HEADER TRANSFERASE/PEPTIDE 14-NOV-13 4NM0
TITLE CRYSTAL STRUCTURE OF PEPTIDE INHIBITOR-FREE GSK-3/AXIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-383;
COMPND 5 SYNONYM: GSK-3 BETA, SERINE/THREONINE-PROTEIN KINASE GSK3B;
COMPND 6 EC: 2.7.11.26, 2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: AXIN-1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: RESIDUES 383-402;
COMPND 12 SYNONYM: AXIS INHIBITION PROTEIN 1, HAXIN;
COMPND 13 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;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON-PLUS RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET29B(+);
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: AXIN, AXIN1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) CODON-PLUS RIL;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: MODIFIED PGEX-KG
KEYWDS WNT, LRP6, AUTO-INHIBITED, GSK-3, AXIN, KINASE, PRIMED SUBSTRATE,
KEYWDS 2 TRANSFERASE-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.L.-H.CHU,J.L.STAMOS,M.D.ENOS,N.SHAH,W.I.WEIS
REVDAT 3 20-SEP-23 4NM0 1 REMARK SEQADV LINK
REVDAT 2 23-APR-14 4NM0 1 JRNL
REVDAT 1 26-MAR-14 4NM0 0
JRNL AUTH J.L.STAMOS,M.L.CHU,M.D.ENOS,N.SHAH,W.I.WEIS
JRNL TITL STRUCTURAL BASIS OF GSK-3 INHIBITION BY N-TERMINAL
JRNL TITL 2 PHOSPHORYLATION AND BY THE WNT RECEPTOR LRP6.
JRNL REF ELIFE V. 3 01998 2014
JRNL REFN ESSN 2050-084X
JRNL PMID 24642411
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.2_1309)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.910
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 19958
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 : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 979
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 39.0527 - 4.7799 1.00 2941 155 0.1836 0.2224
REMARK 3 2 4.7799 - 3.7950 1.00 2752 153 0.1542 0.2019
REMARK 3 3 3.7950 - 3.3156 1.00 2696 139 0.1787 0.2471
REMARK 3 4 3.3156 - 3.0125 1.00 2681 117 0.2114 0.3046
REMARK 3 5 3.0125 - 2.7967 1.00 2650 138 0.2337 0.2965
REMARK 3 6 2.7967 - 2.6318 1.00 2638 139 0.2617 0.2871
REMARK 3 7 2.6318 - 2.5000 1.00 2621 138 0.3163 0.3249
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) : 25.870
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 : 0.003 3079
REMARK 3 ANGLE : 0.626 4198
REMARK 3 CHIRALITY : 0.041 479
REMARK 3 PLANARITY : 0.003 536
REMARK 3 DIHEDRAL : 11.861 1128
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 26 THROUGH 90 )
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1955 45.7472 3.2834
REMARK 3 T TENSOR
REMARK 3 T11: 0.5247 T22: 0.5912
REMARK 3 T33: 0.4820 T12: -0.1022
REMARK 3 T13: 0.1689 T23: -0.0673
REMARK 3 L TENSOR
REMARK 3 L11: 5.4937 L22: 2.0887
REMARK 3 L33: 3.3373 L12: 0.7480
REMARK 3 L13: -0.2418 L23: -1.7032
REMARK 3 S TENSOR
REMARK 3 S11: -0.1180 S12: -0.4831 S13: 0.6214
REMARK 3 S21: 0.5830 S22: -0.0284 S23: 0.3761
REMARK 3 S31: -0.7840 S32: -0.0901 S33: -0.6955
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 91 THROUGH 136 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.4437 41.3012 -4.8623
REMARK 3 T TENSOR
REMARK 3 T11: 0.4090 T22: 0.5823
REMARK 3 T33: 0.4175 T12: -0.0522
REMARK 3 T13: 0.0580 T23: 0.0354
REMARK 3 L TENSOR
REMARK 3 L11: 2.1915 L22: 2.6396
REMARK 3 L33: 1.7352 L12: 0.4531
REMARK 3 L13: -0.5659 L23: 1.4732
REMARK 3 S TENSOR
REMARK 3 S11: 0.1772 S12: 0.4220 S13: 0.1623
REMARK 3 S21: 0.1901 S22: -0.3018 S23: 0.6654
REMARK 3 S31: 0.3517 S32: -0.5624 S33: 0.0385
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 137 THROUGH 218 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.7390 33.2090 -14.3420
REMARK 3 T TENSOR
REMARK 3 T11: 0.4153 T22: 0.3319
REMARK 3 T33: 0.2876 T12: -0.0349
REMARK 3 T13: -0.0573 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 2.8757 L22: 2.3589
REMARK 3 L33: 2.2572 L12: -0.2407
REMARK 3 L13: -0.6952 L23: -0.1690
REMARK 3 S TENSOR
REMARK 3 S11: 0.1949 S12: -0.1852 S13: 0.0205
REMARK 3 S21: 0.2539 S22: -0.1097 S23: -0.1238
REMARK 3 S31: 0.3694 S32: -0.2114 S33: -0.0134
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 383 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8957 26.9964 -24.9416
REMARK 3 T TENSOR
REMARK 3 T11: 0.4148 T22: 0.2774
REMARK 3 T33: 0.3561 T12: 0.0044
REMARK 3 T13: -0.0725 T23: -0.0719
REMARK 3 L TENSOR
REMARK 3 L11: 1.8671 L22: 1.1119
REMARK 3 L33: 3.7843 L12: 0.3466
REMARK 3 L13: 0.0906 L23: -0.6137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0238 S12: 0.0276 S13: -0.3168
REMARK 3 S21: -0.1285 S22: 0.0498 S23: -0.0321
REMARK 3 S31: 0.5261 S32: 0.0699 S33: -0.0005
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 381 THROUGH 401 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.5008 43.8954 -43.5287
REMARK 3 T TENSOR
REMARK 3 T11: 0.6720 T22: 0.4476
REMARK 3 T33: 0.3617 T12: -0.1132
REMARK 3 T13: -0.0226 T23: 0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 4.4011 L22: 3.3652
REMARK 3 L33: 3.7710 L12: 1.0738
REMARK 3 L13: 0.7609 L23: -0.6673
REMARK 3 S TENSOR
REMARK 3 S11: 0.0948 S12: 0.5368 S13: 0.8424
REMARK 3 S21: -0.5332 S22: 0.0070 S23: 0.2285
REMARK 3 S31: -0.7624 S32: -0.2608 S33: -0.0320
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 4NM0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : SI(III)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20069
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 39.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 9.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 1.74300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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: 4NM7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 35,000, 20MM TRIS 7.5, 300MM
REMARK 280 NACL, 5% GLYCEROL, 20MM MGCL2, 400UM ATP, AND 5MM DTT,
REMARK 280 MICRODIALYSIS, TEMPERATURE 277K, PH 7.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 93.60967
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 187.21933
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 140.41450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 234.02417
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 46.80483
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 93.60967
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 187.21933
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 234.02417
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 140.41450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 46.80483
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: 4070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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 LYS A 32
REMARK 465 ASP A 33
REMARK 465 GLY A 34
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 GLY B 379
REMARK 465 GLY B 380
REMARK 465 THR B 402
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 LYS A 27 CG CD CE NZ
REMARK 470 SER A 29 OG
REMARK 470 ARG A 30 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 31 CG OD1 OD2
REMARK 470 SER A 35 OG
REMARK 470 LYS A 36 CG CD CE NZ
REMARK 470 ARG A 92 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 99 CG CD OE1 NE2
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 LYS A 123 CG CD CE NZ
REMARK 470 ASP A 124 CG OD1 OD2
REMARK 470 GLU A 125 CG CD OE1 OE2
REMARK 470 ARG A 209 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 216 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 292 CG CD CE NZ
REMARK 470 LYS A 297 CG CD CE NZ
REMARK 470 ARG A 306 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 308 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 349 CG CD CE NZ
REMARK 470 HIS A 384 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 381 CG1 CG2 CD1
REMARK 470 LEU B 382 CG CD1 CD2
REMARK 470 ARG B 401 CG CD NE CZ NH1 NH2
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 SER A 29 -164.21 -127.10
REMARK 500 ASP A 49 98.79 -61.33
REMARK 500 ASP A 181 40.86 -156.86
REMARK 500 ASP A 200 85.51 56.90
REMARK 500 CYS A 218 144.11 70.19
REMARK 500 TYR A 221 -27.02 78.46
REMARK 500 ASN A 347 39.22 -97.71
REMARK 500 ASN A 370 79.08 -153.96
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 407 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 186 OD1
REMARK 620 2 ASP A 200 OD2 82.0
REMARK 620 3 ADP A 408 O3B 137.6 68.8
REMARK 620 4 ADP A 408 O1A 81.1 81.8 65.4
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 410
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NM3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ITS OWN PHOSPHORYLATED N-TERMINAL
REMARK 900 AUTO-INHIBITORY PS9 PEPTIDE BUT WITHOUT ALF3
REMARK 900 RELATED ID: 4NM5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PHOSPHORYLATED WNT RECEPTOR LRP6 C-
REMARK 900 MOTIF
REMARK 900 RELATED ID: 4NM7 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH PHOSPHORYLATED WNT RECEPTOR LRP6 E-
REMARK 900 MOTIF
REMARK 900 RELATED ID: 4NU1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ITS OWN PHOSPHORYLATED N-TERMINAL
REMARK 900 AUTO-INHIBITORY PS9 PEPTIDE AND ALF3 IS A TRANSITION STATE MIMICRY
DBREF 4NM0 A 1 383 UNP P49841 GSK3B_HUMAN 1 383
DBREF 4NM0 B 383 402 UNP O15169 AXIN1_HUMAN 383 402
SEQADV 4NM0 HIS A 384 UNP P49841 EXPRESSION TAG
SEQADV 4NM0 HIS A 385 UNP P49841 EXPRESSION TAG
SEQADV 4NM0 HIS A 386 UNP P49841 EXPRESSION TAG
SEQADV 4NM0 HIS A 387 UNP P49841 EXPRESSION TAG
SEQADV 4NM0 HIS A 388 UNP P49841 EXPRESSION TAG
SEQADV 4NM0 HIS A 389 UNP P49841 EXPRESSION TAG
SEQADV 4NM0 GLY B 379 UNP O15169 EXPRESSION TAG
SEQADV 4NM0 GLY B 380 UNP O15169 EXPRESSION TAG
SEQADV 4NM0 ILE B 381 UNP O15169 EXPRESSION TAG
SEQADV 4NM0 LEU B 382 UNP O15169 EXPRESSION TAG
SEQRES 1 A 389 MET SER GLY ARG PRO ARG THR THR SER PHE ALA GLU SER
SEQRES 2 A 389 CYS LYS PRO VAL GLN GLN PRO SER ALA PHE GLY SER MET
SEQRES 3 A 389 LYS VAL SER ARG ASP LYS ASP GLY SER LYS VAL THR THR
SEQRES 4 A 389 VAL VAL ALA THR PRO GLY GLN GLY PRO ASP ARG PRO GLN
SEQRES 5 A 389 GLU VAL SER TYR THR ASP THR LYS VAL ILE GLY ASN GLY
SEQRES 6 A 389 SER PHE GLY VAL VAL TYR GLN ALA LYS LEU CYS ASP SER
SEQRES 7 A 389 GLY GLU LEU VAL ALA ILE LYS LYS VAL LEU GLN ASP LYS
SEQRES 8 A 389 ARG PHE LYS ASN ARG GLU LEU GLN ILE MET ARG LYS LEU
SEQRES 9 A 389 ASP HIS CYS ASN ILE VAL ARG LEU ARG TYR PHE PHE TYR
SEQRES 10 A 389 SER SER GLY GLU LYS LYS ASP GLU VAL TYR LEU ASN LEU
SEQRES 11 A 389 VAL LEU ASP TYR VAL PRO GLU THR VAL TYR ARG VAL ALA
SEQRES 12 A 389 ARG HIS TYR SER ARG ALA LYS GLN THR LEU PRO VAL ILE
SEQRES 13 A 389 TYR VAL LYS LEU TYR MET TYR GLN LEU PHE ARG SER LEU
SEQRES 14 A 389 ALA TYR ILE HIS SER PHE GLY ILE CYS HIS ARG ASP ILE
SEQRES 15 A 389 LYS PRO GLN ASN LEU LEU LEU ASP PRO ASP THR ALA VAL
SEQRES 16 A 389 LEU LYS LEU CYS ASP PHE GLY SER ALA LYS GLN LEU VAL
SEQRES 17 A 389 ARG GLY GLU PRO ASN VAL SER TYR ILE CYS SER ARG TYR
SEQRES 18 A 389 TYR ARG ALA PRO GLU LEU ILE PHE GLY ALA THR ASP TYR
SEQRES 19 A 389 THR SER SER ILE ASP VAL TRP SER ALA GLY CYS VAL LEU
SEQRES 20 A 389 ALA GLU LEU LEU LEU GLY GLN PRO ILE PHE PRO GLY ASP
SEQRES 21 A 389 SER GLY VAL ASP GLN LEU VAL GLU ILE ILE LYS VAL LEU
SEQRES 22 A 389 GLY THR PRO THR ARG GLU GLN ILE ARG GLU MET ASN PRO
SEQRES 23 A 389 ASN TYR THR GLU PHE LYS PHE PRO GLN ILE LYS ALA HIS
SEQRES 24 A 389 PRO TRP THR LYS VAL PHE ARG PRO ARG THR PRO PRO GLU
SEQRES 25 A 389 ALA ILE ALA LEU CYS SER ARG LEU LEU GLU TYR THR PRO
SEQRES 26 A 389 THR ALA ARG LEU THR PRO LEU GLU ALA CYS ALA HIS SER
SEQRES 27 A 389 PHE PHE ASP GLU LEU ARG ASP PRO ASN VAL LYS LEU PRO
SEQRES 28 A 389 ASN GLY ARG ASP THR PRO ALA LEU PHE ASN PHE THR THR
SEQRES 29 A 389 GLN GLU LEU SER SER ASN PRO PRO LEU ALA THR ILE LEU
SEQRES 30 A 389 ILE PRO PRO HIS ALA ARG HIS HIS HIS HIS HIS HIS
SEQRES 1 B 24 GLY GLY ILE LEU VAL GLU PRO GLN LYS PHE ALA GLU GLU
SEQRES 2 B 24 LEU ILE HIS ARG LEU GLU ALA VAL GLN ARG THR
HET GOL A 401 6
HET GOL A 402 6
HET GOL A 403 6
HET GOL A 404 6
HET GOL A 405 6
HET MG A 406 1
HET MG A 407 1
HET ADP A 408 27
HET DTT A 409 8
HET CL A 410 1
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
HETSYN DTT 1,4-DITHIOTHREITOL
FORMUL 3 GOL 5(C3 H8 O3)
FORMUL 8 MG 2(MG 2+)
FORMUL 10 ADP C10 H15 N5 O10 P2
FORMUL 11 DTT C4 H10 O2 S2
FORMUL 12 CL CL 1-
FORMUL 13 HOH *164(H2 O)
HELIX 1 1 ASN A 95 ARG A 102 1 8
HELIX 2 2 VAL A 139 ALA A 149 1 11
HELIX 3 3 PRO A 154 PHE A 175 1 22
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 286 THR A 289 5 4
HELIX 10 10 PRO A 300 PHE A 305 1 6
HELIX 11 11 PRO A 310 ARG A 319 1 10
HELIX 12 12 THR A 324 ARG A 328 5 5
HELIX 13 13 THR A 330 ALA A 336 1 7
HELIX 14 14 HIS A 337 ASP A 345 5 9
HELIX 15 15 ASN A 370 PRO A 372 5 3
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 GLU B 384 VAL B 399 1 16
SHEET 1 A 8 LYS A 27 SER A 29 0
SHEET 2 A 8 VAL A 37 PRO A 44 -1 O VAL A 37 N SER A 29
SHEET 3 A 8 LEU A 112 SER A 119 -1 O PHE A 115 N THR A 43
SHEET 4 A 8 VAL A 126 ASP A 133 -1 O TYR A 127 N SER A 118
SHEET 5 A 8 LEU A 81 GLN A 89 -1 N ALA A 83 O LEU A 132
SHEET 6 A 8 GLY A 68 LEU A 75 -1 N TYR A 71 O ILE A 84
SHEET 7 A 8 GLN A 52 ASN A 64 -1 N GLY A 63 O VAL A 70
SHEET 8 A 8 VAL A 37 PRO A 44 -1 N VAL A 40 O VAL A 54
SHEET 1 B 3 GLU A 137 THR A 138 0
SHEET 2 B 3 LEU A 187 LEU A 189 -1 O LEU A 189 N GLU A 137
SHEET 3 B 3 LEU A 196 LEU A 198 -1 O LYS A 197 N LEU A 188
SHEET 1 C 2 ILE A 177 CYS A 178 0
SHEET 2 C 2 LYS A 205 GLN A 206 -1 O LYS A 205 N CYS A 178
LINK OD1 ASN A 186 MG MG A 407 1555 1555 2.44
LINK OD2 ASP A 200 MG MG A 407 1555 1555 2.68
LINK MG MG A 406 O1B ADP A 408 1555 1555 2.05
LINK MG MG A 407 O3B ADP A 408 1555 1555 2.07
LINK MG MG A 407 O1A ADP A 408 1555 1555 2.80
SITE 1 AC1 4 TYR A 56 LYS A 86 SER A 118 ASN A 129
SITE 1 AC2 6 ASP A 49 ARG A 50 TYR A 146 TYR A 157
SITE 2 AC2 6 TYR A 161 PRO A 191
SITE 1 AC3 8 ARG A 144 SER A 147 ARG A 148 LEU A 252
SITE 2 AC3 8 GLN A 254 PRO A 255 VAL A 304 HOH A 621
SITE 1 AC4 5 ARG A 96 ARG A 180 LYS A 205 ASN A 213
SITE 2 AC4 5 VAL A 214
SITE 1 AC5 4 LYS A 292 PRO A 294 HOH A 535 GLU B 397
SITE 1 AC6 2 ASP A 200 ADP A 408
SITE 1 AC7 4 LYS A 183 ASN A 186 ASP A 200 ADP A 408
SITE 1 AC8 16 PHE A 67 ALA A 83 LYS A 85 LEU A 132
SITE 2 AC8 16 ASP A 133 TYR A 134 VAL A 135 THR A 138
SITE 3 AC8 16 ARG A 141 GLN A 185 ASN A 186 ASP A 200
SITE 4 AC8 16 MG A 406 MG A 407 HOH A 549 HOH A 622
SITE 1 AC9 5 ARG A 319 THR A 326 ALA A 327 ARG A 328
SITE 2 AC9 5 GLU A 333
SITE 1 BC1 1 LYS A 297
CRYST1 81.303 81.303 280.829 90.00 90.00 120.00 P 61 2 2 12
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 0.012300 0.007101 0.000000 0.00000
SCALE2 0.000000 0.014202 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003561 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
