HEADER TRANSCRIPTION 16-NOV-16 5MEZ
TITLE CRYSTAL STRUCTURE OF SMAD4-MH1 BOUND TO THE GGCT SITE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MH1 DOMAIN OF HUMAN SMAD4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MOTHERS AGAINST DPP HOMOLOG 4,DELETION TARGET IN PANCREATIC
COMPND 5 CARCINOMA 4,SMAD FAMILY MEMBER 4,HSMAD4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA (5'-D(P*GP*CP*AP*GP*GP*CP*TP*AP*GP*CP*CP*TP*GP*CP*A)-
COMPND 9 3');
COMPND 10 CHAIN: D, E;
COMPND 11 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: SMAD4, DPC4, MADH4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS SMADS, TRANSCRIPTION FACTOR, DNA COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.KACZMARSKA,R.FREIER,J.A.MARQUEZ,M.J.MACIAS
REVDAT 3 17-JAN-24 5MEZ 1 REMARK
REVDAT 2 27-DEC-17 5MEZ 1 JRNL
REVDAT 1 15-NOV-17 5MEZ 0
JRNL AUTH P.MARTIN-MALPARTIDA,M.BATET,Z.KACZMARSKA,R.FREIER,T.GOMES,
JRNL AUTH 2 E.ARAGON,Y.ZOU,Q.WANG,Q.XI,L.RUIZ,A.VEA,J.A.MARQUEZ,
JRNL AUTH 3 J.MASSAGUE,M.J.MACIAS
JRNL TITL STRUCTURAL BASIS FOR GENOME WIDE RECOGNITION OF 5-BP GC
JRNL TITL 2 MOTIFS BY SMAD TRANSCRIPTION FACTORS.
JRNL REF NAT COMMUN V. 8 2070 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 29234012
JRNL DOI 10.1038/S41467-017-02054-6
REMARK 2
REMARK 2 RESOLUTION. 2.98 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.98
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 12239
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) : 0.218
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.740
REMARK 3 FREE R VALUE TEST SET COUNT : 580
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.98
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.26
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.69
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2920
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2640
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2776
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.93
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1904
REMARK 3 NUCLEIC ACID ATOMS : 616
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 7
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 90.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 80.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -12.75280
REMARK 3 B22 (A**2) : -6.70680
REMARK 3 B33 (A**2) : 19.45960
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) : 0.430
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.775
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.343
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.705
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.341
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.904
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2639 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3707 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 802 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 35 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 325 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2639 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 3 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 347 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2722 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.49
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.28
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 13.1631 10.7932 17.7533
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 16.3081 -1.8040 44.4585
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8970 26.1914 16.0827
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { E|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 30.9439 22.7055 16.1406
REMARK 3 T TENSOR
REMARK 3 T11: 0.0000 T22: 0.0000
REMARK 3 T33: 0.0000 T12: 0.0000
REMARK 3 T13: 0.0000 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 0.0000 L12: 0.0000
REMARK 3 L13: 0.0000 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: 0.0000 S13: 0.0000
REMARK 3 S21: 0.0000 S22: 0.0000 S23: 0.0000
REMARK 3 S31: 0.0000 S32: 0.0000 S33: 0.0000
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5MEZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-NOV-16.
REMARK 100 THE DEPOSITION ID IS D_1200002373.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : MASSIF-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9677
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12239
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.980
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 3.830
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.98
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.99
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.06
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.680
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3QSV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 3350, 0.2 M CALCIUM CHLORIDE,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 32.39500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.08000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.53000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.08000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.39500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.53000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 6
REMARK 465 ALA A 7
REMARK 465 MET A 8
REMARK 465 GLY A 9
REMARK 465 PRO A 10
REMARK 465 THR A 11
REMARK 465 SER A 12
REMARK 465 ASN A 13
REMARK 465 ASP A 14
REMARK 465 GLY A 140
REMARK 465 GLY B 6
REMARK 465 ALA B 7
REMARK 465 MET B 8
REMARK 465 GLY B 9
REMARK 465 PRO B 10
REMARK 465 THR B 11
REMARK 465 SER B 12
REMARK 465 ASN B 13
REMARK 465 ASP B 14
REMARK 465 VAL B 137
REMARK 465 SER B 138
REMARK 465 PRO B 139
REMARK 465 GLY B 140
REMARK 465 DT D 1
REMARK 465 DT E 1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LEU A 17 CG CD1 CD2
REMARK 470 SER A 18 OG
REMARK 470 LYS A 48 CG CD CE NZ
REMARK 470 LYS A 51 CG CD CE NZ
REMARK 470 SER A 56 OG
REMARK 470 ILE A 58 CG1 CG2 CD1
REMARK 470 ILE A 61 CG1 CG2 CD1
REMARK 470 LYS A 106 CG CD CE NZ
REMARK 470 LYS A 110 CG CD CE NZ
REMARK 470 LYS A 113 CG CD CE NZ
REMARK 470 ASP A 120 CG OD1 OD2
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 VAL A 126 CG1 CG2
REMARK 470 GLU A 134 CG CD OE1 OE2
REMARK 470 SER A 138 OG
REMARK 470 LEU B 17 CG CD1 CD2
REMARK 470 SER B 18 OG
REMARK 470 GLU B 31 CG CD OE1 OE2
REMARK 470 LYS B 45 CG CD CE NZ
REMARK 470 LYS B 48 CG CD CE NZ
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 GLN B 75 CG CD OE1 NE2
REMARK 470 LYS B 106 CG CD CE NZ
REMARK 470 LYS B 113 CG CD CE NZ
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 ASP B 124 CG OD1 OD2
REMARK 470 VAL B 126 CG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC D 3 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
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 ARG A 100 -54.37 -129.46
REMARK 500 ARG B 100 -51.34 -126.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 71 SG
REMARK 620 2 CYS A 115 SG 108.8
REMARK 620 3 CYS A 127 SG 113.5 112.7
REMARK 620 4 HIS A 132 ND1 104.3 106.4 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 71 SG
REMARK 620 2 CYS B 115 SG 108.9
REMARK 620 3 CYS B 127 SG 104.9 114.0
REMARK 620 4 HIS B 132 ND1 106.3 110.3 111.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 201
DBREF 5MEZ A 10 140 UNP Q13485 SMAD4_HUMAN 10 140
DBREF 5MEZ B 10 140 UNP Q13485 SMAD4_HUMAN 10 140
DBREF 5MEZ D 1 16 PDB 5MEZ 5MEZ 1 16
DBREF 5MEZ E 1 16 PDB 5MEZ 5MEZ 1 16
SEQADV 5MEZ GLY A 6 UNP Q13485 EXPRESSION TAG
SEQADV 5MEZ ALA A 7 UNP Q13485 EXPRESSION TAG
SEQADV 5MEZ MET A 8 UNP Q13485 EXPRESSION TAG
SEQADV 5MEZ GLY A 9 UNP Q13485 EXPRESSION TAG
SEQADV 5MEZ GLY B 6 UNP Q13485 EXPRESSION TAG
SEQADV 5MEZ ALA B 7 UNP Q13485 EXPRESSION TAG
SEQADV 5MEZ MET B 8 UNP Q13485 EXPRESSION TAG
SEQADV 5MEZ GLY B 9 UNP Q13485 EXPRESSION TAG
SEQRES 1 A 135 GLY ALA MET GLY PRO THR SER ASN ASP ALA CYS LEU SER
SEQRES 2 A 135 ILE VAL HIS SER LEU MET CYS HIS ARG GLN GLY GLY GLU
SEQRES 3 A 135 SER GLU THR PHE ALA LYS ARG ALA ILE GLU SER LEU VAL
SEQRES 4 A 135 LYS LYS LEU LYS GLU LYS LYS ASP GLU LEU ASP SER LEU
SEQRES 5 A 135 ILE THR ALA ILE THR THR ASN GLY ALA HIS PRO SER LYS
SEQRES 6 A 135 CYS VAL THR ILE GLN ARG THR LEU ASP GLY ARG LEU GLN
SEQRES 7 A 135 VAL ALA GLY ARG LYS GLY PHE PRO HIS VAL ILE TYR ALA
SEQRES 8 A 135 ARG LEU TRP ARG TRP PRO ASP LEU HIS LYS ASN GLU LEU
SEQRES 9 A 135 LYS HIS VAL LYS TYR CYS GLN TYR ALA PHE ASP LEU LYS
SEQRES 10 A 135 CYS ASP SER VAL CYS VAL ASN PRO TYR HIS TYR GLU ARG
SEQRES 11 A 135 VAL VAL SER PRO GLY
SEQRES 1 B 135 GLY ALA MET GLY PRO THR SER ASN ASP ALA CYS LEU SER
SEQRES 2 B 135 ILE VAL HIS SER LEU MET CYS HIS ARG GLN GLY GLY GLU
SEQRES 3 B 135 SER GLU THR PHE ALA LYS ARG ALA ILE GLU SER LEU VAL
SEQRES 4 B 135 LYS LYS LEU LYS GLU LYS LYS ASP GLU LEU ASP SER LEU
SEQRES 5 B 135 ILE THR ALA ILE THR THR ASN GLY ALA HIS PRO SER LYS
SEQRES 6 B 135 CYS VAL THR ILE GLN ARG THR LEU ASP GLY ARG LEU GLN
SEQRES 7 B 135 VAL ALA GLY ARG LYS GLY PHE PRO HIS VAL ILE TYR ALA
SEQRES 8 B 135 ARG LEU TRP ARG TRP PRO ASP LEU HIS LYS ASN GLU LEU
SEQRES 9 B 135 LYS HIS VAL LYS TYR CYS GLN TYR ALA PHE ASP LEU LYS
SEQRES 10 B 135 CYS ASP SER VAL CYS VAL ASN PRO TYR HIS TYR GLU ARG
SEQRES 11 B 135 VAL VAL SER PRO GLY
SEQRES 1 D 16 DT DG DC DA DG DG DC DT DA DG DC DC DT
SEQRES 2 D 16 DG DC DA
SEQRES 1 E 16 DT DG DC DA DG DG DC DT DA DG DC DC DT
SEQRES 2 E 16 DG DC DA
HET ZN A 201 1
HET CL A 202 1
HET ZN B 201 1
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 CL CL 1-
FORMUL 8 HOH *7(H2 O)
HELIX 1 AA1 LEU A 17 CYS A 25 1 9
HELIX 2 AA2 SER A 32 LEU A 47 1 16
HELIX 3 AA3 LYS A 50 THR A 63 1 14
HELIX 4 AA4 PHE A 90 ARG A 100 1 11
HELIX 5 AA5 ALA A 118 LYS A 122 5 5
HELIX 6 AA6 ASN A 129 TYR A 131 5 3
HELIX 7 AA7 CYS B 16 CYS B 25 1 10
HELIX 8 AA8 SER B 32 LYS B 48 1 17
HELIX 9 AA9 LYS B 50 THR B 63 1 14
HELIX 10 AB1 PHE B 90 ARG B 100 1 11
HELIX 11 AB2 ALA B 118 LYS B 122 5 5
HELIX 12 AB3 ASN B 129 TYR B 131 5 3
SHEET 1 AA1 2 THR A 73 GLN A 75 0
SHEET 2 AA1 2 SER A 125 CYS A 127 -1 O VAL A 126 N ILE A 74
SHEET 1 AA2 2 LEU A 82 VAL A 84 0
SHEET 2 AA2 2 ARG A 87 GLY A 89 -1 O GLY A 89 N LEU A 82
SHEET 1 AA3 2 LEU A 109 HIS A 111 0
SHEET 2 AA3 2 TYR A 133 ARG A 135 -1 O GLU A 134 N LYS A 110
SHEET 1 AA4 2 THR B 73 GLN B 75 0
SHEET 2 AA4 2 SER B 125 CYS B 127 -1 O VAL B 126 N ILE B 74
SHEET 1 AA5 2 LEU B 82 VAL B 84 0
SHEET 2 AA5 2 ARG B 87 GLY B 89 -1 O GLY B 89 N LEU B 82
SHEET 1 AA6 2 LEU B 109 HIS B 111 0
SHEET 2 AA6 2 TYR B 133 ARG B 135 -1 O GLU B 134 N LYS B 110
LINK SG CYS A 71 ZN ZN A 201 1555 1555 2.38
LINK SG CYS A 115 ZN ZN A 201 1555 1555 2.15
LINK SG CYS A 127 ZN ZN A 201 1555 1555 2.35
LINK ND1 HIS A 132 ZN ZN A 201 1555 1555 2.04
LINK SG CYS B 71 ZN ZN B 201 1555 1555 2.36
LINK SG CYS B 115 ZN ZN B 201 1555 1555 2.16
LINK SG CYS B 127 ZN ZN B 201 1555 1555 2.17
LINK ND1 HIS B 132 ZN ZN B 201 1555 1555 1.93
SITE 1 AC1 4 CYS A 71 CYS A 115 CYS A 127 HIS A 132
SITE 1 AC2 5 ARG A 27 GLY A 29 GLY A 30 GLU A 31
SITE 2 AC2 5 LEU A 98
SITE 1 AC3 4 CYS B 71 CYS B 115 CYS B 127 HIS B 132
CRYST1 64.790 79.060 114.160 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015434 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012649 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008760 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
