HEADER SIGNALING PROTEIN/TRANSFERASE 24-NOV-15 5EYA
TITLE TRIM25 RING DOMAIN IN COMPLEX WITH UBC13-UB CONJUGATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME,E2 UBIQUITIN-
COMPND 5 CONJUGATING ENZYME N,UBC13,UBCH13,UBIQUITIN CARRIER PROTEIN N,
COMPND 6 UBIQUITIN-PROTEIN LIGASE N;
COMPND 7 EC: 2.3.2.23;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: TRIPARTITE MOTIF-CONTAINING 25 VARIANT;
COMPND 12 CHAIN: F, G;
COMPND 13 FRAGMENT: UNP RESIDUES 12-97;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: POLYUBIQUITIN-B;
COMPND 17 CHAIN: C, D;
COMPND 18 FRAGMENT: UNP RESIDUES 1-76;
COMPND 19 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: UBE2N, BLU;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 GENE: UBB;
SOURCE 19 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 20 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, E3 LIGASE, UBIQUITINATION, SIGNALING PROTEIN-TRANSFERASE
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR O.PORNILLOS,J.G.SANCHEZ
REVDAT 3 25-DEC-19 5EYA 1 REMARK
REVDAT 2 27-SEP-17 5EYA 1 REMARK
REVDAT 1 17-AUG-16 5EYA 0
JRNL AUTH J.G.SANCHEZ,J.J.CHIANG,K.M.SPARRER,S.L.ALAM,M.CHI,
JRNL AUTH 2 M.D.ROGANOWICZ,B.SANKARAN,M.U.GACK,O.PORNILLOS
JRNL TITL MECHANISM OF TRIM25 CATALYTIC ACTIVATION IN THE ANTIVIRAL
JRNL TITL 2 RIG-I PATHWAY.
JRNL REF CELL REP V. 16 1315 2016
JRNL REFN ESSN 2211-1247
JRNL PMID 27425606
JRNL DOI 10.1016/J.CELREP.2016.06.070
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.97
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.160
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 3 NUMBER OF REFLECTIONS : 24622
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1786
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 28.9685 - 5.6304 0.97 2058 161 0.1645 0.1843
REMARK 3 2 5.6304 - 4.4744 0.97 1935 152 0.1446 0.1756
REMARK 3 3 4.4744 - 3.9103 0.98 1950 153 0.1416 0.1801
REMARK 3 4 3.9103 - 3.5535 0.97 1899 147 0.1781 0.2344
REMARK 3 5 3.5535 - 3.2992 0.96 1870 147 0.2017 0.2359
REMARK 3 6 3.2992 - 3.1049 0.94 1823 142 0.2112 0.2533
REMARK 3 7 3.1049 - 2.9496 0.93 1799 142 0.2108 0.2805
REMARK 3 8 2.9496 - 2.8213 0.92 1784 139 0.2340 0.2726
REMARK 3 9 2.8213 - 2.7127 0.89 1713 134 0.2280 0.2713
REMARK 3 10 2.7127 - 2.6192 0.87 1686 132 0.2346 0.2694
REMARK 3 11 2.6192 - 2.5374 0.83 1585 123 0.2387 0.2631
REMARK 3 12 2.5374 - 2.4649 0.76 1473 116 0.2591 0.2774
REMARK 3 13 2.4649 - 2.4000 0.66 1261 98 0.2868 0.3916
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) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.320
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.05
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 : 0.006 4957
REMARK 3 ANGLE : 1.098 6733
REMARK 3 CHIRALITY : 0.041 757
REMARK 3 PLANARITY : 0.005 878
REMARK 3 DIHEDRAL : 14.766 1887
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 36
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.1007 -11.2420 -15.6566
REMARK 3 T TENSOR
REMARK 3 T11: 0.6622 T22: 0.1939
REMARK 3 T33: -0.2997 T12: -0.5349
REMARK 3 T13: -0.1154 T23: -0.5398
REMARK 3 L TENSOR
REMARK 3 L11: 1.2394 L22: 1.1702
REMARK 3 L33: 1.2826 L12: 0.2751
REMARK 3 L13: 0.5600 L23: 0.4318
REMARK 3 S TENSOR
REMARK 3 S11: 0.0238 S12: -0.0522 S13: -0.6344
REMARK 3 S21: -0.2668 S22: 0.0228 S23: -0.5228
REMARK 3 S31: 0.5233 S32: -0.5701 S33: -0.0227
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.7739 -11.9078 -8.6204
REMARK 3 T TENSOR
REMARK 3 T11: 0.5799 T22: 0.3624
REMARK 3 T33: 0.3436 T12: 0.0105
REMARK 3 T13: -0.0137 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 5.8962 L22: 1.7087
REMARK 3 L33: 1.3448 L12: -0.7183
REMARK 3 L13: -2.3258 L23: 0.2866
REMARK 3 S TENSOR
REMARK 3 S11: -0.1455 S12: -0.3700 S13: -0.7199
REMARK 3 S21: 0.4969 S22: -0.0369 S23: -0.0352
REMARK 3 S31: 0.8046 S32: 0.2356 S33: 0.0359
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 31 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.8921 -4.1775 -6.6646
REMARK 3 T TENSOR
REMARK 3 T11: 0.3494 T22: 0.3001
REMARK 3 T33: 0.1958 T12: 0.0112
REMARK 3 T13: -0.0234 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 3.2134 L22: 1.1776
REMARK 3 L33: 1.3672 L12: 0.9979
REMARK 3 L13: 0.2819 L23: -0.0559
REMARK 3 S TENSOR
REMARK 3 S11: -0.3802 S12: 0.5116 S13: -0.3246
REMARK 3 S21: 0.0413 S22: 0.2571 S23: -0.0874
REMARK 3 S31: 0.4508 S32: -0.0312 S33: 0.0714
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 58 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3840 1.7104 -13.9730
REMARK 3 T TENSOR
REMARK 3 T11: 0.3887 T22: 0.4389
REMARK 3 T33: 0.1905 T12: -0.0505
REMARK 3 T13: 0.0225 T23: -0.0532
REMARK 3 L TENSOR
REMARK 3 L11: 3.2458 L22: 7.0249
REMARK 3 L33: 2.4857 L12: 3.0223
REMARK 3 L13: 0.9290 L23: -1.7646
REMARK 3 S TENSOR
REMARK 3 S11: 0.3910 S12: -0.3697 S13: 0.4776
REMARK 3 S21: -0.0285 S22: -0.0756 S23: 0.3523
REMARK 3 S31: -0.2447 S32: -1.2342 S33: -0.2001
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3603 6.0226 -9.6658
REMARK 3 T TENSOR
REMARK 3 T11: 0.2610 T22: 0.2654
REMARK 3 T33: 0.2596 T12: -0.0135
REMARK 3 T13: -0.0164 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.1860 L22: 1.2765
REMARK 3 L33: 2.3717 L12: 0.7329
REMARK 3 L13: 1.2507 L23: 0.1160
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: -0.3052 S13: 0.3552
REMARK 3 S21: -0.0216 S22: -0.0818 S23: 0.0643
REMARK 3 S31: -0.0848 S32: 0.2682 S33: 0.1096
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 101 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.0170 4.3364 -13.7274
REMARK 3 T TENSOR
REMARK 3 T11: 0.3107 T22: 0.2925
REMARK 3 T33: 0.1905 T12: -0.0727
REMARK 3 T13: -0.1083 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 2.3966 L22: 1.8273
REMARK 3 L33: 2.4171 L12: 0.1287
REMARK 3 L13: 0.0535 L23: 0.3200
REMARK 3 S TENSOR
REMARK 3 S11: -0.2179 S12: 0.0350 S13: 0.2535
REMARK 3 S21: -0.0137 S22: 0.1821 S23: -0.1790
REMARK 3 S31: 0.1539 S32: 1.0626 S33: -0.0150
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5134 6.3811 -2.9195
REMARK 3 T TENSOR
REMARK 3 T11: 0.2486 T22: 0.5388
REMARK 3 T33: 0.3256 T12: -0.0474
REMARK 3 T13: -0.0364 T23: -0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 3.8496 L22: 4.1144
REMARK 3 L33: 4.8180 L12: -0.1298
REMARK 3 L13: -1.1339 L23: -1.7417
REMARK 3 S TENSOR
REMARK 3 S11: 0.0354 S12: -0.2696 S13: 0.8636
REMARK 3 S21: 0.3289 S22: 0.3002 S23: -0.1415
REMARK 3 S31: -0.4620 S32: 0.6576 S33: -0.0919
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 6 THROUGH 10 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3296 -14.2552 -32.3856
REMARK 3 T TENSOR
REMARK 3 T11: 0.5251 T22: 0.2017
REMARK 3 T33: 0.3970 T12: -0.0085
REMARK 3 T13: 0.0685 T23: -0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 3.7712 L22: 3.8649
REMARK 3 L33: 4.9629 L12: 1.8594
REMARK 3 L13: -2.4951 L23: 0.4874
REMARK 3 S TENSOR
REMARK 3 S11: 0.3330 S12: -0.3987 S13: 0.0328
REMARK 3 S21: 0.7563 S22: -0.1875 S23: -0.1175
REMARK 3 S31: 0.4328 S32: 0.1381 S33: 0.0446
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 11 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.3211 -4.0284 -31.4164
REMARK 3 T TENSOR
REMARK 3 T11: 0.2588 T22: 0.1613
REMARK 3 T33: 0.2136 T12: -0.0232
REMARK 3 T13: -0.0356 T23: -0.0341
REMARK 3 L TENSOR
REMARK 3 L11: 1.6394 L22: 1.9690
REMARK 3 L33: 1.9627 L12: -0.8515
REMARK 3 L13: 0.9317 L23: -0.3284
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.0557 S13: -0.1808
REMARK 3 S21: 0.4365 S22: 0.0377 S23: -0.0182
REMARK 3 S31: -0.0187 S32: -0.0561 S33: 0.0683
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 31 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): -29.9431 3.1791 -27.7136
REMARK 3 T TENSOR
REMARK 3 T11: 0.2405 T22: 0.1215
REMARK 3 T33: 0.2446 T12: 0.0072
REMARK 3 T13: -0.0284 T23: -0.0258
REMARK 3 L TENSOR
REMARK 3 L11: 4.4390 L22: 3.4186
REMARK 3 L33: 3.4682 L12: 0.7831
REMARK 3 L13: -0.1254 L23: -1.0757
REMARK 3 S TENSOR
REMARK 3 S11: 0.1339 S12: 0.0152 S13: 0.6965
REMARK 3 S21: 0.6510 S22: -0.0638 S23: -0.0694
REMARK 3 S31: -0.0063 S32: -0.1203 S33: -0.0762
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 44 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.4906 8.4828 -32.0363
REMARK 3 T TENSOR
REMARK 3 T11: 0.2142 T22: 0.1508
REMARK 3 T33: 0.1840 T12: -0.0306
REMARK 3 T13: -0.0205 T23: 0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 2.6377 L22: 2.7897
REMARK 3 L33: 1.6844 L12: 1.0287
REMARK 3 L13: 1.2102 L23: 0.0366
REMARK 3 S TENSOR
REMARK 3 S11: -0.0741 S12: 0.2119 S13: 0.3516
REMARK 3 S21: 0.1862 S22: 0.0208 S23: -0.0493
REMARK 3 S31: -0.1164 S32: 0.2028 S33: 0.1398
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'F' AND (RESID 67 THROUGH 81 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8511 -14.8656 -37.2126
REMARK 3 T TENSOR
REMARK 3 T11: 0.2482 T22: 0.2405
REMARK 3 T33: 0.2658 T12: -0.0227
REMARK 3 T13: -0.0252 T23: 0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 3.4809 L22: 3.7717
REMARK 3 L33: 3.9718 L12: -0.8561
REMARK 3 L13: 0.8077 L23: 0.0220
REMARK 3 S TENSOR
REMARK 3 S11: -0.4567 S12: -0.3808 S13: -0.3428
REMARK 3 S21: -0.1575 S22: 0.6619 S23: 0.0244
REMARK 3 S31: 0.5405 S32: -0.6014 S33: -0.2505
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'G' AND (RESID -2 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.3718 -10.6232 -48.1396
REMARK 3 T TENSOR
REMARK 3 T11: 0.2728 T22: 0.1364
REMARK 3 T33: 0.2402 T12: 0.0387
REMARK 3 T13: -0.0510 T23: 0.0082
REMARK 3 L TENSOR
REMARK 3 L11: 0.6907 L22: 1.5107
REMARK 3 L33: 0.4631 L12: 0.3583
REMARK 3 L13: 0.4295 L23: -0.4164
REMARK 3 S TENSOR
REMARK 3 S11: 0.0182 S12: 0.1128 S13: 0.0029
REMARK 3 S21: 0.0523 S22: -0.1635 S23: -0.0159
REMARK 3 S31: 0.1949 S32: 0.1791 S33: 0.0810
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 31 THROUGH 43 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8325 2.5093 -53.6208
REMARK 3 T TENSOR
REMARK 3 T11: 0.2988 T22: 0.0614
REMARK 3 T33: 0.2362 T12: 0.0026
REMARK 3 T13: 0.0381 T23: -0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 2.2677 L22: 3.4320
REMARK 3 L33: 1.0637 L12: 0.4545
REMARK 3 L13: -0.6518 L23: -1.3026
REMARK 3 S TENSOR
REMARK 3 S11: 0.5211 S12: -0.1880 S13: 0.3112
REMARK 3 S21: -0.0736 S22: -0.1477 S23: -0.3373
REMARK 3 S31: -0.5178 S32: -0.0247 S33: 0.0467
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 44 THROUGH 48 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.2374 13.1204 -55.0199
REMARK 3 T TENSOR
REMARK 3 T11: 0.8154 T22: 0.2930
REMARK 3 T33: 0.3305 T12: 0.0170
REMARK 3 T13: -0.0043 T23: 0.0774
REMARK 3 L TENSOR
REMARK 3 L11: 2.9774 L22: 6.3267
REMARK 3 L33: 5.1024 L12: 0.8296
REMARK 3 L13: -0.2810 L23: -5.6387
REMARK 3 S TENSOR
REMARK 3 S11: 0.3169 S12: 0.6492 S13: -0.1404
REMARK 3 S21: -1.5191 S22: -0.1259 S23: -0.4030
REMARK 3 S31: 1.1444 S32: -0.0099 S33: 0.4678
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 49 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): -32.9297 7.1898 -50.8113
REMARK 3 T TENSOR
REMARK 3 T11: 0.1982 T22: 0.1602
REMARK 3 T33: 0.1941 T12: 0.0028
REMARK 3 T13: -0.0800 T23: 0.0504
REMARK 3 L TENSOR
REMARK 3 L11: 2.5022 L22: 1.4087
REMARK 3 L33: 1.7264 L12: 0.1168
REMARK 3 L13: -0.7876 L23: -0.0977
REMARK 3 S TENSOR
REMARK 3 S11: -0.1328 S12: 0.1931 S13: -0.2404
REMARK 3 S21: -0.3070 S22: 0.1639 S23: 0.0656
REMARK 3 S31: -0.0024 S32: -0.3396 S33: -0.2543
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 59 THROUGH 66 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.6257 5.8790 -44.4160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2509 T22: 0.2134
REMARK 3 T33: 0.2130 T12: 0.0374
REMARK 3 T13: -0.0356 T23: -0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 5.3018 L22: 4.6898
REMARK 3 L33: 2.9134 L12: -4.6896
REMARK 3 L13: 2.8524 L23: -3.3914
REMARK 3 S TENSOR
REMARK 3 S11: -0.2199 S12: -0.2418 S13: 0.7470
REMARK 3 S21: 0.3714 S22: -0.0617 S23: -0.9613
REMARK 3 S31: 0.2497 S32: 0.0976 S33: -0.0556
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 67 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.1185 -12.6513 -42.3179
REMARK 3 T TENSOR
REMARK 3 T11: 0.2696 T22: 0.1594
REMARK 3 T33: 0.2333 T12: 0.0474
REMARK 3 T13: -0.0384 T23: 0.0466
REMARK 3 L TENSOR
REMARK 3 L11: 0.3817 L22: 5.2782
REMARK 3 L33: 3.0838 L12: -0.7603
REMARK 3 L13: -0.6719 L23: 3.0549
REMARK 3 S TENSOR
REMARK 3 S11: -0.0816 S12: -0.0597 S13: 0.0304
REMARK 3 S21: 0.4107 S22: -0.1445 S23: -0.8972
REMARK 3 S31: 0.3965 S32: 0.4133 S33: 0.0880
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 79 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): -13.2966 -27.5950 -42.7984
REMARK 3 T TENSOR
REMARK 3 T11: 0.7610 T22: 0.4326
REMARK 3 T33: 0.9046 T12: 0.0346
REMARK 3 T13: -0.1412 T23: -0.0697
REMARK 3 L TENSOR
REMARK 3 L11: 1.3741 L22: 6.1451
REMARK 3 L33: 2.1564 L12: -2.1016
REMARK 3 L13: 1.3219 L23: -0.3769
REMARK 3 S TENSOR
REMARK 3 S11: 0.3586 S12: 0.0374 S13: -0.1044
REMARK 3 S21: -0.8311 S22: -0.1530 S23: -1.1069
REMARK 3 S31: 0.3879 S32: 0.4720 S33: -0.0529
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): -27.7847 -12.9514 -64.8463
REMARK 3 T TENSOR
REMARK 3 T11: 0.4769 T22: 0.3857
REMARK 3 T33: 0.2666 T12: 0.1759
REMARK 3 T13: -0.1087 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 4.5686 L22: 5.2933
REMARK 3 L33: 3.0253 L12: 1.1487
REMARK 3 L13: -0.8534 L23: 0.4270
REMARK 3 S TENSOR
REMARK 3 S11: 0.5593 S12: -0.1748 S13: -0.7329
REMARK 3 S21: -0.2376 S22: 0.1311 S23: 0.0632
REMARK 3 S31: 0.3635 S32: 0.1764 S33: -0.2282
REMARK 3 TLS GROUP : 21
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 30 )
REMARK 3 ORIGIN FOR THE GROUP (A): -37.3290 -13.8731 -71.7737
REMARK 3 T TENSOR
REMARK 3 T11: 0.4741 T22: 0.3565
REMARK 3 T33: 0.3853 T12: 0.0396
REMARK 3 T13: -0.1383 T23: -0.0639
REMARK 3 L TENSOR
REMARK 3 L11: 6.3221 L22: 2.0837
REMARK 3 L33: 3.0050 L12: -0.3900
REMARK 3 L13: -2.9948 L23: 0.5478
REMARK 3 S TENSOR
REMARK 3 S11: 0.1421 S12: 0.4556 S13: -0.2221
REMARK 3 S21: -0.3328 S22: 0.0855 S23: -0.0532
REMARK 3 S31: 0.8210 S32: 0.1980 S33: -0.2267
REMARK 3 TLS GROUP : 22
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 31 THROUGH 57 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.1126 -6.3425 -74.0606
REMARK 3 T TENSOR
REMARK 3 T11: 0.2911 T22: 0.2234
REMARK 3 T33: 0.1729 T12: -0.0146
REMARK 3 T13: -0.0332 T23: 0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 4.5198 L22: 2.1855
REMARK 3 L33: 1.9449 L12: -0.6939
REMARK 3 L13: 1.4388 L23: -0.2048
REMARK 3 S TENSOR
REMARK 3 S11: 0.1994 S12: -0.1617 S13: -0.1111
REMARK 3 S21: 0.1624 S22: 0.0221 S23: 0.0909
REMARK 3 S31: 0.1049 S32: 0.1739 S33: -0.1948
REMARK 3 TLS GROUP : 23
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 58 THROUGH 67 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.5327 -0.1885 -67.1161
REMARK 3 T TENSOR
REMARK 3 T11: 0.1891 T22: 0.2567
REMARK 3 T33: 0.2395 T12: -0.0335
REMARK 3 T13: 0.0260 T23: -0.0117
REMARK 3 L TENSOR
REMARK 3 L11: 0.7560 L22: 6.2294
REMARK 3 L33: 8.1974 L12: -1.3677
REMARK 3 L13: 0.7010 L23: 3.4625
REMARK 3 S TENSOR
REMARK 3 S11: -0.3054 S12: 0.1457 S13: -0.0410
REMARK 3 S21: -0.5842 S22: 0.6646 S23: -0.1951
REMARK 3 S31: -0.5840 S32: 1.0568 S33: -0.3020
REMARK 3 TLS GROUP : 24
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 68 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): -40.6729 4.0182 -71.4059
REMARK 3 T TENSOR
REMARK 3 T11: 0.1886 T22: 0.2663
REMARK 3 T33: 0.2024 T12: 0.0244
REMARK 3 T13: -0.0077 T23: 0.0199
REMARK 3 L TENSOR
REMARK 3 L11: 2.3087 L22: 1.6469
REMARK 3 L33: 2.1276 L12: -0.1914
REMARK 3 L13: 1.4964 L23: -0.3647
REMARK 3 S TENSOR
REMARK 3 S11: -0.2072 S12: 0.1977 S13: 0.3082
REMARK 3 S21: 0.0413 S22: -0.0938 S23: 0.0468
REMARK 3 S31: -0.0771 S32: -0.1939 S33: 0.2228
REMARK 3 TLS GROUP : 25
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 101 THROUGH 132 )
REMARK 3 ORIGIN FOR THE GROUP (A): -49.4148 6.0275 -69.7860
REMARK 3 T TENSOR
REMARK 3 T11: 0.3139 T22: 0.5201
REMARK 3 T33: 0.3339 T12: 0.1422
REMARK 3 T13: -0.0025 T23: -0.0871
REMARK 3 L TENSOR
REMARK 3 L11: 2.2232 L22: 2.3185
REMARK 3 L33: 1.0221 L12: -0.2898
REMARK 3 L13: 1.5417 L23: -0.1448
REMARK 3 S TENSOR
REMARK 3 S11: -0.1239 S12: -0.5542 S13: 0.4658
REMARK 3 S21: 0.3907 S22: -0.0776 S23: 0.2563
REMARK 3 S31: -0.1560 S32: -1.0602 S33: 0.1236
REMARK 3 TLS GROUP : 26
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 133 THROUGH 151 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.9979 -0.8707 -79.7580
REMARK 3 T TENSOR
REMARK 3 T11: 0.2647 T22: 0.6033
REMARK 3 T33: 0.2526 T12: 0.0142
REMARK 3 T13: -0.0748 T23: 0.0626
REMARK 3 L TENSOR
REMARK 3 L11: 2.2869 L22: 3.7058
REMARK 3 L33: 3.4253 L12: -0.4310
REMARK 3 L13: -0.2491 L23: 0.9599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0815 S12: 0.4236 S13: -0.1571
REMARK 3 S21: -0.3492 S22: -0.0768 S23: 0.7307
REMARK 3 S31: 0.1586 S32: -0.8619 S33: -0.1211
REMARK 3 TLS GROUP : 27
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 16 )
REMARK 3 ORIGIN FOR THE GROUP (A): -43.0340 -13.1945 -50.2718
REMARK 3 T TENSOR
REMARK 3 T11: 0.4168 T22: 0.3282
REMARK 3 T33: 0.1472 T12: -0.1546
REMARK 3 T13: -0.1444 T23: 0.0752
REMARK 3 L TENSOR
REMARK 3 L11: 2.5166 L22: 1.7391
REMARK 3 L33: 0.7873 L12: -0.7420
REMARK 3 L13: -0.2242 L23: 0.9498
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: -0.8280 S13: -0.8512
REMARK 3 S21: 0.4268 S22: -0.2399 S23: 0.2202
REMARK 3 S31: 0.6895 S32: -0.2254 S33: -0.3047
REMARK 3 TLS GROUP : 28
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 17 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -56.5030 -9.9688 -45.3713
REMARK 3 T TENSOR
REMARK 3 T11: 0.1198 T22: 0.9343
REMARK 3 T33: 0.5839 T12: -0.3619
REMARK 3 T13: 0.0616 T23: 0.1474
REMARK 3 L TENSOR
REMARK 3 L11: 0.2129 L22: 0.0126
REMARK 3 L33: 0.0127 L12: 0.0502
REMARK 3 L13: -0.0556 L23: -0.0133
REMARK 3 S TENSOR
REMARK 3 S11: -0.0432 S12: -0.0518 S13: 0.0942
REMARK 3 S21: 0.1733 S22: -0.0596 S23: 0.3787
REMARK 3 S31: 0.0037 S32: -0.2351 S33: -0.1361
REMARK 3 TLS GROUP : 29
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 23 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): -46.0448 -4.4769 -45.4953
REMARK 3 T TENSOR
REMARK 3 T11: 0.2992 T22: 0.4396
REMARK 3 T33: 0.2395 T12: -0.1206
REMARK 3 T13: 0.0247 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 5.0210 L22: 2.4039
REMARK 3 L33: 2.9340 L12: 2.4563
REMARK 3 L13: 2.4755 L23: 0.8831
REMARK 3 S TENSOR
REMARK 3 S11: 0.0660 S12: -0.1202 S13: -0.2529
REMARK 3 S21: 0.5786 S22: -0.2030 S23: 0.1198
REMARK 3 S31: -0.0260 S32: -0.6494 S33: 0.0436
REMARK 3 TLS GROUP : 30
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 35 THROUGH 44 )
REMARK 3 ORIGIN FOR THE GROUP (A): -44.2127 0.4526 -51.8195
REMARK 3 T TENSOR
REMARK 3 T11: 0.2331 T22: 0.2712
REMARK 3 T33: 0.3217 T12: -0.0046
REMARK 3 T13: -0.1529 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 6.4817 L22: 0.5302
REMARK 3 L33: 1.4983 L12: 0.8530
REMARK 3 L13: 1.8568 L23: -0.3680
REMARK 3 S TENSOR
REMARK 3 S11: 0.2013 S12: -0.1936 S13: 1.2736
REMARK 3 S21: 0.1848 S22: 0.3203 S23: 0.3405
REMARK 3 S31: 0.0205 S32: -0.6780 S33: 0.4633
REMARK 3 TLS GROUP : 31
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 45 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -54.1014 -3.7260 -57.3150
REMARK 3 T TENSOR
REMARK 3 T11: 0.2696 T22: 0.7644
REMARK 3 T33: 0.5290 T12: -0.0255
REMARK 3 T13: -0.0733 T23: -0.0550
REMARK 3 L TENSOR
REMARK 3 L11: 2.3620 L22: 4.3540
REMARK 3 L33: 4.7641 L12: -1.3430
REMARK 3 L13: -3.2400 L23: 2.8742
REMARK 3 S TENSOR
REMARK 3 S11: 0.4320 S12: -0.4769 S13: 0.6171
REMARK 3 S21: -0.3442 S22: -0.2900 S23: 0.3998
REMARK 3 S31: -0.5558 S32: -0.4566 S33: -0.0356
REMARK 3 TLS GROUP : 32
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 55 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -50.4668 -7.1051 -55.9751
REMARK 3 T TENSOR
REMARK 3 T11: 0.2768 T22: 0.4677
REMARK 3 T33: 0.2461 T12: -0.0905
REMARK 3 T13: -0.0490 T23: -0.0253
REMARK 3 L TENSOR
REMARK 3 L11: 3.1582 L22: 2.1221
REMARK 3 L33: 2.4023 L12: 0.9536
REMARK 3 L13: -0.9336 L23: -0.4858
REMARK 3 S TENSOR
REMARK 3 S11: 0.1952 S12: -0.0415 S13: 0.0021
REMARK 3 S21: 0.1081 S22: 0.0464 S23: 0.7039
REMARK 3 S31: 0.2834 S32: -0.8052 S33: -0.2102
REMARK 3 TLS GROUP : 33
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 22 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.6298 -11.2108 -31.1325
REMARK 3 T TENSOR
REMARK 3 T11: 0.3742 T22: 0.3500
REMARK 3 T33: 0.2820 T12: 0.0627
REMARK 3 T13: -0.0512 T23: -0.0157
REMARK 3 L TENSOR
REMARK 3 L11: 1.9167 L22: 1.1535
REMARK 3 L33: 0.7386 L12: -0.6712
REMARK 3 L13: -0.3589 L23: -0.2109
REMARK 3 S TENSOR
REMARK 3 S11: -0.1121 S12: 0.5000 S13: -0.4662
REMARK 3 S21: -0.2235 S22: -0.0964 S23: -0.0718
REMARK 3 S31: 0.3870 S32: 0.2052 S33: 0.0074
REMARK 3 TLS GROUP : 34
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 23 THROUGH 34 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5176 -3.5537 -35.1472
REMARK 3 T TENSOR
REMARK 3 T11: 0.3915 T22: 0.3689
REMARK 3 T33: 0.2679 T12: 0.1347
REMARK 3 T13: -0.0181 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 6.9357 L22: 3.0903
REMARK 3 L33: 4.7310 L12: -0.3991
REMARK 3 L13: 1.8544 L23: -0.9649
REMARK 3 S TENSOR
REMARK 3 S11: -0.0114 S12: 0.6813 S13: 0.2617
REMARK 3 S21: -0.5209 S22: -0.4317 S23: -0.1613
REMARK 3 S31: 0.1383 S32: 0.6971 S33: 0.4239
REMARK 3 TLS GROUP : 35
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 35 THROUGH 65 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.8580 -4.1838 -26.2518
REMARK 3 T TENSOR
REMARK 3 T11: 0.2736 T22: 0.5605
REMARK 3 T33: 0.3450 T12: 0.1060
REMARK 3 T13: -0.0907 T23: 0.0415
REMARK 3 L TENSOR
REMARK 3 L11: 2.2124 L22: 0.5498
REMARK 3 L33: 1.4680 L12: 0.0325
REMARK 3 L13: -0.3901 L23: 0.2931
REMARK 3 S TENSOR
REMARK 3 S11: 0.2666 S12: 0.2067 S13: 0.3651
REMARK 3 S21: -0.1239 S22: -0.2800 S23: -0.1406
REMARK 3 S31: 0.0921 S32: 1.2499 S33: 0.1019
REMARK 3 TLS GROUP : 36
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 66 THROUGH 76 )
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5454 1.1606 -22.1886
REMARK 3 T TENSOR
REMARK 3 T11: 0.2915 T22: 0.2292
REMARK 3 T33: 0.2401 T12: 0.0121
REMARK 3 T13: -0.0570 T23: 0.0517
REMARK 3 L TENSOR
REMARK 3 L11: 1.9798 L22: 1.4695
REMARK 3 L33: 3.1052 L12: -0.4267
REMARK 3 L13: -0.3965 L23: 1.7469
REMARK 3 S TENSOR
REMARK 3 S11: 0.0718 S12: 0.0592 S13: 0.0061
REMARK 3 S21: -0.1283 S22: -0.0527 S23: -0.0351
REMARK 3 S31: -0.0745 S32: 0.6350 S33: -0.0555
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 3
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A
REMARK 3 SELECTION : CHAIN B
REMARK 3 ATOM PAIRS NUMBER : 1740
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN C
REMARK 3 SELECTION : CHAIN D
REMARK 3 ATOM PAIRS NUMBER : 902
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN F
REMARK 3 SELECTION : CHAIN G
REMARK 3 ATOM PAIRS NUMBER : 856
REMARK 3 RMSD : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5EYA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-NOV-15.
REMARK 100 THE DEPOSITION ID IS D_1000215697.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27181
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 8.100
REMARK 200 R MERGE (I) : 0.17900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.74300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LI CITRATE, 20% PEG 3350, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 26.52350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.55050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.88950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.55050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.52350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.88950
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F, G, B, C, D
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ILE A 152
REMARK 465 GLY F -2
REMARK 465 SER F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 GLU F 3
REMARK 465 LEU F 4
REMARK 465 CYS F 5
REMARK 465 ALA F 82
REMARK 465 ARG F 83
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ILE B 152
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 102 O HOH B 202 1.48
REMARK 500 HE ARG A 6 OE2 GLU F 18 1.56
REMARK 500 HZ2 LYS A 74 O HOH A 208 1.59
REMARK 500 O HOH A 238 O HOH A 239 1.81
REMARK 500 OE2 GLU F 9 O HOH F 201 1.85
REMARK 500 O HOH B 219 O HOH B 230 1.89
REMARK 500 O HOH B 234 O HOH C 121 1.95
REMARK 500 O HOH C 118 O HOH C 120 2.02
REMARK 500 O CYS G 16 O HOH G 201 2.07
REMARK 500 OD2 ASP B 89 O HOH B 201 2.08
REMARK 500 OG1 THR F 67 O HOH F 202 2.10
REMARK 500 O HOH G 222 O HOH G 227 2.11
REMARK 500 OG1 THR C 66 O HOH C 101 2.17
REMARK 500 OE2 GLU C 24 O HOH C 102 2.19
REMARK 500 OE2 GLU G 9 O HOH G 202 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH C 119 O HOH D 101 1455 1.92
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 GLU A 18 63.94 -117.49
REMARK 500 ASN A 31 113.53 -163.68
REMARK 500 LYS A 92 -104.95 -134.54
REMARK 500 ARG G 54 18.84 59.72
REMARK 500 GLU B 18 61.30 -116.46
REMARK 500 ASN B 31 114.12 -165.99
REMARK 500 LYS B 92 -99.75 -136.32
REMARK 500 ALA B 114 72.70 -150.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 13 SG
REMARK 620 2 CYS F 16 SG 110.2
REMARK 620 3 CYS F 33 SG 101.9 107.1
REMARK 620 4 CYS F 36 SG 112.6 111.8 112.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 28 SG
REMARK 620 2 HIS F 30 ND1 113.7
REMARK 620 3 CYS F 50 SG 106.5 107.3
REMARK 620 4 CYS F 53 SG 114.0 104.5 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 13 SG
REMARK 620 2 CYS G 16 SG 109.6
REMARK 620 3 CYS G 33 SG 104.6 109.1
REMARK 620 4 CYS G 36 SG 110.7 110.4 112.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN G 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS G 28 SG
REMARK 620 2 HIS G 30 ND1 117.0
REMARK 620 3 CYS G 50 SG 107.1 109.1
REMARK 620 4 CYS G 53 SG 106.4 105.9 111.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN F 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN G 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide GLY C 76 and LYS B
REMARK 800 87
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LTB RELATED DB: PDB
REMARK 900 4LTB IS THE COILED-COIL DOMAIN TRIM25
DBREF 5EYA A 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 5EYA F -2 83 UNP Q59GW5 Q59GW5_HUMAN 12 97
DBREF 5EYA G -2 83 UNP Q59GW5 Q59GW5_HUMAN 12 97
DBREF 5EYA B 1 152 UNP P61088 UBE2N_HUMAN 1 152
DBREF 5EYA C 1 76 UNP P0CG47 UBB_HUMAN 1 76
DBREF 5EYA D 1 76 UNP P0CG47 UBB_HUMAN 1 76
SEQADV 5EYA LYS A 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQADV 5EYA HIS F 0 UNP Q59GW5 ALA 14 CONFLICT
SEQADV 5EYA HIS G 0 UNP Q59GW5 ALA 14 CONFLICT
SEQADV 5EYA LYS B 87 UNP P61088 CYS 87 ENGINEERED MUTATION
SEQRES 1 A 152 MET ALA GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN
SEQRES 2 A 152 ARG LEU LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU
SEQRES 3 A 152 PRO ASP GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE
SEQRES 4 A 152 ALA GLY PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE
SEQRES 5 A 152 LYS LEU GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA
SEQRES 6 A 152 ALA PRO LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO
SEQRES 7 A 152 ASN VAL ASP LYS LEU GLY ARG ILE LYS LEU ASP ILE LEU
SEQRES 8 A 152 LYS ASP LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL
SEQRES 9 A 152 LEU LEU SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO
SEQRES 10 A 152 ASP ASP PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS
SEQRES 11 A 152 THR ASN GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP
SEQRES 12 A 152 THR ARG LEU TYR ALA MET ASN ASN ILE
SEQRES 1 F 86 GLY SER HIS MET ALA GLU LEU CYS PRO LEU ALA GLU GLU
SEQRES 2 F 86 LEU SER CYS SER ILE CYS LEU GLU PRO PHE LYS GLU PRO
SEQRES 3 F 86 VAL THR THR PRO CYS GLY HIS ASN PHE CYS GLY SER CYS
SEQRES 4 F 86 LEU ASN GLU THR TRP ALA VAL GLN GLY SER PRO TYR LEU
SEQRES 5 F 86 CYS PRO GLN CYS ARG ALA VAL TYR GLN ALA ARG PRO GLN
SEQRES 6 F 86 LEU HIS LYS ASN THR VAL LEU CYS ASN VAL VAL GLU GLN
SEQRES 7 F 86 PHE LEU GLN ALA ASP LEU ALA ARG
SEQRES 1 G 86 GLY SER HIS MET ALA GLU LEU CYS PRO LEU ALA GLU GLU
SEQRES 2 G 86 LEU SER CYS SER ILE CYS LEU GLU PRO PHE LYS GLU PRO
SEQRES 3 G 86 VAL THR THR PRO CYS GLY HIS ASN PHE CYS GLY SER CYS
SEQRES 4 G 86 LEU ASN GLU THR TRP ALA VAL GLN GLY SER PRO TYR LEU
SEQRES 5 G 86 CYS PRO GLN CYS ARG ALA VAL TYR GLN ALA ARG PRO GLN
SEQRES 6 G 86 LEU HIS LYS ASN THR VAL LEU CYS ASN VAL VAL GLU GLN
SEQRES 7 G 86 PHE LEU GLN ALA ASP LEU ALA ARG
SEQRES 1 B 152 MET ALA GLY LEU PRO ARG ARG ILE ILE LYS GLU THR GLN
SEQRES 2 B 152 ARG LEU LEU ALA GLU PRO VAL PRO GLY ILE LYS ALA GLU
SEQRES 3 B 152 PRO ASP GLU SER ASN ALA ARG TYR PHE HIS VAL VAL ILE
SEQRES 4 B 152 ALA GLY PRO GLN ASP SER PRO PHE GLU GLY GLY THR PHE
SEQRES 5 B 152 LYS LEU GLU LEU PHE LEU PRO GLU GLU TYR PRO MET ALA
SEQRES 6 B 152 ALA PRO LYS VAL ARG PHE MET THR LYS ILE TYR HIS PRO
SEQRES 7 B 152 ASN VAL ASP LYS LEU GLY ARG ILE LYS LEU ASP ILE LEU
SEQRES 8 B 152 LYS ASP LYS TRP SER PRO ALA LEU GLN ILE ARG THR VAL
SEQRES 9 B 152 LEU LEU SER ILE GLN ALA LEU LEU SER ALA PRO ASN PRO
SEQRES 10 B 152 ASP ASP PRO LEU ALA ASN ASP VAL ALA GLU GLN TRP LYS
SEQRES 11 B 152 THR ASN GLU ALA GLN ALA ILE GLU THR ALA ARG ALA TRP
SEQRES 12 B 152 THR ARG LEU TYR ALA MET ASN ASN ILE
SEQRES 1 C 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 C 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 C 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 C 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 C 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 C 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
SEQRES 1 D 76 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 76 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 76 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 76 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 76 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 76 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY
HET ZN F 101 1
HET ZN F 102 1
HET ZN G 101 1
HET ZN G 102 1
HETNAM ZN ZINC ION
FORMUL 7 ZN 4(ZN 2+)
FORMUL 11 HOH *180(H2 O)
HELIX 1 AA1 PRO A 5 GLU A 18 1 14
HELIX 2 AA2 LEU A 88 LYS A 92 5 5
HELIX 3 AA3 GLN A 100 ALA A 114 1 15
HELIX 4 AA4 ALA A 122 ASN A 132 1 11
HELIX 5 AA5 ASN A 132 ALA A 148 1 17
HELIX 6 AA6 LEU F 7 LEU F 11 1 5
HELIX 7 AA7 GLY F 34 GLN F 44 1 11
HELIX 8 AA8 ASN F 66 LEU F 81 1 16
HELIX 9 AA9 MET G 1 ALA G 8 5 8
HELIX 10 AB1 GLY G 34 GLN G 44 1 11
HELIX 11 AB2 ASN G 66 ALA G 79 1 14
HELIX 12 AB3 PRO B 5 GLU B 18 1 14
HELIX 13 AB4 LEU B 88 LYS B 92 5 5
HELIX 14 AB5 GLN B 100 ALA B 114 1 15
HELIX 15 AB6 ALA B 122 ASN B 132 1 11
HELIX 16 AB7 ASN B 132 ALA B 148 1 17
HELIX 17 AB8 THR C 22 GLY C 35 1 14
HELIX 18 AB9 LEU C 56 ASN C 60 5 5
HELIX 19 AC1 THR D 22 GLY D 35 1 14
HELIX 20 AC2 PRO D 37 ASP D 39 5 3
SHEET 1 AA1 4 ILE A 23 ASP A 28 0
SHEET 2 AA1 4 ASN A 31 ALA A 40 -1 O VAL A 38 N LYS A 24
SHEET 3 AA1 4 THR A 51 PHE A 57 -1 O LEU A 56 N PHE A 35
SHEET 4 AA1 4 LYS A 68 PHE A 71 -1 O LYS A 68 N PHE A 57
SHEET 1 AA2 2 PRO F 23 THR F 25 0
SHEET 2 AA2 2 ASN F 31 CYS F 33 -1 O PHE F 32 N VAL F 24
SHEET 1 AA3 2 TYR F 48 LEU F 49 0
SHEET 2 AA3 2 VAL F 56 TYR F 57 -1 O TYR F 57 N TYR F 48
SHEET 1 AA4 2 PRO G 23 THR G 25 0
SHEET 2 AA4 2 ASN G 31 CYS G 33 -1 O PHE G 32 N VAL G 24
SHEET 1 AA5 2 TYR G 48 LEU G 49 0
SHEET 2 AA5 2 VAL G 56 TYR G 57 -1 O TYR G 57 N TYR G 48
SHEET 1 AA6 4 ILE B 23 ASP B 28 0
SHEET 2 AA6 4 ASN B 31 ALA B 40 -1 O VAL B 38 N LYS B 24
SHEET 3 AA6 4 THR B 51 PHE B 57 -1 O LEU B 54 N VAL B 37
SHEET 4 AA6 4 LYS B 68 PHE B 71 -1 O LYS B 68 N PHE B 57
SHEET 1 AA7 5 THR C 12 GLU C 16 0
SHEET 2 AA7 5 GLN C 2 LYS C 6 -1 N ILE C 3 O LEU C 15
SHEET 3 AA7 5 THR C 66 LEU C 71 1 O LEU C 67 N LYS C 6
SHEET 4 AA7 5 GLN C 41 PHE C 45 -1 N ILE C 44 O HIS C 68
SHEET 5 AA7 5 LYS C 48 GLN C 49 -1 O LYS C 48 N PHE C 45
SHEET 1 AA8 5 THR D 12 GLU D 16 0
SHEET 2 AA8 5 GLN D 2 LYS D 6 -1 N ILE D 3 O LEU D 15
SHEET 3 AA8 5 THR D 66 LEU D 71 1 O LEU D 69 N LYS D 6
SHEET 4 AA8 5 GLN D 41 PHE D 45 -1 N ILE D 44 O HIS D 68
SHEET 5 AA8 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
LINK NZ LYS A 87 C GLY D 76 1555 1555 1.32
LINK SG CYS F 13 ZN ZN F 102 1555 1555 2.13
LINK SG CYS F 16 ZN ZN F 102 1555 1555 2.12
LINK SG CYS F 28 ZN ZN F 101 1555 1555 2.13
LINK ND1 HIS F 30 ZN ZN F 101 1555 1555 2.08
LINK SG CYS F 33 ZN ZN F 102 1555 1555 2.15
LINK SG CYS F 36 ZN ZN F 102 1555 1555 2.12
LINK SG CYS F 50 ZN ZN F 101 1555 1555 2.12
LINK SG CYS F 53 ZN ZN F 101 1555 1555 2.11
LINK SG CYS G 13 ZN ZN G 102 1555 1555 2.14
LINK SG CYS G 16 ZN ZN G 102 1555 1555 2.11
LINK SG CYS G 28 ZN ZN G 101 1555 1555 2.13
LINK ND1 HIS G 30 ZN ZN G 101 1555 1555 2.08
LINK SG CYS G 33 ZN ZN G 102 1555 1555 2.14
LINK SG CYS G 36 ZN ZN G 102 1555 1555 2.12
LINK SG CYS G 50 ZN ZN G 101 1555 1555 2.13
LINK SG CYS G 53 ZN ZN G 101 1555 1555 2.11
LINK NZ LYS B 87 C GLY C 76 1555 1555 1.32
CISPEP 1 TYR A 62 PRO A 63 0 6.43
CISPEP 2 SER F 46 PRO F 47 0 1.86
CISPEP 3 SER G 46 PRO G 47 0 1.94
CISPEP 4 TYR B 62 PRO B 63 0 7.54
SITE 1 AC1 4 CYS F 28 HIS F 30 CYS F 50 CYS F 53
SITE 1 AC2 4 CYS F 13 CYS F 16 CYS F 33 CYS F 36
SITE 1 AC3 4 CYS G 28 HIS G 30 CYS G 50 CYS G 53
SITE 1 AC4 4 CYS G 13 CYS G 16 CYS G 33 CYS G 36
SITE 1 AC5 18 PHE B 47 ILE B 75 HIS B 77 ASN B 79
SITE 2 AC5 18 ILE B 86 LEU B 88 ASP B 119 PRO B 120
SITE 3 AC5 18 LEU B 121 GLN B 128 TRP B 129 ALA B 136
SITE 4 AC5 18 THR B 139 TRP B 143 HOH B 212 HOH B 224
SITE 5 AC5 18 ARG C 74 GLY C 75
CRYST1 53.047 75.779 169.101 90.00 90.00 90.00 P 21 21 21 8
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 0.018851 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013196 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005914 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
