HEADER DE NOVO PROTEIN 15-SEP-16 5LW1
TITLE CRYSTAL STRUCTURE OF DARPIN-DARPIN RIGID FUSION, VARIANT DD_232_11_D12
TITLE 2 IN COMPLEX JNK1A1 AND JIP1 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DD_232_11_D12;
COMPND 3 CHAIN: A, D, G;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 8;
COMPND 7 CHAIN: B, E, H;
COMPND 8 SYNONYM: MAPK 8,JNK-46,STRESS-ACTIVATED PROTEIN KINASE 1C,SAPK1C,
COMPND 9 STRESS-ACTIVATED PROTEIN KINASE JNK1,C-JUN N-TERMINAL KINASE 1;
COMPND 10 EC: 2.7.11.24;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: C-JUN-AMINO-TERMINAL KINASE-INTERACTING PROTEIN 1;
COMPND 14 CHAIN: C, F, I;
COMPND 15 SYNONYM: JNK-INTERACTING PROTEIN 1,ISLET-BRAIN 1,IB-1,JNK MAP KINASE
COMPND 16 SCAFFOLD PROTEIN 1,MITOGEN-ACTIVATED PROTEIN KINASE 8-INTERACTING
COMPND 17 PROTEIN 1;
COMPND 18 ENGINEERED: YES;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: PEPSTATIN;
COMPND 21 CHAIN: L;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 3 ORGANISM_TAXID: 32630;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 6 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 GENE: MAPK8, JNK1, PRKM8, SAPK1, SAPK1C;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 14 EXPRESSION_SYSTEM_VARIANT: XL1-BLUE;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 MOL_ID: 4;
SOURCE 21 SYNTHETIC: YES;
SOURCE 22 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 23 ORGANISM_TAXID: 32630
KEYWDS X-RAY CRYSTALLOGRAPHY; DESIGNED ANKYRIN REPEAT PROTEINS; PROTEIN
KEYWDS 2 DESIGN; PROTEIN ENGINEERING; RIGID DOMAIN FUSIONS, TRANSFERASE, DE
KEYWDS 3 NOVO PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.WU,A.BATYUK,P.R.MITTL,A.HONEGGER,A.PLUECKTHUN
REVDAT 5 17-JAN-24 5LW1 1 REMARK
REVDAT 4 01-JAN-20 5LW1 1 REMARK SITE
REVDAT 3 10-JUL-19 5LW1 1 JRNL
REVDAT 2 13-JUN-18 5LW1 1 REMARK
REVDAT 1 13-DEC-17 5LW1 0
JRNL AUTH Y.WU,A.HONEGGER,A.BATYUK,P.R.E.MITTL,A.PLUCKTHUN
JRNL TITL STRUCTURAL BASIS FOR THE SELECTIVE INHIBITION OF C-JUN
JRNL TITL 2 N-TERMINAL KINASE 1 DETERMINED BY RIGID DARPIN-DARPIN
JRNL TITL 3 FUSIONS.
JRNL REF J.MOL.BIOL. V. 430 2128 2018
JRNL REFN ESSN 1089-8638
JRNL PMID 29126898
JRNL DOI 10.1016/J.JMB.2017.10.032
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12_2829: ???)
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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.38
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 58926
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2944
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 49.3888 - 8.8127 0.96 2696 135 0.1534 0.1842
REMARK 3 2 8.8127 - 7.0013 0.99 2734 130 0.1417 0.1654
REMARK 3 3 7.0013 - 6.1181 0.96 2604 158 0.1645 0.1997
REMARK 3 4 6.1181 - 5.5596 0.99 2721 123 0.1614 0.2066
REMARK 3 5 5.5596 - 5.1616 0.99 2718 135 0.1424 0.1836
REMARK 3 6 5.1616 - 4.8575 0.99 2701 139 0.1363 0.1685
REMARK 3 7 4.8575 - 4.6144 0.95 2586 123 0.1293 0.1637
REMARK 3 8 4.6144 - 4.4137 0.97 2623 151 0.1424 0.1628
REMARK 3 9 4.4137 - 4.2439 0.99 2699 151 0.1498 0.1885
REMARK 3 10 4.2439 - 4.0975 0.99 2674 135 0.1674 0.2166
REMARK 3 11 4.0975 - 3.9694 0.99 2679 128 0.1821 0.2256
REMARK 3 12 3.9694 - 3.8560 0.99 2696 122 0.1886 0.2301
REMARK 3 13 3.8560 - 3.7545 0.99 2669 169 0.1987 0.2585
REMARK 3 14 3.7545 - 3.6630 0.99 2710 129 0.2074 0.2255
REMARK 3 15 3.6630 - 3.5797 0.99 2655 160 0.2332 0.2433
REMARK 3 16 3.5797 - 3.5036 0.94 2558 140 0.2754 0.3393
REMARK 3 17 3.5036 - 3.4335 0.98 2628 125 0.2931 0.3307
REMARK 3 18 3.4335 - 3.3687 0.98 2693 143 0.3010 0.3816
REMARK 3 19 3.3687 - 3.3086 0.98 2654 140 0.3202 0.3607
REMARK 3 20 3.3086 - 3.2525 0.98 2648 153 0.3525 0.3781
REMARK 3 21 3.2525 - 3.2000 0.99 2636 155 0.3818 0.4351
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.730
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 16587
REMARK 3 ANGLE : 0.494 22485
REMARK 3 CHIRALITY : 0.041 2544
REMARK 3 PLANARITY : 0.004 2870
REMARK 3 DIHEDRAL : 10.539 9907
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 34
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 23 )
REMARK 3 ORIGIN FOR THE GROUP (A): 204.2690 7.2402 30.2160
REMARK 3 T TENSOR
REMARK 3 T11: 0.8853 T22: 0.8101
REMARK 3 T33: 1.2104 T12: -0.0282
REMARK 3 T13: 0.2317 T23: -0.2734
REMARK 3 L TENSOR
REMARK 3 L11: 0.9559 L22: 0.0887
REMARK 3 L33: 4.0455 L12: 0.2636
REMARK 3 L13: 1.9521 L23: 0.6447
REMARK 3 S TENSOR
REMARK 3 S11: -0.5381 S12: -1.9498 S13: 1.0946
REMARK 3 S21: 1.0488 S22: 0.2282 S23: 0.0884
REMARK 3 S31: -0.0714 S32: -0.1693 S33: 0.5142
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 224.7486 -2.9631 27.9972
REMARK 3 T TENSOR
REMARK 3 T11: 0.6201 T22: 0.8772
REMARK 3 T33: 0.6406 T12: -0.0567
REMARK 3 T13: -0.0928 T23: -0.1546
REMARK 3 L TENSOR
REMARK 3 L11: 7.3003 L22: 2.8075
REMARK 3 L33: 4.5457 L12: -0.2370
REMARK 3 L13: -2.4506 L23: 0.4215
REMARK 3 S TENSOR
REMARK 3 S11: -0.1482 S12: -0.6076 S13: 0.0882
REMARK 3 S21: 0.2702 S22: -0.1403 S23: 0.0323
REMARK 3 S31: 0.4890 S32: 0.0662 S33: 0.2551
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 135 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 243.6012 -9.0485 12.9426
REMARK 3 T TENSOR
REMARK 3 T11: 0.6485 T22: 0.9864
REMARK 3 T33: 0.8519 T12: -0.0925
REMARK 3 T13: -0.0239 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 3.4825 L22: 2.9306
REMARK 3 L33: 4.0864 L12: 0.7968
REMARK 3 L13: 1.1634 L23: 3.4556
REMARK 3 S TENSOR
REMARK 3 S11: -0.2111 S12: 0.2324 S13: 0.2887
REMARK 3 S21: -0.2522 S22: 0.2423 S23: -0.9179
REMARK 3 S31: -0.4189 S32: 0.5536 S33: -0.2055
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 182 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 230.8307 -25.1994 -6.4433
REMARK 3 T TENSOR
REMARK 3 T11: 0.5339 T22: 0.6800
REMARK 3 T33: 0.8850 T12: 0.0209
REMARK 3 T13: 0.1263 T23: -0.0181
REMARK 3 L TENSOR
REMARK 3 L11: 4.5625 L22: 4.0202
REMARK 3 L33: 8.6290 L12: 0.6572
REMARK 3 L13: 2.3872 L23: 0.1229
REMARK 3 S TENSOR
REMARK 3 S11: -0.0474 S12: 0.2313 S13: -0.2248
REMARK 3 S21: 0.0264 S22: 0.2502 S23: 0.1198
REMARK 3 S31: 0.3013 S32: 0.2419 S33: -0.2621
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 8 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): 278.2535 11.6926 35.9807
REMARK 3 T TENSOR
REMARK 3 T11: 1.0614 T22: 1.4686
REMARK 3 T33: 1.3406 T12: -0.2624
REMARK 3 T13: -0.2877 T23: 0.1463
REMARK 3 L TENSOR
REMARK 3 L11: 2.4638 L22: 7.2216
REMARK 3 L33: 8.7922 L12: -0.7881
REMARK 3 L13: -3.8966 L23: -2.7880
REMARK 3 S TENSOR
REMARK 3 S11: -0.7287 S12: -0.5643 S13: -0.0682
REMARK 3 S21: 0.1451 S22: -0.0411 S23: -1.4136
REMARK 3 S31: 0.2371 S32: 1.5638 S33: 0.5815
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 30 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 270.2220 14.8826 32.4744
REMARK 3 T TENSOR
REMARK 3 T11: 0.6950 T22: 1.1387
REMARK 3 T33: 0.7467 T12: -0.2223
REMARK 3 T13: -0.1110 T23: 0.2503
REMARK 3 L TENSOR
REMARK 3 L11: 6.4360 L22: 6.2929
REMARK 3 L33: 5.4146 L12: -0.1888
REMARK 3 L13: 0.7220 L23: 2.2095
REMARK 3 S TENSOR
REMARK 3 S11: -0.2264 S12: -0.3002 S13: -0.3377
REMARK 3 S21: -0.1083 S22: 0.1030 S23: -0.5868
REMARK 3 S31: -0.3111 S32: 0.9127 S33: 0.2446
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 64 THROUGH 144 )
REMARK 3 ORIGIN FOR THE GROUP (A): 262.0556 20.8310 26.0678
REMARK 3 T TENSOR
REMARK 3 T11: 0.7639 T22: 0.8647
REMARK 3 T33: 0.6096 T12: -0.2199
REMARK 3 T13: -0.1010 T23: 0.0109
REMARK 3 L TENSOR
REMARK 3 L11: 4.9886 L22: 6.4179
REMARK 3 L33: 1.8810 L12: -3.3966
REMARK 3 L13: -0.6890 L23: -0.7200
REMARK 3 S TENSOR
REMARK 3 S11: -0.1441 S12: -0.1724 S13: 0.3333
REMARK 3 S21: 0.3714 S22: -0.0153 S23: -0.6986
REMARK 3 S31: -0.4751 S32: 0.6066 S33: 0.1613
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 145 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): 253.6025 18.2783 28.5055
REMARK 3 T TENSOR
REMARK 3 T11: 0.9334 T22: 0.7812
REMARK 3 T33: 0.5866 T12: -0.1316
REMARK 3 T13: -0.0932 T23: 0.0012
REMARK 3 L TENSOR
REMARK 3 L11: 3.4571 L22: 2.7240
REMARK 3 L33: 2.5533 L12: -0.7268
REMARK 3 L13: -0.6222 L23: -1.8118
REMARK 3 S TENSOR
REMARK 3 S11: 0.1303 S12: -0.0072 S13: -0.1420
REMARK 3 S21: -0.2457 S22: -0.3806 S23: 0.1628
REMARK 3 S31: -0.0827 S32: 0.1421 S33: 0.1694
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 192 THROUGH 270 )
REMARK 3 ORIGIN FOR THE GROUP (A): 234.9298 18.2238 27.5132
REMARK 3 T TENSOR
REMARK 3 T11: 0.7978 T22: 0.7273
REMARK 3 T33: 0.6175 T12: 0.0550
REMARK 3 T13: -0.0445 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 5.3260 L22: 5.5434
REMARK 3 L33: 2.1067 L12: 2.3183
REMARK 3 L13: 0.2288 L23: 0.2863
REMARK 3 S TENSOR
REMARK 3 S11: 0.2029 S12: -0.4101 S13: 0.0502
REMARK 3 S21: 0.0595 S22: -0.2181 S23: 0.2905
REMARK 3 S31: -0.2839 S32: -0.4278 S33: 0.0482
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 271 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 240.2289 36.0733 27.1250
REMARK 3 T TENSOR
REMARK 3 T11: 1.1530 T22: 0.6623
REMARK 3 T33: 0.9521 T12: 0.0461
REMARK 3 T13: -0.1048 T23: -0.0680
REMARK 3 L TENSOR
REMARK 3 L11: 5.1523 L22: 6.6451
REMARK 3 L33: 6.4240 L12: 2.2661
REMARK 3 L13: -0.9322 L23: -1.1261
REMARK 3 S TENSOR
REMARK 3 S11: 0.2547 S12: -0.3027 S13: 1.1012
REMARK 3 S21: 0.2442 S22: -0.2807 S23: 1.0220
REMARK 3 S31: -1.5174 S32: 0.1641 S33: 0.0488
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 322 THROUGH 362 )
REMARK 3 ORIGIN FOR THE GROUP (A): 262.5103 15.6041 14.8143
REMARK 3 T TENSOR
REMARK 3 T11: 0.6168 T22: 0.8633
REMARK 3 T33: 0.6840 T12: -0.1394
REMARK 3 T13: 0.0340 T23: 0.0601
REMARK 3 L TENSOR
REMARK 3 L11: 1.8718 L22: 7.1283
REMARK 3 L33: 3.8407 L12: -1.8128
REMARK 3 L13: 0.3079 L23: -0.7701
REMARK 3 S TENSOR
REMARK 3 S11: 0.4190 S12: 0.4184 S13: 0.1400
REMARK 3 S21: -0.7680 S22: -0.6412 S23: 0.0920
REMARK 3 S31: -0.3001 S32: 0.6853 S33: 0.2750
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 154 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): 259.0122 40.2076 33.6161
REMARK 3 T TENSOR
REMARK 3 T11: 1.1527 T22: 1.1382
REMARK 3 T33: 0.8659 T12: -0.4446
REMARK 3 T13: -0.1359 T23: -0.1313
REMARK 3 L TENSOR
REMARK 3 L11: 3.6188 L22: 4.4208
REMARK 3 L33: 7.6314 L12: -1.7424
REMARK 3 L13: 2.7866 L23: -5.7964
REMARK 3 S TENSOR
REMARK 3 S11: -0.4672 S12: 0.3063 S13: 2.0319
REMARK 3 S21: 0.5002 S22: -0.9695 S23: -0.1971
REMARK 3 S31: -2.8392 S32: 1.9797 S33: 1.8084
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 13 THROUGH 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 281.3107 -26.9888 49.6597
REMARK 3 T TENSOR
REMARK 3 T11: 1.0388 T22: 0.7904
REMARK 3 T33: 0.6117 T12: 0.1144
REMARK 3 T13: 0.0969 T23: 0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 4.5410 L22: 4.7460
REMARK 3 L33: 5.9066 L12: -0.8251
REMARK 3 L13: 2.3150 L23: -1.8150
REMARK 3 S TENSOR
REMARK 3 S11: 0.1232 S12: -0.2116 S13: -0.0800
REMARK 3 S21: 0.1369 S22: 0.2770 S23: 0.3187
REMARK 3 S31: -0.3072 S32: 0.0088 S33: -0.4134
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 135 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 268.2551 -12.6891 32.0444
REMARK 3 T TENSOR
REMARK 3 T11: 1.5483 T22: 0.9113
REMARK 3 T33: 0.8469 T12: 0.1324
REMARK 3 T13: -0.0699 T23: 0.0481
REMARK 3 L TENSOR
REMARK 3 L11: 4.2763 L22: 2.8907
REMARK 3 L33: 0.9248 L12: -2.7376
REMARK 3 L13: -1.4179 L23: 0.1632
REMARK 3 S TENSOR
REMARK 3 S11: 0.5889 S12: 0.6012 S13: -0.1906
REMARK 3 S21: -1.3576 S22: -0.5124 S23: -0.0685
REMARK 3 S31: 0.3614 S32: -0.1234 S33: -0.0713
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 182 THROUGH 325 )
REMARK 3 ORIGIN FOR THE GROUP (A): 251.7870 4.9343 47.3345
REMARK 3 T TENSOR
REMARK 3 T11: 0.8038 T22: 0.8735
REMARK 3 T33: 0.5927 T12: -0.0804
REMARK 3 T13: -0.1402 T23: 0.1016
REMARK 3 L TENSOR
REMARK 3 L11: 2.4885 L22: 7.4012
REMARK 3 L33: 5.1691 L12: -0.8949
REMARK 3 L13: -1.3023 L23: 1.8585
REMARK 3 S TENSOR
REMARK 3 S11: -0.0187 S12: -0.3325 S13: -0.0486
REMARK 3 S21: 0.4936 S22: -0.0492 S23: 0.1793
REMARK 3 S31: 0.2371 S32: 0.2395 S33: 0.0054
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 8 THROUGH 29 )
REMARK 3 ORIGIN FOR THE GROUP (A): 289.6862 -29.9317 -6.7884
REMARK 3 T TENSOR
REMARK 3 T11: 1.6578 T22: 0.7136
REMARK 3 T33: 1.0600 T12: 0.1853
REMARK 3 T13: 0.1067 T23: -0.1465
REMARK 3 L TENSOR
REMARK 3 L11: 8.0999 L22: 6.2063
REMARK 3 L33: 8.4918 L12: -2.4714
REMARK 3 L13: 2.2236 L23: -4.9858
REMARK 3 S TENSOR
REMARK 3 S11: 0.2335 S12: 0.4653 S13: -0.2004
REMARK 3 S21: 0.3051 S22: 0.4780 S23: 0.4937
REMARK 3 S31: -1.9877 S32: 0.0488 S33: -0.8829
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 30 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 292.9514 -26.0822 1.0384
REMARK 3 T TENSOR
REMARK 3 T11: 1.6292 T22: 0.6511
REMARK 3 T33: 0.8421 T12: 0.1504
REMARK 3 T13: 0.0260 T23: -0.0960
REMARK 3 L TENSOR
REMARK 3 L11: 6.4783 L22: 5.3178
REMARK 3 L33: 7.3609 L12: -3.1579
REMARK 3 L13: 0.9115 L23: 0.3233
REMARK 3 S TENSOR
REMARK 3 S11: 0.8626 S12: 0.0217 S13: -0.5981
REMARK 3 S21: 0.2184 S22: -0.4207 S23: -0.1723
REMARK 3 S31: -1.8478 S32: 0.1073 S33: -0.4388
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 64 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 292.8877 -14.8261 7.2676
REMARK 3 T TENSOR
REMARK 3 T11: 2.3551 T22: 0.8982
REMARK 3 T33: 0.8112 T12: 0.1684
REMARK 3 T13: 0.2544 T23: -0.2560
REMARK 3 L TENSOR
REMARK 3 L11: 3.6700 L22: 5.2591
REMARK 3 L33: 2.4424 L12: -1.1930
REMARK 3 L13: 1.7638 L23: -1.7508
REMARK 3 S TENSOR
REMARK 3 S11: 0.2355 S12: -0.3404 S13: 0.2753
REMARK 3 S21: -1.9671 S22: 0.0160 S23: 0.7885
REMARK 3 S31: -2.2232 S32: 0.0645 S33: -0.1224
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 93 THROUGH 114 )
REMARK 3 ORIGIN FOR THE GROUP (A): 287.9113 -22.4537 -0.1558
REMARK 3 T TENSOR
REMARK 3 T11: 1.7867 T22: 0.6726
REMARK 3 T33: 0.9391 T12: 0.2151
REMARK 3 T13: 0.0321 T23: -0.1380
REMARK 3 L TENSOR
REMARK 3 L11: 5.6291 L22: 4.0809
REMARK 3 L33: 7.3166 L12: -1.4712
REMARK 3 L13: 2.0127 L23: -0.5212
REMARK 3 S TENSOR
REMARK 3 S11: -0.0337 S12: 0.2420 S13: 0.0850
REMARK 3 S21: -1.0407 S22: 0.1991 S23: 0.5589
REMARK 3 S31: -1.7050 S32: -0.4940 S33: -0.1364
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 115 THROUGH 164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 308.4224 -20.2314 15.8247
REMARK 3 T TENSOR
REMARK 3 T11: 1.4987 T22: 1.0439
REMARK 3 T33: 1.0141 T12: -0.4289
REMARK 3 T13: 0.2247 T23: -0.1848
REMARK 3 L TENSOR
REMARK 3 L11: 6.3293 L22: 6.0230
REMARK 3 L33: 7.7735 L12: -2.4014
REMARK 3 L13: 0.5409 L23: 2.1803
REMARK 3 S TENSOR
REMARK 3 S11: 0.2886 S12: 0.0679 S13: -0.3293
REMARK 3 S21: -1.0034 S22: 0.0384 S23: -0.9337
REMARK 3 S31: -0.7198 S32: 1.4590 S33: -0.2565
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 165 THROUGH 182 )
REMARK 3 ORIGIN FOR THE GROUP (A): 292.7835 -19.3988 17.3845
REMARK 3 T TENSOR
REMARK 3 T11: 1.3495 T22: 1.0420
REMARK 3 T33: 1.1505 T12: -0.0567
REMARK 3 T13: 0.1382 T23: -0.0088
REMARK 3 L TENSOR
REMARK 3 L11: 3.7054 L22: 6.2498
REMARK 3 L33: 9.1331 L12: -3.9950
REMARK 3 L13: -5.1140 L23: 4.0990
REMARK 3 S TENSOR
REMARK 3 S11: 0.9202 S12: -0.7444 S13: 0.3251
REMARK 3 S21: -0.2136 S22: -0.2011 S23: 0.6743
REMARK 3 S31: -1.1937 S32: -0.3828 S33: -1.0414
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 183 THROUGH 241 )
REMARK 3 ORIGIN FOR THE GROUP (A): 300.3209 -24.3690 29.4732
REMARK 3 T TENSOR
REMARK 3 T11: 0.9060 T22: 1.0254
REMARK 3 T33: 0.9022 T12: -0.0718
REMARK 3 T13: 0.0444 T23: -0.1218
REMARK 3 L TENSOR
REMARK 3 L11: 2.7442 L22: 2.3403
REMARK 3 L33: 8.8764 L12: 1.7298
REMARK 3 L13: 0.1293 L23: 1.2650
REMARK 3 S TENSOR
REMARK 3 S11: 0.0798 S12: -0.3330 S13: -0.2381
REMARK 3 S21: 0.0711 S22: 0.2011 S23: -0.1719
REMARK 3 S31: -0.7673 S32: 0.9400 S33: -0.2711
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 242 THROUGH 270 )
REMARK 3 ORIGIN FOR THE GROUP (A): 297.2050 -19.0104 44.4692
REMARK 3 T TENSOR
REMARK 3 T11: 1.2721 T22: 1.1839
REMARK 3 T33: 0.6030 T12: -0.1362
REMARK 3 T13: 0.0032 T23: -0.2182
REMARK 3 L TENSOR
REMARK 3 L11: 8.1554 L22: 5.1327
REMARK 3 L33: 7.2001 L12: 0.4217
REMARK 3 L13: -2.3488 L23: 0.9550
REMARK 3 S TENSOR
REMARK 3 S11: 0.5777 S12: -0.7109 S13: 0.0478
REMARK 3 S21: 0.6286 S22: -0.0537 S23: -0.2330
REMARK 3 S31: -0.9342 S32: 1.2044 S33: -0.4861
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 271 THROUGH 321 )
REMARK 3 ORIGIN FOR THE GROUP (A): 316.4456 -17.7381 28.7815
REMARK 3 T TENSOR
REMARK 3 T11: 1.2261 T22: 1.5911
REMARK 3 T33: 1.3165 T12: -0.5228
REMARK 3 T13: 0.0179 T23: -0.3535
REMARK 3 L TENSOR
REMARK 3 L11: 2.5187 L22: 4.9434
REMARK 3 L33: 2.2960 L12: -2.2377
REMARK 3 L13: -0.9660 L23: 0.0607
REMARK 3 S TENSOR
REMARK 3 S11: 0.1653 S12: -0.6238 S13: 0.0899
REMARK 3 S21: -0.1789 S22: 0.0909 S23: -0.7506
REMARK 3 S31: -0.9072 S32: 1.2176 S33: -0.2539
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 322 THROUGH 362 )
REMARK 3 ORIGIN FOR THE GROUP (A): 291.3342 -8.9533 9.4950
REMARK 3 T TENSOR
REMARK 3 T11: 2.1176 T22: 1.0509
REMARK 3 T33: 1.1236 T12: 0.1634
REMARK 3 T13: 0.0265 T23: 0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 7.1622 L22: 2.5595
REMARK 3 L33: 5.0030 L12: -0.7452
REMARK 3 L13: 2.6510 L23: 1.7265
REMARK 3 S TENSOR
REMARK 3 S11: -0.2171 S12: -0.6652 S13: 1.0411
REMARK 3 S21: -0.6250 S22: -0.2334 S23: 0.2089
REMARK 3 S31: -2.2705 S32: -0.1560 S33: 0.4159
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 154 THROUGH 162 )
REMARK 3 ORIGIN FOR THE GROUP (A): 319.6066 -22.6854 9.1081
REMARK 3 T TENSOR
REMARK 3 T11: 1.4000 T22: 1.6866
REMARK 3 T33: 1.2976 T12: -0.3092
REMARK 3 T13: 0.3455 T23: -0.1941
REMARK 3 L TENSOR
REMARK 3 L11: 5.2379 L22: 6.2711
REMARK 3 L33: 6.2596 L12: 5.6200
REMARK 3 L13: -5.5675 L23: -5.6941
REMARK 3 S TENSOR
REMARK 3 S11: -0.7259 S12: -1.3050 S13: -0.8225
REMARK 3 S21: -3.5047 S22: 1.2022 S23: -3.3113
REMARK 3 S31: -0.4473 S32: 2.0012 S33: -0.6948
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 13 THROUGH 181 )
REMARK 3 ORIGIN FOR THE GROUP (A): 259.2815 -43.5705 -2.7402
REMARK 3 T TENSOR
REMARK 3 T11: 0.8650 T22: 0.8755
REMARK 3 T33: 1.4305 T12: 0.1876
REMARK 3 T13: -0.0115 T23: 0.0554
REMARK 3 L TENSOR
REMARK 3 L11: 2.8335 L22: 3.1429
REMARK 3 L33: 6.1149 L12: 1.6969
REMARK 3 L13: 3.0719 L23: 2.3485
REMARK 3 S TENSOR
REMARK 3 S11: 0.0902 S12: -0.1617 S13: -0.1669
REMARK 3 S21: -0.2062 S22: 0.2248 S23: -0.0905
REMARK 3 S31: 0.4529 S32: -0.0919 S33: -0.3975
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 182 THROUGH 326 )
REMARK 3 ORIGIN FOR THE GROUP (A): 288.5765 -43.2050 19.5477
REMARK 3 T TENSOR
REMARK 3 T11: 0.6900 T22: 0.6885
REMARK 3 T33: 0.8584 T12: 0.1069
REMARK 3 T13: -0.0697 T23: -0.1247
REMARK 3 L TENSOR
REMARK 3 L11: 8.5078 L22: 5.4336
REMARK 3 L33: 4.9918 L12: -1.0628
REMARK 3 L13: -1.2050 L23: 0.8563
REMARK 3 S TENSOR
REMARK 3 S11: 0.1003 S12: -0.2605 S13: -0.2937
REMARK 3 S21: 0.0462 S22: 0.1225 S23: -0.2301
REMARK 3 S31: 0.2758 S32: 0.3369 S33: -0.2434
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 8 THROUGH 145 )
REMARK 3 ORIGIN FOR THE GROUP (A): 242.6880 -3.3725 -16.6150
REMARK 3 T TENSOR
REMARK 3 T11: 0.5521 T22: 0.7794
REMARK 3 T33: 0.9293 T12: -0.0895
REMARK 3 T13: 0.0673 T23: 0.1192
REMARK 3 L TENSOR
REMARK 3 L11: 1.8770 L22: 3.7311
REMARK 3 L33: 3.6219 L12: -0.8268
REMARK 3 L13: -0.5008 L23: 0.9930
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: 0.2688 S13: 0.4482
REMARK 3 S21: 0.2299 S22: -0.1232 S23: -0.1029
REMARK 3 S31: -0.0879 S32: 0.0271 S33: 0.1243
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 146 THROUGH 191 )
REMARK 3 ORIGIN FOR THE GROUP (A): 246.9072 -15.3359 -19.6478
REMARK 3 T TENSOR
REMARK 3 T11: 0.5669 T22: 1.0003
REMARK 3 T33: 0.9465 T12: -0.0456
REMARK 3 T13: 0.1209 T23: 0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 1.3215 L22: 5.3431
REMARK 3 L33: 1.3693 L12: -0.8143
REMARK 3 L13: -0.8872 L23: 0.6776
REMARK 3 S TENSOR
REMARK 3 S11: 0.3550 S12: 0.2179 S13: -0.2076
REMARK 3 S21: 0.2882 S22: -0.1491 S23: -0.2112
REMARK 3 S31: 0.1560 S32: 0.6849 S33: -0.0747
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 192 THROUGH 290 )
REMARK 3 ORIGIN FOR THE GROUP (A): 251.4248 -30.9695 -27.9150
REMARK 3 T TENSOR
REMARK 3 T11: 0.8024 T22: 0.8658
REMARK 3 T33: 0.9022 T12: 0.1521
REMARK 3 T13: 0.1436 T23: -0.1583
REMARK 3 L TENSOR
REMARK 3 L11: 5.0295 L22: 4.2763
REMARK 3 L33: 4.7518 L12: -1.4615
REMARK 3 L13: 2.2265 L23: -2.0448
REMARK 3 S TENSOR
REMARK 3 S11: 0.3547 S12: 0.5073 S13: -0.4764
REMARK 3 S21: -0.5810 S22: -0.0477 S23: -0.3988
REMARK 3 S31: 0.5352 S32: 0.2611 S33: -0.1821
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'H' AND (RESID 291 THROUGH 362 )
REMARK 3 ORIGIN FOR THE GROUP (A): 256.8726 -11.2544 -24.0553
REMARK 3 T TENSOR
REMARK 3 T11: 0.6712 T22: 1.0262
REMARK 3 T33: 1.0448 T12: 0.0840
REMARK 3 T13: 0.1437 T23: 0.1405
REMARK 3 L TENSOR
REMARK 3 L11: 1.8278 L22: 2.3652
REMARK 3 L33: 4.5882 L12: -0.4147
REMARK 3 L13: -0.5472 L23: 1.7182
REMARK 3 S TENSOR
REMARK 3 S11: -0.0562 S12: 0.4653 S13: 0.5486
REMARK 3 S21: -0.3158 S22: -0.0589 S23: -0.5750
REMARK 3 S31: -0.2386 S32: 0.7363 S33: 0.0690
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'I' AND (RESID 154 THROUGH 163 )
REMARK 3 ORIGIN FOR THE GROUP (A): 237.6082 -7.5924 -40.8526
REMARK 3 T TENSOR
REMARK 3 T11: 0.8760 T22: 1.5261
REMARK 3 T33: 1.1303 T12: 0.3215
REMARK 3 T13: 0.2534 T23: 0.2766
REMARK 3 L TENSOR
REMARK 3 L11: 4.0619 L22: 1.9382
REMARK 3 L33: 7.0686 L12: 2.2832
REMARK 3 L13: -0.7935 L23: -0.3774
REMARK 3 S TENSOR
REMARK 3 S11: 0.4675 S12: 2.5168 S13: 1.5758
REMARK 3 S21: -0.3309 S22: -0.6725 S23: 0.3902
REMARK 3 S31: 1.0120 S32: -0.7862 S33: 0.2453
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'L' AND (RESID 2 THROUGH 5 )
REMARK 3 ORIGIN FOR THE GROUP (A): 264.6813 -28.4630 -10.6279
REMARK 3 T TENSOR
REMARK 3 T11: 1.1031 T22: 1.4907
REMARK 3 T33: 2.1403 T12: -0.3748
REMARK 3 T13: 1.0033 T23: -0.1814
REMARK 3 L TENSOR
REMARK 3 L11: 0.1055 L22: 2.1949
REMARK 3 L33: 4.4078 L12: -0.4809
REMARK 3 L13: 0.6821 L23: -3.1112
REMARK 3 S TENSOR
REMARK 3 S11: -0.0335 S12: 2.2822 S13: 0.0713
REMARK 3 S21: -0.2804 S22: 0.1196 S23: -0.7471
REMARK 3 S31: -0.2033 S32: 0.8212 S33: 0.4466
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 5LW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-SEP-16.
REMARK 100 THE DEPOSITION ID IS D_1200001070.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58948
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 49.383
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 7.000
REMARK 200 R MERGE (I) : 0.13450
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.31
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 1.84200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.130
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1SVX CHAIN A AND 1UKH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: LITHIUM SULFATE 1.8 M TRIS 0.1 M
REMARK 280 ADDITIVES (0.002% W/V) ADENOSINE, PEPSTATIN A EPINEPHRINE SODIUM
REMARK 280 PHENYL PHOSPHATE DIBASIC DEHYDRATE INOSINE 5-TRIPHOSPHATE
REMARK 280 TRISODIUM SALT PH 8.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 109.99500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 70.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 109.99500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 70.88000
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, 3
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: 4910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -102.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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: 4740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, I, L
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE PEPSTATIN IS OLIGOPEPTIDE, A MEMBER OF ENZYME INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: PEPSTATIN
REMARK 400 CHAIN: L
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 MET A 1
REMARK 465 ARG A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 ALA A 326
REMARK 465 MET B -9
REMARK 465 ARG B -8
REMARK 465 GLY B -7
REMARK 465 SER B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 GLY B 1
REMARK 465 SER B 2
REMARK 465 ARG B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 ARG B 6
REMARK 465 ASP B 7
REMARK 465 LEU B 363
REMARK 465 ARG C 153
REMARK 465 PHE C 163
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 GLY D 3
REMARK 465 SER D 4
REMARK 465 HIS D 5
REMARK 465 HIS D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 GLY D 11
REMARK 465 SER D 12
REMARK 465 ALA D 326
REMARK 465 MET E -9
REMARK 465 ARG E -8
REMARK 465 GLY E -7
REMARK 465 SER E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 HIS E 0
REMARK 465 GLY E 1
REMARK 465 SER E 2
REMARK 465 ARG E 3
REMARK 465 SER E 4
REMARK 465 LYS E 5
REMARK 465 ARG E 6
REMARK 465 ASP E 7
REMARK 465 LEU E 363
REMARK 465 ARG F 153
REMARK 465 PHE F 163
REMARK 465 MET G 1
REMARK 465 ARG G 2
REMARK 465 GLY G 3
REMARK 465 SER G 4
REMARK 465 HIS G 5
REMARK 465 HIS G 6
REMARK 465 HIS G 7
REMARK 465 HIS G 8
REMARK 465 HIS G 9
REMARK 465 HIS G 10
REMARK 465 GLY G 11
REMARK 465 SER G 12
REMARK 465 MET H -9
REMARK 465 ARG H -8
REMARK 465 GLY H -7
REMARK 465 SER H -6
REMARK 465 HIS H -5
REMARK 465 HIS H -4
REMARK 465 HIS H -3
REMARK 465 HIS H -2
REMARK 465 HIS H -1
REMARK 465 HIS H 0
REMARK 465 GLY H 1
REMARK 465 SER H 2
REMARK 465 ARG H 3
REMARK 465 SER H 4
REMARK 465 LYS H 5
REMARK 465 ARG H 6
REMARK 465 ASP H 7
REMARK 465 LEU H 363
REMARK 465 ARG I 153
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 STA L 4 C - N - CA ANGL. DEV. = 18.1 DEGREES
REMARK 500 STA L 4 CA - C - N ANGL. DEV. = 36.5 DEGREES
REMARK 500 STA L 4 O - C - N ANGL. DEV. = -22.2 DEGREES
REMARK 500 ALA L 5 C - N - CA ANGL. DEV. = 25.7 DEGREES
REMARK 500 ALA L 5 O - C - N ANGL. DEV. = -12.2 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 ASP A 110 -165.94 -104.80
REMARK 500 ASP A 143 -161.70 -108.91
REMARK 500 HIS A 282 78.85 -106.86
REMARK 500 GLN B 102 -64.23 -138.87
REMARK 500 ASP B 151 28.73 -145.10
REMARK 500 ASN B 322 -8.24 -58.36
REMARK 500 GLU B 331 41.82 -94.37
REMARK 500 GLN B 341 55.80 -104.45
REMARK 500 ASP D 110 -166.67 -103.71
REMARK 500 ASP D 143 -161.72 -107.14
REMARK 500 GLN E 102 -65.54 -139.37
REMARK 500 ASP E 151 30.00 -144.05
REMARK 500 ASN E 322 -7.89 -59.30
REMARK 500 GLU E 331 42.16 -94.25
REMARK 500 GLN E 341 51.40 -104.00
REMARK 500 ASP G 110 -167.41 -101.91
REMARK 500 ASP G 143 -160.17 -108.09
REMARK 500 HIS G 282 78.41 -106.95
REMARK 500 GLN H 102 -64.54 -139.13
REMARK 500 ASP H 151 30.38 -143.88
REMARK 500 LYS H 203 -169.63 -104.82
REMARK 500 ASN H 322 -7.41 -58.71
REMARK 500 GLU H 331 42.98 -92.54
REMARK 500 GLN H 341 52.06 -103.78
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 STA L 4 ALA L 5 -115.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 VAL L 3 -20.00
REMARK 500 STA L 4 35.90
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 SO4 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADN E 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADN H 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Pepstatin chain L
DBREF 5LW1 A 1 326 PDB 5LW1 5LW1 1 326
DBREF 5LW1 B 2 363 UNP P45983 MK08_HUMAN 2 363
DBREF 5LW1 C 153 163 UNP Q9UQF2 JIP1_HUMAN 157 167
DBREF 5LW1 D 1 326 PDB 5LW1 5LW1 1 326
DBREF 5LW1 E 2 363 UNP P45983 MK08_HUMAN 2 363
DBREF 5LW1 F 153 163 UNP Q9UQF2 JIP1_HUMAN 157 167
DBREF 5LW1 G 1 326 PDB 5LW1 5LW1 1 326
DBREF 5LW1 H 2 363 UNP P45983 MK08_HUMAN 2 363
DBREF 5LW1 I 153 163 UNP Q9UQF2 JIP1_HUMAN 157 167
DBREF 5LW1 L 1 6 PDB 5LW1 5LW1 1 6
SEQADV 5LW1 MET B -9 UNP P45983 INITIATING METHIONINE
SEQADV 5LW1 ARG B -8 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 GLY B -7 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 SER B -6 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS B -5 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS B -4 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS B -3 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS B -2 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS B -1 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS B 0 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 GLY B 1 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 MET E -9 UNP P45983 INITIATING METHIONINE
SEQADV 5LW1 ARG E -8 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 GLY E -7 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 SER E -6 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS E -5 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS E -4 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS E -3 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS E -2 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS E -1 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS E 0 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 GLY E 1 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 MET H -9 UNP P45983 INITIATING METHIONINE
SEQADV 5LW1 ARG H -8 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 GLY H -7 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 SER H -6 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS H -5 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS H -4 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS H -3 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS H -2 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS H -1 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 HIS H 0 UNP P45983 EXPRESSION TAG
SEQADV 5LW1 GLY H 1 UNP P45983 EXPRESSION TAG
SEQRES 1 A 326 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 A 326 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN
SEQRES 3 A 326 ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP
SEQRES 4 A 326 VAL ASN ALA SER ASP GLN LEU GLY ILE THR PRO LEU HIS
SEQRES 5 A 326 LEU VAL ALA ILE THR GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 A 326 LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA HIS ASP PHE
SEQRES 7 A 326 VAL GLY THR THR PRO LEU HIS LEU ALA ALA PHE LEU GLY
SEQRES 8 A 326 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA
SEQRES 9 A 326 ASP VAL ASN ALA VAL ASP ARG ASP GLY LEU THR PRO LEU
SEQRES 10 A 326 HIS LEU ALA ALA ILE HIS GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 A 326 VAL LEU LEU LYS HIS GLY ALA LEU VAL LYS ALA LYS ASP
SEQRES 12 A 326 LYS PHE GLY LYS THR PRO LYS ASP LEU ALA ARG ASP ASN
SEQRES 13 A 326 GLY ASN GLN PHE ILE TYR GLU LEU LEU GLU LYS ALA GLU
SEQRES 14 A 326 LEU LEU GLU LYS LEU LEU LEU GLU ALA ALA ARG GLU GLY
SEQRES 15 A 326 HIS ARG ASP ARG VAL GLU GLU PHE ILE LYS ARG GLY ALA
SEQRES 16 A 326 ASP VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU
SEQRES 17 A 326 HIS LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU
SEQRES 18 A 326 VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP
SEQRES 19 A 326 GLU ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR
SEQRES 20 A 326 GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY
SEQRES 21 A 326 ALA GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO
SEQRES 22 A 326 LEU HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL
SEQRES 23 A 326 GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN
SEQRES 24 A 326 ASP LYS PHE GLY LYS THR PRO PHE ASP LEU ALA ILE ASP
SEQRES 25 A 326 ASN GLY ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA
SEQRES 26 A 326 ALA
SEQRES 1 B 373 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 B 373 SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY
SEQRES 3 B 373 ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU
SEQRES 4 B 373 LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA
SEQRES 5 B 373 ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS
SEQRES 6 B 373 LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS
SEQRES 7 B 373 ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN
SEQRES 8 B 373 HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO
SEQRES 9 B 373 GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL
SEQRES 10 B 373 MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN
SEQRES 11 B 373 MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR
SEQRES 12 B 373 GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY
SEQRES 13 B 373 ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL
SEQRES 14 B 373 LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU
SEQRES 15 B 373 ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR
SEQRES 16 B 373 VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU
SEQRES 17 B 373 GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL
SEQRES 18 B 373 GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU
SEQRES 19 B 373 PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL
SEQRES 20 B 373 ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS
SEQRES 21 B 373 LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG
SEQRES 22 B 373 PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO
SEQRES 23 B 373 ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU
SEQRES 24 B 373 LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU
SEQRES 25 B 373 VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA
SEQRES 26 B 373 LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER
SEQRES 27 B 373 GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN
SEQRES 28 B 373 LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU
SEQRES 29 B 373 LEU ILE TYR LYS GLU VAL MET ASP LEU
SEQRES 1 C 11 ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE
SEQRES 1 D 326 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 D 326 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN
SEQRES 3 D 326 ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP
SEQRES 4 D 326 VAL ASN ALA SER ASP GLN LEU GLY ILE THR PRO LEU HIS
SEQRES 5 D 326 LEU VAL ALA ILE THR GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 D 326 LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA HIS ASP PHE
SEQRES 7 D 326 VAL GLY THR THR PRO LEU HIS LEU ALA ALA PHE LEU GLY
SEQRES 8 D 326 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA
SEQRES 9 D 326 ASP VAL ASN ALA VAL ASP ARG ASP GLY LEU THR PRO LEU
SEQRES 10 D 326 HIS LEU ALA ALA ILE HIS GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 D 326 VAL LEU LEU LYS HIS GLY ALA LEU VAL LYS ALA LYS ASP
SEQRES 12 D 326 LYS PHE GLY LYS THR PRO LYS ASP LEU ALA ARG ASP ASN
SEQRES 13 D 326 GLY ASN GLN PHE ILE TYR GLU LEU LEU GLU LYS ALA GLU
SEQRES 14 D 326 LEU LEU GLU LYS LEU LEU LEU GLU ALA ALA ARG GLU GLY
SEQRES 15 D 326 HIS ARG ASP ARG VAL GLU GLU PHE ILE LYS ARG GLY ALA
SEQRES 16 D 326 ASP VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU
SEQRES 17 D 326 HIS LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU
SEQRES 18 D 326 VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP
SEQRES 19 D 326 GLU ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR
SEQRES 20 D 326 GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY
SEQRES 21 D 326 ALA GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO
SEQRES 22 D 326 LEU HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL
SEQRES 23 D 326 GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN
SEQRES 24 D 326 ASP LYS PHE GLY LYS THR PRO PHE ASP LEU ALA ILE ASP
SEQRES 25 D 326 ASN GLY ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA
SEQRES 26 D 326 ALA
SEQRES 1 E 373 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 E 373 SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY
SEQRES 3 E 373 ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU
SEQRES 4 E 373 LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA
SEQRES 5 E 373 ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS
SEQRES 6 E 373 LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS
SEQRES 7 E 373 ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN
SEQRES 8 E 373 HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO
SEQRES 9 E 373 GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL
SEQRES 10 E 373 MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN
SEQRES 11 E 373 MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR
SEQRES 12 E 373 GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY
SEQRES 13 E 373 ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL
SEQRES 14 E 373 LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU
SEQRES 15 E 373 ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR
SEQRES 16 E 373 VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU
SEQRES 17 E 373 GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL
SEQRES 18 E 373 GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU
SEQRES 19 E 373 PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL
SEQRES 20 E 373 ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS
SEQRES 21 E 373 LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG
SEQRES 22 E 373 PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO
SEQRES 23 E 373 ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU
SEQRES 24 E 373 LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU
SEQRES 25 E 373 VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA
SEQRES 26 E 373 LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER
SEQRES 27 E 373 GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN
SEQRES 28 E 373 LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU
SEQRES 29 E 373 LEU ILE TYR LYS GLU VAL MET ASP LEU
SEQRES 1 F 11 ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE
SEQRES 1 G 326 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP
SEQRES 2 G 326 LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN
SEQRES 3 G 326 ASP ASP GLU VAL ARG ILE LEU MET ALA ASN GLY ALA ASP
SEQRES 4 G 326 VAL ASN ALA SER ASP GLN LEU GLY ILE THR PRO LEU HIS
SEQRES 5 G 326 LEU VAL ALA ILE THR GLY HIS LEU GLU ILE VAL GLU VAL
SEQRES 6 G 326 LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA HIS ASP PHE
SEQRES 7 G 326 VAL GLY THR THR PRO LEU HIS LEU ALA ALA PHE LEU GLY
SEQRES 8 G 326 HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA
SEQRES 9 G 326 ASP VAL ASN ALA VAL ASP ARG ASP GLY LEU THR PRO LEU
SEQRES 10 G 326 HIS LEU ALA ALA ILE HIS GLY HIS LEU GLU ILE VAL GLU
SEQRES 11 G 326 VAL LEU LEU LYS HIS GLY ALA LEU VAL LYS ALA LYS ASP
SEQRES 12 G 326 LYS PHE GLY LYS THR PRO LYS ASP LEU ALA ARG ASP ASN
SEQRES 13 G 326 GLY ASN GLN PHE ILE TYR GLU LEU LEU GLU LYS ALA GLU
SEQRES 14 G 326 LEU LEU GLU LYS LEU LEU LEU GLU ALA ALA ARG GLU GLY
SEQRES 15 G 326 HIS ARG ASP ARG VAL GLU GLU PHE ILE LYS ARG GLY ALA
SEQRES 16 G 326 ASP VAL ASN THR ALA ASP GLU THR GLY PHE THR PRO LEU
SEQRES 17 G 326 HIS LEU ALA ALA TRP GLU GLY HIS LEU GLY ILE VAL GLU
SEQRES 18 G 326 VAL LEU LEU LYS ASN GLY ALA ASP VAL ASN ALA ASN ASP
SEQRES 19 G 326 GLU ARG GLY HIS THR PRO LEU HIS LEU ALA ALA TYR THR
SEQRES 20 G 326 GLY HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS ASN GLY
SEQRES 21 G 326 ALA GLY VAL ASN ALA THR ASP VAL ILE GLY THR ALA PRO
SEQRES 22 G 326 LEU HIS LEU ALA ALA MET TRP GLY HIS LEU GLU ILE VAL
SEQRES 23 G 326 GLU VAL LEU LEU LYS HIS GLY ALA ASP VAL ASN ALA GLN
SEQRES 24 G 326 ASP LYS PHE GLY LYS THR PRO PHE ASP LEU ALA ILE ASP
SEQRES 25 G 326 ASN GLY ASN GLU ASP ILE ALA GLU VAL LEU GLN LYS ALA
SEQRES 26 G 326 ALA
SEQRES 1 H 373 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 H 373 SER LYS ARG ASP ASN ASN PHE TYR SER VAL GLU ILE GLY
SEQRES 3 H 373 ASP SER THR PHE THR VAL LEU LYS ARG TYR GLN ASN LEU
SEQRES 4 H 373 LYS PRO ILE GLY SER GLY ALA GLN GLY ILE VAL CYS ALA
SEQRES 5 H 373 ALA TYR ASP ALA ILE LEU GLU ARG ASN VAL ALA ILE LYS
SEQRES 6 H 373 LYS LEU SER ARG PRO PHE GLN ASN GLN THR HIS ALA LYS
SEQRES 7 H 373 ARG ALA TYR ARG GLU LEU VAL LEU MET LYS CYS VAL ASN
SEQRES 8 H 373 HIS LYS ASN ILE ILE GLY LEU LEU ASN VAL PHE THR PRO
SEQRES 9 H 373 GLN LYS SER LEU GLU GLU PHE GLN ASP VAL TYR ILE VAL
SEQRES 10 H 373 MET GLU LEU MET ASP ALA ASN LEU CYS GLN VAL ILE GLN
SEQRES 11 H 373 MET GLU LEU ASP HIS GLU ARG MET SER TYR LEU LEU TYR
SEQRES 12 H 373 GLN MET LEU CYS GLY ILE LYS HIS LEU HIS SER ALA GLY
SEQRES 13 H 373 ILE ILE HIS ARG ASP LEU LYS PRO SER ASN ILE VAL VAL
SEQRES 14 H 373 LYS SER ASP CYS THR LEU LYS ILE LEU ASP PHE GLY LEU
SEQRES 15 H 373 ALA ARG THR ALA GLY THR SER PHE MET MET THR PRO TYR
SEQRES 16 H 373 VAL VAL THR ARG TYR TYR ARG ALA PRO GLU VAL ILE LEU
SEQRES 17 H 373 GLY MET GLY TYR LYS GLU ASN VAL ASP LEU TRP SER VAL
SEQRES 18 H 373 GLY CYS ILE MET GLY GLU MET VAL CYS HIS LYS ILE LEU
SEQRES 19 H 373 PHE PRO GLY ARG ASP TYR ILE ASP GLN TRP ASN LYS VAL
SEQRES 20 H 373 ILE GLU GLN LEU GLY THR PRO CYS PRO GLU PHE MET LYS
SEQRES 21 H 373 LYS LEU GLN PRO THR VAL ARG THR TYR VAL GLU ASN ARG
SEQRES 22 H 373 PRO LYS TYR ALA GLY TYR SER PHE GLU LYS LEU PHE PRO
SEQRES 23 H 373 ASP VAL LEU PHE PRO ALA ASP SER GLU HIS ASN LYS LEU
SEQRES 24 H 373 LYS ALA SER GLN ALA ARG ASP LEU LEU SER LYS MET LEU
SEQRES 25 H 373 VAL ILE ASP ALA SER LYS ARG ILE SER VAL ASP GLU ALA
SEQRES 26 H 373 LEU GLN HIS PRO TYR ILE ASN VAL TRP TYR ASP PRO SER
SEQRES 27 H 373 GLU ALA GLU ALA PRO PRO PRO LYS ILE PRO ASP LYS GLN
SEQRES 28 H 373 LEU ASP GLU ARG GLU HIS THR ILE GLU GLU TRP LYS GLU
SEQRES 29 H 373 LEU ILE TYR LYS GLU VAL MET ASP LEU
SEQRES 1 I 11 ARG PRO LYS ARG PRO THR THR LEU ASN LEU PHE
SEQRES 1 L 6 IVA VAL VAL STA ALA STA
HET IVA L 1 6
HET STA L 4 11
HET STA L 6 12
HET SO4 A 401 5
HET SO4 A 402 5
HET ADN B 401 19
HET SO4 B 402 5
HET SO4 B 403 5
HET SO4 B 404 5
HET SO4 B 405 5
HET SO4 B 406 5
HET SO4 D 401 5
HET SO4 D 402 5
HET SO4 D 403 5
HET SO4 D 404 5
HET ADN E 401 19
HET SO4 E 402 5
HET SO4 E 403 5
HET SO4 E 404 5
HET SO4 E 405 5
HET SO4 G 401 5
HET SO4 G 402 5
HET SO4 G 403 5
HET SO4 G 404 5
HET ADN H 401 19
HET SO4 H 402 5
HET SO4 H 403 5
HET SO4 H 404 5
HET SO4 H 405 5
HET SO4 I 201 5
HETNAM IVA ISOVALERIC ACID
HETNAM STA STATINE
HETNAM SO4 SULFATE ION
HETNAM ADN ADENOSINE
FORMUL 10 IVA C5 H10 O2
FORMUL 10 STA 2(C8 H17 N O3)
FORMUL 11 SO4 24(O4 S 2-)
FORMUL 13 ADN 3(C10 H13 N5 O4)
HELIX 1 AA1 ASP A 13 ALA A 24 1 12
HELIX 2 AA2 GLN A 26 ASN A 36 1 11
HELIX 3 AA3 THR A 49 GLY A 58 1 10
HELIX 4 AA4 HIS A 59 ASN A 69 1 11
HELIX 5 AA5 THR A 82 GLY A 91 1 10
HELIX 6 AA6 HIS A 92 TYR A 102 1 11
HELIX 7 AA7 THR A 115 HIS A 123 1 9
HELIX 8 AA8 HIS A 125 HIS A 135 1 11
HELIX 9 AA9 THR A 148 ASN A 156 1 9
HELIX 10 AB1 ASN A 158 GLY A 182 1 25
HELIX 11 AB2 HIS A 183 ARG A 193 1 11
HELIX 12 AB3 THR A 206 GLY A 215 1 10
HELIX 13 AB4 HIS A 216 ASN A 226 1 11
HELIX 14 AB5 THR A 239 GLY A 248 1 10
HELIX 15 AB6 HIS A 249 ASN A 259 1 11
HELIX 16 AB7 ALA A 272 TRP A 280 1 9
HELIX 17 AB8 HIS A 282 HIS A 292 1 11
HELIX 18 AB9 THR A 305 ASN A 313 1 9
HELIX 19 AC1 ASN A 315 ALA A 325 1 11
HELIX 20 AC2 PRO B 60 GLN B 62 5 3
HELIX 21 AC3 ASN B 63 VAL B 80 1 18
HELIX 22 AC4 LEU B 115 MET B 121 1 7
HELIX 23 AC5 ASP B 124 ALA B 145 1 22
HELIX 24 AC6 LYS B 153 SER B 155 5 3
HELIX 25 AC7 VAL B 187 ARG B 192 5 6
HELIX 26 AC8 ALA B 193 LEU B 198 1 6
HELIX 27 AC9 ASN B 205 HIS B 221 1 17
HELIX 28 AD1 ILE B 231 GLY B 242 1 12
HELIX 29 AD2 CYS B 245 LYS B 250 1 6
HELIX 30 AD3 GLN B 253 ASN B 262 1 10
HELIX 31 AD4 SER B 270 PHE B 275 1 6
HELIX 32 AD5 PRO B 276 PHE B 280 5 5
HELIX 33 AD6 LYS B 290 LEU B 302 1 13
HELIX 34 AD7 SER B 311 GLN B 317 1 7
HELIX 35 AD8 ILE B 321 TYR B 325 5 5
HELIX 36 AD9 ASP B 326 GLU B 331 1 6
HELIX 37 AE1 THR B 348 ASP B 362 1 15
HELIX 38 AE2 LEU D 14 ALA D 24 1 11
HELIX 39 AE3 GLN D 26 ASN D 36 1 11
HELIX 40 AE4 THR D 49 GLY D 58 1 10
HELIX 41 AE5 HIS D 59 ASN D 69 1 11
HELIX 42 AE6 THR D 82 GLY D 91 1 10
HELIX 43 AE7 HIS D 92 TYR D 102 1 11
HELIX 44 AE8 THR D 115 HIS D 123 1 9
HELIX 45 AE9 HIS D 125 HIS D 135 1 11
HELIX 46 AF1 THR D 148 ASN D 156 1 9
HELIX 47 AF2 ASN D 158 GLY D 182 1 25
HELIX 48 AF3 HIS D 183 ARG D 193 1 11
HELIX 49 AF4 THR D 206 GLY D 215 1 10
HELIX 50 AF5 HIS D 216 ASN D 226 1 11
HELIX 51 AF6 THR D 239 GLY D 248 1 10
HELIX 52 AF7 HIS D 249 ASN D 259 1 11
HELIX 53 AF8 ALA D 272 TRP D 280 1 9
HELIX 54 AF9 HIS D 282 HIS D 292 1 11
HELIX 55 AG1 THR D 305 ASN D 313 1 9
HELIX 56 AG2 ASN D 315 LYS D 324 1 10
HELIX 57 AG3 PRO E 60 GLN E 62 5 3
HELIX 58 AG4 ASN E 63 VAL E 80 1 18
HELIX 59 AG5 LEU E 115 MET E 121 1 7
HELIX 60 AG6 ASP E 124 ALA E 145 1 22
HELIX 61 AG7 LYS E 153 SER E 155 5 3
HELIX 62 AG8 VAL E 187 ARG E 192 5 6
HELIX 63 AG9 ALA E 193 LEU E 198 1 6
HELIX 64 AH1 ASN E 205 HIS E 221 1 17
HELIX 65 AH2 ILE E 231 GLY E 242 1 12
HELIX 66 AH3 CYS E 245 LYS E 250 1 6
HELIX 67 AH4 GLN E 253 ASN E 262 1 10
HELIX 68 AH5 SER E 270 PHE E 275 1 6
HELIX 69 AH6 PRO E 276 PHE E 280 5 5
HELIX 70 AH7 LYS E 290 LEU E 302 1 13
HELIX 71 AH8 SER E 311 GLN E 317 1 7
HELIX 72 AH9 ILE E 321 TYR E 325 5 5
HELIX 73 AI1 ASP E 326 GLU E 331 1 6
HELIX 74 AI2 THR E 348 ASP E 362 1 15
HELIX 75 AI3 LEU G 14 ALA G 24 1 11
HELIX 76 AI4 GLN G 26 ASN G 36 1 11
HELIX 77 AI5 THR G 49 GLY G 58 1 10
HELIX 78 AI6 HIS G 59 ASN G 69 1 11
HELIX 79 AI7 THR G 82 GLY G 91 1 10
HELIX 80 AI8 HIS G 92 TYR G 102 1 11
HELIX 81 AI9 THR G 115 HIS G 123 1 9
HELIX 82 AJ1 HIS G 125 HIS G 135 1 11
HELIX 83 AJ2 THR G 148 GLY G 157 1 10
HELIX 84 AJ3 ASN G 158 GLY G 182 1 25
HELIX 85 AJ4 HIS G 183 ARG G 193 1 11
HELIX 86 AJ5 THR G 206 GLY G 215 1 10
HELIX 87 AJ6 HIS G 216 ASN G 226 1 11
HELIX 88 AJ7 THR G 239 GLY G 248 1 10
HELIX 89 AJ8 HIS G 249 ASN G 259 1 11
HELIX 90 AJ9 ALA G 272 TRP G 280 1 9
HELIX 91 AK1 HIS G 282 HIS G 292 1 11
HELIX 92 AK2 THR G 305 ASN G 313 1 9
HELIX 93 AK3 ASN G 315 ALA G 325 1 11
HELIX 94 AK4 PRO H 60 GLN H 62 5 3
HELIX 95 AK5 ASN H 63 VAL H 80 1 18
HELIX 96 AK6 LEU H 115 MET H 121 1 7
HELIX 97 AK7 ASP H 124 ALA H 145 1 22
HELIX 98 AK8 VAL H 187 ARG H 192 5 6
HELIX 99 AK9 ALA H 193 LEU H 198 1 6
HELIX 100 AL1 LYS H 203 ASN H 205 5 3
HELIX 101 AL2 VAL H 206 HIS H 221 1 16
HELIX 102 AL3 ILE H 231 GLY H 242 1 12
HELIX 103 AL4 CYS H 245 LYS H 250 1 6
HELIX 104 AL5 GLN H 253 ASN H 262 1 10
HELIX 105 AL6 SER H 270 PHE H 275 1 6
HELIX 106 AL7 PRO H 276 PHE H 280 5 5
HELIX 107 AL8 LYS H 290 LEU H 302 1 13
HELIX 108 AL9 SER H 311 GLN H 317 1 7
HELIX 109 AM1 ILE H 321 TYR H 325 5 5
HELIX 110 AM2 ASP H 326 GLU H 331 1 6
HELIX 111 AM3 THR H 348 ASP H 362 1 15
SHEET 1 AA1 2 PHE B 10 ILE B 15 0
SHEET 2 AA1 2 SER B 18 LEU B 23 -1 O PHE B 20 N VAL B 13
SHEET 1 AA2 5 TYR B 26 SER B 34 0
SHEET 2 AA2 5 ILE B 39 ASP B 45 -1 O ALA B 42 N LYS B 30
SHEET 3 AA2 5 ARG B 50 SER B 58 -1 O ILE B 54 N CYS B 41
SHEET 4 AA2 5 ASP B 103 GLU B 109 -1 O VAL B 104 N LEU B 57
SHEET 5 AA2 5 LEU B 88 PHE B 92 -1 N LEU B 89 O VAL B 107
SHEET 1 AA3 3 ALA B 113 ASN B 114 0
SHEET 2 AA3 3 ILE B 157 VAL B 159 -1 O VAL B 159 N ALA B 113
SHEET 3 AA3 3 LEU B 165 ILE B 167 -1 O LYS B 166 N VAL B 158
SHEET 1 AA4 2 PHE E 10 ILE E 15 0
SHEET 2 AA4 2 SER E 18 LEU E 23 -1 O PHE E 20 N VAL E 13
SHEET 1 AA5 5 TYR E 26 SER E 34 0
SHEET 2 AA5 5 ILE E 39 ASP E 45 -1 O ALA E 42 N LYS E 30
SHEET 3 AA5 5 ARG E 50 SER E 58 -1 O ILE E 54 N CYS E 41
SHEET 4 AA5 5 ASP E 103 GLU E 109 -1 O VAL E 104 N LEU E 57
SHEET 5 AA5 5 LEU E 88 PHE E 92 -1 N ASN E 90 O VAL E 107
SHEET 1 AA6 3 ALA E 113 ASN E 114 0
SHEET 2 AA6 3 ILE E 157 VAL E 159 -1 O VAL E 159 N ALA E 113
SHEET 3 AA6 3 LEU E 165 ILE E 167 -1 O LYS E 166 N VAL E 158
SHEET 1 AA7 2 PHE H 10 ILE H 15 0
SHEET 2 AA7 2 SER H 18 LEU H 23 -1 O PHE H 20 N VAL H 13
SHEET 1 AA8 5 TYR H 26 SER H 34 0
SHEET 2 AA8 5 ILE H 39 ASP H 45 -1 O ALA H 42 N LYS H 30
SHEET 3 AA8 5 ARG H 50 SER H 58 -1 O ILE H 54 N CYS H 41
SHEET 4 AA8 5 ASP H 103 GLU H 109 -1 O VAL H 104 N LEU H 57
SHEET 5 AA8 5 LEU H 88 PHE H 92 -1 N LEU H 89 O VAL H 107
SHEET 1 AA9 3 ALA H 113 ASN H 114 0
SHEET 2 AA9 3 ILE H 157 LYS H 160 -1 O VAL H 159 N ALA H 113
SHEET 3 AA9 3 THR H 164 ILE H 167 -1 O LYS H 166 N VAL H 158
LINK C IVA L 1 N VAL L 2 1555 1555 1.36
LINK C VAL L 3 N STA L 4 1555 1555 1.35
LINK C STA L 4 N ALA L 5 1555 1555 1.37
LINK C ALA L 5 N STA L 6 1555 1555 1.38
SITE 1 AC1 3 GLY A 215 LEU A 217 GLY A 218
SITE 1 AC2 4 PHE A 89 HIS A 123 HIS A 125 TYR B 230
SITE 1 AC3 9 GLY B 33 VAL B 40 ALA B 53 MET B 108
SITE 2 AC3 9 GLU B 109 MET B 111 ASN B 114 SER B 155
SITE 3 AC3 9 LEU B 168
SITE 1 AC4 2 LYS B 250 ARG B 257
SITE 1 AC5 1 ARG B 127
SITE 1 AC6 3 ARG B 189 ARG B 192 TYR B 230
SITE 1 AC7 7 MET B 181 THR B 183 VAL B 186 VAL B 187
SITE 2 AC7 7 THR B 188 TRP D 213 TYR D 246
SITE 1 AC8 2 THR B 348 ILE B 349
SITE 1 AC9 3 HIS D 216 LEU D 217 GLY D 218
SITE 1 AD1 4 GLY D 281 HIS D 282 LEU D 283 GLU D 284
SITE 1 AD2 2 ARG D 184 GLU D 221
SITE 1 AD3 2 VAL D 263 ASN D 264
SITE 1 AD4 9 GLY E 33 VAL E 40 ALA E 53 ILE E 86
SITE 2 AD4 9 MET E 108 GLU E 109 MET E 111 ASN E 114
SITE 3 AD4 9 SER E 155
SITE 1 AD5 3 ARG E 189 ARG E 192 TYR E 230
SITE 1 AD6 1 ARG E 257
SITE 1 AD7 6 THR E 183 VAL E 186 VAL E 187 THR E 188
SITE 2 AD7 6 TRP G 213 TYR G 246
SITE 1 AD8 1 SER E 12
SITE 1 AD9 3 GLY G 215 LEU G 217 GLY G 218
SITE 1 AE1 3 LYS G 16 ASP G 44 GLN G 45
SITE 1 AE2 4 GLY G 281 HIS G 282 LEU G 283 GLU G 284
SITE 1 AE3 2 VAL G 263 ASN G 264
SITE 1 AE4 9 SER H 34 VAL H 40 ALA H 53 MET H 108
SITE 2 AE4 9 GLU H 109 MET H 111 ASN H 114 SER H 155
SITE 3 AE4 9 LEU H 168
SITE 1 AE5 3 ARG H 189 ARG H 192 TYR H 230
SITE 1 AE6 3 ARG G 111 LYS H 250 ARG H 257
SITE 1 AE7 2 LYS H 290 GLN H 293
SITE 1 AE8 2 TYR H 11 SER H 12
SITE 1 AE9 2 ASN A 69 LEU I 160
SITE 1 AF1 9 LEU G 114 ILE G 122 HIS G 123 ASN G 156
SITE 2 AF1 9 THR H 178 GLY H 199 GLY H 201 TYR H 230
SITE 3 AF1 9 ILE H 231
CRYST1 219.990 141.760 119.850 90.00 97.83 90.00 C 1 2 1 12
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 0.004546 0.000000 0.000625 0.00000
SCALE2 0.000000 0.007054 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008422 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
