HEADER SIGNALING PROTEIN 16-APR-08 2VRW
TITLE CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE
TITLE 2 VAV1 EXCHANGE FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-184;
COMPND 5 SYNONYM: P21-RAC1, RAS- LIKE PROTEIN TC25, CELL MIGRATION-INDUCING
COMPND 6 GENE 5 PROTEIN, RAC1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTO-ONCOGENE VAV;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 170-575;
COMPND 12 SYNONYM: P95VAV, VAV1;
COMPND 13 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: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 11 ORGANISM_COMMON: MOUSE;
SOURCE 12 ORGANISM_TAXID: 10090;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 15 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PET24B
KEYWDS LIPOPROTEIN, GTP-BINDING, METAL-BINDING, PROTO-ONCOGENE,
KEYWDS 2 PHOSPHOPROTEIN, EXCHANGE FACTOR, RAC, VAV, GTPASE, MEMBRANE, SH2
KEYWDS 3 DOMAIN, SH3 DOMAIN, METHYLATION, ZINC-FINGER, PRENYLATION,
KEYWDS 4 GUANINE-NUCLEOTIDE RELEASING FACTOR, PHORBOL-ESTER BINDING,
KEYWDS 5 ADP-RIBOSYLATION, NUCLEOTIDE-BINDING, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.RAPLEY,V.TYBULEWICZ,K.RITTINGER
REVDAT 4 13-JUL-11 2VRW 1 VERSN
REVDAT 3 24-FEB-09 2VRW 1 VERSN
REVDAT 2 08-JUL-08 2VRW 1 JRNL REMARK
REVDAT 1 17-JUN-08 2VRW 0
JRNL AUTH J.RAPLEY,V.TYBULEWICZ,K.RITTINGER
JRNL TITL CRUCIAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE
JRNL TITL 2 VAV1 EXCHANGE FACTOR.
JRNL REF EMBO REP. V. 9 655 2008
JRNL REFN ISSN 1469-221X
JRNL PMID 18511940
JRNL DOI 10.1038/EMBOR.2008.80
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 54863
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) : 0.205
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2937
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3906
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 202
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4410
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 2
REMARK 3 SOLVENT ATOMS : 471
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) : 29.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.58000
REMARK 3 B33 (A**2) : 0.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.36000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.338
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4498 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6069 ; 1.031 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 545 ; 5.242 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 217 ;34.943 ;23.917
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 835 ;13.546 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;16.614 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 671 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3377 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2151 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3089 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 420 ; 0.125 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 68 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.153 ; 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): 2821 ; 0.542 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4400 ; 0.901 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1901 ; 1.463 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1668 ; 2.328 ; 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 : 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 1 A 177
REMARK 3 ORIGIN FOR THE GROUP (A): -8.5140 -28.5920 16.8848
REMARK 3 T TENSOR
REMARK 3 T11: -0.0301 T22: -0.0357
REMARK 3 T33: -0.0252 T12: -0.0295
REMARK 3 T13: -0.0283 T23: 0.0407
REMARK 3 L TENSOR
REMARK 3 L11: 1.9408 L22: 1.3813
REMARK 3 L33: 1.1312 L12: -0.7714
REMARK 3 L13: 0.7795 L23: -0.1047
REMARK 3 S TENSOR
REMARK 3 S11: -0.1580 S12: 0.1519 S13: 0.1391
REMARK 3 S21: -0.0534 S22: 0.0393 S23: 0.0722
REMARK 3 S31: -0.1139 S32: 0.0403 S33: 0.1187
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 190 B 373
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0518 -43.2341 34.7584
REMARK 3 T TENSOR
REMARK 3 T11: -0.0190 T22: -0.0311
REMARK 3 T33: -0.0337 T12: -0.0062
REMARK 3 T13: 0.0126 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.5288 L22: 1.2227
REMARK 3 L33: 0.5868 L12: 0.6008
REMARK 3 L13: 0.4449 L23: 0.2923
REMARK 3 S TENSOR
REMARK 3 S11: 0.0201 S12: 0.0040 S13: 0.0121
REMARK 3 S21: 0.0428 S22: 0.0158 S23: 0.0322
REMARK 3 S31: 0.0312 S32: -0.0406 S33: -0.0358
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 374 B 508
REMARK 3 ORIGIN FOR THE GROUP (A): 22.7588 -57.4588 1.9478
REMARK 3 T TENSOR
REMARK 3 T11: -0.0107 T22: -0.0356
REMARK 3 T33: -0.0549 T12: 0.0125
REMARK 3 T13: 0.0067 T23: -0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 1.1124 L22: 0.6104
REMARK 3 L33: 3.1994 L12: -0.1691
REMARK 3 L13: -0.4719 L23: 0.1915
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: 0.1084 S13: -0.0379
REMARK 3 S21: -0.0530 S22: -0.0439 S23: 0.0588
REMARK 3 S31: 0.2326 S32: 0.1855 S33: 0.0188
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 509 B 564
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3111 -45.8784 24.8559
REMARK 3 T TENSOR
REMARK 3 T11: -0.0651 T22: -0.0341
REMARK 3 T33: -0.0200 T12: 0.0006
REMARK 3 T13: -0.0076 T23: -0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 3.9054 L22: 2.1745
REMARK 3 L33: 1.5486 L12: 1.0536
REMARK 3 L13: -0.5063 L23: 0.7488
REMARK 3 S TENSOR
REMARK 3 S11: -0.0792 S12: 0.0040 S13: 0.0134
REMARK 3 S21: 0.0070 S22: 0.0644 S23: -0.0533
REMARK 3 S31: 0.0137 S32: 0.0438 S33: 0.0148
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2VRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-08.
REMARK 100 THE PDBE ID CODE IS EBI-35944.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX10.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.117
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 : DEN
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57653
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.85
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 5.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 200 DATA REDUNDANCY : 3.5
REMARK 200 R MERGE (I) : 0.06
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.20
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.3
REMARK 200 R MERGE FOR SHELL (I) : 0.46
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.80
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BICINE PH9.0 10% PEG 6000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 61.38150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.07150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.38150
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 31.07150
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.7 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 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 CYS A 178
REMARK 465 PRO A 179
REMARK 465 PRO A 180
REMARK 465 PRO A 181
REMARK 465 VAL A 182
REMARK 465 LYS A 183
REMARK 465 LYS A 184
REMARK 465 GLY B 170
REMARK 465 ASP B 171
REMARK 465 GLU B 172
REMARK 465 ILE B 173
REMARK 465 TYR B 174
REMARK 465 GLU B 175
REMARK 465 ASP B 176
REMARK 465 LEU B 177
REMARK 465 MET B 178
REMARK 465 ARG B 179
REMARK 465 LEU B 180
REMARK 465 GLU B 181
REMARK 465 SER B 182
REMARK 465 VAL B 183
REMARK 465 PRO B 184
REMARK 465 THR B 185
REMARK 465 PRO B 186
REMARK 465 PRO B 187
REMARK 465 LYS B 188
REMARK 465 MET B 189
REMARK 465 ASP B 457
REMARK 465 SER B 458
REMARK 465 SER B 459
REMARK 465 GLY B 460
REMARK 465 GLU B 461
REMARK 465 ARG B 462
REMARK 465 ASP B 463
REMARK 465 ASN B 464
REMARK 465 GLY B 565
REMARK 465 ARG B 566
REMARK 465 HIS B 567
REMARK 465 GLY B 568
REMARK 465 GLN B 569
REMARK 465 ASP B 570
REMARK 465 PHE B 571
REMARK 465 ALA B 572
REMARK 465 GLY B 573
REMARK 465 THR B 574
REMARK 465 MET B 575
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 ASP B 456 CG OD1 OD2
REMARK 470 SER B 468 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU B 556 CD GLU B 556 OE2 0.076
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 26 -65.38 73.60
REMARK 500 LYS A 96 -57.68 -129.00
REMARK 500 VAL B 238 -122.03 48.30
REMARK 500 ASN B 316 19.50 -149.38
REMARK 500 TYR B 541 58.48 33.43
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 GLU A 62 24.5 L L OUTSIDE RANGE
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 ZN B1565 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 516 ND1
REMARK 620 2 CYS B 546 SG 108.6
REMARK 620 3 CYS B 549 SG 109.3 107.1
REMARK 620 4 CYS B 564 SG 107.9 113.2 110.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1566 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 532 SG
REMARK 620 2 HIS B 554 ND1 98.2
REMARK 620 3 CYS B 529 SG 110.9 101.8
REMARK 620 4 CYS B 557 SG 115.6 115.8 112.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B1566
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: 1I4D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP
REMARK 900 COMPLEXED WITHARFAPTIN (P21)
REMARK 900 RELATED ID: 1FOE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF RAC1 IN COMPLEX WITH
REMARK 900 THE GUANINENUCLEOTIDE EXCHANGE REGION OF TIAM1
REMARK 900 RELATED ID: 1MH1 RELATED DB: PDB
REMARK 900 SMALL G-PROTEIN
REMARK 900 RELATED ID: 1I4L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP IN
REMARK 900 COMPLEX WITHARFAPTIN (P41)
REMARK 900 RELATED ID: 1HE1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE
REMARK 900 GAP DOMAIN OF THE PSEUDOMONAS AERUGINOSA
REMARK 900 EXOS TOXIN AND HUMAN RAC
REMARK 900 RELATED ID: 1RYF RELATED DB: PDB
REMARK 900 ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B
REMARK 900 , A SELF-ACTIVATING GTPASE
REMARK 900 RELATED ID: 1K1Z RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF N-TERMINAL SH3 DOMAIN
REMARK 900 MUTANT(P33G) OFMURINE VAV
REMARK 900 RELATED ID: 1RYH RELATED DB: PDB
REMARK 900 ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B
REMARK 900 , A SELF-ACTIVATING GTPASE
REMARK 900 RELATED ID: 1HH4 RELATED DB: PDB
REMARK 900 RAC1-RHOGDI COMPLEX INVOLVED IN NADPH
REMARK 900 OXIDASE ACTIVATION
REMARK 900 RELATED ID: 1GCP RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VAV SH3 DOMAIN
REMARK 900 RELATED ID: 1G4U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE
REMARK 900 PHOSPHATASEAND GTPASE ACTIVATING PROTEIN SPTP
REMARK 900 BOUND TO RAC1
REMARK 900 RELATED ID: 2FJU RELATED DB: PDB
REMARK 900 ACTIVATED RAC1 BOUND TO ITS EFFECTOR
REMARK 900 PHOSPHOLIPASE C BETA 2
REMARK 900 RELATED ID: 1F5X RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL
REMARK 900 HOMOLGY DOMAIN
REMARK 900 RELATED ID: 1I4T RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN
REMARK 900 COMPLEX WITHARFAPTIN
REMARK 900 RELATED ID: 1GCQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF VAV AND GRB2 SH3
REMARK 900 DOMAINS
DBREF 2VRW A 1 184 UNP P63000 RAC1_HUMAN 1 184
DBREF 2VRW B 170 575 UNP P27870 VAV_MOUSE 170 575
SEQRES 1 A 184 MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA
SEQRES 2 A 184 VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN
SEQRES 3 A 184 ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN
SEQRES 4 A 184 TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN
SEQRES 5 A 184 LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP
SEQRES 6 A 184 ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE
SEQRES 7 A 184 LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU
SEQRES 8 A 184 ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS
SEQRES 9 A 184 CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU
SEQRES 10 A 184 ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS
SEQRES 11 A 184 GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU
SEQRES 12 A 184 ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU
SEQRES 13 A 184 CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE
SEQRES 14 A 184 ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL
SEQRES 15 A 184 LYS LYS
SEQRES 1 B 406 GLY ASP GLU ILE TYR GLU ASP LEU MET ARG LEU GLU SER
SEQRES 2 B 406 VAL PRO THR PRO PRO LYS MET THR GLU TYR ASP LYS ARG
SEQRES 3 B 406 CYS CYS CYS LEU ARG GLU ILE GLN GLN THR GLU GLU LYS
SEQRES 4 B 406 TYR THR ASP THR LEU GLY SER ILE GLN GLN HIS PHE MET
SEQRES 5 B 406 LYS PRO LEU GLN ARG PHE LEU LYS PRO GLN ASP MET GLU
SEQRES 6 B 406 THR ILE PHE VAL ASN ILE GLU GLU LEU PHE SER VAL HIS
SEQRES 7 B 406 THR HIS PHE LEU LYS GLU LEU LYS ASP ALA LEU ALA GLY
SEQRES 8 B 406 PRO GLY ALA THR THR LEU TYR GLN VAL PHE ILE LYS TYR
SEQRES 9 B 406 LYS GLU ARG PHE LEU VAL TYR GLY ARG TYR CYS SER GLN
SEQRES 10 B 406 VAL GLU SER ALA SER LYS HIS LEU ASP GLN VAL ALA THR
SEQRES 11 B 406 ALA ARG GLU ASP VAL GLN MET LYS LEU GLU GLU CYS SER
SEQRES 12 B 406 GLN ARG ALA ASN ASN GLY ARG PHE THR LEU ARG ASP LEU
SEQRES 13 B 406 LEU MET VAL PRO MET GLN ARG VAL LEU LYS TYR HIS LEU
SEQRES 14 B 406 LEU LEU GLN GLU LEU VAL LYS HIS THR GLN ASP ALA THR
SEQRES 15 B 406 GLU LYS GLU ASN LEU ARG LEU ALA LEU ASP ALA MET ARG
SEQRES 16 B 406 ASP LEU ALA GLN CYS VAL ASN GLU VAL LYS ARG ASP ASN
SEQRES 17 B 406 GLU THR LEU ARG GLN ILE THR ASN PHE GLN LEU SER ILE
SEQRES 18 B 406 GLU ASN LEU ASP GLN SER LEU ALA ASN TYR GLY ARG PRO
SEQRES 19 B 406 LYS ILE ASP GLY GLU LEU LYS ILE THR SER VAL GLU ARG
SEQRES 20 B 406 ARG SER LYS THR ASP ARG TYR ALA PHE LEU LEU ASP LYS
SEQRES 21 B 406 ALA LEU LEU ILE CYS LYS ARG ARG GLY ASP SER TYR ASP
SEQRES 22 B 406 LEU LYS ALA SER VAL ASN LEU HIS SER PHE GLN VAL ARG
SEQRES 23 B 406 ASP ASP SER SER GLY GLU ARG ASP ASN LYS LYS TRP SER
SEQRES 24 B 406 HIS MET PHE LEU LEU ILE GLU ASP GLN GLY ALA GLN GLY
SEQRES 25 B 406 TYR GLU LEU PHE PHE LYS THR ARG GLU LEU LYS LYS LYS
SEQRES 26 B 406 TRP MET GLU GLN PHE GLU MET ALA ILE SER ASN ILE TYR
SEQRES 27 B 406 PRO GLU ASN ALA THR ALA ASN GLY HIS ASP PHE GLN MET
SEQRES 28 B 406 PHE SER PHE GLU GLU THR THR SER CYS LYS ALA CYS GLN
SEQRES 29 B 406 MET LEU LEU ARG GLY THR PHE TYR GLN GLY TYR ARG CYS
SEQRES 30 B 406 TYR ARG CYS ARG ALA PRO ALA HIS LYS GLU CYS LEU GLY
SEQRES 31 B 406 ARG VAL PRO PRO CYS GLY ARG HIS GLY GLN ASP PHE ALA
SEQRES 32 B 406 GLY THR MET
HET ZN B1565 1
HET ZN B1566 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 HOH *471(H2 O)
HELIX 1 1 GLY A 15 ASN A 26 1 12
HELIX 2 2 LEU A 67 TYR A 72 5 6
HELIX 3 3 SER A 86 LYS A 96 1 11
HELIX 4 4 LYS A 96 CYS A 105 1 10
HELIX 5 5 LYS A 116 ASP A 121 1 6
HELIX 6 6 ASP A 122 LYS A 132 1 11
HELIX 7 7 THR A 138 ILE A 149 1 12
HELIX 8 8 GLY A 164 LEU A 177 1 14
HELIX 9 9 THR B 190 PHE B 220 1 31
HELIX 10 10 PHE B 220 GLN B 225 1 6
HELIX 11 11 LYS B 229 VAL B 238 1 10
HELIX 12 12 ASN B 239 GLY B 260 1 22
HELIX 13 13 PRO B 261 THR B 264 5 4
HELIX 14 14 THR B 265 LYS B 274 1 10
HELIX 15 15 GLU B 275 PHE B 277 5 3
HELIX 16 16 LEU B 278 ASN B 317 1 40
HELIX 17 17 THR B 321 LEU B 326 1 6
HELIX 18 18 MET B 327 LEU B 334 1 8
HELIX 19 19 LYS B 335 THR B 347 1 13
HELIX 20 20 ASP B 349 SER B 389 1 41
HELIX 21 21 SER B 396 GLY B 401 5 6
HELIX 22 22 THR B 488 TYR B 507 1 20
HELIX 23 23 THR B 512 HIS B 516 5 5
HELIX 24 24 HIS B 554 VAL B 561 5 8
SHEET 1 AA 6 TYR A 40 VAL A 46 0
SHEET 2 AA 6 LYS A 49 TRP A 56 -1 O LYS A 49 N VAL A 46
SHEET 3 AA 6 ALA A 3 GLY A 10 1 O ILE A 4 N GLY A 54
SHEET 4 AA 6 VAL A 77 SER A 83 1 O VAL A 77 N VAL A 7
SHEET 5 AA 6 ILE A 110 THR A 115 1 O ILE A 111 N ILE A 80
SHEET 6 AA 6 LYS A 153 GLU A 156 1 O LYS A 153 N LEU A 112
SHEET 1 BA 8 ILE B 390 GLU B 391 0
SHEET 2 BA 8 SER B 440 ASN B 448 1 O TYR B 441 N GLU B 391
SHEET 3 BA 8 ALA B 430 ARG B 437 -1 O LEU B 431 N VAL B 447
SHEET 4 BA 8 THR B 420 LEU B 427 -1 O TYR B 423 N CYS B 434
SHEET 5 BA 8 PRO B 403 THR B 412 -1 N LYS B 404 O LEU B 426
SHEET 6 BA 8 GLY B 481 PHE B 486 -1 O GLU B 483 N THR B 412
SHEET 7 BA 8 HIS B 469 GLU B 475 -1 O HIS B 469 N PHE B 486
SHEET 8 BA 8 PHE B 452 ARG B 455 -1 O GLN B 453 N ILE B 474
SHEET 1 BB 3 PHE B 518 PHE B 521 0
SHEET 2 BB 3 GLY B 543 CYS B 546 -1 O GLY B 543 N PHE B 521
SHEET 3 BB 3 PRO B 552 ALA B 553 -1 O ALA B 553 N TYR B 544
LINK ZN ZN B1565 ND1 HIS B 516 1555 1555 2.10
LINK ZN ZN B1565 SG CYS B 546 1555 1555 2.29
LINK ZN ZN B1565 SG CYS B 549 1555 1555 2.29
LINK ZN ZN B1565 SG CYS B 564 1555 1555 2.43
LINK ZN ZN B1566 ND1 HIS B 554 1555 1555 2.16
LINK ZN ZN B1566 SG CYS B 529 1555 1555 2.32
LINK ZN ZN B1566 SG CYS B 557 1555 1555 2.29
LINK ZN ZN B1566 SG CYS B 532 1555 1555 2.30
SITE 1 AC1 4 HIS B 516 CYS B 546 CYS B 549 CYS B 564
SITE 1 AC2 4 CYS B 529 CYS B 532 HIS B 554 CYS B 557
CRYST1 122.763 62.143 103.281 90.00 118.80 90.00 C 1 2 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 0.008146 0.000000 0.004478 0.00000
SCALE2 0.000000 0.016092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011049 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
