HEADER HYDROLASE 22-AUG-06 2I4I
TITLE CRYSTAL STRUCTURE OF HUMAN DEAD-BOX RNA HELICASE DDX3X
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP-DEPENDENT RNA HELICASE DDX3X;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DEAD BOX PROTEIN 3, X- CHROMOSOMAL, HELICASE-LIKE PROTEIN 2,
COMPND 5 HLP2, DEAD BOX, X ISOFORM;
COMPND 6 EC: 3.6.1.-;
COMPND 7 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: DDX3X;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS RNA, HELICASE, DEAD, STRUCTURAL GENOMICS, SGC, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.HOGBOM,T.KARLBERG,C.ARROWSMITH,H.BERGLUND,R.D.BUSAM,R.COLLINS,
AUTHOR 2 A.EDWARDS,M.EHN,S.FLODIN,A.FLORES,S.GRASLUND,B.M.HALLBERG,
AUTHOR 3 M.HAMMARSTROM,I.JOHANSSON,T.KOTENYOVA,A.MAGNUSDOTTIR,P.NILSSON-EHLE,
AUTHOR 4 P.NORDLUND,T.NYMAN,D.OGG,C.PERSSON,J.SAGEMARK,P.STENMARK,
AUTHOR 5 M.SUNDSTROM,A.G.THORSELL,J.UPPENBERG,S.VAN DEN BERG,K.WALLDEN,
AUTHOR 6 J.WEIGELT,M.WELIN,L.HOLMBERG-SCHIAVONE,STRUCTURAL GENOMICS
AUTHOR 7 CONSORTIUM (SGC)
REVDAT 4 13-JUL-11 2I4I 1 VERSN
REVDAT 3 24-FEB-09 2I4I 1 VERSN
REVDAT 2 28-AUG-07 2I4I 1 JRNL
REVDAT 1 05-SEP-06 2I4I 0
JRNL AUTH M.HOGBOM,R.COLLINS,S.VAN DEN BERG,R.-M.JENVERT,T.KARLBERG,
JRNL AUTH 2 T.KOTENYOVA,A.FLORES,G.B.KARLSSON HEDESTAM,
JRNL AUTH 3 L.H.HOLMBERG SCHIAVONE
JRNL TITL CRYSTAL STRUCTURE OF CONSERVED DOMAINS 1 AND 2 OF THE HUMAN
JRNL TITL 2 DEAD-BOX HELICASE DDX3X IN COMPLEX WITH THE MONONUCLEOTIDE
JRNL TITL 3 AMP
JRNL REF J.MOL.BIOL. V. 372 150 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17631897
JRNL DOI 10.1016/J.JMB.2007.06.050
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 32841
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1751
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2321
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 145
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3243
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 23
REMARK 3 SOLVENT ATOMS : 199
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) : 52.85
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.91000
REMARK 3 B22 (A**2) : 1.91000
REMARK 3 B33 (A**2) : -2.87000
REMARK 3 B12 (A**2) : 0.96000
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): 0.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.119
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.982
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3328 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4493 ; 1.584 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 405 ; 6.456 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 159 ;36.451 ;23.396
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 596 ;15.979 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 31 ;18.485 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 496 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2508 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1446 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2246 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 199 ; 0.183 ; 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): 63 ; 0.154 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.202 ; 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): 2099 ; 1.027 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3269 ; 1.650 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1388 ; 2.656 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1224 ; 4.166 ; 4.500
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 : 4
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 167 A 249
REMARK 3 ORIGIN FOR THE GROUP (A): 15.0000 -11.7850 20.3820
REMARK 3 T TENSOR
REMARK 3 T11: -0.1278 T22: -0.0505
REMARK 3 T33: -0.2512 T12: -0.1190
REMARK 3 T13: -0.0205 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 2.5592 L22: 1.3003
REMARK 3 L33: 7.3301 L12: 0.8584
REMARK 3 L13: 1.0927 L23: 0.9687
REMARK 3 S TENSOR
REMARK 3 S11: -0.0909 S12: -0.0125 S13: 0.0531
REMARK 3 S21: -0.1211 S22: -0.0857 S23: 0.1991
REMARK 3 S31: -0.0871 S32: -0.8485 S33: 0.1766
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 250 A 404
REMARK 3 ORIGIN FOR THE GROUP (A): 32.8590 -9.0030 15.0270
REMARK 3 T TENSOR
REMARK 3 T11: -0.0836 T22: -0.1568
REMARK 3 T33: -0.3230 T12: -0.1516
REMARK 3 T13: -0.0038 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 1.4818 L22: 1.6048
REMARK 3 L33: 3.0366 L12: 0.3191
REMARK 3 L13: -1.1849 L23: -0.3347
REMARK 3 S TENSOR
REMARK 3 S11: -0.0654 S12: -0.0306 S13: -0.0548
REMARK 3 S21: -0.2703 S22: 0.0404 S23: -0.1348
REMARK 3 S31: -0.0213 S32: 0.2446 S33: 0.0249
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 405 A 496
REMARK 3 ORIGIN FOR THE GROUP (A): 0.8790 -39.1410 33.0520
REMARK 3 T TENSOR
REMARK 3 T11: -0.0325 T22: -0.0406
REMARK 3 T33: -0.2790 T12: -0.1178
REMARK 3 T13: 0.0757 T23: -0.0085
REMARK 3 L TENSOR
REMARK 3 L11: 0.4768 L22: 4.1568
REMARK 3 L33: 5.6572 L12: -0.0136
REMARK 3 L13: 0.1620 L23: 3.9907
REMARK 3 S TENSOR
REMARK 3 S11: -0.0154 S12: -0.1590 S13: -0.0144
REMARK 3 S21: -0.2341 S22: 0.2068 S23: -0.1118
REMARK 3 S31: -0.1695 S32: 0.2167 S33: -0.1914
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 497 A 580
REMARK 3 ORIGIN FOR THE GROUP (A): 6.0670 -39.1790 18.4090
REMARK 3 T TENSOR
REMARK 3 T11: 0.2280 T22: -0.1081
REMARK 3 T33: -0.2283 T12: -0.2727
REMARK 3 T13: 0.1325 T23: -0.0507
REMARK 3 L TENSOR
REMARK 3 L11: 2.1515 L22: 2.9310
REMARK 3 L33: 9.8694 L12: -0.3504
REMARK 3 L13: -1.9278 L23: 1.2944
REMARK 3 S TENSOR
REMARK 3 S11: 0.1346 S12: -0.1469 S13: 0.1399
REMARK 3 S21: -0.4976 S22: 0.2931 S23: -0.4313
REMARK 3 S31: -1.1652 S32: 0.6649 S33: -0.4277
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 2I4I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-06.
REMARK 100 THE RCSB ID CODE IS RCSB039126.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : THREE SETS OF FOUR DIFFERENT
REMARK 200 THICKNESS OF ALUMINIUM OR CARBON
REMARK 200 FOILS
REMARK 200 OPTICS : NULL
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 : 32841
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 14.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 10.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1WRB FOR THE DEAD DOMAIN AND 2DB3 FOR
REMARK 200 THE HELICASE DOMAIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75M NA FORMATE, 0.1M TRIS PH 7.5,
REMARK 280 20MM ATPGS AND MGCL2, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 84.49000
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 168.98000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 168.98000
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 84.49000
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: 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 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 166
REMARK 465 ARG A 407
REMARK 465 VAL A 408
REMARK 465 GLY A 409
REMARK 465 SER A 410
REMARK 465 VAL A 535
REMARK 465 GLY A 536
REMARK 465 LYS A 581
REMARK 465 GLY A 582
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 THR A 411 OG1 CG2
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 CB CYS A 223 O HOH A 797 1.85
REMARK 500 O HOH A 692 O HOH A 795 2.01
REMARK 500 O HOH A 664 O HOH A 784 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 578 CG HIS A 578 CD2 0.091
REMARK 500 HIS A 578 CE1 HIS A 578 NE2 0.146
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 252 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
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 ASP A 245 57.65 -151.86
REMARK 500 ASP A 368 -143.63 -124.71
REMARK 500 SER A 412 -87.55 -100.23
REMARK 500 LYS A 440 -157.12 48.33
REMARK 500 ASN A 509 31.68 -69.05
REMARK 500 ASN A 546 -158.92 -145.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS A 440 ASP A 441 147.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE A 234 24.7 L L OUTSIDE RANGE
REMARK 500 LEU A 505 22.4 L L OUTSIDE RANGE
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 AMP A 600
DBREF 2I4I A 168 582 UNP O00571 DDX3X_HUMAN 167 581
SEQADV 2I4I SER A 166 UNP O00571 CLONING ARTIFACT
SEQADV 2I4I MET A 167 UNP O00571 CLONING ARTIFACT
SEQRES 1 A 417 SER MET VAL GLU ALA THR GLY ASN ASN CYS PRO PRO HIS
SEQRES 2 A 417 ILE GLU SER PHE SER ASP VAL GLU MET GLY GLU ILE ILE
SEQRES 3 A 417 MET GLY ASN ILE GLU LEU THR ARG TYR THR ARG PRO THR
SEQRES 4 A 417 PRO VAL GLN LYS HIS ALA ILE PRO ILE ILE LYS GLU LYS
SEQRES 5 A 417 ARG ASP LEU MET ALA CYS ALA GLN THR GLY SER GLY LYS
SEQRES 6 A 417 THR ALA ALA PHE LEU LEU PRO ILE LEU SER GLN ILE TYR
SEQRES 7 A 417 SER ASP GLY PRO GLY GLU ALA LEU ARG ALA MET LYS GLU
SEQRES 8 A 417 ASN GLY ARG TYR GLY ARG ARG LYS GLN TYR PRO ILE SER
SEQRES 9 A 417 LEU VAL LEU ALA PRO THR ARG GLU LEU ALA VAL GLN ILE
SEQRES 10 A 417 TYR GLU GLU ALA ARG LYS PHE SER TYR ARG SER ARG VAL
SEQRES 11 A 417 ARG PRO CYS VAL VAL TYR GLY GLY ALA ASP ILE GLY GLN
SEQRES 12 A 417 GLN ILE ARG ASP LEU GLU ARG GLY CYS HIS LEU LEU VAL
SEQRES 13 A 417 ALA THR PRO GLY ARG LEU VAL ASP MET MET GLU ARG GLY
SEQRES 14 A 417 LYS ILE GLY LEU ASP PHE CYS LYS TYR LEU VAL LEU ASP
SEQRES 15 A 417 GLU ALA ASP ARG MET LEU ASP MET GLY PHE GLU PRO GLN
SEQRES 16 A 417 ILE ARG ARG ILE VAL GLU GLN ASP THR MET PRO PRO LYS
SEQRES 17 A 417 GLY VAL ARG HIS THR MET MET PHE SER ALA THR PHE PRO
SEQRES 18 A 417 LYS GLU ILE GLN MET LEU ALA ARG ASP PHE LEU ASP GLU
SEQRES 19 A 417 TYR ILE PHE LEU ALA VAL GLY ARG VAL GLY SER THR SER
SEQRES 20 A 417 GLU ASN ILE THR GLN LYS VAL VAL TRP VAL GLU GLU SER
SEQRES 21 A 417 ASP LYS ARG SER PHE LEU LEU ASP LEU LEU ASN ALA THR
SEQRES 22 A 417 GLY LYS ASP SER LEU THR LEU VAL PHE VAL GLU THR LYS
SEQRES 23 A 417 LYS GLY ALA ASP SER LEU GLU ASP PHE LEU TYR HIS GLU
SEQRES 24 A 417 GLY TYR ALA CYS THR SER ILE HIS GLY ASP ARG SER GLN
SEQRES 25 A 417 ARG ASP ARG GLU GLU ALA LEU HIS GLN PHE ARG SER GLY
SEQRES 26 A 417 LYS SER PRO ILE LEU VAL ALA THR ALA VAL ALA ALA ARG
SEQRES 27 A 417 GLY LEU ASP ILE SER ASN VAL LYS HIS VAL ILE ASN PHE
SEQRES 28 A 417 ASP LEU PRO SER ASP ILE GLU GLU TYR VAL HIS ARG ILE
SEQRES 29 A 417 GLY ARG THR GLY ARG VAL GLY ASN LEU GLY LEU ALA THR
SEQRES 30 A 417 SER PHE PHE ASN GLU ARG ASN ILE ASN ILE THR LYS ASP
SEQRES 31 A 417 LEU LEU ASP LEU LEU VAL GLU ALA LYS GLN GLU VAL PRO
SEQRES 32 A 417 SER TRP LEU GLU ASN MET ALA TYR GLU HIS HIS TYR LYS
SEQRES 33 A 417 GLY
HET AMP A 600 23
HETNAM AMP ADENOSINE MONOPHOSPHATE
FORMUL 2 AMP C10 H14 N5 O7 P
FORMUL 3 HOH *199(H2 O)
HELIX 1 1 SER A 181 VAL A 185 5 5
HELIX 2 2 GLY A 188 ARG A 199 1 12
HELIX 3 3 THR A 204 GLU A 216 1 13
HELIX 4 4 GLY A 229 GLY A 246 1 18
HELIX 5 5 GLY A 248 ASN A 257 1 10
HELIX 6 6 THR A 275 TYR A 291 1 17
HELIX 7 7 ASP A 305 GLU A 314 1 10
HELIX 8 8 THR A 323 ARG A 333 1 11
HELIX 9 9 GLU A 348 MET A 355 1 8
HELIX 10 10 PHE A 357 GLU A 366 1 10
HELIX 11 11 PRO A 386 LEU A 397 1 12
HELIX 12 12 GLU A 423 SER A 425 5 3
HELIX 13 13 ASP A 426 ALA A 437 1 12
HELIX 14 14 THR A 450 GLU A 464 1 15
HELIX 15 15 SER A 476 SER A 489 1 14
HELIX 16 16 THR A 498 ARG A 503 1 6
HELIX 17 17 ASP A 521 GLY A 530 1 10
HELIX 18 18 ASN A 546 ASN A 551 5 6
HELIX 19 19 ILE A 552 ALA A 563 1 12
HELIX 20 20 PRO A 568 TYR A 576 1 9
SHEET 1 A 8 VAL A 168 THR A 171 0
SHEET 2 A 8 ILE A 401 VAL A 405 -1 O PHE A 402 N THR A 171
SHEET 3 A 8 LEU A 220 CYS A 223 1 N CYS A 223 O LEU A 403
SHEET 4 A 8 HIS A 377 SER A 382 1 O MET A 380 N ALA A 222
SHEET 5 A 8 TYR A 343 LEU A 346 1 N LEU A 344 O HIS A 377
SHEET 6 A 8 SER A 269 LEU A 272 1 N LEU A 272 O VAL A 345
SHEET 7 A 8 LEU A 319 ALA A 322 1 O ALA A 322 N VAL A 271
SHEET 8 A 8 PRO A 297 VAL A 300 1 N CYS A 298 O VAL A 321
SHEET 1 B 6 ILE A 415 TRP A 421 0
SHEET 2 B 6 GLY A 539 PHE A 545 1 O ALA A 541 N LYS A 418
SHEET 3 B 6 VAL A 510 ASN A 515 1 N ASN A 515 O PHE A 544
SHEET 4 B 6 LEU A 443 PHE A 447 1 N LEU A 445 O ILE A 514
SHEET 5 B 6 ILE A 494 ALA A 497 1 O LEU A 495 N VAL A 446
SHEET 6 B 6 CYS A 468 ILE A 471 1 N THR A 469 O VAL A 496
SITE 1 AC1 14 TYR A 200 ARG A 202 GLN A 207 THR A 226
SITE 2 AC1 14 GLY A 227 SER A 228 GLY A 229 LYS A 230
SITE 3 AC1 14 THR A 231 HOH A 609 HOH A 670 HOH A 683
SITE 4 AC1 14 HOH A 687 HOH A 782
CRYST1 67.288 67.288 253.470 90.00 90.00 120.00 P 31 2 1 6
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 0.014861 0.008580 0.000000 0.00000
SCALE2 0.000000 0.017161 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003945 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
