HEADER TRANSFERASE 03-DEC-02 1J1C
TITLE BINARY COMPLEX STRUCTURE OF HUMAN TAU PROTEIN KINASE I WITH ADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TAU PROTEIN KINASE I, GSK-3 BETA;
COMPND 5 EC: 2.7.1.37;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS COMPLEX, TAU, KINASE, ADP, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.AOKI,T.YOKOTA,I.SUGIURA,C.SASAKI,T.HASEGAWA,C.OKUMURA,T.KOHNO,
AUTHOR 2 S.SUGIO,T.MATSUZAKI
REVDAT 4 27-DEC-23 1J1C 1 REMARK LINK
REVDAT 3 24-FEB-09 1J1C 1 VERSN
REVDAT 2 24-FEB-04 1J1C 1 REMARK
REVDAT 1 03-DEC-03 1J1C 0
JRNL AUTH M.AOKI,T.YOKOTA,I.SUGIURA,C.SASAKI,T.HASEGAWA,C.OKUMURA,
JRNL AUTH 2 K.ISHIGURO,T.KOHNO,S.SUGIO,T.MATSUZAKI
JRNL TITL STRUCTURAL INSIGHT INTO NUCLEOTIDE RECOGNITION IN
JRNL TITL 2 TAU-PROTEIN KINASE I/GLYCOGEN SYNTHASE KINASE 3 BETA.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 439 2004
JRNL REFN ISSN 0907-4449
JRNL PMID 14993667
JRNL DOI 10.1107/S090744490302938X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.AOKI,M.IWAMOTO-SUGAI,I.SUGIURA,C.SASAKI,T.HASEGAWA,
REMARK 1 AUTH 2 C.OKUMURA,S.SUGIO,T.KOHNO,T.MATSUZAKI
REMARK 1 TITL EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF HUMAN
REMARK 1 TITL 2 TAU-PROTEIN KINASE I/GLYCOGEN SYNTHASE KINASE-3BETA
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 56 1464 2000
REMARK 1 REFN ISSN 0907-4449
REMARK 1 DOI 10.1107/S0907444900010386
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 98.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 74557
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5737
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 267
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : 1.173
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1J1C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000005506.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL; NULL
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY; SPRING-8
REMARK 200 BEAMLINE : BL-6A; BL24XU
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000; 0.835
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4; RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 86325
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 15.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.0
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; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR
REMARK 200 SOFTWARE USED: DM
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, SODIUM CHLORIDE, MAGNESIUM
REMARK 280 CHLORIDE, GLYCEROL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 278K
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 41.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 89.05000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.05000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 89.05000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 41.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.05000
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: 4930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 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 501
REMARK 465 SER B 502
REMARK 465 GLY B 503
REMARK 465 ARG B 504
REMARK 465 PRO B 505
REMARK 465 ARG B 506
REMARK 465 THR B 507
REMARK 465 THR B 508
REMARK 465 SER B 509
REMARK 465 PHE B 510
REMARK 465 ALA B 511
REMARK 465 GLU B 512
REMARK 465 SER B 513
REMARK 465 CYS B 514
REMARK 465 LYS B 515
REMARK 465 PRO B 516
REMARK 465 VAL B 517
REMARK 465 GLN B 518
REMARK 465 GLN B 519
REMARK 465 PRO B 520
REMARK 465 SER B 521
REMARK 465 ALA B 522
REMARK 465 ALA B 887
REMARK 465 ALA B 888
REMARK 465 SER B 889
REMARK 465 THR B 890
REMARK 465 PRO B 891
REMARK 465 THR B 892
REMARK 465 ASN B 893
REMARK 465 ALA B 894
REMARK 465 THR B 895
REMARK 465 ALA B 896
REMARK 465 ALA B 897
REMARK 465 SER B 898
REMARK 465 ASP B 899
REMARK 465 ALA B 900
REMARK 465 ASN B 901
REMARK 465 THR B 902
REMARK 465 GLY B 903
REMARK 465 ASP B 904
REMARK 465 ARG B 905
REMARK 465 GLY B 906
REMARK 465 GLN B 907
REMARK 465 THR B 908
REMARK 465 ASN B 909
REMARK 465 ASN B 910
REMARK 465 ALA B 911
REMARK 465 ALA B 912
REMARK 465 SER B 913
REMARK 465 ALA B 914
REMARK 465 SER B 915
REMARK 465 ALA B 916
REMARK 465 SER B 917
REMARK 465 ASN B 918
REMARK 465 SER B 919
REMARK 465 THR B 920
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 OH TYR A 288 OG SER B 715 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 LYS A 123 -155.41 -179.10
REMARK 500 ASP A 181 47.06 -150.70
REMARK 500 ASP A 200 82.17 62.79
REMARK 500 CYS A 218 130.85 78.17
REMARK 500 TYR A 221 -35.01 99.09
REMARK 500 ASN A 285 102.61 -160.83
REMARK 500 ASN A 287 -64.15 -149.00
REMARK 500 TYR A 288 121.95 -36.51
REMARK 500 PRO A 294 122.76 -34.68
REMARK 500 PRO A 300 109.13 -44.14
REMARK 500 ASN A 370 69.68 178.69
REMARK 500 ASP B 549 79.90 -63.77
REMARK 500 ASN B 564 137.16 -170.29
REMARK 500 GLU B 621 6.21 -56.39
REMARK 500 LYS B 623 -151.99 175.42
REMARK 500 ALA B 649 10.49 -69.16
REMARK 500 ASP B 681 44.04 -149.16
REMARK 500 ASP B 700 82.68 63.33
REMARK 500 CYS B 718 139.86 78.71
REMARK 500 TYR B 721 -36.53 101.62
REMARK 500 ASN B 787 -41.88 -155.41
REMARK 500 THR B 789 -75.92 -69.96
REMARK 500 GLU B 790 119.06 -35.73
REMARK 500 PRO B 794 129.22 -32.59
REMARK 500 ARG B 808 3.14 87.45
REMARK 500 ASN B 852 22.45 -74.73
REMARK 500 ASN B 870 74.61 -169.49
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 431 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 186 OD1
REMARK 620 2 ASP A 200 OD2 80.9
REMARK 620 3 ADP A 430 O1B 140.1 62.3
REMARK 620 4 ADP A 430 O2A 89.4 71.1 65.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 931 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 122 O
REMARK 620 2 ASN B 686 OD1 97.3
REMARK 620 3 ASP B 700 OD2 66.9 76.1
REMARK 620 4 ADP B 930 O2A 132.2 82.0 66.6
REMARK 620 5 ADP B 930 O1B 81.5 134.8 61.9 67.3
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 431
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 931
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 430
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 930
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1J1B RELATED DB: PDB
REMARK 900 HUMAN TAU PROTEIN KINASE I WITH AMPPNP
DBREF 1J1C A 1 420 UNP P49841 GSK3B_HUMAN 1 420
DBREF 1J1C B 501 920 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 MG A 431 1
HET ADP A 430 27
HET MG B 931 1
HET ADP B 930 27
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 3 MG 2(MG 2+)
FORMUL 4 ADP 2(C10 H15 N5 O10 P2)
FORMUL 7 HOH *267(H2 O)
HELIX 1 1 ASN A 95 LEU A 104 1 10
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 PHE A 305 1 6
HELIX 10 10 PRO A 310 LEU A 321 1 12
HELIX 11 11 THR A 324 ARG A 328 5 5
HELIX 12 12 THR A 330 ALA A 336 1 7
HELIX 13 13 HIS A 337 ASP A 345 5 9
HELIX 14 14 THR A 363 SER A 368 1 6
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 ASN B 595 LEU B 604 1 10
HELIX 18 18 VAL B 639 ALA B 649 1 11
HELIX 19 19 PRO B 654 SER B 674 1 21
HELIX 20 20 LYS B 683 GLN B 685 5 3
HELIX 21 21 ALA B 724 PHE B 729 1 6
HELIX 22 22 SER B 736 GLY B 753 1 18
HELIX 23 23 SER B 761 GLY B 774 1 14
HELIX 24 24 THR B 777 ASN B 785 1 9
HELIX 25 25 PRO B 800 PHE B 805 1 6
HELIX 26 26 PRO B 810 LEU B 821 1 12
HELIX 27 27 THR B 824 ARG B 828 5 5
HELIX 28 28 THR B 830 ALA B 836 1 7
HELIX 29 29 HIS B 837 ASP B 845 5 9
HELIX 30 30 THR B 863 SER B 868 1 6
HELIX 31 31 ASN B 870 PRO B 872 5 3
HELIX 32 32 LEU B 873 ILE B 878 1 6
HELIX 33 33 PRO B 879 ILE B 884 5 6
SHEET 1 A 7 THR A 38 PRO A 44 0
SHEET 2 A 7 GLN A 52 ASN A 64 -1 N GLN A 52 O ALA A 42
SHEET 3 A 7 VAL A 69 LEU A 75 -1 O VAL A 70 N ILE A 62
SHEET 4 A 7 LEU A 81 LEU A 88 -1 N VAL A 82 O ALA A 73
SHEET 5 A 7 GLU A 125 ASP A 133 -1 N LEU A 128 O VAL A 87
SHEET 6 A 7 LEU A 112 GLY A 120 -1 N ARG A 113 O VAL A 131
SHEET 7 A 7 THR A 38 PRO A 44 -1 N THR A 43 O PHE A 115
SHEET 1 B 3 GLU A 137 THR A 138 0
SHEET 2 B 3 LEU A 187 ASP A 190 -1 N LEU A 189 O GLU A 137
SHEET 3 B 3 VAL A 195 LEU A 198 -1 O VAL A 195 N ASP A 190
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
SHEET 1 D 8 LYS B 527 ARG B 530 0
SHEET 2 D 8 LYS B 536 PRO B 544 -1 N VAL B 537 O SER B 529
SHEET 3 D 8 GLN B 552 ASN B 564 -1 O GLN B 552 N ALA B 542
SHEET 4 D 8 GLY B 568 LEU B 575 -1 O VAL B 570 N ILE B 562
SHEET 5 D 8 LEU B 581 GLN B 589 -1 N VAL B 582 O ALA B 573
SHEET 6 D 8 VAL B 626 ASP B 633 -1 O VAL B 626 N GLN B 589
SHEET 7 D 8 LEU B 612 SER B 619 -1 N ARG B 613 O VAL B 631
SHEET 8 D 8 LYS B 536 PRO B 544 -1 N THR B 543 O PHE B 615
SHEET 1 E 3 GLU B 637 THR B 638 0
SHEET 2 E 3 LEU B 687 ASP B 690 -1 N LEU B 689 O GLU B 637
SHEET 3 E 3 VAL B 695 LEU B 698 -1 O VAL B 695 N ASP B 690
SHEET 1 F 2 ILE B 677 CYS B 678 0
SHEET 2 F 2 LYS B 705 GLN B 706 -1 O LYS B 705 N CYS B 678
LINK OD1 ASN A 186 MG MG A 431 1555 1555 2.43
LINK OD2 ASP A 200 MG MG A 431 1555 1555 2.58
LINK O1B ADP A 430 MG MG A 431 1555 1555 2.41
LINK O2A ADP A 430 MG MG A 431 1555 1555 2.49
LINK O HOH B 122 MG MG B 931 1555 1555 2.39
LINK OD1 ASN B 686 MG MG B 931 1555 1555 2.36
LINK OD2 ASP B 700 MG MG B 931 1555 1555 2.69
LINK O2A ADP B 930 MG MG B 931 1555 1555 2.39
LINK O1B ADP B 930 MG MG B 931 1555 1555 2.43
SITE 1 AC1 3 ASN A 186 ASP A 200 ADP A 430
SITE 1 AC2 4 HOH B 122 ASN B 686 ASP B 700 ADP B 930
SITE 1 AC3 18 GLY A 65 VAL A 70 ALA A 83 LYS A 85
SITE 2 AC3 18 VAL A 110 ASP A 133 TYR A 134 VAL A 135
SITE 3 AC3 18 ARG A 141 GLN A 185 ASN A 186 LEU A 188
SITE 4 AC3 18 ASP A 200 MG A 431 HOH A 540 HOH A 544
SITE 5 AC3 18 HOH A 556 HOH A 557
SITE 1 AC4 19 HOH B 38 HOH B 66 HOH B 75 HOH B 233
SITE 2 AC4 19 ILE B 562 GLY B 565 VAL B 570 ALA B 583
SITE 3 AC4 19 LYS B 585 VAL B 610 ASP B 633 TYR B 634
SITE 4 AC4 19 VAL B 635 THR B 638 GLN B 685 ASN B 686
SITE 5 AC4 19 LEU B 688 ASP B 700 MG B 931
CRYST1 82.900 86.100 178.100 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 0.012063 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011614 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005615 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
