HEADER PROTEIN FIBRIL REGULATOR 31-JUL-07 2Z6E
TITLE CRYSTAL STRUCTURE OF HUMAN DAAM1 FH2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISHEVELED-ASSOCIATED ACTIVATOR OF MORPHOGENESIS 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: FH2 DOMAIN, UNP RESIDUES 594-1012;
COMPND 5 SYNONYM: FORMIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 GENE: DAAM1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS COILED COIL, ALTERNATIVE SPLICING, CYTOPLASM, PROTEIN FIBRIL
KEYWDS 2 REGULATOR
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YAMASHITA,T.HIGASHI,Y.SATO,R.SHIRAKAWA,T.KITA,H.HORIUCHI,S.FUKAI,
AUTHOR 2 O.NUREKI
REVDAT 3 13-MAR-24 2Z6E 1 REMARK
REVDAT 2 24-FEB-09 2Z6E 1 VERSN
REVDAT 1 27-MAY-08 2Z6E 0
JRNL AUTH M.YAMASHITA,T.HIGASHI,S.SUETSUGU,Y.SATO,T.IKEDA,R.SHIRAKAWA,
JRNL AUTH 2 T.KITA,T.TAKENAWA,H.HORIUCHI,S.FUKAI,O.NUREKI
JRNL TITL CRYSTAL STRUCTURE OF HUMAN DAAM1 FORMIN HOMOLOGY 2 DOMAIN
JRNL REF GENES CELLS V. 12 1255 2007
JRNL REFN ISSN 1356-9597
JRNL PMID 17986009
JRNL DOI 10.1111/J.1365-2443.2007.01132.X
REMARK 2
REMARK 2 RESOLUTION. 2.80 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 3368250.170
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 86.8
REMARK 3 NUMBER OF REFLECTIONS : 49208
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) : 0.225
REMARK 3 FREE R VALUE : 0.289
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2469
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.98
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.90
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6094
REMARK 3 BIN R VALUE (WORKING SET) : 0.4130
REMARK 3 BIN FREE R VALUE : 0.4510
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 323
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.025
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12628
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 122
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -10.35000
REMARK 3 B22 (A**2) : 26.63000
REMARK 3 B33 (A**2) : -16.28000
REMARK 3 B12 (A**2) : 16.41000
REMARK 3 B13 (A**2) : 5.52000
REMARK 3 B23 (A**2) : 16.30000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.76
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) : 0.53
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.82
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 19.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
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) : 4.950 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 7.490 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 6.930 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 9.560 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.28
REMARK 3 BSOL : 23.00
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: NULL
REMARK 4
REMARK 4 2Z6E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000027578.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-05; 25-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; SPRING-8
REMARK 200 BEAMLINE : BL41XU; BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000; 0.9793, 0.9795
REMARK 200 MONOCHROMATOR : SI(111); SI(111)
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : DENZO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49227
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.18400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 6.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 41170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 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: 9710 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 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 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 594
REMARK 465 GLY A 595
REMARK 465 LEU A 596
REMARK 465 ALA A 597
REMARK 465 LEU A 598
REMARK 465 LYS A 599
REMARK 465 LYS A 600
REMARK 465 GLN A 656
REMARK 465 ASP A 657
REMARK 465 PHE A 658
REMARK 465 PHE A 659
REMARK 465 VAL A 660
REMARK 465 ASN A 661
REMARK 465 SER A 662
REMARK 465 ASN A 663
REMARK 465 SER A 664
REMARK 465 LYS A 665
REMARK 465 GLN A 666
REMARK 465 LYS A 667
REMARK 465 GLU A 668
REMARK 465 ALA A 669
REMARK 465 ASP A 670
REMARK 465 ALA A 671
REMARK 465 ILE A 672
REMARK 465 ASP A 673
REMARK 465 ASP A 674
REMARK 465 THR A 675
REMARK 465 LEU A 676
REMARK 465 SER A 677
REMARK 465 SER A 678
REMARK 465 LYS A 679
REMARK 465 VAL B 660
REMARK 465 ASN B 661
REMARK 465 SER B 662
REMARK 465 ASN B 663
REMARK 465 SER B 664
REMARK 465 LYS B 665
REMARK 465 GLN B 666
REMARK 465 LYS B 667
REMARK 465 GLU B 668
REMARK 465 ALA B 669
REMARK 465 ASP B 670
REMARK 465 ALA B 671
REMARK 465 ILE B 672
REMARK 465 ASP B 673
REMARK 465 ASP B 674
REMARK 465 THR B 675
REMARK 465 LEU B 676
REMARK 465 SER B 677
REMARK 465 SER B 678
REMARK 465 LYS B 679
REMARK 465 LEU B 680
REMARK 465 LYS B 681
REMARK 465 GLU B 1012
REMARK 465 MET C 594
REMARK 465 GLY C 595
REMARK 465 LEU C 596
REMARK 465 ALA C 597
REMARK 465 LEU C 598
REMARK 465 LYS C 599
REMARK 465 LYS C 600
REMARK 465 PHE C 658
REMARK 465 PHE C 659
REMARK 465 VAL C 660
REMARK 465 ASN C 661
REMARK 465 SER C 662
REMARK 465 ASN C 663
REMARK 465 SER C 664
REMARK 465 LYS C 665
REMARK 465 GLN C 666
REMARK 465 LYS C 667
REMARK 465 GLU C 668
REMARK 465 ALA C 669
REMARK 465 ASP C 670
REMARK 465 ALA C 671
REMARK 465 ILE C 672
REMARK 465 ASP C 673
REMARK 465 ASP C 674
REMARK 465 THR C 675
REMARK 465 LEU C 676
REMARK 465 SER C 677
REMARK 465 SER C 678
REMARK 465 LYS C 679
REMARK 465 LEU C 680
REMARK 465 ARG C 1003
REMARK 465 ALA C 1004
REMARK 465 ARG C 1005
REMARK 465 MET C 1006
REMARK 465 GLU C 1007
REMARK 465 ALA C 1008
REMARK 465 GLN C 1009
REMARK 465 LEU C 1010
REMARK 465 LYS C 1011
REMARK 465 GLU C 1012
REMARK 465 MET D 594
REMARK 465 GLY D 595
REMARK 465 LEU D 596
REMARK 465 ALA D 597
REMARK 465 LEU D 598
REMARK 465 LYS D 599
REMARK 465 LYS D 600
REMARK 465 PHE D 658
REMARK 465 PHE D 659
REMARK 465 VAL D 660
REMARK 465 ASN D 661
REMARK 465 SER D 662
REMARK 465 ASN D 663
REMARK 465 SER D 664
REMARK 465 LYS D 665
REMARK 465 GLN D 666
REMARK 465 LYS D 667
REMARK 465 GLU D 668
REMARK 465 ALA D 669
REMARK 465 ASP D 670
REMARK 465 ALA D 671
REMARK 465 ILE D 672
REMARK 465 ASP D 673
REMARK 465 ASP D 674
REMARK 465 THR D 675
REMARK 465 LEU D 676
REMARK 465 SER D 677
REMARK 465 SER D 678
REMARK 465 LYS D 679
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 SER A 602 105.67 -48.22
REMARK 500 ASN A 614 44.13 80.46
REMARK 500 LYS A 622 15.37 -68.54
REMARK 500 LYS A 681 173.55 179.71
REMARK 500 GLU A 721 56.97 38.47
REMARK 500 PRO A 736 108.94 -57.70
REMARK 500 GLU A 746 -6.23 -55.86
REMARK 500 ARG A 753 74.07 27.30
REMARK 500 ALA A 755 140.66 -20.52
REMARK 500 LEU A 774 -70.91 -60.16
REMARK 500 LYS A 782 63.57 -112.02
REMARK 500 MET A 824 -105.24 -57.47
REMARK 500 ASN A 825 91.57 -60.20
REMARK 500 LYS A 867 -13.63 -153.29
REMARK 500 TYR A 868 71.50 -150.53
REMARK 500 GLN A 883 35.74 -88.16
REMARK 500 ALA A 884 -22.61 -154.62
REMARK 500 THR A 890 -77.74 -59.05
REMARK 500 SER A 915 34.04 -93.17
REMARK 500 PHE A 924 -72.27 -59.67
REMARK 500 ALA A 964 -111.87 -11.93
REMARK 500 GLN A 981 -74.83 -66.81
REMARK 500 ALA A 982 -37.36 -32.31
REMARK 500 MET A1006 3.74 -69.88
REMARK 500 LYS B 599 54.33 -91.78
REMARK 500 LYS B 601 -85.55 -158.48
REMARK 500 SER B 602 97.64 -62.36
REMARK 500 ASN B 614 44.14 88.53
REMARK 500 TRP B 628 -12.85 -48.63
REMARK 500 GLN B 655 71.30 -32.99
REMARK 500 GLN B 656 96.71 -48.87
REMARK 500 PHE B 658 162.08 -29.81
REMARK 500 ARG B 691 -74.33 -58.41
REMARK 500 GLU B 746 11.57 -56.97
REMARK 500 ARG B 753 80.11 35.05
REMARK 500 ALA B 755 136.33 -32.68
REMARK 500 GLN B 771 -70.15 -45.66
REMARK 500 GLN B 775 -39.09 -39.86
REMARK 500 LYS B 782 71.20 -106.87
REMARK 500 PHE B 783 -40.53 -132.88
REMARK 500 MET B 824 -103.03 -58.32
REMARK 500 ASN B 825 79.04 -62.60
REMARK 500 LYS B 826 -169.15 -72.81
REMARK 500 LYS B 867 3.71 -154.73
REMARK 500 TYR B 868 58.80 -159.71
REMARK 500 GLN B 883 49.91 -80.78
REMARK 500 ALA B 884 -18.78 -160.89
REMARK 500 THR B 890 -73.67 -53.55
REMARK 500 PRO B 918 171.25 -51.88
REMARK 500 LYS B 923 34.89 -87.35
REMARK 500
REMARK 500 THIS ENTRY HAS 99 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 778 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1UX5 RELATED DB: PDB
REMARK 900 YEAST BNI1P FH2
REMARK 900 RELATED ID: 1Y64 RELATED DB: PDB
REMARK 900 YEAST BNI1P FH2-TMRACTIN COMPLEX
REMARK 900 RELATED ID: 1V9D RELATED DB: PDB
REMARK 900 MOUSE MDIA1 FH2 CORE
DBREF 2Z6E A 594 1012 UNP Q9Y4D1 DAAM1_HUMAN 594 1012
DBREF 2Z6E B 594 1012 UNP Q9Y4D1 DAAM1_HUMAN 594 1012
DBREF 2Z6E C 594 1012 UNP Q9Y4D1 DAAM1_HUMAN 594 1012
DBREF 2Z6E D 594 1012 UNP Q9Y4D1 DAAM1_HUMAN 594 1012
SEQRES 1 A 419 MET GLY LEU ALA LEU LYS LYS LYS SER ILE PRO GLN PRO
SEQRES 2 A 419 THR ASN ALA LEU LYS SER PHE ASN TRP SER LYS LEU PRO
SEQRES 3 A 419 GLU ASN LYS LEU GLU GLY THR VAL TRP THR GLU ILE ASP
SEQRES 4 A 419 ASP THR LYS VAL PHE LYS ILE LEU ASP LEU GLU ASP LEU
SEQRES 5 A 419 GLU ARG THR PHE SER ALA TYR GLN ARG GLN GLN ASP PHE
SEQRES 6 A 419 PHE VAL ASN SER ASN SER LYS GLN LYS GLU ALA ASP ALA
SEQRES 7 A 419 ILE ASP ASP THR LEU SER SER LYS LEU LYS VAL LYS GLU
SEQRES 8 A 419 LEU SER VAL ILE ASP GLY ARG ARG ALA GLN ASN CYS ASN
SEQRES 9 A 419 ILE LEU LEU SER ARG LEU LYS LEU SER ASN ASP GLU ILE
SEQRES 10 A 419 LYS ARG ALA ILE LEU THR MET ASP GLU GLN GLU ASP LEU
SEQRES 11 A 419 PRO LYS ASP MET LEU GLU GLN LEU LEU LYS PHE VAL PRO
SEQRES 12 A 419 GLU LYS SER ASP ILE ASP LEU LEU GLU GLU HIS LYS HIS
SEQRES 13 A 419 GLU LEU ASP ARG MET ALA LYS ALA ASP ARG PHE LEU PHE
SEQRES 14 A 419 GLU MET SER ARG ILE ASN HIS TYR GLN GLN ARG LEU GLN
SEQRES 15 A 419 SER LEU TYR PHE LYS LYS LYS PHE ALA GLU ARG VAL ALA
SEQRES 16 A 419 GLU VAL LYS PRO LYS VAL GLU ALA ILE ARG SER GLY SER
SEQRES 17 A 419 GLU GLU VAL PHE ARG SER GLY ALA LEU LYS GLN LEU LEU
SEQRES 18 A 419 GLU VAL VAL LEU ALA PHE GLY ASN TYR MET ASN LYS GLY
SEQRES 19 A 419 GLN ARG GLY ASN ALA TYR GLY PHE LYS ILE SER SER LEU
SEQRES 20 A 419 ASN LYS ILE ALA ASP THR LYS SER SER ILE ASP LYS ASN
SEQRES 21 A 419 ILE THR LEU LEU HIS TYR LEU ILE THR ILE VAL GLU ASN
SEQRES 22 A 419 LYS TYR PRO SER VAL LEU ASN LEU ASN GLU GLU LEU ARG
SEQRES 23 A 419 ASP ILE PRO GLN ALA ALA LYS VAL ASN MET THR GLU LEU
SEQRES 24 A 419 ASP LYS GLU ILE SER THR LEU ARG SER GLY LEU LYS ALA
SEQRES 25 A 419 VAL GLU THR GLU LEU GLU TYR GLN LYS SER GLN PRO PRO
SEQRES 26 A 419 GLN PRO GLY ASP LYS PHE VAL SER VAL VAL SER GLN PHE
SEQRES 27 A 419 ILE THR VAL ALA SER PHE SER PHE SER ASP VAL GLU ASP
SEQRES 28 A 419 LEU LEU ALA GLU ALA LYS ASP LEU PHE THR LYS ALA VAL
SEQRES 29 A 419 LYS HIS PHE GLY GLU GLU ALA GLY LYS ILE GLN PRO ASP
SEQRES 30 A 419 GLU PHE PHE GLY ILE PHE ASP GLN PHE LEU GLN ALA VAL
SEQRES 31 A 419 SER GLU ALA LYS GLN GLU ASN GLU ASN MET ARG LYS LYS
SEQRES 32 A 419 LYS GLU GLU GLU GLU ARG ARG ALA ARG MET GLU ALA GLN
SEQRES 33 A 419 LEU LYS GLU
SEQRES 1 B 419 MET GLY LEU ALA LEU LYS LYS LYS SER ILE PRO GLN PRO
SEQRES 2 B 419 THR ASN ALA LEU LYS SER PHE ASN TRP SER LYS LEU PRO
SEQRES 3 B 419 GLU ASN LYS LEU GLU GLY THR VAL TRP THR GLU ILE ASP
SEQRES 4 B 419 ASP THR LYS VAL PHE LYS ILE LEU ASP LEU GLU ASP LEU
SEQRES 5 B 419 GLU ARG THR PHE SER ALA TYR GLN ARG GLN GLN ASP PHE
SEQRES 6 B 419 PHE VAL ASN SER ASN SER LYS GLN LYS GLU ALA ASP ALA
SEQRES 7 B 419 ILE ASP ASP THR LEU SER SER LYS LEU LYS VAL LYS GLU
SEQRES 8 B 419 LEU SER VAL ILE ASP GLY ARG ARG ALA GLN ASN CYS ASN
SEQRES 9 B 419 ILE LEU LEU SER ARG LEU LYS LEU SER ASN ASP GLU ILE
SEQRES 10 B 419 LYS ARG ALA ILE LEU THR MET ASP GLU GLN GLU ASP LEU
SEQRES 11 B 419 PRO LYS ASP MET LEU GLU GLN LEU LEU LYS PHE VAL PRO
SEQRES 12 B 419 GLU LYS SER ASP ILE ASP LEU LEU GLU GLU HIS LYS HIS
SEQRES 13 B 419 GLU LEU ASP ARG MET ALA LYS ALA ASP ARG PHE LEU PHE
SEQRES 14 B 419 GLU MET SER ARG ILE ASN HIS TYR GLN GLN ARG LEU GLN
SEQRES 15 B 419 SER LEU TYR PHE LYS LYS LYS PHE ALA GLU ARG VAL ALA
SEQRES 16 B 419 GLU VAL LYS PRO LYS VAL GLU ALA ILE ARG SER GLY SER
SEQRES 17 B 419 GLU GLU VAL PHE ARG SER GLY ALA LEU LYS GLN LEU LEU
SEQRES 18 B 419 GLU VAL VAL LEU ALA PHE GLY ASN TYR MET ASN LYS GLY
SEQRES 19 B 419 GLN ARG GLY ASN ALA TYR GLY PHE LYS ILE SER SER LEU
SEQRES 20 B 419 ASN LYS ILE ALA ASP THR LYS SER SER ILE ASP LYS ASN
SEQRES 21 B 419 ILE THR LEU LEU HIS TYR LEU ILE THR ILE VAL GLU ASN
SEQRES 22 B 419 LYS TYR PRO SER VAL LEU ASN LEU ASN GLU GLU LEU ARG
SEQRES 23 B 419 ASP ILE PRO GLN ALA ALA LYS VAL ASN MET THR GLU LEU
SEQRES 24 B 419 ASP LYS GLU ILE SER THR LEU ARG SER GLY LEU LYS ALA
SEQRES 25 B 419 VAL GLU THR GLU LEU GLU TYR GLN LYS SER GLN PRO PRO
SEQRES 26 B 419 GLN PRO GLY ASP LYS PHE VAL SER VAL VAL SER GLN PHE
SEQRES 27 B 419 ILE THR VAL ALA SER PHE SER PHE SER ASP VAL GLU ASP
SEQRES 28 B 419 LEU LEU ALA GLU ALA LYS ASP LEU PHE THR LYS ALA VAL
SEQRES 29 B 419 LYS HIS PHE GLY GLU GLU ALA GLY LYS ILE GLN PRO ASP
SEQRES 30 B 419 GLU PHE PHE GLY ILE PHE ASP GLN PHE LEU GLN ALA VAL
SEQRES 31 B 419 SER GLU ALA LYS GLN GLU ASN GLU ASN MET ARG LYS LYS
SEQRES 32 B 419 LYS GLU GLU GLU GLU ARG ARG ALA ARG MET GLU ALA GLN
SEQRES 33 B 419 LEU LYS GLU
SEQRES 1 C 419 MET GLY LEU ALA LEU LYS LYS LYS SER ILE PRO GLN PRO
SEQRES 2 C 419 THR ASN ALA LEU LYS SER PHE ASN TRP SER LYS LEU PRO
SEQRES 3 C 419 GLU ASN LYS LEU GLU GLY THR VAL TRP THR GLU ILE ASP
SEQRES 4 C 419 ASP THR LYS VAL PHE LYS ILE LEU ASP LEU GLU ASP LEU
SEQRES 5 C 419 GLU ARG THR PHE SER ALA TYR GLN ARG GLN GLN ASP PHE
SEQRES 6 C 419 PHE VAL ASN SER ASN SER LYS GLN LYS GLU ALA ASP ALA
SEQRES 7 C 419 ILE ASP ASP THR LEU SER SER LYS LEU LYS VAL LYS GLU
SEQRES 8 C 419 LEU SER VAL ILE ASP GLY ARG ARG ALA GLN ASN CYS ASN
SEQRES 9 C 419 ILE LEU LEU SER ARG LEU LYS LEU SER ASN ASP GLU ILE
SEQRES 10 C 419 LYS ARG ALA ILE LEU THR MET ASP GLU GLN GLU ASP LEU
SEQRES 11 C 419 PRO LYS ASP MET LEU GLU GLN LEU LEU LYS PHE VAL PRO
SEQRES 12 C 419 GLU LYS SER ASP ILE ASP LEU LEU GLU GLU HIS LYS HIS
SEQRES 13 C 419 GLU LEU ASP ARG MET ALA LYS ALA ASP ARG PHE LEU PHE
SEQRES 14 C 419 GLU MET SER ARG ILE ASN HIS TYR GLN GLN ARG LEU GLN
SEQRES 15 C 419 SER LEU TYR PHE LYS LYS LYS PHE ALA GLU ARG VAL ALA
SEQRES 16 C 419 GLU VAL LYS PRO LYS VAL GLU ALA ILE ARG SER GLY SER
SEQRES 17 C 419 GLU GLU VAL PHE ARG SER GLY ALA LEU LYS GLN LEU LEU
SEQRES 18 C 419 GLU VAL VAL LEU ALA PHE GLY ASN TYR MET ASN LYS GLY
SEQRES 19 C 419 GLN ARG GLY ASN ALA TYR GLY PHE LYS ILE SER SER LEU
SEQRES 20 C 419 ASN LYS ILE ALA ASP THR LYS SER SER ILE ASP LYS ASN
SEQRES 21 C 419 ILE THR LEU LEU HIS TYR LEU ILE THR ILE VAL GLU ASN
SEQRES 22 C 419 LYS TYR PRO SER VAL LEU ASN LEU ASN GLU GLU LEU ARG
SEQRES 23 C 419 ASP ILE PRO GLN ALA ALA LYS VAL ASN MET THR GLU LEU
SEQRES 24 C 419 ASP LYS GLU ILE SER THR LEU ARG SER GLY LEU LYS ALA
SEQRES 25 C 419 VAL GLU THR GLU LEU GLU TYR GLN LYS SER GLN PRO PRO
SEQRES 26 C 419 GLN PRO GLY ASP LYS PHE VAL SER VAL VAL SER GLN PHE
SEQRES 27 C 419 ILE THR VAL ALA SER PHE SER PHE SER ASP VAL GLU ASP
SEQRES 28 C 419 LEU LEU ALA GLU ALA LYS ASP LEU PHE THR LYS ALA VAL
SEQRES 29 C 419 LYS HIS PHE GLY GLU GLU ALA GLY LYS ILE GLN PRO ASP
SEQRES 30 C 419 GLU PHE PHE GLY ILE PHE ASP GLN PHE LEU GLN ALA VAL
SEQRES 31 C 419 SER GLU ALA LYS GLN GLU ASN GLU ASN MET ARG LYS LYS
SEQRES 32 C 419 LYS GLU GLU GLU GLU ARG ARG ALA ARG MET GLU ALA GLN
SEQRES 33 C 419 LEU LYS GLU
SEQRES 1 D 419 MET GLY LEU ALA LEU LYS LYS LYS SER ILE PRO GLN PRO
SEQRES 2 D 419 THR ASN ALA LEU LYS SER PHE ASN TRP SER LYS LEU PRO
SEQRES 3 D 419 GLU ASN LYS LEU GLU GLY THR VAL TRP THR GLU ILE ASP
SEQRES 4 D 419 ASP THR LYS VAL PHE LYS ILE LEU ASP LEU GLU ASP LEU
SEQRES 5 D 419 GLU ARG THR PHE SER ALA TYR GLN ARG GLN GLN ASP PHE
SEQRES 6 D 419 PHE VAL ASN SER ASN SER LYS GLN LYS GLU ALA ASP ALA
SEQRES 7 D 419 ILE ASP ASP THR LEU SER SER LYS LEU LYS VAL LYS GLU
SEQRES 8 D 419 LEU SER VAL ILE ASP GLY ARG ARG ALA GLN ASN CYS ASN
SEQRES 9 D 419 ILE LEU LEU SER ARG LEU LYS LEU SER ASN ASP GLU ILE
SEQRES 10 D 419 LYS ARG ALA ILE LEU THR MET ASP GLU GLN GLU ASP LEU
SEQRES 11 D 419 PRO LYS ASP MET LEU GLU GLN LEU LEU LYS PHE VAL PRO
SEQRES 12 D 419 GLU LYS SER ASP ILE ASP LEU LEU GLU GLU HIS LYS HIS
SEQRES 13 D 419 GLU LEU ASP ARG MET ALA LYS ALA ASP ARG PHE LEU PHE
SEQRES 14 D 419 GLU MET SER ARG ILE ASN HIS TYR GLN GLN ARG LEU GLN
SEQRES 15 D 419 SER LEU TYR PHE LYS LYS LYS PHE ALA GLU ARG VAL ALA
SEQRES 16 D 419 GLU VAL LYS PRO LYS VAL GLU ALA ILE ARG SER GLY SER
SEQRES 17 D 419 GLU GLU VAL PHE ARG SER GLY ALA LEU LYS GLN LEU LEU
SEQRES 18 D 419 GLU VAL VAL LEU ALA PHE GLY ASN TYR MET ASN LYS GLY
SEQRES 19 D 419 GLN ARG GLY ASN ALA TYR GLY PHE LYS ILE SER SER LEU
SEQRES 20 D 419 ASN LYS ILE ALA ASP THR LYS SER SER ILE ASP LYS ASN
SEQRES 21 D 419 ILE THR LEU LEU HIS TYR LEU ILE THR ILE VAL GLU ASN
SEQRES 22 D 419 LYS TYR PRO SER VAL LEU ASN LEU ASN GLU GLU LEU ARG
SEQRES 23 D 419 ASP ILE PRO GLN ALA ALA LYS VAL ASN MET THR GLU LEU
SEQRES 24 D 419 ASP LYS GLU ILE SER THR LEU ARG SER GLY LEU LYS ALA
SEQRES 25 D 419 VAL GLU THR GLU LEU GLU TYR GLN LYS SER GLN PRO PRO
SEQRES 26 D 419 GLN PRO GLY ASP LYS PHE VAL SER VAL VAL SER GLN PHE
SEQRES 27 D 419 ILE THR VAL ALA SER PHE SER PHE SER ASP VAL GLU ASP
SEQRES 28 D 419 LEU LEU ALA GLU ALA LYS ASP LEU PHE THR LYS ALA VAL
SEQRES 29 D 419 LYS HIS PHE GLY GLU GLU ALA GLY LYS ILE GLN PRO ASP
SEQRES 30 D 419 GLU PHE PHE GLY ILE PHE ASP GLN PHE LEU GLN ALA VAL
SEQRES 31 D 419 SER GLU ALA LYS GLN GLU ASN GLU ASN MET ARG LYS LYS
SEQRES 32 D 419 LYS GLU GLU GLU GLU ARG ARG ALA ARG MET GLU ALA GLN
SEQRES 33 D 419 LEU LYS GLU
FORMUL 5 HOH *122(H2 O)
HELIX 1 1 GLU A 620 GLU A 624 5 5
HELIX 2 2 THR A 626 ASP A 632 5 7
HELIX 3 3 ASP A 633 LYS A 638 1 6
HELIX 4 4 ASP A 641 PHE A 649 1 9
HELIX 5 5 ASP A 689 LYS A 704 1 16
HELIX 6 6 SER A 706 THR A 716 1 11
HELIX 7 7 PRO A 724 LEU A 732 1 9
HELIX 8 8 GLU A 737 GLU A 746 1 10
HELIX 9 9 HIS A 747 LEU A 751 5 5
HELIX 10 10 ALA A 755 ARG A 766 1 12
HELIX 11 11 HIS A 769 LYS A 782 1 14
HELIX 12 12 PHE A 783 GLU A 789 1 7
HELIX 13 13 VAL A 790 SER A 807 1 18
HELIX 14 14 SER A 807 MET A 824 1 18
HELIX 15 15 LYS A 836 THR A 846 5 11
HELIX 16 16 THR A 855 ASN A 866 1 12
HELIX 17 17 TYR A 868 LEU A 872 5 5
HELIX 18 18 ASN A 873 LEU A 878 1 6
HELIX 19 19 ASN A 888 SER A 915 1 28
HELIX 20 20 LYS A 923 PHE A 960 1 38
HELIX 21 21 GLN A 968 GLU A 1001 1 34
HELIX 22 22 ALA A 1004 GLN A 1009 1 6
HELIX 23 23 GLU B 620 GLU B 624 5 5
HELIX 24 24 THR B 626 ILE B 631 5 6
HELIX 25 25 ASP B 633 LYS B 638 1 6
HELIX 26 26 ASP B 641 PHE B 649 1 9
HELIX 27 27 ASP B 689 LYS B 704 1 16
HELIX 28 28 SER B 706 THR B 716 1 11
HELIX 29 29 PRO B 724 LEU B 732 1 9
HELIX 30 30 GLU B 737 GLU B 746 1 10
HELIX 31 31 HIS B 747 LEU B 751 5 5
HELIX 32 32 ALA B 755 ARG B 766 1 12
HELIX 33 33 HIS B 769 LYS B 782 1 14
HELIX 34 34 PHE B 783 SER B 807 1 25
HELIX 35 35 SER B 807 MET B 824 1 18
HELIX 36 36 LYS B 826 GLY B 830 5 5
HELIX 37 37 LYS B 836 ILE B 843 5 8
HELIX 38 38 THR B 855 ASN B 866 1 12
HELIX 39 39 TYR B 868 ARG B 879 5 12
HELIX 40 40 ILE B 881 ALA B 885 5 5
HELIX 41 41 ASN B 888 SER B 915 1 28
HELIX 42 42 LYS B 923 PHE B 960 1 38
HELIX 43 43 GLN B 968 LYS B 1011 1 44
HELIX 44 44 GLU C 620 GLU C 624 5 5
HELIX 45 45 THR C 626 ILE C 631 5 6
HELIX 46 46 ASP C 632 LYS C 638 1 7
HELIX 47 47 ASP C 641 PHE C 649 1 9
HELIX 48 48 ASP C 689 LYS C 704 1 16
HELIX 49 49 SER C 706 THR C 716 1 11
HELIX 50 50 PRO C 724 PHE C 734 1 11
HELIX 51 51 GLU C 737 GLU C 746 1 10
HELIX 52 52 HIS C 747 LEU C 751 5 5
HELIX 53 53 ALA C 755 ARG C 766 1 12
HELIX 54 54 HIS C 769 LYS C 782 1 14
HELIX 55 55 PHE C 783 SER C 807 1 25
HELIX 56 56 SER C 807 ASN C 825 1 19
HELIX 57 57 LYS C 836 ILE C 843 5 8
HELIX 58 58 THR C 855 ASN C 866 1 12
HELIX 59 59 TYR C 868 LEU C 872 5 5
HELIX 60 60 ASN C 873 LEU C 878 1 6
HELIX 61 61 ILE C 881 ALA C 885 5 5
HELIX 62 62 ASN C 888 SER C 915 1 28
HELIX 63 63 LYS C 923 PHE C 960 1 38
HELIX 64 64 GLN C 968 ARG C 1002 1 35
HELIX 65 65 GLU D 620 GLU D 624 5 5
HELIX 66 66 THR D 626 ILE D 631 5 6
HELIX 67 67 ASP D 632 LYS D 638 1 7
HELIX 68 68 ASP D 641 PHE D 649 1 9
HELIX 69 69 ASP D 689 LYS D 704 1 16
HELIX 70 70 SER D 706 THR D 716 1 11
HELIX 71 71 PRO D 724 LEU D 732 1 9
HELIX 72 72 GLU D 737 GLU D 746 1 10
HELIX 73 73 HIS D 747 LEU D 751 5 5
HELIX 74 74 ALA D 755 ARG D 766 1 12
HELIX 75 75 HIS D 769 LYS D 782 1 14
HELIX 76 76 PHE D 783 SER D 807 1 25
HELIX 77 77 SER D 807 MET D 824 1 18
HELIX 78 78 LYS D 826 GLY D 830 5 5
HELIX 79 79 LYS D 836 ILE D 843 5 8
HELIX 80 80 THR D 855 ASN D 866 1 12
HELIX 81 81 TYR D 868 LEU D 872 5 5
HELIX 82 82 ASN D 873 LEU D 878 1 6
HELIX 83 83 ILE D 881 ALA D 885 5 5
HELIX 84 84 ASN D 888 SER D 915 1 28
HELIX 85 85 LYS D 923 PHE D 960 1 38
HELIX 86 86 GLN D 968 GLU D 1007 1 40
SHEET 1 A 2 TYR A 652 GLN A 653 0
SHEET 2 A 2 GLU A 684 LEU A 685 -1 O GLU A 684 N GLN A 653
SHEET 1 B 2 TYR B 652 ARG B 654 0
SHEET 2 B 2 LYS B 683 LEU B 685 -1 O GLU B 684 N GLN B 653
SHEET 1 C 2 TYR C 652 GLN C 653 0
SHEET 2 C 2 GLU C 684 LEU C 685 -1 O GLU C 684 N GLN C 653
SHEET 1 D 2 TYR D 652 GLN D 653 0
SHEET 2 D 2 GLU D 684 LEU D 685 -1 O GLU D 684 N GLN D 653
CRYST1 69.213 91.895 97.681 98.12 90.32 104.79 P 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 0.014448 0.003815 0.000651 0.00000
SCALE2 0.000000 0.011255 0.001679 0.00000
SCALE3 0.000000 0.000000 0.010351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
