HEADER LIGASE 22-AUG-18 6M91
TITLE MONOPHOSPHORYLATED PSER33 B-CATENIN PEPTIDE, B-TRCP/SKP1, NRX-103094
TITLE 2 TERNARY COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: F-BOX/WD REPEAT-CONTAINING PROTEIN 1A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: E3RSIKAPPAB,EPIDIDYMIS TISSUE PROTEIN LI 2A,F-BOX AND WD
COMPND 5 REPEATS PROTEIN BETA-TRCP,PIKAPPABALPHA-E3 RECEPTOR SUBUNIT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: S-PHASE KINASE-ASSOCIATED PROTEIN 1;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: CYCLIN-A/CDK2-ASSOCIATED PROTEIN P19,P19A,ORGAN OF CORTI
COMPND 11 PROTEIN 2,OCP-2,ORGAN OF CORTI PROTEIN II,OCP-II,RNA POLYMERASE II
COMPND 12 ELONGATION FACTOR-LIKE PROTEIN,SIII,TRANSCRIPTION ELONGATION FACTOR B
COMPND 13 POLYPEPTIDE 1-LIKE,P19SKP1;
COMPND 14 ENGINEERED: YES;
COMPND 15 MOL_ID: 3;
COMPND 16 MOLECULE: CATENIN BETA-1;
COMPND 17 CHAIN: C;
COMPND 18 SYNONYM: BETA-CATENIN;
COMPND 19 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: BTRC, BTRCP, FBW1A, FBXW1A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: SKP1, EMC19, OCP2, SKP1A, TCEB1L;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606
KEYWDS UBIQUITIN MOLECULAR GLUE ENHANCER, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.R.SIMONETTA,M.C.CLIFTON,R.L.WALTER,G.M.RANIERI,J.J.CARTER
REVDAT 2 10-APR-19 6M91 1 JRNL
REVDAT 1 03-APR-19 6M91 0
JRNL AUTH K.R.SIMONETTA,J.TAYGERLY,K.BOYLE,S.E.BASHAM,C.PADOVANI,
JRNL AUTH 2 Y.LOU,T.J.CUMMINS,S.L.YUNG,S.K.VON SOLY,F.KAYSER,J.KURIYAN,
JRNL AUTH 3 M.RAPE,M.CARDOZO,M.A.GALLOP,N.F.BENCE,P.A.BARSANTI,A.SAHA
JRNL TITL PROSPECTIVE DISCOVERY OF SMALL MOLECULE ENHANCERS OF AN E3
JRNL TITL 2 LIGASE-SUBSTRATE INTERACTION.
JRNL REF NAT COMMUN V. 10 1402 2019
JRNL REFN ESSN 2041-1723
JRNL PMID 30926793
JRNL DOI 10.1038/S41467-019-09358-9
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 33155
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.760
REMARK 3 FREE R VALUE TEST SET COUNT : 1245
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 44.0705 - 4.9902 0.99 3533 135 0.1713 0.2008
REMARK 3 2 4.9902 - 3.9616 1.00 3533 142 0.1577 0.1717
REMARK 3 3 3.9616 - 3.4611 1.00 3573 127 0.1898 0.2140
REMARK 3 4 3.4611 - 3.1447 1.00 3578 131 0.2104 0.2285
REMARK 3 5 3.1447 - 2.9194 1.00 3536 140 0.2291 0.2791
REMARK 3 6 2.9194 - 2.7473 1.00 3536 144 0.2370 0.2754
REMARK 3 7 2.7473 - 2.6097 1.00 3560 140 0.2589 0.3018
REMARK 3 8 2.6097 - 2.4961 0.99 3519 140 0.2716 0.3113
REMARK 3 9 2.4961 - 2.4000 0.99 3542 146 0.3156 0.3325
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 68.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 138 THROUGH 252 )
REMARK 3 ORIGIN FOR THE GROUP (A): 33.5083 -43.5830 -11.5324
REMARK 3 T TENSOR
REMARK 3 T11: 1.0527 T22: 0.7475
REMARK 3 T33: 0.9171 T12: 0.3794
REMARK 3 T13: 0.0560 T23: -0.0382
REMARK 3 L TENSOR
REMARK 3 L11: 1.3314 L22: 1.9275
REMARK 3 L33: 0.4557 L12: -0.1409
REMARK 3 L13: 0.4767 L23: 0.5512
REMARK 3 S TENSOR
REMARK 3 S11: 0.0444 S12: 0.1873 S13: 0.4129
REMARK 3 S21: -0.0958 S22: -0.1610 S23: 0.0946
REMARK 3 S31: 0.0859 S32: 0.1920 S33: 0.1004
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 548 )
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4421 -13.4314 -1.6466
REMARK 3 T TENSOR
REMARK 3 T11: 0.7374 T22: 0.3676
REMARK 3 T33: 0.6135 T12: 0.1018
REMARK 3 T13: -0.0753 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 3.2216 L22: 2.2841
REMARK 3 L33: 2.5514 L12: -0.6705
REMARK 3 L13: -0.0892 L23: -0.1586
REMARK 3 S TENSOR
REMARK 3 S11: 0.2394 S12: 0.1515 S13: -0.2347
REMARK 3 S21: -0.0171 S22: -0.1141 S23: -0.3180
REMARK 3 S31: 0.1882 S32: 0.0022 S33: -0.1131
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 2 THROUGH 58 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.8164 -69.4707 -9.2563
REMARK 3 T TENSOR
REMARK 3 T11: 0.9732 T22: 1.4715
REMARK 3 T33: 0.9711 T12: 0.1775
REMARK 3 T13: 0.3763 T23: 0.0548
REMARK 3 L TENSOR
REMARK 3 L11: 3.8469 L22: 1.3975
REMARK 3 L33: 1.5140 L12: -0.3228
REMARK 3 L13: -0.5916 L23: 0.6480
REMARK 3 S TENSOR
REMARK 3 S11: -0.0633 S12: -0.5873 S13: 0.1188
REMARK 3 S21: 0.5921 S22: -0.3435 S23: 0.7915
REMARK 3 S31: 0.0191 S32: -1.2736 S33: 0.3817
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 59 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 18.3344 -59.5611 4.4838
REMARK 3 T TENSOR
REMARK 3 T11: 1.2485 T22: 1.3238
REMARK 3 T33: 0.8304 T12: 0.1841
REMARK 3 T13: 0.3653 T23: -0.1548
REMARK 3 L TENSOR
REMARK 3 L11: 1.1735 L22: 2.2535
REMARK 3 L33: 4.0614 L12: 0.4425
REMARK 3 L13: 1.5588 L23: -1.4518
REMARK 3 S TENSOR
REMARK 3 S11: 0.7452 S12: -0.1302 S13: 0.4563
REMARK 3 S21: 0.1995 S22: -1.3596 S23: 0.3398
REMARK 3 S31: -0.4309 S32: -0.6669 S33: 0.4504
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 79 THROUGH 139 )
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0029 -57.5171 -5.9798
REMARK 3 T TENSOR
REMARK 3 T11: 1.1124 T22: 0.8267
REMARK 3 T33: 0.6264 T12: 0.4440
REMARK 3 T13: 0.1004 T23: 0.0125
REMARK 3 L TENSOR
REMARK 3 L11: 5.7483 L22: 3.2679
REMARK 3 L33: 1.7221 L12: 1.2966
REMARK 3 L13: 0.5666 L23: 0.0759
REMARK 3 S TENSOR
REMARK 3 S11: 0.0251 S12: -0.3329 S13: 0.1556
REMARK 3 S21: 0.9104 S22: -0.0057 S23: -0.2069
REMARK 3 S31: -0.2824 S32: -0.3690 S33: 0.1063
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 29 THROUGH 38 )
REMARK 3 ORIGIN FOR THE GROUP (A): 7.0595 -0.2166 3.9811
REMARK 3 T TENSOR
REMARK 3 T11: 0.9790 T22: 0.5074
REMARK 3 T33: 0.5238 T12: 0.1247
REMARK 3 T13: -0.0403 T23: -0.0343
REMARK 3 L TENSOR
REMARK 3 L11: 2.0224 L22: 1.5806
REMARK 3 L33: 5.6932 L12: -1.1730
REMARK 3 L13: 0.1284 L23: -1.2510
REMARK 3 S TENSOR
REMARK 3 S11: 0.2254 S12: -0.4823 S13: 0.6415
REMARK 3 S21: 0.4935 S22: -0.5310 S23: 0.0272
REMARK 3 S31: -0.5421 S32: -0.2353 S33: 0.1965
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 6M91 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1000236372.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-15
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 : CLSI
REMARK 200 BEAMLINE : 08ID-1
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33157
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 44.063
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 4.232
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.6900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.25
REMARK 200 R MERGE FOR SHELL (I) : 1.39100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.990
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 4000 0.1M BTP PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 37.32000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 74.64000
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 LYS A 218
REMARK 465 ASN A 219
REMARK 465 LYS A 220
REMARK 465 PRO A 221
REMARK 465 PRO A 222
REMARK 465 ASP A 223
REMARK 465 GLY A 224
REMARK 465 ASN A 225
REMARK 465 ALA A 226
REMARK 465 ASP A 549
REMARK 465 PRO A 550
REMARK 465 ALA A 551
REMARK 465 ALA A 552
REMARK 465 GLN A 553
REMARK 465 ALA A 554
REMARK 465 GLU A 555
REMARK 465 PRO A 556
REMARK 465 PRO A 557
REMARK 465 ARG A 558
REMARK 465 SER A 559
REMARK 465 PRO A 560
REMARK 465 SER A 561
REMARK 465 ARG A 562
REMARK 465 THR A 563
REMARK 465 TYR A 564
REMARK 465 THR A 565
REMARK 465 TYR A 566
REMARK 465 ILE A 567
REMARK 465 SER A 568
REMARK 465 ARG A 569
REMARK 465 ASP B 61
REMARK 465 ASP B 62
REMARK 465 PRO B 63
REMARK 465 PRO B 64
REMARK 465 ASP B 65
REMARK 465 ASP B 66
REMARK 465 GLN B 140
REMARK 465 TRP B 141
REMARK 465 CYS B 142
REMARK 465 GLU B 143
REMARK 465 GLU B 144
REMARK 465 LYS B 145
REMARK 465 CYS C 16
REMARK 465 ASP C 17
REMARK 465 ARG C 18
REMARK 465 LYS C 19
REMARK 465 ALA C 20
REMARK 465 ALA C 21
REMARK 465 VAL C 22
REMARK 465 SER C 23
REMARK 465 HIS C 24
REMARK 465 TRP C 25
REMARK 465 GLN C 26
REMARK 465 GLN C 27
REMARK 465 GLN C 28
REMARK 465 ALA C 39
REMARK 465 THR C 40
REMARK 465 THR C 41
REMARK 465 THR C 42
REMARK 465 ALA C 43
REMARK 465 PRO C 44
REMARK 465 SER C 45
REMARK 465 LEU C 46
REMARK 465 SER C 47
REMARK 465 GLY C 48
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 SER A 138 OG
REMARK 470 LYS A 167 CG CD CE NZ
REMARK 470 GLU A 208 CG CD OE1 OE2
REMARK 470 GLN A 214 CG CD OE1 NE2
REMARK 470 GLU A 244 CG CD OE1 OE2
REMARK 470 ARG A 251 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 254 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 298 CG CD OE1 OE2
REMARK 470 LYS A 300 CG CD CE NZ
REMARK 470 ASN A 357 CG OD1 ND2
REMARK 470 LYS A 430 CG CD CE NZ
REMARK 470 GLU A 471 CG CD OE1 OE2
REMARK 470 ARG A 504 CG CD NE CZ NH1 NH2
REMARK 470 PRO B 2 CG CD
REMARK 470 ILE B 4 CG1 CG2 CD1
REMARK 470 LYS B 5 CG CD CE NZ
REMARK 470 GLU B 15 CG CD OE1 OE2
REMARK 470 ASP B 17 CG OD1 OD2
REMARK 470 GLU B 19 CG CD OE1 OE2
REMARK 470 ILE B 20 CG1 CG2 CD1
REMARK 470 LYS B 28 CG CD CE NZ
REMARK 470 LYS B 50 CG CD CE NZ
REMARK 470 LYS B 51 CG CD CE NZ
REMARK 470 LYS B 60 CG CD CE NZ
REMARK 470 LYS B 76 CG CD CE NZ
REMARK 470 LYS B 95 CG CD CE NZ
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 LYS B 110 CG CD CE NZ
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 LYS B 119 CG CD CE NZ
REMARK 470 GLU B 129 CG CD OE1 OE2
REMARK 470 GLU B 130 CG CD OE1 OE2
REMARK 470 ARG B 136 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 137 CG CD CE NZ
REMARK 470 SER C 29 OG
REMARK 470 TYR C 30 CG CD1 CD2 CE1 CE2 CZ OH
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 OD2 ASP A 154 NH2 ARG A 390 3544 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 266 -79.21 -119.00
REMARK 500 ASN A 287 2.95 88.00
REMARK 500 ASP A 316 -159.36 -130.71
REMARK 500 SER A 327 7.22 80.06
REMARK 500 HIS A 345 -54.90 -163.75
REMARK 500 ASN A 356 137.35 -175.63
REMARK 500 ARG A 367 7.34 83.22
REMARK 500 ASP A 440 -113.39 60.30
REMARK 500 ARG A 464 137.22 -172.04
REMARK 500 ASP A 479 -149.26 -123.48
REMARK 500 LEU C 31 13.87 -68.08
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 J97 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 101
DBREF 6M91 A 139 569 UNP Q9Y297 FBW1A_HUMAN 175 605
DBREF 6M91 B 2 145 UNP P63208 SKP1_HUMAN 2 163
DBREF 6M91 C 17 48 UNP P35222 CTNB1_HUMAN 17 48
SEQADV 6M91 SER A 138 UNP Q9Y297 EXPRESSION TAG
SEQADV 6M91 B UNP P63208 ASP 37 DELETION
SEQADV 6M91 B UNP P63208 ASP 38 DELETION
SEQADV 6M91 B UNP P63208 GLU 39 DELETION
SEQADV 6M91 B UNP P63208 GLY 40 DELETION
SEQADV 6M91 B UNP P63208 ASP 41 DELETION
SEQADV 6M91 B UNP P63208 ASP 42 DELETION
SEQADV 6M91 B UNP P63208 PRO 71 DELETION
SEQADV 6M91 B UNP P63208 PRO 72 DELETION
SEQADV 6M91 B UNP P63208 GLU 73 DELETION
SEQADV 6M91 B UNP P63208 ASP 74 DELETION
SEQADV 6M91 B UNP P63208 ASP 75 DELETION
SEQADV 6M91 B UNP P63208 GLU 76 DELETION
SEQADV 6M91 B UNP P63208 ASN 77 DELETION
SEQADV 6M91 B UNP P63208 LYS 78 DELETION
SEQADV 6M91 B UNP P63208 GLU 79 DELETION
SEQADV 6M91 B UNP P63208 LYS 80 DELETION
SEQADV 6M91 B UNP P63208 ARG 81 DELETION
SEQADV 6M91 B UNP P63208 THR 82 DELETION
SEQADV 6M91 CYS C 16 UNP P35222 EXPRESSION TAG
SEQADV 6M91 ALA C 37 UNP P35222 SER 37 CONFLICT
SEQRES 1 A 432 SER MET LEU GLN ARG ASP PHE ILE THR ALA LEU PRO ALA
SEQRES 2 A 432 ARG GLY LEU ASP HIS ILE ALA GLU ASN ILE LEU SER TYR
SEQRES 3 A 432 LEU ASP ALA LYS SER LEU CYS ALA ALA GLU LEU VAL CYS
SEQRES 4 A 432 LYS GLU TRP TYR ARG VAL THR SER ASP GLY MET LEU TRP
SEQRES 5 A 432 LYS LYS LEU ILE GLU ARG MET VAL ARG THR ASP SER LEU
SEQRES 6 A 432 TRP ARG GLY LEU ALA GLU ARG ARG GLY TRP GLY GLN TYR
SEQRES 7 A 432 LEU PHE LYS ASN LYS PRO PRO ASP GLY ASN ALA PRO PRO
SEQRES 8 A 432 ASN SER PHE TYR ARG ALA LEU TYR PRO LYS ILE ILE GLN
SEQRES 9 A 432 ASP ILE GLU THR ILE GLU SER ASN TRP ARG CYS GLY ARG
SEQRES 10 A 432 HIS SER LEU GLN ARG ILE HIS CYS ARG SER GLU THR SER
SEQRES 11 A 432 LYS GLY VAL TYR CYS LEU GLN TYR ASP ASP GLN LYS ILE
SEQRES 12 A 432 VAL SER GLY LEU ARG ASP ASN THR ILE LYS ILE TRP ASP
SEQRES 13 A 432 LYS ASN THR LEU GLU CYS LYS ARG ILE LEU THR GLY HIS
SEQRES 14 A 432 THR GLY SER VAL LEU CYS LEU GLN TYR ASP GLU ARG VAL
SEQRES 15 A 432 ILE ILE THR GLY SER SER ASP SER THR VAL ARG VAL TRP
SEQRES 16 A 432 ASP VAL ASN THR GLY GLU MET LEU ASN THR LEU ILE HIS
SEQRES 17 A 432 HIS CYS GLU ALA VAL LEU HIS LEU ARG PHE ASN ASN GLY
SEQRES 18 A 432 MET MET VAL THR CYS SER LYS ASP ARG SER ILE ALA VAL
SEQRES 19 A 432 TRP ASP MET ALA SER PRO THR ASP ILE THR LEU ARG ARG
SEQRES 20 A 432 VAL LEU VAL GLY HIS ARG ALA ALA VAL ASN VAL VAL ASP
SEQRES 21 A 432 PHE ASP ASP LYS TYR ILE VAL SER ALA SER GLY ASP ARG
SEQRES 22 A 432 THR ILE LYS VAL TRP ASN THR SER THR CYS GLU PHE VAL
SEQRES 23 A 432 ARG THR LEU ASN GLY HIS LYS ARG GLY ILE ALA CYS LEU
SEQRES 24 A 432 GLN TYR ARG ASP ARG LEU VAL VAL SER GLY SER SER ASP
SEQRES 25 A 432 ASN THR ILE ARG LEU TRP ASP ILE GLU CYS GLY ALA CYS
SEQRES 26 A 432 LEU ARG VAL LEU GLU GLY HIS GLU GLU LEU VAL ARG CYS
SEQRES 27 A 432 ILE ARG PHE ASP ASN LYS ARG ILE VAL SER GLY ALA TYR
SEQRES 28 A 432 ASP GLY LYS ILE LYS VAL TRP ASP LEU VAL ALA ALA LEU
SEQRES 29 A 432 ASP PRO ARG ALA PRO ALA GLY THR LEU CYS LEU ARG THR
SEQRES 30 A 432 LEU VAL GLU HIS SER GLY ARG VAL PHE ARG LEU GLN PHE
SEQRES 31 A 432 ASP GLU PHE GLN ILE VAL SER SER SER HIS ASP ASP THR
SEQRES 32 A 432 ILE LEU ILE TRP ASP PHE LEU ASN ASP PRO ALA ALA GLN
SEQRES 33 A 432 ALA GLU PRO PRO ARG SER PRO SER ARG THR TYR THR TYR
SEQRES 34 A 432 ILE SER ARG
SEQRES 1 B 144 PRO SER ILE LYS LEU GLN SER SER ASP GLY GLU ILE PHE
SEQRES 2 B 144 GLU VAL ASP VAL GLU ILE ALA LYS GLN SER VAL THR ILE
SEQRES 3 B 144 LYS THR MET LEU GLU ASP LEU GLY MET ASP PRO VAL PRO
SEQRES 4 B 144 LEU PRO ASN VAL ASN ALA ALA ILE LEU LYS LYS VAL ILE
SEQRES 5 B 144 GLN TRP CYS THR HIS HIS LYS ASP ASP PRO PRO ASP ASP
SEQRES 6 B 144 ILE PRO VAL TRP ASP GLN GLU PHE LEU LYS VAL ASP GLN
SEQRES 7 B 144 GLY THR LEU PHE GLU LEU ILE LEU ALA ALA ASN TYR LEU
SEQRES 8 B 144 ASP ILE LYS GLY LEU LEU ASP VAL THR CYS LYS THR VAL
SEQRES 9 B 144 ALA ASN MET ILE LYS GLY LYS THR PRO GLU GLU ILE ARG
SEQRES 10 B 144 LYS THR PHE ASN ILE LYS ASN ASP PHE THR GLU GLU GLU
SEQRES 11 B 144 GLU ALA GLN VAL ARG LYS GLU ASN GLN TRP CYS GLU GLU
SEQRES 12 B 144 LYS
SEQRES 1 C 33 CYS ASP ARG LYS ALA ALA VAL SER HIS TRP GLN GLN GLN
SEQRES 2 C 33 SER TYR LEU ASP SEP GLY ILE HIS ALA GLY ALA THR THR
SEQRES 3 C 33 THR ALA PRO SER LEU SER GLY
MODRES 6M91 SEP C 33 SER MODIFIED RESIDUE
HET SEP C 33 10
HET J97 A 601 32
HET PO4 A 602 5
HET CL C 101 1
HETNAM SEP PHOSPHOSERINE
HETNAM J97 3-({4-[(2,6-DICHLOROPHENYL)SULFANYL]-2-OXO-6-
HETNAM 2 J97 (TRIFLUOROMETHYL)-1,2-DIHYDROPYRIDINE-3-
HETNAM 3 J97 CARBONYL}AMINO)BENZOIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM CL CHLORIDE ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 3 SEP C3 H8 N O6 P
FORMUL 4 J97 C20 H11 CL2 F3 N2 O4 S
FORMUL 5 PO4 O4 P 3-
FORMUL 6 CL CL 1-
FORMUL 7 HOH *25(H2 O)
HELIX 1 AA1 ASP A 143 ARG A 151 1 9
HELIX 2 AA2 LEU A 153 SER A 162 1 10
HELIX 3 AA3 ASP A 165 LEU A 174 1 10
HELIX 4 AA4 CYS A 176 GLY A 186 1 11
HELIX 5 AA5 MET A 187 ASP A 200 1 14
HELIX 6 AA6 ASP A 200 GLY A 211 1 12
HELIX 7 AA7 TRP A 212 LEU A 216 5 5
HELIX 8 AA8 PRO A 228 GLY A 253 1 26
HELIX 9 AA9 LEU A 497 ASP A 502 1 6
HELIX 10 AB1 PRO A 506 THR A 509 5 4
HELIX 11 AB2 VAL B 18 LYS B 22 1 5
HELIX 12 AB3 SER B 24 ASP B 33 1 10
HELIX 13 AB4 ASN B 45 HIS B 59 1 15
HELIX 14 AB5 PRO B 68 LEU B 75 1 8
HELIX 15 AB6 ASP B 78 ASP B 93 1 16
HELIX 16 AB7 ILE B 94 LYS B 110 1 17
HELIX 17 AB8 THR B 113 ASN B 122 1 10
HELIX 18 AB9 THR B 128 GLU B 138 1 11
SHEET 1 AA1 4 SER A 256 HIS A 261 0
SHEET 2 AA1 4 THR A 540 ASP A 545 -1 O ILE A 541 N ILE A 260
SHEET 3 AA1 4 GLN A 531 SER A 536 -1 N ILE A 532 O TRP A 544
SHEET 4 AA1 4 VAL A 522 PHE A 527 -1 N GLN A 526 O VAL A 533
SHEET 1 AA2 4 VAL A 270 TYR A 275 0
SHEET 2 AA2 4 LYS A 279 LEU A 284 -1 O VAL A 281 N GLN A 274
SHEET 3 AA2 4 ILE A 289 ASP A 293 -1 O TRP A 292 N ILE A 280
SHEET 4 AA2 4 CYS A 299 LEU A 303 -1 O LEU A 303 N ILE A 289
SHEET 1 AA3 4 VAL A 310 TYR A 315 0
SHEET 2 AA3 4 VAL A 319 SER A 324 -1 O ILE A 321 N GLN A 314
SHEET 3 AA3 4 THR A 328 ASP A 333 -1 O TRP A 332 N ILE A 320
SHEET 4 AA3 4 MET A 339 ILE A 344 -1 O LEU A 340 N VAL A 331
SHEET 1 AA4 4 VAL A 350 ASN A 356 0
SHEET 2 AA4 4 MET A 359 SER A 364 -1 O VAL A 361 N ARG A 354
SHEET 3 AA4 4 ILE A 369 SER A 376 -1 O TRP A 372 N MET A 360
SHEET 4 AA4 4 ASP A 379 LEU A 386 -1 O ARG A 383 N VAL A 371
SHEET 1 AA5 4 VAL A 393 PHE A 398 0
SHEET 2 AA5 4 TYR A 402 SER A 407 -1 O VAL A 404 N ASP A 397
SHEET 3 AA5 4 ILE A 412 ASN A 416 -1 O TRP A 415 N ILE A 403
SHEET 4 AA5 4 PHE A 422 LEU A 426 -1 O LEU A 426 N ILE A 412
SHEET 1 AA6 4 ILE A 433 ARG A 439 0
SHEET 2 AA6 4 LEU A 442 SER A 447 -1 O GLY A 446 N CYS A 435
SHEET 3 AA6 4 ILE A 452 ASP A 456 -1 O TRP A 455 N VAL A 443
SHEET 4 AA6 4 CYS A 462 LEU A 466 -1 O LEU A 466 N ILE A 452
SHEET 1 AA7 4 VAL A 473 PHE A 478 0
SHEET 2 AA7 4 ARG A 482 ALA A 487 -1 O VAL A 484 N ARG A 477
SHEET 3 AA7 4 LYS A 491 ASP A 496 -1 O TRP A 495 N ILE A 483
SHEET 4 AA7 4 CYS A 511 VAL A 516 -1 O LEU A 515 N ILE A 492
SHEET 1 AA8 3 ILE B 13 ASP B 17 0
SHEET 2 AA8 3 SER B 3 SER B 8 -1 N ILE B 4 O VAL B 16
SHEET 3 AA8 3 VAL B 39 LEU B 41 1 O VAL B 39 N GLN B 7
LINK C ASP C 32 N SEP C 33 1555 1555 1.33
LINK C SEP C 33 N GLY C 34 1555 1555 1.33
CISPEP 1 ASP B 37 PRO B 38 0 -5.74
SITE 1 AC1 19 ARG A 330 MET A 339 THR A 342 ASN A 394
SITE 2 AC1 19 GLY A 408 ARG A 410 ARG A 431 GLY A 432
SITE 3 AC1 19 ILE A 433 ALA A 434 SER A 448 LEU A 472
SITE 4 AC1 19 TYR A 488 SER C 29 ASP C 32 ILE C 35
SITE 5 AC1 19 HIS C 36 ALA C 37 CL C 101
SITE 1 AC2 5 GLN A 437 ARG A 477 PHE A 478 GLN A 526
SITE 2 AC2 5 PHE A 527
SITE 1 AC3 1 J97 A 601
CRYST1 82.490 82.490 111.960 90.00 90.00 120.00 P 31 3
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 0.012123 0.006999 0.000000 0.00000
SCALE2 0.000000 0.013998 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008932 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
