HEADER CELL CYCLE 02-JUL-09 2WMN
TITLE STRUCTURE OF THE COMPLEX BETWEEN DOCK9 AND CDC42-GDP.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DEDICATOR OF CYTOKINESIS PROTEIN 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DHR2 DOMAIN, RESIDUES 1605-1652,1676-2053;
COMPND 5 SYNONYM: CDC42 GUANINE NUCLEOTIDE EXCHANGE FACTOR ZIZIMIN-1, DOCK9;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CELL DIVISION CONTROL PROTEIN 42 HOMOLOG;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: G25K GTP-BINDING PROTEIN, CDC42;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CELL CYCLE, ALTERNATIVE SPLICING, METHYLATION, PRENYLATION,
KEYWDS 2 LIPOPROTEIN, COILED COIL, GEFS, DOCK9, CDC42, MEMBRANE, NUCLEOTIDE,
KEYWDS 3 PHOSPHOPROTEIN, NUCLEOTIDE-BINDING, GTP-BINDING, POLYMORPHISM, CELL
KEYWDS 4 MEMBRANE, GUANINE-NUCLEOTIDE RELEASING FACTOR
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YANG,S.M.ROE,D.BARFORD
REVDAT 2 13-DEC-23 2WMN 1 REMARK
REVDAT 1 22-SEP-09 2WMN 0
JRNL AUTH J.YANG,Z.ZHANG,S.M.ROE,C.J.MARSHALL,D.BARFORD
JRNL TITL ACTIVATION OF RHO GTPASES BY DOCK EXCHANGE FACTORS IS
JRNL TITL 2 MEDIATED BY A NUCLEOTIDE SENSOR.
JRNL REF SCIENCE V. 325 1398 2009
JRNL REFN ISSN 0036-8075
JRNL PMID 19745154
JRNL DOI 10.1126/SCIENCE.1174468
REMARK 2
REMARK 2 RESOLUTION. 2.39 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.45
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 28748
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1448
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 37.4583 - 5.1477 0.96 2933 147 0.2013 0.2477
REMARK 3 2 5.1477 - 4.0875 0.99 2874 155 0.1919 0.2318
REMARK 3 3 4.0875 - 3.5713 1.00 2845 157 0.2064 0.2964
REMARK 3 4 3.5713 - 3.2449 1.00 2851 155 0.2118 0.2679
REMARK 3 5 3.2449 - 3.0125 1.00 2832 143 0.2238 0.2952
REMARK 3 6 3.0125 - 2.8349 0.92 2627 137 0.2303 0.2857
REMARK 3 7 2.8349 - 2.6930 0.92 2592 126 0.2340 0.2497
REMARK 3 8 2.6930 - 2.5758 0.93 2591 159 0.2329 0.3247
REMARK 3 9 2.5758 - 2.4767 0.93 2631 142 0.2343 0.2954
REMARK 3 10 2.4767 - 2.3912 0.90 2524 127 0.2661 0.3253
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 : 0.34
REMARK 3 B_SOL : 54.18
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.45710
REMARK 3 B22 (A**2) : -13.43040
REMARK 3 B33 (A**2) : 10.97340
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 : 0.009 4667
REMARK 3 ANGLE : 1.120 6335
REMARK 3 CHIRALITY : 0.073 722
REMARK 3 PLANARITY : 0.004 812
REMARK 3 DIHEDRAL : 17.271 1678
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2WMN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1290040314.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.2822
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28789
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 47.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: PDB ENTRY 2WM9
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0
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 46.52500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.23600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.52500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.23600
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.3 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 BIOMT1 2 -1.000000 0.000000 0.000000 -93.05000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 88.47200
REMARK 350 BIOMT3 2 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 A2020 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 LYS A 1
REMARK 465 SER A 2
REMARK 465 TYR A 3
REMARK 465 ALA A 4
REMARK 465 SER A 70
REMARK 465 MET A 71
REMARK 465 MET A 72
REMARK 465 GLU A 73
REMARK 465 ASP A 74
REMARK 465 VAL A 75
REMARK 465 GLY A 76
REMARK 465 MET A 77
REMARK 465 GLN A 78
REMARK 465 ASP A 79
REMARK 465 VAL A 80
REMARK 465 THR A 264
REMARK 465 GLY A 265
REMARK 465 LYS A 266
REMARK 465 THR A 362
REMARK 465 ASN A 363
REMARK 465 THR A 364
REMARK 465 LYS A 365
REMARK 465 ARG A 366
REMARK 465 TYR A 367
REMARK 465 GLY A 428
REMARK 465 GLU B 178
REMARK 465 PRO B 179
REMARK 465 PRO B 180
REMARK 465 GLU B 181
REMARK 465 PRO B 182
REMARK 465 LYS B 183
REMARK 465 LYS B 184
REMARK 465 SER B 185
REMARK 465 ARG B 186
REMARK 465 ARG B 187
REMARK 465 CYS B 188
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 A 5 OG
REMARK 470 GLU A 8 CG CD OE1 OE2
REMARK 470 LYS A 23 CE NZ
REMARK 470 HIS A 81 CG ND1 CD2 CE1 NE2
REMARK 470 GLN A 163 CG CD OE1 NE2
REMARK 470 PHE A 165 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 172 CG CD CE NZ
REMARK 470 LYS A 193 CG CD CE NZ
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 LYS A 205 CD CE NZ
REMARK 470 LYS A 212 CG CD CE NZ
REMARK 470 LYS A 216 CG CD CE NZ
REMARK 470 LYS A 221 CG CD CE NZ
REMARK 470 GLU A 236 CG CD OE1 OE2
REMARK 470 GLN A 240 CG CD OE1 NE2
REMARK 470 GLU A 329 CG CD OE1 OE2
REMARK 470 GLN A 346 CG CD OE1 NE2
REMARK 470 ASP A 361 CG OD1 OD2
REMARK 470 LYS A 373 CG CD CE NZ
REMARK 470 GLU A 377 CG CD OE1 OE2
REMARK 470 GLU A 384 CG CD OE1 OE2
REMARK 470 GLN A 388 CG CD OE1 NE2
REMARK 470 ARG A 395 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 398 CE NZ
REMARK 470 GLU A 399 CG CD OE1 OE2
REMARK 470 LEU A 402 CG CD1 CD2
REMARK 470 LYS A 409 CG CD CE NZ
REMARK 470 GLU A 414 CG CD OE1 OE2
REMARK 470 LYS A 417 CG CD CE NZ
REMARK 470 GLN A 426 CG CD OE1 NE2
REMARK 470 LEU A 427 CG CD1 CD2
REMARK 470 SER B -1 OG
REMARK 470 HIS B 0 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 66 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 91 CG CD OE1 OE2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 LYS B 107 CD CE NZ
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 LYS B 128 NZ
REMARK 470 LYS B 131 CG CD CE NZ
REMARK 470 LYS B 133 CG CD CE NZ
REMARK 470 LYS B 135 CG CD CE NZ
REMARK 470 LYS B 144 CE NZ
REMARK 470 LYS B 150 CG CD CE NZ
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 GLN A 53 -87.63 -111.35
REMARK 500 CYS A 55 -40.90 -12.08
REMARK 500 ASP A 66 -16.99 -49.49
REMARK 500 ARG A 103 63.30 -100.32
REMARK 500 GLU A 105 -14.26 -46.77
REMARK 500 GLU A 167 -118.40 63.32
REMARK 500 LYS A 180 -116.64 40.38
REMARK 500 SER A 188 -70.71 -45.04
REMARK 500 LEU A 192 -71.77 -64.52
REMARK 500 GLN A 208 71.20 -104.03
REMARK 500 LYS A 216 3.65 -56.46
REMARK 500 ASP A 217 40.29 -149.69
REMARK 500 SER A 220 -9.84 -55.50
REMARK 500 SER A 326 75.07 -66.67
REMARK 500 SER A 344 49.98 -100.24
REMARK 500 ALA A 349 -72.82 -61.23
REMARK 500 PRO A 351 -18.23 -48.44
REMARK 500 LEU A 359 43.79 -103.84
REMARK 500 ASP A 360 -159.41 -112.52
REMARK 500 ASP A 369 128.18 172.15
REMARK 500 LYS A 398 42.32 -76.78
REMARK 500 GLU A 399 -44.46 66.85
REMARK 500 GLN A 401 -87.99 -83.94
REMARK 500 LEU A 402 -63.25 50.67
REMARK 500 ASN B 39 156.35 70.20
REMARK 500 GLN B 74 -9.56 93.45
REMARK 500 TRP B 97 -70.20 -74.69
REMARK 500 HIS B 103 -70.97 -57.52
REMARK 500 LYS B 133 61.14 67.35
REMARK 500 LYS B 150 44.19 70.56
REMARK 500 GLN B 162 15.50 56.29
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 A2003 DISTANCE = 6.97 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1178
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WG7 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF PLECKSTRIN HOMOLOGY DOMAIN FROM HUMANKIAA1058
REMARK 900 PROTEIN
REMARK 900 RELATED ID: 1AM4 RELATED DB: PDB
REMARK 900 COMPLEX BETWEEN CDC42HS.GMPPNP AND P50 RHOGAP (H. SAPIENS)
REMARK 900 RELATED ID: 1NF3 RELATED DB: PDB
REMARK 900 STRUCTURE OF CDC42 IN A COMPLEX WITH THE GTPASE-BINDINGDOMAIN OF
REMARK 900 THE CELL POLARITY PROTEIN, PAR6
REMARK 900 RELATED ID: 1DOA RELATED DB: PDB
REMARK 900 STRUCTURE OF THE RHO FAMILY GTP-BINDING PROTEIN CDC42 INCOMPLEX
REMARK 900 WITH THE MULTIFUNCTIONAL REGULATOR RHOGDI
REMARK 900 RELATED ID: 1AJE RELATED DB: PDB
REMARK 900 CDC42 FROM HUMAN, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1KI1 RELATED DB: PDB
REMARK 900 GUANINE NUCLEOTIDE EXCHANGE REGION OF INTERSECTIN INCOMPLEX WITH
REMARK 900 CDC42
REMARK 900 RELATED ID: 1GZS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GEF DOMAIN OF THE
REMARK 900 SALMONELLA TYPHIMURIUM SOPE TOXIN AND HUMAN CDC42
REMARK 900 RELATED ID: 1KZG RELATED DB: PDB
REMARK 900 DBSCDC42(Y889F)
REMARK 900 RELATED ID: 1CEE RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CDC42 IN COMPLEX WITH THE GTPASE BINDING
REMARK 900 DOMAIN OF WASP
REMARK 900 RELATED ID: 2DFK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDC42-COLLYBISTIN II COMPLEX
REMARK 900 RELATED ID: 1EES RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF CDC42HS COMPLEXED WITH A PEPTIDE DERIVED FROM
REMARK 900 P-21 ACTIVATED KINASE, NMR, 20 STRUCTURES
REMARK 900 RELATED ID: 1AN0 RELATED DB: PDB
REMARK 900 CDC42HS-GDP COMPLEX
REMARK 900 RELATED ID: 1KZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DH/PH FRAGMENT OF MURINE DBS INCOMPLEX
REMARK 900 WITH THE PLACENTAL ISOFORM OF HUMAN CDC42
REMARK 900 RELATED ID: 1E0A RELATED DB: PDB
REMARK 900 CDC42 COMPLEXED WITH THE GTPASE BINDING DOMAIN OF P21 ACTIVATED
REMARK 900 KINASE
REMARK 900 RELATED ID: 2WM9 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COMPLEX BETWEEN DOCK9 AND CDC42.
REMARK 900 RELATED ID: 1A4R RELATED DB: PDB
REMARK 900 G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM
REMARK 900 RELATED ID: 2ASE RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE F28L MUTANT OF CDC42HS
REMARK 900 RELATED ID: 1CF4 RELATED DB: PDB
REMARK 900 CDC42/ACK GTPASE-BINDING DOMAIN COMPLEX
REMARK 900 RELATED ID: 2NGR RELATED DB: PDB
REMARK 900 TRANSITION STATE COMPLEX FOR GTP HYDROLYSIS BY CDC42: COMPARISONS
REMARK 900 OF THE HIGH RESOLUTION STRUCTURES FOR CDC42 BOUND TO THE ACTIVE AND
REMARK 900 CATALYTICALLY COMPROMISED FORMS OF THE CDC42-GAP.
REMARK 900 RELATED ID: 1GRN RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CDC42/CDC42GAP/ALF3 COMPLEX.
REMARK 900 RELATED ID: 2WMO RELATED DB: PDB
REMARK 900 STRUCTURE OF THE COMPLEX BETWEEN DOCK9 AND CDC42.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ISOFORM 2
DBREF 2WMN A 1 48 UNP Q9BZ29 DOCK9_HUMAN 1605 1652
DBREF 2WMN A 49 426 UNP Q9BZ29 DOCK9_HUMAN 1676 2053
DBREF 2WMN A 427 428 PDB 2WMN 2WMN 427 428
DBREF 2WMN B -1 0 PDB 2WMN 2WMN -1 0
DBREF 2WMN B 1 188 UNP P60953 CDC42_HUMAN 1 188
SEQRES 1 A 428 LYS SER TYR ALA SER THR PRO GLU LEU ARG LYS THR TRP
SEQRES 2 A 428 LEU ASP SER MET ALA ARG ILE HIS VAL LYS ASN GLY ASP
SEQRES 3 A 428 LEU SER GLU ALA ALA MET CYS TYR VAL HIS VAL THR ALA
SEQRES 4 A 428 LEU VAL ALA GLU TYR LEU THR ARG LYS GLY VAL PHE ARG
SEQRES 5 A 428 GLN GLY CYS THR ALA PHE ARG VAL ILE THR PRO ASN ILE
SEQRES 6 A 428 ASP GLU GLU ALA SER MET MET GLU ASP VAL GLY MET GLN
SEQRES 7 A 428 ASP VAL HIS PHE ASN GLU ASP VAL LEU MET GLU LEU LEU
SEQRES 8 A 428 GLU GLN CYS ALA ASP GLY LEU TRP LYS ALA GLU ARG TYR
SEQRES 9 A 428 GLU LEU ILE ALA ASP ILE TYR LYS LEU ILE ILE PRO ILE
SEQRES 10 A 428 TYR GLU LYS ARG ARG ASP PHE GLU ARG LEU ALA HIS LEU
SEQRES 11 A 428 TYR ASP THR LEU HIS ARG ALA TYR SER LYS VAL THR GLU
SEQRES 12 A 428 VAL MET HIS SER GLY ARG ARG LEU LEU GLY THR TYR PHE
SEQRES 13 A 428 ARG VAL ALA PHE PHE GLY GLN GLY PHE PHE GLU ASP GLU
SEQRES 14 A 428 ASP GLY LYS GLU TYR ILE TYR LYS GLU PRO LYS LEU THR
SEQRES 15 A 428 PRO LEU SER GLU ILE SER GLN ARG LEU LEU LYS LEU TYR
SEQRES 16 A 428 SER ASP LYS PHE GLY SER GLU ASN VAL LYS MET ILE GLN
SEQRES 17 A 428 ASP SER GLY LYS VAL ASN PRO LYS ASP LEU ASP SER LYS
SEQRES 18 A 428 TYR ALA TYR ILE GLN VAL THR HIS VAL ILE PRO PHE PHE
SEQRES 19 A 428 ASP GLU LYS GLU LEU GLN GLU ARG LYS THR GLU PHE GLU
SEQRES 20 A 428 ARG SER HIS ASN ILE ARG ARG PHE MET PHE GLU MET PRO
SEQRES 21 A 428 PHE THR GLN THR GLY LYS ARG GLN GLY GLY VAL GLU GLU
SEQRES 22 A 428 GLN CYS LYS ARG ARG THR ILE LEU THR ALA ILE HIS CYS
SEQRES 23 A 428 PHE PRO TYR VAL LYS LYS ARG ILE PRO VAL MET TYR GLN
SEQRES 24 A 428 HIS HIS THR ASP LEU ASN PRO ILE GLU VAL ALA ILE ASP
SEQRES 25 A 428 GLU MET SER LYS LYS VAL ALA GLU LEU ARG GLN LEU CYS
SEQRES 26 A 428 SER SER ALA GLU VAL ASP MET ILE LYS LEU GLN LEU LYS
SEQRES 27 A 428 LEU GLN GLY SER VAL SER VAL GLN VAL ASN ALA GLY PRO
SEQRES 28 A 428 LEU ALA TYR ALA ARG ALA PHE LEU ASP ASP THR ASN THR
SEQRES 29 A 428 LYS ARG TYR PRO ASP ASN LYS VAL LYS LEU LEU LYS GLU
SEQRES 30 A 428 VAL PHE ARG GLN PHE VAL GLU ALA CYS GLY GLN ALA LEU
SEQRES 31 A 428 ALA VAL ASN GLU ARG LEU ILE LYS GLU ASP GLN LEU GLU
SEQRES 32 A 428 TYR GLN GLU GLU MET LYS ALA ASN TYR ARG GLU MET ALA
SEQRES 33 A 428 LYS GLU LEU SER GLU ILE MET HIS GLU GLN LEU GLY
SEQRES 1 B 190 SER HIS MET GLN THR ILE LYS CYS VAL VAL VAL GLY ASP
SEQRES 2 B 190 GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR
SEQRES 3 B 190 THR ASN LYS PHE PRO SER GLU TYR VAL PRO THR VAL PHE
SEQRES 4 B 190 ASP ASN TYR ALA VAL THR VAL MET ILE GLY GLY GLU PRO
SEQRES 5 B 190 TYR THR LEU GLY LEU PHE ASP THR ALA GLY GLN GLU ASP
SEQRES 6 B 190 TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP
SEQRES 7 B 190 VAL PHE LEU VAL CYS PHE SER VAL VAL SER PRO SER SER
SEQRES 8 B 190 PHE GLU ASN VAL LYS GLU LYS TRP VAL PRO GLU ILE THR
SEQRES 9 B 190 HIS HIS CYS PRO LYS THR PRO PHE LEU LEU VAL GLY THR
SEQRES 10 B 190 GLN ILE ASP LEU ARG ASP ASP PRO SER THR ILE GLU LYS
SEQRES 11 B 190 LEU ALA LYS ASN LYS GLN LYS PRO ILE THR PRO GLU THR
SEQRES 12 B 190 ALA GLU LYS LEU ALA ARG ASP LEU LYS ALA VAL LYS TYR
SEQRES 13 B 190 VAL GLU CYS SER ALA LEU THR GLN LYS GLY LEU LYS ASN
SEQRES 14 B 190 VAL PHE ASP GLU ALA ILE LEU ALA ALA LEU GLU PRO PRO
SEQRES 15 B 190 GLU PRO LYS LYS SER ARG ARG CYS
HET GDP B1178 28
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 3 GDP C10 H15 N5 O11 P2
FORMUL 4 HOH *177(H2 O)
HELIX 1 1 SER A 5 GLY A 25 1 21
HELIX 2 2 ASP A 26 LYS A 48 1 23
HELIX 3 3 THR A 62 GLU A 68 5 7
HELIX 4 4 ASN A 83 ALA A 101 1 19
HELIX 5 5 ARG A 103 GLU A 105 5 3
HELIX 6 6 LEU A 106 ARG A 121 1 16
HELIX 7 7 ASP A 123 GLY A 148 1 26
HELIX 8 8 GLY A 162 GLU A 167 1 6
HELIX 9 9 ASP A 168 ASP A 170 5 3
HELIX 10 10 PRO A 183 GLY A 200 1 18
HELIX 11 11 ASN A 214 LEU A 218 5 5
HELIX 12 12 ASP A 235 ARG A 242 1 8
HELIX 13 13 PHE A 246 HIS A 250 5 5
HELIX 14 14 GLY A 270 GLN A 274 5 5
HELIX 15 15 ASN A 305 SER A 326 1 22
HELIX 16 16 ASP A 331 SER A 344 1 14
HELIX 17 17 PRO A 351 LEU A 359 1 9
HELIX 18 18 LYS A 371 ARG A 395 1 25
HELIX 19 19 LEU A 402 HIS A 424 1 23
HELIX 20 20 GLY B 15 ASN B 26 1 12
HELIX 21 21 PHE B 28 TYR B 32 5 5
HELIX 22 22 GLN B 61 ASP B 65 5 5
HELIX 23 23 LEU B 67 TYR B 72 5 6
HELIX 24 24 SER B 86 LYS B 96 1 11
HELIX 25 25 LYS B 96 CYS B 105 1 10
HELIX 26 26 GLN B 116 ASP B 121 5 6
HELIX 27 27 ASP B 122 LYS B 131 1 10
HELIX 28 28 THR B 138 LEU B 149 1 12
HELIX 29 29 GLY B 164 LEU B 177 1 14
SHEET 1 AA 9 THR A 154 PHE A 161 0
SHEET 2 AA 9 GLU A 173 GLU A 178 -1 O TYR A 174 N VAL A 158
SHEET 3 AA 9 ARG A 293 LEU A 304 -1 O ILE A 294 N ILE A 175
SHEET 4 AA 9 CYS A 275 PHE A 287 -1 O LYS A 276 N LEU A 304
SHEET 5 AA 9 ILE A 252 PHE A 261 -1 O ILE A 252 N PHE A 287
SHEET 6 AA 9 ALA A 223 PRO A 232 1 O ILE A 231 N MET A 256
SHEET 7 AA 9 THR A 154 PHE A 161 -1 O TYR A 155 N VAL A 230
SHEET 8 AA 9 GLU A 173 GLU A 178 -1 O TYR A 174 N VAL A 158
SHEET 9 AA 9 THR A 154 PHE A 161 -1 O THR A 154 N GLU A 178
SHEET 1 BA 6 TYR B 40 ILE B 46 0
SHEET 2 BA 6 GLU B 49 ASP B 57 -1 O GLU B 49 N ILE B 46
SHEET 3 BA 6 THR B 3 GLY B 10 1 O ILE B 4 N GLY B 54
SHEET 4 BA 6 VAL B 77 SER B 83 1 O VAL B 77 N VAL B 7
SHEET 5 BA 6 PHE B 110 THR B 115 1 O LEU B 111 N VAL B 80
SHEET 6 BA 6 TYR B 154 GLU B 156 1 O VAL B 155 N GLY B 114
CISPEP 1 PHE A 287 PRO A 288 0 -2.62
SITE 1 AC1 18 ASP B 11 GLY B 12 ALA B 13 VAL B 14
SITE 2 AC1 18 GLY B 15 LYS B 16 THR B 17 CYS B 18
SITE 3 AC1 18 GLN B 116 ASP B 118 LEU B 119 SER B 158
SITE 4 AC1 18 ALA B 159 LEU B 160 HOH B2017 HOH B2022
SITE 5 AC1 18 HOH B2023 HOH B2025
CRYST1 93.050 88.472 90.120 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 0.010747 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011303 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011096 0.00000
(ATOM LINES ARE NOT SHOWN.)
END