HEADER TRANSFERASE/TRANSFERASE INHIBITOR 08-OCT-17 6B8J
TITLE CO-STRUCTURE OF HUMAN GLYCOGEN SYNTHASE KINASE BETA WITH A SELECTIVE
TITLE 2 (5-IMIDAZOL-2-YL-4-PHENYLPYRIMIDIN-2-YL)[2-(2-PYRIDYLAMINO)
TITLE 3 ETHYL]AMINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GSK-3 BETA,SERINE/THREONINE-PROTEIN KINASE GSK3B;
COMPND 5 EC: 2.7.11.26,2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: VAL-SEP-ARG-ARG;
COMPND 9 CHAIN: C;
COMPND 10 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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_TAXID: 9606
KEYWDS KINASE, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.BUSSIERE
REVDAT 1 08-NOV-17 6B8J 0
JRNL AUTH A.S.WAGMAN,R.S.BOYCE,S.P.BROWN,E.FANG,D.GOFF,J.M.JANSEN,
JRNL AUTH 2 V.P.LE,B.H.LEVINE,S.C.NG,Z.J.NI,J.M.NUSS,K.B.PFISTER,
JRNL AUTH 3 S.RAMURTHY,P.A.RENHOWE,D.B.RING,W.SHU,S.SUBRAMANIAN,
JRNL AUTH 4 X.A.ZHOU,C.M.SHAFER,S.D.HARRISON,K.W.JOHNSON,D.E.BUSSIERE
JRNL TITL SYNTHESIS, BINDING MODE, AND ANTIHYPERGLYCEMIC ACTIVITY OF
JRNL TITL 2 POTENT AND SELECTIVE
JRNL TITL 3 (5-IMIDAZOL-2-YL-4-PHENYLPYRIMIDIN-2-YL)[2-(2-PYRIDYLAMINO)
JRNL TITL 4 ETHYL]AMINE INHIBITORS OF GLYCOGEN SYNTHASE KINASE 3.
JRNL REF J. MED. CHEM. V. 60 8482 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 29016121
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00922
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 12125
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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 2.6980 - 2.5950 0.00 0 0 0.2605 0.3037
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
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 : 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 : 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 6B8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230451.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JAN-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS II
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12763
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.595
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7-12% (W:V) PEG 6000 AND 5-8% MPD
REMARK 280 (V:V), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 32.53500
REMARK 290 SMTRY3 2 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: 810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16660 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 SER A 35
REMARK 465 LYS A 36
REMARK 465 GLU A 121
REMARK 465 LYS A 122
REMARK 465 LYS A 123
REMARK 465 GLN A 385
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 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 ASP A 49 CG OD1 OD2
REMARK 470 ARG A 50 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 89 CG CD OE1 NE2
REMARK 470 ARG A 92 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 211 CG CD OE1 OE2
REMARK 470 ARG A 282 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 297 CG CD CE NZ
REMARK 470 ARG C 3 CG CD NE CZ NH1 NH2
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 NZ LYS A 205 OD1 ASN A 213 1.88
REMARK 500 OG1 THR A 43 O PHE A 115 1.92
REMARK 500 OE2 GLU A 226 NH2 ARG A 328 2.00
REMARK 500 O HOH A 646 O HOH A 718 2.03
REMARK 500 O LEU A 153 O HOH A 601 2.04
REMARK 500 O ALA A 170 O HOH A 602 2.06
REMARK 500 O HOH A 620 O HOH A 758 2.10
REMARK 500 OE1 GLU A 312 O HOH A 603 2.10
REMARK 500 O ARG A 92 N ARG C 4 2.11
REMARK 500 O PRO A 372 O HOH A 604 2.12
REMARK 500 O HOH A 750 O HOH A 783 2.15
REMARK 500 NH1 ARG A 180 O2P SEP C 2 2.16
REMARK 500 OH TYR A 117 O HOH A 605 2.16
REMARK 500 O HOH A 714 O HOH A 788 2.16
REMARK 500 OD1 ASN A 186 O HOH A 606 2.17
REMARK 500 NZ LYS A 349 OD1 ASP A 355 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG C 4 N ARG C 4 CA 0.752
REMARK 500 ARG C 4 CA ARG C 4 CB -0.285
REMARK 500 ARG C 4 CA ARG C 4 C 0.757
REMARK 500
REMARK 500 REMARK: NULL
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 PHE A 291 C - N - CA ANGL. DEV. = 15.9 DEGREES
REMARK 500 ARG C 4 C - N - CA ANGL. DEV. = -22.0 DEGREES
REMARK 500 ARG C 4 CB - CA - C ANGL. DEV. = 29.3 DEGREES
REMARK 500 ARG C 4 N - CA - CB ANGL. DEV. = 23.6 DEGREES
REMARK 500 ARG C 4 CA - CB - CG ANGL. DEV. = -19.5 DEGREES
REMARK 500 ARG C 4 CB - CG - CD ANGL. DEV. = -16.6 DEGREES
REMARK 500 ARG C 4 N - CA - C ANGL. DEV. = -39.0 DEGREES
REMARK 500 ARG C 4 CA - C - O ANGL. DEV. = 28.9 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 PRO A 48 -155.68 -90.95
REMARK 500 ASP A 49 79.93 -118.52
REMARK 500 LEU A 88 156.42 169.47
REMARK 500 LYS A 91 -165.48 26.37
REMARK 500 GLN A 99 -20.30 82.72
REMARK 500 ASP A 181 50.94 -154.10
REMARK 500 ASP A 200 72.80 56.86
REMARK 500 CYS A 218 121.62 61.94
REMARK 500 CYS A 218 116.74 69.29
REMARK 500 SER A 219 137.94 -38.51
REMARK 500 THR A 289 -82.39 -128.93
REMARK 500 PHE A 293 129.45 69.65
REMARK 500 ASN A 347 48.15 -95.24
REMARK 500 ASN A 370 80.52 -169.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 88 GLN A 89 65.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS A 91 11.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 791 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 792 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A 793 DISTANCE = 6.28 ANGSTROMS
REMARK 525 HOH A 794 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A 795 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 796 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 797 DISTANCE = 7.04 ANGSTROMS
REMARK 525 HOH A 798 DISTANCE = 7.41 ANGSTROMS
REMARK 525 HOH A 799 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH A 800 DISTANCE = 8.22 ANGSTROMS
REMARK 525 HOH A 801 DISTANCE = 14.69 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 65C A 502
DBREF 6B8J A 1 420 UNP P49841 GSK3B_HUMAN 1 420
DBREF 6B8J C 1 4 PDB 6B8J 6B8J 1 4
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 PTR 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 C 4 VAL SEP ARG ARG
MODRES 6B8J PTR A 216 TYR MODIFIED RESIDUE
HET PTR A 216 16
HET SEP C 2 10
HET GOL A 501 6
HET 65C A 502 32
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM SEP PHOSPHOSERINE
HETNAM GOL GLYCEROL
HETNAM 65C CHIR99021
HETSYN PTR PHOSPHONOTYROSINE
HETSYN SEP PHOSPHONOSERINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN 65C 6-[(2-{[4-(2,4-DICHLOROPHENYL)-5-(4-METHYL-1H-IMIDAZOL-
HETSYN 2 65C 2-YL)PYRIMIDIN-2-YL]AMINO}ETHYL)AMINO]PYRIDINE-3-
HETSYN 3 65C CARBONITRILE
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 2 SEP C3 H8 N O6 P
FORMUL 3 GOL C3 H8 O3
FORMUL 4 65C C22 H18 CL2 N8
FORMUL 5 HOH *203(H2 O)
HELIX 1 AA1 ARG A 96 MET A 101 1 6
HELIX 2 AA2 VAL A 139 ALA A 149 1 11
HELIX 3 AA3 PRO A 154 PHE A 175 1 22
HELIX 4 AA4 LYS A 183 GLN A 185 5 3
HELIX 5 AA5 SER A 219 ARG A 223 5 5
HELIX 6 AA6 ALA A 224 PHE A 229 1 6
HELIX 7 AA7 SER A 236 GLY A 253 1 18
HELIX 8 AA8 SER A 261 GLY A 274 1 14
HELIX 9 AA9 GLU A 279 ASN A 285 1 7
HELIX 10 AB1 PRO A 300 PHE A 305 1 6
HELIX 11 AB2 PRO A 310 ARG A 319 1 10
HELIX 12 AB3 THR A 324 ARG A 328 5 5
HELIX 13 AB4 THR A 330 ALA A 336 1 7
HELIX 14 AB5 HIS A 337 ASP A 345 5 9
HELIX 15 AB6 ASN A 370 PRO A 372 5 3
HELIX 16 AB7 LEU A 373 ILE A 378 1 6
HELIX 17 AB8 PRO A 379 ARG A 383 5 5
SHEET 1 AA1 6 THR A 39 THR A 43 0
SHEET 2 AA1 6 GLN A 52 GLY A 65 -1 O TYR A 56 N THR A 39
SHEET 3 AA1 6 GLY A 68 LEU A 75 -1 O VAL A 70 N ILE A 62
SHEET 4 AA1 6 LEU A 81 VAL A 87 -1 O LYS A 86 N VAL A 69
SHEET 5 AA1 6 LEU A 128 ASP A 133 -1 O LEU A 132 N ALA A 83
SHEET 6 AA1 6 LEU A 112 PHE A 115 -1 N TYR A 114 O VAL A 131
SHEET 1 AA2 3 GLU A 137 THR A 138 0
SHEET 2 AA2 3 LEU A 187 ASP A 190 -1 O LEU A 189 N GLU A 137
SHEET 3 AA2 3 VAL A 195 LEU A 198 -1 O LYS A 197 N LEU A 188
SHEET 1 AA3 2 ILE A 177 CYS A 178 0
SHEET 2 AA3 2 LYS A 205 GLN A 206 -1 O LYS A 205 N CYS A 178
LINK C SER A 215 N PTR A 216 1555 1555 1.33
LINK C PTR A 216 N ILE A 217 1555 1555 1.33
LINK C VAL C 1 N SEP C 2 1555 1555 1.33
LINK C SEP C 2 N ARG C 3 1555 1555 1.33
CISPEP 1 ARG A 278 GLU A 279 0 14.63
SITE 1 AC1 1 SER A 174
SITE 1 AC2 17 ILE A 62 GLY A 63 ASN A 64 PHE A 67
SITE 2 AC2 17 VAL A 70 ALA A 83 LEU A 132 ASP A 133
SITE 3 AC2 17 TYR A 134 VAL A 135 ARG A 141 GLN A 185
SITE 4 AC2 17 LEU A 188 HOH A 633 HOH A 635 HOH A 643
SITE 5 AC2 17 HOH A 652
CRYST1 56.747 65.070 57.336 90.00 100.53 90.00 P 1 21 1 2
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 0.017622 0.000000 0.003276 0.00000
SCALE2 0.000000 0.015368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017740 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
