HEADER HYDROLASE 19-MAR-07 2P6N
TITLE HUMAN DEAD-BOX RNA HELICASE DDX41, HELICASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX41;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: HELICASE DOMAIN;
COMPND 5 SYNONYM: DEAD BOX PROTEIN 41, DEAD BOX PROTEIN ABSTRAKT HOMOLOG;
COMPND 6 EC: 3.6.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: DDX41, ABS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) GOLD PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS RNA, HELICASE, DEAD, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KARLBERG,D.OGG,C.H.ARROWSMITH,H.BERGLUND,R.D.BUSAM,R.COLLINS,
AUTHOR 2 L.G.DAHLGREN,A.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,B.M.HALLBERG,
AUTHOR 3 M.HAMMARSTROM,I.JOHANSSON,T.KOTENYOVA,L.LEHTIO,M.MOCHE,P.NORDLUND,
AUTHOR 4 T.NYMAN,C.PERSSON,J.SAGEMARK,P.STENMARK,M.SUNDSTROM,A.G.THORSELL,
AUTHOR 5 S.VAN DEN BERG,J.WEIGELT,L.HOLMBERG-SCHIAVONE,STRUCTURAL GENOMICS
AUTHOR 6 CONSORTIUM (SGC)
REVDAT 6 30-AUG-23 2P6N 1 REMARK
REVDAT 5 20-OCT-21 2P6N 1 SEQADV
REVDAT 4 13-JUL-11 2P6N 1 VERSN
REVDAT 3 27-OCT-10 2P6N 1 JRNL
REVDAT 2 24-FEB-09 2P6N 1 VERSN
REVDAT 1 03-APR-07 2P6N 0
JRNL AUTH P.SCHUTZ,T.KARLBERG,S.VAN DEN BERG,R.COLLINS,L.LEHTIO,
JRNL AUTH 2 M.HOGBOM,L.HOLMBERG-SCHIAVONE,W.TEMPEL,H.W.PARK,
JRNL AUTH 3 M.HAMMARSTROM,M.MOCHE,A.G.THORSELL,H.SCHULER
JRNL TITL COMPARATIVE STRUCTURAL ANALYSIS OF HUMAN DEAD-BOX RNA
JRNL TITL 2 HELICASES.
JRNL REF PLOS ONE V. 5 12791 2010
JRNL REFN ESSN 1932-6203
JRNL PMID 20941364
JRNL DOI 10.1371/JOURNAL.PONE.0012791
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0032
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 13220
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) : 0.246
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 696
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 929
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.3980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2481
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.559
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.337
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.266
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.859
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2518 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1691 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3404 ; 1.602 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4192 ; 0.909 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 314 ; 6.343 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;42.956 ;25.943
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 474 ;18.747 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;24.418 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 405 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2726 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 430 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 562 ; 0.250 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 1756 ; 0.196 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1227 ; 0.186 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1351 ; 0.093 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 51 ; 0.150 ; 0.200
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): 16 ; 0.216 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 18 ; 0.246 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.218 ; 0.200
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): 1733 ; 0.635 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 636 ; 0.123 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2564 ; 0.942 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1009 ; 1.612 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 840 ; 2.548 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 406 A 565 5
REMARK 3 1 B 406 B 565 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 926 ; 0.23 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 B (A): 1130 ; 0.51 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 926 ; 0.32 ; 2.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1130 ; 0.44 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
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 406 A 431
REMARK 3 ORIGIN FOR THE GROUP (A): -19.9110 33.9770 191.6930
REMARK 3 T TENSOR
REMARK 3 T11: -0.0312 T22: 0.0619
REMARK 3 T33: -0.2277 T12: -0.0803
REMARK 3 T13: -0.0162 T23: -0.0490
REMARK 3 L TENSOR
REMARK 3 L11: 7.1667 L22: 6.5293
REMARK 3 L33: 8.3378 L12: -3.4473
REMARK 3 L13: -1.3977 L23: -0.8578
REMARK 3 S TENSOR
REMARK 3 S11: 0.0183 S12: -0.1145 S13: 0.4293
REMARK 3 S21: 0.7234 S22: -0.0013 S23: -0.2410
REMARK 3 S31: -0.2354 S32: 0.0780 S33: -0.0171
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 432 A 508
REMARK 3 ORIGIN FOR THE GROUP (A): -24.5130 33.2650 176.1220
REMARK 3 T TENSOR
REMARK 3 T11: -0.0344 T22: 0.0962
REMARK 3 T33: -0.0934 T12: -0.0576
REMARK 3 T13: 0.0201 T23: 0.0817
REMARK 3 L TENSOR
REMARK 3 L11: 4.0322 L22: 3.7860
REMARK 3 L33: 6.7715 L12: 0.8659
REMARK 3 L13: -0.1556 L23: 0.6366
REMARK 3 S TENSOR
REMARK 3 S11: -0.1180 S12: 0.4739 S13: 0.2612
REMARK 3 S21: -0.2955 S22: 0.1424 S23: 0.0251
REMARK 3 S31: -0.1877 S32: -0.1230 S33: -0.0244
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 509 A 568
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9970 25.5280 190.7190
REMARK 3 T TENSOR
REMARK 3 T11: -0.0877 T22: 0.1135
REMARK 3 T33: -0.0660 T12: -0.0555
REMARK 3 T13: 0.0328 T23: 0.0184
REMARK 3 L TENSOR
REMARK 3 L11: 7.1827 L22: 4.6970
REMARK 3 L33: 6.7789 L12: -1.3006
REMARK 3 L13: 2.3128 L23: 0.7031
REMARK 3 S TENSOR
REMARK 3 S11: -0.0416 S12: 0.0180 S13: -0.1703
REMARK 3 S21: -0.1530 S22: -0.3045 S23: -0.3727
REMARK 3 S31: 0.2022 S32: 0.4636 S33: 0.3460
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 : B 406 B 431
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1990 24.5760 191.8520
REMARK 3 T TENSOR
REMARK 3 T11: 0.0191 T22: 0.2121
REMARK 3 T33: -0.1241 T12: -0.0498
REMARK 3 T13: 0.0772 T23: -0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 6.2403 L22: 3.5007
REMARK 3 L33: 5.6320 L12: 3.7737
REMARK 3 L13: 1.2534 L23: 0.6441
REMARK 3 S TENSOR
REMARK 3 S11: -0.0328 S12: 1.2220 S13: -0.3384
REMARK 3 S21: -0.5125 S22: 0.2112 S23: 0.0387
REMARK 3 S31: 0.3996 S32: 0.0914 S33: -0.1783
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 : B 432 B 508
REMARK 3 ORIGIN FOR THE GROUP (A): 9.4520 25.6870 207.2840
REMARK 3 T TENSOR
REMARK 3 T11: -0.0520 T22: 0.0349
REMARK 3 T33: -0.1025 T12: 0.0349
REMARK 3 T13: 0.0645 T23: 0.0455
REMARK 3 L TENSOR
REMARK 3 L11: 4.9156 L22: 3.3541
REMARK 3 L33: 5.6513 L12: -1.3656
REMARK 3 L13: -0.4729 L23: 1.1903
REMARK 3 S TENSOR
REMARK 3 S11: -0.2117 S12: -0.2211 S13: -0.0516
REMARK 3 S21: 0.1108 S22: 0.2445 S23: 0.1148
REMARK 3 S31: 0.1333 S32: -0.1278 S33: -0.0329
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 : B 509 B 565
REMARK 3 ORIGIN FOR THE GROUP (A): 22.6650 32.8900 193.4090
REMARK 3 T TENSOR
REMARK 3 T11: -0.0815 T22: 0.1469
REMARK 3 T33: -0.0453 T12: 0.0212
REMARK 3 T13: 0.0657 T23: 0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 6.8775 L22: 6.0641
REMARK 3 L33: 4.3295 L12: 1.1452
REMARK 3 L13: -1.4436 L23: 0.5550
REMARK 3 S TENSOR
REMARK 3 S11: -0.1777 S12: 0.4082 S13: 0.3967
REMARK 3 S21: -0.1833 S22: 0.2227 S23: -0.3175
REMARK 3 S31: -0.0228 S32: 0.0447 S33: -0.0450
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 2P6N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-MAR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042032.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04005
REMARK 200 MONOCHROMATOR : KHOZU, WITH A MCLENNON
REMARK 200 CONTROLLER CONTAINING A LN2
REMARK 200 COOLED SI111 CRYSTAL
REMARK 200 OPTICS : DOUBLE CRYSTAL, SI(111) OR
REMARK 200 SI(311), TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13827
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 40.00
REMARK 200 R MERGE (I) : 0.10300
REMARK 200 R SYM (I) : 0.02900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 41.80
REMARK 200 R MERGE FOR SHELL (I) : 0.45000
REMARK 200 R SYM FOR SHELL (I) : 0.08400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 12.60
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: PDB ENTRY 2I4I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.93
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 200MM LITHIUM SULFATE,
REMARK 280 100MM BIS-TRIS, PH 5.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K, PH 5.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 203.73600
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 101.86800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 152.80200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 50.93400
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 254.67000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 203.73600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 101.86800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 50.93400
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 152.80200
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 254.67000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). AUTHORS STATE THAT THE
REMARK 300 BIOLOGICAL UNIT OF THIS PROTEIN IS A MONOMER.
REMARK 300 SEE REMARK 350 FOR INFORMATION ON GENERATING THE
REMARK 300 BIOLOGICAL MOLECULE(S).
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: MONOMERIC
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 379
REMARK 465 HIS A 380
REMARK 465 HIS A 381
REMARK 465 HIS A 382
REMARK 465 HIS A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 SER A 386
REMARK 465 SER A 387
REMARK 465 GLY A 388
REMARK 465 VAL A 389
REMARK 465 ASP A 390
REMARK 465 LEU A 391
REMARK 465 GLY A 392
REMARK 465 THR A 393
REMARK 465 GLU A 394
REMARK 465 ASN A 395
REMARK 465 LEU A 396
REMARK 465 TYR A 397
REMARK 465 PHE A 398
REMARK 465 GLN A 399
REMARK 465 SER A 400
REMARK 465 MET A 401
REMARK 465 GLY A 402
REMARK 465 ALA A 403
REMARK 465 ALA A 404
REMARK 465 SER A 405
REMARK 465 SER A 526
REMARK 465 GLY A 527
REMARK 465 ASN A 528
REMARK 465 GLY A 569
REMARK 465 MET B 379
REMARK 465 HIS B 380
REMARK 465 HIS B 381
REMARK 465 HIS B 382
REMARK 465 HIS B 383
REMARK 465 HIS B 384
REMARK 465 HIS B 385
REMARK 465 SER B 386
REMARK 465 SER B 387
REMARK 465 GLY B 388
REMARK 465 VAL B 389
REMARK 465 ASP B 390
REMARK 465 LEU B 391
REMARK 465 GLY B 392
REMARK 465 THR B 393
REMARK 465 GLU B 394
REMARK 465 ASN B 395
REMARK 465 LEU B 396
REMARK 465 TYR B 397
REMARK 465 PHE B 398
REMARK 465 GLN B 399
REMARK 465 SER B 400
REMARK 465 MET B 401
REMARK 465 GLY B 402
REMARK 465 ALA B 403
REMARK 465 ALA B 404
REMARK 465 SER B 405
REMARK 465 GLY B 527
REMARK 465 ASN B 528
REMARK 465 LEU B 566
REMARK 465 HIS B 567
REMARK 465 CYS B 568
REMARK 465 GLY B 569
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 GLU B 542 CG CD OE1 OE2
REMARK 470 SER B 543 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 GLU A 458 91.94 -66.37
REMARK 500 ALA A 500 101.56 -59.90
REMARK 500 HIS A 503 115.10 -160.96
REMARK 500 ASN A 537 -164.22 -162.91
REMARK 500 LEU A 566 -63.50 -29.62
REMARK 500 ASP B 467 -170.91 -66.12
REMARK 500 ALA B 500 103.83 -53.96
REMARK 500 SER B 543 -71.56 -36.45
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2P6N A 402 569 UNP Q9UJV9 DDX41_HUMAN 402 569
DBREF 2P6N B 402 569 UNP Q9UJV9 DDX41_HUMAN 402 569
SEQADV 2P6N MET A 379 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS A 380 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS A 381 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS A 382 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS A 383 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS A 384 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS A 385 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N SER A 386 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N SER A 387 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLY A 388 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N VAL A 389 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N ASP A 390 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N LEU A 391 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLY A 392 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N THR A 393 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLU A 394 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N ASN A 395 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N LEU A 396 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N TYR A 397 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N PHE A 398 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLN A 399 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N SER A 400 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N MET A 401 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N CYS A 525 UNP Q9UJV9 ARG 525 ENGINEERED MUTATION
SEQADV 2P6N MET B 379 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS B 380 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS B 381 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS B 382 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS B 383 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS B 384 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N HIS B 385 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N SER B 386 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N SER B 387 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLY B 388 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N VAL B 389 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N ASP B 390 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N LEU B 391 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLY B 392 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N THR B 393 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLU B 394 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N ASN B 395 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N LEU B 396 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N TYR B 397 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N PHE B 398 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N GLN B 399 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N SER B 400 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N MET B 401 UNP Q9UJV9 CLONING ARTIFACT
SEQADV 2P6N CYS B 525 UNP Q9UJV9 ARG 525 ENGINEERED MUTATION
SEQRES 1 A 191 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 191 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY ALA ALA
SEQRES 3 A 191 SER LEU ASP VAL ILE GLN GLU VAL GLU TYR VAL LYS GLU
SEQRES 4 A 191 GLU ALA LYS MET VAL TYR LEU LEU GLU CYS LEU GLN LYS
SEQRES 5 A 191 THR PRO PRO PRO VAL LEU ILE PHE ALA GLU LYS LYS ALA
SEQRES 6 A 191 ASP VAL ASP ALA ILE HIS GLU TYR LEU LEU LEU LYS GLY
SEQRES 7 A 191 VAL GLU ALA VAL ALA ILE HIS GLY GLY LYS ASP GLN GLU
SEQRES 8 A 191 GLU ARG THR LYS ALA ILE GLU ALA PHE ARG GLU GLY LYS
SEQRES 9 A 191 LYS ASP VAL LEU VAL ALA THR ASP VAL ALA SER LYS GLY
SEQRES 10 A 191 LEU ASP PHE PRO ALA ILE GLN HIS VAL ILE ASN TYR ASP
SEQRES 11 A 191 MET PRO GLU GLU ILE GLU ASN TYR VAL HIS ARG ILE GLY
SEQRES 12 A 191 ARG THR GLY CYS SER GLY ASN THR GLY ILE ALA THR THR
SEQRES 13 A 191 PHE ILE ASN LYS ALA CYS ASP GLU SER VAL LEU MET ASP
SEQRES 14 A 191 LEU LYS ALA LEU LEU LEU GLU ALA LYS GLN LYS VAL PRO
SEQRES 15 A 191 PRO VAL LEU GLN VAL LEU HIS CYS GLY
SEQRES 1 B 191 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 191 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY ALA ALA
SEQRES 3 B 191 SER LEU ASP VAL ILE GLN GLU VAL GLU TYR VAL LYS GLU
SEQRES 4 B 191 GLU ALA LYS MET VAL TYR LEU LEU GLU CYS LEU GLN LYS
SEQRES 5 B 191 THR PRO PRO PRO VAL LEU ILE PHE ALA GLU LYS LYS ALA
SEQRES 6 B 191 ASP VAL ASP ALA ILE HIS GLU TYR LEU LEU LEU LYS GLY
SEQRES 7 B 191 VAL GLU ALA VAL ALA ILE HIS GLY GLY LYS ASP GLN GLU
SEQRES 8 B 191 GLU ARG THR LYS ALA ILE GLU ALA PHE ARG GLU GLY LYS
SEQRES 9 B 191 LYS ASP VAL LEU VAL ALA THR ASP VAL ALA SER LYS GLY
SEQRES 10 B 191 LEU ASP PHE PRO ALA ILE GLN HIS VAL ILE ASN TYR ASP
SEQRES 11 B 191 MET PRO GLU GLU ILE GLU ASN TYR VAL HIS ARG ILE GLY
SEQRES 12 B 191 ARG THR GLY CYS SER GLY ASN THR GLY ILE ALA THR THR
SEQRES 13 B 191 PHE ILE ASN LYS ALA CYS ASP GLU SER VAL LEU MET ASP
SEQRES 14 B 191 LEU LYS ALA LEU LEU LEU GLU ALA LYS GLN LYS VAL PRO
SEQRES 15 B 191 PRO VAL LEU GLN VAL LEU HIS CYS GLY
HELIX 1 1 LYS A 416 GLU A 418 5 3
HELIX 2 2 ALA A 419 GLN A 429 1 11
HELIX 3 3 LYS A 441 GLY A 456 1 16
HELIX 4 4 ASP A 467 GLY A 481 1 15
HELIX 5 5 THR A 489 LYS A 494 1 6
HELIX 6 6 GLU A 512 GLY A 521 1 10
HELIX 7 7 ASP A 541 ALA A 555 1 15
HELIX 8 8 PRO A 560 VAL A 565 1 6
HELIX 9 9 LYS B 416 GLU B 418 5 3
HELIX 10 10 ALA B 419 LEU B 428 1 10
HELIX 11 11 GLN B 429 THR B 431 5 3
HELIX 12 12 LYS B 441 LYS B 455 1 15
HELIX 13 13 ASP B 467 GLU B 480 1 14
HELIX 14 14 THR B 489 LYS B 494 1 6
HELIX 15 15 GLU B 512 GLY B 521 1 10
HELIX 16 16 ASP B 541 ALA B 555 1 15
HELIX 17 17 PRO B 560 GLN B 564 5 5
SHEET 1 A 6 ILE A 409 TYR A 414 0
SHEET 2 A 6 ILE A 531 ILE A 536 1 O ALA A 532 N GLU A 411
SHEET 3 A 6 HIS A 503 ASN A 506 1 N ASN A 506 O THR A 533
SHEET 4 A 6 VAL A 435 PHE A 438 1 N LEU A 436 O ILE A 505
SHEET 5 A 6 VAL A 485 ALA A 488 1 O ALA A 488 N ILE A 437
SHEET 6 A 6 ALA A 459 ILE A 462 1 N VAL A 460 O VAL A 487
SHEET 1 B 6 VAL B 408 TYR B 414 0
SHEET 2 B 6 GLY B 530 ILE B 536 1 O ILE B 536 N GLU B 413
SHEET 3 B 6 HIS B 503 ASN B 506 1 N ASN B 506 O THR B 533
SHEET 4 B 6 VAL B 435 PHE B 438 1 N LEU B 436 O ILE B 505
SHEET 5 B 6 VAL B 485 ALA B 488 1 O LEU B 486 N ILE B 437
SHEET 6 B 6 ALA B 459 ILE B 462 1 N ILE B 462 O VAL B 487
CISPEP 1 PRO A 433 PRO A 434 0 1.35
CISPEP 2 PRO B 433 PRO B 434 0 1.27
CRYST1 68.013 68.013 305.604 90.00 90.00 120.00 P 65 2 2 24
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 0.014703 0.008489 0.000000 0.00000
SCALE2 0.000000 0.016978 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003272 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
