HEADER PROTEIN BINDING 07-JAN-12 3VE6
TITLE CRYSTAL STRUCTURE ANALYSIS OF VENEZUELAN EQUINE ENCEPHALITIS VIRUS
TITLE 2 CAPSID PROTEIN NLS AND IMPORTIN ALPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMPORTIN SUBUNIT ALPHA-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: IMPORTIN ALPHA P1, KARYOPHERIN SUBUNIT ALPHA-2, PENDULIN,
COMPND 5 PORE TARGETING COMPLEX 58 KDA SUBUNIT, PTAC58, RAG COHORT PROTEIN 1,
COMPND 6 SRP1-ALPHA;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: VENEZUELAN EQUINE ENCEPHALITIS VIRUS CAPSID PROTEIN NLS;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: KPNA2, RCH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: VENEZUELAN EQUINE ENCEPHALITIS VIRUS;
SOURCE 12 ORGANISM_TAXID: 11036;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS IMPORTIN, IMPORTIN ALPHA, VENEZUELAN EQUINE ENCEPHALITIS VIRUS,
KEYWDS 2 CAPSID PROTEIN NLS, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FAN
REVDAT 4 28-FEB-24 3VE6 1 REMARK
REVDAT 3 28-MAR-12 3VE6 1 SOURCE
REVDAT 2 08-FEB-12 3VE6 1 JRNL
REVDAT 1 25-JAN-12 3VE6 0
JRNL AUTH F.FAN
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF VENEZUELAN EQUINE ENCEPHALITIS
JRNL TITL 2 VIRUS CAPSID PROTEIN NLS AND IMPORTIN ALPHA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 2011_12_24_0706
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 17446
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 882
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 50.9449 - 5.1394 1.00 2922 144 0.2073 0.2363
REMARK 3 2 5.1394 - 4.0798 1.00 2761 158 0.2008 0.2259
REMARK 3 3 4.0798 - 3.5643 1.00 2758 133 0.2231 0.3108
REMARK 3 4 3.5643 - 3.2384 1.00 2709 157 0.2535 0.2850
REMARK 3 5 3.2384 - 3.0064 1.00 2726 137 0.2643 0.3513
REMARK 3 6 3.0064 - 2.8290 1.00 2688 153 0.2817 0.3098
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.37
REMARK 3 B_SOL : 27.90
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 53.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.001 3395
REMARK 3 ANGLE : 0.462 4622
REMARK 3 CHIRALITY : 0.030 555
REMARK 3 PLANARITY : 0.002 593
REMARK 3 DIHEDRAL : 10.757 1249
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3VE6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.953692
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17446
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.829
REMARK 200 RESOLUTION RANGE LOW (A) : 50.937
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.47500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.79000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.87500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.79000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.47500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.87500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1613 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ASN A 5 62.93 61.63
REMARK 500 GLN A 39 89.41 32.43
REMARK 500 LYS A 60 89.19 -65.73
REMARK 500 ASN A 169 151.50 69.19
REMARK 500 PRO A 212 170.59 -56.70
REMARK 500 GLU A 386 41.24 -98.56
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3VE6 A 1 426 UNP P52293 IMA2_MOUSE 71 496
DBREF 3VE6 B 1 12 UNP Q9WCF8 Q9WCF8_9VIRU 59 70
SEQRES 1 A 426 GLN GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL LYS
SEQRES 2 A 426 GLY ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN ALA
SEQRES 3 A 426 THR GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS GLN
SEQRES 4 A 426 PRO PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE PRO
SEQRES 5 A 426 LYS PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER PRO
SEQRES 6 A 426 ILE GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE ALA
SEQRES 7 A 426 SER GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP GLY
SEQRES 8 A 426 GLY ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER PRO
SEQRES 9 A 426 HIS ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU GLY
SEQRES 10 A 426 ASN ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU VAL
SEQRES 11 A 426 ILE LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU LEU
SEQRES 12 A 426 ALA VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR LEU
SEQRES 13 A 426 ARG ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG ASN
SEQRES 14 A 426 LYS ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN ILE
SEQRES 15 A 426 LEU PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP PRO
SEQRES 16 A 426 GLU VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR LEU
SEQRES 17 A 426 THR ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL LYS
SEQRES 18 A 426 LYS GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY ALA
SEQRES 19 A 426 THR GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA ILE
SEQRES 20 A 426 GLY ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN LYS
SEQRES 21 A 426 VAL ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER LEU
SEQRES 22 A 426 LEU THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA THR
SEQRES 23 A 426 TRP THR MET SER ASN ILE THR ALA GLY ARG GLN ASP GLN
SEQRES 24 A 426 ILE GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE LEU
SEQRES 25 A 426 VAL GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN LYS
SEQRES 26 A 426 GLU ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY GLY
SEQRES 27 A 426 THR VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY ILE
SEQRES 28 A 426 ILE GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP THR
SEQRES 29 A 426 LYS ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN ILE
SEQRES 30 A 426 PHE GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS LEU
SEQRES 31 A 426 SER ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS ILE
SEQRES 32 A 426 GLU ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR LYS
SEQRES 33 A 426 ALA SER LEU ASN LEU ILE GLU LYS TYR PHE
SEQRES 1 B 12 GLU GLY PRO SER ALA LYS LYS PRO LYS LYS GLU ALA
HELIX 1 1 SER A 7 ASN A 16 1 10
HELIX 2 2 ASN A 19 SER A 35 1 17
HELIX 3 3 PRO A 41 ALA A 48 1 8
HELIX 4 4 LEU A 50 LEU A 58 1 9
HELIX 5 5 CYS A 63 SER A 79 1 17
HELIX 6 6 THR A 81 GLY A 91 1 11
HELIX 7 7 ALA A 93 LEU A 101 1 9
HELIX 8 8 HIS A 105 ASP A 122 1 18
HELIX 9 9 GLY A 123 HIS A 133 1 11
HELIX 10 10 ALA A 135 LEU A 142 1 8
HELIX 11 11 ASP A 147 LEU A 151 5 5
HELIX 12 12 ALA A 152 LEU A 166 1 15
HELIX 13 13 PRO A 175 LEU A 190 1 16
HELIX 14 14 ASP A 194 ASP A 210 1 17
HELIX 15 15 PRO A 212 LYS A 221 1 10
HELIX 16 16 VAL A 224 GLY A 233 1 10
HELIX 17 17 GLU A 236 VAL A 251 1 16
HELIX 18 18 THR A 254 GLY A 265 1 12
HELIX 19 19 ALA A 266 ALA A 268 5 3
HELIX 20 20 VAL A 269 LEU A 274 1 6
HELIX 21 21 LYS A 278 ASN A 291 1 14
HELIX 22 22 ARG A 296 HIS A 306 1 11
HELIX 23 23 LEU A 308 LYS A 318 1 11
HELIX 24 24 ASP A 320 GLY A 338 1 19
HELIX 25 25 THR A 339 CYS A 349 1 11
HELIX 26 26 ILE A 351 ASN A 357 1 7
HELIX 27 27 LEU A 358 ALA A 361 5 4
HELIX 28 28 ASP A 363 GLU A 382 1 20
HELIX 29 29 GLU A 386 GLU A 396 1 11
HELIX 30 30 GLY A 399 GLN A 407 1 9
HELIX 31 31 ASN A 411 TYR A 425 1 15
CISPEP 1 ASN A 171 PRO A 172 0 -4.22
CRYST1 78.950 89.750 99.580 90.00 90.00 90.00 P 21 21 21 4
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 0.012666 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010042 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
