HEADER GENE REGULATION 11-JUL-18 6H1E
TITLE CRYSTAL STRUCTURE OF C21ORF127-TRMT112 IN COMPLEX WITH SAH AND H4
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEMK METHYLTRANSFERASE FAMILY MEMBER 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: M.HSAHEMK2P,N(6)-ADENINE-SPECIFIC DNA METHYLTRANSFERASE 1;
COMPND 5 EC: 2.1.1.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: MULTIFUNCTIONAL METHYLTRANSFERASE SUBUNIT TRM112-LIKE
COMPND 9 PROTEIN;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: TRNA METHYLTRANSFERASE 112 HOMOLOG;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: HISTONE H4 PEPTIDE;
COMPND 15 CHAIN: S;
COMPND 16 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: N6AMT1, C21ORF127, HEMK2, PRED28;
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 GENE: TRMT112, AD-001, HSPC152, HSPC170;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
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
KEYWDS PROTEIN METHYLTRANSFERASE, HISTONE METHYLATION, COMPLEX, SAH, GENE
KEYWDS 2 REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.WANG,B.HERMANN,E.METZGER,L.PENG,O.EINSLE,R.SCHUELE
REVDAT 2 17-JAN-24 6H1E 1 REMARK
REVDAT 1 22-MAY-19 6H1E 0
JRNL AUTH E.METZGER,S.WANG,S.URBAN,D.WILLMANN,A.SCHMIDT,A.OFFERMANN,
JRNL AUTH 2 A.ALLEN,M.SUM,N.OBIER,F.COTTARD,S.ULFERTS,B.T.PRECA,
JRNL AUTH 3 B.HERMANN,J.MAURER,H.GRESCHIK,V.HORNUNG,O.EINSLE,S.PERNER,
JRNL AUTH 4 A.IMHOF,M.JUNG,R.SCHULE
JRNL TITL KMT9 MONOMETHYLATES HISTONE H4 LYSINE 12 AND CONTROLS
JRNL TITL 2 PROLIFERATION OF PROSTATE CANCER CELLS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 26 361 2019
JRNL REFN ESSN 1545-9985
JRNL PMID 31061526
JRNL DOI 10.1038/S41594-019-0219-9
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 27325
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.940
REMARK 3 FREE R VALUE TEST SET COUNT : 1349
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 47.0200 - 4.0900 1.00 2814 148 0.1573 0.2073
REMARK 3 2 4.0900 - 3.2500 1.00 2616 149 0.1601 0.2116
REMARK 3 3 3.2500 - 2.8400 1.00 2619 146 0.2007 0.2400
REMARK 3 4 2.8400 - 2.5800 1.00 2571 135 0.2088 0.2828
REMARK 3 5 2.5800 - 2.3900 1.00 2583 133 0.2041 0.2594
REMARK 3 6 2.3900 - 2.2500 1.00 2574 120 0.2180 0.2984
REMARK 3 7 2.2500 - 2.1400 1.00 2552 142 0.2360 0.2766
REMARK 3 8 2.1400 - 2.0500 1.00 2521 147 0.2629 0.2940
REMARK 3 9 2.0500 - 1.9700 1.00 2577 113 0.2958 0.3032
REMARK 3 10 1.9700 - 1.9000 1.00 2549 116 0.3463 0.3772
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.287
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.55
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.97
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 : 0.007 2587
REMARK 3 ANGLE : 0.917 3510
REMARK 3 CHIRALITY : 0.055 404
REMARK 3 PLANARITY : 0.006 454
REMARK 3 DIHEDRAL : 7.239 1564
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 16
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'S' AND (RESID 11 THROUGH 15 )
REMARK 3 ORIGIN FOR THE GROUP (A): -7.5154 -20.8498 -25.0822
REMARK 3 T TENSOR
REMARK 3 T11: 0.8958 T22: 0.7547
REMARK 3 T33: 0.5310 T12: -0.0955
REMARK 3 T13: 0.0037 T23: -0.2189
REMARK 3 L TENSOR
REMARK 3 L11: 9.3503 L22: 3.3928
REMARK 3 L33: 0.0216 L12: -4.0396
REMARK 3 L13: 0.2214 L23: -0.0832
REMARK 3 S TENSOR
REMARK 3 S11: 0.9850 S12: 0.5432 S13: -0.4383
REMARK 3 S21: -0.6414 S22: 0.2623 S23: -0.9183
REMARK 3 S31: 0.6133 S32: 0.4255 S33: -0.1853
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 7 THROUGH 26 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.9906 -10.2834 -21.1700
REMARK 3 T TENSOR
REMARK 3 T11: 0.4067 T22: 0.6120
REMARK 3 T33: 0.5016 T12: -0.0815
REMARK 3 T13: 0.0591 T23: -0.1323
REMARK 3 L TENSOR
REMARK 3 L11: 2.2833 L22: 3.4390
REMARK 3 L33: 2.3871 L12: 1.0709
REMARK 3 L13: -1.3777 L23: 0.9903
REMARK 3 S TENSOR
REMARK 3 S11: 0.0305 S12: 0.1244 S13: 0.2036
REMARK 3 S21: -0.4299 S22: 0.1692 S23: -1.1619
REMARK 3 S31: -0.1265 S32: 1.3054 S33: -0.1339
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 27 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1560 -4.6640 -22.6427
REMARK 3 T TENSOR
REMARK 3 T11: 0.4010 T22: 0.2264
REMARK 3 T33: 0.1749 T12: -0.0508
REMARK 3 T13: 0.0310 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.9070 L22: 2.7633
REMARK 3 L33: 1.8182 L12: -0.7156
REMARK 3 L13: -0.1538 L23: 1.1771
REMARK 3 S TENSOR
REMARK 3 S11: 0.0889 S12: 0.3299 S13: 0.0575
REMARK 3 S21: -0.6725 S22: 0.0538 S23: -0.2967
REMARK 3 S31: -0.4741 S32: 0.1204 S33: -0.0532
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 129 )
REMARK 3 ORIGIN FOR THE GROUP (A): -20.8334 -9.7278 -16.5934
REMARK 3 T TENSOR
REMARK 3 T11: 0.2288 T22: 0.1522
REMARK 3 T33: 0.2236 T12: -0.0345
REMARK 3 T13: -0.0328 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 0.5869 L22: 1.8589
REMARK 3 L33: 2.1915 L12: -0.9874
REMARK 3 L13: -0.1946 L23: 0.6706
REMARK 3 S TENSOR
REMARK 3 S11: 0.1761 S12: 0.1835 S13: 0.0372
REMARK 3 S21: -0.5064 S22: -0.0802 S23: 0.2042
REMARK 3 S31: -0.1104 S32: -0.1108 S33: 0.0081
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 130 THROUGH 149 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4011 -26.3567 -17.5184
REMARK 3 T TENSOR
REMARK 3 T11: 0.3949 T22: 0.2533
REMARK 3 T33: 0.2997 T12: 0.0024
REMARK 3 T13: -0.0221 T23: -0.0934
REMARK 3 L TENSOR
REMARK 3 L11: 0.5569 L22: 1.4174
REMARK 3 L33: 2.0002 L12: -0.6793
REMARK 3 L13: -0.2335 L23: -0.4700
REMARK 3 S TENSOR
REMARK 3 S11: 0.0435 S12: 0.2355 S13: -0.4261
REMARK 3 S21: 0.0906 S22: 0.0727 S23: 0.1099
REMARK 3 S31: 0.6031 S32: 0.1979 S33: -0.0806
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 150 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): -26.4249 -15.5897 -23.2086
REMARK 3 T TENSOR
REMARK 3 T11: 0.3295 T22: 0.2863
REMARK 3 T33: 0.2861 T12: -0.0286
REMARK 3 T13: -0.0899 T23: -0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 2.4740 L22: 1.3056
REMARK 3 L33: 2.2224 L12: 0.1730
REMARK 3 L13: -0.0530 L23: 0.3475
REMARK 3 S TENSOR
REMARK 3 S11: 0.0933 S12: 0.3430 S13: -0.0942
REMARK 3 S21: -0.3352 S22: -0.1306 S23: 0.2141
REMARK 3 S31: 0.0606 S32: -0.3419 S33: 0.0528
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 178 THROUGH 188 )
REMARK 3 ORIGIN FOR THE GROUP (A): -31.4925 -21.6708 -29.7927
REMARK 3 T TENSOR
REMARK 3 T11: 0.4597 T22: 0.5194
REMARK 3 T33: 0.4509 T12: -0.0681
REMARK 3 T13: -0.1959 T23: -0.0924
REMARK 3 L TENSOR
REMARK 3 L11: 0.5062 L22: 4.0967
REMARK 3 L33: 1.2455 L12: -0.7476
REMARK 3 L13: -0.7713 L23: 1.4394
REMARK 3 S TENSOR
REMARK 3 S11: -0.2601 S12: 0.6186 S13: -0.5901
REMARK 3 S21: -0.0983 S22: 0.2041 S23: 1.1077
REMARK 3 S31: 0.3615 S32: -0.1705 S33: 0.1887
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 189 THROUGH 213 )
REMARK 3 ORIGIN FOR THE GROUP (A): -23.1959 -16.1188 -32.8612
REMARK 3 T TENSOR
REMARK 3 T11: 0.4546 T22: 0.4266
REMARK 3 T33: 0.2395 T12: -0.0185
REMARK 3 T13: -0.0898 T23: -0.0751
REMARK 3 L TENSOR
REMARK 3 L11: 2.0617 L22: 2.5890
REMARK 3 L33: 2.8658 L12: -0.6890
REMARK 3 L13: -0.3697 L23: 1.4479
REMARK 3 S TENSOR
REMARK 3 S11: 0.4039 S12: 0.3613 S13: -0.2126
REMARK 3 S21: -0.6604 S22: -0.2608 S23: 0.2071
REMARK 3 S31: -0.1473 S32: -0.2353 S33: 0.0163
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 9 )
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5493 1.7313 -6.2607
REMARK 3 T TENSOR
REMARK 3 T11: 0.1636 T22: 0.1650
REMARK 3 T33: 0.2629 T12: 0.0006
REMARK 3 T13: -0.0440 T23: -0.0013
REMARK 3 L TENSOR
REMARK 3 L11: 1.1195 L22: 2.7691
REMARK 3 L33: 2.1989 L12: -0.4874
REMARK 3 L13: 0.5059 L23: -0.1784
REMARK 3 S TENSOR
REMARK 3 S11: -0.2715 S12: 0.1905 S13: 0.1515
REMARK 3 S21: -0.1684 S22: 0.1381 S23: 0.1679
REMARK 3 S31: 0.2232 S32: -0.0563 S33: -0.0165
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 10 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0281 -4.1323 0.8574
REMARK 3 T TENSOR
REMARK 3 T11: 0.1757 T22: 0.1874
REMARK 3 T33: 0.2411 T12: -0.0268
REMARK 3 T13: 0.0049 T23: 0.0351
REMARK 3 L TENSOR
REMARK 3 L11: 1.6346 L22: 3.1923
REMARK 3 L33: 2.7082 L12: -0.4058
REMARK 3 L13: 0.8810 L23: -0.0573
REMARK 3 S TENSOR
REMARK 3 S11: -0.0711 S12: -0.2400 S13: -0.2583
REMARK 3 S21: 0.1833 S22: 0.1817 S23: 0.2206
REMARK 3 S31: 0.3757 S32: -0.3645 S33: -0.0177
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 34 THROUGH 51 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2893 10.0190 -14.2047
REMARK 3 T TENSOR
REMARK 3 T11: 0.2850 T22: 0.2540
REMARK 3 T33: 0.2409 T12: 0.0041
REMARK 3 T13: -0.0606 T23: 0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 3.2862 L22: 2.7794
REMARK 3 L33: 1.9275 L12: -0.6289
REMARK 3 L13: 0.5170 L23: -0.2585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0966 S12: 0.4477 S13: 0.0689
REMARK 3 S21: -0.1655 S22: -0.0283 S23: 0.1981
REMARK 3 S31: -0.0426 S32: 0.1217 S33: -0.0016
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 52 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): -25.5669 11.5474 0.0856
REMARK 3 T TENSOR
REMARK 3 T11: 0.1709 T22: 0.2041
REMARK 3 T33: 0.3508 T12: 0.0643
REMARK 3 T13: -0.0450 T23: -0.0453
REMARK 3 L TENSOR
REMARK 3 L11: 1.8054 L22: 3.0172
REMARK 3 L33: 2.3010 L12: -0.3006
REMARK 3 L13: -0.3373 L23: -0.0733
REMARK 3 S TENSOR
REMARK 3 S11: -0.0778 S12: -0.3419 S13: 0.5400
REMARK 3 S21: 0.1434 S22: 0.0633 S23: 0.3765
REMARK 3 S31: -0.4523 S32: -0.4511 S33: -0.0359
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 75 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8970 16.4236 -10.7054
REMARK 3 T TENSOR
REMARK 3 T11: 0.2579 T22: 0.1984
REMARK 3 T33: 0.3274 T12: -0.0151
REMARK 3 T13: -0.1029 T23: 0.0674
REMARK 3 L TENSOR
REMARK 3 L11: 3.6612 L22: 2.8333
REMARK 3 L33: 1.6245 L12: -0.4276
REMARK 3 L13: 0.6638 L23: -0.4060
REMARK 3 S TENSOR
REMARK 3 S11: -0.0768 S12: 0.0453 S13: 0.3189
REMARK 3 S21: -0.5636 S22: 0.2348 S23: 0.4475
REMARK 3 S31: -0.1898 S32: -0.2909 S33: 0.0784
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 91 THROUGH 100 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7044 0.4309 -0.4696
REMARK 3 T TENSOR
REMARK 3 T11: 0.1586 T22: 0.1832
REMARK 3 T33: 0.2377 T12: -0.0060
REMARK 3 T13: -0.0317 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 1.2179 L22: 3.0900
REMARK 3 L33: 1.1050 L12: -0.3227
REMARK 3 L13: 0.2289 L23: -0.6731
REMARK 3 S TENSOR
REMARK 3 S11: -0.2238 S12: -0.0646 S13: -0.0586
REMARK 3 S21: 0.0208 S22: 0.1337 S23: -0.0208
REMARK 3 S31: -0.1637 S32: -0.0002 S33: 0.0469
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 101 THROUGH 110 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.7759 -9.5204 4.0614
REMARK 3 T TENSOR
REMARK 3 T11: 0.1471 T22: 0.2671
REMARK 3 T33: 0.3675 T12: -0.0210
REMARK 3 T13: 0.0103 T23: 0.0861
REMARK 3 L TENSOR
REMARK 3 L11: 6.1020 L22: 2.7926
REMARK 3 L33: 3.6254 L12: 1.2200
REMARK 3 L13: -3.1885 L23: -1.1410
REMARK 3 S TENSOR
REMARK 3 S11: -0.1184 S12: -0.0601 S13: -0.0999
REMARK 3 S21: -0.1378 S22: 0.2732 S23: 0.8941
REMARK 3 S31: 0.0803 S32: -0.3794 S33: 0.0147
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 119 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6576 -9.3754 -4.1361
REMARK 3 T TENSOR
REMARK 3 T11: 0.2562 T22: 0.2036
REMARK 3 T33: 0.2662 T12: -0.0308
REMARK 3 T13: 0.0197 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 3.8929 L22: 5.9452
REMARK 3 L33: 3.1675 L12: 0.6024
REMARK 3 L13: 1.0554 L23: 0.4585
REMARK 3 S TENSOR
REMARK 3 S11: 0.1659 S12: -0.0406 S13: -0.5926
REMARK 3 S21: 0.0643 S22: -0.2318 S23: 0.0955
REMARK 3 S31: 0.5896 S32: 0.1085 S33: 0.0165
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 6H1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUL-18.
REMARK 100 THE DEPOSITION ID IS D_1200010863.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-17
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27384
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 22.50
REMARK 200 R MERGE (I) : 0.18700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 1.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 21.90
REMARK 200 R MERGE FOR SHELL (I) : 2.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 6H1D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 1.1-1.3 M SODIUM
REMARK 280 CITRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 35.61550
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.61550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 65.40400
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.61550
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.61550
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 65.40400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.61550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.61550
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 65.40400
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.61550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.61550
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 65.40400
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, S
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 SER A 214
REMARK 465 MET B 1
REMARK 465 VAL B 17
REMARK 465 GLY B 18
REMARK 465 SER B 19
REMARK 465 SER B 120
REMARK 465 GLU B 121
REMARK 465 GLU B 122
REMARK 465 GLU B 123
REMARK 465 THR B 124
REMARK 465 GLU B 125
REMARK 465 SER B 126
REMARK 465 SER S 1
REMARK 465 GLY S 2
REMARK 465 ARG S 3
REMARK 465 GLY S 4
REMARK 465 LYS S 5
REMARK 465 GLY S 6
REMARK 465 GLY S 7
REMARK 465 LYS S 8
REMARK 465 GLY S 9
REMARK 465 LEU S 10
REMARK 465 LYS S 16
REMARK 465 ARG S 17
REMARK 465 HIS S 18
REMARK 465 ARG S 19
REMARK 465 LYS S 20
REMARK 465 VAL S 21
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 HIS A 11 40.09 -151.35
REMARK 500 LEU A 104 -101.96 53.78
REMARK 500 MLZ S 12 61.05 37.94
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 SAH A 301
DBREF 6H1E A 8 214 UNP Q9Y5N5 HEMK2_HUMAN 8 214
DBREF 6H1E B 3 126 UNP Q9UI30 TR112_HUMAN 2 125
DBREF 6H1E S 1 21 PDB 6H1E 6H1E 1 21
SEQADV 6H1E SER A 7 UNP Q9Y5N5 EXPRESSION TAG
SEQADV 6H1E MET B 1 UNP Q9UI30 INITIATING METHIONINE
SEQADV 6H1E GLY B 2 UNP Q9UI30 EXPRESSION TAG
SEQRES 1 A 208 SER THR PRO PHE HIS GLY HIS VAL GLY ARG GLY ALA PHE
SEQRES 2 A 208 SER ASP VAL TYR GLU PRO ALA GLU ASP THR PHE LEU LEU
SEQRES 3 A 208 LEU ASP ALA LEU GLU ALA ALA ALA ALA GLU LEU ALA GLY
SEQRES 4 A 208 VAL GLU ILE CYS LEU GLU VAL GLY SER GLY SER GLY VAL
SEQRES 5 A 208 VAL SER ALA PHE LEU ALA SER MET ILE GLY PRO GLN ALA
SEQRES 6 A 208 LEU TYR MET CYS THR ASP ILE ASN PRO GLU ALA ALA ALA
SEQRES 7 A 208 CYS THR LEU GLU THR ALA ARG CYS ASN LYS VAL HIS ILE
SEQRES 8 A 208 GLN PRO VAL ILE THR ASP LEU VAL LYS GLY LEU LEU PRO
SEQRES 9 A 208 ARG LEU THR GLU LYS VAL ASP LEU LEU VAL PHE ASN PRO
SEQRES 10 A 208 PRO TYR VAL VAL THR PRO PRO GLN GLU VAL GLY SER HIS
SEQRES 11 A 208 GLY ILE GLU ALA ALA TRP ALA GLY GLY ARG ASN GLY ARG
SEQRES 12 A 208 GLU VAL MET ASP ARG PHE PHE PRO LEU VAL PRO ASP LEU
SEQRES 13 A 208 LEU SER PRO ARG GLY LEU PHE TYR LEU VAL THR ILE LYS
SEQRES 14 A 208 GLU ASN ASN PRO GLU GLU ILE LEU LYS ILE MET LYS THR
SEQRES 15 A 208 LYS GLY LEU GLN GLY THR THR ALA LEU SER ARG GLN ALA
SEQRES 16 A 208 GLY GLN GLU THR LEU SER VAL LEU LYS PHE THR LYS SER
SEQRES 1 B 126 MET GLY LYS LEU LEU THR HIS ASN LEU LEU SER SER HIS
SEQRES 2 B 126 VAL ARG GLY VAL GLY SER ARG GLY PHE PRO LEU ARG LEU
SEQRES 3 B 126 GLN ALA THR GLU VAL ARG ILE CYS PRO VAL GLU PHE ASN
SEQRES 4 B 126 PRO ASN PHE VAL ALA ARG MET ILE PRO LYS VAL GLU TRP
SEQRES 5 B 126 SER ALA PHE LEU GLU ALA ALA ASP ASN LEU ARG LEU ILE
SEQRES 6 B 126 GLN VAL PRO LYS GLY PRO VAL GLU GLY TYR GLU GLU ASN
SEQRES 7 B 126 GLU GLU PHE LEU ARG THR MET HIS HIS LEU LEU LEU GLU
SEQRES 8 B 126 VAL GLU VAL ILE GLU GLY THR LEU GLN CYS PRO GLU SER
SEQRES 9 B 126 GLY ARG MET PHE PRO ILE SER ARG GLY ILE PRO ASN MET
SEQRES 10 B 126 LEU LEU SER GLU GLU GLU THR GLU SER
SEQRES 1 S 21 SER GLY ARG GLY LYS GLY GLY LYS GLY LEU GLY MLZ GLY
SEQRES 2 S 21 GLY ALA LYS ARG HIS ARG LYS VAL
HET MLZ S 12 10
HET SAH A 301 26
HETNAM MLZ N-METHYL-LYSINE
HETNAM SAH S-ADENOSYL-L-HOMOCYSTEINE
FORMUL 3 MLZ C7 H16 N2 O2
FORMUL 4 SAH C14 H20 N6 O5 S
FORMUL 5 HOH *74(H2 O)
HELIX 1 AA1 ARG A 16 SER A 20 5 5
HELIX 2 AA2 ALA A 26 ALA A 39 1 14
HELIX 3 AA3 ALA A 40 ALA A 44 5 5
HELIX 4 AA4 GLY A 57 GLY A 68 1 12
HELIX 5 AA5 ASN A 79 ASN A 93 1 15
HELIX 6 AA6 PRO A 129 VAL A 133 5 5
HELIX 7 AA7 GLY A 137 TRP A 142 5 6
HELIX 8 AA8 GLY A 145 GLY A 148 5 4
HELIX 9 AA9 ARG A 149 PHE A 156 1 8
HELIX 10 AB1 LEU A 158 LEU A 162 1 5
HELIX 11 AB2 ASN A 178 LYS A 189 1 12
HELIX 12 AB3 LYS B 3 ASN B 8 1 6
HELIX 13 AB4 ASN B 39 ILE B 47 1 9
HELIX 14 AB5 PRO B 48 VAL B 50 5 3
HELIX 15 AB6 GLU B 51 LEU B 62 1 12
HELIX 16 AB7 GLY B 74 GLU B 77 5 4
HELIX 17 AB8 ASN B 78 GLU B 91 1 14
SHEET 1 AA1 7 GLN A 98 ILE A 101 0
SHEET 2 AA1 7 LEU A 72 ASP A 77 1 N TYR A 73 O GLN A 98
SHEET 3 AA1 7 ILE A 48 VAL A 52 1 N CYS A 49 O MET A 74
SHEET 4 AA1 7 VAL A 116 PHE A 121 1 O VAL A 120 N VAL A 52
SHEET 5 AA1 7 LEU A 163 ILE A 174 1 O LEU A 168 N LEU A 119
SHEET 6 AA1 7 GLU A 204 THR A 212 -1 O LEU A 209 N LEU A 171
SHEET 7 AA1 7 GLN A 192 ALA A 201 -1 N LEU A 197 O VAL A 208
SHEET 1 AA2 4 ARG B 25 ILE B 33 0
SHEET 2 AA2 4 VAL B 92 GLN B 100 -1 O GLU B 93 N ARG B 32
SHEET 3 AA2 4 MET B 107 SER B 111 -1 O PHE B 108 N LEU B 99
SHEET 4 AA2 4 ILE B 114 PRO B 115 -1 O ILE B 114 N SER B 111
LINK C GLY S 11 N MLZ S 12 1555 1555 1.33
LINK C MLZ S 12 N GLY S 13 1555 1555 1.33
CISPEP 1 LEU A 109 PRO A 110 0 6.50
CISPEP 2 PHE B 22 PRO B 23 0 -3.31
SITE 1 AC1 21 TYR A 23 THR A 29 GLU A 51 GLY A 53
SITE 2 AC1 21 SER A 54 GLY A 55 VAL A 59 ASP A 77
SITE 3 AC1 21 ILE A 78 THR A 102 ASP A 103 LEU A 104
SITE 4 AC1 21 ASN A 122 ALA A 140 ARG A 154 HOH A 406
SITE 5 AC1 21 HOH A 412 HOH A 414 HOH A 420 HOH A 425
SITE 6 AC1 21 MLZ S 12
CRYST1 71.231 71.231 130.808 90.00 90.00 90.00 P 42 21 2 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 0.014039 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014039 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007645 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
