HEADER TRANSFERASE 28-JUN-11 3SMQ
TITLE CRYSTAL STRUCTURE OF PROTEIN ARGININE METHYLTRANSFERASE 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN ARGININE N-METHYLTRANSFERASE 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 211-531;
COMPND 5 SYNONYM: HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN METHYLTRANSFERASE-
COMPND 6 LIKE PROTEIN 3;
COMPND 7 EC: 2.1.1.-;
COMPND 8 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: PRMT3, HRMT1L3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-V2R-PRAR2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC
KEYWDS STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, PRMT3,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.DOBROVETSKY,A.DONG,J.R.WALKER,A.SIARHEYEVA,G.SENISTERRA,G.A.WASNEY,
AUTHOR 2 D.SMIL,Y.BOLSHAN,K.T.NGUYEN,A.ALLALI-HASSANI,T.HAJIAN,G.PODA,
AUTHOR 3 C.BOUNTRA,J.WEIGELT,A.M.EDWARDS,R.AL-AWAR,P.J.BROWN,M.SCHAPIRA,
AUTHOR 4 C.H.ARROWSMITH,M.VEDADI,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 13-SEP-23 3SMQ 1 REMARK SEQADV
REVDAT 2 24-JUL-13 3SMQ 1 JRNL
REVDAT 1 31-AUG-11 3SMQ 0
JRNL AUTH A.SIARHEYEVA,G.SENISTERRA,A.ALLALI-HASSANI,A.DONG,
JRNL AUTH 2 E.DOBROVETSKY,G.A.WASNEY,I.CHAU,R.MARCELLUS,T.HAJIAN,F.LIU,
JRNL AUTH 3 I.KORBOUKH,D.SMIL,Y.BOLSHAN,J.MIN,H.WU,H.ZENG,P.LOPPNAU,
JRNL AUTH 4 G.PODA,C.GRIFFIN,A.AMAN,P.J.BROWN,J.JIN,R.AL-AWAR,
JRNL AUTH 5 C.H.ARROWSMITH,M.SCHAPIRA,M.VEDADI
JRNL TITL AN ALLOSTERIC INHIBITOR OF PROTEIN ARGININE
JRNL TITL 2 METHYLTRANSFERASE 3.
JRNL REF STRUCTURE V. 20 1425 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22795084
JRNL DOI 10.1016/J.STR.2012.06.001
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 28754
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT : 954
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1776
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.73
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2330
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 223
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : 1.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.030
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2450 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3324 ; 1.214 ; 1.968
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 307 ; 5.788 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;35.162 ;24.787
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 434 ;11.952 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ;18.008 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 386 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1795 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1514 ; 0.524 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2468 ; 1.027 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 936 ; 1.750 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 856 ; 2.901 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 243 A 253
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8556 12.0996 -3.8731
REMARK 3 T TENSOR
REMARK 3 T11: 0.1414 T22: 0.0900
REMARK 3 T33: 0.2269 T12: 0.0760
REMARK 3 T13: -0.0199 T23: 0.0769
REMARK 3 L TENSOR
REMARK 3 L11: 1.5507 L22: 3.8413
REMARK 3 L33: 11.9432 L12: 3.2745
REMARK 3 L13: -3.7164 L23: -7.2377
REMARK 3 S TENSOR
REMARK 3 S11: -0.0409 S12: -0.1931 S13: -0.1542
REMARK 3 S21: -0.0070 S22: -0.3129 S23: -0.5362
REMARK 3 S31: 0.3613 S32: 0.1300 S33: 0.3538
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 254 A 294
REMARK 3 ORIGIN FOR THE GROUP (A): -17.1681 23.6402 2.5944
REMARK 3 T TENSOR
REMARK 3 T11: 0.1127 T22: 0.1384
REMARK 3 T33: 0.1483 T12: 0.0373
REMARK 3 T13: 0.0078 T23: 0.0269
REMARK 3 L TENSOR
REMARK 3 L11: 0.5825 L22: 1.0477
REMARK 3 L33: 1.1270 L12: -0.3720
REMARK 3 L13: -0.3571 L23: -0.1512
REMARK 3 S TENSOR
REMARK 3 S11: 0.0334 S12: 0.0957 S13: 0.0525
REMARK 3 S21: -0.0236 S22: -0.0233 S23: -0.0091
REMARK 3 S31: 0.0300 S32: -0.1015 S33: -0.0100
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 295 A 337
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4118 30.2660 -4.8683
REMARK 3 T TENSOR
REMARK 3 T11: 0.0966 T22: 0.0951
REMARK 3 T33: 0.2026 T12: 0.0046
REMARK 3 T13: 0.0516 T23: 0.0890
REMARK 3 L TENSOR
REMARK 3 L11: 1.1349 L22: 1.0556
REMARK 3 L33: 1.9990 L12: 0.1513
REMARK 3 L13: 0.4248 L23: 0.7290
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: 0.1815 S13: 0.1750
REMARK 3 S21: -0.1401 S22: -0.0416 S23: -0.2084
REMARK 3 S31: -0.2149 S32: 0.1530 S33: 0.0117
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 338 A 379
REMARK 3 ORIGIN FOR THE GROUP (A): -5.8974 25.1563 11.3920
REMARK 3 T TENSOR
REMARK 3 T11: 0.1294 T22: 0.1166
REMARK 3 T33: 0.1817 T12: 0.0056
REMARK 3 T13: -0.0155 T23: -0.0241
REMARK 3 L TENSOR
REMARK 3 L11: 0.7247 L22: 2.3688
REMARK 3 L33: 0.3990 L12: -1.1110
REMARK 3 L13: 0.3530 L23: -0.7901
REMARK 3 S TENSOR
REMARK 3 S11: -0.0171 S12: -0.0188 S13: 0.0915
REMARK 3 S21: 0.1052 S22: -0.0443 S23: -0.1427
REMARK 3 S31: -0.0861 S32: 0.0938 S33: 0.0614
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 380 A 412
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0877 -8.4137 14.7124
REMARK 3 T TENSOR
REMARK 3 T11: 0.1783 T22: 0.1235
REMARK 3 T33: 0.1038 T12: 0.0289
REMARK 3 T13: -0.0038 T23: 0.0072
REMARK 3 L TENSOR
REMARK 3 L11: 1.4808 L22: 0.9301
REMARK 3 L33: 0.4431 L12: -0.8606
REMARK 3 L13: -0.5045 L23: 0.6727
REMARK 3 S TENSOR
REMARK 3 S11: -0.0173 S12: 0.0327 S13: -0.0812
REMARK 3 S21: 0.0792 S22: 0.0252 S23: 0.0581
REMARK 3 S31: 0.1006 S32: 0.0165 S33: -0.0078
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 413 A 438
REMARK 3 ORIGIN FOR THE GROUP (A): -3.0130 0.9207 18.2255
REMARK 3 T TENSOR
REMARK 3 T11: 0.1271 T22: 0.0956
REMARK 3 T33: 0.1319 T12: -0.0029
REMARK 3 T13: -0.0023 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 1.0655 L22: 1.3349
REMARK 3 L33: 0.8388 L12: -0.8622
REMARK 3 L13: 0.6796 L23: 0.1143
REMARK 3 S TENSOR
REMARK 3 S11: 0.0351 S12: -0.0061 S13: -0.0273
REMARK 3 S21: -0.0308 S22: -0.0137 S23: 0.0926
REMARK 3 S31: 0.0644 S32: -0.0174 S33: -0.0214
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 439 A 465
REMARK 3 ORIGIN FOR THE GROUP (A): -4.4378 10.6707 24.7069
REMARK 3 T TENSOR
REMARK 3 T11: 0.0773 T22: 0.1106
REMARK 3 T33: 0.1503 T12: 0.0246
REMARK 3 T13: -0.0030 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.6020 L22: 3.7098
REMARK 3 L33: 0.8206 L12: -0.2728
REMARK 3 L13: 0.4162 L23: -0.7315
REMARK 3 S TENSOR
REMARK 3 S11: -0.1293 S12: -0.2294 S13: 0.0859
REMARK 3 S21: 0.1230 S22: 0.0055 S23: -0.0751
REMARK 3 S31: -0.0492 S32: -0.1209 S33: 0.1238
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 466 A 494
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6711 12.2243 14.6784
REMARK 3 T TENSOR
REMARK 3 T11: 0.1490 T22: 0.1495
REMARK 3 T33: 0.1510 T12: 0.0189
REMARK 3 T13: 0.0093 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.7779 L22: 1.4566
REMARK 3 L33: 0.1692 L12: -1.1329
REMARK 3 L13: 0.4670 L23: -0.6484
REMARK 3 S TENSOR
REMARK 3 S11: -0.0476 S12: -0.0841 S13: -0.0395
REMARK 3 S21: 0.1127 S22: 0.0751 S23: 0.0677
REMARK 3 S31: 0.0098 S32: -0.0619 S33: -0.0275
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 495 A 519
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9063 -0.5274 22.1766
REMARK 3 T TENSOR
REMARK 3 T11: 0.1356 T22: 0.1133
REMARK 3 T33: 0.1324 T12: -0.0124
REMARK 3 T13: 0.0208 T23: 0.0355
REMARK 3 L TENSOR
REMARK 3 L11: 1.0590 L22: 1.2791
REMARK 3 L33: 0.2727 L12: -0.7388
REMARK 3 L13: 0.4967 L23: -0.0796
REMARK 3 S TENSOR
REMARK 3 S11: 0.0516 S12: 0.0098 S13: -0.1056
REMARK 3 S21: 0.0568 S22: -0.0565 S23: 0.0523
REMARK 3 S31: 0.0098 S32: 0.0940 S33: 0.0049
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 520 A 547
REMARK 3 ORIGIN FOR THE GROUP (A): 6.6695 6.8105 23.2092
REMARK 3 T TENSOR
REMARK 3 T11: 0.1229 T22: 0.1368
REMARK 3 T33: 0.1398 T12: -0.0198
REMARK 3 T13: -0.0102 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 1.6415 L22: 1.0050
REMARK 3 L33: 1.8020 L12: -0.8364
REMARK 3 L13: 0.4379 L23: 0.2191
REMARK 3 S TENSOR
REMARK 3 S11: -0.0277 S12: 0.1018 S13: 0.1018
REMARK 3 S21: 0.0721 S22: -0.0006 S23: -0.1973
REMARK 3 S31: -0.0875 S32: 0.0341 S33: 0.0283
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3SMQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29893
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 11.50
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : 0.07800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.55800
REMARK 200 R SYM FOR SHELL (I) : 0.55800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2FYT
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20.0% PEG 4K, 0.2M MG OAC, 0.1M NA
REMARK 280 CACO PH6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 85.98850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.32450
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.32450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 128.98275
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.32450
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.32450
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 42.99425
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.32450
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.32450
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 128.98275
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.32450
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.32450
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 42.99425
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 85.98850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3690 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 209
REMARK 465 GLY A 210
REMARK 465 SER A 211
REMARK 465 SER A 212
REMARK 465 HIS A 213
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 HIS A 216
REMARK 465 HIS A 217
REMARK 465 HIS A 218
REMARK 465 SER A 219
REMARK 465 SER A 220
REMARK 465 GLY A 221
REMARK 465 LEU A 222
REMARK 465 VAL A 223
REMARK 465 PRO A 224
REMARK 465 ARG A 225
REMARK 465 GLY A 226
REMARK 465 SER A 227
REMARK 465 ASP A 228
REMARK 465 LEU A 229
REMARK 465 GLN A 230
REMARK 465 GLU A 231
REMARK 465 ASP A 232
REMARK 465 GLU A 233
REMARK 465 ASP A 234
REMARK 465 GLY A 235
REMARK 465 VAL A 236
REMARK 465 TYR A 237
REMARK 465 PHE A 238
REMARK 465 SER A 239
REMARK 465 SER A 240
REMARK 465 TYR A 241
REMARK 465 GLY A 242
REMARK 465 ASN A 525
REMARK 465 LYS A 526
REMARK 465 LYS A 527
REMARK 465 ASP A 528
REMARK 465 PRO A 529
REMARK 465 ARG A 530
REMARK 465 GLN A 548
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 243 CG ND1 CD2 CE1 NE2
REMARK 470 ILE A 246 CD1
REMARK 470 GLU A 305 CD OE1 OE2
REMARK 470 ARG A 315 CZ NH1 NH2
REMARK 470 LYS A 329 CE NZ
REMARK 470 GLU A 355 CG CD OE1 OE2
REMARK 470 LYS A 367 CE NZ
REMARK 470 LYS A 371 CD CE NZ
REMARK 470 LYS A 427 CE NZ
REMARK 470 ILE A 446 CD1
REMARK 470 LYS A 458 NZ
REMARK 470 LYS A 524 CG CD CE NZ
REMARK 470 SER A 531 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LEU A 352 -51.58 67.70
REMARK 500 ASP A 389 77.21 -153.37
REMARK 500 GLU A 477 -55.08 -124.12
REMARK 500 GLU A 477 -42.13 -131.13
REMARK 500 LYS A 498 -139.92 47.94
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 TDU A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1000
DBREF 3SMQ A 228 548 UNP O60678 ANM3_HUMAN 211 531
SEQADV 3SMQ MET A 209 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ GLY A 210 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ SER A 211 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ SER A 212 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ HIS A 213 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ HIS A 214 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ HIS A 215 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ HIS A 216 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ HIS A 217 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ HIS A 218 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ SER A 219 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ SER A 220 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ GLY A 221 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ LEU A 222 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ VAL A 223 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ PRO A 224 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ ARG A 225 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ GLY A 226 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ SER A 227 UNP O60678 EXPRESSION TAG
SEQADV 3SMQ ASN A 525 UNP O60678 SER 508 VARIANT
SEQRES 1 A 340 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 340 LEU VAL PRO ARG GLY SER ASP LEU GLN GLU ASP GLU ASP
SEQRES 3 A 340 GLY VAL TYR PHE SER SER TYR GLY HIS TYR GLY ILE HIS
SEQRES 4 A 340 GLU GLU MET LEU LYS ASP LYS ILE ARG THR GLU SER TYR
SEQRES 5 A 340 ARG ASP PHE ILE TYR GLN ASN PRO HIS ILE PHE LYS ASP
SEQRES 6 A 340 LYS VAL VAL LEU ASP VAL GLY CYS GLY THR GLY ILE LEU
SEQRES 7 A 340 SER MET PHE ALA ALA LYS ALA GLY ALA LYS LYS VAL LEU
SEQRES 8 A 340 GLY VAL ASP GLN SER GLU ILE LEU TYR GLN ALA MET ASP
SEQRES 9 A 340 ILE ILE ARG LEU ASN LYS LEU GLU ASP THR ILE THR LEU
SEQRES 10 A 340 ILE LYS GLY LYS ILE GLU GLU VAL HIS LEU PRO VAL GLU
SEQRES 11 A 340 LYS VAL ASP VAL ILE ILE SER GLU TRP MET GLY TYR PHE
SEQRES 12 A 340 LEU LEU PHE GLU SER MET LEU ASP SER VAL LEU TYR ALA
SEQRES 13 A 340 LYS ASN LYS TYR LEU ALA LYS GLY GLY SER VAL TYR PRO
SEQRES 14 A 340 ASP ILE CYS THR ILE SER LEU VAL ALA VAL SER ASP VAL
SEQRES 15 A 340 ASN LYS HIS ALA ASP ARG ILE ALA PHE TRP ASP ASP VAL
SEQRES 16 A 340 TYR GLY PHE LYS MET SER CYS MET LYS LYS ALA VAL ILE
SEQRES 17 A 340 PRO GLU ALA VAL VAL GLU VAL LEU ASP PRO LYS THR LEU
SEQRES 18 A 340 ILE SER GLU PRO CYS GLY ILE LYS HIS ILE ASP CYS HIS
SEQRES 19 A 340 THR THR SER ILE SER ASP LEU GLU PHE SER SER ASP PHE
SEQRES 20 A 340 THR LEU LYS ILE THR ARG THR SER MET CYS THR ALA ILE
SEQRES 21 A 340 ALA GLY TYR PHE ASP ILE TYR PHE GLU LYS ASN CYS HIS
SEQRES 22 A 340 ASN ARG VAL VAL PHE SER THR GLY PRO GLN SER THR LYS
SEQRES 23 A 340 THR HIS TRP LYS GLN THR VAL PHE LEU LEU GLU LYS PRO
SEQRES 24 A 340 PHE SER VAL LYS ALA GLY GLU ALA LEU LYS GLY LYS VAL
SEQRES 25 A 340 THR VAL HIS LYS ASN LYS LYS ASP PRO ARG SER LEU THR
SEQRES 26 A 340 VAL THR LEU THR LEU ASN ASN SER THR GLN THR TYR GLY
SEQRES 27 A 340 LEU GLN
HET TDU A 1 21
HET CL A1000 1
HET UNX A 549 1
HET UNX A 2 1
HET UNX A 3 1
HET UNX A 4 1
HET UNX A 5 1
HET UNX A 7 1
HET UNX A 8 1
HET UNX A 9 1
HET UNX A 11 1
HET UNX A 12 1
HETNAM TDU 1-(1,2,3-BENZOTHIADIAZOL-6-YL)-3-[2-(CYCLOHEX-1-EN-1-
HETNAM 2 TDU YL)ETHYL]UREA
HETNAM CL CHLORIDE ION
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN TDU 1-(BENZO[D][1,2,3]THIADIAZOL-6-YL)-3-(2-
HETSYN 2 TDU CYCLOHEXENYLETHYL)UREA
FORMUL 2 TDU C15 H18 N4 O S
FORMUL 3 CL CL 1-
FORMUL 4 UNX 10(X)
FORMUL 14 HOH *223(H2 O)
HELIX 1 1 HIS A 243 LYS A 252 1 10
HELIX 2 2 ASP A 253 ASN A 267 1 15
HELIX 3 3 PRO A 268 PHE A 271 5 4
HELIX 4 4 GLY A 284 ALA A 293 1 10
HELIX 5 5 GLU A 305 ASN A 317 1 13
HELIX 6 6 MET A 357 TYR A 368 1 12
HELIX 7 7 ASP A 389 ILE A 397 1 9
HELIX 8 8 ALA A 398 ASP A 402 5 5
HELIX 9 9 MET A 408 CYS A 410 5 3
HELIX 10 10 MET A 411 ILE A 416 1 6
HELIX 11 11 ASP A 425 LEU A 429 5 5
HELIX 12 12 SER A 445 GLU A 450 5 6
SHEET 1 A 5 ILE A 323 LYS A 327 0
SHEET 2 A 5 LYS A 297 ASP A 302 1 N VAL A 298 O THR A 324
SHEET 3 A 5 VAL A 275 VAL A 279 1 N ASP A 278 O LEU A 299
SHEET 4 A 5 VAL A 340 ILE A 344 1 O VAL A 342 N LEU A 277
SHEET 5 A 5 LEU A 369 TYR A 376 1 O ALA A 370 N VAL A 340
SHEET 1 B 5 VAL A 420 GLU A 422 0
SHEET 2 B 5 GLN A 499 VAL A 510 -1 O VAL A 501 N VAL A 420
SHEET 3 B 5 SER A 463 PHE A 476 -1 N SER A 463 O VAL A 510
SHEET 4 B 5 ILE A 379 VAL A 387 -1 N VAL A 385 O ALA A 469
SHEET 5 B 5 CYS A 434 ASP A 440 -1 O ILE A 436 N ILE A 382
SHEET 1 C 4 VAL A 420 GLU A 422 0
SHEET 2 C 4 GLN A 499 VAL A 510 -1 O VAL A 501 N VAL A 420
SHEET 3 C 4 SER A 463 PHE A 476 -1 N SER A 463 O VAL A 510
SHEET 4 C 4 VAL A 484 SER A 487 -1 O VAL A 484 N PHE A 476
SHEET 1 D 4 PHE A 451 LYS A 458 0
SHEET 2 D 4 ALA A 515 HIS A 523 -1 O LEU A 516 N LEU A 457
SHEET 3 D 4 THR A 533 LEU A 538 -1 O THR A 535 N THR A 521
SHEET 4 D 4 SER A 541 GLY A 546 -1 O TYR A 545 N VAL A 534
CISPEP 1 TYR A 376 PRO A 377 0 -1.24
SITE 1 AC1 11 GLY A 245 GLU A 248 VAL A 387 ASP A 389
SITE 2 AC1 11 LYS A 392 HIS A 393 ARG A 396 VAL A 420
SITE 3 AC1 11 GLU A 422 THR A 466 ALA A 467
SITE 1 AC2 3 SER A 388 SER A 463 MET A 464
CRYST1 70.649 70.649 171.977 90.00 90.00 90.00 P 43 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 0.014154 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014154 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005815 0.00000
(ATOM LINES ARE NOT SHOWN.)
END