HEADER SIGNALING PROTEIN 07-OCT-09 3A8P
TITLE CRYSTAL STRUCTURE OF THE TIAM2 PHCCEX DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: T-LYMPHOMA INVASION AND METASTASIS-INDUCING PROTEIN 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: PHCCEX DOMAIN, RESIDUES 500-757;
COMPND 5 SYNONYM: TIAM-2, SIF AND TIAM1-LIKE EXCHANGE FACTOR;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TIAM2, KIAA2016, STEF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-3
KEYWDS GUANINE NUCLEOTIDE EXCHANGE FACTOR, ALTERNATIVE SPLICING, CELL
KEYWDS 2 PROJECTION, COILED COIL, CYTOPLASM, GUANINE-NUCLEOTIDE RELEASING
KEYWDS 3 FACTOR, LIPOPROTEIN, MYRISTATE, PHOSPHOPROTEIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.TERAWAKI,K.KITANO,T.MORI,Y.ZHAI,Y.HIGUCHI,N.ITOH,T.WATANABE,
AUTHOR 2 K.KAIBUCHI,T.HAKOSHIMA
REVDAT 3 01-NOV-23 3A8P 1 SEQADV
REVDAT 2 19-JAN-10 3A8P 1 JRNL
REVDAT 1 24-NOV-09 3A8P 0
JRNL AUTH S.TERAWAKI,K.KITANO,T.MORI,Y.ZHAI,Y.HIGUCHI,N.ITOH,
JRNL AUTH 2 T.WATANABE,K.KAIBUCHI,T.HAKOSHIMA
JRNL TITL THE PHCCEX DOMAIN OF TIAM1/2 IS A NOVEL PROTEIN- AND
JRNL TITL 2 MEMBRANE-BINDING MODULE
JRNL REF EMBO J. V. 29 236 2010
JRNL REFN ISSN 0261-4189
JRNL PMID 19893486
JRNL DOI 10.1038/EMBOJ.2009.323
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1845113.440
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 63378
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) : 0.211
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 6404
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8957
REMARK 3 BIN R VALUE (WORKING SET) : 0.2840
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1001
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7371
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 383
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.24000
REMARK 3 B22 (A**2) : -8.90000
REMARK 3 B33 (A**2) : -2.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -5.28000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.27
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) : 0.32
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.31
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.680
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) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 60.77
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 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3A8P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1000028951.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-MAY-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : ROTATED-INCLINED DOUBLE-CRYSTAL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64571
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.080
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.600
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) : 2.08
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3A8Q
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 8000, 100MM TRIS-HCL, 200MM
REMARK 280 MAGNESIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 52.39500
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, 3, 4
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 495
REMARK 465 PRO A 496
REMARK 465 LEU A 497
REMARK 465 GLY A 498
REMARK 465 SER A 499
REMARK 465 LYS A 500
REMARK 465 GLU A 501
REMARK 465 GLN A 502
REMARK 465 GLY A 503
REMARK 465 ASN A 554
REMARK 465 SER A 555
REMARK 465 THR A 556
REMARK 465 GLU A 557
REMARK 465 GLN A 558
REMARK 465 ASN A 559
REMARK 465 ASP A 742
REMARK 465 SER A 743
REMARK 465 THR A 744
REMARK 465 LEU A 745
REMARK 465 ARG A 746
REMARK 465 LYS A 747
REMARK 465 ARG A 748
REMARK 465 THR A 749
REMARK 465 LEU A 750
REMARK 465 SER A 751
REMARK 465 LEU A 752
REMARK 465 THR A 753
REMARK 465 GLN A 754
REMARK 465 ARG A 755
REMARK 465 GLY A 756
REMARK 465 LYS A 757
REMARK 465 GLY B 495
REMARK 465 PRO B 496
REMARK 465 LEU B 497
REMARK 465 GLY B 498
REMARK 465 SER B 499
REMARK 465 LYS B 500
REMARK 465 GLU B 501
REMARK 465 GLN B 502
REMARK 465 GLY B 503
REMARK 465 GLY B 552
REMARK 465 LYS B 553
REMARK 465 ASN B 554
REMARK 465 SER B 555
REMARK 465 THR B 556
REMARK 465 GLU B 557
REMARK 465 GLN B 558
REMARK 465 ASN B 559
REMARK 465 SER B 743
REMARK 465 THR B 744
REMARK 465 LEU B 745
REMARK 465 ARG B 746
REMARK 465 LYS B 747
REMARK 465 ARG B 748
REMARK 465 THR B 749
REMARK 465 LEU B 750
REMARK 465 SER B 751
REMARK 465 LEU B 752
REMARK 465 THR B 753
REMARK 465 GLN B 754
REMARK 465 ARG B 755
REMARK 465 GLY B 756
REMARK 465 LYS B 757
REMARK 465 GLY C 495
REMARK 465 PRO C 496
REMARK 465 LEU C 497
REMARK 465 GLY C 498
REMARK 465 SER C 499
REMARK 465 LYS C 500
REMARK 465 GLU C 501
REMARK 465 GLN C 502
REMARK 465 GLY C 503
REMARK 465 GLY C 552
REMARK 465 LYS C 553
REMARK 465 ASN C 554
REMARK 465 SER C 555
REMARK 465 THR C 556
REMARK 465 GLU C 557
REMARK 465 GLN C 558
REMARK 465 ASN C 559
REMARK 465 SER C 560
REMARK 465 ASP C 742
REMARK 465 SER C 743
REMARK 465 THR C 744
REMARK 465 LEU C 745
REMARK 465 ARG C 746
REMARK 465 LYS C 747
REMARK 465 ARG C 748
REMARK 465 THR C 749
REMARK 465 LEU C 750
REMARK 465 SER C 751
REMARK 465 LEU C 752
REMARK 465 THR C 753
REMARK 465 GLN C 754
REMARK 465 ARG C 755
REMARK 465 GLY C 756
REMARK 465 LYS C 757
REMARK 465 GLY D 495
REMARK 465 PRO D 496
REMARK 465 LEU D 497
REMARK 465 GLY D 498
REMARK 465 SER D 499
REMARK 465 LYS D 500
REMARK 465 GLU D 501
REMARK 465 THR D 550
REMARK 465 TYR D 551
REMARK 465 GLY D 552
REMARK 465 LYS D 553
REMARK 465 ASN D 554
REMARK 465 SER D 555
REMARK 465 THR D 556
REMARK 465 GLU D 557
REMARK 465 GLN D 558
REMARK 465 ASN D 559
REMARK 465 SER D 560
REMARK 465 ALA D 561
REMARK 465 ASP D 742
REMARK 465 SER D 743
REMARK 465 THR D 744
REMARK 465 LEU D 745
REMARK 465 ARG D 746
REMARK 465 LYS D 747
REMARK 465 ARG D 748
REMARK 465 THR D 749
REMARK 465 LEU D 750
REMARK 465 SER D 751
REMARK 465 LEU D 752
REMARK 465 THR D 753
REMARK 465 GLN D 754
REMARK 465 ARG D 755
REMARK 465 GLY D 756
REMARK 465 LYS D 757
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 LYS A 553 CG CD CE NZ
REMARK 470 SER A 560 OG
REMARK 470 ASP B 742 CG OD1 OD2
REMARK 470 ASP C 741 CG OD1 OD2
REMARK 470 GLN D 502 CG CD OE1 NE2
REMARK 470 GLU D 549 CG CD OE1 OE2
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 LYS A 521 152.89 -47.47
REMARK 500 GLU A 522 -3.18 83.09
REMARK 500 ALA B 529 101.17 -42.55
REMARK 500 ARG B 530 83.96 -24.54
REMARK 500 ASP B 664 109.93 -45.76
REMARK 500 ASP B 741 96.80 -65.45
REMARK 500 LYS C 514 116.34 -161.54
REMARK 500 LEU C 516 -55.07 -121.77
REMARK 500 GLN C 520 -158.22 -104.00
REMARK 500 GLU C 522 70.78 64.77
REMARK 500 ALA C 529 -104.55 -63.11
REMARK 500 ASP C 664 157.28 -45.21
REMARK 500 PRO C 665 -108.88 -57.46
REMARK 500 LYS C 666 0.28 -69.74
REMARK 500 LEU D 516 -51.96 -124.29
REMARK 500 ARG D 523 50.69 37.47
REMARK 500 ASP D 664 111.06 70.58
REMARK 500 LYS D 666 37.40 -67.97
REMARK 500 ASN D 667 -39.61 -151.35
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3A8N RELATED DB: PDB
REMARK 900 TIAM1 PHCCEX DOMAIN
REMARK 900 RELATED ID: 3A8Q RELATED DB: PDB
REMARK 900 TIAM2 PHCCEX DOMAIN AT LOW RESOLUTION
DBREF 3A8P A 500 757 UNP Q6ZPF3 TIAM2_MOUSE 500 757
DBREF 3A8P B 500 757 UNP Q6ZPF3 TIAM2_MOUSE 500 757
DBREF 3A8P C 500 757 UNP Q6ZPF3 TIAM2_MOUSE 500 757
DBREF 3A8P D 500 757 UNP Q6ZPF3 TIAM2_MOUSE 500 757
SEQADV 3A8P GLY A 495 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P PRO A 496 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P LEU A 497 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P GLY A 498 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P SER A 499 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P GLY B 495 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P PRO B 496 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P LEU B 497 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P GLY B 498 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P SER B 499 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P GLY C 495 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P PRO C 496 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P LEU C 497 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P GLY C 498 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P SER C 499 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P GLY D 495 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P PRO D 496 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P LEU D 497 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P GLY D 498 UNP Q6ZPF3 EXPRESSION TAG
SEQADV 3A8P SER D 499 UNP Q6ZPF3 EXPRESSION TAG
SEQRES 1 A 263 GLY PRO LEU GLY SER LYS GLU GLN GLY VAL VAL ARG LYS
SEQRES 2 A 263 ALA GLY TRP LEU PHE PHE LYS PRO LEU VAL THR LEU GLN
SEQRES 3 A 263 LYS GLU ARG LYS LEU GLU LEU VAL ALA ARG ARG LYS TRP
SEQRES 4 A 263 LYS GLN TYR TRP VAL THR LEU LYS GLY CYS THR LEU LEU
SEQRES 5 A 263 PHE TYR GLU THR TYR GLY LYS ASN SER THR GLU GLN ASN
SEQRES 6 A 263 SER ALA PRO ARG CYS ALA LEU PHE ALA GLU ASP SER ILE
SEQRES 7 A 263 VAL GLN SER VAL PRO GLU HIS PRO LYS LYS GLU HIS VAL
SEQRES 8 A 263 PHE CYS LEU SER ASN SER CYS GLY ASP VAL TYR LEU PHE
SEQRES 9 A 263 GLN ALA THR SER GLN THR ASP LEU GLU ASN TRP VAL THR
SEQRES 10 A 263 ALA ILE HIS SER ALA CYS ALA SER LEU PHE ALA LYS LYS
SEQRES 11 A 263 HIS GLY LYS GLU ASP THR VAL ARG LEU LEU LYS SER GLN
SEQRES 12 A 263 THR ARG SER LEU LEU GLN LYS ILE ASP MET ASP SER LYS
SEQRES 13 A 263 MET LYS LYS MET ALA GLU LEU GLN LEU SER VAL VAL SER
SEQRES 14 A 263 ASP PRO LYS ASN ARG LYS ALA ILE GLU ASN GLN ILE ARG
SEQRES 15 A 263 GLN TRP GLU GLN ASN LEU GLU LYS PHE HIS MET ASP LEU
SEQRES 16 A 263 PHE ARG MET ARG CYS TYR LEU ALA SER LEU GLN GLY GLY
SEQRES 17 A 263 GLU LEU PRO ASN PRO LYS SER LEU LEU ALA ALA THR SER
SEQRES 18 A 263 ARG PRO SER LYS LEU ALA LEU GLY ARG LEU GLY VAL LEU
SEQRES 19 A 263 SER VAL SER SER PHE HIS ALA LEU VAL CYS SER ARG ASP
SEQRES 20 A 263 ASP SER THR LEU ARG LYS ARG THR LEU SER LEU THR GLN
SEQRES 21 A 263 ARG GLY LYS
SEQRES 1 B 263 GLY PRO LEU GLY SER LYS GLU GLN GLY VAL VAL ARG LYS
SEQRES 2 B 263 ALA GLY TRP LEU PHE PHE LYS PRO LEU VAL THR LEU GLN
SEQRES 3 B 263 LYS GLU ARG LYS LEU GLU LEU VAL ALA ARG ARG LYS TRP
SEQRES 4 B 263 LYS GLN TYR TRP VAL THR LEU LYS GLY CYS THR LEU LEU
SEQRES 5 B 263 PHE TYR GLU THR TYR GLY LYS ASN SER THR GLU GLN ASN
SEQRES 6 B 263 SER ALA PRO ARG CYS ALA LEU PHE ALA GLU ASP SER ILE
SEQRES 7 B 263 VAL GLN SER VAL PRO GLU HIS PRO LYS LYS GLU HIS VAL
SEQRES 8 B 263 PHE CYS LEU SER ASN SER CYS GLY ASP VAL TYR LEU PHE
SEQRES 9 B 263 GLN ALA THR SER GLN THR ASP LEU GLU ASN TRP VAL THR
SEQRES 10 B 263 ALA ILE HIS SER ALA CYS ALA SER LEU PHE ALA LYS LYS
SEQRES 11 B 263 HIS GLY LYS GLU ASP THR VAL ARG LEU LEU LYS SER GLN
SEQRES 12 B 263 THR ARG SER LEU LEU GLN LYS ILE ASP MET ASP SER LYS
SEQRES 13 B 263 MET LYS LYS MET ALA GLU LEU GLN LEU SER VAL VAL SER
SEQRES 14 B 263 ASP PRO LYS ASN ARG LYS ALA ILE GLU ASN GLN ILE ARG
SEQRES 15 B 263 GLN TRP GLU GLN ASN LEU GLU LYS PHE HIS MET ASP LEU
SEQRES 16 B 263 PHE ARG MET ARG CYS TYR LEU ALA SER LEU GLN GLY GLY
SEQRES 17 B 263 GLU LEU PRO ASN PRO LYS SER LEU LEU ALA ALA THR SER
SEQRES 18 B 263 ARG PRO SER LYS LEU ALA LEU GLY ARG LEU GLY VAL LEU
SEQRES 19 B 263 SER VAL SER SER PHE HIS ALA LEU VAL CYS SER ARG ASP
SEQRES 20 B 263 ASP SER THR LEU ARG LYS ARG THR LEU SER LEU THR GLN
SEQRES 21 B 263 ARG GLY LYS
SEQRES 1 C 263 GLY PRO LEU GLY SER LYS GLU GLN GLY VAL VAL ARG LYS
SEQRES 2 C 263 ALA GLY TRP LEU PHE PHE LYS PRO LEU VAL THR LEU GLN
SEQRES 3 C 263 LYS GLU ARG LYS LEU GLU LEU VAL ALA ARG ARG LYS TRP
SEQRES 4 C 263 LYS GLN TYR TRP VAL THR LEU LYS GLY CYS THR LEU LEU
SEQRES 5 C 263 PHE TYR GLU THR TYR GLY LYS ASN SER THR GLU GLN ASN
SEQRES 6 C 263 SER ALA PRO ARG CYS ALA LEU PHE ALA GLU ASP SER ILE
SEQRES 7 C 263 VAL GLN SER VAL PRO GLU HIS PRO LYS LYS GLU HIS VAL
SEQRES 8 C 263 PHE CYS LEU SER ASN SER CYS GLY ASP VAL TYR LEU PHE
SEQRES 9 C 263 GLN ALA THR SER GLN THR ASP LEU GLU ASN TRP VAL THR
SEQRES 10 C 263 ALA ILE HIS SER ALA CYS ALA SER LEU PHE ALA LYS LYS
SEQRES 11 C 263 HIS GLY LYS GLU ASP THR VAL ARG LEU LEU LYS SER GLN
SEQRES 12 C 263 THR ARG SER LEU LEU GLN LYS ILE ASP MET ASP SER LYS
SEQRES 13 C 263 MET LYS LYS MET ALA GLU LEU GLN LEU SER VAL VAL SER
SEQRES 14 C 263 ASP PRO LYS ASN ARG LYS ALA ILE GLU ASN GLN ILE ARG
SEQRES 15 C 263 GLN TRP GLU GLN ASN LEU GLU LYS PHE HIS MET ASP LEU
SEQRES 16 C 263 PHE ARG MET ARG CYS TYR LEU ALA SER LEU GLN GLY GLY
SEQRES 17 C 263 GLU LEU PRO ASN PRO LYS SER LEU LEU ALA ALA THR SER
SEQRES 18 C 263 ARG PRO SER LYS LEU ALA LEU GLY ARG LEU GLY VAL LEU
SEQRES 19 C 263 SER VAL SER SER PHE HIS ALA LEU VAL CYS SER ARG ASP
SEQRES 20 C 263 ASP SER THR LEU ARG LYS ARG THR LEU SER LEU THR GLN
SEQRES 21 C 263 ARG GLY LYS
SEQRES 1 D 263 GLY PRO LEU GLY SER LYS GLU GLN GLY VAL VAL ARG LYS
SEQRES 2 D 263 ALA GLY TRP LEU PHE PHE LYS PRO LEU VAL THR LEU GLN
SEQRES 3 D 263 LYS GLU ARG LYS LEU GLU LEU VAL ALA ARG ARG LYS TRP
SEQRES 4 D 263 LYS GLN TYR TRP VAL THR LEU LYS GLY CYS THR LEU LEU
SEQRES 5 D 263 PHE TYR GLU THR TYR GLY LYS ASN SER THR GLU GLN ASN
SEQRES 6 D 263 SER ALA PRO ARG CYS ALA LEU PHE ALA GLU ASP SER ILE
SEQRES 7 D 263 VAL GLN SER VAL PRO GLU HIS PRO LYS LYS GLU HIS VAL
SEQRES 8 D 263 PHE CYS LEU SER ASN SER CYS GLY ASP VAL TYR LEU PHE
SEQRES 9 D 263 GLN ALA THR SER GLN THR ASP LEU GLU ASN TRP VAL THR
SEQRES 10 D 263 ALA ILE HIS SER ALA CYS ALA SER LEU PHE ALA LYS LYS
SEQRES 11 D 263 HIS GLY LYS GLU ASP THR VAL ARG LEU LEU LYS SER GLN
SEQRES 12 D 263 THR ARG SER LEU LEU GLN LYS ILE ASP MET ASP SER LYS
SEQRES 13 D 263 MET LYS LYS MET ALA GLU LEU GLN LEU SER VAL VAL SER
SEQRES 14 D 263 ASP PRO LYS ASN ARG LYS ALA ILE GLU ASN GLN ILE ARG
SEQRES 15 D 263 GLN TRP GLU GLN ASN LEU GLU LYS PHE HIS MET ASP LEU
SEQRES 16 D 263 PHE ARG MET ARG CYS TYR LEU ALA SER LEU GLN GLY GLY
SEQRES 17 D 263 GLU LEU PRO ASN PRO LYS SER LEU LEU ALA ALA THR SER
SEQRES 18 D 263 ARG PRO SER LYS LEU ALA LEU GLY ARG LEU GLY VAL LEU
SEQRES 19 D 263 SER VAL SER SER PHE HIS ALA LEU VAL CYS SER ARG ASP
SEQRES 20 D 263 ASP SER THR LEU ARG LYS ARG THR LEU SER LEU THR GLN
SEQRES 21 D 263 ARG GLY LYS
FORMUL 5 HOH *383(H2 O)
HELIX 1 1 LYS A 521 ARG A 523 5 3
HELIX 2 2 SER A 602 HIS A 625 1 24
HELIX 3 3 ASP A 629 SER A 660 1 32
HELIX 4 4 ASP A 664 GLY A 701 1 38
HELIX 5 5 ASN A 706 ALA A 712 1 7
HELIX 6 6 SER A 715 GLY A 726 1 12
HELIX 7 7 SER A 729 ARG A 740 1 12
HELIX 8 8 SER B 602 HIS B 625 1 24
HELIX 9 9 ASP B 629 SER B 660 1 32
HELIX 10 10 ASP B 664 GLY B 701 1 38
HELIX 11 11 ASN B 706 ALA B 712 1 7
HELIX 12 12 SER B 715 ARG B 724 1 10
HELIX 13 13 SER B 729 SER B 739 1 11
HELIX 14 14 SER C 602 LYS C 624 1 23
HELIX 15 15 ASP C 629 VAL C 661 1 33
HELIX 16 16 LYS C 669 GLY C 701 1 33
HELIX 17 17 ASN C 706 ALA C 712 1 7
HELIX 18 18 SER C 715 GLY C 726 1 12
HELIX 19 19 SER C 729 ASP C 741 1 13
HELIX 20 20 SER D 602 HIS D 625 1 24
HELIX 21 21 ASP D 629 SER D 660 1 32
HELIX 22 22 ASP D 664 GLY D 701 1 38
HELIX 23 23 ASN D 706 ALA D 712 1 7
HELIX 24 24 SER D 715 GLY D 726 1 12
HELIX 25 25 SER D 729 ARG D 740 1 12
SHEET 1 A 5 LYS A 524 LEU A 527 0
SHEET 2 A 5 VAL A 505 GLN A 520 -1 N GLN A 520 O LYS A 524
SHEET 3 A 5 LYS A 534 LYS A 541 -1 O LEU A 540 N ARG A 506
SHEET 4 A 5 THR A 544 TYR A 548 -1 O TYR A 548 N TRP A 537
SHEET 5 A 5 CYS A 564 PHE A 567 -1 O LEU A 566 N LEU A 545
SHEET 1 B 5 LYS A 524 LEU A 527 0
SHEET 2 B 5 VAL A 505 GLN A 520 -1 N GLN A 520 O LYS A 524
SHEET 3 B 5 VAL A 595 GLN A 599 -1 O LEU A 597 N LYS A 514
SHEET 4 B 5 VAL A 585 SER A 589 -1 N LEU A 588 O TYR A 596
SHEET 5 B 5 ILE A 572 SER A 575 -1 N GLN A 574 O CYS A 587
SHEET 1 C 5 LYS B 524 LEU B 527 0
SHEET 2 C 5 VAL B 505 GLN B 520 -1 N THR B 518 O GLU B 526
SHEET 3 C 5 LYS B 534 LYS B 541 -1 O LEU B 540 N ARG B 506
SHEET 4 C 5 THR B 544 TYR B 548 -1 O LEU B 546 N THR B 539
SHEET 5 C 5 CYS B 564 PHE B 567 -1 O LEU B 566 N LEU B 545
SHEET 1 D 5 LYS B 524 LEU B 527 0
SHEET 2 D 5 VAL B 505 GLN B 520 -1 N THR B 518 O GLU B 526
SHEET 3 D 5 VAL B 595 GLN B 599 -1 O VAL B 595 N LEU B 516
SHEET 4 D 5 VAL B 585 SER B 589 -1 N LEU B 588 O TYR B 596
SHEET 5 D 5 ILE B 572 SER B 575 -1 N GLN B 574 O CYS B 587
SHEET 1 E 5 LYS C 524 LEU C 527 0
SHEET 2 E 5 VAL C 505 GLN C 520 -1 N GLN C 520 O LYS C 524
SHEET 3 E 5 LYS C 534 LYS C 541 -1 O LYS C 534 N PHE C 513
SHEET 4 E 5 THR C 544 TYR C 548 -1 O TYR C 548 N TRP C 537
SHEET 5 E 5 CYS C 564 PHE C 567 -1 O LEU C 566 N LEU C 545
SHEET 1 F 5 LYS C 524 LEU C 527 0
SHEET 2 F 5 VAL C 505 GLN C 520 -1 N GLN C 520 O LYS C 524
SHEET 3 F 5 VAL C 595 GLN C 599 -1 O VAL C 595 N VAL C 517
SHEET 4 F 5 VAL C 585 SER C 589 -1 N LEU C 588 O TYR C 596
SHEET 5 F 5 ILE C 572 SER C 575 -1 N GLN C 574 O CYS C 587
SHEET 1 G 5 LYS D 524 LEU D 527 0
SHEET 2 G 5 VAL D 505 GLN D 520 -1 N GLN D 520 O LYS D 524
SHEET 3 G 5 LYS D 534 LYS D 541 -1 O VAL D 538 N GLY D 509
SHEET 4 G 5 THR D 544 TYR D 548 -1 O LEU D 546 N THR D 539
SHEET 5 G 5 CYS D 564 PHE D 567 -1 O LEU D 566 N LEU D 545
SHEET 1 H 5 LYS D 524 LEU D 527 0
SHEET 2 H 5 VAL D 505 GLN D 520 -1 N GLN D 520 O LYS D 524
SHEET 3 H 5 VAL D 595 GLN D 599 -1 O VAL D 595 N LEU D 516
SHEET 4 H 5 VAL D 585 SER D 589 -1 N LEU D 588 O TYR D 596
SHEET 5 H 5 ILE D 572 SER D 575 -1 N GLN D 574 O CYS D 587
CRYST1 46.690 104.790 115.970 90.00 80.55 90.00 P 1 21 1 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 0.021418 0.000000 -0.003565 0.00000
SCALE2 0.000000 0.009543 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008742 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
