HEADER RNA BINDING PROTEIN/DNA 29-DEC-11 3VAK
TITLE STRUCTURE OF U2AF65 VARIANT WITH BRU5 DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPLICING FACTOR U2AF 65 KDA SUBUNIT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RNA BINDING DOMAINS 1 AND 2;
COMPND 5 SYNONYM: U2 AUXILIARY FACTOR 65 KDA SUBUNIT, HU2AF(65), HU2AF65, U2
COMPND 6 SNRNP AUXILIARY FACTOR LARGE SUBUNIT;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(*UP*UP*UP*UP*(BRU)P*UP*U)-3');
COMPND 10 CHAIN: P, E;
COMPND 11 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: U2AF2, U2AF65;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 14 ORGANISM_TAXID: 32630;
SOURCE 15 OTHER_DETAILS: DNA
KEYWDS RNA SPLICING FACTOR, RNA RECOGNITION MOTIF, RNA BINDING PROTEIN, RNA
KEYWDS 2 BINDING PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.L.JENKINS,C.L.KIELKOPF
REVDAT 3 16-AUG-17 3VAK 1 SOURCE REMARK
REVDAT 2 22-MAY-13 3VAK 1 JRNL
REVDAT 1 13-FEB-13 3VAK 0
JRNL AUTH J.L.JENKINS,A.A.AGRAWAL,A.GUPTA,M.R.GREEN,C.L.KIELKOPF
JRNL TITL U2AF65 ADAPTS TO DIVERSE PRE-MRNA SPLICE SITES THROUGH
JRNL TITL 2 CONFORMATIONAL SELECTION OF SPECIFIC AND PROMISCUOUS RNA
JRNL TITL 3 RECOGNITION MOTIFS.
JRNL REF NUCLEIC ACIDS RES. V. 41 3859 2013
JRNL REFN ISSN 0305-1048
JRNL PMID 23376934
JRNL DOI 10.1093/NAR/GKT046
REMARK 2
REMARK 2 RESOLUTION. 2.17 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) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 24457
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2710
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) : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1506
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE SET COUNT : 166
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2686
REMARK 3 NUCLEIC ACID ATOMS : 262
REMARK 3 HETEROGEN ATOMS : 116
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.70000
REMARK 3 B22 (A**2) : -1.33000
REMARK 3 B33 (A**2) : 3.21000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.237
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.126
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3182 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2113 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4351 ; 1.257 ; 2.114
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5164 ; 1.187 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 352 ; 5.249 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;34.638 ;24.924
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 464 ;13.951 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;16.451 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3280 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 563 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 455 ; 0.176 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2007 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1428 ; 0.174 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1557 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 144 ; 0.133 ; 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 ; 0.123 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 48 ; 0.152 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.179 ; 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): 2223 ; 0.571 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2759 ; 0.653 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1690 ; 1.152 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1562 ; 1.917 ; 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 : 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 143 A 237
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2714 -19.7343 31.3021
REMARK 3 T TENSOR
REMARK 3 T11: -0.1825 T22: -0.2298
REMARK 3 T33: -0.1465 T12: -0.0122
REMARK 3 T13: -0.0042 T23: -0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 1.8040 L22: 2.2877
REMARK 3 L33: 4.1997 L12: 1.4871
REMARK 3 L13: -0.3560 L23: -0.7465
REMARK 3 S TENSOR
REMARK 3 S11: 0.0122 S12: -0.0917 S13: -0.0991
REMARK 3 S21: -0.0556 S22: -0.0726 S23: -0.0977
REMARK 3 S31: 0.0388 S32: 0.0143 S33: 0.0604
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 258 A 336
REMARK 3 ORIGIN FOR THE GROUP (A): -32.8816 5.9580 26.9324
REMARK 3 T TENSOR
REMARK 3 T11: -0.1435 T22: -0.2059
REMARK 3 T33: -0.1429 T12: -0.0618
REMARK 3 T13: 0.0142 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 7.9885 L22: 2.2857
REMARK 3 L33: 2.5961 L12: 1.1524
REMARK 3 L13: 0.6378 L23: -0.1032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0897 S12: 0.0450 S13: 0.0061
REMARK 3 S21: -0.0971 S22: 0.1542 S23: -0.0515
REMARK 3 S31: -0.2142 S32: 0.1106 S33: -0.0645
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 : B 143 B 237
REMARK 3 ORIGIN FOR THE GROUP (A): 25.8972 -28.1244 28.9458
REMARK 3 T TENSOR
REMARK 3 T11: -0.1722 T22: -0.1715
REMARK 3 T33: -0.1907 T12: -0.0431
REMARK 3 T13: -0.0367 T23: 0.0018
REMARK 3 L TENSOR
REMARK 3 L11: 4.0039 L22: 4.5308
REMARK 3 L33: 3.5384 L12: 2.2104
REMARK 3 L13: -0.4433 L23: -0.7651
REMARK 3 S TENSOR
REMARK 3 S11: -0.2110 S12: 0.1248 S13: -0.0816
REMARK 3 S21: -0.2366 S22: 0.2440 S23: 0.2113
REMARK 3 S31: 0.1233 S32: -0.2742 S33: -0.0330
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 258 B 336
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7912 -3.7379 13.8983
REMARK 3 T TENSOR
REMARK 3 T11: -0.0940 T22: -0.1382
REMARK 3 T33: -0.2195 T12: -0.0758
REMARK 3 T13: 0.0097 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 7.1493 L22: 2.6943
REMARK 3 L33: 6.2213 L12: 1.3925
REMARK 3 L13: 1.0403 L23: -0.2333
REMARK 3 S TENSOR
REMARK 3 S11: -0.0890 S12: 0.3829 S13: 0.0312
REMARK 3 S21: -0.3290 S22: 0.0657 S23: -0.2187
REMARK 3 S31: -0.2317 S32: 0.1665 S33: 0.0234
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 3VAK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069802.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-07
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 : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.987
REMARK 200 MONOCHROMATOR : HORIZONTAL FOCUSING 5.05?
REMARK 200 ASYMMETRIC CUT SI(111)
REMARK 200 OPTICS : RH COATED SI VERTICAL FOCUS
REMARK 200 MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27427
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.160
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.14000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.16
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.36500
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 10% DIOXANE,
REMARK 280 0.1M MES PH 6.5, DEOXY-BIG CHAP, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 1.000000 0.000000 0.000000 83.20300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.86300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 83.20300
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.86300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -107.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 -83.20300
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 18.86300
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, P
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
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 DU P 4 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DU E 1 O4' - C4' - C3' ANGL. DEV. = 4.5 DEGREES
REMARK 500 DU E 1 C5' - C4' - C3' ANGL. DEV. = 10.1 DEGREES
REMARK 500 DU E 1 C5' - C4' - O4' ANGL. DEV. = 11.5 DEGREES
REMARK 500 DU E 2 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DU E 4 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CPQ B 404
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPQ B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 408
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G4B RELATED DB: PDB
REMARK 900 U2AF65 VARIANT WITH POLYURIDINE TRACT
REMARK 900 RELATED ID: 2HZC RELATED DB: PDB
REMARK 900 N-TERMINAL RRM OF U2AF65
REMARK 900 RELATED ID: 3VAF RELATED DB: PDB
REMARK 900 RELATED ID: 3VAG RELATED DB: PDB
REMARK 900 RELATED ID: 3VAH RELATED DB: PDB
REMARK 900 RELATED ID: 3VAI RELATED DB: PDB
REMARK 900 RELATED ID: 3VAJ RELATED DB: PDB
REMARK 900 RELATED ID: 3VAL RELATED DB: PDB
REMARK 900 RELATED ID: 3VAM RELATED DB: PDB
REMARK 900 RELATED ID: 3VAN RELATED DB: PDB
REMARK 900 RELATED ID: 3VAO RELATED DB: PDB
DBREF 3VAK A 148 237 UNP P26368 U2AF2_HUMAN 148 237
DBREF 3VAK A 258 336 UNP P26368 U2AF2_HUMAN 258 336
DBREF 3VAK B 148 237 UNP P26368 U2AF2_HUMAN 148 237
DBREF 3VAK B 258 336 UNP P26368 U2AF2_HUMAN 258 336
DBREF 3VAK P 1 7 PDB 3VAK 3VAK 1 7
DBREF 3VAK E 1 7 PDB 3VAK 3VAK 1 7
SEQADV 3VAK GLY A 143 UNP P26368 EXPRESSION TAG
SEQADV 3VAK PRO A 144 UNP P26368 EXPRESSION TAG
SEQADV 3VAK LEU A 145 UNP P26368 EXPRESSION TAG
SEQADV 3VAK GLY A 146 UNP P26368 EXPRESSION TAG
SEQADV 3VAK SER A 147 UNP P26368 EXPRESSION TAG
SEQADV 3VAK GLY B 143 UNP P26368 EXPRESSION TAG
SEQADV 3VAK PRO B 144 UNP P26368 EXPRESSION TAG
SEQADV 3VAK LEU B 145 UNP P26368 EXPRESSION TAG
SEQADV 3VAK GLY B 146 UNP P26368 EXPRESSION TAG
SEQADV 3VAK SER B 147 UNP P26368 EXPRESSION TAG
SEQRES 1 A 174 GLY PRO LEU GLY SER ALA ARG ARG LEU TYR VAL GLY ASN
SEQRES 2 A 174 ILE PRO PHE GLY ILE THR GLU GLU ALA MET MET ASP PHE
SEQRES 3 A 174 PHE ASN ALA GLN MET ARG LEU GLY GLY LEU THR GLN ALA
SEQRES 4 A 174 PRO GLY ASN PRO VAL LEU ALA VAL GLN ILE ASN GLN ASP
SEQRES 5 A 174 LYS ASN PHE ALA PHE LEU GLU PHE ARG SER VAL ASP GLU
SEQRES 6 A 174 THR THR GLN ALA MET ALA PHE ASP GLY ILE ILE PHE GLN
SEQRES 7 A 174 GLY GLN SER LEU LYS ILE ARG ARG PRO HIS ASP TYR GLN
SEQRES 8 A 174 PRO LEU PRO GLY ALA HIS LYS LEU PHE ILE GLY GLY LEU
SEQRES 9 A 174 PRO ASN TYR LEU ASN ASP ASP GLN VAL LYS GLU LEU LEU
SEQRES 10 A 174 THR SER PHE GLY PRO LEU LYS ALA PHE ASN LEU VAL LYS
SEQRES 11 A 174 ASP SER ALA THR GLY LEU SER LYS GLY TYR ALA PHE CYS
SEQRES 12 A 174 GLU TYR VAL ASP ILE ASN VAL THR ASP GLN ALA ILE ALA
SEQRES 13 A 174 GLY LEU ASN GLY MET GLN LEU GLY ASP LYS LYS LEU LEU
SEQRES 14 A 174 VAL GLN ARG ALA SER
SEQRES 1 B 174 GLY PRO LEU GLY SER ALA ARG ARG LEU TYR VAL GLY ASN
SEQRES 2 B 174 ILE PRO PHE GLY ILE THR GLU GLU ALA MET MET ASP PHE
SEQRES 3 B 174 PHE ASN ALA GLN MET ARG LEU GLY GLY LEU THR GLN ALA
SEQRES 4 B 174 PRO GLY ASN PRO VAL LEU ALA VAL GLN ILE ASN GLN ASP
SEQRES 5 B 174 LYS ASN PHE ALA PHE LEU GLU PHE ARG SER VAL ASP GLU
SEQRES 6 B 174 THR THR GLN ALA MET ALA PHE ASP GLY ILE ILE PHE GLN
SEQRES 7 B 174 GLY GLN SER LEU LYS ILE ARG ARG PRO HIS ASP TYR GLN
SEQRES 8 B 174 PRO LEU PRO GLY ALA HIS LYS LEU PHE ILE GLY GLY LEU
SEQRES 9 B 174 PRO ASN TYR LEU ASN ASP ASP GLN VAL LYS GLU LEU LEU
SEQRES 10 B 174 THR SER PHE GLY PRO LEU LYS ALA PHE ASN LEU VAL LYS
SEQRES 11 B 174 ASP SER ALA THR GLY LEU SER LYS GLY TYR ALA PHE CYS
SEQRES 12 B 174 GLU TYR VAL ASP ILE ASN VAL THR ASP GLN ALA ILE ALA
SEQRES 13 B 174 GLY LEU ASN GLY MET GLN LEU GLY ASP LYS LYS LEU LEU
SEQRES 14 B 174 VAL GLN ARG ALA SER
SEQRES 1 P 7 DU DU DU DU BRU DU DU
SEQRES 1 E 7 DU DU DU DU BRU DU DU
MODRES 3VAK BRU P 5 DU
MODRES 3VAK BRU E 5 DU
HET BRU P 5 20
HET BRU E 5 20
HET DIO A 401 6
HET DIO A 402 6
HET SO4 A 403 5
HET SO4 A 404 5
HET SO4 A 405 5
HET SO4 A 406 5
HET GOL A 407 6
HET GOL A 408 6
HET GOL A 409 6
HET DIO B 401 6
HET DIO B 402 6
HET DIO B 403 6
HET CPQ B 404 27
HET SO4 B 405 5
HET SO4 B 406 5
HET SO4 B 407 5
HET GOL B 408 6
HETNAM BRU 5-BROMO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM CPQ N,N-BIS(3-D-GLUCONAMIDOPROPYL)DEOXYCHOLAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN CPQ DEOXY-BIGCHAP
FORMUL 3 BRU 2(C9 H12 BR N2 O8 P)
FORMUL 5 DIO 5(C4 H8 O2)
FORMUL 7 SO4 7(O4 S 2-)
FORMUL 11 GOL 4(C3 H8 O3)
FORMUL 17 CPQ C42 H75 N3 O15
FORMUL 22 HOH *272(H2 O)
HELIX 1 1 THR A 161 GLY A 176 1 16
HELIX 2 2 SER A 204 MET A 212 1 9
HELIX 3 3 ALA A 213 ASP A 215 5 3
HELIX 4 4 ASN A 271 THR A 280 1 10
HELIX 5 5 ASN A 311 ASN A 321 1 11
HELIX 6 6 GLY B 146 ALA B 148 5 3
HELIX 7 7 THR B 161 GLY B 176 1 16
HELIX 8 8 SER B 204 MET B 212 1 9
HELIX 9 9 ALA B 213 ASP B 215 5 3
HELIX 10 10 ASN B 271 THR B 280 1 10
HELIX 11 11 ASP B 309 ASN B 311 5 3
HELIX 12 12 VAL B 312 ASN B 321 1 10
SHEET 1 A 4 VAL A 186 ASN A 192 0
SHEET 2 A 4 PHE A 197 PHE A 202 -1 O PHE A 197 N ASN A 192
SHEET 3 A 4 ARG A 150 GLY A 154 -1 N VAL A 153 O ALA A 198
SHEET 4 A 4 LYS A 225 ARG A 227 -1 O LYS A 225 N GLY A 154
SHEET 1 B 2 ILE A 218 PHE A 219 0
SHEET 2 B 2 GLN A 222 SER A 223 -1 O GLN A 222 N PHE A 219
SHEET 1 C 4 LEU A 285 LYS A 292 0
SHEET 2 C 4 SER A 299 TYR A 307 -1 O GLU A 306 N LYS A 286
SHEET 3 C 4 LEU A 261 GLY A 264 -1 N LEU A 261 O CYS A 305
SHEET 4 C 4 LEU A 331 ARG A 334 -1 O GLN A 333 N PHE A 262
SHEET 1 D 2 GLN A 324 LEU A 325 0
SHEET 2 D 2 LYS A 328 LYS A 329 -1 O LYS A 328 N LEU A 325
SHEET 1 E 4 VAL B 186 ASN B 192 0
SHEET 2 E 4 PHE B 197 PHE B 202 -1 O PHE B 197 N ASN B 192
SHEET 3 E 4 ARG B 150 GLY B 154 -1 N VAL B 153 O ALA B 198
SHEET 4 E 4 LYS B 225 ARG B 227 -1 O LYS B 225 N GLY B 154
SHEET 1 F 2 ILE B 218 PHE B 219 0
SHEET 2 F 2 GLN B 222 SER B 223 -1 O GLN B 222 N PHE B 219
SHEET 1 G 4 LEU B 285 ASP B 293 0
SHEET 2 G 4 LEU B 298 TYR B 307 -1 O LEU B 298 N ASP B 293
SHEET 3 G 4 LEU B 261 GLY B 264 -1 N ILE B 263 O ALA B 303
SHEET 4 G 4 LEU B 331 ARG B 334 -1 O GLN B 333 N PHE B 262
SHEET 1 H 2 GLN B 324 LEU B 325 0
SHEET 2 H 2 LYS B 328 LYS B 329 -1 O LYS B 328 N LEU B 325
LINK C GLY A 237 N ALA A 258 1555 1555 1.33
LINK C GLY B 237 N ALA B 258 1555 1555 1.33
LINK O3' DU P 4 P BRU P 5 1555 1555 1.59
LINK O3' BRU P 5 P DU P 6 1555 1555 1.61
LINK O3' DU E 4 P BRU E 5 1555 1555 1.59
LINK O3' BRU E 5 P DU E 6 1555 1555 1.61
CISPEP 1 GLY A 143 PRO A 144 0 -3.26
SITE 1 AC1 5 TYR A 269 ASN A 271 GLY A 297 LEU A 298
SITE 2 AC1 5 SER A 299
SITE 1 AC2 4 PRO A 144 ALA A 148 GLN A 233 LEU A 325
SITE 1 AC3 3 LYS A 225 ARG A 227 HOH A 613
SITE 1 AC4 4 GLN A 190 ILE A 191 HOH A 585 DU P 6
SITE 1 AC5 6 ARG A 149 ARG A 150 GLU A 201 SER A 281
SITE 2 AC5 6 HOH A 507 DU P 7
SITE 1 AC6 2 ARG A 228 ILE A 310
SITE 1 AC7 2 ASN A 192 ASP A 194
SITE 1 AC8 3 LEU A 285 HOH A 544 HOH A 640
SITE 1 AC9 5 LYS B 276 LEU B 285 LYS B 286 PHE B 288
SITE 2 AC9 5 HOH B 589
SITE 1 BC1 3 PRO B 182 GLY B 183 HIS B 259
SITE 1 BC2 4 TYR B 269 GLY B 297 SER B 299 HOH B 574
SITE 1 BC3 1 GLN B 274
SITE 1 BC4 5 ARG B 149 ARG B 203 SER B 204 VAL B 205
SITE 2 BC4 5 HOH B 547
SITE 1 BC5 2 ARG A 174 ARG B 227
SITE 1 BC6 2 MET B 212 ARG B 228
SITE 1 BC7 3 ALA B 181 ARG B 334 HOH B 507
CRYST1 166.406 37.726 101.631 90.00 125.43 90.00 C 1 2 1 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 0.006009 0.000000 0.004275 0.00000
SCALE2 0.000000 0.026507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012076 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
