HEADER SIGNALING PROTEIN/SIGNALING PROTEIN 22-MAR-13 4JS0
TITLE COMPLEX OF CDC42 WITH THE CRIB-PR DOMAIN OF IRSP53
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION CONTROL PROTEIN 42 HOMOLOG;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: G25K GTP-BINDING PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BRAIN-SPECIFIC ANGIOGENESIS INHIBITOR 1-ASSOCIATED PROTEIN
COMPND 9 2;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: CRIB-PR DOMAIN;
COMPND 12 SYNONYM: BAI-ASSOCIATED PROTEIN 2, BAI1-ASSOCIATED PROTEIN 2, PROTEIN
COMPND 13 BAP2, FAS LIGAND-ASSOCIATED FACTOR 3, FLAF3, INSULIN RECEPTOR
COMPND 14 SUBSTRATE P53/P58, IRS-58, IRSP53/58, INSULIN RECEPTOR SUBSTRATE
COMPND 15 PROTEIN OF 53 KDA, IRSP53, INSULIN RECEPTOR SUBSTRATE P53;
COMPND 16 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: CDC42;
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 EXPRESSION_SYSTEM_PLASMID: PTYB11;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS GTPASE BINDING DOMAIN, CRIB DOMAIN, CYTOSKELETON REGULATION,
KEYWDS 2 SIGNALING PROTEIN-SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.J.KAST,R.DOMINGUEZ
REVDAT 4 28-FEB-24 4JS0 1 REMARK SEQADV LINK
REVDAT 3 30-APR-14 4JS0 1 JRNL
REVDAT 2 02-APR-14 4JS0 1 JRNL
REVDAT 1 05-MAR-14 4JS0 0
JRNL AUTH D.J.KAST,C.YANG,A.DISANZA,M.BOCZKOWSKA,Y.MADASU,G.SCITA,
JRNL AUTH 2 T.SVITKINA,R.DOMINGUEZ
JRNL TITL MECHANISM OF IRSP53 INHIBITION AND COMBINATORIAL ACTIVATION
JRNL TITL 2 BY CDC42 AND DOWNSTREAM EFFECTORS.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 21 413 2014
JRNL REFN ISSN 1545-9993
JRNL PMID 24584464
JRNL DOI 10.1038/NSMB.2781
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 14959
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.148
REMARK 3 R VALUE (WORKING SET) : 0.146
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 754
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 34.3019 - 3.2486 1.00 3023 153 0.1421 0.1857
REMARK 3 2 3.2486 - 2.5788 1.00 2836 141 0.1506 0.2050
REMARK 3 3 2.5788 - 2.2529 1.00 2816 161 0.1423 0.1878
REMARK 3 4 2.2529 - 2.0469 1.00 2783 145 0.1418 0.2286
REMARK 3 5 2.0469 - 1.9000 0.99 2747 154 0.1613 0.2210
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.520
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.015 1745
REMARK 3 ANGLE : 1.689 2397
REMARK 3 CHIRALITY : 0.082 275
REMARK 3 PLANARITY : 0.007 295
REMARK 3 DIHEDRAL : 17.174 663
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESID 1:15 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.2091 -25.0490 17.4372
REMARK 3 T TENSOR
REMARK 3 T11: 0.0958 T22: 0.2296
REMARK 3 T33: 0.1782 T12: -0.0226
REMARK 3 T13: -0.0145 T23: 0.0399
REMARK 3 L TENSOR
REMARK 3 L11: 1.0467 L22: 2.0030
REMARK 3 L33: 1.7518 L12: 0.1111
REMARK 3 L13: -0.2296 L23: 0.4162
REMARK 3 S TENSOR
REMARK 3 S11: 0.0751 S12: -0.2878 S13: -0.1721
REMARK 3 S21: 0.0996 S22: -0.0042 S23: -0.3183
REMARK 3 S31: 0.0885 S32: 0.2539 S33: -0.0866
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESID 16:58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6733 -31.8544 13.6871
REMARK 3 T TENSOR
REMARK 3 T11: 0.1206 T22: 0.1717
REMARK 3 T33: 0.2768 T12: -0.0208
REMARK 3 T13: -0.0240 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 4.3433 L22: 1.1597
REMARK 3 L33: 3.1425 L12: 0.5967
REMARK 3 L13: 0.2473 L23: 0.6501
REMARK 3 S TENSOR
REMARK 3 S11: 0.0090 S12: -0.1377 S13: -0.2392
REMARK 3 S21: 0.0770 S22: -0.0049 S23: -0.4780
REMARK 3 S31: 0.1266 S32: 0.1658 S33: -0.0254
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESID 59:71 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7901 -26.1215 25.8649
REMARK 3 T TENSOR
REMARK 3 T11: 0.2821 T22: 0.5397
REMARK 3 T33: 0.2168 T12: -0.1011
REMARK 3 T13: 0.0730 T23: 0.0746
REMARK 3 L TENSOR
REMARK 3 L11: 3.0561 L22: 8.5080
REMARK 3 L33: 1.7732 L12: -1.0744
REMARK 3 L13: 0.7674 L23: 0.9820
REMARK 3 S TENSOR
REMARK 3 S11: -0.1125 S12: -0.5009 S13: -0.2845
REMARK 3 S21: 0.9678 S22: -0.0104 S23: 0.9241
REMARK 3 S31: 0.2730 S32: -0.7544 S33: 0.0839
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESID 72:122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2327 -18.8032 14.2244
REMARK 3 T TENSOR
REMARK 3 T11: 0.0835 T22: 0.1863
REMARK 3 T33: 0.1169 T12: -0.0271
REMARK 3 T13: 0.0078 T23: 0.0398
REMARK 3 L TENSOR
REMARK 3 L11: 3.0039 L22: 2.5899
REMARK 3 L33: 3.3161 L12: 0.5946
REMARK 3 L13: 0.8139 L23: 1.2159
REMARK 3 S TENSOR
REMARK 3 S11: 0.0102 S12: -0.2914 S13: 0.1969
REMARK 3 S21: 0.0681 S22: 0.0311 S23: 0.0312
REMARK 3 S31: -0.1973 S32: -0.0880 S33: -0.0450
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESID 123:164 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.2003 -19.0664 2.5943
REMARK 3 T TENSOR
REMARK 3 T11: 0.1670 T22: 0.2436
REMARK 3 T33: 0.1352 T12: -0.0486
REMARK 3 T13: -0.0015 T23: 0.0842
REMARK 3 L TENSOR
REMARK 3 L11: 3.2350 L22: 2.3994
REMARK 3 L33: 1.8242 L12: 0.0087
REMARK 3 L13: 0.5029 L23: 0.4121
REMARK 3 S TENSOR
REMARK 3 S11: -0.0622 S12: 0.1676 S13: 0.2149
REMARK 3 S21: -0.2723 S22: 0.1004 S23: 0.0275
REMARK 3 S31: -0.2261 S32: -0.1248 S33: -0.0184
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN A AND (RESID 165:178 )
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8060 -20.7967 8.3971
REMARK 3 T TENSOR
REMARK 3 T11: 0.1274 T22: 0.2032
REMARK 3 T33: 0.1653 T12: -0.0497
REMARK 3 T13: 0.0070 T23: 0.0488
REMARK 3 L TENSOR
REMARK 3 L11: 4.1385 L22: 8.7135
REMARK 3 L33: 9.4291 L12: 3.0872
REMARK 3 L13: 2.7746 L23: 7.0593
REMARK 3 S TENSOR
REMARK 3 S11: -0.0192 S12: 0.1618 S13: -0.0008
REMARK 3 S21: -0.1541 S22: 0.2934 S23: -0.4682
REMARK 3 S31: -0.1842 S32: 0.4941 S33: -0.3178
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN B AND (RESID 263:280 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3343 -28.2573 13.1876
REMARK 3 T TENSOR
REMARK 3 T11: 0.1909 T22: 0.3350
REMARK 3 T33: 0.3489 T12: -0.0830
REMARK 3 T13: 0.0474 T23: -0.0080
REMARK 3 L TENSOR
REMARK 3 L11: 4.7191 L22: 3.1725
REMARK 3 L33: 6.7043 L12: -1.7821
REMARK 3 L13: -0.6478 L23: 0.1486
REMARK 3 S TENSOR
REMARK 3 S11: 0.0466 S12: -0.3680 S13: -0.1366
REMARK 3 S21: -0.0780 S22: -0.2439 S23: -0.5518
REMARK 3 S31: -0.2306 S32: 0.7127 S33: 0.2067
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN B AND (RESID 281:286 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.7015 -32.7290 31.8750
REMARK 3 T TENSOR
REMARK 3 T11: 0.3223 T22: 0.6236
REMARK 3 T33: 0.2001 T12: -0.0466
REMARK 3 T13: -0.0160 T23: 0.0972
REMARK 3 L TENSOR
REMARK 3 L11: 8.8455 L22: 8.4890
REMARK 3 L33: 3.9540 L12: -2.3954
REMARK 3 L13: 5.5014 L23: 0.1389
REMARK 3 S TENSOR
REMARK 3 S11: 0.2479 S12: -0.8971 S13: 0.0577
REMARK 3 S21: 0.6490 S22: -0.2238 S23: -0.2241
REMARK 3 S31: 0.9411 S32: 0.7572 S33: -0.0360
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN B AND (RESID 287:291 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8462 -38.6962 20.8421
REMARK 3 T TENSOR
REMARK 3 T11: 0.7089 T22: 0.7851
REMARK 3 T33: 0.5293 T12: -0.1521
REMARK 3 T13: 0.1311 T23: 0.0901
REMARK 3 L TENSOR
REMARK 3 L11: 2.9522 L22: 1.1929
REMARK 3 L33: 4.4596 L12: 0.7317
REMARK 3 L13: 0.8013 L23: -1.8353
REMARK 3 S TENSOR
REMARK 3 S11: -0.7469 S12: 0.8359 S13: -0.9099
REMARK 3 S21: -1.2889 S22: 0.1525 S23: 0.2546
REMARK 3 S31: 1.6167 S32: -2.8036 S33: 0.5826
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 4JS0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078430.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-JUN-11
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 : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9769
REMARK 200 MONOCHROMATOR : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15019
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 17.80
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 18.40
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: PHENIX PHASER-MR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 36.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-20% PEG 4000, 0.2M MAGNESIUM
REMARK 280 CHLORIDE, 0.004M BETAIN HYDROCHLORIDE, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2
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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-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 0.000000 -1.000000 0.000000 33.61500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 33.61500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.87500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 33.61500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 33.61500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 39.87500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 33.61500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 33.61500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 39.87500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 33.61500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 33.61500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 39.87500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 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: 4010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10950 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 311 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 322 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 420 LIES ON A SPECIAL POSITION.
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 ALA B 260
REMARK 465 SER B 261
REMARK 465 LYS B 262
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 SER B 263 CB OG
REMARK 470 ARG B 289 CG CD NE CZ NH1 NH2
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 HOH A 317 O HOH B 303 2.10
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 VAL A 36 -69.39 -100.86
REMARK 500 LYS A 96 -57.82 -134.98
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 PE4 A 204
REMARK 610 PE4 A 205
REMARK 610 PE4 A 206
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 17 OG1
REMARK 620 2 THR A 35 OG1 81.6
REMARK 620 3 GNP A 201 O2G 171.1 89.6
REMARK 620 4 GNP A 201 O1B 90.9 172.1 97.9
REMARK 620 5 HOH A 302 O 86.8 88.9 93.5 93.2
REMARK 620 6 HOH A 304 O 89.0 89.8 90.6 87.5 175.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 341 O
REMARK 620 2 HOH A 346 O 83.4
REMARK 620 3 HOH A 372 O 87.7 89.0
REMARK 620 4 HOH A 384 O 99.7 175.6 94.2
REMARK 620 5 HOH A 385 O 161.4 86.2 107.5 89.9
REMARK 620 6 HOH A 414 O 75.7 77.3 159.5 100.4 87.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE4 A 206
DBREF 4JS0 A 1 178 UNP P60953 CDC42_HUMAN 1 178
DBREF 4JS0 B 260 291 UNP Q9UQB8 BAIP2_HUMAN 260 291
SEQADV 4JS0 VAL A 12 UNP P60953 GLY 12 ENGINEERED MUTATION
SEQRES 1 A 178 MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP VAL ALA
SEQRES 2 A 178 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 178 LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE ASP ASN
SEQRES 4 A 178 TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO TYR THR
SEQRES 5 A 178 LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 178 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 178 LEU VAL CYS PHE SER VAL VAL SER PRO SER SER PHE GLU
SEQRES 8 A 178 ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR HIS HIS
SEQRES 9 A 178 CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR GLN ILE
SEQRES 10 A 178 ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS LEU ALA
SEQRES 11 A 178 LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR ALA GLU
SEQRES 12 A 178 LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR VAL GLU
SEQRES 13 A 178 CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN VAL PHE
SEQRES 14 A 178 ASP GLU ALA ILE LEU ALA ALA LEU GLU
SEQRES 1 B 32 ALA SER LYS SER ASN LEU VAL ILE SER ASP PRO ILE PRO
SEQRES 2 B 32 GLY ALA LYS PRO LEU PRO VAL PRO PRO GLU LEU ALA PRO
SEQRES 3 B 32 PHE VAL GLY ARG MET SER
HET GNP A 201 40
HET MG A 202 1
HET MG A 203 1
HET PE4 A 204 4
HET PE4 A 205 13
HET PE4 A 206 10
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
HETNAM PE4 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-
HETNAM 2 PE4 ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL
HETSYN PE4 POLYETHYLENE GLYCOL PEG4000
FORMUL 3 GNP C10 H17 N6 O13 P3
FORMUL 4 MG 2(MG 2+)
FORMUL 6 PE4 3(C16 H34 O8)
FORMUL 9 HOH *151(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 GLN A 61 ASP A 65 5 5
HELIX 3 3 LEU A 67 TYR A 72 5 6
HELIX 4 4 SER A 86 LYS A 96 1 11
HELIX 5 5 LYS A 96 CYS A 105 1 10
HELIX 6 6 GLN A 116 ARG A 120 5 5
HELIX 7 7 ASP A 122 ASN A 132 1 11
HELIX 8 8 THR A 138 LYS A 150 1 13
HELIX 9 9 GLY A 164 GLU A 178 1 15
HELIX 10 10 PRO B 280 VAL B 287 5 8
SHEET 1 A 6 PHE A 37 ILE A 46 0
SHEET 2 A 6 GLU A 49 THR A 58 -1 O LEU A 53 N VAL A 42
SHEET 3 A 6 THR A 3 GLY A 10 1 N CYS A 6 O GLY A 54
SHEET 4 A 6 VAL A 77 SER A 83 1 O CYS A 81 N VAL A 9
SHEET 5 A 6 PHE A 110 THR A 115 1 O VAL A 113 N VAL A 80
SHEET 6 A 6 TYR A 154 GLU A 156 1 O VAL A 155 N GLY A 114
LINK OG1 THR A 17 MG MG A 202 1555 1555 2.15
LINK OG1 THR A 35 MG MG A 202 1555 1555 2.12
LINK O2G GNP A 201 MG MG A 202 1555 1555 1.96
LINK O1B GNP A 201 MG MG A 202 1555 1555 2.09
LINK MG MG A 202 O HOH A 302 1555 1555 2.03
LINK MG MG A 202 O HOH A 304 1555 1555 2.14
LINK MG MG A 203 O HOH A 341 1555 1555 2.17
LINK MG MG A 203 O HOH A 346 1555 1555 2.09
LINK MG MG A 203 O HOH A 372 1555 1555 2.06
LINK MG MG A 203 O HOH A 384 1555 1555 1.99
LINK MG MG A 203 O HOH A 385 1555 1555 2.02
LINK MG MG A 203 O HOH A 414 1555 1555 2.11
CISPEP 1 GLY B 288 ARG B 289 0 -0.20
SITE 1 AC1 28 VAL A 12 ALA A 13 VAL A 14 GLY A 15
SITE 2 AC1 28 LYS A 16 THR A 17 CYS A 18 PHE A 28
SITE 3 AC1 28 TYR A 32 PRO A 34 THR A 35 GLY A 60
SITE 4 AC1 28 GLN A 116 ASP A 118 LEU A 119 LYS A 128
SITE 5 AC1 28 SER A 158 ALA A 159 LEU A 160 MG A 202
SITE 6 AC1 28 HOH A 302 HOH A 304 HOH A 309 HOH A 333
SITE 7 AC1 28 HOH A 338 HOH A 355 HOH A 364 HOH A 373
SITE 1 AC2 5 THR A 17 THR A 35 GNP A 201 HOH A 302
SITE 2 AC2 5 HOH A 304
SITE 1 AC3 6 HOH A 341 HOH A 346 HOH A 372 HOH A 384
SITE 2 AC3 6 HOH A 385 HOH A 414
SITE 1 AC4 4 VAL A 85 LYS A 128 HOH A 364 HOH A 375
SITE 1 AC5 7 PHE A 90 GLU A 91 LYS A 94 ASP A 148
SITE 2 AC5 7 HOH A 371 HOH A 381 HOH A 382
SITE 1 AC6 4 THR A 24 ASN A 26 PRO B 270 PRO B 272
CRYST1 67.230 67.230 79.750 90.00 90.00 90.00 P 42 21 2 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 0.014874 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014874 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012539 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
