HEADER STRUCTURAL PROTEIN 27-OCT-18 6I14
TITLE CRYSTAL STRUCTURE OF FASCIN IN COMPLEX WITH COMPOUND 9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FASCIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 55 KDA ACTIN-BUNDLING PROTEIN,SINGED-LIKE PROTEIN,P55;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: FSCN1, FAN1, HSN, SNL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBDDP-SPR3
KEYWDS ACTIN BUNDLING, SMALL MOLECULE INHIBITION, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.W.SCHUETTELKOPF
REVDAT 3 24-JAN-24 6I14 1 REMARK
REVDAT 2 20-MAR-19 6I14 1 JRNL
REVDAT 1 27-FEB-19 6I14 0
JRNL AUTH S.FRANCIS,D.CROFT,A.W.SCHUTTELKOPF,C.PARRY,A.PUGLIESE,
JRNL AUTH 2 K.CAMERON,S.CLAYDON,M.DRYSDALE,C.GARDNER,A.GOHLKE,G.GOODWIN,
JRNL AUTH 3 C.H.GRAY,J.KONCZAL,L.MCDONALD,M.MEZNA,A.PANNIFER,N.R.PAUL,
JRNL AUTH 4 L.MACHESKY,H.MCKINNON,J.BOWER
JRNL TITL STRUCTURE-BASED DESIGN, SYNTHESIS AND BIOLOGICAL EVALUATION
JRNL TITL 2 OF A NOVEL SERIES OF ISOQUINOLONE AND
JRNL TITL 3 PYRAZOLO[4,3-C]PYRIDINE INHIBITORS OF FASCIN 1 AS POTENTIAL
JRNL TITL 4 ANTI-METASTATIC AGENTS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 29 1023 2019
JRNL REFN ESSN 1464-3405
JRNL PMID 30773430
JRNL DOI 10.1016/J.BMCL.2019.01.035
REMARK 2
REMARK 2 RESOLUTION. 1.73 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.73
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 51.54
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 52292
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2720
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) : 1.73
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.78
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3805
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3340
REMARK 3 BIN FREE R VALUE SET COUNT : 227
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3784
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 274
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 33.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.09000
REMARK 3 B22 (A**2) : 0.91000
REMARK 3 B33 (A**2) : -1.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.112
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.089
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.647
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3914 ; 0.015 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 3385 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5298 ; 1.629 ; 1.670
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7941 ; 1.598 ; 1.652
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 487 ; 5.120 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 222 ;30.428 ;21.396
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 640 ;12.328 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;14.131 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 497 ; 0.100 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4523 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 770 ; 0.012 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1946 ; 1.126 ; 1.803
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1944 ; 1.122 ; 1.803
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2433 ; 1.798 ; 2.698
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 5
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 10 A 138
REMARK 3 ORIGIN FOR THE GROUP (A): 4.7550 8.7990 -7.5200
REMARK 3 T TENSOR
REMARK 3 T11: 0.0172 T22: 0.0746
REMARK 3 T33: 0.0282 T12: -0.0074
REMARK 3 T13: 0.0013 T23: -0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 3.1565 L22: 2.3327
REMARK 3 L33: 2.5181 L12: -0.1507
REMARK 3 L13: 0.9671 L23: -0.1041
REMARK 3 S TENSOR
REMARK 3 S11: -0.0229 S12: 0.0890 S13: -0.0299
REMARK 3 S21: -0.0180 S22: 0.0246 S23: -0.2343
REMARK 3 S31: 0.0905 S32: 0.2284 S33: -0.0016
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 139 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): -13.5800 -3.4890 -23.7330
REMARK 3 T TENSOR
REMARK 3 T11: 0.0868 T22: 0.0319
REMARK 3 T33: 0.0722 T12: 0.0041
REMARK 3 T13: -0.0335 T23: -0.0375
REMARK 3 L TENSOR
REMARK 3 L11: 2.5474 L22: 1.9719
REMARK 3 L33: 3.4255 L12: -0.0837
REMARK 3 L13: 0.6258 L23: 0.0226
REMARK 3 S TENSOR
REMARK 3 S11: 0.1422 S12: 0.0978 S13: -0.3344
REMARK 3 S21: -0.0451 S22: 0.0153 S23: -0.0435
REMARK 3 S31: 0.4180 S32: 0.0770 S33: -0.1575
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 : A 261 A 384
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1000 19.7940 -43.8620
REMARK 3 T TENSOR
REMARK 3 T11: 0.2662 T22: 0.1543
REMARK 3 T33: 0.0809 T12: 0.0111
REMARK 3 T13: 0.0077 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 1.1890 L22: 3.8461
REMARK 3 L33: 4.0685 L12: -0.3850
REMARK 3 L13: -0.7567 L23: 0.2734
REMARK 3 S TENSOR
REMARK 3 S11: 0.1197 S12: 0.3414 S13: 0.1841
REMARK 3 S21: -0.6538 S22: 0.0423 S23: 0.0448
REMARK 3 S31: -0.5998 S32: -0.1589 S33: -0.1620
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 : A 385 A 493
REMARK 3 ORIGIN FOR THE GROUP (A): -24.1010 20.9870 -17.9190
REMARK 3 T TENSOR
REMARK 3 T11: 0.0386 T22: 0.0286
REMARK 3 T33: 0.0364 T12: 0.0166
REMARK 3 T13: 0.0104 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 2.8288 L22: 2.2695
REMARK 3 L33: 3.5641 L12: -0.5896
REMARK 3 L13: 0.6757 L23: 0.7006
REMARK 3 S TENSOR
REMARK 3 S11: 0.0333 S12: -0.0274 S13: 0.2284
REMARK 3 S21: -0.0564 S22: -0.0080 S23: 0.0463
REMARK 3 S31: -0.2662 S32: -0.1211 S33: -0.0253
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 502 A 502
REMARK 3 RESIDUE RANGE : A 601 A 874
REMARK 3 RESIDUE RANGE : A 501 A 501
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0290 10.9700 -17.9750
REMARK 3 T TENSOR
REMARK 3 T11: 0.1396 T22: 0.1516
REMARK 3 T33: 0.1062 T12: -0.0188
REMARK 3 T13: 0.0185 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 1.1442 L22: 0.4980
REMARK 3 L33: 1.1590 L12: -0.2496
REMARK 3 L13: 0.7253 L23: -0.0835
REMARK 3 S TENSOR
REMARK 3 S11: -0.0043 S12: -0.0390 S13: 0.0143
REMARK 3 S21: -0.0083 S22: 0.0368 S23: 0.0062
REMARK 3 S31: -0.0173 S32: -0.0599 S33: -0.0325
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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: U VALUES : WITH TLS ADDED HYDROGENS
REMARK 3 HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 4
REMARK 4 6I14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1200012617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 0.3.8.0
REMARK 200 DATA SCALING SOFTWARE : XIA2 0.3.8.0
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55080
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.730
REMARK 200 RESOLUTION RANGE LOW (A) : 51.540
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.73
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.77
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 1.55900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 6I10
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18-22% PEG 8000, 100-130 MM MGAC2, 100
REMARK 280 MM CITRIC ACID PH 5.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 30.29500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.01500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.71000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.01500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 30.29500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.71000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL
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 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 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 ASN A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 ALA A 9
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 LYS A 32 CD CE NZ
REMARK 480 LYS A 42 CD CE NZ
REMARK 480 GLN A 50 CD OE1 NE2
REMARK 480 ARG A 158 CG CD NE CZ NH1 NH2
REMARK 480 ARG A 229 CD NE CZ NH1 NH2
REMARK 480 LYS A 244 CG CD CE NZ
REMARK 480 LYS A 247 CD CE NZ
REMARK 480 LYS A 250 CG CD CE NZ
REMARK 480 GLU A 270 CG CD OE1 OE2
REMARK 480 ASP A 286 CG OD1 OD2
REMARK 480 ARG A 300 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 303 CD CE NZ
REMARK 480 LYS A 353 CD CE NZ
REMARK 480 LYS A 359 CG CD CE NZ
REMARK 480 LYS A 399 CG CD CE NZ
REMARK 480 GLU A 483 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 ALA A 58 43.62 -106.08
REMARK 500 GLU A 116 -125.51 52.18
REMARK 500 VAL A 165 73.12 -118.19
REMARK 500 ASP A 166 11.04 -142.58
REMARK 500 ASP A 183 -120.24 59.72
REMARK 500 HIS A 193 -3.27 82.71
REMARK 500 ASP A 342 -116.20 61.14
REMARK 500 VAL A 400 -62.46 76.45
REMARK 500 SER A 444 11.16 -144.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS A 304 -10.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GZN A 502
DBREF 6I14 A 1 493 UNP Q16658 FSCN1_HUMAN 1 493
SEQRES 1 A 493 MET THR ALA ASN GLY THR ALA GLU ALA VAL GLN ILE GLN
SEQRES 2 A 493 PHE GLY LEU ILE ASN CYS GLY ASN LYS TYR LEU THR ALA
SEQRES 3 A 493 GLU ALA PHE GLY PHE LYS VAL ASN ALA SER ALA SER SER
SEQRES 4 A 493 LEU LYS LYS LYS GLN ILE TRP THR LEU GLU GLN PRO PRO
SEQRES 5 A 493 ASP GLU ALA GLY SER ALA ALA VAL CYS LEU ARG SER HIS
SEQRES 6 A 493 LEU GLY ARG TYR LEU ALA ALA ASP LYS ASP GLY ASN VAL
SEQRES 7 A 493 THR CYS GLU ARG GLU VAL PRO GLY PRO ASP CYS ARG PHE
SEQRES 8 A 493 LEU ILE VAL ALA HIS ASP ASP GLY ARG TRP SER LEU GLN
SEQRES 9 A 493 SER GLU ALA HIS ARG ARG TYR PHE GLY GLY THR GLU ASP
SEQRES 10 A 493 ARG LEU SER CYS PHE ALA GLN THR VAL SER PRO ALA GLU
SEQRES 11 A 493 LYS TRP SER VAL HIS ILE ALA MET HIS PRO GLN VAL ASN
SEQRES 12 A 493 ILE TYR SER VAL THR ARG LYS ARG TYR ALA HIS LEU SER
SEQRES 13 A 493 ALA ARG PRO ALA ASP GLU ILE ALA VAL ASP ARG ASP VAL
SEQRES 14 A 493 PRO TRP GLY VAL ASP SER LEU ILE THR LEU ALA PHE GLN
SEQRES 15 A 493 ASP GLN ARG TYR SER VAL GLN THR ALA ASP HIS ARG PHE
SEQRES 16 A 493 LEU ARG HIS ASP GLY ARG LEU VAL ALA ARG PRO GLU PRO
SEQRES 17 A 493 ALA THR GLY TYR THR LEU GLU PHE ARG SER GLY LYS VAL
SEQRES 18 A 493 ALA PHE ARG ASP CYS GLU GLY ARG TYR LEU ALA PRO SER
SEQRES 19 A 493 GLY PRO SER GLY THR LEU LYS ALA GLY LYS ALA THR LYS
SEQRES 20 A 493 VAL GLY LYS ASP GLU LEU PHE ALA LEU GLU GLN SER CYS
SEQRES 21 A 493 ALA GLN VAL VAL LEU GLN ALA ALA ASN GLU ARG ASN VAL
SEQRES 22 A 493 SER THR ARG GLN GLY MET ASP LEU SER ALA ASN GLN ASP
SEQRES 23 A 493 GLU GLU THR ASP GLN GLU THR PHE GLN LEU GLU ILE ASP
SEQRES 24 A 493 ARG ASP THR LYS LYS CYS ALA PHE ARG THR HIS THR GLY
SEQRES 25 A 493 LYS TYR TRP THR LEU THR ALA THR GLY GLY VAL GLN SER
SEQRES 26 A 493 THR ALA SER SER LYS ASN ALA SER CYS TYR PHE ASP ILE
SEQRES 27 A 493 GLU TRP ARG ASP ARG ARG ILE THR LEU ARG ALA SER ASN
SEQRES 28 A 493 GLY LYS PHE VAL THR SER LYS LYS ASN GLY GLN LEU ALA
SEQRES 29 A 493 ALA SER VAL GLU THR ALA GLY ASP SER GLU LEU PHE LEU
SEQRES 30 A 493 MET LYS LEU ILE ASN ARG PRO ILE ILE VAL PHE ARG GLY
SEQRES 31 A 493 GLU HIS GLY PHE ILE GLY CYS ARG LYS VAL THR GLY THR
SEQRES 32 A 493 LEU ASP ALA ASN ARG SER SER TYR ASP VAL PHE GLN LEU
SEQRES 33 A 493 GLU PHE ASN ASP GLY ALA TYR ASN ILE LYS ASP SER THR
SEQRES 34 A 493 GLY LYS TYR TRP THR VAL GLY SER ASP SER ALA VAL THR
SEQRES 35 A 493 SER SER GLY ASP THR PRO VAL ASP PHE PHE PHE GLU PHE
SEQRES 36 A 493 CYS ASP TYR ASN LYS VAL ALA ILE LYS VAL GLY GLY ARG
SEQRES 37 A 493 TYR LEU LYS GLY ASP HIS ALA GLY VAL LEU LYS ALA SER
SEQRES 38 A 493 ALA GLU THR VAL ASP PRO ALA SER LEU TRP GLU TYR
HET ACT A 501 4
HET GZN A 502 29
HETNAM ACT ACETATE ION
HETNAM GZN 2-[(3,4-DICHLOROPHENYL)METHYL]-~{N}-(1-METHYLPYRAZOL-4-
HETNAM 2 GZN YL)-1-OXIDANYLIDENE-ISOQUINOLINE-4-CARBOXAMIDE
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 GZN C21 H16 CL2 N4 O2
FORMUL 4 HOH *274(H2 O)
HELIX 1 AA1 LYS A 41 GLN A 44 5 4
HELIX 2 AA2 GLY A 86 CYS A 89 5 4
HELIX 3 AA3 SER A 127 LYS A 131 5 5
HELIX 4 AA4 GLY A 172 LEU A 176 5 5
HELIX 5 AA5 GLU A 207 GLY A 211 5 5
HELIX 6 AA6 GLY A 249 GLU A 252 5 4
HELIX 7 AA7 THR A 289 THR A 293 5 5
HELIX 8 AA8 ASN A 331 TYR A 335 5 5
HELIX 9 AA9 GLY A 371 LEU A 375 5 5
HELIX 10 AB1 ASP A 486 LEU A 490 5 5
SHEET 1 AA1 2 PHE A 14 ILE A 17 0
SHEET 2 AA1 2 SER A 133 ILE A 136 -1 O SER A 133 N ILE A 17
SHEET 1 AA2 2 TYR A 23 ALA A 26 0
SHEET 2 AA2 2 VAL A 33 ALA A 37 -1 O ASN A 34 N THR A 25
SHEET 1 AA3 2 TRP A 46 GLU A 49 0
SHEET 2 AA3 2 CYS A 61 SER A 64 -1 O ARG A 63 N THR A 47
SHEET 1 AA4 2 TYR A 69 ALA A 72 0
SHEET 2 AA4 2 VAL A 78 ARG A 82 -1 O ARG A 82 N TYR A 69
SHEET 1 AA5 2 PHE A 91 ALA A 95 0
SHEET 2 AA5 2 TRP A 101 SER A 105 -1 O GLN A 104 N LEU A 92
SHEET 1 AA6 2 TYR A 111 GLY A 113 0
SHEET 2 AA6 2 SER A 120 ALA A 123 -1 O SER A 120 N GLY A 113
SHEET 1 AA7 3 ILE A 177 THR A 178 0
SHEET 2 AA7 3 GLN A 141 SER A 146 -1 N VAL A 142 O ILE A 177
SHEET 3 AA7 3 PHE A 254 GLN A 258 -1 O ALA A 255 N TYR A 145
SHEET 1 AA8 2 TYR A 152 LEU A 155 0
SHEET 2 AA8 2 ILE A 163 ARG A 167 -1 O ARG A 167 N TYR A 152
SHEET 1 AA9 2 PHE A 181 GLN A 182 0
SHEET 2 AA9 2 ARG A 185 TYR A 186 -1 O ARG A 185 N GLN A 182
SHEET 1 AB1 2 PHE A 195 LEU A 196 0
SHEET 2 AB1 2 LEU A 202 VAL A 203 -1 O VAL A 203 N PHE A 195
SHEET 1 AB2 2 THR A 213 ARG A 217 0
SHEET 2 AB2 2 LYS A 220 ARG A 224 -1 O ARG A 224 N THR A 213
SHEET 1 AB3 2 LEU A 231 SER A 234 0
SHEET 2 AB3 2 THR A 239 ALA A 242 -1 O LYS A 241 N ALA A 232
SHEET 1 AB4 4 CYS A 305 ARG A 308 0
SHEET 2 AB4 4 PHE A 294 ILE A 298 -1 N GLU A 297 O ALA A 306
SHEET 3 AB4 4 GLN A 262 GLN A 266 -1 N VAL A 263 O PHE A 294
SHEET 4 AB4 4 LEU A 377 LEU A 380 -1 O LEU A 377 N GLN A 266
SHEET 1 AB5 2 ASN A 272 SER A 274 0
SHEET 2 AB5 2 SER A 282 GLN A 285 -1 O GLN A 285 N ASN A 272
SHEET 1 AB6 2 TYR A 314 LEU A 317 0
SHEET 2 AB6 2 VAL A 323 ALA A 327 -1 O ALA A 327 N TYR A 314
SHEET 1 AB7 2 ASP A 337 ARG A 341 0
SHEET 2 AB7 2 ARG A 344 ARG A 348 -1 O ARG A 348 N ASP A 337
SHEET 1 AB8 2 PHE A 354 SER A 357 0
SHEET 2 AB8 2 LEU A 363 VAL A 367 -1 O VAL A 367 N PHE A 354
SHEET 1 AB9 3 ILE A 385 ILE A 386 0
SHEET 2 AB9 3 PHE A 414 ASN A 419 -1 O PHE A 414 N ILE A 386
SHEET 3 AB9 3 ALA A 422 LYS A 426 -1 O LYS A 426 N GLN A 415
SHEET 1 AC1 3 ARG A 389 GLY A 390 0
SHEET 2 AC1 3 GLY A 393 CYS A 397 -1 O GLY A 393 N GLY A 390
SHEET 3 AC1 3 LEU A 404 ARG A 408 -1 O ARG A 408 N PHE A 394
SHEET 1 AC2 2 TYR A 432 VAL A 435 0
SHEET 2 AC2 2 VAL A 441 GLY A 445 -1 O GLY A 445 N TYR A 432
SHEET 1 AC3 4 PHE A 452 ASP A 457 0
SHEET 2 AC3 4 LYS A 460 VAL A 465 -1 O LYS A 464 N PHE A 452
SHEET 3 AC3 4 ARG A 468 GLY A 472 -1 O ARG A 468 N VAL A 465
SHEET 4 AC3 4 LEU A 478 ALA A 482 -1 O ALA A 482 N TYR A 469
SHEET 1 AC4 3 PHE A 452 ASP A 457 0
SHEET 2 AC4 3 LYS A 460 VAL A 465 -1 O LYS A 464 N PHE A 452
SHEET 3 AC4 3 TRP A 491 GLU A 492 -1 O TRP A 491 N VAL A 461
CISPEP 1 ARG A 158 PRO A 159 0 26.74
SITE 1 AC1 6 TRP A 101 VAL A 134 TYR A 186 THR A 213
SITE 2 AC1 6 LEU A 214 HOH A 647
SITE 1 AC2 10 LEU A 48 ILE A 93 TRP A 101 VAL A 134
SITE 2 AC2 10 LEU A 214 GLU A 215 PHE A 216 ARG A 217
SITE 3 AC2 10 GLN A 277 HOH A 791
CRYST1 60.590 87.420 98.030 90.00 90.00 90.00 P 21 21 21 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 0.016504 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011439 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010201 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
