HEADER SIGNALING PROTEIN 18-NOV-00 1HE1
TITLE CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE GAP DOMAIN OF
TITLE 2 THE PSEUDOMONAS AERUGINOSA EXOS TOXIN AND HUMAN RAC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXOENZYME S;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: 96-234, GTPASE-ACTIVATING PROTEIN (GAP-DOMAIN);
COMPND 5 SYNONYM: EXOS;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: 2-184;
COMPND 11 SYNONYM: P21-RAC1, RAS-LIKE PROTEIN TC25;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: EXOS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS SIGNALING PROTEIN, SIGNALLING COMPLEX, EXOS, RAC,
KEYWDS 2 PSEUDOMONAS AERUGINOSA, GAP, TOXIN, VIRULENCE FACTOR,
KEYWDS 3 TRANSITION STATE, PROTEIN-PROTEIN COMPLEX, GTPASE, SIGNAL
KEYWDS 4 TRANSDUCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.WURTELE,E.WOLF,K.J.PEDERSON,G.BUCHWALD,M.R.AHMADIAN,
AUTHOR 2 J.T.BARBIERI,A.WITTINGHOFER
REVDAT 3 24-FEB-09 1HE1 1 VERSN
REVDAT 2 24-JUL-07 1HE1 1 COMPND
REVDAT 1 02-JAN-01 1HE1 0
JRNL AUTH M.WURTELE,E.WOLF,K.J.PEDERSON,G.BUCHWALD,
JRNL AUTH 2 M.R.AHMADIAN,J.T.BARBIERI,A.WITTINGHOFER
JRNL TITL HOW THE PSEUDOMONAS AERUGINOSA EXOS TOXIN
JRNL TITL 2 DOWNREGULATES RAC
JRNL REF NAT.STRUCT.BIOL. V. 8 23 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11135665
JRNL DOI 10.1038/83007
REMARK 2
REMARK 2 RESOLUTION. 2.0 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2288865.96
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 53886
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 SET) : 0.175
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.1
REMARK 3 FREE R VALUE TEST SET COUNT : 2739
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.9
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8396
REMARK 3 BIN R VALUE (WORKING SET) : 0.195
REMARK 3 BIN FREE R VALUE : 0.252
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 439
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4742
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 71
REMARK 3 SOLVENT ATOMS : 712
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.7
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.56
REMARK 3 B22 (A**2) : 0.68
REMARK 3 B33 (A**2) : -2.23
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.19
REMARK 3 ESD FROM SIGMAA (A) : 0.11
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.15
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.4
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.5
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.91
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.29 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.96 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.29 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.43 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.372576
REMARK 3 BSOL : 53.2816
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : GDP.PAR
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : GDP.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HE1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-NOV-00.
REMARK 100 THE PDBE ID CODE IS EBI-5475.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 527331
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.3000
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 (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1DS6 CHAIN A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 6000, 3MM NICL2,
REMARK 280 100 MM TRIS/HCL PH8.5
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 23.01250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.14200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 62.54350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.14200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.01250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 62.54350
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
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 GENERATING THE BIOMOLECULE
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 2550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.8 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 LEU C 19 CA - CB - CG ANGL. DEV. = 15.6 DEGREES
REMARK 500 LEU D 19 CA - CB - CG ANGL. DEV. = 18.0 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 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 LYS C 96 -55.98 -129.00
REMARK 500 LYS D 96 -59.85 -125.29
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 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 TYR D 72 24.2 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 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 NI A 230 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 211 ND1
REMARK 620 2 HOH A2067 O 176.3
REMARK 620 3 HOH A2115 O 99.8 77.6
REMARK 620 4 HOH A2117 O 85.0 97.8 93.6
REMARK 620 5 HOH C2023 O 105.4 71.5 78.0 167.5
REMARK 620 6 HOH C2025 O 92.8 89.7 167.3 88.9 97.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI C 203 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 103 NE2
REMARK 620 2 HOH C2092 O 85.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI D 203 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS D 103 NE2
REMARK 620 2 HOH D2091 O 94.9
REMARK 620 3 HOH D2092 O 84.7 117.4
REMARK 620 4 HOH D2093 O 87.5 167.6 74.9
REMARK 620 5 HOH D2143 O 162.7 71.9 91.5 107.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH C2224 O
REMARK 620 2 THR C 35 OG1 88.2
REMARK 620 3 GDP C 200 O2B 89.8 176.5
REMARK 620 4 AF3 C 201 F3 90.4 89.1 93.8
REMARK 620 5 HOH C2047 O 178.0 93.6 88.4 90.6
REMARK 620 6 THR C 17 OG1 90.0 79.6 97.6 168.7 89.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AF3 D 201 F1
REMARK 620 2 THR D 35 OG1 90.3
REMARK 620 3 THR D 17 OG1 170.3 80.3
REMARK 620 4 GDP D 200 O2B 94.0 174.2 95.1
REMARK 620 5 HOH D2224 O 91.6 94.3 91.8 89.5
REMARK 620 6 HOH D2046 O 87.9 89.9 89.4 86.4 175.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 C 201 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 AF3 C 201 F1
REMARK 620 2 HOH C2026 O 52.3
REMARK 620 3 MG C 202 MG 134.6 92.7
REMARK 620 4 GDP C 200 O2B 123.7 109.3 33.9
REMARK 620 5 AF3 C 201 F3 123.8 73.9 23.7 56.5
REMARK 620 6 HOH C2050 O 83.3 66.8 111.0 144.4 90.1
REMARK 620 7 GDP C 200 O3B 88.5 106.8 73.8 41.5 93.1 171.7
REMARK 620 8 AF3 C 201 F2 110.6 150.0 112.6 100.7 125.0 88.4 96.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 AF3 D 201 AL
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH D2049 O
REMARK 620 2 GDP D 200 O3B 173.1
REMARK 620 3 AF3 D 201 F1 89.5 91.9
REMARK 620 4 AF3 D 201 F2 82.5 91.0 120.6
REMARK 620 5 HOH D2025 O 66.9 106.9 76.2 46.6
REMARK 620 6 MG D 202 MG 109.4 73.3 22.0 130.7 93.0
REMARK 620 7 GDP D 200 O2B 142.4 41.5 55.3 124.6 110.7 33.8
REMARK 620 8 AF3 D 201 F3 87.6 97.0 125.3 113.1 147.6 115.0 101.7
REMARK 620 N 1 2 3 4 5 6 7
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 200
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AF3 D 201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E96 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE RAC/P67PHOX COMPLEX
REMARK 900 RELATED ID: 1MH1 RELATED DB: PDB
REMARK 900 SMALL G-PROTEIN
REMARK 900 RELATED ID: 1HE9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE GAP DOMAIN OF THE PSEUDOMONAS
REMARK 900 AERUGINOSA EXOS TOXIN
DBREF 1HE1 A 95 229 UNP Q51451 Q51451 95 229
DBREF 1HE1 B 95 229 UNP Q51451 Q51451 95 229
DBREF 1HE1 C 1 176 UNP P15154 RAC1_HUMAN 1 176
DBREF 1HE1 D 1 176 UNP P15154 RAC1_HUMAN 1 176
SEQADV 1HE1 ALA A 95 UNP Q51451 MET 1 CLONING ARTIFACT
SEQADV 1HE1 ALA B 95 UNP Q51451 MET 1 CLONING ARTIFACT
SEQADV 1HE1 PRO C 1 UNP P15154 MET 1 CLONING ARTIFACT
SEQADV 1HE1 PRO D 1 UNP P15154 MET 1 CLONING ARTIFACT
SEQRES 1 A 135 ALA SER SER ALA VAL VAL PHE LYS GLN MET VAL LEU GLN
SEQRES 2 A 135 GLN ALA LEU PRO MET THR LEU LYS GLY LEU ASP LYS ALA
SEQRES 3 A 135 SER GLU LEU ALA THR LEU THR PRO GLU GLY LEU ALA ARG
SEQRES 4 A 135 GLU HIS SER ARG LEU ALA SER GLY ASP GLY ALA LEU ARG
SEQRES 5 A 135 SER LEU SER THR ALA LEU ALA GLY ILE ARG ALA GLY SER
SEQRES 6 A 135 GLN VAL GLU GLU SER ARG ILE GLN ALA GLY ARG LEU LEU
SEQRES 7 A 135 GLU ARG SER ILE GLY GLY ILE ALA LEU GLN GLN TRP GLY
SEQRES 8 A 135 THR THR GLY GLY ALA ALA SER GLN LEU VAL LEU ASP ALA
SEQRES 9 A 135 SER PRO GLU LEU ARG ARG GLU ILE THR ASP GLN LEU HIS
SEQRES 10 A 135 GLN VAL MET SER GLU VAL ALA LEU LEU ARG GLN ALA VAL
SEQRES 11 A 135 GLU SER GLU VAL SER
SEQRES 1 B 135 ALA SER SER ALA VAL VAL PHE LYS GLN MET VAL LEU GLN
SEQRES 2 B 135 GLN ALA LEU PRO MET THR LEU LYS GLY LEU ASP LYS ALA
SEQRES 3 B 135 SER GLU LEU ALA THR LEU THR PRO GLU GLY LEU ALA ARG
SEQRES 4 B 135 GLU HIS SER ARG LEU ALA SER GLY ASP GLY ALA LEU ARG
SEQRES 5 B 135 SER LEU SER THR ALA LEU ALA GLY ILE ARG ALA GLY SER
SEQRES 6 B 135 GLN VAL GLU GLU SER ARG ILE GLN ALA GLY ARG LEU LEU
SEQRES 7 B 135 GLU ARG SER ILE GLY GLY ILE ALA LEU GLN GLN TRP GLY
SEQRES 8 B 135 THR THR GLY GLY ALA ALA SER GLN LEU VAL LEU ASP ALA
SEQRES 9 B 135 SER PRO GLU LEU ARG ARG GLU ILE THR ASP GLN LEU HIS
SEQRES 10 B 135 GLN VAL MET SER GLU VAL ALA LEU LEU ARG GLN ALA VAL
SEQRES 11 B 135 GLU SER GLU VAL SER
SEQRES 1 C 176 PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 C 176 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 C 176 ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN
SEQRES 4 C 176 TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN
SEQRES 5 C 176 LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 C 176 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 C 176 LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU
SEQRES 8 C 176 ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS
SEQRES 9 C 176 CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU
SEQRES 10 C 176 ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS
SEQRES 11 C 176 GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU
SEQRES 12 C 176 ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU
SEQRES 13 C 176 CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE
SEQRES 14 C 176 ASP GLU ALA ILE ARG ALA VAL
SEQRES 1 D 176 PRO GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 D 176 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 D 176 ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN
SEQRES 4 D 176 TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN
SEQRES 5 D 176 LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 D 176 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 D 176 LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU
SEQRES 8 D 176 ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS
SEQRES 9 D 176 CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU
SEQRES 10 D 176 ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS
SEQRES 11 D 176 GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU
SEQRES 12 D 176 ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU
SEQRES 13 D 176 CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE
SEQRES 14 D 176 ASP GLU ALA ILE ARG ALA VAL
HET NI A 230 1
HET MG C 202 1
HET NI C 203 1
HET NI C 204 2
HET MG D 202 1
HET NI D 203 1
HET GDP C 200 28
HET AF3 C 201 4
HET GDP D 200 28
HET AF3 D 201 4
HETNAM NI NICKEL (II) ION
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM AF3 ALUMINUM FLUORIDE
FORMUL 5 NI 4(NI 2+)
FORMUL 6 MG 2(MG 2+)
FORMUL 11 GDP 2(C10 H15 N5 O11 P2)
FORMUL 12 AF3 2()
FORMUL 15 HOH *712(H2 O1)
HELIX 1 1 SER A 96 ALA A 109 1 14
HELIX 2 2 ALA A 109 ALA A 120 1 12
HELIX 3 3 SER A 121 LEU A 126 5 6
HELIX 4 4 THR A 127 HIS A 135 1 9
HELIX 5 5 GLU A 134 ALA A 139 1 6
HELIX 6 6 GLY A 143 SER A 159 1 17
HELIX 7 7 VAL A 161 GLU A 173 1 13
HELIX 8 8 LEU A 181 GLY A 185 1 5
HELIX 9 9 GLY A 189 ALA A 198 1 10
HELIX 10 10 SER A 199 SER A 229 1 31
HELIX 11 11 ALA B 95 ALA B 109 1 15
HELIX 12 12 ALA B 109 ALA B 120 1 12
HELIX 13 13 SER B 121 LEU B 126 5 6
HELIX 14 14 THR B 127 HIS B 135 1 9
HELIX 15 15 GLU B 134 ALA B 139 1 6
HELIX 16 16 GLY B 143 SER B 159 1 17
HELIX 17 17 VAL B 161 ARG B 174 1 14
HELIX 18 18 LEU B 181 GLY B 185 1 5
HELIX 19 19 GLY B 189 ALA B 198 1 10
HELIX 20 20 SER B 199 SER B 229 1 31
HELIX 21 21 GLY C 15 ASN C 26 1 12
HELIX 22 22 GLN C 61 ASP C 65 5 5
HELIX 23 23 LEU C 67 TYR C 72 5 6
HELIX 24 24 SER C 86 LYS C 96 1 11
HELIX 25 25 LYS C 96 CYS C 105 1 10
HELIX 26 26 LYS C 116 ASP C 121 5 6
HELIX 27 27 ASP C 122 LYS C 132 1 11
HELIX 28 28 THR C 138 ILE C 149 1 12
HELIX 29 29 GLY C 164 ALA C 175 1 12
HELIX 30 30 GLY D 15 ASN D 26 1 12
HELIX 31 31 GLN D 61 ASP D 65 5 5
HELIX 32 32 LEU D 67 TYR D 72 5 6
HELIX 33 33 SER D 86 LYS D 96 1 11
HELIX 34 34 LYS D 96 CYS D 105 1 10
HELIX 35 35 LYS D 116 ARG D 120 5 5
HELIX 36 36 ASP D 122 GLU D 131 1 10
HELIX 37 37 THR D 138 GLY D 150 1 13
HELIX 38 38 GLY D 164 ALA D 175 1 12
SHEET 1 AA 2 SER A 175 ILE A 176 0
SHEET 2 AA 2 ILE A 179 ALA A 180 -1 O ILE A 179 N ILE A 176
SHEET 1 BA 2 SER B 175 ILE B 176 0
SHEET 2 BA 2 ILE B 179 ALA B 180 -1 O ILE B 179 N ILE B 176
SHEET 1 CA 6 PHE C 37 VAL C 46 0
SHEET 2 CA 6 LYS C 49 THR C 58 -1 O LYS C 49 N VAL C 46
SHEET 3 CA 6 GLN C 2 GLY C 10 1 O GLN C 2 N ASN C 52
SHEET 4 CA 6 VAL C 77 SER C 83 1 O VAL C 77 N VAL C 7
SHEET 5 CA 6 ILE C 110 THR C 115 1 O ILE C 111 N ILE C 80
SHEET 6 CA 6 LYS C 153 GLU C 156 1 O LYS C 153 N LEU C 112
SHEET 1 DA 6 PHE D 37 VAL D 46 0
SHEET 2 DA 6 LYS D 49 THR D 58 -1 O LYS D 49 N VAL D 46
SHEET 3 DA 6 GLN D 2 VAL D 9 1 O GLN D 2 N ASN D 52
SHEET 4 DA 6 VAL D 77 SER D 83 1 O VAL D 77 N VAL D 7
SHEET 5 DA 6 ILE D 110 THR D 115 1 O ILE D 111 N ILE D 80
SHEET 6 DA 6 LYS D 153 GLU D 156 1 O LYS D 153 N LEU D 112
LINK NI NI A 230 ND1 HIS A 211 1555 1555 2.14
LINK NI NI A 230 O HOH A2067 1555 1555 2.36
LINK NI NI A 230 O HOH A2115 1555 1555 2.11
LINK NI NI A 230 O HOH A2117 1555 1555 2.09
LINK NI NI A 230 O HOH C2023 1555 4455 2.11
LINK NI NI A 230 O HOH C2025 1555 4455 1.87
LINK O2B GDP C 200 MG MG C 202 1555 1555 2.03
LINK O3B GDP C 200 AL AF3 C 201 1555 1555 2.03
LINK AL AF3 C 201 O HOH C2050 1555 1555 2.23
LINK AL AF3 C 201 O2B GDP C 200 1555 1555 3.51
LINK AL AF3 C 201 O HOH C2026 1555 1555 3.55
LINK F3 AF3 C 201 MG MG C 202 1555 1555 1.99
LINK AL AF3 C 201 MG MG C 202 1555 1555 3.46
LINK MG MG C 202 O HOH C2224 1555 1555 2.22
LINK MG MG C 202 OG1 THR C 35 1555 1555 2.14
LINK MG MG C 202 O HOH C2047 1555 1555 2.05
LINK MG MG C 202 OG1 THR C 17 1555 1555 2.03
LINK NI NI C 203 NE2 HIS C 103 1555 1555 2.17
LINK NI NI C 203 O HOH C2092 1555 1555 2.04
LINK NI B NI C 204 OD1 ASP D 76 1555 1555 2.12
LINK NI A NI C 204 OD1 ASP C 76 1555 1555 2.08
LINK O3B GDP D 200 AL AF3 D 201 1555 1555 2.04
LINK O2B GDP D 200 MG MG D 202 1555 1555 2.04
LINK AL AF3 D 201 O2B GDP D 200 1555 1555 3.51
LINK F1 AF3 D 201 MG MG D 202 1555 1555 1.91
LINK AL AF3 D 201 O HOH D2049 1555 1555 2.21
LINK AL AF3 D 201 O HOH D2025 1555 1555 3.50
LINK AL AF3 D 201 MG MG D 202 1555 1555 3.49
LINK MG MG D 202 O HOH D2046 1555 1555 2.13
LINK MG MG D 202 O HOH D2224 1555 1555 2.06
LINK MG MG D 202 OG1 THR D 17 1555 1555 2.06
LINK MG MG D 202 OG1 THR D 35 1555 1555 2.11
LINK NI NI D 203 O HOH D2143 1555 1555 2.21
LINK NI NI D 203 O HOH D2093 1555 1555 2.30
LINK NI NI D 203 O HOH D2092 1555 1555 1.83
LINK NI NI D 203 O HOH D2091 1555 1555 1.99
LINK NI NI D 203 NE2 HIS D 103 1555 1555 2.07
SITE 1 AC1 6 HIS A 211 HOH A2067 HOH A2115 HOH A2117
SITE 2 AC1 6 HOH C2023 HOH C2025
SITE 1 AC2 6 THR C 17 THR C 35 GDP C 200 AF3 C 201
SITE 2 AC2 6 HOH C2047 HOH C2224
SITE 1 AC3 2 HIS C 103 HOH C2092
SITE 1 AC4 2 ASP C 76 ASP D 76
SITE 1 AC5 6 THR D 17 THR D 35 GDP D 200 AF3 D 201
SITE 2 AC5 6 HOH D2046 HOH D2224
SITE 1 AC6 5 HIS D 103 HOH D2091 HOH D2092 HOH D2093
SITE 2 AC6 5 HOH D2143
SITE 1 AC7 27 ARG A 146 THR A 186 THR A 187 GLY A 188
SITE 2 AC7 27 HOH A2094 ALA C 13 VAL C 14 GLY C 15
SITE 3 AC7 27 LYS C 16 THR C 17 CYS C 18 TYR C 32
SITE 4 AC7 27 LYS C 116 ASP C 118 LEU C 119 SER C 158
SITE 5 AC7 27 ALA C 159 LEU C 160 AF3 C 201 MG C 202
SITE 6 AC7 27 HOH C2006 HOH C2047 HOH C2224 HOH C2225
SITE 7 AC7 27 HOH C2226 HOH C2227 HOH C2228
SITE 1 AC8 15 ARG A 146 GLY C 12 ALA C 13 LYS C 16
SITE 2 AC8 15 THR C 35 THR C 58 ALA C 59 GLY C 60
SITE 3 AC8 15 GLN C 61 GDP C 200 MG C 202 HOH C2026
SITE 4 AC8 15 HOH C2047 HOH C2050 HOH C2224
SITE 1 AC9 25 ARG B 146 THR B 186 THR B 187 GLY B 188
SITE 2 AC9 25 ALA D 13 VAL D 14 GLY D 15 LYS D 16
SITE 3 AC9 25 THR D 17 CYS D 18 TYR D 32 LYS D 116
SITE 4 AC9 25 ASP D 118 LEU D 119 SER D 158 ALA D 159
SITE 5 AC9 25 LEU D 160 AF3 D 201 MG D 202 HOH D2046
SITE 6 AC9 25 HOH D2221 HOH D2223 HOH D2224 HOH D2225
SITE 7 AC9 25 HOH D2226
SITE 1 BC1 13 ARG B 146 GLY D 12 ALA D 13 LYS D 16
SITE 2 BC1 13 THR D 35 GLY D 60 GLN D 61 GDP D 200
SITE 3 BC1 13 MG D 202 HOH D2025 HOH D2046 HOH D2049
SITE 4 BC1 13 HOH D2224
CRYST1 46.025 125.087 136.284 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 0.021727 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007994 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007338 0.00000
MTRIX1 1 -0.117000 0.849200 0.514900 -49.90880 1
MTRIX2 1 0.860200 -0.172500 0.480000 25.66220 1
MTRIX3 1 0.496400 0.499000 -0.710300 43.16680 1
(ATOM LINES ARE NOT SHOWN.)
END
