HEADER PROTEIN TRANSPORT/PROTEIN BINDING 10-NOV-11 3UKY
TITLE MOUSE IMPORTIN ALPHA: YEAST CBP80 CNLS COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMPORTIN SUBUNIT ALPHA-2;
COMPND 3 CHAIN: B;
COMPND 4 FRAGMENT: UNP RESIDUES 70-529;
COMPND 5 SYNONYM: IMPORTIN ALPHA P1, KARYOPHERIN SUBUNIT ALPHA-2, PENDULIN,
COMPND 6 PORE TARGETING COMPLEX 58 KDA SUBUNIT, PTAC58, RAG COHORT PROTEIN 1,
COMPND 7 SRP1-ALPHA;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: NUCLEAR CAP-BINDING PROTEIN COMPLEX SUBUNIT 1;
COMPND 11 CHAIN: C;
COMPND 12 FRAGMENT: YCBP80 CNLS PEPTIDE, RESIDUES 1-30;
COMPND 13 SYNONYM: CAP-BINDING PROTEIN 80, CBP80;
COMPND 14 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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 10 ORGANISM_COMMON: YEAST;
SOURCE 11 ORGANISM_TAXID: 559292;
SOURCE 12 STRAIN: S288C;
SOURCE 13 GENE: CBP80;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ARM REPEAT, ARMADILLO REPEAT, NUCLEAR TRANSPORT, NUCLEAR LOCALISATION
KEYWDS 2 SIGNAL BINDING, IMPORTIN BETA BINDING, PROTEIN TRANSPORT-PROTEIN
KEYWDS 3 BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MARFORI,J.K.FORWOOD,T.G.LONHIENNE,B.KOBE
REVDAT 2 01-NOV-23 3UKY 1 SEQADV
REVDAT 1 03-OCT-12 3UKY 0
JRNL AUTH M.MARFORI,T.G.LONHIENNE,J.K.FORWOOD,B.KOBE
JRNL TITL STRUCTURAL BASIS OF HIGH-AFFINITY NUCLEAR LOCALIZATION
JRNL TITL 2 SIGNAL INTERACTIONS WITH IMPORTIN-ALPHA
JRNL REF TRAFFIC V. 13 532 2012
JRNL REFN ISSN 1398-9219
JRNL PMID 22248489
JRNL DOI 10.1111/J.1600-0854.2012.01329.X
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.18
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 28351
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1437
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 43.1868 - 5.0605 1.00 2975 160 0.1740 0.1893
REMARK 3 2 5.0605 - 4.0176 1.00 2847 149 0.1437 0.1638
REMARK 3 3 4.0176 - 3.5100 1.00 2790 149 0.1694 0.1883
REMARK 3 4 3.5100 - 3.1892 0.99 2770 161 0.1956 0.2108
REMARK 3 5 3.1892 - 2.9607 0.98 2743 142 0.1971 0.2243
REMARK 3 6 2.9607 - 2.7861 0.98 2722 131 0.2008 0.2405
REMARK 3 7 2.7861 - 2.6466 0.95 2605 162 0.2237 0.2714
REMARK 3 8 2.6466 - 2.5314 0.93 2560 131 0.2408 0.3050
REMARK 3 9 2.5314 - 2.4340 0.91 2510 130 0.2545 0.3295
REMARK 3 10 2.4340 - 2.3500 0.86 2392 122 0.2502 0.2592
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 27.98
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.66
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.66690
REMARK 3 B22 (A**2) : -6.31260
REMARK 3 B33 (A**2) : 6.97950
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 : 0.002 3451
REMARK 3 ANGLE : 0.596 4696
REMARK 3 CHIRALITY : 0.043 561
REMARK 3 PLANARITY : 0.003 604
REMARK 3 DIHEDRAL : 12.439 1283
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN B AND RESID 71:78)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.0265 -16.9729 -13.8950
REMARK 3 T TENSOR
REMARK 3 T11: 0.5799 T22: 0.2067
REMARK 3 T33: 0.4601 T12: -0.2446
REMARK 3 T13: 0.0517 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.0923 L22: 0.5357
REMARK 3 L33: 0.5183 L12: -0.2003
REMARK 3 L13: 0.0719 L23: -0.2496
REMARK 3 S TENSOR
REMARK 3 S11: -0.3472 S12: -0.2171 S13: -0.0923
REMARK 3 S21: 0.3648 S22: -0.2074 S23: 0.6467
REMARK 3 S31: 0.1964 S32: -0.5727 S33: -0.0343
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 79:123)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.5180 -11.6778 -13.6378
REMARK 3 T TENSOR
REMARK 3 T11: 0.2378 T22: 0.1730
REMARK 3 T33: 0.2092 T12: -0.0369
REMARK 3 T13: -0.0372 T23: -0.0053
REMARK 3 L TENSOR
REMARK 3 L11: 1.1462 L22: 1.0108
REMARK 3 L33: 0.6187 L12: -0.1878
REMARK 3 L13: 0.3132 L23: 0.0367
REMARK 3 S TENSOR
REMARK 3 S11: 0.1740 S12: -0.0961 S13: -0.2471
REMARK 3 S21: 0.2889 S22: -0.0585 S23: 0.0126
REMARK 3 S31: 0.2623 S32: -0.0316 S33: -0.0145
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 124:220)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9673 5.8289 -17.7704
REMARK 3 T TENSOR
REMARK 3 T11: 0.1584 T22: 0.1119
REMARK 3 T33: 0.1347 T12: 0.0145
REMARK 3 T13: -0.0237 T23: -0.0152
REMARK 3 L TENSOR
REMARK 3 L11: 0.5963 L22: 0.9125
REMARK 3 L33: -0.3736 L12: -0.0088
REMARK 3 L13: 0.0976 L23: 0.2601
REMARK 3 S TENSOR
REMARK 3 S11: 0.0800 S12: 0.0172 S13: 0.0321
REMARK 3 S21: -0.0567 S22: -0.0532 S23: 0.0093
REMARK 3 S31: 0.0354 S32: 0.0272 S33: -0.0100
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 221:310)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.9828 23.4357 -11.1454
REMARK 3 T TENSOR
REMARK 3 T11: 0.0829 T22: 0.0801
REMARK 3 T33: 0.1746 T12: -0.0053
REMARK 3 T13: 0.0047 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.3880 L22: 0.6249
REMARK 3 L33: 0.5983 L12: -0.6258
REMARK 3 L13: -0.2472 L23: 0.5126
REMARK 3 S TENSOR
REMARK 3 S11: 0.0467 S12: -0.0448 S13: 0.0933
REMARK 3 S21: -0.0699 S22: -0.0186 S23: -0.0485
REMARK 3 S31: -0.0105 S32: 0.0166 S33: -0.0356
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN B AND RESID 311:414)
REMARK 3 ORIGIN FOR THE GROUP (A): -8.3488 35.5800 7.0825
REMARK 3 T TENSOR
REMARK 3 T11: 0.1071 T22: 0.0888
REMARK 3 T33: 0.2230 T12: -0.0071
REMARK 3 T13: 0.0090 T23: -0.0477
REMARK 3 L TENSOR
REMARK 3 L11: 1.4569 L22: 0.2545
REMARK 3 L33: 1.4263 L12: -0.6441
REMARK 3 L13: -0.8469 L23: 0.3065
REMARK 3 S TENSOR
REMARK 3 S11: 0.0366 S12: -0.1584 S13: 0.1961
REMARK 3 S21: -0.0605 S22: 0.1268 S23: -0.2515
REMARK 3 S31: -0.0855 S32: 0.1083 S33: 0.0921
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN B AND RESID 415:449)
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9221 37.3585 23.3107
REMARK 3 T TENSOR
REMARK 3 T11: 0.2262 T22: 0.4135
REMARK 3 T33: 0.2837 T12: 0.0175
REMARK 3 T13: -0.0715 T23: -0.0883
REMARK 3 L TENSOR
REMARK 3 L11: 0.5017 L22: 0.2731
REMARK 3 L33: 0.3497 L12: 0.0444
REMARK 3 L13: -0.1847 L23: 0.1521
REMARK 3 S TENSOR
REMARK 3 S11: -0.0310 S12: -0.9552 S13: 0.4757
REMARK 3 S21: 0.1701 S22: 0.1292 S23: -0.0939
REMARK 3 S31: -0.0092 S32: 0.2382 S33: -0.0663
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN B AND RESID 450:472)
REMARK 3 ORIGIN FOR THE GROUP (A): -11.7510 46.0992 29.9622
REMARK 3 T TENSOR
REMARK 3 T11: 0.5442 T22: 0.6944
REMARK 3 T33: 0.3997 T12: -0.0679
REMARK 3 T13: -0.0560 T23: -0.2660
REMARK 3 L TENSOR
REMARK 3 L11: 2.3278 L22: 2.8305
REMARK 3 L33: 1.2219 L12: -0.5282
REMARK 3 L13: 0.4260 L23: 1.4365
REMARK 3 S TENSOR
REMARK 3 S11: -0.6766 S12: -1.8379 S13: 0.3050
REMARK 3 S21: 1.1751 S22: 0.9972 S23: 0.0804
REMARK 3 S31: -0.4022 S32: 0.0477 S33: -0.1050
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: (CHAIN B AND RESID 473:497)
REMARK 3 ORIGIN FOR THE GROUP (A): -0.2022 37.5467 34.4157
REMARK 3 T TENSOR
REMARK 3 T11: 0.8134 T22: 1.1879
REMARK 3 T33: 0.5476 T12: 0.0382
REMARK 3 T13: -0.3030 T23: -0.0965
REMARK 3 L TENSOR
REMARK 3 L11: 1.0004 L22: 1.2081
REMARK 3 L33: -0.0016 L12: -0.6476
REMARK 3 L13: 0.0629 L23: -0.0827
REMARK 3 S TENSOR
REMARK 3 S11: 0.2854 S12: -0.8857 S13: 0.0265
REMARK 3 S21: 1.3108 S22: 0.3231 S23: -0.6859
REMARK 3 S31: 0.3799 S32: 1.0173 S33: -0.1061
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: (CHAIN C AND RESID 3:23)
REMARK 3 ORIGIN FOR THE GROUP (A): 2.7536 30.9928 6.8270
REMARK 3 T TENSOR
REMARK 3 T11: 0.6160 T22: 0.4302
REMARK 3 T33: 0.5824 T12: 0.0538
REMARK 3 T13: 0.1116 T23: -0.1714
REMARK 3 L TENSOR
REMARK 3 L11: 0.2729 L22: 0.6055
REMARK 3 L33: 0.2852 L12: 0.2297
REMARK 3 L13: 0.0786 L23: 0.1686
REMARK 3 S TENSOR
REMARK 3 S11: 0.0601 S12: -0.0288 S13: -0.7994
REMARK 3 S21: -0.2116 S22: 0.1713 S23: -0.0728
REMARK 3 S31: 0.9195 S32: 0.3915 S33: -0.0847
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: (CHAIN C AND RESID 24:30)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.7412 2.8751 -9.5607
REMARK 3 T TENSOR
REMARK 3 T11: 0.3291 T22: 0.2971
REMARK 3 T33: 0.3104 T12: -0.0522
REMARK 3 T13: -0.0009 T23: -0.0906
REMARK 3 L TENSOR
REMARK 3 L11: 1.6173 L22: 2.0945
REMARK 3 L33: 1.4257 L12: -0.1457
REMARK 3 L13: 1.2219 L23: -0.1853
REMARK 3 S TENSOR
REMARK 3 S11: 0.3071 S12: 0.1082 S13: -0.1780
REMARK 3 S21: -0.0812 S22: -0.2596 S23: 0.7848
REMARK 3 S31: 0.1850 S32: -0.2326 S33: -0.0919
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 3UKY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-NOV-11.
REMARK 100 THE DEPOSITION ID IS D_1000068884.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 0.953693
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29432
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 68.4
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: 1PJN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.91
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M SODIUM CITRATE, 10MM DTT, 0.1M
REMARK 280 HEPES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 39.09750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.25500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.87350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.25500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.09750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.87350
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: 2380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 B 20
REMARK 465 HIS B 21
REMARK 465 HIS B 22
REMARK 465 HIS B 23
REMARK 465 HIS B 24
REMARK 465 HIS B 25
REMARK 465 HIS B 26
REMARK 465 SER B 27
REMARK 465 SER B 28
REMARK 465 GLY B 29
REMARK 465 LEU B 30
REMARK 465 VAL B 31
REMARK 465 PRO B 32
REMARK 465 ARG B 33
REMARK 465 GLY B 34
REMARK 465 SER B 35
REMARK 465 GLY B 36
REMARK 465 MET B 37
REMARK 465 LEU B 38
REMARK 465 GLU B 39
REMARK 465 THR B 40
REMARK 465 ALA B 41
REMARK 465 ALA B 42
REMARK 465 ALA B 43
REMARK 465 LEU B 44
REMARK 465 PHE B 45
REMARK 465 GLU B 46
REMARK 465 ARG B 47
REMARK 465 ASN B 48
REMARK 465 HIS B 49
REMARK 465 MET B 50
REMARK 465 ASP B 51
REMARK 465 SER B 52
REMARK 465 PRO B 53
REMARK 465 ASP B 54
REMARK 465 LEU B 55
REMARK 465 GLY B 56
REMARK 465 THR B 57
REMARK 465 ASP B 58
REMARK 465 ASP B 59
REMARK 465 ASP B 60
REMARK 465 ASP B 61
REMARK 465 LEU B 62
REMARK 465 ALA B 63
REMARK 465 MET B 64
REMARK 465 ALA B 65
REMARK 465 ASP B 66
REMARK 465 ILE B 67
REMARK 465 GLY B 68
REMARK 465 SER B 69
REMARK 465 ASN B 70
REMARK 465 VAL B 498
REMARK 465 GLU B 499
REMARK 465 GLU B 500
REMARK 465 GLU B 501
REMARK 465 GLU B 502
REMARK 465 ASP B 503
REMARK 465 GLN B 504
REMARK 465 ASN B 505
REMARK 465 VAL B 506
REMARK 465 VAL B 507
REMARK 465 PRO B 508
REMARK 465 GLU B 509
REMARK 465 THR B 510
REMARK 465 THR B 511
REMARK 465 SER B 512
REMARK 465 GLU B 513
REMARK 465 GLY B 514
REMARK 465 PHE B 515
REMARK 465 ALA B 516
REMARK 465 PHE B 517
REMARK 465 GLN B 518
REMARK 465 VAL B 519
REMARK 465 GLN B 520
REMARK 465 ASP B 521
REMARK 465 GLY B 522
REMARK 465 ALA B 523
REMARK 465 PRO B 524
REMARK 465 GLY B 525
REMARK 465 THR B 526
REMARK 465 PHE B 527
REMARK 465 ASN B 528
REMARK 465 PHE B 529
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 MET C 1
REMARK 465 PHE C 2
REMARK 465 ASP C 9
REMARK 465 PHE C 10
REMARK 465 ASP C 11
REMARK 465 GLU C 12
REMARK 465 ASP C 13
REMARK 465 GLU C 14
REMARK 465 ASN C 15
REMARK 465 TYR C 16
REMARK 465 ARG C 17
REMARK 465 ASP C 18
REMARK 465 PHE C 19
REMARK 465 ARG C 20
REMARK 465 PRO C 21
REMARK 465 ARG C 22
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 O ARG C 4 O HOH C 159 2.10
REMARK 500 O HOH B 539 O HOH B 592 2.14
REMARK 500 O HOH B 627 O HOH B 683 2.18
REMARK 500 O HOH B 654 O HOH B 701 2.19
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 ASN B 239 153.48 85.40
REMARK 500 ALA B 389 167.75 179.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IAL RELATED DB: PDB
REMARK 900 IMPORTIN ALPHA, MOUSE
REMARK 900 RELATED ID: 3FEX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CBC-IMPORTIN ALPHA COMPLEX
REMARK 900 RELATED ID: 3FEY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CBC-IMPORTIN ALPHA COMPLEX
REMARK 900 RELATED ID: 3UKW RELATED DB: PDB
REMARK 900 RELATED ID: 3UKX RELATED DB: PDB
REMARK 900 RELATED ID: 3UKZ RELATED DB: PDB
REMARK 900 RELATED ID: 3UL0 RELATED DB: PDB
REMARK 900 RELATED ID: 3UL1 RELATED DB: PDB
DBREF 3UKY B 70 529 UNP P52293 IMA2_MOUSE 70 529
DBREF 3UKY C 1 30 UNP P34160 NCBP1_YEAST 1 30
SEQADV 3UKY MET B 20 UNP P52293 EXPRESSION TAG
SEQADV 3UKY HIS B 21 UNP P52293 EXPRESSION TAG
SEQADV 3UKY HIS B 22 UNP P52293 EXPRESSION TAG
SEQADV 3UKY HIS B 23 UNP P52293 EXPRESSION TAG
SEQADV 3UKY HIS B 24 UNP P52293 EXPRESSION TAG
SEQADV 3UKY HIS B 25 UNP P52293 EXPRESSION TAG
SEQADV 3UKY HIS B 26 UNP P52293 EXPRESSION TAG
SEQADV 3UKY SER B 27 UNP P52293 EXPRESSION TAG
SEQADV 3UKY SER B 28 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLY B 29 UNP P52293 EXPRESSION TAG
SEQADV 3UKY LEU B 30 UNP P52293 EXPRESSION TAG
SEQADV 3UKY VAL B 31 UNP P52293 EXPRESSION TAG
SEQADV 3UKY PRO B 32 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ARG B 33 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLY B 34 UNP P52293 EXPRESSION TAG
SEQADV 3UKY SER B 35 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLY B 36 UNP P52293 EXPRESSION TAG
SEQADV 3UKY MET B 37 UNP P52293 EXPRESSION TAG
SEQADV 3UKY LEU B 38 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLU B 39 UNP P52293 EXPRESSION TAG
SEQADV 3UKY THR B 40 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ALA B 41 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ALA B 42 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ALA B 43 UNP P52293 EXPRESSION TAG
SEQADV 3UKY LEU B 44 UNP P52293 EXPRESSION TAG
SEQADV 3UKY PHE B 45 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLU B 46 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ARG B 47 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASN B 48 UNP P52293 EXPRESSION TAG
SEQADV 3UKY HIS B 49 UNP P52293 EXPRESSION TAG
SEQADV 3UKY MET B 50 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASP B 51 UNP P52293 EXPRESSION TAG
SEQADV 3UKY SER B 52 UNP P52293 EXPRESSION TAG
SEQADV 3UKY PRO B 53 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASP B 54 UNP P52293 EXPRESSION TAG
SEQADV 3UKY LEU B 55 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLY B 56 UNP P52293 EXPRESSION TAG
SEQADV 3UKY THR B 57 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASP B 58 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASP B 59 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASP B 60 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASP B 61 UNP P52293 EXPRESSION TAG
SEQADV 3UKY LEU B 62 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ALA B 63 UNP P52293 EXPRESSION TAG
SEQADV 3UKY MET B 64 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ALA B 65 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ASP B 66 UNP P52293 EXPRESSION TAG
SEQADV 3UKY ILE B 67 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLY B 68 UNP P52293 EXPRESSION TAG
SEQADV 3UKY SER B 69 UNP P52293 EXPRESSION TAG
SEQADV 3UKY GLY C -1 UNP P34160 EXPRESSION TAG
SEQADV 3UKY SER C 0 UNP P34160 EXPRESSION TAG
SEQRES 1 B 510 MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO
SEQRES 2 B 510 ARG GLY SER GLY MET LEU GLU THR ALA ALA ALA LEU PHE
SEQRES 3 B 510 GLU ARG ASN HIS MET ASP SER PRO ASP LEU GLY THR ASP
SEQRES 4 B 510 ASP ASP ASP LEU ALA MET ALA ASP ILE GLY SER ASN GLN
SEQRES 5 B 510 GLY THR VAL ASN TRP SER VAL GLU ASP ILE VAL LYS GLY
SEQRES 6 B 510 ILE ASN SER ASN ASN LEU GLU SER GLN LEU GLN ALA THR
SEQRES 7 B 510 GLN ALA ALA ARG LYS LEU LEU SER ARG GLU LYS GLN PRO
SEQRES 8 B 510 PRO ILE ASP ASN ILE ILE ARG ALA GLY LEU ILE PRO LYS
SEQRES 9 B 510 PHE VAL SER PHE LEU GLY LYS THR ASP CYS SER PRO ILE
SEQRES 10 B 510 GLN PHE GLU SER ALA TRP ALA LEU THR ASN ILE ALA SER
SEQRES 11 B 510 GLY THR SER GLU GLN THR LYS ALA VAL VAL ASP GLY GLY
SEQRES 12 B 510 ALA ILE PRO ALA PHE ILE SER LEU LEU ALA SER PRO HIS
SEQRES 13 B 510 ALA HIS ILE SER GLU GLN ALA VAL TRP ALA LEU GLY ASN
SEQRES 14 B 510 ILE ALA GLY ASP GLY SER ALA PHE ARG ASP LEU VAL ILE
SEQRES 15 B 510 LYS HIS GLY ALA ILE ASP PRO LEU LEU ALA LEU LEU ALA
SEQRES 16 B 510 VAL PRO ASP LEU SER THR LEU ALA CYS GLY TYR LEU ARG
SEQRES 17 B 510 ASN LEU THR TRP THR LEU SER ASN LEU CYS ARG ASN LYS
SEQRES 18 B 510 ASN PRO ALA PRO PRO LEU ASP ALA VAL GLU GLN ILE LEU
SEQRES 19 B 510 PRO THR LEU VAL ARG LEU LEU HIS HIS ASN ASP PRO GLU
SEQRES 20 B 510 VAL LEU ALA ASP SER CYS TRP ALA ILE SER TYR LEU THR
SEQRES 21 B 510 ASP GLY PRO ASN GLU ARG ILE GLU MET VAL VAL LYS LYS
SEQRES 22 B 510 GLY VAL VAL PRO GLN LEU VAL LYS LEU LEU GLY ALA THR
SEQRES 23 B 510 GLU LEU PRO ILE VAL THR PRO ALA LEU ARG ALA ILE GLY
SEQRES 24 B 510 ASN ILE VAL THR GLY THR ASP GLU GLN THR GLN LYS VAL
SEQRES 25 B 510 ILE ASP ALA GLY ALA LEU ALA VAL PHE PRO SER LEU LEU
SEQRES 26 B 510 THR ASN PRO LYS THR ASN ILE GLN LYS GLU ALA THR TRP
SEQRES 27 B 510 THR MET SER ASN ILE THR ALA GLY ARG GLN ASP GLN ILE
SEQRES 28 B 510 GLN GLN VAL VAL ASN HIS GLY LEU VAL PRO PHE LEU VAL
SEQRES 29 B 510 GLY VAL LEU SER LYS ALA ASP PHE LYS THR GLN LYS GLU
SEQRES 30 B 510 ALA ALA TRP ALA ILE THR ASN TYR THR SER GLY GLY THR
SEQRES 31 B 510 VAL GLU GLN ILE VAL TYR LEU VAL HIS CYS GLY ILE ILE
SEQRES 32 B 510 GLU PRO LEU MET ASN LEU LEU SER ALA LYS ASP THR LYS
SEQRES 33 B 510 ILE ILE GLN VAL ILE LEU ASP ALA ILE SER ASN ILE PHE
SEQRES 34 B 510 GLN ALA ALA GLU LYS LEU GLY GLU THR GLU LYS LEU SER
SEQRES 35 B 510 ILE MET ILE GLU GLU CYS GLY GLY LEU ASP LYS ILE GLU
SEQRES 36 B 510 ALA LEU GLN ARG HIS GLU ASN GLU SER VAL TYR LYS ALA
SEQRES 37 B 510 SER LEU ASN LEU ILE GLU LYS TYR PHE SER VAL GLU GLU
SEQRES 38 B 510 GLU GLU ASP GLN ASN VAL VAL PRO GLU THR THR SER GLU
SEQRES 39 B 510 GLY PHE ALA PHE GLN VAL GLN ASP GLY ALA PRO GLY THR
SEQRES 40 B 510 PHE ASN PHE
SEQRES 1 C 32 GLY SER MET PHE ASN ARG LYS ARG ARG GLY ASP PHE ASP
SEQRES 2 C 32 GLU ASP GLU ASN TYR ARG ASP PHE ARG PRO ARG MET PRO
SEQRES 3 C 32 LYS ARG GLN ARG ILE PRO
FORMUL 3 HOH *212(H2 O)
HELIX 1 1 SER B 77 SER B 87 1 11
HELIX 2 2 ASN B 89 SER B 105 1 17
HELIX 3 3 PRO B 111 ALA B 118 1 8
HELIX 4 4 LEU B 120 LEU B 128 1 9
HELIX 5 5 CYS B 133 SER B 149 1 17
HELIX 6 6 THR B 151 GLY B 161 1 11
HELIX 7 7 GLY B 162 LEU B 171 1 10
HELIX 8 8 HIS B 175 GLY B 191 1 17
HELIX 9 9 GLY B 193 HIS B 203 1 11
HELIX 10 10 ALA B 205 LEU B 212 1 8
HELIX 11 11 ASP B 217 LEU B 221 5 5
HELIX 12 12 ALA B 222 CYS B 237 1 16
HELIX 13 13 PRO B 245 LEU B 260 1 16
HELIX 14 14 ASP B 264 THR B 279 1 16
HELIX 15 15 PRO B 282 LYS B 291 1 10
HELIX 16 16 VAL B 294 LEU B 302 1 9
HELIX 17 17 GLU B 306 VAL B 321 1 16
HELIX 18 18 THR B 324 ALA B 334 1 11
HELIX 19 19 GLY B 335 ALA B 338 5 4
HELIX 20 20 VAL B 339 LEU B 344 1 6
HELIX 21 21 LYS B 348 THR B 363 1 16
HELIX 22 22 ARG B 366 HIS B 376 1 11
HELIX 23 23 LEU B 378 LYS B 388 1 11
HELIX 24 24 ASP B 390 GLY B 408 1 19
HELIX 25 25 THR B 409 CYS B 419 1 11
HELIX 26 26 ILE B 421 LEU B 428 1 8
HELIX 27 27 LEU B 429 ALA B 431 5 3
HELIX 28 28 ASP B 433 LYS B 453 1 21
HELIX 29 29 GLU B 456 CYS B 467 1 12
HELIX 30 30 GLY B 468 LEU B 476 1 9
HELIX 31 31 GLN B 477 HIS B 479 5 3
HELIX 32 32 ASN B 481 PHE B 496 1 16
CISPEP 1 ASN B 241 PRO B 242 0 -1.80
CRYST1 78.195 89.747 98.510 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 0.012789 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011142 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010151 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
