HEADER SIGNALING PROTEIN,CELL CYCLE 22-NOV-06 2NZ8
TITLE N-TERMINAL DHPH CASSETTE OF TRIO IN COMPLEX WITH NUCLEOTIDE-
TITLE 2 FREE RAC1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1
COMPND 3 ISOFORM RAC1;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: SOLUBLE PART (RESIDUES 1-177);
COMPND 6 SYNONYM: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1; P21-
COMPND 7 RAC1; RAS-LIKE PROTEIN TC25;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: TRIPLE FUNCTIONAL DOMAIN PROTEIN;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: N-TERMINAL DH/PH CASSETTE (RESIDUES 1226-1535);
COMPND 13 SYNONYM: PTPRF-INTERACTING PROTEIN;
COMPND 14 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: RAC1;
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: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: TRIO;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PPROEX-HTA
KEYWDS TRIO; RAC1; DBL-FAMILY GEF; RHO-FAMILY GTPASE; DH/PH
KEYWDS 2 CASSETTE, SIGNALING PROTEIN,CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.K.CHHATRIWALA,L.BETTS,D.K.WORTHYLAKE,J.SONDEK
REVDAT 3 24-FEB-09 2NZ8 1 VERSN
REVDAT 2 05-JUN-07 2NZ8 1 JRNL
REVDAT 1 10-APR-07 2NZ8 0
JRNL AUTH M.K.CHHATRIWALA,L.BETTS,D.K.WORTHYLAKE,J.SONDEK
JRNL TITL THE DH AND PH DOMAINS OF TRIO COORDINATELY ENGAGE
JRNL TITL 2 RHO GTPASES FOR THEIR EFFICIENT ACTIVATION
JRNL REF J.MOL.BIOL. V. 368 1307 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17391702
JRNL DOI 10.1016/J.JMB.2007.02.060
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 38900
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) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1968
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2718
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.89
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.3070
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3663
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 242
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : -0.21000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.565
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.939
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3737 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5043 ; 1.138 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 451 ; 5.078 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 170 ;34.698 ;24.824
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 696 ;15.149 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;16.585 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 564 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2767 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1729 ; 0.190 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2539 ; 0.300 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 251 ; 0.148 ; 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): 42 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.094 ; 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): 2359 ; 0.520 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3679 ; 0.848 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1584 ; 1.260 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1364 ; 1.913 ; 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 1 A 177
REMARK 3 ORIGIN FOR THE GROUP (A): 48.0850 32.1290 -7.1214
REMARK 3 T TENSOR
REMARK 3 T11: -0.1328 T22: -0.1902
REMARK 3 T33: -0.1971 T12: -0.0171
REMARK 3 T13: -0.0041 T23: 0.0069
REMARK 3 L TENSOR
REMARK 3 L11: 1.7443 L22: 2.4427
REMARK 3 L33: 4.6849 L12: 0.1444
REMARK 3 L13: -0.8049 L23: 0.2378
REMARK 3 S TENSOR
REMARK 3 S11: -0.0496 S12: 0.0714 S13: -0.0816
REMARK 3 S21: -0.3355 S22: 0.0723 S23: -0.1213
REMARK 3 S31: 0.3195 S32: 0.0851 S33: -0.0227
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 : B 1231 B 1411
REMARK 3 ORIGIN FOR THE GROUP (A): 44.3108 41.1008 15.5037
REMARK 3 T TENSOR
REMARK 3 T11: -0.1602 T22: -0.1770
REMARK 3 T33: -0.2421 T12: -0.0394
REMARK 3 T13: 0.0117 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 2.5060 L22: 3.5037
REMARK 3 L33: 1.8732 L12: -0.0472
REMARK 3 L13: -0.2673 L23: -0.2385
REMARK 3 S TENSOR
REMARK 3 S11: 0.0028 S12: -0.1939 S13: 0.0513
REMARK 3 S21: 0.3334 S22: 0.0504 S23: -0.0188
REMARK 3 S31: 0.0679 S32: 0.0635 S33: -0.0531
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1412 B 1417
REMARK 3 RESIDUE RANGE : B 1423 B 1434
REMARK 3 RESIDUE RANGE : B 1449 B 1497
REMARK 3 RESIDUE RANGE : B 1505 B 1535
REMARK 3 ORIGIN FOR THE GROUP (A): 32.2525 11.8642 14.9497
REMARK 3 T TENSOR
REMARK 3 T11: 0.2877 T22: -0.0272
REMARK 3 T33: 1.2075 T12: -0.2386
REMARK 3 T13: -0.6478 T23: 0.3116
REMARK 3 L TENSOR
REMARK 3 L11: 30.0993 L22: 12.5573
REMARK 3 L33: 14.3880 L12: -1.8593
REMARK 3 L13: 13.3474 L23: -1.6695
REMARK 3 S TENSOR
REMARK 3 S11: 2.9268 S12: -1.1897 S13: -5.8947
REMARK 3 S21: 0.3162 S22: -0.0338 S23: -0.0182
REMARK 3 S31: 2.5485 S32: -0.6843 S33: -2.8930
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 2000 B 2241
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9646 37.1742 4.9849
REMARK 3 T TENSOR
REMARK 3 T11: -0.0604 T22: -0.0833
REMARK 3 T33: -0.0568 T12: -0.0114
REMARK 3 T13: -0.0088 T23: 0.0335
REMARK 3 L TENSOR
REMARK 3 L11: 1.1617 L22: 2.3093
REMARK 3 L33: 2.3013 L12: -0.2572
REMARK 3 L13: -0.4692 L23: 0.5297
REMARK 3 S TENSOR
REMARK 3 S11: -0.0079 S12: -0.0112 S13: 0.0247
REMARK 3 S21: -0.0661 S22: 0.0337 S23: 0.1927
REMARK 3 S31: 0.0196 S32: -0.0923 S33: -0.0258
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2NZ8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-06.
REMARK 100 THE RCSB ID CODE IS RCSB040486.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0712
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI (220)
REMARK 200 CRYOGENICALLY COOLED
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39416
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: RESIDUES 1231-1390 OF PDB ENTRY 1NTY AND
REMARK 200 RESIDUES 1-177 OF PDB ENTRY 1FOE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CACODYLATE PH 5.5 TO
REMARK 280 6.5, 14 TO 18% (W/V) PEG 8000, AND 300-500 MM CALCIUM ACETATE,
REMARK 280 PH 6.0, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 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 -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 48.74600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.27900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 48.74600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.27900
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 300 REMARK: THERE IS ONE BIOLOGICAL UNIT IN EACH ASSYMETRIC UNIT
REMARK 300 (COMPLEX BETWEEN RAC1 AND TRIO DH/PH)
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: 2590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 A2175 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2221 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 GLY B 1223
REMARK 465 ALA B 1224
REMARK 465 MET B 1225
REMARK 465 GLU B 1226
REMARK 465 LYS B 1227
REMARK 465 ARG B 1228
REMARK 465 LYS B 1229
REMARK 465 SER B 1230
REMARK 465 ASP B 1418
REMARK 465 GLU B 1419
REMARK 465 ASN B 1420
REMARK 465 ILE B 1421
REMARK 465 GLU B 1422
REMARK 465 VAL B 1435
REMARK 465 TRP B 1436
REMARK 465 ASP B 1437
REMARK 465 PRO B 1438
REMARK 465 LYS B 1439
REMARK 465 THR B 1440
REMARK 465 LEU B 1441
REMARK 465 ILE B 1442
REMARK 465 ARG B 1443
REMARK 465 LYS B 1444
REMARK 465 GLY B 1445
REMARK 465 ARG B 1446
REMARK 465 GLU B 1447
REMARK 465 ARG B 1448
REMARK 465 LEU B 1498
REMARK 465 TRP B 1499
REMARK 465 VAL B 1500
REMARK 465 GLY B 1501
REMARK 465 ARG B 1502
REMARK 465 THR B 1503
REMARK 465 PRO B 1504
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 NH2 ARG A 68 O HOH A 2133 2.04
REMARK 500 OD2 ASP A 38 O HOH A 2199 2.06
REMARK 500 OD1 ASP B 1251 O HOH B 2156 2.13
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 GLN B1434 C GLN B1434 O 0.132
REMARK 500 GLU B1482 CD GLU B1482 OE1 0.144
REMARK 500 GLU B1482 CD GLU B1482 OE2 0.144
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 PRO A 29 94.05 -66.72
REMARK 500 LYS A 96 -58.66 -127.02
REMARK 500 THR B1258 -80.44 -111.94
REMARK 500 ASN B1284 35.50 -96.34
REMARK 500 GLU B1390 -0.18 82.84
REMARK 500 SER B1481 -69.90 -164.21
REMARK 500 VAL B1489 -107.31 -117.93
REMARK 500 PRO B1493 172.81 -56.48
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2NZ8 A 1 177 UNP P63000 RAC1_HUMAN 1 177
DBREF 2NZ8 B 1226 1535 UNP O75962 TRIO_HUMAN 1226 1535
SEQADV 2NZ8 GLY B 1223 UNP O75962 CLONING ARTIFACT
SEQADV 2NZ8 ALA B 1224 UNP O75962 CLONING ARTIFACT
SEQADV 2NZ8 MET B 1225 UNP O75962 INITIATING METHIONINE
SEQRES 1 A 177 MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 177 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 177 ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN
SEQRES 4 A 177 TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN
SEQRES 5 A 177 LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 177 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 177 LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU
SEQRES 8 A 177 ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS
SEQRES 9 A 177 CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU
SEQRES 10 A 177 ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS
SEQRES 11 A 177 GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU
SEQRES 12 A 177 ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU
SEQRES 13 A 177 CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE
SEQRES 14 A 177 ASP GLU ALA ILE ARG ALA VAL LEU
SEQRES 1 B 313 GLY ALA MET GLU LYS ARG LYS SER ALA ARG ARG LYS GLU
SEQRES 2 B 313 PHE ILE MET ALA GLU LEU ILE GLN THR GLU LYS ALA TYR
SEQRES 3 B 313 VAL ARG ASP LEU ARG GLU CYS MET ASP THR TYR LEU TRP
SEQRES 4 B 313 GLU MET THR SER GLY VAL GLU GLU ILE PRO PRO GLY ILE
SEQRES 5 B 313 VAL ASN LYS GLU LEU ILE ILE PHE GLY ASN MET GLN GLU
SEQRES 6 B 313 ILE TYR GLU PHE HIS ASN ASN ILE PHE LEU LYS GLU LEU
SEQRES 7 B 313 GLU LYS TYR GLU GLN LEU PRO GLU ASP VAL GLY HIS CYS
SEQRES 8 B 313 PHE VAL THR TRP ALA ASP LYS PHE GLN MET TYR VAL THR
SEQRES 9 B 313 TYR CYS LYS ASN LYS PRO ASP SER THR GLN LEU ILE LEU
SEQRES 10 B 313 GLU HIS ALA GLY SER TYR PHE ASP GLU ILE GLN GLN ARG
SEQRES 11 B 313 HIS GLY LEU ALA ASN SER ILE SER SER TYR LEU ILE LYS
SEQRES 12 B 313 PRO VAL GLN ARG ILE THR LYS TYR GLN LEU LEU LEU LYS
SEQRES 13 B 313 GLU LEU LEU THR CYS CYS GLU GLU GLY LYS GLY GLU ILE
SEQRES 14 B 313 LYS ASP GLY LEU GLU VAL MET LEU SER VAL PRO LYS ARG
SEQRES 15 B 313 ALA ASN ASP ALA MET HIS LEU SER MET LEU GLU GLY PHE
SEQRES 16 B 313 ASP GLU ASN ILE GLU SER GLN GLY GLU LEU ILE LEU GLN
SEQRES 17 B 313 GLU SER PHE GLN VAL TRP ASP PRO LYS THR LEU ILE ARG
SEQRES 18 B 313 LYS GLY ARG GLU ARG HIS LEU PHE LEU PHE GLU MET SER
SEQRES 19 B 313 LEU VAL PHE SER LYS GLU VAL LYS ASP SER SER GLY ARG
SEQRES 20 B 313 SER LYS TYR LEU TYR LYS SER LYS LEU PHE THR SER GLU
SEQRES 21 B 313 LEU GLY VAL THR GLU HIS VAL GLU GLY ASP PRO CYS LYS
SEQRES 22 B 313 PHE ALA LEU TRP VAL GLY ARG THR PRO THR SER ASP ASN
SEQRES 23 B 313 LYS ILE VAL LEU LYS ALA SER SER ILE GLU ASN LYS GLN
SEQRES 24 B 313 ASP TRP ILE LYS HIS ILE ARG GLU VAL ILE GLN GLU ARG
SEQRES 25 B 313 THR
FORMUL 3 HOH *242(H2 O)
HELIX 1 1 GLY A 12 VAL A 14 5 3
HELIX 2 2 GLY A 15 THR A 25 1 11
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 LYS A 116 ARG A 120 5 5
HELIX 7 7 ASP A 122 GLU A 131 1 10
HELIX 8 8 THR A 138 GLY A 150 1 13
HELIX 9 9 GLY A 164 LEU A 177 1 14
HELIX 10 10 ALA B 1231 THR B 1258 1 28
HELIX 11 11 THR B 1258 GLY B 1266 1 9
HELIX 12 12 LYS B 1277 GLY B 1283 1 7
HELIX 13 13 ASN B 1284 ILE B 1295 1 12
HELIX 14 14 ILE B 1295 TYR B 1303 1 9
HELIX 15 15 LEU B 1306 ASP B 1309 5 4
HELIX 16 16 VAL B 1310 TRP B 1317 1 8
HELIX 17 17 ALA B 1318 PHE B 1321 5 4
HELIX 18 18 GLN B 1322 ALA B 1342 1 21
HELIX 19 19 SER B 1344 GLY B 1354 1 11
HELIX 20 20 SER B 1358 CYS B 1383 1 26
HELIX 21 21 GLU B 1390 SER B 1412 1 23
HELIX 22 22 SER B 1516 GLU B 1533 1 18
SHEET 1 A 6 TYR A 40 VAL A 46 0
SHEET 2 A 6 LYS A 49 TRP A 56 -1 O VAL A 51 N VAL A 44
SHEET 3 A 6 ALA A 3 GLY A 10 1 N ILE A 4 O ASN A 52
SHEET 4 A 6 VAL A 77 SER A 83 1 O LEU A 79 N VAL A 9
SHEET 5 A 6 ILE A 110 THR A 115 1 O THR A 115 N PHE A 82
SHEET 6 A 6 LYS A 153 GLU A 156 1 O LEU A 155 N GLY A 114
SHEET 1 B 5 LEU B1414 GLU B1415 0
SHEET 2 B 5 SER B1470 LEU B1478 1 O TYR B1472 N GLU B1415
SHEET 3 B 5 LEU B1457 LYS B1464 -1 N LYS B1461 O LEU B1473
SHEET 4 B 5 LEU B1450 PHE B1453 -1 N PHE B1451 O VAL B1458
SHEET 5 B 5 LEU B1427 GLU B1431 -1 N GLU B1431 O LEU B1450
SHEET 1 C 2 LYS B1495 PHE B1496 0
SHEET 2 C 2 LEU B1512 LYS B1513 -1 O LEU B1512 N PHE B1496
CISPEP 1 SER B 1423 GLN B 1424 0 0.68
CRYST1 97.492 108.558 53.416 90.00 90.00 90.00 P 21 21 2 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 0.010257 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009212 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018721 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
