HEADER CELL CYCLE 02-MAR-06 2DFK
TITLE CRYSTAL STRUCTURE OF THE CDC42-COLLYBISTIN II COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COLLYBISTIN II;
COMPND 3 CHAIN: A, C;
COMPND 4 FRAGMENT: RESIDUES 10-411;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: CELL DIVISION CYCLE 42 ISOFORM 1;
COMPND 8 CHAIN: B, D;
COMPND 9 SYNONYM: GTP-BINDING PROTEIN, 25KD; CDC42;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTYB12;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS DH DOMAIN, PH DOMAIN, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.XIANG,E.Y.KIM,J.J.CONNELLY,N.NASSAR,J.KIRSCH,J.WINKING,G.SCHWARZ,
AUTHOR 2 H.SCHINDELIN
REVDAT 4 13-JUL-11 2DFK 1 VERSN
REVDAT 3 24-FEB-09 2DFK 1 VERSN
REVDAT 2 23-MAY-06 2DFK 1 JRNL
REVDAT 1 02-MAY-06 2DFK 0
JRNL AUTH S.XIANG,E.Y.KIM,J.J.CONNELLY,N.NASSAR,J.KIRSCH,J.WINKING,
JRNL AUTH 2 G.SCHWARZ,H.SCHINDELIN
JRNL TITL THE CRYSTAL STRUCTURE OF CDC42 IN COMPLEX WITH COLLYBISTIN
JRNL TITL 2 II, A GEPHYRIN-INTERACTING GUANINE NUCLEOTIDE EXCHANGE
JRNL TITL 3 FACTOR.
JRNL REF J.MOL.BIOL. V. 359 35 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16616186
JRNL DOI 10.1016/J.JMB.2006.03.019
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.67
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 72076
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3782
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4417
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 224
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9002
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 581
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.10000
REMARK 3 B22 (A**2) : 0.44000
REMARK 3 B33 (A**2) : -0.34000
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): 0.213
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.120
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.593
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9247 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 8336 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12448 ; 1.833 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 19465 ; 0.981 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1088 ; 6.631 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1338 ; 0.123 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10114 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1897 ; 0.012 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2029 ; 0.231 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 9566 ; 0.240 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 5644 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 440 ; 0.212 ; 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): 22 ; 0.278 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 86 ; 0.275 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.137 ; 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): 5460 ; 1.070 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8850 ; 2.049 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3787 ; 3.326 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3598 ; 5.520 ; 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 : 6
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 43 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): 40.8202 11.5297 20.8668
REMARK 3 T TENSOR
REMARK 3 T11: 0.2039 T22: 0.2419
REMARK 3 T33: 0.2639 T12: 0.0110
REMARK 3 T13: -0.0118 T23: -0.0087
REMARK 3 L TENSOR
REMARK 3 L11: 0.6897 L22: 1.6748
REMARK 3 L33: 1.3454 L12: -0.0185
REMARK 3 L13: 0.1867 L23: 0.5639
REMARK 3 S TENSOR
REMARK 3 S11: 0.0667 S12: 0.0205 S13: -0.0700
REMARK 3 S21: -0.0065 S22: -0.0598 S23: 0.0363
REMARK 3 S31: -0.1129 S32: -0.0004 S33: -0.0069
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 247 A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 23.7753 22.6372 -13.4878
REMARK 3 T TENSOR
REMARK 3 T11: 0.2738 T22: 0.2451
REMARK 3 T33: 0.1201 T12: 0.1474
REMARK 3 T13: 0.0214 T23: 0.1473
REMARK 3 L TENSOR
REMARK 3 L11: 4.0656 L22: 3.8265
REMARK 3 L33: 5.4229 L12: -0.5002
REMARK 3 L13: 1.5046 L23: -0.9889
REMARK 3 S TENSOR
REMARK 3 S11: -0.0060 S12: -0.4153 S13: -0.2685
REMARK 3 S21: 0.1084 S22: 0.1904 S23: 0.3077
REMARK 3 S31: 0.2125 S32: -0.4546 S33: -0.1844
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 1 B 191
REMARK 3 ORIGIN FOR THE GROUP (A): 54.0935 -0.1561 6.3448
REMARK 3 T TENSOR
REMARK 3 T11: 0.2089 T22: 0.2882
REMARK 3 T33: 0.2910 T12: 0.0361
REMARK 3 T13: 0.0662 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.6118 L22: 2.3947
REMARK 3 L33: 1.5895 L12: -0.0618
REMARK 3 L13: 0.1071 L23: 0.4732
REMARK 3 S TENSOR
REMARK 3 S11: 0.0414 S12: 0.0909 S13: -0.0537
REMARK 3 S21: -0.2885 S22: -0.0391 S23: -0.3384
REMARK 3 S31: -0.0120 S32: 0.2851 S33: -0.0023
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 : C 51 C 246
REMARK 3 ORIGIN FOR THE GROUP (A): 48.7864 -33.6330 36.9794
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.2544
REMARK 3 T33: 0.2778 T12: -0.0257
REMARK 3 T13: -0.0069 T23: 0.0423
REMARK 3 L TENSOR
REMARK 3 L11: 0.8634 L22: 1.3443
REMARK 3 L33: 0.8136 L12: -0.5237
REMARK 3 L13: 0.4092 L23: -0.5183
REMARK 3 S TENSOR
REMARK 3 S11: -0.0268 S12: -0.0516 S13: 0.0152
REMARK 3 S21: 0.0177 S22: 0.0746 S23: -0.0451
REMARK 3 S31: -0.0222 S32: 0.0392 S33: -0.0478
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 247 C 397
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3390 -37.7865 -2.6298
REMARK 3 T TENSOR
REMARK 3 T11: 0.2633 T22: 0.2459
REMARK 3 T33: 0.2255 T12: -0.0058
REMARK 3 T13: 0.0169 T23: -0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 1.1471 L22: 1.7504
REMARK 3 L33: 5.5846 L12: -0.0751
REMARK 3 L13: -0.1765 L23: -1.2230
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: 0.1462 S13: -0.1767
REMARK 3 S21: -0.1826 S22: 0.0022 S23: -0.0812
REMARK 3 S31: 0.5534 S32: -0.0768 S33: -0.0280
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D -2 D 191
REMARK 3 ORIGIN FOR THE GROUP (A): 25.5993 -38.6721 40.5404
REMARK 3 T TENSOR
REMARK 3 T11: 0.2305 T22: 0.2220
REMARK 3 T33: 0.2672 T12: -0.0152
REMARK 3 T13: 0.0132 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 1.6139 L22: 0.9730
REMARK 3 L33: 1.6739 L12: 0.2304
REMARK 3 L13: -0.0380 L23: 0.1007
REMARK 3 S TENSOR
REMARK 3 S11: 0.0221 S12: 0.0264 S13: 0.0455
REMARK 3 S21: 0.0174 S22: -0.0611 S23: 0.1028
REMARK 3 S31: -0.0453 S32: -0.1364 S33: 0.0390
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2DFK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-MAR-06.
REMARK 100 THE RCSB ID CODE IS RCSB025359.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-AUG-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X26C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 72590
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.1
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.52000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1FOE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, POTASSIUM DIHYDROGEN
REMARK 280 PHOSPHATE, NACL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K,
REMARK 280 PH 8.00
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 28.97850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.61000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 73.74950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.61000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.97850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 73.74950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 29180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 3910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 53250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 A 10
REMARK 465 LEU A 11
REMARK 465 TRP A 12
REMARK 465 VAL A 13
REMARK 465 ASN A 14
REMARK 465 GLN A 15
REMARK 465 GLU A 16
REMARK 465 ASP A 17
REMARK 465 GLY A 18
REMARK 465 VAL A 19
REMARK 465 GLU A 20
REMARK 465 GLU A 21
REMARK 465 GLY A 22
REMARK 465 PRO A 23
REMARK 465 SER A 24
REMARK 465 ASP A 25
REMARK 465 VAL A 26
REMARK 465 GLN A 27
REMARK 465 ASN A 28
REMARK 465 GLY A 29
REMARK 465 HIS A 30
REMARK 465 LEU A 31
REMARK 465 ASP A 32
REMARK 465 PRO A 33
REMARK 465 ASN A 34
REMARK 465 SER A 35
REMARK 465 ASP A 36
REMARK 465 GLN A 402
REMARK 465 LYS A 403
REMARK 465 VAL A 404
REMARK 465 THR A 405
REMARK 465 GLN A 406
REMARK 465 ARG A 407
REMARK 465 LYS A 408
REMARK 465 TRP A 409
REMARK 465 HIS A 410
REMARK 465 TYR A 411
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 PRO B 180
REMARK 465 GLU B 181
REMARK 465 PRO B 182
REMARK 465 LYS B 183
REMARK 465 MET C 10
REMARK 465 LEU C 11
REMARK 465 TRP C 12
REMARK 465 VAL C 13
REMARK 465 ASN C 14
REMARK 465 GLN C 15
REMARK 465 GLU C 16
REMARK 465 ASP C 17
REMARK 465 GLY C 18
REMARK 465 VAL C 19
REMARK 465 GLU C 20
REMARK 465 GLU C 21
REMARK 465 GLY C 22
REMARK 465 PRO C 23
REMARK 465 SER C 24
REMARK 465 ASP C 25
REMARK 465 VAL C 26
REMARK 465 GLN C 27
REMARK 465 ASN C 28
REMARK 465 GLY C 29
REMARK 465 HIS C 30
REMARK 465 LEU C 31
REMARK 465 ASP C 32
REMARK 465 PRO C 33
REMARK 465 ASN C 34
REMARK 465 SER C 35
REMARK 465 ASP C 36
REMARK 465 CYS C 37
REMARK 465 LEU C 38
REMARK 465 CYS C 39
REMARK 465 LEU C 40
REMARK 465 GLY C 41
REMARK 465 ARG C 42
REMARK 465 PRO C 43
REMARK 465 LEU C 44
REMARK 465 LYS C 398
REMARK 465 ALA C 399
REMARK 465 SER C 400
REMARK 465 LYS C 401
REMARK 465 GLN C 402
REMARK 465 LYS C 403
REMARK 465 VAL C 404
REMARK 465 THR C 405
REMARK 465 GLN C 406
REMARK 465 ARG C 407
REMARK 465 LYS C 408
REMARK 465 TRP C 409
REMARK 465 HIS C 410
REMARK 465 TYR C 411
REMARK 465 PRO D 180
REMARK 465 GLU D 181
REMARK 465 PRO D 182
REMARK 465 LYS D 183
REMARK 465 LYS D 184
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 OE1 GLN C 106 O HOH C 603 1.73
REMARK 500 O HOH C 429 O HOH C 578 1.79
REMARK 500 NZ LYS C 195 O HOH C 472 1.83
REMARK 500 NE2 GLN C 106 O HOH C 605 2.01
REMARK 500 OE2 GLU C 133 O HOH C 594 2.09
REMARK 500 NZ LYS C 235 OE1 GLU C 239 2.11
REMARK 500 O HOH A 656 O HOH A 729 2.14
REMARK 500 O HOH C 479 O HOH C 567 2.15
REMARK 500 OE2 GLU C 62 O HOH C 605 2.18
REMARK 500 NZ LYS C 235 O HOH C 518 2.19
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 GLU A 202 CD GLU A 202 OE2 0.072
REMARK 500 GLU C 233 CD GLU C 233 OE2 0.086
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 51 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG A 104 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP A 112 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP A 121 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 210 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 LEU A 296 CA - CB - CG ANGL. DEV. = 18.3 DEGREES
REMARK 500 ASP A 314 CB - CG - OD2 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ASP A 316 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 PHE A 331 N - CA - C ANGL. DEV. = 18.4 DEGREES
REMARK 500 ARG C 63 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP C 112 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG C 237 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP C 242 CB - CG - OD2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ASP C 261 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG C 262 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 262 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ASP C 314 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP C 329 CB - CG - OD2 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ARG C 368 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG C 368 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP D 11 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 LEU D 19 CB - CG - CD1 ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP D 38 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP D 76 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP D 118 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP D 122 CB - CG - OD2 ANGL. DEV. = 8.4 DEGREES
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 A 98 30.38 -99.10
REMARK 500 ASP A 121 78.83 -154.39
REMARK 500 SER A 264 17.53 -144.39
REMARK 500 TYR A 279 -0.29 74.92
REMARK 500 HIS A 292 -23.84 86.25
REMARK 500 ASP A 325 153.30 -49.75
REMARK 500 ASP A 330 90.20 -24.55
REMARK 500 PHE A 331 -68.49 15.75
REMARK 500 ASN A 337 71.83 65.71
REMARK 500 GLU A 358 -38.52 -36.33
REMARK 500 ALA A 399 56.72 -92.95
REMARK 500 SER A 400 111.03 49.95
REMARK 500 LYS B 96 -62.05 -129.11
REMARK 500 SER B 185 -48.11 139.95
REMARK 500 LEU B 190 110.30 20.38
REMARK 500 ARG C 83 76.16 -112.64
REMARK 500 ASN C 98 33.93 -97.06
REMARK 500 ASP C 121 80.20 -157.89
REMARK 500 SER C 264 -2.78 -142.26
REMARK 500 HIS C 292 -18.73 82.26
REMARK 500 ASP C 305 -50.09 -29.34
REMARK 500 THR C 346 -117.91 -140.35
REMARK 500 GLU C 347 -15.34 177.96
REMARK 500 SER D -1 -153.96 99.21
REMARK 500 TYR D 32 116.62 -162.82
REMARK 500 ASN D 39 134.65 -38.45
REMARK 500 LYS D 96 -64.46 -105.69
REMARK 500 VAL D 189 -149.60 -122.48
REMARK 500 LEU D 190 170.40 39.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LYS B 184 SER B 185 -149.66
REMARK 500 THR C 346 GLU C 347 -142.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 PHE A 331 19.9 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 647 DISTANCE = 5.23 ANGSTROMS
REMARK 525 HOH A 745 DISTANCE = 5.29 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 606
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FOE RELATED DB: PDB
REMARK 900 RELATED ID: 1KZ7 RELATED DB: PDB
REMARK 900 RELATED ID: 1KZG RELATED DB: PDB
REMARK 900 RELATED ID: 1LB1 RELATED DB: PDB
REMARK 900 RELATED ID: 1KI1 RELATED DB: PDB
REMARK 900 RELATED ID: 1DBH RELATED DB: PDB
DBREF 2DFK A 10 411 UNP Q9QX73 ARHG9_RAT 10 411
DBREF 2DFK C 10 411 UNP Q9QX73 ARHG9_RAT 10 411
DBREF 2DFK B 1 191 UNP P60953 CDC42_HUMAN 1 191
DBREF 2DFK D 1 191 UNP P60953 CDC42_HUMAN 1 191
SEQADV 2DFK GLY B -2 UNP P60953 CLONING ARTIFACT
SEQADV 2DFK SER B -1 UNP P60953 CLONING ARTIFACT
SEQADV 2DFK HIS B 0 UNP P60953 CLONING ARTIFACT
SEQADV 2DFK GLY D -2 UNP P60953 CLONING ARTIFACT
SEQADV 2DFK SER D -1 UNP P60953 CLONING ARTIFACT
SEQADV 2DFK HIS D 0 UNP P60953 CLONING ARTIFACT
SEQRES 1 A 402 MET LEU TRP VAL ASN GLN GLU ASP GLY VAL GLU GLU GLY
SEQRES 2 A 402 PRO SER ASP VAL GLN ASN GLY HIS LEU ASP PRO ASN SER
SEQRES 3 A 402 ASP CYS LEU CYS LEU GLY ARG PRO LEU GLN ASN ARG ASP
SEQRES 4 A 402 GLN MET ARG ALA ASN VAL ILE ASN GLU ILE MET SER THR
SEQRES 5 A 402 GLU ARG HIS TYR ILE LYS HIS LEU LYS ASP ILE CYS GLU
SEQRES 6 A 402 GLY TYR LEU LYS GLN CYS ARG LYS ARG ARG ASP MET PHE
SEQRES 7 A 402 SER ASP GLU GLN LEU LYS VAL ILE PHE GLY ASN ILE GLU
SEQRES 8 A 402 ASP ILE TYR ARG PHE GLN MET GLY PHE VAL ARG ASP LEU
SEQRES 9 A 402 GLU LYS GLN TYR ASN ASN ASP ASP PRO HIS LEU SER GLU
SEQRES 10 A 402 ILE GLY PRO CYS PHE LEU GLU HIS GLN ASP GLY PHE TRP
SEQRES 11 A 402 ILE TYR SER GLU TYR CYS ASN ASN HIS LEU ASP ALA CYS
SEQRES 12 A 402 MET GLU LEU SER LYS LEU MET LYS ASP SER ARG TYR GLN
SEQRES 13 A 402 HIS PHE PHE GLU ALA CYS ARG LEU LEU GLN GLN MET ILE
SEQRES 14 A 402 ASP ILE ALA ILE ASP GLY PHE LEU LEU THR PRO VAL GLN
SEQRES 15 A 402 LYS ILE CYS LYS TYR PRO LEU GLN LEU ALA GLU LEU LEU
SEQRES 16 A 402 LYS TYR THR ALA GLN ASP HIS SER ASP TYR ARG TYR VAL
SEQRES 17 A 402 ALA ALA ALA LEU ALA VAL MET ARG ASN VAL THR GLN GLN
SEQRES 18 A 402 ILE ASN GLU ARG LYS ARG ARG LEU GLU ASN ILE ASP LYS
SEQRES 19 A 402 ILE ALA GLN TRP GLN ALA SER VAL LEU ASP TRP GLU GLY
SEQRES 20 A 402 ASP ASP ILE LEU ASP ARG SER SER GLU LEU ILE TYR THR
SEQRES 21 A 402 GLY GLU MET ALA TRP ILE TYR GLN PRO TYR GLY ARG ASN
SEQRES 22 A 402 GLN GLN ARG VAL PHE PHE LEU PHE ASP HIS GLN MET VAL
SEQRES 23 A 402 LEU CYS LYS LYS ASP LEU ILE ARG ARG ASP ILE LEU TYR
SEQRES 24 A 402 TYR LYS GLY ARG ILE ASP MET ASP LYS TYR GLU VAL ILE
SEQRES 25 A 402 ASP ILE GLU ASP GLY ARG ASP ASP ASP PHE ASN VAL SER
SEQRES 26 A 402 MET LYS ASN ALA PHE LYS LEU HIS ASN LYS GLU THR GLU
SEQRES 27 A 402 GLU VAL HIS LEU PHE PHE ALA LYS LYS LEU GLU GLU LYS
SEQRES 28 A 402 ILE ARG TRP LEU ARG ALA PHE ARG GLU GLU ARG LYS MET
SEQRES 29 A 402 VAL GLN GLU ASP GLU LYS ILE GLY PHE GLU ILE SER GLU
SEQRES 30 A 402 ASN GLN LYS ARG GLN ALA ALA MET THR VAL ARG LYS ALA
SEQRES 31 A 402 SER LYS GLN LYS VAL THR GLN ARG LYS TRP HIS TYR
SEQRES 1 B 194 GLY SER HIS MET GLN THR ILE LYS CYS VAL VAL VAL GLY
SEQRES 2 B 194 ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR
SEQRES 3 B 194 THR THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL
SEQRES 4 B 194 PHE ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU
SEQRES 5 B 194 PRO TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU
SEQRES 6 B 194 ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR
SEQRES 7 B 194 ASP VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER
SEQRES 8 B 194 SER PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE
SEQRES 9 B 194 THR HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY
SEQRES 10 B 194 THR GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU
SEQRES 11 B 194 LYS LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU
SEQRES 12 B 194 THR ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS
SEQRES 13 B 194 TYR VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS
SEQRES 14 B 194 ASN VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO
SEQRES 15 B 194 PRO GLU PRO LYS LYS SER ARG ARG CYS VAL LEU LEU
SEQRES 1 C 402 MET LEU TRP VAL ASN GLN GLU ASP GLY VAL GLU GLU GLY
SEQRES 2 C 402 PRO SER ASP VAL GLN ASN GLY HIS LEU ASP PRO ASN SER
SEQRES 3 C 402 ASP CYS LEU CYS LEU GLY ARG PRO LEU GLN ASN ARG ASP
SEQRES 4 C 402 GLN MET ARG ALA ASN VAL ILE ASN GLU ILE MET SER THR
SEQRES 5 C 402 GLU ARG HIS TYR ILE LYS HIS LEU LYS ASP ILE CYS GLU
SEQRES 6 C 402 GLY TYR LEU LYS GLN CYS ARG LYS ARG ARG ASP MET PHE
SEQRES 7 C 402 SER ASP GLU GLN LEU LYS VAL ILE PHE GLY ASN ILE GLU
SEQRES 8 C 402 ASP ILE TYR ARG PHE GLN MET GLY PHE VAL ARG ASP LEU
SEQRES 9 C 402 GLU LYS GLN TYR ASN ASN ASP ASP PRO HIS LEU SER GLU
SEQRES 10 C 402 ILE GLY PRO CYS PHE LEU GLU HIS GLN ASP GLY PHE TRP
SEQRES 11 C 402 ILE TYR SER GLU TYR CYS ASN ASN HIS LEU ASP ALA CYS
SEQRES 12 C 402 MET GLU LEU SER LYS LEU MET LYS ASP SER ARG TYR GLN
SEQRES 13 C 402 HIS PHE PHE GLU ALA CYS ARG LEU LEU GLN GLN MET ILE
SEQRES 14 C 402 ASP ILE ALA ILE ASP GLY PHE LEU LEU THR PRO VAL GLN
SEQRES 15 C 402 LYS ILE CYS LYS TYR PRO LEU GLN LEU ALA GLU LEU LEU
SEQRES 16 C 402 LYS TYR THR ALA GLN ASP HIS SER ASP TYR ARG TYR VAL
SEQRES 17 C 402 ALA ALA ALA LEU ALA VAL MET ARG ASN VAL THR GLN GLN
SEQRES 18 C 402 ILE ASN GLU ARG LYS ARG ARG LEU GLU ASN ILE ASP LYS
SEQRES 19 C 402 ILE ALA GLN TRP GLN ALA SER VAL LEU ASP TRP GLU GLY
SEQRES 20 C 402 ASP ASP ILE LEU ASP ARG SER SER GLU LEU ILE TYR THR
SEQRES 21 C 402 GLY GLU MET ALA TRP ILE TYR GLN PRO TYR GLY ARG ASN
SEQRES 22 C 402 GLN GLN ARG VAL PHE PHE LEU PHE ASP HIS GLN MET VAL
SEQRES 23 C 402 LEU CYS LYS LYS ASP LEU ILE ARG ARG ASP ILE LEU TYR
SEQRES 24 C 402 TYR LYS GLY ARG ILE ASP MET ASP LYS TYR GLU VAL ILE
SEQRES 25 C 402 ASP ILE GLU ASP GLY ARG ASP ASP ASP PHE ASN VAL SER
SEQRES 26 C 402 MET LYS ASN ALA PHE LYS LEU HIS ASN LYS GLU THR GLU
SEQRES 27 C 402 GLU VAL HIS LEU PHE PHE ALA LYS LYS LEU GLU GLU LYS
SEQRES 28 C 402 ILE ARG TRP LEU ARG ALA PHE ARG GLU GLU ARG LYS MET
SEQRES 29 C 402 VAL GLN GLU ASP GLU LYS ILE GLY PHE GLU ILE SER GLU
SEQRES 30 C 402 ASN GLN LYS ARG GLN ALA ALA MET THR VAL ARG LYS ALA
SEQRES 31 C 402 SER LYS GLN LYS VAL THR GLN ARG LYS TRP HIS TYR
SEQRES 1 D 194 GLY SER HIS MET GLN THR ILE LYS CYS VAL VAL VAL GLY
SEQRES 2 D 194 ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR
SEQRES 3 D 194 THR THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL
SEQRES 4 D 194 PHE ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU
SEQRES 5 D 194 PRO TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU
SEQRES 6 D 194 ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR
SEQRES 7 D 194 ASP VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER
SEQRES 8 D 194 SER PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE
SEQRES 9 D 194 THR HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY
SEQRES 10 D 194 THR GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU
SEQRES 11 D 194 LYS LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU
SEQRES 12 D 194 THR ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS
SEQRES 13 D 194 TYR VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS
SEQRES 14 D 194 ASN VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO
SEQRES 15 D 194 PRO GLU PRO LYS LYS SER ARG ARG CYS VAL LEU LEU
HET SO4 D 701 5
HET SO4 B 702 5
HET GOL A 601 6
HET GOL A 602 6
HET GOL B 603 6
HET GOL D 604 6
HET GOL D 605 6
HET GOL A 606 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 GOL 6(C3 H8 O3)
FORMUL 13 HOH *581(H2 O)
HELIX 1 1 ASN A 46 TYR A 76 1 31
HELIX 2 2 TYR A 76 ARG A 83 1 8
HELIX 3 3 SER A 88 GLY A 97 1 10
HELIX 4 4 ASN A 98 TYR A 117 1 20
HELIX 5 5 ASP A 121 SER A 125 5 5
HELIX 6 6 ILE A 127 HIS A 134 1 8
HELIX 7 7 ASP A 136 PHE A 138 5 3
HELIX 8 8 TRP A 139 MET A 159 1 21
HELIX 9 9 ASP A 161 GLN A 175 1 15
HELIX 10 10 ALA A 181 LEU A 187 1 7
HELIX 11 11 LEU A 187 TYR A 206 1 20
HELIX 12 12 ASP A 213 ASN A 240 1 28
HELIX 13 13 ASN A 240 VAL A 251 1 12
HELIX 14 14 ASP A 258 ARG A 262 5 5
HELIX 15 15 LYS A 356 GLY A 381 1 26
HELIX 16 16 SER A 385 ALA A 399 1 15
HELIX 17 17 GLY B 15 THR B 25 1 11
HELIX 18 18 LEU B 67 TYR B 72 5 6
HELIX 19 19 SER B 86 LYS B 96 1 11
HELIX 20 20 LYS B 96 CYS B 105 1 10
HELIX 21 21 GLN B 116 ASP B 121 5 6
HELIX 22 22 ASP B 122 ASN B 132 1 11
HELIX 23 23 THR B 138 LEU B 149 1 12
HELIX 24 24 GLY B 164 GLU B 178 1 15
HELIX 25 25 ASN C 46 GLY C 75 1 30
HELIX 26 26 GLY C 75 LYS C 82 1 8
HELIX 27 27 SER C 88 GLY C 97 1 10
HELIX 28 28 ASN C 98 TYR C 117 1 20
HELIX 29 29 ASP C 121 SER C 125 5 5
HELIX 30 30 ILE C 127 HIS C 134 1 8
HELIX 31 31 GLN C 135 PHE C 138 5 4
HELIX 32 32 TRP C 139 MET C 159 1 21
HELIX 33 33 ASP C 161 GLN C 175 1 15
HELIX 34 34 ALA C 181 LEU C 187 1 7
HELIX 35 35 LEU C 187 TYR C 206 1 20
HELIX 36 36 ASP C 213 ASN C 240 1 28
HELIX 37 37 ASN C 240 VAL C 251 1 12
HELIX 38 38 ASP C 258 ARG C 262 5 5
HELIX 39 39 LYS C 356 GLY C 381 1 26
HELIX 40 40 SER C 385 MET C 394 1 10
HELIX 41 41 GLY D 15 ASN D 26 1 12
HELIX 42 42 LEU D 67 TYR D 72 5 6
HELIX 43 43 SER D 86 LYS D 96 1 11
HELIX 44 44 LYS D 96 CYS D 105 1 10
HELIX 45 45 GLN D 116 ASP D 121 5 6
HELIX 46 46 ASP D 122 ASN D 132 1 11
HELIX 47 47 THR D 138 LYS D 150 1 13
HELIX 48 48 GLY D 164 LEU D 177 1 14
SHEET 1 A 7 LEU A 307 ASP A 314 0
SHEET 2 A 7 GLN A 293 LYS A 299 -1 N MET A 294 O ILE A 313
SHEET 3 A 7 GLN A 283 PHE A 290 -1 N VAL A 286 O CYS A 297
SHEET 4 A 7 LEU A 266 ILE A 275 -1 N ILE A 267 O LEU A 289
SHEET 5 A 7 VAL A 349 PHE A 353 -1 O LEU A 351 N ILE A 275
SHEET 6 A 7 ALA A 338 ASN A 343 -1 N PHE A 339 O PHE A 352
SHEET 7 A 7 TYR A 318 ASP A 322 -1 N ILE A 321 O LYS A 340
SHEET 1 B 2 GLY A 326 ARG A 327 0
SHEET 2 B 2 SER A 334 MET A 335 -1 O MET A 335 N GLY A 326
SHEET 1 C 6 TYR B 40 ILE B 46 0
SHEET 2 C 6 GLU B 49 PHE B 56 -1 O LEU B 53 N VAL B 42
SHEET 3 C 6 THR B 3 GLY B 10 1 N ILE B 4 O GLY B 54
SHEET 4 C 6 VAL B 77 SER B 83 1 O CYS B 81 N VAL B 9
SHEET 5 C 6 PHE B 110 THR B 115 1 O LEU B 111 N VAL B 80
SHEET 6 C 6 TYR B 154 GLU B 156 1 O VAL B 155 N GLY B 114
SHEET 1 D 7 LEU C 307 ASP C 314 0
SHEET 2 D 7 GLN C 293 LYS C 299 -1 N LEU C 296 O GLY C 311
SHEET 3 D 7 GLN C 283 PHE C 290 -1 N PHE C 290 O GLN C 293
SHEET 4 D 7 LEU C 266 ILE C 275 -1 N GLY C 270 O PHE C 287
SHEET 5 D 7 VAL C 349 PHE C 353 -1 O PHE C 353 N ALA C 273
SHEET 6 D 7 ALA C 338 ASN C 343 -1 N PHE C 339 O PHE C 352
SHEET 7 D 7 TYR C 318 ASP C 322 -1 N GLU C 319 O HIS C 342
SHEET 1 E 2 GLY C 326 ARG C 327 0
SHEET 2 E 2 SER C 334 MET C 335 -1 O MET C 335 N GLY C 326
SHEET 1 F 6 TYR D 40 ILE D 46 0
SHEET 2 F 6 GLU D 49 PHE D 56 -1 O LEU D 53 N VAL D 42
SHEET 3 F 6 ILE D 4 VAL D 9 1 N CYS D 6 O GLY D 54
SHEET 4 F 6 VAL D 77 SER D 83 1 O LEU D 79 N VAL D 9
SHEET 5 F 6 PHE D 110 THR D 115 1 O VAL D 113 N VAL D 80
SHEET 6 F 6 TYR D 154 GLU D 156 1 O VAL D 155 N LEU D 112
SSBOND 1 CYS B 105 CYS B 188 1555 1555 2.11
SSBOND 2 CYS D 105 CYS D 188 1555 1555 2.11
CISPEP 1 ASP A 330 PHE A 331 0 3.06
SITE 1 AC1 11 ASP D 11 GLY D 12 ALA D 13 VAL D 14
SITE 2 AC1 11 GLY D 15 LYS D 16 THR D 17 ALA D 59
SITE 3 AC1 11 HOH D 731 HOH D 746 HOH D 777
SITE 1 AC2 10 ASP B 11 GLY B 12 ALA B 13 VAL B 14
SITE 2 AC2 10 GLY B 15 LYS B 16 THR B 17 GLU B 62
SITE 3 AC2 10 HOH B 715 HOH B 733
SITE 1 AC3 4 ARG A 104 LYS D 153 GLU D 171 GLU D 178
SITE 1 AC4 5 ARG A 215 TYR A 216 HOH A 769 MET B 45
SITE 2 AC4 5 GLY B 48
SITE 1 AC5 5 SER B 22 TYR B 23 THR B 25 ASN B 26
SITE 2 AC5 5 GLN B 162
SITE 1 AC6 2 THR D 24 THR D 25
SITE 1 AC7 5 THR D 24 PHE D 37 ASP D 38 TYR D 40
SITE 2 AC7 5 HOH D 784
SITE 1 AC8 6 LYS A 115 GLN A 116 TYR A 117 ASN A 118
SITE 2 AC8 6 HOH A 655 HOH A 660
CRYST1 57.957 147.499 167.220 90.00 90.00 90.00 P 21 21 21 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 0.017254 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006780 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005980 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
