HEADER TRANSFERASE/TRANSFERASE INHIBITOR 05-MAR-10 3M1S
TITLE STRUCTURE OF RUTHENIUM HALF-SANDWICH COMPLEX BOUND TO GLYCOGEN
TITLE 2 SYNTHASE KINASE 3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GSK-3 BETA;
COMPND 5 EC: 2.7.11.26;
COMPND 6 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: GSK3B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS TRANSFERASE, ENZYME INHIBITOR, ORGANOMETALLIC COMPOUND, RUTHENIUM
KEYWDS 2 CENTER, RUTHENIUM PYRIDOCARBAZOLE, ATP-BINDING, KINASE,
KEYWDS 3 PHOSPHOPROTEIN, SERINE/THREONINE-PROTEIN KINASE, WNT SIGNALING
KEYWDS 4 PATHWAY, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR G.E.ATILLA-GOKCUMEN,L.DI COSTANZO,G.ZIMMERMANN,E.MEGGERS
REVDAT 3 06-SEP-23 3M1S 1 REMARK
REVDAT 2 26-JUN-13 3M1S 1 JRNL VERSN
REVDAT 1 22-DEC-10 3M1S 0
JRNL AUTH G.E.ATILLA-GOKCUMEN,L.DI COSTANZO,E.MEGGERS
JRNL TITL STRUCTURE OF ANTICANCER RUTHENIUM HALF-SANDWICH COMPLEX
JRNL TITL 2 BOUND TO GLYCOGEN SYNTHASE KINASE 3BETA
JRNL REF J.BIOL.INORG.CHEM. V. 16 45 2011
JRNL REFN ISSN 0949-8257
JRNL PMID 20821241
JRNL DOI 10.1007/S00775-010-0699-X
REMARK 2
REMARK 2 RESOLUTION. 3.13 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 3.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 21318
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.500
REMARK 3 FREE R VALUE TEST SET COUNT : 747
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 38.2271 - 5.3551 0.89 4144 136 0.1889 0.2365
REMARK 3 2 5.3551 - 4.2523 0.93 4138 160 0.1380 0.1914
REMARK 3 3 4.2523 - 3.7153 0.94 4165 153 0.1445 0.1998
REMARK 3 4 3.7153 - 3.3758 0.95 4156 137 0.1791 0.2734
REMARK 3 5 3.3758 - 3.1340 0.92 3968 161 0.2092 0.2709
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 : 0.33
REMARK 3 B_SOL : 34.43
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
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) : 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 : 0.013 5647
REMARK 3 ANGLE : 1.591 7760
REMARK 3 CHIRALITY : 0.090 877
REMARK 3 PLANARITY : 0.008 985
REMARK 3 DIHEDRAL : 18.754 2025
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 3M1S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-10.
REMARK 100 THE DEPOSITION ID IS D_1000057999.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21365
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.134
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.14800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: PDB ENTRY 1H8F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS, 10 % PEG 8000, SEEDING
REMARK 280 PROCESS, PH 7.2, EVAPORATION, TEMPERATURE 298K
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 41.52050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 88.69900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.05700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 88.69900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.52050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.05700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 GLY A 3
REMARK 465 ARG A 4
REMARK 465 PRO A 5
REMARK 465 ARG A 6
REMARK 465 THR A 7
REMARK 465 THR A 8
REMARK 465 SER A 9
REMARK 465 PHE A 10
REMARK 465 ALA A 11
REMARK 465 GLU A 12
REMARK 465 SER A 13
REMARK 465 CYS A 14
REMARK 465 LYS A 15
REMARK 465 PRO A 16
REMARK 465 VAL A 17
REMARK 465 GLN A 18
REMARK 465 GLN A 19
REMARK 465 PRO A 20
REMARK 465 SER A 21
REMARK 465 ALA A 22
REMARK 465 PHE A 23
REMARK 465 GLY A 24
REMARK 465 SER A 25
REMARK 465 MET A 26
REMARK 465 LYS A 27
REMARK 465 VAL A 28
REMARK 465 SER A 29
REMARK 465 ARG A 30
REMARK 465 ASP A 31
REMARK 465 LYS A 32
REMARK 465 ASP A 33
REMARK 465 GLY A 34
REMARK 465 GLY A 120
REMARK 465 GLU A 290
REMARK 465 LYS A 292
REMARK 465 ALA A 386
REMARK 465 ALA A 387
REMARK 465 ALA A 388
REMARK 465 SER A 389
REMARK 465 THR A 390
REMARK 465 PRO A 391
REMARK 465 THR A 392
REMARK 465 ASN A 393
REMARK 465 ALA A 394
REMARK 465 THR A 395
REMARK 465 ALA A 396
REMARK 465 ALA A 397
REMARK 465 SER A 398
REMARK 465 ASP A 399
REMARK 465 ALA A 400
REMARK 465 ASN A 401
REMARK 465 THR A 402
REMARK 465 GLY A 403
REMARK 465 ASP A 404
REMARK 465 ARG A 405
REMARK 465 GLY A 406
REMARK 465 GLN A 407
REMARK 465 THR A 408
REMARK 465 ASN A 409
REMARK 465 ASN A 410
REMARK 465 ALA A 411
REMARK 465 ALA A 412
REMARK 465 SER A 413
REMARK 465 ALA A 414
REMARK 465 SER A 415
REMARK 465 ALA A 416
REMARK 465 SER A 417
REMARK 465 ASN A 418
REMARK 465 SER A 419
REMARK 465 THR A 420
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLY B 3
REMARK 465 ARG B 4
REMARK 465 PRO B 5
REMARK 465 ARG B 6
REMARK 465 THR B 7
REMARK 465 THR B 8
REMARK 465 SER B 9
REMARK 465 PHE B 10
REMARK 465 ALA B 11
REMARK 465 GLU B 12
REMARK 465 SER B 13
REMARK 465 CYS B 14
REMARK 465 LYS B 15
REMARK 465 PRO B 16
REMARK 465 VAL B 17
REMARK 465 GLN B 18
REMARK 465 GLN B 19
REMARK 465 PRO B 20
REMARK 465 SER B 21
REMARK 465 ALA B 22
REMARK 465 PHE B 23
REMARK 465 GLY B 24
REMARK 465 SER B 25
REMARK 465 MET B 26
REMARK 465 LYS B 27
REMARK 465 VAL B 28
REMARK 465 SER B 29
REMARK 465 ARG B 30
REMARK 465 ASP B 31
REMARK 465 LYS B 32
REMARK 465 ASP B 33
REMARK 465 GLY B 34
REMARK 465 LYS B 292
REMARK 465 GLN B 385
REMARK 465 ALA B 386
REMARK 465 ALA B 387
REMARK 465 ALA B 388
REMARK 465 SER B 389
REMARK 465 THR B 390
REMARK 465 PRO B 391
REMARK 465 THR B 392
REMARK 465 ASN B 393
REMARK 465 ALA B 394
REMARK 465 THR B 395
REMARK 465 ALA B 396
REMARK 465 ALA B 397
REMARK 465 SER B 398
REMARK 465 ASP B 399
REMARK 465 ALA B 400
REMARK 465 ASN B 401
REMARK 465 THR B 402
REMARK 465 GLY B 403
REMARK 465 ASP B 404
REMARK 465 ARG B 405
REMARK 465 GLY B 406
REMARK 465 GLN B 407
REMARK 465 THR B 408
REMARK 465 ASN B 409
REMARK 465 ASN B 410
REMARK 465 ALA B 411
REMARK 465 ALA B 412
REMARK 465 SER B 413
REMARK 465 ALA B 414
REMARK 465 SER B 415
REMARK 465 ALA B 416
REMARK 465 SER B 417
REMARK 465 ASN B 418
REMARK 465 SER B 419
REMARK 465 THR B 420
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 35 OG
REMARK 470 LYS A 91 CG CD CE NZ
REMARK 470 ARG A 92 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 93 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 LYS A 122 CD CE NZ
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 ASP A 124 CG OD1 OD2
REMARK 470 ARG A 148 CD NE CZ NH1 NH2
REMARK 470 LYS A 150 CE NZ
REMARK 470 GLN A 151 CD OE1 NE2
REMARK 470 ARG A 209 NE CZ NH1 NH2
REMARK 470 ARG A 278 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 279 CG CD OE1 OE2
REMARK 470 ARG A 282 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 287 CG OD1 ND2
REMARK 470 THR A 289 OG1 CG2
REMARK 470 PHE A 291 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 297 CG CD CE NZ
REMARK 470 THR A 302 OG1 CG2
REMARK 470 LYS A 303 CG CD CE NZ
REMARK 470 LYS A 349 NZ
REMARK 470 SER B 35 OG
REMARK 470 LYS B 36 CG CD CE NZ
REMARK 470 GLU B 53 CD OE1 OE2
REMARK 470 ASP B 90 CG OD1 OD2
REMARK 470 LYS B 91 CG CD CE NZ
REMARK 470 ARG B 92 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 93 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 94 CD CE NZ
REMARK 470 GLU B 121 CD OE1 OE2
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 LYS B 123 CG CD CE NZ
REMARK 470 ASP B 124 CG OD1 OD2
REMARK 470 GLU B 125 CG CD OE1 OE2
REMARK 470 LYS B 150 CD CE NZ
REMARK 470 ARG B 209 CD NE CZ NH1 NH2
REMARK 470 ARG B 278 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 282 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 290 CG CD OE1 OE2
REMARK 470 LYS B 303 CG CD CE NZ
REMARK 470 ARG B 306 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 308 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 349 NZ
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 HIS A 145 CG
REMARK 480 TYR A 221 N CA C O CB
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 CYS A 107 CA - CB - SG ANGL. DEV. = 7.1 DEGREES
REMARK 500 PRO A 286 C - N - CA ANGL. DEV. = 10.1 DEGREES
REMARK 500 PRO B 286 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO B 380 C - N - CA ANGL. DEV. = 10.2 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 ASP A 49 95.14 -44.99
REMARK 500 ASN A 64 148.46 164.56
REMARK 500 CYS A 76 -77.54 -41.78
REMARK 500 ASP A 77 -94.60 -23.70
REMARK 500 PHE A 116 149.31 166.95
REMARK 500 SER A 118 -164.48 -173.51
REMARK 500 LYS A 150 -1.26 45.45
REMARK 500 PRO A 154 127.58 -33.48
REMARK 500 ILE A 156 -71.80 -37.26
REMARK 500 TYR A 157 -30.52 -38.13
REMARK 500 ASP A 181 59.62 -168.22
REMARK 500 ASP A 200 87.87 55.83
REMARK 500 CYS A 218 144.37 82.48
REMARK 500 ARG A 220 103.41 9.38
REMARK 500 ARG A 220 103.99 9.38
REMARK 500 TYR A 221 -45.78 116.42
REMARK 500 TYR A 221 -49.86 116.58
REMARK 500 PHE A 229 26.62 -71.54
REMARK 500 LYS A 271 4.06 -36.63
REMARK 500 VAL A 272 -50.43 -140.87
REMARK 500 MET A 284 -70.29 -69.66
REMARK 500 ASN A 287 42.58 -61.99
REMARK 500 TYR A 288 -6.61 -148.54
REMARK 500 ALA A 298 99.92 -59.07
REMARK 500 PRO A 300 94.09 -57.65
REMARK 500 TRP A 301 -50.13 -9.60
REMARK 500 ARG A 306 160.93 -35.36
REMARK 500 ALA A 336 49.67 -96.33
REMARK 500 VAL A 348 121.19 -28.37
REMARK 500 ASN A 352 19.55 -62.23
REMARK 500 ASN A 361 67.81 -69.64
REMARK 500 ASN A 370 91.92 171.84
REMARK 500 PRO A 380 -54.81 -28.13
REMARK 500 GLN B 46 -118.15 -95.52
REMARK 500 PRO B 48 -145.88 -67.39
REMARK 500 ASP B 58 49.75 75.26
REMARK 500 VAL B 61 75.63 -117.18
REMARK 500 ILE B 62 -41.16 -28.26
REMARK 500 ASN B 64 132.50 172.05
REMARK 500 PHE B 67 28.88 -65.50
REMARK 500 ASP B 77 -88.66 -48.13
REMARK 500 ARG B 92 -1.63 -53.66
REMARK 500 ARG B 148 -72.45 -33.08
REMARK 500 ALA B 149 -4.44 -43.61
REMARK 500 ASP B 181 46.29 -178.40
REMARK 500 ASP B 200 99.58 70.86
REMARK 500 CYS B 218 134.65 90.21
REMARK 500 ARG B 220 -69.43 -22.57
REMARK 500 ARG B 220 -69.54 -22.57
REMARK 500 SER B 236 -37.49 -19.46
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
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 DW1 A 421
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DW1 B 421
DBREF 3M1S A 1 420 UNP P49841 GSK3B_HUMAN 1 420
DBREF 3M1S B 1 420 UNP P49841 GSK3B_HUMAN 1 420
SEQRES 1 A 420 MET SER GLY ARG PRO ARG THR THR SER PHE ALA GLU SER
SEQRES 2 A 420 CYS LYS PRO VAL GLN GLN PRO SER ALA PHE GLY SER MET
SEQRES 3 A 420 LYS VAL SER ARG ASP LYS ASP GLY SER LYS VAL THR THR
SEQRES 4 A 420 VAL VAL ALA THR PRO GLY GLN GLY PRO ASP ARG PRO GLN
SEQRES 5 A 420 GLU VAL SER TYR THR ASP THR LYS VAL ILE GLY ASN GLY
SEQRES 6 A 420 SER PHE GLY VAL VAL TYR GLN ALA LYS LEU CYS ASP SER
SEQRES 7 A 420 GLY GLU LEU VAL ALA ILE LYS LYS VAL LEU GLN ASP LYS
SEQRES 8 A 420 ARG PHE LYS ASN ARG GLU LEU GLN ILE MET ARG LYS LEU
SEQRES 9 A 420 ASP HIS CYS ASN ILE VAL ARG LEU ARG TYR PHE PHE TYR
SEQRES 10 A 420 SER SER GLY GLU LYS LYS ASP GLU VAL TYR LEU ASN LEU
SEQRES 11 A 420 VAL LEU ASP TYR VAL PRO GLU THR VAL TYR ARG VAL ALA
SEQRES 12 A 420 ARG HIS TYR SER ARG ALA LYS GLN THR LEU PRO VAL ILE
SEQRES 13 A 420 TYR VAL LYS LEU TYR MET TYR GLN LEU PHE ARG SER LEU
SEQRES 14 A 420 ALA TYR ILE HIS SER PHE GLY ILE CYS HIS ARG ASP ILE
SEQRES 15 A 420 LYS PRO GLN ASN LEU LEU LEU ASP PRO ASP THR ALA VAL
SEQRES 16 A 420 LEU LYS LEU CYS ASP PHE GLY SER ALA LYS GLN LEU VAL
SEQRES 17 A 420 ARG GLY GLU PRO ASN VAL SER TYR ILE CYS SER ARG TYR
SEQRES 18 A 420 TYR ARG ALA PRO GLU LEU ILE PHE GLY ALA THR ASP TYR
SEQRES 19 A 420 THR SER SER ILE ASP VAL TRP SER ALA GLY CYS VAL LEU
SEQRES 20 A 420 ALA GLU LEU LEU LEU GLY GLN PRO ILE PHE PRO GLY ASP
SEQRES 21 A 420 SER GLY VAL ASP GLN LEU VAL GLU ILE ILE LYS VAL LEU
SEQRES 22 A 420 GLY THR PRO THR ARG GLU GLN ILE ARG GLU MET ASN PRO
SEQRES 23 A 420 ASN TYR THR GLU PHE LYS PHE PRO GLN ILE LYS ALA HIS
SEQRES 24 A 420 PRO TRP THR LYS VAL PHE ARG PRO ARG THR PRO PRO GLU
SEQRES 25 A 420 ALA ILE ALA LEU CYS SER ARG LEU LEU GLU TYR THR PRO
SEQRES 26 A 420 THR ALA ARG LEU THR PRO LEU GLU ALA CYS ALA HIS SER
SEQRES 27 A 420 PHE PHE ASP GLU LEU ARG ASP PRO ASN VAL LYS LEU PRO
SEQRES 28 A 420 ASN GLY ARG ASP THR PRO ALA LEU PHE ASN PHE THR THR
SEQRES 29 A 420 GLN GLU LEU SER SER ASN PRO PRO LEU ALA THR ILE LEU
SEQRES 30 A 420 ILE PRO PRO HIS ALA ARG ILE GLN ALA ALA ALA SER THR
SEQRES 31 A 420 PRO THR ASN ALA THR ALA ALA SER ASP ALA ASN THR GLY
SEQRES 32 A 420 ASP ARG GLY GLN THR ASN ASN ALA ALA SER ALA SER ALA
SEQRES 33 A 420 SER ASN SER THR
SEQRES 1 B 420 MET SER GLY ARG PRO ARG THR THR SER PHE ALA GLU SER
SEQRES 2 B 420 CYS LYS PRO VAL GLN GLN PRO SER ALA PHE GLY SER MET
SEQRES 3 B 420 LYS VAL SER ARG ASP LYS ASP GLY SER LYS VAL THR THR
SEQRES 4 B 420 VAL VAL ALA THR PRO GLY GLN GLY PRO ASP ARG PRO GLN
SEQRES 5 B 420 GLU VAL SER TYR THR ASP THR LYS VAL ILE GLY ASN GLY
SEQRES 6 B 420 SER PHE GLY VAL VAL TYR GLN ALA LYS LEU CYS ASP SER
SEQRES 7 B 420 GLY GLU LEU VAL ALA ILE LYS LYS VAL LEU GLN ASP LYS
SEQRES 8 B 420 ARG PHE LYS ASN ARG GLU LEU GLN ILE MET ARG LYS LEU
SEQRES 9 B 420 ASP HIS CYS ASN ILE VAL ARG LEU ARG TYR PHE PHE TYR
SEQRES 10 B 420 SER SER GLY GLU LYS LYS ASP GLU VAL TYR LEU ASN LEU
SEQRES 11 B 420 VAL LEU ASP TYR VAL PRO GLU THR VAL TYR ARG VAL ALA
SEQRES 12 B 420 ARG HIS TYR SER ARG ALA LYS GLN THR LEU PRO VAL ILE
SEQRES 13 B 420 TYR VAL LYS LEU TYR MET TYR GLN LEU PHE ARG SER LEU
SEQRES 14 B 420 ALA TYR ILE HIS SER PHE GLY ILE CYS HIS ARG ASP ILE
SEQRES 15 B 420 LYS PRO GLN ASN LEU LEU LEU ASP PRO ASP THR ALA VAL
SEQRES 16 B 420 LEU LYS LEU CYS ASP PHE GLY SER ALA LYS GLN LEU VAL
SEQRES 17 B 420 ARG GLY GLU PRO ASN VAL SER TYR ILE CYS SER ARG TYR
SEQRES 18 B 420 TYR ARG ALA PRO GLU LEU ILE PHE GLY ALA THR ASP TYR
SEQRES 19 B 420 THR SER SER ILE ASP VAL TRP SER ALA GLY CYS VAL LEU
SEQRES 20 B 420 ALA GLU LEU LEU LEU GLY GLN PRO ILE PHE PRO GLY ASP
SEQRES 21 B 420 SER GLY VAL ASP GLN LEU VAL GLU ILE ILE LYS VAL LEU
SEQRES 22 B 420 GLY THR PRO THR ARG GLU GLN ILE ARG GLU MET ASN PRO
SEQRES 23 B 420 ASN TYR THR GLU PHE LYS PHE PRO GLN ILE LYS ALA HIS
SEQRES 24 B 420 PRO TRP THR LYS VAL PHE ARG PRO ARG THR PRO PRO GLU
SEQRES 25 B 420 ALA ILE ALA LEU CYS SER ARG LEU LEU GLU TYR THR PRO
SEQRES 26 B 420 THR ALA ARG LEU THR PRO LEU GLU ALA CYS ALA HIS SER
SEQRES 27 B 420 PHE PHE ASP GLU LEU ARG ASP PRO ASN VAL LYS LEU PRO
SEQRES 28 B 420 ASN GLY ARG ASP THR PRO ALA LEU PHE ASN PHE THR THR
SEQRES 29 B 420 GLN GLU LEU SER SER ASN PRO PRO LEU ALA THR ILE LEU
SEQRES 30 B 420 ILE PRO PRO HIS ALA ARG ILE GLN ALA ALA ALA SER THR
SEQRES 31 B 420 PRO THR ASN ALA THR ALA ALA SER ASP ALA ASN THR GLY
SEQRES 32 B 420 ASP ARG GLY GLN THR ASN ASN ALA ALA SER ALA SER ALA
SEQRES 33 B 420 SER ASN SER THR
HET DW1 A 421 31
HET DW1 B 421 31
HETNAM DW1 RUTHENIUM PYRIDOCARBAZOLE
FORMUL 3 DW1 2(C23 H13 N3 O4 RU)
FORMUL 5 HOH *91(H2 O)
HELIX 1 1 ASN A 95 LYS A 103 1 9
HELIX 2 2 VAL A 139 ALA A 149 1 11
HELIX 3 3 PRO A 154 SER A 174 1 21
HELIX 4 4 LYS A 183 GLN A 185 5 3
HELIX 5 5 ALA A 224 PHE A 229 1 6
HELIX 6 6 SER A 236 GLY A 253 1 18
HELIX 7 7 SER A 261 GLY A 274 1 14
HELIX 8 8 THR A 277 ASN A 285 1 9
HELIX 9 9 PRO A 300 VAL A 304 5 5
HELIX 10 10 PRO A 310 LEU A 321 1 12
HELIX 11 11 THR A 330 ALA A 336 1 7
HELIX 12 12 HIS A 337 PHE A 339 5 3
HELIX 13 13 PHE A 340 ASP A 345 1 6
HELIX 14 14 THR A 363 SER A 368 1 6
HELIX 15 15 SER A 369 PRO A 372 5 4
HELIX 16 16 LEU A 373 ILE A 378 1 6
HELIX 17 17 PRO A 379 ARG A 383 5 5
HELIX 18 18 ASN B 95 ARG B 102 1 8
HELIX 19 19 VAL B 139 ALA B 149 1 11
HELIX 20 20 PRO B 154 PHE B 175 1 22
HELIX 21 21 LYS B 183 GLN B 185 5 3
HELIX 22 22 SER B 219 ARG B 223 5 5
HELIX 23 23 ALA B 224 PHE B 229 1 6
HELIX 24 24 SER B 236 GLY B 253 1 18
HELIX 25 25 SER B 261 GLY B 274 1 14
HELIX 26 26 THR B 277 ASN B 285 1 9
HELIX 27 27 TRP B 301 PHE B 305 5 5
HELIX 28 28 PRO B 310 LEU B 321 1 12
HELIX 29 29 THR B 324 ARG B 328 5 5
HELIX 30 30 THR B 330 ALA B 336 1 7
HELIX 31 31 HIS B 337 PHE B 339 5 3
HELIX 32 32 PHE B 340 ASP B 345 1 6
HELIX 33 33 THR B 363 SER B 368 1 6
HELIX 34 34 ASN B 370 PRO B 372 5 3
HELIX 35 35 LEU B 373 ILE B 378 1 6
SHEET 1 A 7 VAL A 61 ASN A 64 0
SHEET 2 A 7 VAL A 69 LEU A 75 -1 O VAL A 70 N ILE A 62
SHEET 3 A 7 GLN A 52 THR A 57 -1 N THR A 57 O LYS A 74
SHEET 4 A 7 THR A 38 PRO A 44 -1 N VAL A 40 O VAL A 54
SHEET 5 A 7 LEU A 112 PHE A 115 -1 O PHE A 115 N THR A 43
SHEET 6 A 7 TYR A 127 ASP A 133 -1 O VAL A 131 N ARG A 113
SHEET 7 A 7 TYR A 117 SER A 118 -1 N SER A 118 O TYR A 127
SHEET 1 B 5 VAL A 61 ASN A 64 0
SHEET 2 B 5 VAL A 69 LEU A 75 -1 O VAL A 70 N ILE A 62
SHEET 3 B 5 LEU A 81 LEU A 88 -1 O VAL A 82 N ALA A 73
SHEET 4 B 5 TYR A 127 ASP A 133 -1 O LEU A 132 N ALA A 83
SHEET 5 B 5 TYR A 117 SER A 118 -1 N SER A 118 O TYR A 127
SHEET 1 C 3 GLU A 137 THR A 138 0
SHEET 2 C 3 LEU A 187 LEU A 189 -1 O LEU A 189 N GLU A 137
SHEET 3 C 3 LEU A 196 LEU A 198 -1 O LYS A 197 N LEU A 188
SHEET 1 D 2 ILE A 177 CYS A 178 0
SHEET 2 D 2 LYS A 205 GLN A 206 -1 O LYS A 205 N CYS A 178
SHEET 1 E 8 GLY B 63 GLY B 65 0
SHEET 2 E 8 GLY B 68 LEU B 75 -1 O VAL B 70 N GLY B 63
SHEET 3 E 8 LEU B 81 LEU B 88 -1 O VAL B 82 N ALA B 73
SHEET 4 E 8 TYR B 127 ASP B 133 -1 O LEU B 132 N ALA B 83
SHEET 5 E 8 LEU B 112 SER B 118 -1 N PHE B 116 O ASN B 129
SHEET 6 E 8 VAL B 37 PRO B 44 -1 N THR B 43 O PHE B 115
SHEET 7 E 8 GLN B 52 THR B 57 -1 O TYR B 56 N THR B 38
SHEET 8 E 8 GLY B 68 LEU B 75 -1 O LYS B 74 N THR B 57
SHEET 1 F 3 GLU B 137 THR B 138 0
SHEET 2 F 3 LEU B 187 ASP B 190 -1 O LEU B 189 N GLU B 137
SHEET 3 F 3 VAL B 195 LEU B 198 -1 O VAL B 195 N ASP B 190
SHEET 1 G 2 ILE B 177 CYS B 178 0
SHEET 2 G 2 LYS B 205 GLN B 206 -1 O LYS B 205 N CYS B 178
SITE 1 AC1 17 ILE A 62 GLY A 63 ASN A 64 PHE A 67
SITE 2 AC1 17 VAL A 70 ALA A 83 LEU A 132 ASP A 133
SITE 3 AC1 17 TYR A 134 VAL A 135 PRO A 136 THR A 138
SITE 4 AC1 17 ARG A 141 GLN A 185 LEU A 188 ASP A 200
SITE 5 AC1 17 HOH A 460
SITE 1 AC2 20 ILE B 62 GLY B 63 ASN B 64 PHE B 67
SITE 2 AC2 20 VAL B 70 ALA B 83 LYS B 85 LEU B 132
SITE 3 AC2 20 ASP B 133 TYR B 134 VAL B 135 PRO B 136
SITE 4 AC2 20 GLU B 137 THR B 138 GLN B 185 ASN B 186
SITE 5 AC2 20 LEU B 188 ASP B 200 HOH B 437 HOH B 460
CRYST1 83.041 86.114 177.398 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 0.012042 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011613 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005637 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
