HEADER SIGNALING PROTEIN 18-AUG-11 3TH5
TITLE CRYSTAL STRUCTURE OF WILD-TYPE RAC1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 2-177;
COMPND 5 SYNONYM: CELL MIGRATION-INDUCING GENE 5 PROTEIN, RAS-LIKE PROTEIN
COMPND 6 TC25, P21-RAC1;
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 GENE: RAC1, TC25, MIG5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: MODIFIED PET-28
KEYWDS ROSSMANN FOLD, GTPASE, GTP BINDING, PROTEIN BINDING, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.HA,T.J.BOGGON
REVDAT 4 12-DEC-12 3TH5 1 REMARK
REVDAT 3 19-SEP-12 3TH5 1 JRNL
REVDAT 2 29-AUG-12 3TH5 1 JRNL
REVDAT 1 18-JUL-12 3TH5 0
JRNL AUTH M.KRAUTHAMMER,Y.KONG,B.H.HA,P.EVANS,A.BACCHIOCCHI,
JRNL AUTH 2 J.P.MCCUSKER,E.CHENG,M.J.DAVIS,G.GOH,M.CHOI,S.ARIYAN,
JRNL AUTH 3 D.NARAYAN,K.DUTTON-REGESTER,A.CAPATANA,E.C.HOLMAN,
JRNL AUTH 4 M.BOSENBERG,M.SZNOL,H.M.KLUGER,D.E.BRASH,D.F.STERN,
JRNL AUTH 5 M.A.MATERIN,R.S.LO,S.MANE,S.MA,K.K.KIDD,N.K.HAYWARD,
JRNL AUTH 6 R.P.LIFTON,J.SCHLESSINGER,T.J.BOGGON,R.HALABAN
JRNL TITL EXOME SEQUENCING IDENTIFIES RECURRENT SOMATIC RAC1 MUTATIONS
JRNL TITL 2 IN MELANOMA.
JRNL REF NAT.GENET. V. 44 1006 2012
JRNL REFN ISSN 1061-4036
JRNL PMID 22842228
JRNL DOI 10.1038/NG.2359
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 17830
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 910
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1259
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.10
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2710
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 23
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.50
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.52
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.48000
REMARK 3 B22 (A**2) : -2.34000
REMARK 3 B33 (A**2) : 0.87000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.253
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.250
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.911
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2863 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3915 ; 1.106 ; 2.008
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 352 ; 5.041 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 116 ;39.487 ;24.397
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 482 ;14.714 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 15 ;14.567 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 451 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2107 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1744 ; 0.204 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2842 ; 0.385 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1119 ; 0.500 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1069 ; 0.827 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 177 4
REMARK 3 1 B 2 B 177 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1311 ; 0.23 ; 0.50
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1311 ; 0.12 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 76
REMARK 3 ORIGIN FOR THE GROUP (A): -2.6680 -6.6970 -2.2400
REMARK 3 T TENSOR
REMARK 3 T11: 0.2623 T22: 0.7249
REMARK 3 T33: 0.5935 T12: 0.0258
REMARK 3 T13: -0.0463 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 8.6763 L22: 5.6796
REMARK 3 L33: 8.9141 L12: 1.2895
REMARK 3 L13: 1.7593 L23: -0.0740
REMARK 3 S TENSOR
REMARK 3 S11: -0.2774 S12: -0.2464 S13: 1.6547
REMARK 3 S21: -0.1156 S22: 0.1816 S23: 0.2893
REMARK 3 S31: -0.9330 S32: -0.2306 S33: 0.0958
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 77 A 177
REMARK 3 ORIGIN FOR THE GROUP (A): -4.6580 -21.1840 -3.7070
REMARK 3 T TENSOR
REMARK 3 T11: 0.1577 T22: 0.8582
REMARK 3 T33: 0.2593 T12: -0.0107
REMARK 3 T13: -0.0297 T23: 0.0461
REMARK 3 L TENSOR
REMARK 3 L11: 4.5940 L22: 3.1818
REMARK 3 L33: 6.0691 L12: 0.9611
REMARK 3 L13: 0.3057 L23: -0.3342
REMARK 3 S TENSOR
REMARK 3 S11: 0.0760 S12: -0.0933 S13: -0.0102
REMARK 3 S21: -0.2231 S22: 0.1027 S23: 0.0196
REMARK 3 S31: 0.3048 S32: -0.3128 S33: -0.1787
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 2 B 76
REMARK 3 ORIGIN FOR THE GROUP (A): 5.3570 -40.1460 -27.3570
REMARK 3 T TENSOR
REMARK 3 T11: 0.2766 T22: 0.8137
REMARK 3 T33: 0.6506 T12: 0.0370
REMARK 3 T13: 0.0592 T23: -0.0580
REMARK 3 L TENSOR
REMARK 3 L11: 9.5918 L22: 5.6657
REMARK 3 L33: 7.8487 L12: 1.3888
REMARK 3 L13: -2.5051 L23: -0.7769
REMARK 3 S TENSOR
REMARK 3 S11: -0.2911 S12: -0.0883 S13: -1.6185
REMARK 3 S21: -0.0718 S22: 0.3042 S23: -0.3715
REMARK 3 S31: 1.3454 S32: 0.0227 S33: -0.0131
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 : B 77 B 177
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3090 -25.6200 -28.2400
REMARK 3 T TENSOR
REMARK 3 T11: 0.0385 T22: 0.8921
REMARK 3 T33: 0.2870 T12: 0.0138
REMARK 3 T13: 0.0157 T23: -0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 5.3630 L22: 6.4646
REMARK 3 L33: 5.4203 L12: -0.0391
REMARK 3 L13: -0.1218 L23: -0.8359
REMARK 3 S TENSOR
REMARK 3 S11: -0.1017 S12: 0.0620 S13: 0.0129
REMARK 3 S21: -0.0093 S22: 0.1128 S23: -0.4189
REMARK 3 S31: -0.1188 S32: 0.4167 S33: -0.0112
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 3TH5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-11.
REMARK 100 THE RCSB ID CODE IS RCSB067471.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97921
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18169
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.29500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
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 3SBD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG4000, 7% ISOPROPANOL, 0.1M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 48.92550
REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 MET A -26
REMARK 465 GLY A -25
REMARK 465 SER A -24
REMARK 465 SER A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 LEU A -13
REMARK 465 VAL A -12
REMARK 465 PRO A -11
REMARK 465 ARG A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 HIS A -7
REMARK 465 MET A -6
REMARK 465 GLU A -5
REMARK 465 ASN A -4
REMARK 465 LEU A -3
REMARK 465 TYR A -2
REMARK 465 PHE A -1
REMARK 465 GLN A 0
REMARK 465 GLY A 1
REMARK 465 MET B -26
REMARK 465 GLY B -25
REMARK 465 SER B -24
REMARK 465 SER B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 LEU B -13
REMARK 465 VAL B -12
REMARK 465 PRO B -11
REMARK 465 ARG B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 HIS B -7
REMARK 465 MET B -6
REMARK 465 GLU B -5
REMARK 465 ASN B -4
REMARK 465 LEU B -3
REMARK 465 TYR B -2
REMARK 465 PHE B -1
REMARK 465 GLN B 0
REMARK 465 GLY B 1
REMARK 465 GLY B 30
REMARK 465 GLU B 31
REMARK 465 TYR B 32
REMARK 465 ILE B 33
REMARK 465 PRO B 34
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 VAL A 36 -61.68 -95.17
REMARK 500 PHE A 37 122.35 -172.20
REMARK 500 LYS A 96 -53.32 -124.28
REMARK 500 ALA B 13 15.22 86.51
REMARK 500 PHE B 37 130.18 -172.42
REMARK 500 LYS B 96 -53.47 -120.67
REMARK 500 ASP B 121 64.38 -108.55
REMARK 500 LYS B 123 -81.26 -51.55
REMARK 500
REMARK 500 REMARK: NULL
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 A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 35 OG1
REMARK 620 2 GNP A1001 O2G 92.6
REMARK 620 3 GNP A1001 O2B 168.7 86.2
REMARK 620 4 THR A 17 OG1 82.5 171.8 97.4
REMARK 620 5 HOH A 188 O 97.6 99.8 93.7 87.4
REMARK 620 6 HOH A 187 O 83.4 81.6 85.3 91.2 178.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 17 OG1
REMARK 620 2 GNP B1001 O2B 95.5
REMARK 620 3 GNP B1001 O2G 158.6 86.6
REMARK 620 4 THR B 35 OG1 81.4 152.1 86.8
REMARK 620 5 HOH B 186 O 109.5 100.9 90.9 106.3
REMARK 620 6 HOH B 184 O 79.8 79.7 79.6 72.5 170.5
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 GNP A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3SBD RELATED DB: PDB
REMARK 900 RELATED ID: 3SBE RELATED DB: PDB
REMARK 900 RELATED ID: 4GZL RELATED DB: PDB
REMARK 900 RELATED ID: 4GZM RELATED DB: PDB
DBREF 3TH5 A 2 177 UNP P63000 RAC1_HUMAN 2 177
DBREF 3TH5 B 2 177 UNP P63000 RAC1_HUMAN 2 177
SEQADV 3TH5 MET A -26 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY A -25 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER A -24 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER A -23 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS A -22 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS A -21 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS A -20 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS A -19 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS A -18 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS A -17 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER A -16 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER A -15 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY A -14 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 LEU A -13 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 VAL A -12 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 PRO A -11 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 ARG A -10 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY A -9 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER A -8 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS A -7 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 MET A -6 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLU A -5 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 ASN A -4 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 LEU A -3 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 TYR A -2 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 PHE A -1 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLN A 0 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY A 1 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 MET B -26 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY B -25 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER B -24 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER B -23 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS B -22 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS B -21 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS B -20 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS B -19 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS B -18 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS B -17 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER B -16 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER B -15 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY B -14 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 LEU B -13 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 VAL B -12 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 PRO B -11 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 ARG B -10 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY B -9 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 SER B -8 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 HIS B -7 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 MET B -6 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLU B -5 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 ASN B -4 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 LEU B -3 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 TYR B -2 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 PHE B -1 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLN B 0 UNP P63000 EXPRESSION TAG
SEQADV 3TH5 GLY B 1 UNP P63000 EXPRESSION TAG
SEQRES 1 A 204 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 204 LEU VAL PRO ARG GLY SER HIS MET GLU ASN LEU TYR PHE
SEQRES 3 A 204 GLN GLY GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY
SEQRES 4 A 204 ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR
SEQRES 5 A 204 ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP
SEQRES 6 A 204 ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL
SEQRES 7 A 204 ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR
SEQRES 8 A 204 ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL
SEQRES 9 A 204 PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE
SEQRES 10 A 204 GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS
SEQRES 11 A 204 HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS
SEQRES 12 A 204 LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU
SEQRES 13 A 204 LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY
SEQRES 14 A 204 LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU
SEQRES 15 A 204 GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL
SEQRES 16 A 204 PHE ASP GLU ALA ILE ARG ALA VAL LEU
SEQRES 1 B 204 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 204 LEU VAL PRO ARG GLY SER HIS MET GLU ASN LEU TYR PHE
SEQRES 3 B 204 GLN GLY GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY
SEQRES 4 B 204 ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR
SEQRES 5 B 204 ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP
SEQRES 6 B 204 ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL
SEQRES 7 B 204 ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR
SEQRES 8 B 204 ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL
SEQRES 9 B 204 PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE
SEQRES 10 B 204 GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS
SEQRES 11 B 204 HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS
SEQRES 12 B 204 LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU
SEQRES 13 B 204 LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY
SEQRES 14 B 204 LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU
SEQRES 15 B 204 GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL
SEQRES 16 B 204 PHE ASP GLU ALA ILE ARG ALA VAL LEU
HET GNP A1001 32
HET MG A1002 1
HET GNP B1001 32
HET MG B1002 1
HETNAM GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER
HETNAM MG MAGNESIUM ION
FORMUL 3 GNP 2(C10 H17 N6 O13 P3)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *23(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 GLN A 61 ASP A 65 5 5
HELIX 3 3 LEU A 67 TYR A 72 5 6
HELIX 4 4 SER A 86 LYS A 96 1 11
HELIX 5 5 LYS A 96 CYS A 105 1 10
HELIX 6 6 LYS A 116 ASP A 121 5 6
HELIX 7 7 ASP A 122 GLU A 131 1 10
HELIX 8 8 THR A 138 ILE A 149 1 12
HELIX 9 9 GLY A 164 ALA A 175 1 12
HELIX 10 10 GLY B 15 ASN B 26 1 12
HELIX 11 11 GLN B 61 ASP B 65 5 5
HELIX 12 12 LEU B 67 TYR B 72 5 6
HELIX 13 13 SER B 86 LYS B 96 1 11
HELIX 14 14 LYS B 96 CYS B 105 1 10
HELIX 15 15 LYS B 116 ASP B 121 1 6
HELIX 16 16 ASP B 122 GLU B 131 1 10
HELIX 17 17 THR B 138 ILE B 149 1 12
HELIX 18 18 GLY B 164 ALA B 175 1 12
SHEET 1 A 6 PHE A 37 VAL A 46 0
SHEET 2 A 6 LYS A 49 THR A 58 -1 O LEU A 55 N TYR A 40
SHEET 3 A 6 ALA A 3 GLY A 10 1 N CYS A 6 O GLY A 54
SHEET 4 A 6 VAL A 77 SER A 83 1 O LEU A 79 N VAL A 7
SHEET 5 A 6 ILE A 110 THR A 115 1 O ILE A 111 N PHE A 78
SHEET 6 A 6 LYS A 153 GLU A 156 1 O LYS A 153 N LEU A 112
SHEET 1 B 6 ASP B 38 VAL B 46 0
SHEET 2 B 6 LYS B 49 ASP B 57 -1 O LEU B 55 N TYR B 40
SHEET 3 B 6 ALA B 3 GLY B 10 1 N ILE B 4 O GLY B 54
SHEET 4 B 6 VAL B 77 SER B 83 1 O LEU B 79 N VAL B 9
SHEET 5 B 6 ILE B 110 THR B 115 1 O VAL B 113 N ILE B 80
SHEET 6 B 6 LYS B 153 GLU B 156 1 O LEU B 155 N GLY B 114
LINK OG1 THR A 35 MG MG A1002 1555 1555 1.84
LINK OG1 THR B 17 MG MG B1002 1555 1555 1.88
LINK O2G GNP A1001 MG MG A1002 1555 1555 1.94
LINK O2B GNP B1001 MG MG B1002 1555 1555 1.99
LINK O2B GNP A1001 MG MG A1002 1555 1555 2.00
LINK O2G GNP B1001 MG MG B1002 1555 1555 2.00
LINK OG1 THR A 17 MG MG A1002 1555 1555 2.12
LINK OG1 THR B 35 MG MG B1002 1555 1555 2.23
LINK MG MG B1002 O HOH B 186 1555 1555 1.95
LINK MG MG A1002 O HOH A 188 1555 1555 2.03
LINK MG MG B1002 O HOH B 184 1555 1555 2.26
LINK MG MG A1002 O HOH A 187 1555 1555 2.40
SITE 1 AC1 21 GLY A 12 ALA A 13 VAL A 14 GLY A 15
SITE 2 AC1 21 LYS A 16 THR A 17 CYS A 18 PHE A 28
SITE 3 AC1 21 TYR A 32 THR A 35 GLY A 60 LYS A 116
SITE 4 AC1 21 ASP A 118 LEU A 119 SER A 158 ALA A 159
SITE 5 AC1 21 LEU A 160 HOH A 180 HOH A 187 HOH A 188
SITE 6 AC1 21 MG A1002
SITE 1 AC2 5 THR A 17 THR A 35 HOH A 187 HOH A 188
SITE 2 AC2 5 GNP A1001
SITE 1 AC3 19 GLY B 12 ALA B 13 VAL B 14 GLY B 15
SITE 2 AC3 19 LYS B 16 THR B 17 CYS B 18 PHE B 28
SITE 3 AC3 19 THR B 35 GLY B 60 LYS B 116 ASP B 118
SITE 4 AC3 19 LEU B 119 SER B 158 ALA B 159 LEU B 160
SITE 5 AC3 19 HOH B 184 HOH B 186 MG B1002
SITE 1 AC4 6 THR B 17 THR B 35 ASP B 57 HOH B 184
SITE 2 AC4 6 HOH B 186 GNP B1001
CRYST1 40.925 97.851 51.733 90.00 96.59 90.00 P 1 21 1 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 0.024435 0.000000 0.002823 0.00000
SCALE2 0.000000 0.010220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019459 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
