HEADER TRANSFERASE 08-JUL-16 5LGS
TITLE CRYSTAL STRUCTURE OF MOUSE CARM1 IN COMPLEX WITH LIGAND P2C3U
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE-ARGININE METHYLTRANSFERASE CARM1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: COACTIVATOR-ASSOCIATED ARGININE METHYLTRANSFERASE 1,PROTEIN
COMPND 5 ARGININE N-METHYLTRANSFERASE 4;
COMPND 6 EC: 2.1.1.319;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: POLYADENYLATE-BINDING PROTEIN 1;
COMPND 10 CHAIN: E, F, G, H;
COMPND 11 SYNONYM: POLY(A)-BINDING PROTEIN 1;
COMPND 12 ENGINEERED: YES;
COMPND 13 OTHER_DETAILS: PABP1(456-466) PAAPRPPFSTM
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CARM1, PRMT4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606
KEYWDS PROTEIN ARGININE METHYLTRANSFERASE, CATALYTIC DOMAIN, CHROMATIN
KEYWDS 2 REGULATOR, MRNA PROCESSING, MRNA SPLICING, NUCLEUS, S-ADENOSYL-L-
KEYWDS 3 METHIONINE, TRANSCRIPTION, TRANSCRIPTION REGULATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MARECHAL,N.TROFFER-CHARLIER,V.CURA,L.BONNEFOND,J.CAVARELLI
REVDAT 4 10-JAN-24 5LGS 1 REMARK
REVDAT 3 12-APR-17 5LGS 1 JRNL
REVDAT 2 05-APR-17 5LGS 1 JRNL
REVDAT 1 22-MAR-17 5LGS 0
JRNL AUTH M.J.VAN HAREN,N.MARECHAL,N.TROFFER-CHARLIER,A.CIANCIULLI,
JRNL AUTH 2 G.SBARDELLA,J.CAVARELLI,N.I.MARTIN
JRNL TITL TRANSITION STATE MIMICS ARE VALUABLE MECHANISTIC PROBES FOR
JRNL TITL 2 STRUCTURAL STUDIES WITH THE ARGININE METHYLTRANSFERASE
JRNL TITL 3 CARM1.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 3625 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28330993
JRNL DOI 10.1073/PNAS.1618401114
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (DEV_2386: ???)
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.970
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 90760
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 4503
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 47.9837 - 6.5199 0.99 3072 177 0.1766 0.1949
REMARK 3 2 6.5199 - 5.1771 1.00 2965 168 0.1614 0.1856
REMARK 3 3 5.1771 - 4.5232 1.00 2967 136 0.1214 0.1605
REMARK 3 4 4.5232 - 4.1099 1.00 2908 155 0.1281 0.1519
REMARK 3 5 4.1099 - 3.8154 1.00 2900 173 0.1370 0.1606
REMARK 3 6 3.8154 - 3.5906 1.00 2886 155 0.1500 0.1898
REMARK 3 7 3.5906 - 3.4108 1.00 2882 133 0.1698 0.2089
REMARK 3 8 3.4108 - 3.2624 1.00 2881 150 0.1850 0.2200
REMARK 3 9 3.2624 - 3.1368 1.00 2932 138 0.1884 0.2175
REMARK 3 10 3.1368 - 3.0286 1.00 2851 167 0.1984 0.2016
REMARK 3 11 3.0286 - 2.9339 1.00 2868 148 0.1943 0.2151
REMARK 3 12 2.9339 - 2.8500 1.00 2870 143 0.1931 0.2281
REMARK 3 13 2.8500 - 2.7750 1.00 2859 156 0.2062 0.2484
REMARK 3 14 2.7750 - 2.7073 1.00 2905 130 0.2150 0.2682
REMARK 3 15 2.7073 - 2.6458 1.00 2823 157 0.2058 0.2349
REMARK 3 16 2.6458 - 2.5895 1.00 2849 143 0.2110 0.2331
REMARK 3 17 2.5895 - 2.5377 1.00 2847 165 0.2150 0.2473
REMARK 3 18 2.5377 - 2.4898 1.00 2870 127 0.2143 0.2559
REMARK 3 19 2.4898 - 2.4453 1.00 2868 151 0.2253 0.2470
REMARK 3 20 2.4453 - 2.4039 1.00 2833 161 0.2265 0.2400
REMARK 3 21 2.4039 - 2.3651 1.00 2847 149 0.2417 0.2659
REMARK 3 22 2.3651 - 2.3287 1.00 2861 123 0.2484 0.3178
REMARK 3 23 2.3287 - 2.2945 1.00 2836 140 0.2555 0.2533
REMARK 3 24 2.2945 - 2.2622 1.00 2869 155 0.2760 0.2828
REMARK 3 25 2.2622 - 2.2316 1.00 2853 144 0.2896 0.3199
REMARK 3 26 2.2316 - 2.2026 1.00 2807 173 0.3090 0.3642
REMARK 3 27 2.2026 - 2.1751 1.00 2843 142 0.3104 0.3444
REMARK 3 28 2.1751 - 2.1489 1.00 2826 158 0.3186 0.3111
REMARK 3 29 2.1489 - 2.1239 1.00 2861 153 0.3227 0.3509
REMARK 3 30 2.1239 - 2.1000 1.00 2818 133 0.3386 0.3770
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.93
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 11747
REMARK 3 ANGLE : 0.516 15913
REMARK 3 CHIRALITY : 0.043 1729
REMARK 3 PLANARITY : 0.003 2089
REMARK 3 DIHEDRAL : 14.443 6988
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 136:282)
REMARK 3 ORIGIN FOR THE GROUP (A): 55.1006 40.0472 134.3161
REMARK 3 T TENSOR
REMARK 3 T11: 0.3192 T22: 0.2060
REMARK 3 T33: 0.3172 T12: -0.0485
REMARK 3 T13: 0.0288 T23: -0.0766
REMARK 3 L TENSOR
REMARK 3 L11: 1.4065 L22: 0.8177
REMARK 3 L33: 0.9611 L12: 0.0896
REMARK 3 L13: -0.2279 L23: -0.0296
REMARK 3 S TENSOR
REMARK 3 S11: 0.0051 S12: -0.1664 S13: 0.1668
REMARK 3 S21: 0.0824 S22: -0.0362 S23: 0.0160
REMARK 3 S31: -0.0495 S32: 0.0900 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 283:349)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0014 11.9541 119.8569
REMARK 3 T TENSOR
REMARK 3 T11: 0.2066 T22: 0.1432
REMARK 3 T33: 0.3522 T12: 0.0053
REMARK 3 T13: -0.0072 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.9707 L22: -0.4467
REMARK 3 L33: 0.4057 L12: 0.3872
REMARK 3 L13: 0.3154 L23: 0.1055
REMARK 3 S TENSOR
REMARK 3 S11: 0.0047 S12: -0.0168 S13: -0.0198
REMARK 3 S21: 0.0099 S22: 0.0171 S23: 0.0451
REMARK 3 S31: -0.0069 S32: 0.0627 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 350:478)
REMARK 3 ORIGIN FOR THE GROUP (A): 60.3955 19.3536 119.8470
REMARK 3 T TENSOR
REMARK 3 T11: 0.2060 T22: 0.1917
REMARK 3 T33: 0.3167 T12: -0.0389
REMARK 3 T13: 0.0441 T23: -0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 0.3004 L22: 1.3876
REMARK 3 L33: 1.2527 L12: -0.1235
REMARK 3 L13: -0.1742 L23: 0.0711
REMARK 3 S TENSOR
REMARK 3 S11: -0.0377 S12: -0.0348 S13: -0.0590
REMARK 3 S21: -0.1052 S22: 0.0044 S23: -0.0510
REMARK 3 S31: 0.0001 S32: 0.0854 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 135:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.0083 19.8713 115.5947
REMARK 3 T TENSOR
REMARK 3 T11: 0.2527 T22: 0.1943
REMARK 3 T33: 0.3186 T12: 0.0746
REMARK 3 T13: 0.0274 T23: 0.0389
REMARK 3 L TENSOR
REMARK 3 L11: 1.0660 L22: 0.9503
REMARK 3 L33: 1.3643 L12: -0.2580
REMARK 3 L13: -0.1380 L23: 0.2875
REMARK 3 S TENSOR
REMARK 3 S11: 0.1041 S12: 0.0265 S13: -0.0068
REMARK 3 S21: 0.0060 S22: 0.0076 S23: -0.0042
REMARK 3 S31: -0.1816 S32: -0.1524 S33: 0.0010
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 294:336)
REMARK 3 ORIGIN FOR THE GROUP (A): 38.3150 28.6263 149.1030
REMARK 3 T TENSOR
REMARK 3 T11: 0.4328 T22: 0.4458
REMARK 3 T33: 0.3729 T12: -0.0262
REMARK 3 T13: 0.0605 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 0.4165 L22: -0.1118
REMARK 3 L33: 0.0565 L12: 0.3083
REMARK 3 L13: 0.2177 L23: -0.0188
REMARK 3 S TENSOR
REMARK 3 S11: 0.1788 S12: -0.1321 S13: 0.0020
REMARK 3 S21: 0.1298 S22: -0.0257 S23: 0.0241
REMARK 3 S31: 0.0021 S32: 0.0192 S33: 0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 337:365)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1578 21.5234 138.5920
REMARK 3 T TENSOR
REMARK 3 T11: 0.3364 T22: 0.3903
REMARK 3 T33: 0.3571 T12: 0.0299
REMARK 3 T13: 0.0697 T23: 0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 0.4951 L22: 0.6746
REMARK 3 L33: 0.5531 L12: 0.1117
REMARK 3 L13: 0.1206 L23: 0.6419
REMARK 3 S TENSOR
REMARK 3 S11: 0.1146 S12: -0.2393 S13: 0.2125
REMARK 3 S21: 0.0029 S22: -0.1169 S23: -0.0673
REMARK 3 S31: 0.0943 S32: -0.1909 S33: 0.0002
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 366:445)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.9992 22.3698 140.7299
REMARK 3 T TENSOR
REMARK 3 T11: 0.3295 T22: 0.3505
REMARK 3 T33: 0.3401 T12: 0.0252
REMARK 3 T13: 0.0489 T23: 0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 0.7135 L22: -0.1092
REMARK 3 L33: 0.7290 L12: -0.0809
REMARK 3 L13: -0.2408 L23: 0.3789
REMARK 3 S TENSOR
REMARK 3 S11: 0.0738 S12: -0.2641 S13: -0.0556
REMARK 3 S21: 0.0765 S22: 0.0223 S23: 0.0720
REMARK 3 S31: 0.0146 S32: -0.1503 S33: 0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 446:477)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.5583 29.7736 142.4957
REMARK 3 T TENSOR
REMARK 3 T11: 0.4055 T22: 0.3726
REMARK 3 T33: 0.4346 T12: 0.0094
REMARK 3 T13: 0.0700 T23: 0.0380
REMARK 3 L TENSOR
REMARK 3 L11: 0.5480 L22: 0.1403
REMARK 3 L33: 0.4422 L12: -0.0869
REMARK 3 L13: 0.5749 L23: 0.0168
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: -0.1693 S13: -0.1969
REMARK 3 S21: 0.0210 S22: -0.0039 S23: -0.1863
REMARK 3 S31: -0.1205 S32: 0.1432 S33: 0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID 136:257)
REMARK 3 ORIGIN FOR THE GROUP (A): 23.2214 41.7341 176.0899
REMARK 3 T TENSOR
REMARK 3 T11: 0.5698 T22: 0.5541
REMARK 3 T33: 0.3363 T12: 0.1107
REMARK 3 T13: 0.0452 T23: -0.0005
REMARK 3 L TENSOR
REMARK 3 L11: 1.0554 L22: 0.3419
REMARK 3 L33: 0.8046 L12: 0.0505
REMARK 3 L13: -0.4158 L23: -0.5695
REMARK 3 S TENSOR
REMARK 3 S11: -0.0213 S12: 0.0736 S13: 0.1018
REMARK 3 S21: 0.0348 S22: 0.1034 S23: 0.0268
REMARK 3 S31: -0.2851 S32: -0.2119 S33: 0.0001
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 258:336)
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0674 21.0556 191.9072
REMARK 3 T TENSOR
REMARK 3 T11: 0.3810 T22: 0.5197
REMARK 3 T33: 0.3086 T12: 0.0567
REMARK 3 T13: 0.0486 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.1345 L22: 0.1687
REMARK 3 L33: 0.2974 L12: -0.1094
REMARK 3 L13: 0.2761 L23: -0.0957
REMARK 3 S TENSOR
REMARK 3 S11: 0.1227 S12: -0.0071 S13: -0.1411
REMARK 3 S21: 0.0131 S22: -0.0747 S23: 0.0539
REMARK 3 S31: -0.0933 S32: -0.1770 S33: 0.0348
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: (CHAIN C AND RESID 337:478)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1715 20.1191 191.9946
REMARK 3 T TENSOR
REMARK 3 T11: 0.3775 T22: 0.5753
REMARK 3 T33: 0.3303 T12: 0.0609
REMARK 3 T13: 0.0743 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 0.3482 L22: 0.8114
REMARK 3 L33: 0.6779 L12: -0.2046
REMARK 3 L13: -0.7359 L23: -0.0367
REMARK 3 S TENSOR
REMARK 3 S11: -0.0717 S12: 0.0331 S13: -0.0592
REMARK 3 S21: 0.0467 S22: 0.0148 S23: 0.0422
REMARK 3 S31: -0.0336 S32: -0.2222 S33: -0.0009
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: (CHAIN D AND RESID 136:293)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.4159 18.1410 196.8741
REMARK 3 T TENSOR
REMARK 3 T11: 0.4266 T22: 0.5669
REMARK 3 T33: 0.3257 T12: -0.1248
REMARK 3 T13: 0.0208 T23: -0.0489
REMARK 3 L TENSOR
REMARK 3 L11: 1.0329 L22: 1.1326
REMARK 3 L33: 1.2265 L12: 0.5104
REMARK 3 L13: -0.3521 L23: -0.1946
REMARK 3 S TENSOR
REMARK 3 S11: 0.1861 S12: -0.1468 S13: -0.0388
REMARK 3 S21: 0.1135 S22: -0.1335 S23: -0.0577
REMARK 3 S31: -0.2067 S32: 0.2311 S33: 0.0000
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: (CHAIN D AND RESID 294:344)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9202 27.4807 164.7858
REMARK 3 T TENSOR
REMARK 3 T11: 0.4874 T22: 0.5712
REMARK 3 T33: 0.3569 T12: 0.0016
REMARK 3 T13: 0.0674 T23: -0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.3378 L22: 0.0611
REMARK 3 L33: 0.3366 L12: -0.5348
REMARK 3 L13: 0.2688 L23: 0.0278
REMARK 3 S TENSOR
REMARK 3 S11: 0.1643 S12: 0.1022 S13: -0.0447
REMARK 3 S21: 0.0914 S22: -0.0941 S23: 0.0322
REMARK 3 S31: -0.0529 S32: 0.0276 S33: -0.0000
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: (CHAIN D AND RESID 345:372)
REMARK 3 ORIGIN FOR THE GROUP (A): 63.6540 23.0724 176.1786
REMARK 3 T TENSOR
REMARK 3 T11: 0.4929 T22: 0.6768
REMARK 3 T33: 0.3685 T12: -0.0125
REMARK 3 T13: 0.0259 T23: -0.0390
REMARK 3 L TENSOR
REMARK 3 L11: 0.1005 L22: 0.1231
REMARK 3 L33: 0.3006 L12: 0.0597
REMARK 3 L13: 0.1435 L23: -0.1601
REMARK 3 S TENSOR
REMARK 3 S11: -0.0250 S12: 0.3304 S13: -0.0794
REMARK 3 S21: 0.0831 S22: -0.0450 S23: 0.0807
REMARK 3 S31: -0.0887 S32: 0.5074 S33: -0.0000
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: (CHAIN D AND RESID 373:430)
REMARK 3 ORIGIN FOR THE GROUP (A): 58.6013 17.2488 171.2267
REMARK 3 T TENSOR
REMARK 3 T11: 0.4655 T22: 0.5787
REMARK 3 T33: 0.3751 T12: 0.0288
REMARK 3 T13: 0.0174 T23: -0.0524
REMARK 3 L TENSOR
REMARK 3 L11: 0.4433 L22: 0.2244
REMARK 3 L33: 0.3514 L12: 0.3417
REMARK 3 L13: -0.4254 L23: -0.4206
REMARK 3 S TENSOR
REMARK 3 S11: 0.1389 S12: 0.1241 S13: -0.0652
REMARK 3 S21: -0.0484 S22: -0.1067 S23: -0.0389
REMARK 3 S31: -0.0100 S32: 0.2325 S33: -0.0000
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: (CHAIN D AND RESID 431:477)
REMARK 3 ORIGIN FOR THE GROUP (A): 54.6581 29.1229 169.8354
REMARK 3 T TENSOR
REMARK 3 T11: 0.5494 T22: 0.6448
REMARK 3 T33: 0.4038 T12: -0.0323
REMARK 3 T13: 0.0517 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 0.4512 L22: 0.4589
REMARK 3 L33: 0.4105 L12: -0.2362
REMARK 3 L13: 0.4286 L23: -0.4026
REMARK 3 S TENSOR
REMARK 3 S11: 0.3067 S12: 0.0752 S13: 0.0306
REMARK 3 S21: 0.1559 S22: -0.1231 S23: 0.0943
REMARK 3 S31: -0.2596 S32: -0.0007 S33: 0.0000
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 5LGS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-DEC-16.
REMARK 100 THE DEPOSITION ID IS D_1200000042.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97857
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 : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90877
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 47.971
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 2.75300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.700
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: 5IH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS-HCL PH 8.5 100 MM PEG 3350 20 %
REMARK 280 A.S. 200 MM, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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 37.49300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.29800
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.49300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.29800
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 18540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 51000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 127
REMARK 465 HIS A 128
REMARK 465 MET A 129
REMARK 465 GLY A 130
REMARK 465 HIS A 131
REMARK 465 THR A 132
REMARK 465 LEU A 133
REMARK 465 GLU A 134
REMARK 465 GLY A 479
REMARK 465 THR A 480
REMARK 465 THR A 481
REMARK 465 PRO A 482
REMARK 465 SER A 483
REMARK 465 PRO A 484
REMARK 465 PRO A 485
REMARK 465 PRO A 486
REMARK 465 GLY A 487
REMARK 465 GLY B 127
REMARK 465 HIS B 128
REMARK 465 MET B 129
REMARK 465 GLY B 130
REMARK 465 HIS B 131
REMARK 465 THR B 132
REMARK 465 LEU B 133
REMARK 465 GLU B 134
REMARK 465 THR B 478
REMARK 465 GLY B 479
REMARK 465 THR B 480
REMARK 465 THR B 481
REMARK 465 PRO B 482
REMARK 465 SER B 483
REMARK 465 PRO B 484
REMARK 465 PRO B 485
REMARK 465 PRO B 486
REMARK 465 GLY B 487
REMARK 465 GLY C 127
REMARK 465 HIS C 128
REMARK 465 MET C 129
REMARK 465 GLY C 130
REMARK 465 HIS C 131
REMARK 465 THR C 132
REMARK 465 LEU C 133
REMARK 465 GLU C 134
REMARK 465 ARG C 135
REMARK 465 GLY C 479
REMARK 465 THR C 480
REMARK 465 THR C 481
REMARK 465 PRO C 482
REMARK 465 SER C 483
REMARK 465 PRO C 484
REMARK 465 PRO C 485
REMARK 465 PRO C 486
REMARK 465 GLY C 487
REMARK 465 GLY D 127
REMARK 465 HIS D 128
REMARK 465 MET D 129
REMARK 465 GLY D 130
REMARK 465 HIS D 131
REMARK 465 THR D 132
REMARK 465 LEU D 133
REMARK 465 GLU D 134
REMARK 465 THR D 478
REMARK 465 GLY D 479
REMARK 465 THR D 480
REMARK 465 THR D 481
REMARK 465 PRO D 482
REMARK 465 SER D 483
REMARK 465 PRO D 484
REMARK 465 PRO D 485
REMARK 465 PRO D 486
REMARK 465 GLY D 487
REMARK 465 PRO E -3
REMARK 465 PRO G -3
REMARK 465 PRO H -3
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 HE ARG B 169 OE2 GLU B 258 1.57
REMARK 500 O SER B 318 HG SER D 462 1.59
REMARK 500 O HOH B 694 O HOH B 757 2.06
REMARK 500 O HOH A 735 O HOH A 787 2.08
REMARK 500 O HOH A 756 O HOH A 758 2.09
REMARK 500 O HOH B 726 O HOH B 742 2.09
REMARK 500 O HOH A 644 O HOH A 699 2.11
REMARK 500 O HOH B 728 O HOH B 760 2.12
REMARK 500 O HOH A 737 O HOH B 607 2.14
REMARK 500 O HOH B 760 O HOH B 763 2.15
REMARK 500 O HOH A 689 O HOH A 690 2.15
REMARK 500 O HOH A 639 O HOH A 763 2.16
REMARK 500 O THR B 182 O HOH B 601 2.17
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 MET A 263 19.18 58.42
REMARK 500 LEU A 264 -51.44 72.96
REMARK 500 GLU A 267 -19.95 90.63
REMARK 500 ASP A 300 82.69 -156.21
REMARK 500 SER A 318 71.86 -153.47
REMARK 500 ASP A 342 -172.83 -175.51
REMARK 500 TYR A 417 -143.00 50.19
REMARK 500 SER A 448 -156.30 -153.62
REMARK 500 ARG B 235 -32.59 -130.03
REMARK 500 LEU B 264 -51.23 75.93
REMARK 500 GLU B 267 -17.40 84.28
REMARK 500 ASP B 300 82.95 -155.36
REMARK 500 SER B 318 60.50 -153.29
REMARK 500 ASP B 342 -175.48 -172.89
REMARK 500 TYR B 417 -139.34 53.59
REMARK 500 ASN C 180 52.79 -115.92
REMARK 500 LEU C 264 -52.28 71.86
REMARK 500 GLU C 267 -18.91 82.52
REMARK 500 SER C 318 74.18 -150.87
REMARK 500 ASP C 342 -173.52 -173.14
REMARK 500 TYR C 417 -137.22 50.19
REMARK 500 ASP D 166 95.01 -64.31
REMARK 500 ASN D 180 47.73 -108.21
REMARK 500 ARG D 235 -23.96 -143.55
REMARK 500 LEU D 264 -51.20 73.71
REMARK 500 GLU D 267 -19.44 86.40
REMARK 500 ASP D 300 80.90 -156.87
REMARK 500 SER D 318 62.65 -150.43
REMARK 500 ASP D 342 -172.09 -170.04
REMARK 500 TYR D 417 -143.72 51.72
REMARK 500 SER D 448 -154.39 -147.22
REMARK 500 ASN D 472 74.16 -116.69
REMARK 500 ALA H -1 85.37 65.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 771 DISTANCE = 6.40 ANGSTROMS
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DXE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DXE B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DXE D 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide QVR E 1001 and ARG E
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide QVR F 1001 and ARG F
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide QVR G 101 and ARG G
REMARK 800 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide QVR H 101 and ARG H
REMARK 800 1
DBREF 5LGS A 130 487 UNP Q9WVG6 CARM1_MOUSE 130 487
DBREF 5LGS B 130 487 UNP Q9WVG6 CARM1_MOUSE 130 487
DBREF 5LGS C 130 487 UNP Q9WVG6 CARM1_MOUSE 130 487
DBREF 5LGS D 130 487 UNP Q9WVG6 CARM1_MOUSE 130 487
DBREF 5LGS E -3 5 UNP P11940 PABP1_HUMAN 456 464
DBREF 5LGS F -3 5 UNP P11940 PABP1_HUMAN 456 464
DBREF 5LGS G -3 5 UNP P11940 PABP1_HUMAN 456 464
DBREF 5LGS H -3 5 UNP P11940 PABP1_HUMAN 456 464
SEQADV 5LGS GLY A 127 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS HIS A 128 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS MET A 129 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS GLY B 127 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS HIS B 128 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS MET B 129 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS GLY C 127 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS HIS C 128 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS MET C 129 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS GLY D 127 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS HIS D 128 UNP Q9WVG6 EXPRESSION TAG
SEQADV 5LGS MET D 129 UNP Q9WVG6 EXPRESSION TAG
SEQRES 1 A 361 GLY HIS MET GLY HIS THR LEU GLU ARG SER VAL PHE SER
SEQRES 2 A 361 GLU ARG THR GLU GLU SER SER ALA VAL GLN TYR PHE GLN
SEQRES 3 A 361 PHE TYR GLY TYR LEU SER GLN GLN GLN ASN MET MET GLN
SEQRES 4 A 361 ASP TYR VAL ARG THR GLY THR TYR GLN ARG ALA ILE LEU
SEQRES 5 A 361 GLN ASN HIS THR ASP PHE LYS ASP LYS ILE VAL LEU ASP
SEQRES 6 A 361 VAL GLY CYS GLY SER GLY ILE LEU SER PHE PHE ALA ALA
SEQRES 7 A 361 GLN ALA GLY ALA ARG LYS ILE TYR ALA VAL GLU ALA SER
SEQRES 8 A 361 THR MET ALA GLN HIS ALA GLU VAL LEU VAL LYS SER ASN
SEQRES 9 A 361 ASN LEU THR ASP ARG ILE VAL VAL ILE PRO GLY LYS VAL
SEQRES 10 A 361 GLU GLU VAL SER LEU PRO GLU GLN VAL ASP ILE ILE ILE
SEQRES 11 A 361 SER GLU PRO MET GLY TYR MET LEU PHE ASN GLU ARG MET
SEQRES 12 A 361 LEU GLU SER TYR LEU HIS ALA LYS LYS TYR LEU LYS PRO
SEQRES 13 A 361 SER GLY ASN MET PHE PRO THR ILE GLY ASP VAL HIS LEU
SEQRES 14 A 361 ALA PRO PHE THR ASP GLU GLN LEU TYR MET GLU GLN PHE
SEQRES 15 A 361 THR LYS ALA ASN PHE TRP TYR GLN PRO SER PHE HIS GLY
SEQRES 16 A 361 VAL ASP LEU SER ALA LEU ARG GLY ALA ALA VAL ASP GLU
SEQRES 17 A 361 TYR PHE ARG GLN PRO VAL VAL ASP THR PHE ASP ILE ARG
SEQRES 18 A 361 ILE LEU MET ALA LYS SER VAL LYS TYR THR VAL ASN PHE
SEQRES 19 A 361 LEU GLU ALA LYS GLU GLY ASP LEU HIS ARG ILE GLU ILE
SEQRES 20 A 361 PRO PHE LYS PHE HIS MET LEU HIS SER GLY LEU VAL HIS
SEQRES 21 A 361 GLY LEU ALA PHE TRP PHE ASP VAL ALA PHE ILE GLY SER
SEQRES 22 A 361 ILE MET THR VAL TRP LEU SER THR ALA PRO THR GLU PRO
SEQRES 23 A 361 LEU THR HIS TRP TYR GLN VAL ARG CYS LEU PHE GLN SER
SEQRES 24 A 361 PRO LEU PHE ALA LYS ALA GLY ASP THR LEU SER GLY THR
SEQRES 25 A 361 CYS LEU LEU ILE ALA ASN LYS ARG GLN SER TYR ASP ILE
SEQRES 26 A 361 SER ILE VAL ALA GLN VAL ASP GLN THR GLY SER LYS SER
SEQRES 27 A 361 SER ASN LEU LEU ASP LEU LYS ASN PRO PHE PHE ARG TYR
SEQRES 28 A 361 THR GLY THR THR PRO SER PRO PRO PRO GLY
SEQRES 1 B 361 GLY HIS MET GLY HIS THR LEU GLU ARG SER VAL PHE SER
SEQRES 2 B 361 GLU ARG THR GLU GLU SER SER ALA VAL GLN TYR PHE GLN
SEQRES 3 B 361 PHE TYR GLY TYR LEU SER GLN GLN GLN ASN MET MET GLN
SEQRES 4 B 361 ASP TYR VAL ARG THR GLY THR TYR GLN ARG ALA ILE LEU
SEQRES 5 B 361 GLN ASN HIS THR ASP PHE LYS ASP LYS ILE VAL LEU ASP
SEQRES 6 B 361 VAL GLY CYS GLY SER GLY ILE LEU SER PHE PHE ALA ALA
SEQRES 7 B 361 GLN ALA GLY ALA ARG LYS ILE TYR ALA VAL GLU ALA SER
SEQRES 8 B 361 THR MET ALA GLN HIS ALA GLU VAL LEU VAL LYS SER ASN
SEQRES 9 B 361 ASN LEU THR ASP ARG ILE VAL VAL ILE PRO GLY LYS VAL
SEQRES 10 B 361 GLU GLU VAL SER LEU PRO GLU GLN VAL ASP ILE ILE ILE
SEQRES 11 B 361 SER GLU PRO MET GLY TYR MET LEU PHE ASN GLU ARG MET
SEQRES 12 B 361 LEU GLU SER TYR LEU HIS ALA LYS LYS TYR LEU LYS PRO
SEQRES 13 B 361 SER GLY ASN MET PHE PRO THR ILE GLY ASP VAL HIS LEU
SEQRES 14 B 361 ALA PRO PHE THR ASP GLU GLN LEU TYR MET GLU GLN PHE
SEQRES 15 B 361 THR LYS ALA ASN PHE TRP TYR GLN PRO SER PHE HIS GLY
SEQRES 16 B 361 VAL ASP LEU SER ALA LEU ARG GLY ALA ALA VAL ASP GLU
SEQRES 17 B 361 TYR PHE ARG GLN PRO VAL VAL ASP THR PHE ASP ILE ARG
SEQRES 18 B 361 ILE LEU MET ALA LYS SER VAL LYS TYR THR VAL ASN PHE
SEQRES 19 B 361 LEU GLU ALA LYS GLU GLY ASP LEU HIS ARG ILE GLU ILE
SEQRES 20 B 361 PRO PHE LYS PHE HIS MET LEU HIS SER GLY LEU VAL HIS
SEQRES 21 B 361 GLY LEU ALA PHE TRP PHE ASP VAL ALA PHE ILE GLY SER
SEQRES 22 B 361 ILE MET THR VAL TRP LEU SER THR ALA PRO THR GLU PRO
SEQRES 23 B 361 LEU THR HIS TRP TYR GLN VAL ARG CYS LEU PHE GLN SER
SEQRES 24 B 361 PRO LEU PHE ALA LYS ALA GLY ASP THR LEU SER GLY THR
SEQRES 25 B 361 CYS LEU LEU ILE ALA ASN LYS ARG GLN SER TYR ASP ILE
SEQRES 26 B 361 SER ILE VAL ALA GLN VAL ASP GLN THR GLY SER LYS SER
SEQRES 27 B 361 SER ASN LEU LEU ASP LEU LYS ASN PRO PHE PHE ARG TYR
SEQRES 28 B 361 THR GLY THR THR PRO SER PRO PRO PRO GLY
SEQRES 1 C 361 GLY HIS MET GLY HIS THR LEU GLU ARG SER VAL PHE SER
SEQRES 2 C 361 GLU ARG THR GLU GLU SER SER ALA VAL GLN TYR PHE GLN
SEQRES 3 C 361 PHE TYR GLY TYR LEU SER GLN GLN GLN ASN MET MET GLN
SEQRES 4 C 361 ASP TYR VAL ARG THR GLY THR TYR GLN ARG ALA ILE LEU
SEQRES 5 C 361 GLN ASN HIS THR ASP PHE LYS ASP LYS ILE VAL LEU ASP
SEQRES 6 C 361 VAL GLY CYS GLY SER GLY ILE LEU SER PHE PHE ALA ALA
SEQRES 7 C 361 GLN ALA GLY ALA ARG LYS ILE TYR ALA VAL GLU ALA SER
SEQRES 8 C 361 THR MET ALA GLN HIS ALA GLU VAL LEU VAL LYS SER ASN
SEQRES 9 C 361 ASN LEU THR ASP ARG ILE VAL VAL ILE PRO GLY LYS VAL
SEQRES 10 C 361 GLU GLU VAL SER LEU PRO GLU GLN VAL ASP ILE ILE ILE
SEQRES 11 C 361 SER GLU PRO MET GLY TYR MET LEU PHE ASN GLU ARG MET
SEQRES 12 C 361 LEU GLU SER TYR LEU HIS ALA LYS LYS TYR LEU LYS PRO
SEQRES 13 C 361 SER GLY ASN MET PHE PRO THR ILE GLY ASP VAL HIS LEU
SEQRES 14 C 361 ALA PRO PHE THR ASP GLU GLN LEU TYR MET GLU GLN PHE
SEQRES 15 C 361 THR LYS ALA ASN PHE TRP TYR GLN PRO SER PHE HIS GLY
SEQRES 16 C 361 VAL ASP LEU SER ALA LEU ARG GLY ALA ALA VAL ASP GLU
SEQRES 17 C 361 TYR PHE ARG GLN PRO VAL VAL ASP THR PHE ASP ILE ARG
SEQRES 18 C 361 ILE LEU MET ALA LYS SER VAL LYS TYR THR VAL ASN PHE
SEQRES 19 C 361 LEU GLU ALA LYS GLU GLY ASP LEU HIS ARG ILE GLU ILE
SEQRES 20 C 361 PRO PHE LYS PHE HIS MET LEU HIS SER GLY LEU VAL HIS
SEQRES 21 C 361 GLY LEU ALA PHE TRP PHE ASP VAL ALA PHE ILE GLY SER
SEQRES 22 C 361 ILE MET THR VAL TRP LEU SER THR ALA PRO THR GLU PRO
SEQRES 23 C 361 LEU THR HIS TRP TYR GLN VAL ARG CYS LEU PHE GLN SER
SEQRES 24 C 361 PRO LEU PHE ALA LYS ALA GLY ASP THR LEU SER GLY THR
SEQRES 25 C 361 CYS LEU LEU ILE ALA ASN LYS ARG GLN SER TYR ASP ILE
SEQRES 26 C 361 SER ILE VAL ALA GLN VAL ASP GLN THR GLY SER LYS SER
SEQRES 27 C 361 SER ASN LEU LEU ASP LEU LYS ASN PRO PHE PHE ARG TYR
SEQRES 28 C 361 THR GLY THR THR PRO SER PRO PRO PRO GLY
SEQRES 1 D 361 GLY HIS MET GLY HIS THR LEU GLU ARG SER VAL PHE SER
SEQRES 2 D 361 GLU ARG THR GLU GLU SER SER ALA VAL GLN TYR PHE GLN
SEQRES 3 D 361 PHE TYR GLY TYR LEU SER GLN GLN GLN ASN MET MET GLN
SEQRES 4 D 361 ASP TYR VAL ARG THR GLY THR TYR GLN ARG ALA ILE LEU
SEQRES 5 D 361 GLN ASN HIS THR ASP PHE LYS ASP LYS ILE VAL LEU ASP
SEQRES 6 D 361 VAL GLY CYS GLY SER GLY ILE LEU SER PHE PHE ALA ALA
SEQRES 7 D 361 GLN ALA GLY ALA ARG LYS ILE TYR ALA VAL GLU ALA SER
SEQRES 8 D 361 THR MET ALA GLN HIS ALA GLU VAL LEU VAL LYS SER ASN
SEQRES 9 D 361 ASN LEU THR ASP ARG ILE VAL VAL ILE PRO GLY LYS VAL
SEQRES 10 D 361 GLU GLU VAL SER LEU PRO GLU GLN VAL ASP ILE ILE ILE
SEQRES 11 D 361 SER GLU PRO MET GLY TYR MET LEU PHE ASN GLU ARG MET
SEQRES 12 D 361 LEU GLU SER TYR LEU HIS ALA LYS LYS TYR LEU LYS PRO
SEQRES 13 D 361 SER GLY ASN MET PHE PRO THR ILE GLY ASP VAL HIS LEU
SEQRES 14 D 361 ALA PRO PHE THR ASP GLU GLN LEU TYR MET GLU GLN PHE
SEQRES 15 D 361 THR LYS ALA ASN PHE TRP TYR GLN PRO SER PHE HIS GLY
SEQRES 16 D 361 VAL ASP LEU SER ALA LEU ARG GLY ALA ALA VAL ASP GLU
SEQRES 17 D 361 TYR PHE ARG GLN PRO VAL VAL ASP THR PHE ASP ILE ARG
SEQRES 18 D 361 ILE LEU MET ALA LYS SER VAL LYS TYR THR VAL ASN PHE
SEQRES 19 D 361 LEU GLU ALA LYS GLU GLY ASP LEU HIS ARG ILE GLU ILE
SEQRES 20 D 361 PRO PHE LYS PHE HIS MET LEU HIS SER GLY LEU VAL HIS
SEQRES 21 D 361 GLY LEU ALA PHE TRP PHE ASP VAL ALA PHE ILE GLY SER
SEQRES 22 D 361 ILE MET THR VAL TRP LEU SER THR ALA PRO THR GLU PRO
SEQRES 23 D 361 LEU THR HIS TRP TYR GLN VAL ARG CYS LEU PHE GLN SER
SEQRES 24 D 361 PRO LEU PHE ALA LYS ALA GLY ASP THR LEU SER GLY THR
SEQRES 25 D 361 CYS LEU LEU ILE ALA ASN LYS ARG GLN SER TYR ASP ILE
SEQRES 26 D 361 SER ILE VAL ALA GLN VAL ASP GLN THR GLY SER LYS SER
SEQRES 27 D 361 SER ASN LEU LEU ASP LEU LYS ASN PRO PHE PHE ARG TYR
SEQRES 28 D 361 THR GLY THR THR PRO SER PRO PRO PRO GLY
SEQRES 1 E 9 PRO ALA ALA PRO ARG PRO PRO PHE SER
SEQRES 1 F 9 PRO ALA ALA PRO ARG PRO PRO PHE SER
SEQRES 1 G 9 PRO ALA ALA PRO ARG PRO PRO PHE SER
SEQRES 1 H 9 PRO ALA ALA PRO ARG PRO PRO PHE SER
HET SO4 A 501 5
HET DXE A 502 16
HET PEG A 503 17
HET DXE B 501 16
HET PG4 B 502 31
HET EDO C 501 10
HET EDO C 502 10
HET EDO D 501 10
HET DXE D 502 16
HET QVR E1001 34
HET QVR F1001 34
HET QVR G 101 34
HET QVR H 101 34
HETNAM SO4 SULFATE ION
HETNAM DXE 1,2-DIMETHOXYETHANE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETNAM QVR (2~{R},3~{R},4~{S},5~{R})-2-(6-AMINOPURIN-9-YL)-5-
HETNAM 2 QVR [(~{E})-PROP-1-ENYL]OXOLANE-3,4-DIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 9 SO4 O4 S 2-
FORMUL 10 DXE 3(C4 H10 O2)
FORMUL 11 PEG C4 H10 O3
FORMUL 13 PG4 C8 H18 O5
FORMUL 14 EDO 3(C2 H6 O2)
FORMUL 18 QVR 4(C12 H15 N5 O3)
FORMUL 22 HOH *584(H2 O)
HELIX 1 AA1 SER A 136 THR A 142 1 7
HELIX 2 AA2 GLU A 143 TYR A 154 1 12
HELIX 3 AA3 TYR A 156 GLN A 165 1 10
HELIX 4 AA4 ASP A 166 GLN A 179 1 14
HELIX 5 AA5 ASN A 180 PHE A 184 5 5
HELIX 6 AA6 GLY A 197 ALA A 206 1 10
HELIX 7 AA7 THR A 218 ASN A 230 1 13
HELIX 8 AA8 MET A 269 ALA A 276 1 8
HELIX 9 AA9 ASP A 300 ASN A 312 1 13
HELIX 10 AB1 PHE A 313 TYR A 315 5 3
HELIX 11 AB2 LEU A 324 ALA A 326 5 3
HELIX 12 AB3 LEU A 327 ARG A 337 1 11
HELIX 13 AB4 ASP A 345 LEU A 349 5 5
HELIX 14 AB5 LYS A 364 LEU A 368 5 5
HELIX 15 AB6 SER B 136 THR B 142 1 7
HELIX 16 AB7 GLU B 143 TYR B 154 1 12
HELIX 17 AB8 TYR B 156 GLN B 165 1 10
HELIX 18 AB9 ASP B 166 ASN B 180 1 15
HELIX 19 AC1 HIS B 181 PHE B 184 5 4
HELIX 20 AC2 GLY B 197 ALA B 206 1 10
HELIX 21 AC3 THR B 218 ASN B 230 1 13
HELIX 22 AC4 PHE B 265 GLU B 267 5 3
HELIX 23 AC5 ARG B 268 ALA B 276 1 9
HELIX 24 AC6 ASP B 300 ASN B 312 1 13
HELIX 25 AC7 PHE B 313 GLN B 316 5 4
HELIX 26 AC8 SER B 318 VAL B 322 5 5
HELIX 27 AC9 LEU B 324 ALA B 326 5 3
HELIX 28 AD1 LEU B 327 ARG B 337 1 11
HELIX 29 AD2 ASP B 345 LEU B 349 5 5
HELIX 30 AD3 LYS B 364 LEU B 368 5 5
HELIX 31 AD4 VAL C 137 ARG C 141 1 5
HELIX 32 AD5 GLU C 143 GLY C 155 1 13
HELIX 33 AD6 TYR C 156 GLN C 165 1 10
HELIX 34 AD7 ASP C 166 GLN C 179 1 14
HELIX 35 AD8 ASN C 180 PHE C 184 5 5
HELIX 36 AD9 GLY C 197 ALA C 206 1 10
HELIX 37 AE1 THR C 218 ASN C 230 1 13
HELIX 38 AE2 PHE C 265 ARG C 268 5 4
HELIX 39 AE3 MET C 269 ALA C 276 1 8
HELIX 40 AE4 ASP C 300 ASN C 312 1 13
HELIX 41 AE5 PHE C 313 TYR C 315 5 3
HELIX 42 AE6 LEU C 324 ALA C 326 5 3
HELIX 43 AE7 LEU C 327 ARG C 337 1 11
HELIX 44 AE8 ASP C 345 LEU C 349 5 5
HELIX 45 AE9 LYS C 364 LEU C 368 5 5
HELIX 46 AF1 SER D 136 ARG D 141 1 6
HELIX 47 AF2 GLU D 143 TYR D 154 1 12
HELIX 48 AF3 TYR D 156 GLN D 165 1 10
HELIX 49 AF4 ASP D 166 ASN D 180 1 15
HELIX 50 AF5 HIS D 181 PHE D 184 5 4
HELIX 51 AF6 GLY D 197 ALA D 206 1 10
HELIX 52 AF7 THR D 218 ASN D 230 1 13
HELIX 53 AF8 PHE D 265 GLU D 267 5 3
HELIX 54 AF9 ARG D 268 ALA D 276 1 9
HELIX 55 AG1 ASP D 300 ASN D 312 1 13
HELIX 56 AG2 PHE D 313 GLN D 316 5 4
HELIX 57 AG3 SER D 318 VAL D 322 5 5
HELIX 58 AG4 LEU D 324 ALA D 326 5 3
HELIX 59 AG5 LEU D 327 ARG D 337 1 11
HELIX 60 AG6 ASP D 345 LEU D 349 5 5
HELIX 61 AG7 LYS D 364 LEU D 368 5 5
SHEET 1 AA1 5 ILE A 236 PRO A 240 0
SHEET 2 AA1 5 LYS A 210 GLU A 215 1 N ALA A 213 O ILE A 239
SHEET 3 AA1 5 ILE A 188 VAL A 192 1 N VAL A 189 O TYR A 212
SHEET 4 AA1 5 VAL A 252 SER A 257 1 O ILE A 256 N LEU A 190
SHEET 5 AA1 5 LEU A 280 PHE A 287 1 O PHE A 287 N ILE A 255
SHEET 1 AA2 4 VAL A 354 ASN A 359 0
SHEET 2 AA2 4 ILE A 290 PHE A 298 -1 N GLY A 291 O VAL A 358
SHEET 3 AA2 4 GLY A 383 ILE A 397 -1 O ALA A 389 N ALA A 296
SHEET 4 AA2 4 THR A 402 SER A 406 -1 O VAL A 403 N PHE A 396
SHEET 1 AA3 6 VAL A 354 ASN A 359 0
SHEET 2 AA3 6 ILE A 290 PHE A 298 -1 N GLY A 291 O VAL A 358
SHEET 3 AA3 6 GLY A 383 ILE A 397 -1 O ALA A 389 N ALA A 296
SHEET 4 AA3 6 GLN A 418 ALA A 429 -1 O VAL A 419 N PHE A 390
SHEET 5 AA3 6 VAL A 340 ASP A 342 -1 N VAL A 340 O ARG A 420
SHEET 6 AA3 6 PHE A 474 PHE A 475 1 O PHE A 474 N VAL A 341
SHEET 1 AA4 4 ARG A 370 HIS A 378 0
SHEET 2 AA4 4 THR A 434 ALA A 443 -1 O LEU A 435 N PHE A 377
SHEET 3 AA4 4 TYR A 449 VAL A 457 -1 O SER A 452 N LEU A 440
SHEET 4 AA4 4 LYS A 463 ASP A 469 -1 O LEU A 468 N ILE A 451
SHEET 1 AA5 5 ILE B 236 PRO B 240 0
SHEET 2 AA5 5 LYS B 210 GLU B 215 1 N ILE B 211 O VAL B 237
SHEET 3 AA5 5 ILE B 188 VAL B 192 1 N ASP B 191 O TYR B 212
SHEET 4 AA5 5 VAL B 252 SER B 257 1 O ILE B 256 N LEU B 190
SHEET 5 AA5 5 LEU B 280 PHE B 287 1 O PHE B 287 N ILE B 255
SHEET 1 AA6 4 VAL B 354 ASN B 359 0
SHEET 2 AA6 4 ILE B 290 PHE B 298 -1 N VAL B 293 O TYR B 356
SHEET 3 AA6 4 GLY B 383 ILE B 397 -1 O ASP B 393 N ASP B 292
SHEET 4 AA6 4 THR B 402 SER B 406 -1 O VAL B 403 N PHE B 396
SHEET 1 AA7 6 VAL B 354 ASN B 359 0
SHEET 2 AA7 6 ILE B 290 PHE B 298 -1 N VAL B 293 O TYR B 356
SHEET 3 AA7 6 GLY B 383 ILE B 397 -1 O ASP B 393 N ASP B 292
SHEET 4 AA7 6 GLN B 418 ALA B 429 -1 O VAL B 419 N PHE B 390
SHEET 5 AA7 6 VAL B 340 ASP B 342 -1 N VAL B 340 O ARG B 420
SHEET 6 AA7 6 PHE B 474 PHE B 475 1 O PHE B 474 N VAL B 341
SHEET 1 AA8 4 ARG B 370 HIS B 378 0
SHEET 2 AA8 4 THR B 434 ASN B 444 -1 O CYS B 439 N ILE B 373
SHEET 3 AA8 4 SER B 448 VAL B 457 -1 O ASP B 450 N ILE B 442
SHEET 4 AA8 4 LYS B 463 ASP B 469 -1 O SER B 464 N ALA B 455
SHEET 1 AA9 5 ILE C 236 PRO C 240 0
SHEET 2 AA9 5 LYS C 210 GLU C 215 1 N ALA C 213 O ILE C 239
SHEET 3 AA9 5 ILE C 188 VAL C 192 1 N ASP C 191 O TYR C 212
SHEET 4 AA9 5 VAL C 252 SER C 257 1 O ILE C 256 N LEU C 190
SHEET 5 AA9 5 LEU C 280 PHE C 287 1 O PHE C 287 N ILE C 255
SHEET 1 AB1 4 VAL C 354 ASN C 359 0
SHEET 2 AB1 4 ILE C 290 PHE C 298 -1 N LEU C 295 O VAL C 354
SHEET 3 AB1 4 GLY C 383 ILE C 397 -1 O ALA C 389 N ALA C 296
SHEET 4 AB1 4 THR C 402 SER C 406 -1 O VAL C 403 N PHE C 396
SHEET 1 AB2 6 VAL C 354 ASN C 359 0
SHEET 2 AB2 6 ILE C 290 PHE C 298 -1 N LEU C 295 O VAL C 354
SHEET 3 AB2 6 GLY C 383 ILE C 397 -1 O ALA C 389 N ALA C 296
SHEET 4 AB2 6 GLN C 418 ALA C 429 -1 O VAL C 419 N PHE C 390
SHEET 5 AB2 6 VAL C 340 ASP C 342 -1 N VAL C 340 O ARG C 420
SHEET 6 AB2 6 PHE C 474 PHE C 475 1 O PHE C 474 N VAL C 341
SHEET 1 AB3 4 ARG C 370 HIS C 378 0
SHEET 2 AB3 4 THR C 434 ASN C 444 -1 O LEU C 441 N ILE C 371
SHEET 3 AB3 4 SER C 448 VAL C 457 -1 O SER C 452 N LEU C 440
SHEET 4 AB3 4 LYS C 463 ASP C 469 -1 O LEU C 468 N ILE C 451
SHEET 1 AB4 5 ILE D 236 PRO D 240 0
SHEET 2 AB4 5 LYS D 210 GLU D 215 1 N ILE D 211 O VAL D 237
SHEET 3 AB4 5 ILE D 188 VAL D 192 1 N ASP D 191 O TYR D 212
SHEET 4 AB4 5 VAL D 252 SER D 257 1 O ILE D 256 N LEU D 190
SHEET 5 AB4 5 LEU D 280 PHE D 287 1 O PHE D 287 N ILE D 255
SHEET 1 AB5 4 VAL D 354 ASN D 359 0
SHEET 2 AB5 4 ILE D 290 PHE D 298 -1 N VAL D 293 O TYR D 356
SHEET 3 AB5 4 GLY D 383 ILE D 397 -1 O ASP D 393 N ASP D 292
SHEET 4 AB5 4 THR D 402 SER D 406 -1 O VAL D 403 N PHE D 396
SHEET 1 AB6 6 VAL D 354 ASN D 359 0
SHEET 2 AB6 6 ILE D 290 PHE D 298 -1 N VAL D 293 O TYR D 356
SHEET 3 AB6 6 GLY D 383 ILE D 397 -1 O ASP D 393 N ASP D 292
SHEET 4 AB6 6 GLN D 418 ALA D 429 -1 O VAL D 419 N PHE D 390
SHEET 5 AB6 6 VAL D 340 ASP D 342 -1 N VAL D 340 O ARG D 420
SHEET 6 AB6 6 PHE D 474 PHE D 475 1 O PHE D 474 N VAL D 341
SHEET 1 AB7 4 ARG D 370 HIS D 378 0
SHEET 2 AB7 4 THR D 434 ALA D 443 -1 O LEU D 441 N ILE D 371
SHEET 3 AB7 4 TYR D 449 VAL D 457 -1 O ASP D 450 N ILE D 442
SHEET 4 AB7 4 SER D 462 ASP D 469 -1 O SER D 464 N ALA D 455
LINK NH2 ARG E 1 C24 QVR E1001 1555 1555 1.46
LINK NH2 ARG F 1 C24 QVR F1001 1555 1555 1.46
LINK NH2 ARG G 1 C24 QVR G 101 1555 1555 1.46
LINK NH2 ARG H 1 C24 QVR H 101 1555 1555 1.46
CISPEP 1 PHE A 287 PRO A 288 0 3.85
CISPEP 2 PHE B 287 PRO B 288 0 4.16
CISPEP 3 PHE C 287 PRO C 288 0 6.61
CISPEP 4 PHE D 287 PRO D 288 0 2.28
SITE 1 AC1 5 ASN A 444 LYS A 445 HOH A 618 HOH A 673
SITE 2 AC1 5 ARG B 209
SITE 1 AC2 1 GLY A 398
SITE 1 AC3 1 ASP B 393
SITE 1 AC4 4 LYS A 463 SER B 136 GLU B 244 GLU B 245
SITE 1 AC5 1 TRP C 404
SITE 1 AC6 1 GLN C 205
SITE 1 AC7 1 ASP D 393
SITE 1 AC8 3 LEU A 178 GLN A 205 GLY D 461
SITE 1 AC9 25 TYR A 150 PHE A 151 TYR A 154 MET A 163
SITE 2 AC9 25 GLY A 193 GLU A 215 ALA A 216 GLY A 241
SITE 3 AC9 25 LYS A 242 VAL A 243 GLU A 244 GLU A 258
SITE 4 AC9 25 MET A 260 GLU A 267 MET A 269 SER A 272
SITE 5 AC9 25 HIS A 415 HOH A 642 ALA E -1 PRO E 0
SITE 6 AC9 25 PRO E 2 PRO E 3 HOH E1103 HOH E1104
SITE 7 AC9 25 HOH E1105
SITE 1 AD1 25 TYR B 150 PHE B 151 TYR B 154 MET B 163
SITE 2 AD1 25 GLY B 193 GLU B 215 ALA B 216 GLY B 241
SITE 3 AD1 25 LYS B 242 VAL B 243 GLU B 244 GLU B 258
SITE 4 AD1 25 MET B 260 GLU B 267 MET B 269 SER B 272
SITE 5 AD1 25 HIS B 415 HOH B 671 ALA F -1 PRO F 0
SITE 6 AD1 25 PRO F 2 PRO F 3 HOH F1103 HOH F1104
SITE 7 AD1 25 HOH F1106
SITE 1 AD2 22 TYR C 150 PHE C 151 TYR C 154 MET C 163
SITE 2 AD2 22 GLY C 193 GLU C 215 ALA C 216 LYS C 242
SITE 3 AD2 22 VAL C 243 GLU C 244 GLU C 258 MET C 260
SITE 4 AD2 22 GLU C 267 MET C 269 SER C 272 HIS C 415
SITE 5 AD2 22 HOH C 628 ALA G -1 PRO G 0 PRO G 2
SITE 6 AD2 22 PRO G 3 HOH G 201
SITE 1 AD3 22 TYR D 150 TYR D 154 MET D 163 GLY D 193
SITE 2 AD3 22 GLU D 215 ALA D 216 LYS D 242 VAL D 243
SITE 3 AD3 22 GLU D 244 GLU D 258 MET D 260 GLU D 267
SITE 4 AD3 22 MET D 269 SER D 272 HIS D 415 ALA H -1
SITE 5 AD3 22 PRO H 0 PRO H 2 PRO H 3 HOH H 202
SITE 6 AD3 22 HOH H 203 HOH H 204
CRYST1 74.986 98.596 208.172 90.00 90.00 90.00 P 21 21 2 16
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 0.013336 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004804 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
