HEADER SIGNALING PROTEIN 01-APR-02 1LB1
TITLE CRYSTAL STRUCTURE OF THE DBL AND PLECKSTRIN HOMOLOGY DOMAINS OF DBS IN
TITLE 2 COMPLEX WITH RHOA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GUANINE NUCLEOTIDE EXCHANGE FACTOR DBS;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: DBL HOMOLOGY DOMAIN (RESIDUES 623-818) AND PLECKSTRIN
COMPND 5 HOMOLOGY DOMAIN (RESIDUES 819-967);
COMPND 6 SYNONYM: DBL'S BIG SISTER, DBS;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TRANSFORMING PROTEIN RHOA;
COMPND 10 CHAIN: B, D, F, H;
COMPND 11 FRAGMENT: RESIDUES 1-190;
COMPND 12 SYNONYM: H12;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: DBS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-28A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RHOA;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PPRO EX HT
KEYWDS GUANINE NUCLEOTIDE EXCHANGE FACTOR, SMALL G-PROTEIN, RHOA, DBS, DH
KEYWDS 2 DOMAIN, PH DOMAIN, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.T.SNYDER,D.K.WORTHYLAKE,K.L.ROSSMAN,L.BETTS,W.M.PRUITT,
AUTHOR 2 D.P.SIDEROVSKI,C.J.DER,J.SONDEK
REVDAT 4 16-AUG-23 1LB1 1 REMARK
REVDAT 3 27-OCT-21 1LB1 1 SEQADV
REVDAT 2 24-FEB-09 1LB1 1 VERSN
REVDAT 1 29-MAY-02 1LB1 0
JRNL AUTH J.T.SNYDER,D.K.WORTHYLAKE,K.L.ROSSMAN,L.BETTS,W.M.PRUITT,
JRNL AUTH 2 D.P.SIDEROVSKI,C.J.DER,J.SONDEK
JRNL TITL STRUCTURAL BASIS FOR THE SELECTIVE ACTIVATION OF RHO GTPASES
JRNL TITL 2 BY DBL EXCHANGE FACTORS.
JRNL REF NAT.STRUCT.BIOL. V. 9 468 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 12006984
JRNL DOI 10.1038/NSB796
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 93.7
REMARK 3 NUMBER OF REFLECTIONS : 85993
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) : 0.236
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4358
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.94
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 9880
REMARK 3 BIN R VALUE (WORKING SET) : 0.4030
REMARK 3 BIN FREE R VALUE : 0.4370
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 527
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.019
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16236
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 87.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.23000
REMARK 3 B22 (A**2) : -7.23000
REMARK 3 B33 (A**2) : 14.46000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.39
REMARK 3 ESD FROM SIGMAA (A) : 0.53
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) : 0.44
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.58
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 45.48
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 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LB1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-FEB-02
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85993
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.810
REMARK 200 RESOLUTION RANGE LOW (A) : 47.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
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: AMORE
REMARK 200 STARTING MODEL: DBS-CDC42 (PDB CODE 1KZ7)
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, LITHIUM CITRATE, INOSITOL
REMARK 280 1,4,5-TRISPHOSPHATE, PH 8.4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
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 75.89550
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 113.84325
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 37.94775
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23680 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 622
REMARK 465 GLY A 623
REMARK 465 HIS A 847
REMARK 465 THR A 848
REMARK 465 LYS A 849
REMARK 465 VAL A 850
REMARK 465 LYS A 851
REMARK 465 GLU A 852
REMARK 465 GLU A 954
REMARK 465 ALA A 955
REMARK 465 SER A 956
REMARK 465 GLN A 957
REMARK 465 HIS A 958
REMARK 465 ARG A 959
REMARK 465 ALA A 960
REMARK 465 LEU A 961
REMARK 465 GLU A 962
REMARK 465 GLN A 963
REMARK 465 SER A 964
REMARK 465 HIS A 965
REMARK 465 SER A 966
REMARK 465 LEU A 967
REMARK 465 GLU A 968
REMARK 465 HIS A 969
REMARK 465 HIS A 970
REMARK 465 HIS A 971
REMARK 465 HIS A 972
REMARK 465 HIS A 973
REMARK 465 HIS A 974
REMARK 465 GLY B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 181
REMARK 465 ARG B 182
REMARK 465 ARG B 183
REMARK 465 GLY B 184
REMARK 465 LYS B 185
REMARK 465 LYS B 186
REMARK 465 LYS B 187
REMARK 465 SER B 188
REMARK 465 GLY B 189
REMARK 465 SER B 190
REMARK 465 MET C 622
REMARK 465 GLY C 623
REMARK 465 HIS C 847
REMARK 465 THR C 848
REMARK 465 LYS C 849
REMARK 465 VAL C 850
REMARK 465 LYS C 851
REMARK 465 GLU C 852
REMARK 465 GLU C 954
REMARK 465 ALA C 955
REMARK 465 SER C 956
REMARK 465 GLN C 957
REMARK 465 HIS C 958
REMARK 465 ARG C 959
REMARK 465 ALA C 960
REMARK 465 LEU C 961
REMARK 465 GLU C 962
REMARK 465 GLN C 963
REMARK 465 SER C 964
REMARK 465 HIS C 965
REMARK 465 SER C 966
REMARK 465 LEU C 967
REMARK 465 GLU C 968
REMARK 465 HIS C 969
REMARK 465 HIS C 970
REMARK 465 HIS C 971
REMARK 465 HIS C 972
REMARK 465 HIS C 973
REMARK 465 HIS C 974
REMARK 465 GLY D -1
REMARK 465 ALA D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 ALA D 181
REMARK 465 ARG D 182
REMARK 465 ARG D 183
REMARK 465 GLY D 184
REMARK 465 LYS D 185
REMARK 465 LYS D 186
REMARK 465 LYS D 187
REMARK 465 SER D 188
REMARK 465 GLY D 189
REMARK 465 SER D 190
REMARK 465 MET E 622
REMARK 465 GLY E 623
REMARK 465 HIS E 847
REMARK 465 THR E 848
REMARK 465 LYS E 849
REMARK 465 VAL E 850
REMARK 465 LYS E 851
REMARK 465 GLU E 852
REMARK 465 GLU E 954
REMARK 465 ALA E 955
REMARK 465 SER E 956
REMARK 465 GLN E 957
REMARK 465 HIS E 958
REMARK 465 ARG E 959
REMARK 465 ALA E 960
REMARK 465 LEU E 961
REMARK 465 GLU E 962
REMARK 465 GLN E 963
REMARK 465 SER E 964
REMARK 465 HIS E 965
REMARK 465 SER E 966
REMARK 465 LEU E 967
REMARK 465 GLU E 968
REMARK 465 HIS E 969
REMARK 465 HIS E 970
REMARK 465 HIS E 971
REMARK 465 HIS E 972
REMARK 465 HIS E 973
REMARK 465 HIS E 974
REMARK 465 GLY F -1
REMARK 465 ALA F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 ALA F 181
REMARK 465 ARG F 182
REMARK 465 ARG F 183
REMARK 465 GLY F 184
REMARK 465 LYS F 185
REMARK 465 LYS F 186
REMARK 465 LYS F 187
REMARK 465 SER F 188
REMARK 465 GLY F 189
REMARK 465 SER F 190
REMARK 465 MET G 622
REMARK 465 GLY G 623
REMARK 465 HIS G 847
REMARK 465 THR G 848
REMARK 465 LYS G 849
REMARK 465 VAL G 850
REMARK 465 LYS G 851
REMARK 465 GLU G 852
REMARK 465 GLU G 954
REMARK 465 ALA G 955
REMARK 465 SER G 956
REMARK 465 GLN G 957
REMARK 465 HIS G 958
REMARK 465 ARG G 959
REMARK 465 ALA G 960
REMARK 465 LEU G 961
REMARK 465 GLU G 962
REMARK 465 GLN G 963
REMARK 465 SER G 964
REMARK 465 HIS G 965
REMARK 465 SER G 966
REMARK 465 LEU G 967
REMARK 465 GLU G 968
REMARK 465 HIS G 969
REMARK 465 HIS G 970
REMARK 465 HIS G 971
REMARK 465 HIS G 972
REMARK 465 HIS G 973
REMARK 465 HIS G 974
REMARK 465 GLY H -1
REMARK 465 ALA H 0
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 ALA H 181
REMARK 465 ARG H 182
REMARK 465 ARG H 183
REMARK 465 GLY H 184
REMARK 465 LYS H 185
REMARK 465 LYS H 186
REMARK 465 LYS H 187
REMARK 465 SER H 188
REMARK 465 GLY H 189
REMARK 465 SER H 190
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ARG C 953 OE2 GLU G 627 3554 2.13
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 TYR A 658 -63.23 -134.93
REMARK 500 ILE A 696 -62.57 -123.10
REMARK 500 ASP A 842 51.04 -159.18
REMARK 500 ALA A 854 30.66 102.85
REMARK 500 LYS A 892 -85.58 -112.92
REMARK 500 ASN A 918 88.88 35.74
REMARK 500 ALA A 919 20.51 49.33
REMARK 500 CYS A 952 22.91 -78.44
REMARK 500 GLN B 29 123.54 -172.73
REMARK 500 ASN B 41 116.43 -35.72
REMARK 500 ASP B 87 35.90 -92.65
REMARK 500 SER B 88 85.31 -158.31
REMARK 500 LYS B 98 -71.22 -115.22
REMARK 500 PRO B 138 161.93 -45.40
REMARK 500 TYR C 658 -63.10 -134.04
REMARK 500 ILE C 696 -62.44 -123.27
REMARK 500 ASP C 842 49.90 -160.07
REMARK 500 ALA C 854 28.80 103.26
REMARK 500 LYS C 892 -86.23 -112.53
REMARK 500 ASN C 918 87.77 34.68
REMARK 500 ALA C 919 19.55 50.80
REMARK 500 CYS C 952 22.35 -79.08
REMARK 500 GLN D 29 124.53 -172.00
REMARK 500 ASN D 41 117.70 -37.48
REMARK 500 ASP D 87 35.99 -94.12
REMARK 500 SER D 88 85.36 -158.48
REMARK 500 LYS D 98 -71.30 -117.25
REMARK 500 PRO D 138 161.97 -45.62
REMARK 500 TYR E 658 -63.26 -132.48
REMARK 500 ILE E 696 -63.57 -123.44
REMARK 500 ASP E 842 49.45 -160.54
REMARK 500 ALA E 854 29.83 104.80
REMARK 500 LYS E 892 -86.00 -111.74
REMARK 500 ASN E 918 88.02 35.75
REMARK 500 CYS E 952 23.32 -77.41
REMARK 500 GLN F 29 123.72 -172.76
REMARK 500 ASN F 41 117.81 -36.22
REMARK 500 ASP F 87 36.42 -92.67
REMARK 500 SER F 88 86.33 -159.08
REMARK 500 PRO F 138 162.29 -45.62
REMARK 500 TYR G 658 -64.19 -133.85
REMARK 500 ILE G 696 -62.94 -124.34
REMARK 500 ASP G 842 50.05 -160.03
REMARK 500 ALA G 854 30.42 103.79
REMARK 500 LYS G 892 -86.68 -111.88
REMARK 500 ASN G 918 88.65 35.17
REMARK 500 ALA G 919 20.73 49.65
REMARK 500 CYS G 952 22.55 -77.91
REMARK 500 GLN H 29 124.00 -172.69
REMARK 500 ASN H 41 116.97 -37.50
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DH/PH FRAGMENT OF MURINE DBS IN COMPLEX
REMARK 900 WITH THE PLACENTAL ISOFORM OF HUMAN CDC42
REMARK 900 RELATED ID: 1KZG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DH/PH FRAGMENT (Y889F MUTANT)OF MURINE DBS
REMARK 900 IN COMPLEX WITH THE PLACENTAL ISOFORM OF HUMAN CDC42
REMARK 900 RELATED ID: 1FOE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DH/PH FRAGMENT OF MURINE TIAM1 IN COMPLEX
REMARK 900 WITH HUMAN RAC1
REMARK 900 RELATED ID: 1KI1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DH/PH FRAGMENT OF INTERSECTIN IN COMPLEX
REMARK 900 WITH THE PLACENTAL ISOFORM OF HUMAN CDC42
DBREF 1LB1 A 623 967 UNP Q64096 MCF2L_MOUSE 623 967
DBREF 1LB1 C 623 967 UNP Q64096 MCF2L_MOUSE 623 967
DBREF 1LB1 E 623 967 UNP Q64096 MCF2L_MOUSE 623 967
DBREF 1LB1 G 623 967 UNP Q64096 MCF2L_MOUSE 623 967
DBREF 1LB1 B 1 190 UNP P61586 RHOA_HUMAN 1 190
DBREF 1LB1 D 1 190 UNP P61586 RHOA_HUMAN 1 190
DBREF 1LB1 F 1 190 UNP P61586 RHOA_HUMAN 1 190
DBREF 1LB1 H 1 190 UNP P61586 RHOA_HUMAN 1 190
SEQADV 1LB1 MET A 622 UNP Q64096 SEE REMARK 999
SEQADV 1LB1 ILE A 696 UNP Q64096 ASN 696 SEE REMARK 999
SEQADV 1LB1 PHE A 697 UNP Q64096 ILE 697 SEE REMARK 999
SEQADV 1LB1 LEU A 698 UNP Q64096 PRO 698 SEE REMARK 999
SEQADV 1LB1 ARG A 699 UNP Q64096 ALA 699 SEE REMARK 999
SEQADV 1LB1 GLU A 700 UNP Q64096 GLY 700 SEE REMARK 999
SEQADV 1LB1 LEU A 701 UNP Q64096 VAL 701 SEE REMARK 999
SEQADV 1LB1 GLU A 968 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS A 969 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS A 970 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS A 971 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS A 972 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS A 973 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS A 974 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 MET C 622 UNP Q64096 SEE REMARK 999
SEQADV 1LB1 ILE C 696 UNP Q64096 ASN 696 SEE REMARK 999
SEQADV 1LB1 PHE C 697 UNP Q64096 ILE 697 SEE REMARK 999
SEQADV 1LB1 LEU C 698 UNP Q64096 PRO 698 SEE REMARK 999
SEQADV 1LB1 ARG C 699 UNP Q64096 ALA 699 SEE REMARK 999
SEQADV 1LB1 GLU C 700 UNP Q64096 GLY 700 SEE REMARK 999
SEQADV 1LB1 LEU C 701 UNP Q64096 VAL 701 SEE REMARK 999
SEQADV 1LB1 GLU C 968 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS C 969 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS C 970 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS C 971 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS C 972 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS C 973 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS C 974 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 MET E 622 UNP Q64096 SEE REMARK 999
SEQADV 1LB1 ILE E 696 UNP Q64096 ASN 696 SEE REMARK 999
SEQADV 1LB1 PHE E 697 UNP Q64096 ILE 697 SEE REMARK 999
SEQADV 1LB1 LEU E 698 UNP Q64096 PRO 698 SEE REMARK 999
SEQADV 1LB1 ARG E 699 UNP Q64096 ALA 699 SEE REMARK 999
SEQADV 1LB1 GLU E 700 UNP Q64096 GLY 700 SEE REMARK 999
SEQADV 1LB1 LEU E 701 UNP Q64096 VAL 701 SEE REMARK 999
SEQADV 1LB1 GLU E 968 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS E 969 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS E 970 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS E 971 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS E 972 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS E 973 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS E 974 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 MET G 622 UNP Q64096 SEE REMARK 999
SEQADV 1LB1 ILE G 696 UNP Q64096 ASN 696 SEE REMARK 999
SEQADV 1LB1 PHE G 697 UNP Q64096 ILE 697 SEE REMARK 999
SEQADV 1LB1 LEU G 698 UNP Q64096 PRO 698 SEE REMARK 999
SEQADV 1LB1 ARG G 699 UNP Q64096 ALA 699 SEE REMARK 999
SEQADV 1LB1 GLU G 700 UNP Q64096 GLY 700 SEE REMARK 999
SEQADV 1LB1 LEU G 701 UNP Q64096 VAL 701 SEE REMARK 999
SEQADV 1LB1 GLU G 968 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS G 969 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS G 970 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS G 971 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS G 972 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS G 973 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 HIS G 974 UNP Q64096 EXPRESSION TAG
SEQADV 1LB1 GLY B -1 UNP P61586 SEE REMARK 999
SEQADV 1LB1 ALA B 0 UNP P61586 SEE REMARK 999
SEQADV 1LB1 SER B 190 UNP P61586 CYS 190 ENGINEERED MUTATION
SEQADV 1LB1 GLY D -1 UNP P61586 SEE REMARK 999
SEQADV 1LB1 ALA D 0 UNP P61586 SEE REMARK 999
SEQADV 1LB1 SER D 190 UNP P61586 CYS 190 ENGINEERED MUTATION
SEQADV 1LB1 GLY F -1 UNP P61586 SEE REMARK 999
SEQADV 1LB1 ALA F 0 UNP P61586 SEE REMARK 999
SEQADV 1LB1 SER F 190 UNP P61586 CYS 190 ENGINEERED MUTATION
SEQADV 1LB1 GLY H -1 UNP P61586 SEE REMARK 999
SEQADV 1LB1 ALA H 0 UNP P61586 SEE REMARK 999
SEQADV 1LB1 SER H 190 UNP P61586 CYS 190 ENGINEERED MUTATION
SEQRES 1 A 353 MET GLY GLU GLU GLU GLU SER LEU ALA ILE LEU ARG ARG
SEQRES 2 A 353 HIS VAL MET ASN GLU LEU LEU ASP THR GLU ARG ALA TYR
SEQRES 3 A 353 VAL GLU GLU LEU LEU CYS VAL LEU GLU GLY TYR ALA ALA
SEQRES 4 A 353 GLU MET ASP ASN PRO LEU MET ALA HIS LEU ILE SER THR
SEQRES 5 A 353 GLY LEU GLN ASN LYS LYS ASN ILE LEU PHE GLY ASN MET
SEQRES 6 A 353 GLU GLU ILE TYR HIS PHE HIS ASN ARG ILE PHE LEU ARG
SEQRES 7 A 353 GLU LEU GLU SER CYS ILE ASP CYS PRO GLU LEU VAL GLY
SEQRES 8 A 353 ARG CYS PHE LEU GLU ARG MET GLU GLU PHE GLN ILE TYR
SEQRES 9 A 353 GLU LYS TYR CYS GLN ASN LYS PRO ARG SER GLU SER LEU
SEQRES 10 A 353 TRP ARG GLN CYS SER ASP CYS PRO PHE PHE GLN GLU CYS
SEQRES 11 A 353 GLN LYS LYS LEU ASP HIS LYS LEU SER LEU ASP SER TYR
SEQRES 12 A 353 LEU LEU LYS PRO VAL GLN ARG ILE THR LYS TYR GLN LEU
SEQRES 13 A 353 LEU LEU LYS GLU MET LEU LYS TYR SER LYS HIS CYS GLU
SEQRES 14 A 353 GLY ALA GLU ASP LEU GLN GLU ALA LEU SER SER ILE LEU
SEQRES 15 A 353 GLY ILE LEU LYS ALA VAL ASN ASP SER MET HIS LEU ILE
SEQRES 16 A 353 ALA ILE THR GLY TYR ASP GLY ASN LEU GLY ASP LEU GLY
SEQRES 17 A 353 LYS LEU LEU MET GLN GLY SER PHE SER VAL TRP THR ASP
SEQRES 18 A 353 HIS LYS LYS GLY HIS THR LYS VAL LYS GLU LEU ALA ARG
SEQRES 19 A 353 PHE LYS PRO MET GLN ARG HIS LEU PHE LEU HIS GLU LYS
SEQRES 20 A 353 ALA VAL LEU PHE CYS LYS LYS ARG GLU GLU ASN GLY GLU
SEQRES 21 A 353 GLY TYR GLU LYS ALA PRO SER TYR SER TYR LYS GLN SER
SEQRES 22 A 353 LEU ASN MET THR ALA VAL GLY ILE THR GLU ASN VAL LYS
SEQRES 23 A 353 GLY ASP THR LYS LYS PHE GLU ILE TRP TYR ASN ALA ARG
SEQRES 24 A 353 GLU GLU VAL TYR ILE ILE GLN ALA PRO THR PRO GLU ILE
SEQRES 25 A 353 LYS ALA ALA TRP VAL ASN GLU ILE ARG LYS VAL LEU THR
SEQRES 26 A 353 SER GLN LEU GLN ALA CYS ARG GLU ALA SER GLN HIS ARG
SEQRES 27 A 353 ALA LEU GLU GLN SER HIS SER LEU GLU HIS HIS HIS HIS
SEQRES 28 A 353 HIS HIS
SEQRES 1 B 192 GLY ALA MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL
SEQRES 2 B 192 GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL
SEQRES 3 B 192 PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR
SEQRES 4 B 192 VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY
SEQRES 5 B 192 LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN
SEQRES 6 B 192 GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP
SEQRES 7 B 192 THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO
SEQRES 8 B 192 ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU
SEQRES 9 B 192 VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL
SEQRES 10 B 192 GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG
SEQRES 11 B 192 ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO
SEQRES 12 B 192 GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE
SEQRES 13 B 192 GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL
SEQRES 14 B 192 ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN
SEQRES 15 B 192 ALA ARG ARG GLY LYS LYS LYS SER GLY SER
SEQRES 1 C 353 MET GLY GLU GLU GLU GLU SER LEU ALA ILE LEU ARG ARG
SEQRES 2 C 353 HIS VAL MET ASN GLU LEU LEU ASP THR GLU ARG ALA TYR
SEQRES 3 C 353 VAL GLU GLU LEU LEU CYS VAL LEU GLU GLY TYR ALA ALA
SEQRES 4 C 353 GLU MET ASP ASN PRO LEU MET ALA HIS LEU ILE SER THR
SEQRES 5 C 353 GLY LEU GLN ASN LYS LYS ASN ILE LEU PHE GLY ASN MET
SEQRES 6 C 353 GLU GLU ILE TYR HIS PHE HIS ASN ARG ILE PHE LEU ARG
SEQRES 7 C 353 GLU LEU GLU SER CYS ILE ASP CYS PRO GLU LEU VAL GLY
SEQRES 8 C 353 ARG CYS PHE LEU GLU ARG MET GLU GLU PHE GLN ILE TYR
SEQRES 9 C 353 GLU LYS TYR CYS GLN ASN LYS PRO ARG SER GLU SER LEU
SEQRES 10 C 353 TRP ARG GLN CYS SER ASP CYS PRO PHE PHE GLN GLU CYS
SEQRES 11 C 353 GLN LYS LYS LEU ASP HIS LYS LEU SER LEU ASP SER TYR
SEQRES 12 C 353 LEU LEU LYS PRO VAL GLN ARG ILE THR LYS TYR GLN LEU
SEQRES 13 C 353 LEU LEU LYS GLU MET LEU LYS TYR SER LYS HIS CYS GLU
SEQRES 14 C 353 GLY ALA GLU ASP LEU GLN GLU ALA LEU SER SER ILE LEU
SEQRES 15 C 353 GLY ILE LEU LYS ALA VAL ASN ASP SER MET HIS LEU ILE
SEQRES 16 C 353 ALA ILE THR GLY TYR ASP GLY ASN LEU GLY ASP LEU GLY
SEQRES 17 C 353 LYS LEU LEU MET GLN GLY SER PHE SER VAL TRP THR ASP
SEQRES 18 C 353 HIS LYS LYS GLY HIS THR LYS VAL LYS GLU LEU ALA ARG
SEQRES 19 C 353 PHE LYS PRO MET GLN ARG HIS LEU PHE LEU HIS GLU LYS
SEQRES 20 C 353 ALA VAL LEU PHE CYS LYS LYS ARG GLU GLU ASN GLY GLU
SEQRES 21 C 353 GLY TYR GLU LYS ALA PRO SER TYR SER TYR LYS GLN SER
SEQRES 22 C 353 LEU ASN MET THR ALA VAL GLY ILE THR GLU ASN VAL LYS
SEQRES 23 C 353 GLY ASP THR LYS LYS PHE GLU ILE TRP TYR ASN ALA ARG
SEQRES 24 C 353 GLU GLU VAL TYR ILE ILE GLN ALA PRO THR PRO GLU ILE
SEQRES 25 C 353 LYS ALA ALA TRP VAL ASN GLU ILE ARG LYS VAL LEU THR
SEQRES 26 C 353 SER GLN LEU GLN ALA CYS ARG GLU ALA SER GLN HIS ARG
SEQRES 27 C 353 ALA LEU GLU GLN SER HIS SER LEU GLU HIS HIS HIS HIS
SEQRES 28 C 353 HIS HIS
SEQRES 1 D 192 GLY ALA MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL
SEQRES 2 D 192 GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL
SEQRES 3 D 192 PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR
SEQRES 4 D 192 VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY
SEQRES 5 D 192 LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN
SEQRES 6 D 192 GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP
SEQRES 7 D 192 THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO
SEQRES 8 D 192 ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU
SEQRES 9 D 192 VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL
SEQRES 10 D 192 GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG
SEQRES 11 D 192 ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO
SEQRES 12 D 192 GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE
SEQRES 13 D 192 GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL
SEQRES 14 D 192 ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN
SEQRES 15 D 192 ALA ARG ARG GLY LYS LYS LYS SER GLY SER
SEQRES 1 E 353 MET GLY GLU GLU GLU GLU SER LEU ALA ILE LEU ARG ARG
SEQRES 2 E 353 HIS VAL MET ASN GLU LEU LEU ASP THR GLU ARG ALA TYR
SEQRES 3 E 353 VAL GLU GLU LEU LEU CYS VAL LEU GLU GLY TYR ALA ALA
SEQRES 4 E 353 GLU MET ASP ASN PRO LEU MET ALA HIS LEU ILE SER THR
SEQRES 5 E 353 GLY LEU GLN ASN LYS LYS ASN ILE LEU PHE GLY ASN MET
SEQRES 6 E 353 GLU GLU ILE TYR HIS PHE HIS ASN ARG ILE PHE LEU ARG
SEQRES 7 E 353 GLU LEU GLU SER CYS ILE ASP CYS PRO GLU LEU VAL GLY
SEQRES 8 E 353 ARG CYS PHE LEU GLU ARG MET GLU GLU PHE GLN ILE TYR
SEQRES 9 E 353 GLU LYS TYR CYS GLN ASN LYS PRO ARG SER GLU SER LEU
SEQRES 10 E 353 TRP ARG GLN CYS SER ASP CYS PRO PHE PHE GLN GLU CYS
SEQRES 11 E 353 GLN LYS LYS LEU ASP HIS LYS LEU SER LEU ASP SER TYR
SEQRES 12 E 353 LEU LEU LYS PRO VAL GLN ARG ILE THR LYS TYR GLN LEU
SEQRES 13 E 353 LEU LEU LYS GLU MET LEU LYS TYR SER LYS HIS CYS GLU
SEQRES 14 E 353 GLY ALA GLU ASP LEU GLN GLU ALA LEU SER SER ILE LEU
SEQRES 15 E 353 GLY ILE LEU LYS ALA VAL ASN ASP SER MET HIS LEU ILE
SEQRES 16 E 353 ALA ILE THR GLY TYR ASP GLY ASN LEU GLY ASP LEU GLY
SEQRES 17 E 353 LYS LEU LEU MET GLN GLY SER PHE SER VAL TRP THR ASP
SEQRES 18 E 353 HIS LYS LYS GLY HIS THR LYS VAL LYS GLU LEU ALA ARG
SEQRES 19 E 353 PHE LYS PRO MET GLN ARG HIS LEU PHE LEU HIS GLU LYS
SEQRES 20 E 353 ALA VAL LEU PHE CYS LYS LYS ARG GLU GLU ASN GLY GLU
SEQRES 21 E 353 GLY TYR GLU LYS ALA PRO SER TYR SER TYR LYS GLN SER
SEQRES 22 E 353 LEU ASN MET THR ALA VAL GLY ILE THR GLU ASN VAL LYS
SEQRES 23 E 353 GLY ASP THR LYS LYS PHE GLU ILE TRP TYR ASN ALA ARG
SEQRES 24 E 353 GLU GLU VAL TYR ILE ILE GLN ALA PRO THR PRO GLU ILE
SEQRES 25 E 353 LYS ALA ALA TRP VAL ASN GLU ILE ARG LYS VAL LEU THR
SEQRES 26 E 353 SER GLN LEU GLN ALA CYS ARG GLU ALA SER GLN HIS ARG
SEQRES 27 E 353 ALA LEU GLU GLN SER HIS SER LEU GLU HIS HIS HIS HIS
SEQRES 28 E 353 HIS HIS
SEQRES 1 F 192 GLY ALA MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL
SEQRES 2 F 192 GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL
SEQRES 3 F 192 PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR
SEQRES 4 F 192 VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY
SEQRES 5 F 192 LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN
SEQRES 6 F 192 GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP
SEQRES 7 F 192 THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO
SEQRES 8 F 192 ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU
SEQRES 9 F 192 VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL
SEQRES 10 F 192 GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG
SEQRES 11 F 192 ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO
SEQRES 12 F 192 GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE
SEQRES 13 F 192 GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL
SEQRES 14 F 192 ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN
SEQRES 15 F 192 ALA ARG ARG GLY LYS LYS LYS SER GLY SER
SEQRES 1 G 353 MET GLY GLU GLU GLU GLU SER LEU ALA ILE LEU ARG ARG
SEQRES 2 G 353 HIS VAL MET ASN GLU LEU LEU ASP THR GLU ARG ALA TYR
SEQRES 3 G 353 VAL GLU GLU LEU LEU CYS VAL LEU GLU GLY TYR ALA ALA
SEQRES 4 G 353 GLU MET ASP ASN PRO LEU MET ALA HIS LEU ILE SER THR
SEQRES 5 G 353 GLY LEU GLN ASN LYS LYS ASN ILE LEU PHE GLY ASN MET
SEQRES 6 G 353 GLU GLU ILE TYR HIS PHE HIS ASN ARG ILE PHE LEU ARG
SEQRES 7 G 353 GLU LEU GLU SER CYS ILE ASP CYS PRO GLU LEU VAL GLY
SEQRES 8 G 353 ARG CYS PHE LEU GLU ARG MET GLU GLU PHE GLN ILE TYR
SEQRES 9 G 353 GLU LYS TYR CYS GLN ASN LYS PRO ARG SER GLU SER LEU
SEQRES 10 G 353 TRP ARG GLN CYS SER ASP CYS PRO PHE PHE GLN GLU CYS
SEQRES 11 G 353 GLN LYS LYS LEU ASP HIS LYS LEU SER LEU ASP SER TYR
SEQRES 12 G 353 LEU LEU LYS PRO VAL GLN ARG ILE THR LYS TYR GLN LEU
SEQRES 13 G 353 LEU LEU LYS GLU MET LEU LYS TYR SER LYS HIS CYS GLU
SEQRES 14 G 353 GLY ALA GLU ASP LEU GLN GLU ALA LEU SER SER ILE LEU
SEQRES 15 G 353 GLY ILE LEU LYS ALA VAL ASN ASP SER MET HIS LEU ILE
SEQRES 16 G 353 ALA ILE THR GLY TYR ASP GLY ASN LEU GLY ASP LEU GLY
SEQRES 17 G 353 LYS LEU LEU MET GLN GLY SER PHE SER VAL TRP THR ASP
SEQRES 18 G 353 HIS LYS LYS GLY HIS THR LYS VAL LYS GLU LEU ALA ARG
SEQRES 19 G 353 PHE LYS PRO MET GLN ARG HIS LEU PHE LEU HIS GLU LYS
SEQRES 20 G 353 ALA VAL LEU PHE CYS LYS LYS ARG GLU GLU ASN GLY GLU
SEQRES 21 G 353 GLY TYR GLU LYS ALA PRO SER TYR SER TYR LYS GLN SER
SEQRES 22 G 353 LEU ASN MET THR ALA VAL GLY ILE THR GLU ASN VAL LYS
SEQRES 23 G 353 GLY ASP THR LYS LYS PHE GLU ILE TRP TYR ASN ALA ARG
SEQRES 24 G 353 GLU GLU VAL TYR ILE ILE GLN ALA PRO THR PRO GLU ILE
SEQRES 25 G 353 LYS ALA ALA TRP VAL ASN GLU ILE ARG LYS VAL LEU THR
SEQRES 26 G 353 SER GLN LEU GLN ALA CYS ARG GLU ALA SER GLN HIS ARG
SEQRES 27 G 353 ALA LEU GLU GLN SER HIS SER LEU GLU HIS HIS HIS HIS
SEQRES 28 G 353 HIS HIS
SEQRES 1 H 192 GLY ALA MET ALA ALA ILE ARG LYS LYS LEU VAL ILE VAL
SEQRES 2 H 192 GLY ASP GLY ALA CYS GLY LYS THR CYS LEU LEU ILE VAL
SEQRES 3 H 192 PHE SER LYS ASP GLN PHE PRO GLU VAL TYR VAL PRO THR
SEQRES 4 H 192 VAL PHE GLU ASN TYR VAL ALA ASP ILE GLU VAL ASP GLY
SEQRES 5 H 192 LYS GLN VAL GLU LEU ALA LEU TRP ASP THR ALA GLY GLN
SEQRES 6 H 192 GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO ASP
SEQRES 7 H 192 THR ASP VAL ILE LEU MET CYS PHE SER ILE ASP SER PRO
SEQRES 8 H 192 ASP SER LEU GLU ASN ILE PRO GLU LYS TRP THR PRO GLU
SEQRES 9 H 192 VAL LYS HIS PHE CYS PRO ASN VAL PRO ILE ILE LEU VAL
SEQRES 10 H 192 GLY ASN LYS LYS ASP LEU ARG ASN ASP GLU HIS THR ARG
SEQRES 11 H 192 ARG GLU LEU ALA LYS MET LYS GLN GLU PRO VAL LYS PRO
SEQRES 12 H 192 GLU GLU GLY ARG ASP MET ALA ASN ARG ILE GLY ALA PHE
SEQRES 13 H 192 GLY TYR MET GLU CYS SER ALA LYS THR LYS ASP GLY VAL
SEQRES 14 H 192 ARG GLU VAL PHE GLU MET ALA THR ARG ALA ALA LEU GLN
SEQRES 15 H 192 ALA ARG ARG GLY LYS LYS LYS SER GLY SER
HELIX 1 1 GLU A 624 TYR A 658 1 35
HELIX 2 2 ALA A 659 ILE A 671 5 13
HELIX 3 3 SER A 672 LYS A 678 1 7
HELIX 4 4 LYS A 678 GLY A 684 1 7
HELIX 5 5 ASN A 685 ILE A 696 1 12
HELIX 6 6 ILE A 696 SER A 703 1 8
HELIX 7 7 CYS A 707 LEU A 710 5 4
HELIX 8 8 VAL A 711 GLU A 717 1 7
HELIX 9 9 ARG A 718 MET A 719 5 2
HELIX 10 10 GLU A 720 PHE A 722 5 3
HELIX 11 11 GLN A 723 SER A 743 1 21
HELIX 12 12 CYS A 745 ASP A 756 1 12
HELIX 13 13 SER A 760 LEU A 766 1 7
HELIX 14 14 LEU A 766 THR A 773 1 8
HELIX 15 15 LYS A 774 TYR A 785 1 12
HELIX 16 16 GLY A 791 ILE A 816 1 26
HELIX 17 17 LEU A 825 GLY A 829 5 5
HELIX 18 18 GLY A 882 ALA A 886 5 5
HELIX 19 19 THR A 930 CYS A 952 1 23
HELIX 20 20 GLY B 17 ASP B 28 1 12
HELIX 21 21 LEU B 69 TYR B 74 5 6
HELIX 22 22 SER B 88 LYS B 98 1 11
HELIX 23 23 LYS B 98 CYS B 107 1 10
HELIX 24 24 LYS B 118 ARG B 122 5 5
HELIX 25 25 ASP B 124 MET B 134 1 11
HELIX 26 26 LYS B 140 GLY B 152 1 13
HELIX 27 27 GLY B 166 GLN B 180 1 15
HELIX 28 28 GLU C 624 TYR C 658 1 35
HELIX 29 29 ALA C 659 ILE C 671 5 13
HELIX 30 30 SER C 672 LYS C 678 1 7
HELIX 31 31 LYS C 678 GLY C 684 1 7
HELIX 32 32 ASN C 685 ILE C 696 1 12
HELIX 33 33 ILE C 696 SER C 703 1 8
HELIX 34 34 CYS C 707 GLU C 709 5 3
HELIX 35 35 LEU C 710 GLU C 717 1 8
HELIX 36 36 ARG C 718 MET C 719 5 2
HELIX 37 37 GLU C 720 PHE C 722 5 3
HELIX 38 38 GLN C 723 SER C 743 1 21
HELIX 39 39 CYS C 745 ASP C 756 1 12
HELIX 40 40 SER C 760 LEU C 766 1 7
HELIX 41 41 LEU C 766 THR C 773 1 8
HELIX 42 42 LYS C 774 TYR C 785 1 12
HELIX 43 43 GLY C 791 ILE C 816 1 26
HELIX 44 44 LEU C 825 GLY C 829 5 5
HELIX 45 45 GLY C 882 ALA C 886 5 5
HELIX 46 46 THR C 930 CYS C 952 1 23
HELIX 47 47 GLY D 17 ASP D 28 1 12
HELIX 48 48 LEU D 69 TYR D 74 5 6
HELIX 49 49 SER D 88 LYS D 98 1 11
HELIX 50 50 LYS D 98 CYS D 107 1 10
HELIX 51 51 LYS D 118 ARG D 122 5 5
HELIX 52 52 ASP D 124 MET D 134 1 11
HELIX 53 53 LYS D 140 GLY D 152 1 13
HELIX 54 54 GLY D 166 GLN D 180 1 15
HELIX 55 55 GLU E 624 TYR E 658 1 35
HELIX 56 56 ALA E 659 ILE E 671 5 13
HELIX 57 57 SER E 672 LYS E 678 1 7
HELIX 58 58 LYS E 678 GLY E 684 1 7
HELIX 59 59 ASN E 685 ILE E 696 1 12
HELIX 60 60 ILE E 696 SER E 703 1 8
HELIX 61 61 CYS E 707 LEU E 710 5 4
HELIX 62 62 VAL E 711 GLU E 717 1 7
HELIX 63 63 ARG E 718 MET E 719 5 2
HELIX 64 64 GLU E 720 PHE E 722 5 3
HELIX 65 65 GLN E 723 SER E 743 1 21
HELIX 66 66 CYS E 745 ASP E 756 1 12
HELIX 67 67 SER E 760 LEU E 766 1 7
HELIX 68 68 LEU E 766 THR E 773 1 8
HELIX 69 69 LYS E 774 TYR E 785 1 12
HELIX 70 70 GLY E 791 ILE E 816 1 26
HELIX 71 71 LEU E 825 GLY E 829 5 5
HELIX 72 72 GLY E 882 ALA E 886 5 5
HELIX 73 73 THR E 930 CYS E 952 1 23
HELIX 74 74 GLY F 17 ASP F 28 1 12
HELIX 75 75 LEU F 69 TYR F 74 5 6
HELIX 76 76 SER F 88 LYS F 98 1 11
HELIX 77 77 LYS F 98 CYS F 107 1 10
HELIX 78 78 LYS F 118 ARG F 122 5 5
HELIX 79 79 ASP F 124 MET F 134 1 11
HELIX 80 80 LYS F 140 GLY F 152 1 13
HELIX 81 81 GLY F 166 GLN F 180 1 15
HELIX 82 82 GLU G 624 TYR G 658 1 35
HELIX 83 83 ALA G 659 ILE G 671 5 13
HELIX 84 84 SER G 672 LYS G 678 1 7
HELIX 85 85 LYS G 678 GLY G 684 1 7
HELIX 86 86 ASN G 685 ILE G 696 1 12
HELIX 87 87 ILE G 696 SER G 703 1 8
HELIX 88 88 CYS G 707 LEU G 710 5 4
HELIX 89 89 VAL G 711 GLU G 717 1 7
HELIX 90 90 ARG G 718 MET G 719 5 2
HELIX 91 91 GLU G 720 PHE G 722 5 3
HELIX 92 92 GLN G 723 SER G 743 1 21
HELIX 93 93 CYS G 745 ASP G 756 1 12
HELIX 94 94 SER G 760 LEU G 766 1 7
HELIX 95 95 LEU G 766 THR G 773 1 8
HELIX 96 96 LYS G 774 TYR G 785 1 12
HELIX 97 97 GLY G 791 ILE G 816 1 26
HELIX 98 98 LEU G 825 GLY G 829 5 5
HELIX 99 99 GLY G 882 ALA G 886 5 5
HELIX 100 100 THR G 930 CYS G 952 1 23
HELIX 101 101 GLY H 17 ASP H 28 1 12
HELIX 102 102 LEU H 69 TYR H 74 5 6
HELIX 103 103 SER H 88 LYS H 98 1 11
HELIX 104 104 LYS H 98 CYS H 107 1 10
HELIX 105 105 LYS H 118 ARG H 122 5 5
HELIX 106 106 ASP H 124 MET H 134 1 11
HELIX 107 107 LYS H 140 GLY H 152 1 13
HELIX 108 108 GLY H 166 GLN H 180 1 15
SHEET 1 A 8 ILE A 818 THR A 819 0
SHEET 2 A 8 SER A 888 ASN A 896 1 O TYR A 889 N THR A 819
SHEET 3 A 8 ALA A 869 ARG A 876 -1 N ARG A 876 O SER A 888
SHEET 4 A 8 MET A 859 HIS A 866 -1 N HIS A 862 O CYS A 873
SHEET 5 A 8 LEU A 831 THR A 841 -1 N GLY A 835 O LEU A 863
SHEET 6 A 8 GLU A 922 GLN A 927 -1 O ILE A 925 N TRP A 840
SHEET 7 A 8 LYS A 912 TYR A 917 -1 N PHE A 913 O ILE A 926
SHEET 8 A 8 VAL A 900 THR A 903 -1 N THR A 903 O GLU A 914
SHEET 1 B 6 TYR B 42 VAL B 48 0
SHEET 2 B 6 LYS B 51 TRP B 58 -1 O LEU B 57 N TYR B 42
SHEET 3 B 6 ILE B 4 VAL B 11 1 N ILE B 4 O GLU B 54
SHEET 4 B 6 VAL B 79 SER B 85 1 O CYS B 83 N VAL B 11
SHEET 5 B 6 LEU B 114 ASN B 117 1 O ASN B 117 N PHE B 84
SHEET 6 B 6 TYR B 156 GLU B 158 1 O MET B 157 N GLY B 116
SHEET 1 C 8 ILE C 818 THR C 819 0
SHEET 2 C 8 SER C 888 ASN C 896 1 O TYR C 889 N THR C 819
SHEET 3 C 8 ALA C 869 ARG C 876 -1 N ARG C 876 O SER C 888
SHEET 4 C 8 MET C 859 HIS C 866 -1 N HIS C 862 O CYS C 873
SHEET 5 C 8 LEU C 831 THR C 841 -1 N GLY C 835 O LEU C 863
SHEET 6 C 8 GLU C 922 GLN C 927 -1 O ILE C 925 N TRP C 840
SHEET 7 C 8 LYS C 912 TYR C 917 -1 N PHE C 913 O ILE C 926
SHEET 8 C 8 VAL C 900 THR C 903 -1 N THR C 903 O GLU C 914
SHEET 1 D 6 TYR D 42 VAL D 48 0
SHEET 2 D 6 LYS D 51 TRP D 58 -1 O LEU D 57 N TYR D 42
SHEET 3 D 6 ILE D 4 VAL D 11 1 N ILE D 4 O GLU D 54
SHEET 4 D 6 VAL D 79 SER D 85 1 O CYS D 83 N VAL D 11
SHEET 5 D 6 LEU D 114 ASN D 117 1 O ASN D 117 N PHE D 84
SHEET 6 D 6 TYR D 156 GLU D 158 1 O MET D 157 N GLY D 116
SHEET 1 E 8 ILE E 818 THR E 819 0
SHEET 2 E 8 SER E 888 ASN E 896 1 O TYR E 889 N THR E 819
SHEET 3 E 8 ALA E 869 ARG E 876 -1 N ARG E 876 O SER E 888
SHEET 4 E 8 MET E 859 HIS E 866 -1 N HIS E 862 O CYS E 873
SHEET 5 E 8 LEU E 831 THR E 841 -1 N VAL E 839 O MET E 859
SHEET 6 E 8 GLU E 922 GLN E 927 -1 O ILE E 925 N TRP E 840
SHEET 7 E 8 LYS E 912 TYR E 917 -1 N PHE E 913 O ILE E 926
SHEET 8 E 8 VAL E 900 THR E 903 -1 N THR E 903 O GLU E 914
SHEET 1 F 6 TYR F 42 VAL F 48 0
SHEET 2 F 6 LYS F 51 TRP F 58 -1 O LEU F 57 N TYR F 42
SHEET 3 F 6 ILE F 4 VAL F 11 1 N ILE F 4 O GLU F 54
SHEET 4 F 6 VAL F 79 SER F 85 1 O CYS F 83 N VAL F 11
SHEET 5 F 6 LEU F 114 ASN F 117 1 O ASN F 117 N PHE F 84
SHEET 6 F 6 TYR F 156 GLU F 158 1 O MET F 157 N GLY F 116
SHEET 1 G 8 ILE G 818 THR G 819 0
SHEET 2 G 8 SER G 888 ASN G 896 1 O TYR G 889 N THR G 819
SHEET 3 G 8 ALA G 869 ARG G 876 -1 N ARG G 876 O SER G 888
SHEET 4 G 8 MET G 859 HIS G 866 -1 N HIS G 862 O CYS G 873
SHEET 5 G 8 LEU G 831 THR G 841 -1 N VAL G 839 O MET G 859
SHEET 6 G 8 GLU G 922 GLN G 927 -1 O ILE G 925 N TRP G 840
SHEET 7 G 8 LYS G 912 TYR G 917 -1 N PHE G 913 O ILE G 926
SHEET 8 G 8 VAL G 900 THR G 903 -1 N THR G 903 O GLU G 914
SHEET 1 H 6 TYR H 42 VAL H 48 0
SHEET 2 H 6 LYS H 51 TRP H 58 -1 O LEU H 57 N TYR H 42
SHEET 3 H 6 ILE H 4 VAL H 11 1 N ILE H 4 O GLU H 54
SHEET 4 H 6 VAL H 79 SER H 85 1 O CYS H 83 N VAL H 11
SHEET 5 H 6 LEU H 114 ASN H 117 1 O ASN H 117 N PHE H 84
SHEET 6 H 6 TYR H 156 GLU H 158 1 O MET H 157 N GLY H 116
CRYST1 158.897 158.897 151.791 90.00 90.00 90.00 P 43 16
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 0.006293 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006293 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006588 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
