HEADER HYDROLASE 22-DEC-03 1RYF
TITLE ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B, A SELF-ACTIVATING GTPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1 ISOFORM RAC1B;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 1-201;
COMPND 5 SYNONYM: RAC1B;
COMPND 6 EC: 3.6.5.2;
COMPND 7 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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX4T1
KEYWDS GTP BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.R.AHMADIAN,D.FIEGEN
REVDAT 4 13-JUL-11 1RYF 1 VERSN
REVDAT 3 24-FEB-09 1RYF 1 VERSN
REVDAT 2 10-FEB-04 1RYF 1 JRNL
REVDAT 1 27-JAN-04 1RYF 0
JRNL AUTH D.FIEGEN,L.C.HAEUSLER,L.BLUMENSTEIN,U.HERBRAND,R.DVORSKY,
JRNL AUTH 2 I.R.VETTER,M.R.AHMADIAN
JRNL TITL ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B, A
JRNL TITL 2 SELF-ACTIVATING GTPASE
JRNL REF J.BIOL.CHEM. V. 279 4743 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 14625275
JRNL DOI 10.1074/JBC.M310281200
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.19
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.92
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 37724
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1958
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2657
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2360
REMARK 3 BIN FREE R VALUE SET COUNT : 139
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2580
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 273
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.24000
REMARK 3 B22 (A**2) : 0.24000
REMARK 3 B33 (A**2) : -0.48000
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): 0.113
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.111
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.456
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.951
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2701 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2473 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3688 ; 1.873 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5786 ; 0.966 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 333 ; 6.774 ; 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): 434 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2884 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 486 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 507 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2815 ; 0.249 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1562 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 190 ; 0.173 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.033 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 13 ; 0.208 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.356 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.186 ; 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): 1684 ; 1.164 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2739 ; 1.974 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1017 ; 2.881 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 949 ; 4.429 ; 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 : 2
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 201
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7810 62.6790 41.1640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0546 T22: 0.0536
REMARK 3 T33: 0.0701 T12: -0.0103
REMARK 3 T13: -0.0236 T23: 0.0298
REMARK 3 L TENSOR
REMARK 3 L11: 2.6853 L22: 1.9991
REMARK 3 L33: 2.5305 L12: 0.7860
REMARK 3 L13: -1.2975 L23: -0.2259
REMARK 3 S TENSOR
REMARK 3 S11: -0.1242 S12: 0.2702 S13: 0.1571
REMARK 3 S21: -0.1221 S22: 0.1368 S23: 0.0012
REMARK 3 S31: -0.0013 S32: -0.1219 S33: -0.0126
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 1 B 199
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1320 62.7900 7.2190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0064 T22: 0.0554
REMARK 3 T33: 0.0822 T12: -0.0110
REMARK 3 T13: -0.0095 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 2.9507 L22: 1.7649
REMARK 3 L33: 2.1915 L12: -0.2766
REMARK 3 L13: -0.9545 L23: -0.0428
REMARK 3 S TENSOR
REMARK 3 S11: -0.0145 S12: -0.2814 S13: 0.2241
REMARK 3 S21: 0.1290 S22: 0.0542 S23: 0.0070
REMARK 3 S31: 0.0049 S32: 0.0557 S33: -0.0397
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 1RYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-DEC-03.
REMARK 100 THE RCSB ID CODE IS RCSB021147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39688
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 24.922
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1MH1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 25.82000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.39500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.34500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.39500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.82000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.34500
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 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 A 60
REMARK 465 GLN A 61
REMARK 465 GLU A 62
REMARK 465 ASP A 63
REMARK 465 TYR A 64
REMARK 465 ASP A 65
REMARK 465 ARG A 66
REMARK 465 LEU A 67
REMARK 465 ARG A 68
REMARK 465 PRO A 69
REMARK 465 LEU A 70
REMARK 465 SER A 71
REMARK 465 TYR A 72
REMARK 465 PRO A 73
REMARK 465 GLN A 74
REMARK 465 THR A 75
REMARK 465 VAL A 76
REMARK 465 GLY A 77
REMARK 465 GLU A 78
REMARK 465 THR A 79
REMARK 465 TYR A 80
REMARK 465 GLY A 81
REMARK 465 LYS A 82
REMARK 465 ASP A 83
REMARK 465 ILE A 84
REMARK 465 THR A 85
REMARK 465 SER A 86
REMARK 465 ARG A 87
REMARK 465 GLY A 88
REMARK 465 LYS A 89
REMARK 465 ASP A 90
REMARK 465 LYS A 91
REMARK 465 PRO A 92
REMARK 465 ALA B 59
REMARK 465 GLY B 60
REMARK 465 GLN B 61
REMARK 465 GLU B 62
REMARK 465 ASP B 63
REMARK 465 TYR B 64
REMARK 465 ASP B 65
REMARK 465 ARG B 66
REMARK 465 LEU B 67
REMARK 465 ARG B 68
REMARK 465 PRO B 69
REMARK 465 LEU B 70
REMARK 465 SER B 71
REMARK 465 TYR B 72
REMARK 465 PRO B 73
REMARK 465 GLN B 74
REMARK 465 THR B 75
REMARK 465 VAL B 76
REMARK 465 GLY B 77
REMARK 465 GLU B 78
REMARK 465 THR B 79
REMARK 465 TYR B 80
REMARK 465 GLY B 81
REMARK 465 LYS B 82
REMARK 465 ASP B 83
REMARK 465 ILE B 84
REMARK 465 THR B 85
REMARK 465 SER B 86
REMARK 465 ARG B 87
REMARK 465 GLY B 88
REMARK 465 LYS B 89
REMARK 465 ASP B 90
REMARK 465 LYS B 91
REMARK 465 PRO B 92
REMARK 465 PRO B 200
REMARK 465 VAL B 201
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 VAL A 36 CG1 CG2
REMARK 470 ILE A 93 CG1 CG2 CD1
REMARK 470 VAL A 201 CG1 CG2
REMARK 470 VAL B 36 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 1553 O HOH B 1651 1.92
REMARK 500 O HOH A 623 O HOH A 643 2.18
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 ARG A 139 CG ARG A 139 CD -0.152
REMARK 500 VAL A 171 CB VAL A 171 CG2 -0.130
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 ASP A 47 CB - CG - OD2 ANGL. DEV. = 7.1 DEGREES
REMARK 500 ASP A 95 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 140 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP A 141 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 38 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 47 CB - CG - OD2 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ASP B 95 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP B 143 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG B 182 NE - CZ - NH2 ANGL. DEV. = -4.8 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 SER A 2A 97.48 63.08
REMARK 500 LYS A 115 -52.96 -124.55
REMARK 500 LYS B 115 -51.83 -127.26
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 THR B 127 24.8 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 661 DISTANCE = 6.04 ANGSTROMS
REMARK 525 HOH A 663 DISTANCE = 5.51 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 539 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP A 538 O2B
REMARK 620 2 HOH A 541 O 93.4
REMARK 620 3 HOH A 605 O 96.8 88.6
REMARK 620 4 THR A 17 OG1 93.0 172.9 87.5
REMARK 620 5 HOH A 606 O 86.2 91.5 176.9 92.1
REMARK 620 6 HOH A 540 O 175.0 84.9 87.8 89.1 89.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1539 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GDP B1538 O2B
REMARK 620 2 HOH B1585 O 102.5
REMARK 620 3 HOH B1587 O 95.5 92.0
REMARK 620 4 HOH B1586 O 87.8 167.6 93.9
REMARK 620 5 HOH B1584 O 172.5 84.5 87.1 85.0
REMARK 620 6 THR B 17 OG1 93.2 85.3 171.3 87.3 84.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1539
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 538
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 1538
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1RYH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH 5'-GUANOSYL-IMIDO-
REMARK 900 TRIPHOSPHATE
DBREF 1RYF A 1 201 UNP P63000 RAC1_HUMAN 1 201
DBREF 1RYF B 1 201 UNP P63000 RAC1_HUMAN 1 201
SEQADV 1RYF GLY A 1A UNP P63000 CLONING ARTIFACT
SEQADV 1RYF SER A 2A UNP P63000 CLONING ARTIFACT
SEQADV 1RYF GLY B 1A UNP P63000 CLONING ARTIFACT
SEQADV 1RYF SER B 2A UNP P63000 CLONING ARTIFACT
SEQRES 1 A 203 GLY SER MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP
SEQRES 2 A 203 GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR
SEQRES 3 A 203 THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE
SEQRES 4 A 203 ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO
SEQRES 5 A 203 VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP
SEQRES 6 A 203 TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR VAL
SEQRES 7 A 203 GLY GLU THR TYR GLY LYS ASP ILE THR SER ARG GLY LYS
SEQRES 8 A 203 ASP LYS PRO ILE ALA ASP VAL PHE LEU ILE CYS PHE SER
SEQRES 9 A 203 LEU VAL SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS
SEQRES 10 A 203 TRP TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO
SEQRES 11 A 203 ILE ILE LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP
SEQRES 12 A 203 LYS ASP THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR
SEQRES 13 A 203 PRO ILE THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU
SEQRES 14 A 203 ILE GLY ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR
SEQRES 15 A 203 GLN ARG GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG
SEQRES 16 A 203 ALA VAL LEU CYS PRO PRO PRO VAL
SEQRES 1 B 203 GLY SER MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP
SEQRES 2 B 203 GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR
SEQRES 3 B 203 THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE
SEQRES 4 B 203 ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO
SEQRES 5 B 203 VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP
SEQRES 6 B 203 TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR VAL
SEQRES 7 B 203 GLY GLU THR TYR GLY LYS ASP ILE THR SER ARG GLY LYS
SEQRES 8 B 203 ASP LYS PRO ILE ALA ASP VAL PHE LEU ILE CYS PHE SER
SEQRES 9 B 203 LEU VAL SER PRO ALA SER PHE GLU ASN VAL ARG ALA LYS
SEQRES 10 B 203 TRP TYR PRO GLU VAL ARG HIS HIS CYS PRO ASN THR PRO
SEQRES 11 B 203 ILE ILE LEU VAL GLY THR LYS LEU ASP LEU ARG ASP ASP
SEQRES 12 B 203 LYS ASP THR ILE GLU LYS LEU LYS GLU LYS LYS LEU THR
SEQRES 13 B 203 PRO ILE THR TYR PRO GLN GLY LEU ALA MET ALA LYS GLU
SEQRES 14 B 203 ILE GLY ALA VAL LYS TYR LEU GLU CYS SER ALA LEU THR
SEQRES 15 B 203 GLN ARG GLY LEU LYS THR VAL PHE ASP GLU ALA ILE ARG
SEQRES 16 B 203 ALA VAL LEU CYS PRO PRO PRO VAL
HET MG A 539 1
HET MG B1539 1
HET GDP A 538 28
HET GDP B1538 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 5 GDP 2(C10 H15 N5 O11 P2)
FORMUL 7 HOH *273(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 SER A 105 LYS A 115 1 11
HELIX 3 3 LYS A 115 CYS A 124 1 10
HELIX 4 4 LYS A 135 ASP A 140 1 6
HELIX 5 5 ASP A 141 GLU A 150 1 10
HELIX 6 6 THR A 157 GLY A 169 1 13
HELIX 7 7 GLY A 183 CYS A 197 1 15
HELIX 8 8 GLY B 15 ASN B 26 1 12
HELIX 9 9 SER B 105 LYS B 115 1 11
HELIX 10 10 LYS B 115 CYS B 124 1 10
HELIX 11 11 LYS B 135 ASP B 140 1 6
HELIX 12 12 ASP B 141 LYS B 151 1 11
HELIX 13 13 THR B 157 GLY B 169 1 13
HELIX 14 14 GLY B 183 CYS B 197 1 15
SHEET 1 A 6 ASN A 39 VAL A 46 0
SHEET 2 A 6 LYS A 49 ASP A 57 -1 O LEU A 55 N TYR A 40
SHEET 3 A 6 SER A 2A GLY A 10 1 N CYS A 6 O GLY A 54
SHEET 4 A 6 SER B 2A GLY B 10 -1 O MET B 1 N MET A 1
SHEET 5 A 6 LYS B 49 ASP B 57 1 O GLY B 54 N CYS B 6
SHEET 6 A 6 ASN B 39 VAL B 46 -1 N TYR B 40 O LEU B 55
SHEET 1 B 8 LYS A 172 GLU A 175 0
SHEET 2 B 8 ILE A 129 THR A 134 1 N LEU A 131 O LYS A 172
SHEET 3 B 8 VAL A 96 SER A 102 1 N PHE A 97 O ILE A 130
SHEET 4 B 8 SER A 2A GLY A 10 1 N VAL A 9 O CYS A 100
SHEET 5 B 8 SER B 2A GLY B 10 -1 O MET B 1 N MET A 1
SHEET 6 B 8 VAL B 96 SER B 102 1 O CYS B 100 N VAL B 9
SHEET 7 B 8 ILE B 129 THR B 134 1 O ILE B 130 N PHE B 97
SHEET 8 B 8 LYS B 172 GLU B 175 1 O LEU B 174 N GLY B 133
LINK O2B GDP A 538 MG MG A 539 1555 1555 2.00
LINK MG MG A 539 O HOH A 541 1555 1555 2.10
LINK MG MG A 539 O HOH A 605 1555 1555 2.05
LINK MG MG A 539 OG1 THR A 17 1555 1555 2.09
LINK MG MG A 539 O HOH A 606 1555 1555 2.08
LINK MG MG A 539 O HOH A 540 1555 1555 2.20
LINK O2B GDP B1538 MG MG B1539 1555 1555 1.96
LINK MG MG B1539 O HOH B1585 1555 1555 2.08
LINK MG MG B1539 O HOH B1587 1555 1555 2.07
LINK MG MG B1539 O HOH B1586 1555 1555 2.06
LINK MG MG B1539 O HOH B1584 1555 1555 2.36
LINK MG MG B1539 OG1 THR B 17 1555 1555 2.09
CISPEP 1 GLY A 1A SER A 2A 0 26.66
SITE 1 AC1 6 THR A 17 GDP A 538 HOH A 540 HOH A 541
SITE 2 AC1 6 HOH A 605 HOH A 606
SITE 1 AC2 6 THR B 17 GDP B1538 HOH B1584 HOH B1585
SITE 2 AC2 6 HOH B1586 HOH B1587
SITE 1 AC3 23 ALA A 13 VAL A 14 GLY A 15 LYS A 16
SITE 2 AC3 23 THR A 17 CYS A 18 PHE A 28 LYS A 135
SITE 3 AC3 23 ASP A 137 LEU A 138 SER A 177 ALA A 178
SITE 4 AC3 23 LEU A 179 MG A 539 HOH A 541 HOH A 542
SITE 5 AC3 23 HOH A 575 HOH A 585 HOH A 605 HOH A 606
SITE 6 AC3 23 HOH A 623 HOH A 641 HOH A 645
SITE 1 AC4 21 ALA B 13 VAL B 14 GLY B 15 LYS B 16
SITE 2 AC4 21 THR B 17 CYS B 18 PHE B 28 LYS B 135
SITE 3 AC4 21 ASP B 137 LEU B 138 SER B 177 ALA B 178
SITE 4 AC4 21 LEU B 179 MG B1539 HOH B1558 HOH B1575
SITE 5 AC4 21 HOH B1586 HOH B1587 HOH B1598 HOH B1642
SITE 6 AC4 21 HOH B1663
CRYST1 51.640 78.690 96.790 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 0.019365 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012708 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
