 15 3.3797 - 3.3030 0.99 2627 146 0.2606 0.3800
REMARK 3 16 3.3030 - 3.2327 0.99 2706 152 0.2859 0.3842
REMARK 3 17 3.2327 - 3.1681 1.00 2666 141 0.3228 0.3968
REMARK 3 18 3.1681 - 3.1083 0.99 2651 156 0.3326 0.4253
REMARK 3 19 3.1083 - 3.0528 0.99 2705 127 0.3480 0.3831
REMARK 3 20 3.0528 - 3.0000 0.95 2526 136 0.3739 0.4701
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 74.26
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 1.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.110
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) : -8.49550
REMARK 3 B22 (A**2) : 23.25860
REMARK 3 B33 (A**2) : -14.76310
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.07190
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 : 0.010 14154
REMARK 3 ANGLE : 1.306 19089
REMARK 3 CHIRALITY : 0.085 2198
REMARK 3 PLANARITY : 0.005 2389
REMARK 3 DIHEDRAL : 20.919 5322
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 420:455 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.9977 -59.3383 4.8443
REMARK 3 T TENSOR
REMARK 3 T11: 1.5746 T22: 0.6548
REMARK 3 T33: 1.2022 T12: 0.0364
REMARK 3 T13: -0.2466 T23: 0.1516
REMARK 3 L TENSOR
REMARK 3 L11: 7.6156 L22: 4.7512
REMARK 3 L33: 6.7108 L12: 4.2305
REMARK 3 L13: 2.8778 L23: 3.5137
REMARK 3 S TENSOR
REMARK 3 S11: 0.5653 S12: 0.4054 S13: -1.5821
REMARK 3 S21: 1.5858 S22: 0.3292 S23: 0.1583
REMARK 3 S31: 1.8941 S32: -0.3112 S33: -0.4785
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 458:531 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1855 -43.9331 1.0378
REMARK 3 T TENSOR
REMARK 3 T11: 0.7606 T22: 0.5858
REMARK 3 T33: 0.4948 T12: 0.1298
REMARK 3 T13: -0.3150 T23: 0.1335
REMARK 3 L TENSOR
REMARK 3 L11: 7.7586 L22: 9.2303
REMARK 3 L33: 3.8447 L12: 3.6380
REMARK 3 L13: -0.5392 L23: 0.0322
REMARK 3 S TENSOR
REMARK 3 S11: 0.4023 S12: -0.1184 S13: -1.5386
REMARK 3 S21: -0.3637 S22: 0.2808 S23: -0.1629
REMARK 3 S31: 1.2052 S32: 0.0719 S33: -0.5568
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 532:569 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8633 -26.9886 7.0144
REMARK 3 T TENSOR
REMARK 3 T11: 0.4823 T22: 0.3873
REMARK 3 T33: 0.4727 T12: 0.0077
REMARK 3 T13: 0.0464 T23: 0.0903
REMARK 3 L TENSOR
REMARK 3 L11: 0.1997 L22: 6.8552
REMARK 3 L33: 8.6497 L12: -0.7448
REMARK 3 L13: -0.3067 L23: 3.1095
REMARK 3 S TENSOR
REMARK 3 S11: 0.2325 S12: 0.3594 S13: 0.2756
REMARK 3 S21: -0.5770 S22: -0.5297 S23: -0.1568
REMARK 3 S31: -0.6263 S32: -0.3868 S33: 0.2425
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN A AND RESID 570:644 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.0512 -24.5878 18.5534
REMARK 3 T TENSOR
REMARK 3 T11: 0.2356 T22: 0.4743
REMARK 3 T33: 0.4394 T12: 0.0442
REMARK 3 T13: -0.0051 T23: 0.0808
REMARK 3 L TENSOR
REMARK 3 L11: 4.1662 L22: 2.9234
REMARK 3 L33: 6.2832 L12: 0.6908
REMARK 3 L13: -2.2297 L23: 0.0927
REMARK 3 S TENSOR
REMARK 3 S11: 0.1736 S12: 0.2295 S13: 0.0647
REMARK 3 S21: 0.0424 S22: -0.0491 S23: -0.0489
REMARK 3 S31: -0.6236 S32: 0.2518 S33: -0.0648
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN A AND RESID 645:689 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5907 -28.4318 31.4491
REMARK 3 T TENSOR
REMARK 3 T11: 0.4300 T22: 0.7343
REMARK 3 T33: 0.3251 T12: 0.0262
REMARK 3 T13: 0.0576 T23: 0.1175
REMARK 3 L TENSOR
REMARK 3 L11: 7.8092 L22: 5.3973
REMARK 3 L33: 6.0169 L12: 0.0612
REMARK 3 L13: -1.2191 L23: 0.0108
REMARK 3 S TENSOR
REMARK 3 S11: 0.5609 S12: -0.6310 S13: -0.2078
REMARK 3 S21: 0.4465 S22: -0.6360 S23: 0.5077
REMARK 3 S31: 0.2173 S32: -1.0289 S33: 0.0386
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 20:44 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8382 -23.5835 3.2920
REMARK 3 T TENSOR
REMARK 3 T11: 0.2606 T22: 0.7234
REMARK 3 T33: 0.3628 T12: -0.0136
REMARK 3 T13: 0.1214 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 3.2557 L22: 3.3871
REMARK 3 L33: 2.6439 L12: -0.2122
REMARK 3 L13: -0.7563 L23: -0.0649
REMARK 3 S TENSOR
REMARK 3 S11: 0.2525 S12: 0.2697 S13: 0.1687
REMARK 3 S21: 0.0408 S22: -0.5100 S23: 0.0343
REMARK 3 S31: 0.6153 S32: 0.6086 S33: 0.2412
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 45:58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5747 -5.4228 -20.0630
REMARK 3 T TENSOR
REMARK 3 T11: 0.8705 T22: 1.3329
REMARK 3 T33: 0.7921 T12: 0.8302
REMARK 3 T13: -0.0427 T23: 0.8325
REMARK 3 L TENSOR
REMARK 3 L11: 5.5022 L22: 6.5915
REMARK 3 L33: 3.1247 L12: -2.2520
REMARK 3 L13: -0.1185 L23: 1.2509
REMARK 3 S TENSOR
REMARK 3 S11: -0.7945 S12: 1.6532 S13: 1.6296
REMARK 3 S21: -0.4946 S22: -0.6631 S23: -0.4103
REMARK 3 S31: 0.0527 S32: 0.2625 S33: 0.8575
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 59:66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.2910 5.5397 -25.9785
REMARK 3 T TENSOR
REMARK 3 T11: 1.3729 T22: 0.9357
REMARK 3 T33: 1.6736 T12: -0.2572
REMARK 3 T13: -0.1613 T23: 0.3725
REMARK 3 L TENSOR
REMARK 3 L11: 4.4441 L22: 4.3429
REMARK 3 L33: 3.8513 L12: -4.3956
REMARK 3 L13: -4.1391 L23: 4.0876
REMARK 3 S TENSOR
REMARK 3 S11: -1.3606 S12: 0.4618 S13: 1.2988
REMARK 3 S21: -1.8247 S22: -0.0126 S23: -2.4109
REMARK 3 S31: -1.8619 S32: 1.6678 S33: 1.6092
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN B AND RESID 68:96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 10.2127 -3.7935 -18.1766
REMARK 3 T TENSOR
REMARK 3 T11: 0.6255 T22: 1.4381
REMARK 3 T33: 1.0421 T12: -0.0075
REMARK 3 T13: 0.1300 T23: 0.5177
REMARK 3 L TENSOR
REMARK 3 L11: 9.3142 L22: 4.6655
REMARK 3 L33: 7.4680 L12: 1.4763
REMARK 3 L13: 1.8962 L23: -1.8783
REMARK 3 S TENSOR
REMARK 3 S11: 0.5291 S12: 1.4440 S13: 0.6094
REMARK 3 S21: -0.8602 S22: -1.0001 S23: -0.3809
REMARK 3 S31: -0.4121 S32: 1.9631 S33: 0.1893
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN B AND RESID 97:104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 17.7411 -6.5326 -18.7155
REMARK 3 T TENSOR
REMARK 3 T11: 0.8063 T22: 1.9781
REMARK 3 T33: 0.8823 T12: 0.0296
REMARK 3 T13: 0.0950 T23: 0.4172
REMARK 3 L TENSOR
REMARK 3 L11: 6.4248 L22: 4.6716
REMARK 3 L33: 8.1552 L12: -4.2881
REMARK 3 L13: 7.1376 L23: -4.1442
REMARK 3 S TENSOR
REMARK 3 S11: -0.2372 S12: -1.1237 S13: 0.0398
REMARK 3 S21: -0.3437 S22: -0.3225 S23: -0.8055
REMARK 3 S31: -0.4580 S32: 1.5208 S33: 0.8919
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 419:456 )
REMARK 3 ORIGIN FOR THE GROUP (A): 21.8421 -7.3782 66.2163
REMARK 3 T TENSOR
REMARK 3 T11: 1.2887 T22: 1.0922
REMARK 3 T33: 0.9963 T12: -0.0426
REMARK 3 T13: -0.1789 T23: 0.1821
REMARK 3 L TENSOR
REMARK 3 L11: 9.2548 L22: 5.9780
REMARK 3 L33: 8.0071 L12: -5.0033
REMARK 3 L13: -6.1159 L23: 4.2193
REMARK 3 S TENSOR
REMARK 3 S11: -0.8823 S12: 0.1544 S13: 1.2169
REMARK 3 S21: 0.3619 S22: 0.7864 S23: -0.5591
REMARK 3 S31: 0.1233 S32: -0.5314 S33: -0.5766
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN C AND RESID 461:522 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0861 -20.5835 70.8416
REMARK 3 T TENSOR
REMARK 3 T11: 1.2138 T22: 1.1147
REMARK 3 T33: 0.6573 T12: 0.1101
REMARK 3 T13: 0.1470 T23: 0.1385
REMARK 3 L TENSOR
REMARK 3 L11: 8.3097 L22: 9.4074
REMARK 3 L33: 1.6706 L12: -6.7763
REMARK 3 L13: 0.6960 L23: 2.1318
REMARK 3 S TENSOR
REMARK 3 S11: 0.0958 S12: 0.2766 S13: 1.0287
REMARK 3 S21: 0.1216 S22: 0.2625 S23: -0.4827
REMARK 3 S31: -0.6352 S32: 0.0697 S33: -0.4288
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN C AND RESID 523:569 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5681 -40.4932 66.0267
REMARK 3 T TENSOR
REMARK 3 T11: 0.6008 T22: 1.0561
REMARK 3 T33: 0.4366 T12: 0.2904
REMARK 3 T13: 0.0860 T23: 0.1598
REMARK 3 L TENSOR
REMARK 3 L11: 1.0860 L22: 9.3333
REMARK 3 L33: 4.7274 L12: 3.1250
REMARK 3 L13: 1.3292 L23: 3.2706
REMARK 3 S TENSOR
REMARK 3 S11: -0.3723 S12: -0.7099 S13: -0.5165
REMARK 3 S21: 0.6449 S22: 0.8230 S23: 0.0492
REMARK 3 S31: 0.3019 S32: 0.8428 S33: -0.3756
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN C AND RESID 570:624 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.6801 -42.3246 54.9165
REMARK 3 T TENSOR
REMARK 3 T11: 0.2865 T22: 1.1424
REMARK 3 T33: 0.2632 T12: 0.2666
REMARK 3 T13: -0.0118 T23: 0.1403
REMARK 3 L TENSOR
REMARK 3 L11: 3.0655 L22: 4.5185
REMARK 3 L33: 3.6240 L12: -0.0110
REMARK 3 L13: 1.1159 L23: -1.6614
REMARK 3 S TENSOR
REMARK 3 S11: -0.1938 S12: -0.2671 S13: 0.3696
REMARK 3 S21: 0.1690 S22: 0.3907 S23: -0.1424
REMARK 3 S31: 0.7060 S32: 1.1791 S33: -0.1023
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN C AND RESID 625:688 )
REMARK 3 ORIGIN FOR THE GROUP (A): 19.1994 -40.7381 44.4833
REMARK 3 T TENSOR
REMARK 3 T11: 0.3727 T22: 0.7796
REMARK 3 T33: 0.3670 T12: -0.0068
REMARK 3 T13: -0.0358 T23: 0.2343
REMARK 3 L TENSOR
REMARK 3 L11: 5.9178 L22: 4.8463
REMARK 3 L33: 6.0815 L12: 0.4559
REMARK 3 L13: 0.9954 L23: -0.1744
REMARK 3 S TENSOR
REMARK 3 S11: 0.2694 S12: -0.2011 S13: -0.0903
REMARK 3 S21: -0.3185 S22: -0.1343 S23: 0.6201
REMARK 3 S31: 0.0439 S32: -0.2307 S33: -0.1404
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID 21:45 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8003 -43.0121 71.5490
REMARK 3 T TENSOR
REMARK 3 T11: 0.5817 T22: 1.5202
REMARK 3 T33: -0.3772 T12: 0.3017
REMARK 3 T13: -0.2275 T23: -0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 0.6219 L22: 2.1863
REMARK 3 L33: 2.9595 L12: 0.9560
REMARK 3 L13: -1.1936 L23: -1.7749
REMARK 3 S TENSOR
REMARK 3 S11: 0.3371 S12: 0.3652 S13: 0.0529
REMARK 3 S21: 0.7742 S22: -0.8124 S23: 0.4460
REMARK 3 S31: -1.0071 S32: -0.1079 S33: 0.2146
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: (CHAIN D AND RESID 46:80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 27.4586 -60.2418 97.7184
REMARK 3 T TENSOR
REMARK 3 T11: 0.9378 T22: 0.9031
REMARK 3 T33: 0.6757 T12: 0.1712
REMARK 3 T13: -0.1212 T23: 0.0748
REMARK 3 L TENSOR
REMARK 3 L11: 3.4515 L22: 8.8712
REMARK 3 L33: 9.2572 L12: 4.0556
REMARK 3 L13: -4.4520 L23: -1.2524
REMARK 3 S TENSOR
REMARK 3 S11: 0.2178 S12: -1.0513 S13: -0.1341
REMARK 3 S21: 0.8312 S22: -0.4083 S23: 0.1390
REMARK 3 S31: -0.1576 S32: 1.3895 S33: 0.4258
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: (CHAIN D AND RESID 81:87 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8591 -65.0270 92.7091
REMARK 3 T TENSOR
REMARK 3 T11: 1.3037 T22: 1.1463
REMARK 3 T33: 0.9623 T12: 0.6765
REMARK 3 T13: -0.0691 T23: 0.3861
REMARK 3 L TENSOR
REMARK 3 L11: 6.8453 L22: 6.2038
REMARK 3 L33: 5.6248 L12: 2.4245
REMARK 3 L13: -0.3926 L23: 4.8584
REMARK 3 S TENSOR
REMARK 3 S11: 0.0652 S12: -0.9603 S13: -0.4887
REMARK 3 S21: 1.4266 S22: -0.4555 S23: -1.3903
REMARK 3 S31: -0.1923 S32: -0.7740 S33: 0.2811
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: (CHAIN D AND RESID 88:96 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.2390 -63.4580 87.6148
REMARK 3 T TENSOR
REMARK 3 T11: 0.9156 T22: 1.7786
REMARK 3 T33: 0.6709 T12: 0.6495
REMARK 3 T13: 0.1035 T23: 0.1783
REMARK 3 L TENSOR
REMARK 3 L11: 7.0930 L22: 6.4923
REMARK 3 L33: 6.0860 L12: 6.6133
REMARK 3 L13: -1.0673 L23: -2.3588
REMARK 3 S TENSOR
REMARK 3 S11: -0.6975 S12: 1.1594 S13: -1.5912
REMARK 3 S21: -1.5013 S22: 0.0027 S23: -0.9032
REMARK 3 S31: 1.7775 S32: 2.8283 S33: 0.6637
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: (CHAIN D AND RESID 97:104 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.0394 -58.0712 93.3824
REMARK 3 T TENSOR
REMARK 3 T11: 1.4895 T22: 1.6582
REMARK 3 T33: 0.6105 T12: 0.2335
REMARK 3 T13: -0.1773 T23: 0.0444
REMARK 3 L TENSOR
REMARK 3 L11: 4.9585 L22: 6.6324
REMARK 3 L33: 5.1843 L12: 5.7297
REMARK 3 L13: -5.0731 L23: -5.8609
REMARK 3 S TENSOR
REMARK 3 S11: -0.5117 S12: -0.2232 S13: -0.7165
REMARK 3 S21: 0.2174 S22: -0.5570 S23: 0.4545
REMARK 3 S31: -1.1744 S32: 3.2160 S33: 1.1087
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: (CHAIN E AND RESID 1:38 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.2199 -93.8273 -12.3245
REMARK 3 T TENSOR
REMARK 3 T11: 1.0241 T22: 0.8389
REMARK 3 T33: 1.3801 T12: 0.0774
REMARK 3 T13: -0.1650 T23: 0.6315
REMARK 3 L TENSOR
REMARK 3 L11: 6.2135 L22: 2.2497
REMARK 3 L33: 5.8550 L12: 2.2252
REMARK 3 L13: -1.8760 L23: -0.2755
REMARK 3 S TENSOR
REMARK 3 S11: -0.6525 S12: -2.2184 S13: -1.6868
REMARK 3 S21: 1.2240 S22: 0.3325 S23: 0.1004
REMARK 3 S31: -0.2858 S32: -0.0758 S33: -0.0544
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: (CHAIN E AND RESID 39:110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1781 -83.8969 -22.1501
REMARK 3 T TENSOR
REMARK 3 T11: 1.1292 T22: 0.3897
REMARK 3 T33: 1.0864 T12: 0.1927
REMARK 3 T13: -0.1932 T23: 0.1893
REMARK 3 L TENSOR
REMARK 3 L11: 6.7390 L22: 2.7155
REMARK 3 L33: 5.8592 L12: -1.0274
REMARK 3 L13: -0.1431 L23: 1.5909
REMARK 3 S TENSOR
REMARK 3 S11: 0.0212 S12: 0.3428 S13: 0.0758
REMARK 3 S21: -1.6943 S22: 0.1006 S23: 0.4903
REMARK 3 S31: -0.0471 S32: 0.2750 S33: 0.0808
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: (CHAIN E AND RESID 111:284 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.3255 -59.5612 -23.1339
REMARK 3 T TENSOR
REMARK 3 T11: 0.7398 T22: 0.5432
REMARK 3 T33: 0.4714 T12: 0.1358
REMARK 3 T13: -0.1608 T23: 0.0078
REMARK 3 L TENSOR
REMARK 3 L11: 6.5620 L22: 8.5738
REMARK 3 L33: 4.7048 L12: -1.7060
REMARK 3 L13: -0.3675 L23: -0.8644
REMARK 3 S TENSOR
REMARK 3 S11: 0.3825 S12: 0.6380 S13: -1.0363
REMARK 3 S21: -0.2535 S22: -0.2552 S23: 0.6149
REMARK 3 S31: 0.6159 S32: 0.0054 S33: -0.1582
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: (CHAIN E AND RESID 285:452 )
REMARK 3 ORIGIN FOR THE GROUP (A): -17.5458 -24.9387 -17.0549
REMARK 3 T TENSOR
REMARK 3 T11: 0.2983 T22: 0.4663
REMARK 3 T33: 0.3338 T12: 0.1406
REMARK 3 T13: 0.0149 T23: -0.0437
REMARK 3 L TENSOR
REMARK 3 L11: 2.7033 L22: 4.6021
REMARK 3 L33: 2.8936 L12: 1.9465
REMARK 3 L13: 0.0559 L23: 2.8580
REMARK 3 S TENSOR
REMARK 3 S11: -0.1508 S12: -0.1787 S13: 0.3493
REMARK 3 S21: -0.3546 S22: -0.1360 S23: 0.7962
REMARK 3 S31: -0.0330 S32: -0.3209 S33: 0.3312
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: (CHAIN E AND RESID 453:583 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.1063 -5.7019 -1.3375
REMARK 3 T TENSOR
REMARK 3 T11: 0.4044 T22: 0.2897
REMARK 3 T33: 0.7077 T12: -0.1051
REMARK 3 T13: 0.0238 T23: -0.0371
REMARK 3 L TENSOR
REMARK 3 L11: 7.9704 L22: 3.7348
REMARK 3 L33: 6.0035 L12: -2.2862
REMARK 3 L13: 3.4024 L23: -1.3012
REMARK 3 S TENSOR
REMARK 3 S11: -0.4193 S12: -0.3240 S13: 1.2060
REMARK 3 S21: 0.0585 S22: -0.1902 S23: 0.0574
REMARK 3 S31: -0.3859 S32: 0.0463 S33: 0.5393
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: (CHAIN F AND RESID 1:143 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5609 19.3251 89.1051
REMARK 3 T TENSOR
REMARK 3 T11: 1.1980 T22: 0.8982
REMARK 3 T33: 0.8099 T12: 0.2081
REMARK 3 T13: -0.2062 T23: -0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.3758 L22: 8.7270
REMARK 3 L33: 2.5413 L12: 2.4944
REMARK 3 L13: 0.0214 L23: -2.2241
REMARK 3 S TENSOR
REMARK 3 S11: -0.4862 S12: 0.2886 S13: 0.3618
REMARK 3 S21: 0.5881 S22: 0.7660 S23: 0.1186
REMARK 3 S31: -0.0901 S32: 0.3797 S33: -0.1079
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: (CHAIN F AND RESID 144:259 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2815 -8.9815 95.9794
REMARK 3 T TENSOR
REMARK 3 T11: 1.5410 T22: 1.0011
REMARK 3 T33: 0.5623 T12: 0.5507
REMARK 3 T13: 0.1200 T23: 0.1867
REMARK 3 L TENSOR
REMARK 3 L11: 2.3331 L22: 2.5739
REMARK 3 L33: 2.9895 L12: -0.6457
REMARK 3 L13: 0.3012 L23: -0.0463
REMARK 3 S TENSOR
REMARK 3 S11: -0.1661 S12: -0.4218 S13: 0.0103
REMARK 3 S21: -0.3369 S22: 0.0398 S23: 0.0183
REMARK 3 S31: -0.7292 S32: -0.2617 S33: 0.1247
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: (CHAIN F AND RESID 279:432 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.7127 -37.2652 90.7243
REMARK 3 T TENSOR
REMARK 3 T11: 0.5909 T22: 0.6880
REMARK 3 T33: 0.3459 T12: 0.2865
REMARK 3 T13: -0.0700 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 3.0815 L22: 4.3230
REMARK 3 L33: 5.0997 L12: -0.8019
REMARK 3 L13: -1.5334 L23: 1.3437
REMARK 3 S TENSOR
REMARK 3 S11: 0.2779 S12: 0.6010 S13: 0.0978
REMARK 3 S21: -0.0340 S22: -0.0813 S23: 0.3704
REMARK 3 S31: -0.7908 S32: -1.3184 S33: -0.1338
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: (CHAIN F AND RESID 439:464 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.9980 -57.5048 76.4892
REMARK 3 T TENSOR
REMARK 3 T11: 0.3763 T22: 0.8742
REMARK 3 T33: 0.8569 T12: -0.1407
REMARK 3 T13: -0.3800 T23: -0.1387
REMARK 3 L TENSOR
REMARK 3 L11: 8.9057 L22: 4.3665
REMARK 3 L33: 2.5629 L12: 0.8727
REMARK 3 L13: 3.9850 L23: 2.2428
REMARK 3 S TENSOR
REMARK 3 S11: 0.1153 S12: 2.4978 S13: -0.8750
REMARK 3 S21: -1.4319 S22: -0.5001 S23: 0.7386
REMARK 3 S31: -0.9673 S32: -0.3953 S33: 0.2516
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: (CHAIN F AND RESID 465:583 )
REMARK 3 ORIGIN FOR THE GROUP (A): 29.4696 -61.6623 77.0463
REMARK 3 T TENSOR
REMARK 3 T11: 0.7670 T22: 0.6660
REMARK 3 T33: 0.6449 T12: 0.2099
REMARK 3 T13: -0.0059 T23: -0.2387
REMARK 3 L TENSOR
REMARK 3 L11: 7.3698 L22: 2.4547
REMARK 3 L33: 5.7227 L12: 2.6703
REMARK 3 L13: -3.2644 L23: -1.8223
REMARK 3 S TENSOR
REMARK 3 S11: -0.5977 S12: 0.8968 S13: -1.1356
REMARK 3 S21: -0.2549 S22: 0.1755 S23: -0.1750
REMARK 3 S31: 1.0911 S32: 0.1345 S33: 0.4474
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 4F52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000072464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : CRYO-COOLED DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56830
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
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) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1
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: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-21% PEG3350, 0.3-0.45M AMMONIUM
REMARK 280 CITRATE, 10MM DTT, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 96.96600
REMARK 290 SMTRY3 2 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 43300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 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 A 409
REMARK 465 SER A 410
REMARK 465 MET A 411
REMARK 465 ALA A 412
REMARK 465 GLN A 413
REMARK 465 SER A 414
REMARK 465 SER A 415
REMARK 465 SER A 416
REMARK 465 LYS A 417
REMARK 465 SER A 418
REMARK 465 PRO A 419
REMARK 465 LYS A 432
REMARK 465 SER A 433
REMARK 465 SER A 434
REMARK 465 LYS A 435
REMARK 465 ASN A 436
REMARK 465 PRO A 437
REMARK 465 GLU A 438
REMARK 465 GLU A 439
REMARK 465 ALA A 440
REMARK 465 GLU A 441
REMARK 465 ILE A 456
REMARK 465 GLU A 457
REMARK 465 THR A 690
REMARK 465 GLY B 3
REMARK 465 SER B 4
REMARK 465 MET B 5
REMARK 465 ASP B 6
REMARK 465 VAL B 7
REMARK 465 ASP B 8
REMARK 465 THR B 9
REMARK 465 PRO B 10
REMARK 465 SER B 11
REMARK 465 GLY B 12
REMARK 465 THR B 13
REMARK 465 ASN B 14
REMARK 465 SER B 15
REMARK 465 GLY B 16
REMARK 465 ALA B 17
REMARK 465 GLY B 18
REMARK 465 LYS B 19
REMARK 465 GLU B 67
REMARK 465 LYS B 105
REMARK 465 TYR B 106
REMARK 465 GLY B 107
REMARK 465 HIS B 108
REMARK 465 GLY C 409
REMARK 465 SER C 410
REMARK 465 MET C 411
REMARK 465 ALA C 412
REMARK 465 GLN C 413
REMARK 465 SER C 414
REMARK 465 SER C 415
REMARK 465 SER C 416
REMARK 465 LYS C 417
REMARK 465 SER C 418
REMARK 465 LYS C 432
REMARK 465 SER C 433
REMARK 465 SER C 434
REMARK 465 LYS C 435
REMARK 465 ASN C 436
REMARK 465 PRO C 437
REMARK 465 GLU C 438
REMARK 465 GLU C 439
REMARK 465 ALA C 440
REMARK 465 GLU C 441
REMARK 465 GLU C 457
REMARK 465 ASP C 458
REMARK 465 LYS C 459
REMARK 465 ASP C 460
REMARK 465 ALA C 495
REMARK 465 CYS C 496
REMARK 465 LYS C 689
REMARK 465 THR C 690
REMARK 465 GLY D 3
REMARK 465 SER D 4
REMARK 465 MET D 5
REMARK 465 ASP D 6
REMARK 465 VAL D 7
REMARK 465 ASP D 8
REMARK 465 THR D 9
REMARK 465 PRO D 10
REMARK 465 SER D 11
REMARK 465 GLY D 12
REMARK 465 THR D 13
REMARK 465 ASN D 14
REMARK 465 SER D 15
REMARK 465 GLY D 16
REMARK 465 ALA D 17
REMARK 465 GLY D 18
REMARK 465 LYS D 19
REMARK 465 LYS D 105
REMARK 465 TYR D 106
REMARK 465 GLY D 107
REMARK 465 HIS D 108
REMARK 465 GLY E -1
REMARK 465 SER E 0
REMARK 465 GLU E 18
REMARK 465 GLN E 19
REMARK 465 ASP E 20
REMARK 465 PHE E 21
REMARK 465 LYS E 22
REMARK 465 GLU E 23
REMARK 465 GLU E 24
REMARK 465 ASP E 25
REMARK 465 PHE E 26
REMARK 465 GLU E 164
REMARK 465 GLN E 165
REMARK 465 ILE E 166
REMARK 465 GLN E 167
REMARK 465 GLU E 227
REMARK 465 GLN E 228
REMARK 465 SER E 229
REMARK 465 GLU E 230
REMARK 465 GLU E 231
REMARK 465 GLY E 232
REMARK 465 GLY E 233
REMARK 465 ASN E 234
REMARK 465 ILE E 259
REMARK 465 PHE E 260
REMARK 465 ASN E 261
REMARK 465 HIS E 262
REMARK 465 GLY E 263
REMARK 465 ARG E 264
REMARK 465 LYS E 265
REMARK 465 LYS E 266
REMARK 465 ARG E 267
REMARK 465 THR E 268
REMARK 465 TRP E 269
REMARK 465 ASN E 270
REMARK 465 TYR E 271
REMARK 465 LEU E 272
REMARK 465 GLU E 273
REMARK 465 PHE E 274
REMARK 465 GLU E 275
REMARK 465 GLU E 276
REMARK 465 GLU E 277
REMARK 465 GLU E 278
REMARK 465 ASN E 279
REMARK 465 THR E 435
REMARK 465 ARG E 436
REMARK 465 ASN E 437
REMARK 465 ASN E 438
REMARK 465 LEU E 536
REMARK 465 CYS E 537
REMARK 465 SER E 538
REMARK 465 ILE E 539
REMARK 465 THR E 540
REMARK 465 VAL E 541
REMARK 465 SER E 542
REMARK 465 GLY E 543
REMARK 465 GLU E 544
REMARK 465 GLU E 545
REMARK 465 ILE E 546
REMARK 465 PRO E 547
REMARK 465 ASN E 548
REMARK 465 MET E 549
REMARK 465 LYS E 584
REMARK 465 SER E 585
REMARK 465 THR E 586
REMARK 465 SER E 587
REMARK 465 GLU E 588
REMARK 465 GLU E 589
REMARK 465 ASN E 590
REMARK 465 ILE E 591
REMARK 465 GLY E 592
REMARK 465 ILE E 593
REMARK 465 LYS E 594
REMARK 465 GLY F -1
REMARK 465 SER F 0
REMARK 465 ASP F 20
REMARK 465 PHE F 21
REMARK 465 GLY F 40
REMARK 465 HIS F 41
REMARK 465 THR F 42
REMARK 465 ASP F 43
REMARK 465 GLN F 44
REMARK 465 LYS F 76
REMARK 465 ASP F 77
REMARK 465 LYS F 78
REMARK 465 GLU F 79
REMARK 465 ASP F 80
REMARK 465 SER F 162
REMARK 465 LYS F 163
REMARK 465 GLU F 164
REMARK 465 ASN F 194
REMARK 465 LYS F 195
REMARK 465 GLU F 196
REMARK 465 ASN F 197
REMARK 465 SER F 198
REMARK 465 LEU F 199
REMARK 465 GLU F 200
REMARK 465 GLU F 227
REMARK 465 GLN F 228
REMARK 465 SER F 229
REMARK 465 GLU F 230
REMARK 465 GLU F 231
REMARK 465 GLY F 232
REMARK 465 GLY F 233
REMARK 465 PHE F 260
REMARK 465 ASN F 261
REMARK 465 HIS F 262
REMARK 465 GLY F 263
REMARK 465 ARG F 264
REMARK 465 LYS F 265
REMARK 465 LYS F 266
REMARK 465 ARG F 267
REMARK 465 THR F 268
REMARK 465 TRP F 269
REMARK 465 ASN F 270
REMARK 465 TYR F 271
REMARK 465 LEU F 272
REMARK 465 GLU F 273
REMARK 465 PHE F 274
REMARK 465 GLU F 275
REMARK 465 GLU F 276
REMARK 465 GLU F 277
REMARK 465 GLU F 278
REMARK 465 LYS F 433
REMARK 465 ARG F 434
REMARK 465 THR F 435
REMARK 465 ARG F 436
REMARK 465 ASN F 437
REMARK 465 ASN F 438
REMARK 465 SER F 533
REMARK 465 LYS F 534
REMARK 465 ASP F 535
REMARK 465 LEU F 536
REMARK 465 CYS F 537
REMARK 465 SER F 538
REMARK 465 ILE F 539
REMARK 465 THR F 540
REMARK 465 VAL F 541
REMARK 465 SER F 542
REMARK 465 GLY F 543
REMARK 465 GLU F 544
REMARK 465 GLU F 545
REMARK 465 ILE F 546
REMARK 465 PRO F 547
REMARK 465 ASN F 548
REMARK 465 MET F 549
REMARK 465 LYS F 584
REMARK 465 SER F 585
REMARK 465 THR F 586
REMARK 465 SER F 587
REMARK 465 GLU F 588
REMARK 465 GLU F 589
REMARK 465 ASN F 590
REMARK 465 ILE F 591
REMARK 465 GLY F 592
REMARK 465 ILE F 593
REMARK 465 LYS F 594
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 CE1 HIS B 77 ZN ZN B 202 1.20
REMARK 500 O PRO C 530 NH2 ARG C 561 1.68
REMARK 500 NE2 HIS B 77 OD2 ASP B 97 2.04
REMARK 500 OH TYR C 563 OD2 ASP F 463 2.04
REMARK 500 OG SER A 487 NZ LYS A 491 2.08
REMARK 500 NH2 ARG F 405 OG SER F 448 2.09
REMARK 500 OH TYR F 401 O GLN F 445 2.11
REMARK 500 O PHE F 213 OG SER F 285 2.11
REMARK 500 OD1 ASN F 476 NH1 ARG F 479 2.13
REMARK 500 O LEU E 567 OG SER E 570 2.14
REMARK 500 OG SER A 528 OG SER E 527 2.14
REMARK 500 CE1 HIS B 77 OD2 ASP B 97 2.15
REMARK 500 O LEU C 525 CB GLU C 529 2.15
REMARK 500 O LYS E 163 N MET E 168 2.16
REMARK 500 O VAL E 482 NZ LYS E 582 2.16
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 C 530 C - N - CD ANGL. DEV. = -18.2 DEGREES
REMARK 500 PRO E 376 C - N - CA ANGL. DEV. = 13.1 DEGREES
REMARK 500 PRO E 376 C - N - CD ANGL. DEV. = -13.3 DEGREES
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 LEU A 474 -65.43 -92.10
REMARK 500 GLN A 477 -129.85 59.47
REMARK 500 ASN A 478 -132.10 46.57
REMARK 500 ALA A 480 -124.29 43.46
REMARK 500 GLN A 549 -9.71 64.69
REMARK 500 SER A 550 -145.70 49.50
REMARK 500 THR A 616 -61.97 -103.78
REMARK 500 SER A 628 -58.83 -123.06
REMARK 500 GLU A 660 -63.58 -128.10
REMARK 500 MET B 50 -7.28 79.96
REMARK 500 ASN B 76 -15.32 79.98
REMARK 500 THR B 90 -63.23 -123.73
REMARK 500 LEU C 533 -169.90 -76.84
REMARK 500 LYS C 647 -2.69 81.66
REMARK 500 CYS D 53 -178.79 -69.93
REMARK 500 SER D 65 -73.69 -51.50
REMARK 500 GLU D 67 -76.15 -107.44
REMARK 500 ILE E 10 -70.49 -56.82
REMARK 500 ASN E 51 -4.86 80.30
REMARK 500 MET E 61 -57.99 -124.93
REMARK 500 LEU E 73 -63.16 -91.41
REMARK 500 LYS E 78 -136.52 60.69
REMARK 500 SER E 162 -2.65 74.44
REMARK 500 GLN E 281 -7.45 65.33
REMARK 500 VAL E 306 -113.71 51.77
REMARK 500 LEU E 307 -3.29 84.45
REMARK 500 THR E 462 158.10 -44.63
REMARK 500 ASN E 488 -8.88 81.29
REMARK 500 ASP E 489 -67.05 -106.46
REMARK 500 PHE E 505 -62.85 -129.07
REMARK 500 PRO E 551 66.47 -65.82
REMARK 500 GLU F 18 6.54 81.65
REMARK 500 LEU F 46 6.73 81.26
REMARK 500 PRO F 113 -172.90 -58.61
REMARK 500 LYS F 217 -72.29 -78.87
REMARK 500 ALA F 223 -114.76 51.39
REMARK 500 GLN F 224 74.39 61.48
REMARK 500 LYS F 257 -13.59 78.56
REMARK 500 ASN F 349 -1.96 64.09
REMARK 500 ASN F 409 -64.27 -102.83
REMARK 500 THR F 442 -73.19 -106.58
REMARK 500 ASP F 463 67.22 63.73
REMARK 500 ASN F 467 -7.20 71.95
REMARK 500 ASN F 488 -71.98 -50.76
REMARK 500 GLN F 491 -62.60 -120.38
REMARK 500 PHE F 505 -60.59 -129.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 501 SER A 502 -149.06
REMARK 500 GLU E 111 GLU E 112 -145.28
REMARK 500 LEU E 432 LYS E 433 131.60
REMARK 500 THR E 492 GLY E 493 122.55
REMARK 500 GLY E 493 LEU E 494 -132.11
REMARK 500 GLU F 112 PRO F 113 -144.83
REMARK 500 SER F 114 GLY F 115 138.47
REMARK 500 GLY F 115 LYS F 116 45.52
REMARK 500 THR F 492 GLY F 493 131.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 42 SG
REMARK 620 2 CYS B 45 SG 126.7
REMARK 620 3 HIS B 80 ND1 108.9 107.7
REMARK 620 4 CYS B 83 SG 110.6 94.1 106.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 53 SG
REMARK 620 2 CYS B 56 SG 112.1
REMARK 620 3 CYS B 68 SG 103.3 119.4
REMARK 620 4 HIS B 82 ND1 120.2 99.9 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 75 SG
REMARK 620 2 HIS B 77 ND1 95.5
REMARK 620 3 HIS B 77 NE2 91.6 59.9
REMARK 620 4 CYS B 94 SG 111.1 112.0 157.0
REMARK 620 5 ASP B 97 OD2 103.7 113.7 56.8 118.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 42 SG
REMARK 620 2 CYS D 45 SG 125.2
REMARK 620 3 HIS D 80 ND1 104.5 98.0
REMARK 620 4 CYS D 83 SG 115.7 102.0 109.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 53 SG
REMARK 620 2 CYS D 56 SG 101.8
REMARK 620 3 CYS D 68 SG 108.4 123.9
REMARK 620 4 HIS D 82 ND1 113.9 94.2 113.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 75 SG
REMARK 620 2 HIS D 77 ND1 108.3
REMARK 620 3 CYS D 94 SG 111.6 114.7
REMARK 620 4 ASP D 97 OD1 169.5 73.9 75.7
REMARK 620 5 ASP D 97 OD2 102.5 97.5 120.7 67.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 203
DBREF 4F52 A 411 690 UNP Q13616 CUL1_HUMAN 411 690
DBREF 4F52 B 5 108 UNP P62877 RBX1_HUMAN 5 108
DBREF 4F52 C 411 690 UNP Q13616 CUL1_HUMAN 411 690
DBREF 4F52 D 5 108 UNP P62877 RBX1_HUMAN 5 108
DBREF 4F52 E 1 594 UNP Q92990 GLMN_HUMAN 1 594
DBREF 4F52 F 1 594 UNP Q92990 GLMN_HUMAN 1 594
SEQADV 4F52 GLY A 409 UNP Q13616 EXPRESSION TAG
SEQADV 4F52 SER A 410 UNP Q13616 EXPRESSION TAG
SEQADV 4F52 GLU A 421 UNP Q13616 LEU 421 ENGINEERED MUTATION
SEQADV 4F52 GLU A 451 UNP Q13616 VAL 451 ENGINEERED MUTATION
SEQADV 4F52 LYS A 452 UNP Q13616 VAL 452 ENGINEERED MUTATION
SEQADV 4F52 LYS A 455 UNP Q13616 TYR 455 ENGINEERED MUTATION
SEQADV 4F52 GLY B 3 UNP P62877 EXPRESSION TAG
SEQADV 4F52 SER B 4 UNP P62877 EXPRESSION TAG
SEQADV 4F52 GLY C 409 UNP Q13616 EXPRESSION TAG
SEQADV 4F52 SER C 410 UNP Q13616 EXPRESSION TAG
SEQADV 4F52 GLU C 421 UNP Q13616 LEU 421 ENGINEERED MUTATION
SEQADV 4F52 GLU C 451 UNP Q13616 VAL 451 ENGINEERED MUTATION
SEQADV 4F52 LYS C 452 UNP Q13616 VAL 452 ENGINEERED MUTATION
SEQADV 4F52 LYS C 455 UNP Q13616 TYR 455 ENGINEERED MUTATION
SEQADV 4F52 GLY D 3 UNP P62877 EXPRESSION TAG
SEQADV 4F52 SER D 4 UNP P62877 EXPRESSION TAG
SEQADV 4F52 GLY E -1 UNP Q92990 EXPRESSION TAG
SEQADV 4F52 SER E 0 UNP Q92990 EXPRESSION TAG
SEQADV 4F52 GLY F -1 UNP Q92990 EXPRESSION TAG
SEQADV 4F52 SER F 0 UNP Q92990 EXPRESSION TAG
SEQRES 1 A 282 GLY SER MET ALA GLN SER SER SER LYS SER PRO GLU GLU
SEQRES 2 A 282 LEU ALA ARG TYR CYS ASP SER LEU LEU LYS LYS SER SER
SEQRES 3 A 282 LYS ASN PRO GLU GLU ALA GLU LEU GLU ASP THR LEU ASN
SEQRES 4 A 282 GLN VAL MET GLU LYS PHE LYS LYS ILE GLU ASP LYS ASP
SEQRES 5 A 282 VAL PHE GLN LYS PHE TYR ALA LYS MET LEU ALA LYS ARG
SEQRES 6 A 282 LEU VAL HIS GLN ASN SER ALA SER ASP ASP ALA GLU ALA
SEQRES 7 A 282 SER MET ILE SER LYS LEU LYS GLN ALA CYS GLY PHE GLU
SEQRES 8 A 282 TYR THR SER LYS LEU GLN ARG MET PHE GLN ASP ILE GLY
SEQRES 9 A 282 VAL SER LYS ASP LEU ASN GLU GLN PHE LYS LYS HIS LEU
SEQRES 10 A 282 THR ASN SER GLU PRO LEU ASP LEU ASP PHE SER ILE GLN
SEQRES 11 A 282 VAL LEU SER SER GLY SER TRP PRO PHE GLN GLN SER CYS
SEQRES 12 A 282 THR PHE ALA LEU PRO SER GLU LEU GLU ARG SER TYR GLN
SEQRES 13 A 282 ARG PHE THR ALA PHE TYR ALA SER ARG HIS SER GLY ARG
SEQRES 14 A 282 LYS LEU THR TRP LEU TYR GLN LEU SER LYS GLY GLU LEU
SEQRES 15 A 282 VAL THR ASN CYS PHE LYS ASN ARG TYR THR LEU GLN ALA
SEQRES 16 A 282 SER THR PHE GLN MET ALA ILE LEU LEU GLN TYR ASN THR
SEQRES 17 A 282 GLU ASP ALA TYR THR VAL GLN GLN LEU THR ASP SER THR
SEQRES 18 A 282 GLN ILE LYS MET ASP ILE LEU ALA GLN VAL LEU GLN ILE
SEQRES 19 A 282 LEU LEU LYS SER LYS LEU LEU VAL LEU GLU ASP GLU ASN
SEQRES 20 A 282 ALA ASN VAL ASP GLU VAL GLU LEU LYS PRO ASP THR LEU
SEQRES 21 A 282 ILE LYS LEU TYR LEU GLY TYR LYS ASN LYS LYS LEU ARG
SEQRES 22 A 282 VAL ASN ILE ASN VAL PRO MET LYS THR
SEQRES 1 B 106 GLY SER MET ASP VAL ASP THR PRO SER GLY THR ASN SER
SEQRES 2 B 106 GLY ALA GLY LYS LYS ARG PHE GLU VAL LYS LYS TRP ASN
SEQRES 3 B 106 ALA VAL ALA LEU TRP ALA TRP ASP ILE VAL VAL ASP ASN
SEQRES 4 B 106 CYS ALA ILE CYS ARG ASN HIS ILE MET ASP LEU CYS ILE
SEQRES 5 B 106 GLU CYS GLN ALA ASN GLN ALA SER ALA THR SER GLU GLU
SEQRES 6 B 106 CYS THR VAL ALA TRP GLY VAL CYS ASN HIS ALA PHE HIS
SEQRES 7 B 106 PHE HIS CYS ILE SER ARG TRP LEU LYS THR ARG GLN VAL
SEQRES 8 B 106 CYS PRO LEU ASP ASN ARG GLU TRP GLU PHE GLN LYS TYR
SEQRES 9 B 106 GLY HIS
SEQRES 1 C 282 GLY SER MET ALA GLN SER SER SER LYS SER PRO GLU GLU
SEQRES 2 C 282 LEU ALA ARG TYR CYS ASP SER LEU LEU LYS LYS SER SER
SEQRES 3 C 282 LYS ASN PRO GLU GLU ALA GLU LEU GLU ASP THR LEU ASN
SEQRES 4 C 282 GLN VAL MET GLU LYS PHE LYS LYS ILE GLU ASP LYS ASP
SEQRES 5 C 282 VAL PHE GLN LYS PHE TYR ALA LYS MET LEU ALA LYS ARG
SEQRES 6 C 282 LEU VAL HIS GLN ASN SER ALA SER ASP ASP ALA GLU ALA
SEQRES 7 C 282 SER MET ILE SER LYS LEU LYS GLN ALA CYS GLY PHE GLU
SEQRES 8 C 282 TYR THR SER LYS LEU GLN ARG MET PHE GLN ASP ILE GLY
SEQRES 9 C 282 VAL SER LYS ASP LEU ASN GLU GLN PHE LYS LYS HIS LEU
SEQRES 10 C 282 THR ASN SER GLU PRO LEU ASP LEU ASP PHE SER ILE GLN
SEQRES 11 C 282 VAL LEU SER SER GLY SER TRP PRO PHE GLN GLN SER CYS
SEQRES 12 C 282 THR PHE ALA LEU PRO SER GLU LEU GLU ARG SER TYR GLN
SEQRES 13 C 282 ARG PHE THR ALA PHE TYR ALA SER ARG HIS SER GLY ARG
SEQRES 14 C 282 LYS LEU THR TRP LEU TYR GLN LEU SER LYS GLY GLU LEU
SEQRES 15 C 282 VAL THR ASN CYS PHE LYS ASN ARG TYR THR LEU GLN ALA
SEQRES 16 C 282 SER THR PHE GLN MET ALA ILE LEU LEU GLN TYR ASN THR
SEQRES 17 C 282 GLU ASP ALA TYR THR VAL GLN GLN LEU THR ASP SER THR
SEQRES 18 C 282 GLN ILE LYS MET ASP ILE LEU ALA GLN VAL LEU GLN ILE
SEQRES 19 C 282 LEU LEU LYS SER LYS LEU LEU VAL LEU GLU ASP GLU ASN
SEQRES 20 C 282 ALA ASN VAL ASP GLU VAL GLU LEU LYS PRO ASP THR LEU
SEQRES 21 C 282 ILE LYS LEU TYR LEU GLY TYR LYS ASN LYS LYS LEU ARG
SEQRES 22 C 282 VAL ASN ILE ASN VAL PRO MET LYS THR
SEQRES 1 D 106 GLY SER MET ASP VAL ASP THR PRO SER GLY THR ASN SER
SEQRES 2 D 106 GLY ALA GLY LYS LYS ARG PHE GLU VAL LYS LYS TRP ASN
SEQRES 3 D 106 ALA VAL ALA LEU TRP ALA TRP ASP ILE VAL VAL ASP ASN
SEQRES 4 D 106 CYS ALA ILE CYS ARG ASN HIS ILE MET ASP LEU CYS ILE
SEQRES 5 D 106 GLU CYS GLN ALA ASN GLN ALA SER ALA THR SER GLU GLU
SEQRES 6 D 106 CYS THR VAL ALA TRP GLY VAL CYS ASN HIS ALA PHE HIS
SEQRES 7 D 106 PHE HIS CYS ILE SER ARG TRP LEU LYS THR ARG GLN VAL
SEQRES 8 D 106 CYS PRO LEU ASP ASN ARG GLU TRP GLU PHE GLN LYS TYR
SEQRES 9 D 106 GLY HIS
SEQRES 1 E 596 GLY SER MET ALA VAL GLU GLU LEU GLN SER ILE ILE LYS
SEQRES 2 E 596 ARG CYS GLN ILE LEU GLU GLU GLN ASP PHE LYS GLU GLU
SEQRES 3 E 596 ASP PHE GLY LEU PHE GLN LEU ALA GLY GLN ARG CYS ILE
SEQRES 4 E 596 GLU GLU GLY HIS THR ASP GLN LEU LEU GLU ILE ILE GLN
SEQRES 5 E 596 ASN GLU LYS ASN LYS VAL ILE ILE LYS ASN MET GLY TRP
SEQRES 6 E 596 ASN LEU VAL GLY PRO VAL VAL ARG CYS LEU LEU CYS LYS
SEQRES 7 E 596 ASP LYS GLU ASP SER LYS ARG LYS VAL TYR PHE LEU ILE
SEQRES 8 E 596 PHE ASP LEU LEU VAL LYS LEU CYS ASN PRO LYS GLU LEU
SEQRES 9 E 596 LEU LEU GLY LEU LEU GLU LEU ILE GLU GLU PRO SER GLY
SEQRES 10 E 596 LYS GLN ILE SER GLN SER ILE LEU LEU LEU LEU GLN PRO
SEQRES 11 E 596 LEU GLN THR VAL ILE GLN LYS LEU HIS ASN LYS ALA TYR
SEQRES 12 E 596 SER ILE GLY LEU ALA LEU SER THR LEU TRP ASN GLN LEU
SEQRES 13 E 596 SER LEU LEU PRO VAL PRO TYR SER LYS GLU GLN ILE GLN
SEQRES 14 E 596 MET ASP ASP TYR GLY LEU CYS GLN CYS CYS LYS ALA LEU
SEQRES 15 E 596 ILE GLU PHE THR LYS PRO PHE VAL GLU GLU VAL ILE ASP
SEQRES 16 E 596 ASN LYS GLU ASN SER LEU GLU ASN GLU LYS LEU LYS ASP
SEQRES 17 E 596 GLU LEU LEU LYS PHE CYS PHE LYS SER LEU LYS CYS PRO
SEQRES 18 E 596 LEU LEU THR ALA GLN PHE PHE GLU GLN SER GLU GLU GLY
SEQRES 19 E 596 GLY ASN ASP PRO PHE ARG TYR PHE ALA SER GLU ILE ILE
SEQRES 20 E 596 GLY PHE LEU SER ALA ILE GLY HIS PRO PHE PRO LYS MET
SEQRES 21 E 596 ILE PHE ASN HIS GLY ARG LYS LYS ARG THR TRP ASN TYR
SEQRES 22 E 596 LEU GLU PHE GLU GLU GLU GLU ASN LYS GLN LEU ALA ASP
SEQRES 23 E 596 SER MET ALA SER LEU ALA TYR LEU VAL PHE VAL GLN GLY
SEQRES 24 E 596 ILE HIS ILE ASP GLN LEU PRO MET VAL LEU SER PRO LEU
SEQRES 25 E 596 TYR LEU LEU GLN PHE ASN MET GLY HIS ILE GLU VAL PHE
SEQRES 26 E 596 LEU GLN ARG THR GLU GLU SER VAL ILE SER LYS GLY LEU
SEQRES 27 E 596 GLU LEU LEU GLU ASN SER LEU LEU ARG ILE GLU ASP ASN
SEQRES 28 E 596 SER LEU LEU TYR GLN TYR LEU GLU ILE LYS SER PHE LEU
SEQRES 29 E 596 THR VAL PRO GLN GLY LEU VAL LYS VAL MET THR LEU CYS
SEQRES 30 E 596 PRO ILE GLU THR LEU ARG LYS LYS SER LEU ALA MET LEU
SEQRES 31 E 596 GLN LEU TYR ILE ASN LYS LEU ASP SER GLN GLY LYS TYR
SEQRES 32 E 596 THR LEU PHE ARG CYS LEU LEU ASN THR SER ASN HIS SER
SEQRES 33 E 596 GLY VAL GLU ALA PHE ILE ILE GLN ASN ILE LYS ASN GLN
SEQRES 34 E 596 ILE ASP MET SER LEU LYS ARG THR ARG ASN ASN LYS TRP
SEQRES 35 E 596 PHE THR GLY PRO GLN LEU ILE SER LEU LEU ASP LEU VAL
SEQRES 36 E 596 LEU PHE LEU PRO GLU GLY ALA GLU THR ASP LEU LEU GLN
SEQRES 37 E 596 ASN SER ASP ARG ILE MET ALA SER LEU ASN LEU LEU ARG
SEQRES 38 E 596 TYR LEU VAL ILE LYS ASP ASN GLU ASN ASP ASN GLN THR
SEQRES 39 E 596 GLY LEU TRP THR GLU LEU GLY ASN ILE GLU ASN ASN PHE
SEQRES 40 E 596 LEU LYS PRO LEU HIS ILE GLY LEU ASN MET SER LYS ALA
SEQRES 41 E 596 HIS TYR GLU ALA GLU ILE LYS ASN SER GLN GLU ALA GLN
SEQRES 42 E 596 LYS SER LYS ASP LEU CYS SER ILE THR VAL SER GLY GLU
SEQRES 43 E 596 GLU ILE PRO ASN MET PRO PRO GLU MET GLN LEU LYS VAL
SEQRES 44 E 596 LEU HIS SER ALA LEU PHE THR PHE ASP LEU ILE GLU SER
SEQRES 45 E 596 VAL LEU ALA ARG VAL GLU GLU LEU ILE GLU ILE LYS THR
SEQRES 46 E 596 LYS SER THR SER GLU GLU ASN ILE GLY ILE LYS
SEQRES 1 F 596 GLY SER MET ALA VAL GLU GLU LEU GLN SER ILE ILE LYS
SEQRES 2 F 596 ARG CYS GLN ILE LEU GLU GLU GLN ASP PHE LYS GLU GLU
SEQRES 3 F 596 ASP PHE GLY LEU PHE GLN LEU ALA GLY GLN ARG CYS ILE
SEQRES 4 F 596 GLU GLU GLY HIS THR ASP GLN LEU LEU GLU ILE ILE GLN
SEQRES 5 F 596 ASN GLU LYS ASN LYS VAL ILE ILE LYS ASN MET GLY TRP
SEQRES 6 F 596 ASN LEU VAL GLY PRO VAL VAL ARG CYS LEU LEU CYS LYS
SEQRES 7 F 596 ASP LYS GLU ASP SER LYS ARG LYS VAL TYR PHE LEU ILE
SEQRES 8 F 596 PHE ASP LEU LEU VAL LYS LEU CYS ASN PRO LYS GLU LEU
SEQRES 9 F 596 LEU LEU GLY LEU LEU GLU LEU ILE GLU GLU PRO SER GLY
SEQRES 10 F 596 LYS GLN ILE SER GLN SER ILE LEU LEU LEU LEU GLN PRO
SEQRES 11 F 596 LEU GLN THR VAL ILE GLN LYS LEU HIS ASN LYS ALA TYR
SEQRES 12 F 596 SER ILE GLY LEU ALA LEU SER THR LEU TRP ASN GLN LEU
SEQRES 13 F 596 SER LEU LEU PRO VAL PRO TYR SER LYS GLU GLN ILE GLN
SEQRES 14 F 596 MET ASP ASP TYR GLY LEU CYS GLN CYS CYS LYS ALA LEU
SEQRES 15 F 596 ILE GLU PHE THR LYS PRO PHE VAL GLU GLU VAL ILE ASP
SEQRES 16 F 596 ASN LYS GLU ASN SER LEU GLU ASN GLU LYS LEU LYS ASP
SEQRES 17 F 596 GLU LEU LEU LYS PHE CYS PHE LYS SER LEU LYS CYS PRO
SEQRES 18 F 596 LEU LEU THR ALA GLN PHE PHE GLU GLN SER GLU GLU GLY
SEQRES 19 F 596 GLY ASN ASP PRO PHE ARG TYR PHE ALA SER GLU ILE ILE
SEQRES 20 F 596 GLY PHE LEU SER ALA ILE GLY HIS PRO PHE PRO LYS MET
SEQRES 21 F 596 ILE PHE ASN HIS GLY ARG LYS LYS ARG THR TRP ASN TYR
SEQRES 22 F 596 LEU GLU PHE GLU GLU GLU GLU ASN LYS GLN LEU ALA ASP
SEQRES 23 F 596 SER MET ALA SER LEU ALA TYR LEU VAL PHE VAL GLN GLY
SEQRES 24 F 596 ILE HIS ILE ASP GLN LEU PRO MET VAL LEU SER PRO LEU
SEQRES 25 F 596 TYR LEU LEU GLN PHE ASN MET GLY HIS ILE GLU VAL PHE
SEQRES 26 F 596 LEU GLN ARG THR GLU GLU SER VAL ILE SER LYS GLY LEU
SEQRES 27 F 596 GLU LEU LEU GLU ASN SER LEU LEU ARG ILE GLU ASP ASN
SEQRES 28 F 596 SER LEU LEU TYR GLN TYR LEU GLU ILE LYS SER PHE LEU
SEQRES 29 F 596 THR VAL PRO GLN GLY LEU VAL LYS VAL MET THR LEU CYS
SEQRES 30 F 596 PRO ILE GLU THR LEU ARG LYS LYS SER LEU ALA MET LEU
SEQRES 31 F 596 GLN LEU TYR ILE ASN LYS LEU ASP SER GLN GLY LYS TYR
SEQRES 32 F 596 THR LEU PHE ARG CYS LEU LEU ASN THR SER ASN HIS SER
SEQRES 33 F 596 GLY VAL GLU ALA PHE ILE ILE GLN ASN ILE LYS ASN GLN
SEQRES 34 F 596 ILE ASP MET SER LEU LYS ARG THR ARG ASN ASN LYS TRP
SEQRES 35 F 596 PHE THR GLY PRO GLN LEU ILE SER LEU LEU ASP LEU VAL
SEQRES 36 F 596 LEU PHE LEU PRO GLU GLY ALA GLU THR ASP LEU LEU GLN
SEQRES 37 F 596 ASN SER ASP ARG ILE MET ALA SER LEU ASN LEU LEU ARG
SEQRES 38 F 596 TYR LEU VAL ILE LYS ASP ASN GLU ASN ASP ASN GLN THR
SEQRES 39 F 596 GLY LEU TRP THR GLU LEU GLY ASN ILE GLU ASN ASN PHE
SEQRES 40 F 596 LEU LYS PRO LEU HIS ILE GLY LEU ASN MET SER LYS ALA
SEQRES 41 F 596 HIS TYR GLU ALA GLU ILE LYS ASN SER GLN GLU ALA GLN
SEQRES 42 F 596 LYS SER LYS ASP LEU CYS SER ILE THR VAL SER GLY GLU
SEQRES 43 F 596 GLU ILE PRO ASN MET PRO PRO GLU MET GLN LEU LYS VAL
SEQRES 44 F 596 LEU HIS SER ALA LEU PHE THR PHE ASP LEU ILE GLU SER
SEQRES 45 F 596 VAL LEU ALA ARG VAL GLU GLU LEU ILE GLU ILE LYS THR
SEQRES 46 F 596 LYS SER THR SER GLU GLU ASN ILE GLY ILE LYS
HET ZN B 201 1
HET ZN B 202 1
HET ZN B 203 1
HET ZN D 201 1
HET ZN D 202 1
HET ZN D 203 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 6(ZN 2+)
HELIX 1 1 GLU A 420 LYS A 431 1 12
HELIX 2 2 GLU A 443 LYS A 455 1 13
HELIX 3 3 LYS A 459 HIS A 476 1 18
HELIX 4 4 SER A 481 GLY A 497 1 17
HELIX 5 5 GLY A 497 THR A 526 1 30
HELIX 6 6 PRO A 556 HIS A 574 1 19
HELIX 7 7 THR A 605 LEU A 612 1 8
HELIX 8 8 GLN A 613 THR A 616 5 4
HELIX 9 9 VAL A 622 GLN A 630 1 9
HELIX 10 10 LYS A 632 SER A 646 1 15
HELIX 11 11 CYS B 53 ALA B 58 1 6
HELIX 12 12 PHE B 81 LEU B 88 1 8
HELIX 13 13 GLU C 420 LEU C 429 1 10
HELIX 14 14 THR C 445 LYS C 455 1 11
HELIX 15 15 PHE C 462 HIS C 476 1 15
HELIX 16 16 ASP C 482 LYS C 493 1 12
HELIX 17 17 PHE C 498 ASN C 527 1 30
HELIX 18 18 PRO C 556 HIS C 574 1 19
HELIX 19 19 TYR C 583 LEU C 585 5 3
HELIX 20 20 THR C 605 GLN C 613 1 9
HELIX 21 21 TYR C 614 THR C 616 5 3
HELIX 22 22 VAL C 622 GLN C 630 1 9
HELIX 23 23 LYS C 632 SER C 646 1 15
HELIX 24 24 CYS D 53 ASN D 59 1 7
HELIX 25 25 PHE D 81 ARG D 91 1 11
HELIX 26 26 ALA E 2 GLN E 14 1 13
HELIX 27 27 LEU E 28 GLU E 38 1 11
HELIX 28 28 THR E 42 GLN E 50 1 9
HELIX 29 29 ASN E 54 MET E 61 1 8
HELIX 30 30 GLY E 62 ASN E 64 5 3
HELIX 31 31 LEU E 65 CYS E 75 1 11
HELIX 32 32 ARG E 83 CYS E 97 1 15
HELIX 33 33 ASN E 98 LYS E 100 5 3
HELIX 34 34 GLU E 101 LEU E 107 1 7
HELIX 35 35 GLU E 108 GLU E 111 5 4
HELIX 36 36 SER E 114 LYS E 116 5 3
HELIX 37 37 GLN E 117 LEU E 136 1 20
HELIX 38 38 LYS E 139 LEU E 157 1 19
HELIX 39 39 GLY E 172 ASP E 193 1 22
HELIX 40 40 SER E 198 ALA E 223 1 26
HELIX 41 41 PRO E 236 ILE E 251 1 16
HELIX 42 42 PRO E 254 MET E 258 5 5
HELIX 43 43 LEU E 282 VAL E 295 1 14
HELIX 44 44 SER E 308 GLN E 325 1 18
HELIX 45 45 GLU E 328 ARG E 345 1 18
HELIX 46 46 LEU E 352 GLU E 357 5 6
HELIX 47 47 ILE E 358 CYS E 375 1 18
HELIX 48 48 ILE E 377 LEU E 395 1 19
HELIX 49 49 ASP E 396 ASN E 412 1 17
HELIX 50 50 HIS E 413 SER E 431 1 19
HELIX 51 51 GLY E 443 LEU E 454 1 12
HELIX 52 52 ASN E 467 ASP E 485 1 19
HELIX 53 53 GLY E 493 THR E 496 5 4
HELIX 54 54 GLU E 497 PHE E 505 1 9
HELIX 55 55 PHE E 505 LYS E 534 1 30
HELIX 56 56 GLU E 552 GLN E 554 5 3
HELIX 57 57 LEU E 555 LYS E 582 1 28
HELIX 58 58 ALA F 2 ILE F 15 1 14
HELIX 59 59 GLU F 23 GLU F 38 1 16
HELIX 60 60 ASN F 54 MET F 61 1 8
HELIX 61 61 GLY F 62 ASN F 64 5 3
HELIX 62 62 LEU F 65 LEU F 74 1 10
HELIX 63 63 ARG F 83 LEU F 96 1 14
HELIX 64 64 ASN F 98 GLU F 108 1 11
HELIX 65 65 LEU F 109 GLU F 111 5 3
HELIX 66 66 LYS F 116 LEU F 136 1 21
HELIX 67 67 ALA F 140 SER F 155 1 16
HELIX 68 68 GLY F 172 ASP F 193 1 22
HELIX 69 69 GLU F 202 ALA F 223 1 22
HELIX 70 70 ASP F 235 ILE F 251 1 17
HELIX 71 71 LEU F 282 VAL F 295 1 14
HELIX 72 72 HIS F 299 LEU F 303 5 5
HELIX 73 73 SER F 308 GLN F 325 1 18
HELIX 74 74 GLU F 328 LEU F 344 1 17
HELIX 75 75 LEU F 352 GLU F 357 5 6
HELIX 76 76 ILE F 358 CYS F 375 1 18
HELIX 77 77 ILE F 377 LEU F 395 1 19
HELIX 78 78 ASP F 396 SER F 411 1 16
HELIX 79 79 HIS F 413 MET F 430 1 18
HELIX 80 80 GLY F 443 LEU F 454 1 12
HELIX 81 81 ASN F 467 ASP F 485 1 19
HELIX 82 82 GLU F 497 PHE F 505 1 9
HELIX 83 83 PHE F 505 ALA F 530 1 26
HELIX 84 84 PRO F 551 THR F 583 1 33
SHEET 1 A 5 ASP A 534 SER A 541 0
SHEET 2 A 5 PHE B 22 TRP B 35 1 O TRP B 33 N LEU A 540
SHEET 3 A 5 ARG A 577 THR A 592 -1 N LYS A 578 O ALA B 34
SHEET 4 A 5 THR A 600 SER A 604 -1 O ALA A 603 N GLY A 588
SHEET 5 A 5 ARG A 681 ASN A 683 1 O VAL A 682 N THR A 600
SHEET 1 B 3 ALA A 619 THR A 621 0
SHEET 2 B 3 LEU A 668 LEU A 671 -1 O ILE A 669 N TYR A 620
SHEET 3 B 3 LEU A 649 VAL A 650 -1 N VAL A 650 O LYS A 670
SHEET 1 C 2 VAL B 70 TRP B 72 0
SHEET 2 C 2 ALA B 78 HIS B 80 -1 O PHE B 79 N ALA B 71
SHEET 1 D 3 ASP C 534 SER C 541 0
SHEET 2 D 3 PHE D 22 ALA D 34 1 O TRP D 33 N LEU C 540
SHEET 3 D 3 LYS C 578 TRP C 581 -1 N LYS C 578 O ALA D 34
SHEET 1 E 5 ASP C 534 SER C 541 0
SHEET 2 E 5 PHE D 22 ALA D 34 1 O TRP D 33 N LEU C 540
SHEET 3 E 5 LYS C 587 THR C 592 -1 N GLU C 589 O LYS D 26
SHEET 4 E 5 THR C 600 SER C 604 -1 O LEU C 601 N LEU C 590
SHEET 5 E 5 ARG C 681 ASN C 683 1 O VAL C 682 N THR C 600
SHEET 1 F 3 ALA C 619 THR C 621 0
SHEET 2 F 3 LEU C 668 LEU C 671 -1 O ILE C 669 N TYR C 620
SHEET 3 F 3 LEU C 649 LEU C 651 -1 N VAL C 650 O LYS C 670
SHEET 1 G 2 VAL D 70 TRP D 72 0
SHEET 2 G 2 ALA D 78 HIS D 80 -1 O PHE D 79 N ALA D 71
LINK SG CYS B 42 ZN ZN B 201 1555 1555 2.11
LINK SG CYS B 45 ZN ZN B 201 1555 1555 2.27
LINK SG CYS B 53 ZN ZN B 203 1555 1555 2.57
LINK SG CYS B 56 ZN ZN B 203 1555 1555 2.28
LINK SG CYS B 68 ZN ZN B 203 1555 1555 2.30
LINK SG CYS B 75 ZN ZN B 202 1555 1555 2.37
LINK ND1 HIS B 77 ZN ZN B 202 1555 1555 2.07
LINK NE2 HIS B 77 ZN ZN B 202 1555 1555 2.20
LINK ND1 HIS B 80 ZN ZN B 201 1555 1555 2.07
LINK ND1 HIS B 82 ZN ZN B 203 1555 1555 2.13
LINK SG CYS B 83 ZN ZN B 201 1555 1555 2.43
LINK SG CYS B 94 ZN ZN B 202 1555 1555 2.26
LINK OD2 ASP B 97 ZN ZN B 202 1555 1555 2.08
LINK SG CYS D 42 ZN ZN D 201 1555 1555 2.24
LINK SG CYS D 45 ZN ZN D 201 1555 1555 2.41
LINK SG CYS D 53 ZN ZN D 203 1555 1555 2.47
LINK SG CYS D 56 ZN ZN D 203 1555 1555 2.28
LINK SG CYS D 68 ZN ZN D 203 1555 1555 2.00
LINK SG CYS D 75 ZN ZN D 202 1555 1555 2.29
LINK ND1 HIS D 77 ZN ZN D 202 1555 1555 2.06
LINK ND1 HIS D 80 ZN ZN D 201 1555 1555 2.06
LINK ND1 HIS D 82 ZN ZN D 203 1555 1555 1.92
LINK SG CYS D 83 ZN ZN D 201 1555 1555 2.49
LINK SG CYS D 94 ZN ZN D 202 1555 1555 2.50
LINK OD1 ASP D 97 ZN ZN D 202 1555 1555 1.90
LINK OD2 ASP D 97 ZN ZN D 202 1555 1555 2.05
CISPEP 1 LYS E 53 ASN E 54 0 0.52
CISPEP 2 MET F 168 ASP F 169 0 -11.14
CISPEP 3 LEU F 456 PRO F 457 0 -20.04
CISPEP 4 LEU F 494 TRP F 495 0 0.88
SITE 1 AC1 4 CYS B 42 CYS B 45 HIS B 80 CYS B 83
SITE 1 AC2 4 CYS B 75 HIS B 77 CYS B 94 ASP B 97
SITE 1 AC3 4 CYS B 53 CYS B 56 CYS B 68 HIS B 82
SITE 1 AC4 4 CYS D 42 CYS D 45 HIS D 80 CYS D 83
SITE 1 AC5 4 CYS D 75 HIS D 77 CYS D 94 ASP D 97
SITE 1 AC6 4 CYS D 53 CYS D 56 CYS D 68 HIS D 82
CRYST1 53.333 193.932 142.075 90.00 98.81 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 0.018750 0.000000 0.002906 0.00000
SCALE2 0.000000 0.005156 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007123 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
