HEADER CELL ADHESION 26-APR-12 4EVP
TITLE CRYSTAL STRUCTURE OF MOUSE CATENIN BETA-59 IN 7.2M UREA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CATENIN BETA-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 134-671;
COMPND 5 SYNONYM: BETA-CATENIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: CTNNB1, CATNB;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS MOUSE BETA CATENIN, UREA, CELL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WANG,G.Y.ZHANG
REVDAT 2 28-FEB-24 4EVP 1 REMARK
REVDAT 1 01-MAY-13 4EVP 0
JRNL AUTH C.WANG,G.Y.ZHANG
JRNL TITL CRYSTAL STRUCTURE OF MOUSE CATENIN BETA-59 IN 7.2M UREA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 29433
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 1494
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 47.0056 - 5.0128 1.00 2668 155 0.1982 0.2150
REMARK 3 2 5.0128 - 3.9795 1.00 2576 151 0.1651 0.2062
REMARK 3 3 3.9795 - 3.4766 1.00 2573 131 0.1728 0.2051
REMARK 3 4 3.4766 - 3.1588 1.00 2540 132 0.2003 0.2405
REMARK 3 5 3.1588 - 2.9325 1.00 2533 127 0.2018 0.2210
REMARK 3 6 2.9325 - 2.7596 1.00 2536 118 0.2007 0.2322
REMARK 3 7 2.7596 - 2.6214 1.00 2528 131 0.2015 0.2473
REMARK 3 8 2.6214 - 2.5073 1.00 2527 133 0.1989 0.2271
REMARK 3 9 2.5073 - 2.4108 1.00 2490 131 0.2059 0.2727
REMARK 3 10 2.4108 - 2.3276 1.00 2506 137 0.2130 0.2810
REMARK 3 11 2.3276 - 2.2548 0.98 2462 148 0.2293 0.2856
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 41.03
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.210
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.70730
REMARK 3 B22 (A**2) : 9.14410
REMARK 3 B33 (A**2) : -8.43690
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.005 3919
REMARK 3 ANGLE : 0.958 5273
REMARK 3 CHIRALITY : 0.061 627
REMARK 3 PLANARITY : 0.004 702
REMARK 3 DIHEDRAL : 13.528 1413
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4EVP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000072127.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAR-10
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 : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : 0.99
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29497
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.255
REMARK 200 RESOLUTION RANGE LOW (A) : 46.995
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 14.50
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.0600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.10
REMARK 200 R MERGE FOR SHELL (I) : 0.72900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.780
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 93.43550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 93.43550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.07700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.22050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.07700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.22050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 93.43550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.07700
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.22050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.43550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.07700
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.22050
REMARK 290 SMTRY3 8 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 C URE A 701 LIES ON A SPECIAL POSITION.
REMARK 375 O URE A 701 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 801 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 810 LIES ON A SPECIAL POSITION.
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 HIS A 134
REMARK 465 ALA A 135
REMARK 465 VAL A 136
REMARK 465 VAL A 137
REMARK 465 ASN A 138
REMARK 465 LEU A 139
REMARK 465 ILE A 140
REMARK 465 ASN A 141
REMARK 465 TYR A 142
REMARK 465 GLN A 143
REMARK 465 ASP A 144
REMARK 465 ASP A 145
REMARK 465 ALA A 146
REMARK 465 GLU A 147
REMARK 465 LEU A 148
REMARK 465 ALA A 149
REMARK 465 THR A 150
REMARK 465 ARG A 151
REMARK 465 ALA A 152
REMARK 465 ILE A 153
REMARK 465 PRO A 154
REMARK 465 GLU A 155
REMARK 465 LEU A 156
REMARK 465 THR A 157
REMARK 465 LYS A 158
REMARK 465 LEU A 159
REMARK 465 LEU A 160
REMARK 465 ASN A 161
REMARK 465 ARG A 550
REMARK 465 THR A 551
REMARK 465 SER A 552
REMARK 465 MET A 553
REMARK 465 GLY A 554
REMARK 465 GLY A 555
REMARK 465 THR A 556
REMARK 465 GLN A 557
REMARK 465 GLN A 558
REMARK 465 GLN A 559
REMARK 465 PHE A 560
REMARK 465 VAL A 561
REMARK 465 SER A 663
REMARK 465 GLU A 664
REMARK 465 ASP A 665
REMARK 465 LYS A 666
REMARK 465 PRO A 667
REMARK 465 GLN A 668
REMARK 465 ASP A 669
REMARK 465 TYR A 670
REMARK 465 LYS A 671
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 N1 URE A 740 O HOH A 978 1.93
REMARK 500 O HOH A 889 O HOH A 901 1.94
REMARK 500 O HOH A 867 O HOH A 877 2.01
REMARK 500 NH1 ARG A 469 O HOH A 922 2.02
REMARK 500 OH TYR A 254 N1 URE A 733 2.02
REMARK 500 O THR A 393 O HOH A 884 2.04
REMARK 500 OE2 GLU A 445 N1 URE A 739 2.09
REMARK 500 OG1 THR A 330 N1 URE A 735 2.11
REMARK 500 OE1 GLN A 538 O HOH A 854 2.13
REMARK 500 SG CYS A 466 O HOH A 912 2.13
REMARK 500 O URE A 710 O HOH A 824 2.15
REMARK 500 O HOH A 828 O HOH A 981 2.17
REMARK 500 OD1 ASP A 249 O HOH A 952 2.17
REMARK 500
REMARK 500 REMARK: NULL
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 OE1 GLU A 629 O HOH A 806 7655 1.88
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 GLU A 163 -169.66 -122.54
REMARK 500 VAL A 167 -61.96 -120.65
REMARK 500 LYS A 170 6.25 -57.17
REMARK 500 SER A 179 -10.72 -41.48
REMARK 500 LYS A 181 103.79 -57.80
REMARK 500 PRO A 192 41.60 -63.84
REMARK 500 GLN A 193 -29.19 -146.29
REMARK 500 ALA A 581 0.40 -69.44
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 URE A 709
REMARK 615 URE A 712
REMARK 615 URE A 715
REMARK 615 URE A 716
REMARK 615 URE A 718
REMARK 615 URE A 719
REMARK 615 URE A 721
REMARK 615 URE A 723
REMARK 615 URE A 724
REMARK 615 URE A 728
REMARK 615 URE A 729
REMARK 615 URE A 730
REMARK 615 URE A 735
REMARK 615 URE A 738
REMARK 615 URE A 739
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 714
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 715
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 716
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 717
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 718
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 719
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 720
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 721
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 722
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 723
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 724
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 725
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 726
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 727
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 728
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 729
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 730
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 731
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 732
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 733
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 734
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 735
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 736
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 737
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 738
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 739
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 740
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 741
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 742
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE URE A 743
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BCT RELATED DB: PDB
REMARK 900 RELATED ID: 4EV8 RELATED DB: PDB
REMARK 900 RELATED ID: 4EV9 RELATED DB: PDB
REMARK 900 RELATED ID: 4EVA RELATED DB: PDB
REMARK 900 RELATED ID: 4EVT RELATED DB: PDB
DBREF 4EVP A 134 671 UNP Q02248 CTNB1_MOUSE 134 671
SEQRES 1 A 538 HIS ALA VAL VAL ASN LEU ILE ASN TYR GLN ASP ASP ALA
SEQRES 2 A 538 GLU LEU ALA THR ARG ALA ILE PRO GLU LEU THR LYS LEU
SEQRES 3 A 538 LEU ASN ASP GLU ASP GLN VAL VAL VAL ASN LYS ALA ALA
SEQRES 4 A 538 VAL MET VAL HIS GLN LEU SER LYS LYS GLU ALA SER ARG
SEQRES 5 A 538 HIS ALA ILE MET ARG SER PRO GLN MET VAL SER ALA ILE
SEQRES 6 A 538 VAL ARG THR MET GLN ASN THR ASN ASP VAL GLU THR ALA
SEQRES 7 A 538 ARG CYS THR ALA GLY THR LEU HIS ASN LEU SER HIS HIS
SEQRES 8 A 538 ARG GLU GLY LEU LEU ALA ILE PHE LYS SER GLY GLY ILE
SEQRES 9 A 538 PRO ALA LEU VAL LYS MET LEU GLY SER PRO VAL ASP SER
SEQRES 10 A 538 VAL LEU PHE TYR ALA ILE THR THR LEU HIS ASN LEU LEU
SEQRES 11 A 538 LEU HIS GLN GLU GLY ALA LYS MET ALA VAL ARG LEU ALA
SEQRES 12 A 538 GLY GLY LEU GLN LYS MET VAL ALA LEU LEU ASN LYS THR
SEQRES 13 A 538 ASN VAL LYS PHE LEU ALA ILE THR THR ASP CYS LEU GLN
SEQRES 14 A 538 ILE LEU ALA TYR GLY ASN GLN GLU SER LYS LEU ILE ILE
SEQRES 15 A 538 LEU ALA SER GLY GLY PRO GLN ALA LEU VAL ASN ILE MET
SEQRES 16 A 538 ARG THR TYR THR TYR GLU LYS LEU LEU TRP THR THR SER
SEQRES 17 A 538 ARG VAL LEU LYS VAL LEU SER VAL CYS SER SER ASN LYS
SEQRES 18 A 538 PRO ALA ILE VAL GLU ALA GLY GLY MET GLN ALA LEU GLY
SEQRES 19 A 538 LEU HIS LEU THR ASP PRO SER GLN ARG LEU VAL GLN ASN
SEQRES 20 A 538 CYS LEU TRP THR LEU ARG ASN LEU SER ASP ALA ALA THR
SEQRES 21 A 538 LYS GLN GLU GLY MET GLU GLY LEU LEU GLY THR LEU VAL
SEQRES 22 A 538 GLN LEU LEU GLY SER ASP ASP ILE ASN VAL VAL THR CYS
SEQRES 23 A 538 ALA ALA GLY ILE LEU SER ASN LEU THR CYS ASN ASN TYR
SEQRES 24 A 538 LYS ASN LYS MET MET VAL CYS GLN VAL GLY GLY ILE GLU
SEQRES 25 A 538 ALA LEU VAL ARG THR VAL LEU ARG ALA GLY ASP ARG GLU
SEQRES 26 A 538 ASP ILE THR GLU PRO ALA ILE CYS ALA LEU ARG HIS LEU
SEQRES 27 A 538 THR SER ARG HIS GLN GLU ALA GLU MET ALA GLN ASN ALA
SEQRES 28 A 538 VAL ARG LEU HIS TYR GLY LEU PRO VAL VAL VAL LYS LEU
SEQRES 29 A 538 LEU HIS PRO PRO SER HIS TRP PRO LEU ILE LYS ALA THR
SEQRES 30 A 538 VAL GLY LEU ILE ARG ASN LEU ALA LEU CYS PRO ALA ASN
SEQRES 31 A 538 HIS ALA PRO LEU ARG GLU GLN GLY ALA ILE PRO ARG LEU
SEQRES 32 A 538 VAL GLN LEU LEU VAL ARG ALA HIS GLN ASP THR GLN ARG
SEQRES 33 A 538 ARG THR SER MET GLY GLY THR GLN GLN GLN PHE VAL GLU
SEQRES 34 A 538 GLY VAL ARG MET GLU GLU ILE VAL GLU GLY CYS THR GLY
SEQRES 35 A 538 ALA LEU HIS ILE LEU ALA ARG ASP VAL HIS ASN ARG ILE
SEQRES 36 A 538 VAL ILE ARG GLY LEU ASN THR ILE PRO LEU PHE VAL GLN
SEQRES 37 A 538 LEU LEU TYR SER PRO ILE GLU ASN ILE GLN ARG VAL ALA
SEQRES 38 A 538 ALA GLY VAL LEU CYS GLU LEU ALA GLN ASP LYS GLU ALA
SEQRES 39 A 538 ALA GLU ALA ILE GLU ALA GLU GLY ALA THR ALA PRO LEU
SEQRES 40 A 538 THR GLU LEU LEU HIS SER ARG ASN GLU GLY VAL ALA THR
SEQRES 41 A 538 TYR ALA ALA ALA VAL LEU PHE ARG MET SER GLU ASP LYS
SEQRES 42 A 538 PRO GLN ASP TYR LYS
HET URE A 701 4
HET URE A 702 4
HET URE A 703 4
HET URE A 704 4
HET URE A 705 4
HET URE A 706 4
HET URE A 707 4
HET URE A 708 4
HET URE A 709 4
HET URE A 710 4
HET URE A 711 4
HET URE A 712 4
HET URE A 713 4
HET URE A 714 4
HET URE A 715 4
HET URE A 716 4
HET URE A 717 4
HET URE A 718 4
HET URE A 719 4
HET URE A 720 4
HET URE A 721 4
HET URE A 722 4
HET URE A 723 4
HET URE A 724 4
HET URE A 725 4
HET URE A 726 4
HET URE A 727 4
HET URE A 728 4
HET URE A 729 4
HET URE A 730 4
HET URE A 731 4
HET URE A 732 4
HET URE A 733 4
HET URE A 734 4
HET URE A 735 4
HET URE A 736 4
HET URE A 737 4
HET URE A 738 4
HET URE A 739 4
HET URE A 740 4
HET URE A 741 4
HET URE A 742 4
HET URE A 743 4
HETNAM URE UREA
FORMUL 2 URE 43(C H4 N2 O)
FORMUL 45 HOH *191(H2 O)
HELIX 1 1 VAL A 168 LYS A 170 5 3
HELIX 2 2 ALA A 171 SER A 179 1 9
HELIX 3 3 LYS A 181 MET A 189 1 9
HELIX 4 4 GLN A 193 THR A 205 1 13
HELIX 5 5 ASP A 207 SER A 222 1 16
HELIX 6 6 HIS A 224 SER A 234 1 11
HELIX 7 7 GLY A 235 MET A 243 1 9
HELIX 8 8 LEU A 244 SER A 246 5 3
HELIX 9 9 VAL A 248 GLN A 266 1 19
HELIX 10 10 GLY A 268 ALA A 276 1 9
HELIX 11 11 GLY A 277 LEU A 285 1 9
HELIX 12 12 LEU A 286 LYS A 288 5 3
HELIX 13 13 ASN A 290 TYR A 306 1 17
HELIX 14 14 ASN A 308 SER A 318 1 11
HELIX 15 15 GLY A 319 TYR A 331 1 13
HELIX 16 16 TYR A 333 SER A 348 1 16
HELIX 17 17 SER A 352 ALA A 360 1 9
HELIX 18 18 GLY A 361 LEU A 368 1 8
HELIX 19 19 SER A 374 ASP A 390 1 17
HELIX 20 20 MET A 398 LEU A 409 1 12
HELIX 21 21 ASP A 413 CYS A 429 1 17
HELIX 22 22 ASN A 431 VAL A 441 1 11
HELIX 23 23 GLY A 442 GLY A 455 1 14
HELIX 24 24 ARG A 457 THR A 472 1 16
HELIX 25 25 GLU A 477 HIS A 488 1 12
HELIX 26 26 GLY A 490 LEU A 497 1 8
HELIX 27 27 HIS A 503 ALA A 518 1 16
HELIX 28 28 LEU A 519 ALA A 522 5 4
HELIX 29 29 ASN A 523 GLN A 530 1 8
HELIX 30 30 GLY A 531 GLN A 548 1 18
HELIX 31 31 ARG A 565 ALA A 581 1 17
HELIX 32 32 ASP A 583 LEU A 593 1 11
HELIX 33 33 THR A 595 LEU A 603 1 9
HELIX 34 34 ILE A 607 ALA A 622 1 16
HELIX 35 35 ASP A 624 GLU A 634 1 11
HELIX 36 36 ALA A 636 LEU A 644 1 9
HELIX 37 37 ASN A 648 MET A 662 1 15
CISPEP 1 PRO A 500 PRO A 501 0 6.97
SITE 1 AC1 3 THR A 330 TYR A 331 HOH A 803
SITE 1 AC2 5 THR A 332 GLU A 334 ASP A 372 HOH A 817
SITE 2 AC2 5 HOH A 892
SITE 1 AC3 5 ARG A 474 LEU A 644 HIS A 645 SER A 646
SITE 2 AC3 5 ALA A 652
SITE 1 AC4 5 LEU A 286 ASN A 287 LYS A 288 TYR A 331
SITE 2 AC4 5 URE A 735
SITE 1 AC5 9 THR A 289 ASN A 290 VAL A 291 THR A 330
SITE 2 AC5 9 THR A 332 URE A 718 URE A 732 HOH A 837
SITE 3 AC5 9 HOH A 872
SITE 1 AC6 6 VAL A 358 GLU A 359 ALA A 360 GLY A 361
SITE 2 AC6 6 GLN A 395 HOH A 886
SITE 1 AC7 2 VAL A 349 GLU A 629
SITE 1 AC8 6 ASN A 430 LYS A 435 HIS A 470 ARG A 474
SITE 2 AC8 6 ARG A 647 HOH A 957
SITE 1 AC9 3 GLN A 302 TYR A 306 HOH A 976
SITE 1 BC1 3 PRO A 355 GLU A 359 HOH A 824
SITE 1 BC2 4 VAL A 541 LEU A 593 ASN A 594 HOH A 982
SITE 1 BC3 2 TYR A 604 PRO A 606
SITE 1 BC4 4 PRO A 606 ILE A 607 GLU A 608 HOH A 842
SITE 1 BC5 4 GLU A 310 ARG A 486 TYR A 489 URE A 729
SITE 1 BC6 3 GLN A 280 LEU A 487 HIS A 488
SITE 1 BC7 3 ARG A 582 GLU A 620 HOH A 900
SITE 1 BC8 4 LYS A 270 ALA A 633 GLU A 634 HOH A 949
SITE 1 BC9 7 THR A 289 ASN A 290 ARG A 329 URE A 705
SITE 2 BC9 7 URE A 732 HOH A 939 HOH A 951
SITE 1 CC1 2 LYS A 354 ASN A 387
SITE 1 CC2 4 GLY A 367 GLY A 400 THR A 404 HOH A 834
SITE 1 CC3 3 GLN A 407 GLY A 410 SER A 411
SITE 1 CC4 4 SER A 502 URE A 728 URE A 743 HOH A 868
SITE 1 CC5 1 ASN A 594
SITE 1 CC6 4 ARG A 612 GLU A 649 GLY A 650 TYR A 654
SITE 1 CC7 4 ASP A 456 ARG A 457 GLU A 458 ASP A 459
SITE 1 CC8 4 ARG A 515 ASN A 516 HOH A 832 HOH A 973
SITE 1 CC9 4 PRO A 501 SER A 502 HIS A 503 URE A 728
SITE 1 DC1 5 HIS A 503 TRP A 504 URE A 722 URE A 727
SITE 2 DC1 5 HOH A 911
SITE 1 DC2 3 LEU A 313 URE A 714 HOH A 871
SITE 1 DC3 6 LEU A 603 TYR A 604 SER A 605 GLN A 611
SITE 2 DC3 6 GLU A 642 URE A 741
SITE 1 DC4 4 LEU A 368 THR A 371 ASP A 372 HOH A 838
SITE 1 DC5 5 ARG A 329 LEU A 368 URE A 705 URE A 718
SITE 2 DC5 5 HOH A 872
SITE 1 DC6 3 HIS A 176 LYS A 180 TYR A 254
SITE 1 DC7 4 VAL A 349 CYS A 350 SER A 351 GLU A 626
SITE 1 DC8 3 ASN A 326 THR A 330 URE A 704
SITE 1 DC9 2 CYS A 429 ASN A 430
SITE 1 EC1 5 LYS A 394 ASN A 430 ASN A 431 TYR A 432
SITE 2 EC1 5 LYS A 433
SITE 1 EC2 3 CYS A 439 MET A 480 HOH A 820
SITE 1 EC3 5 GLU A 445 ARG A 449 HOH A 895 HOH A 936
SITE 2 EC3 5 HOH A 981
SITE 1 EC4 4 TYR A 604 GLY A 635 ALA A 638 HOH A 978
SITE 1 EC5 5 GLU A 642 LEU A 643 HIS A 645 SER A 646
SITE 2 EC5 5 URE A 730
SITE 1 EC6 2 GLU A 608 ARG A 647
SITE 1 EC7 4 PRO A 500 ARG A 542 URE A 722 HOH A 845
CRYST1 64.154 102.441 186.871 90.00 90.00 90.00 C 2 2 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 0.015587 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009762 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005351 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
