HEADER TRANSFERASE 08-OCT-02 1O6K
TITLE STRUCTURE OF ACTIVATED FORM OF PKB KINASE DOMAIN S474D WITH
TITLE 2 GSK3 PEPTIDE AND AMP-PNP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RAC-BETA SERINE/THREONINE PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 146-481;
COMPND 5 SYNONYM: RAC-PK-BETA, PROTEIN KINASE AKT-2, PROTEIN KINASE
COMPND 6 B, BETA, PKB BETA, PROTEIN KINASE BETA, AKT2;
COMPND 7 EC: 2.7.1.-;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: GLYCOGEN SYNTHASE KINASE-3 BETA;
COMPND 12 CHAIN: C;
COMPND 13 FRAGMENT: PEPTIDE, RESIDUES 3-12;
COMPND 14 SYNONYM: GSK-3 BETA;
COMPND 15 EC: 2.7.1.37;
COMPND 16 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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS PROTEIN KINASE, TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.YANG,P.CRON,V.M.GOOD,V.THOMPSON,B.A.HEMMINGS,D.BARFORD
REVDAT 2 24-FEB-09 1O6K 1 VERSN
REVDAT 1 19-NOV-02 1O6K 0
JRNL AUTH J.YANG,P.CRON,V.M.GOOD,V.THOMPSON,B.A.HEMMINGS,
JRNL AUTH 2 D.BARFORD
JRNL TITL CRYSTAL STRUCTURE OF AN ACTIVATED AKT/PROTEIN
JRNL TITL 2 KINASE B TERNARY COMPLEX WITH GSK-3 PEPTIDE AND
JRNL TITL 3 AMP-PNP
JRNL REF NAT.STRUCT.BIOL. V. 9 940 2002
JRNL REFN ISSN 1072-8368
JRNL PMID 12434148
JRNL DOI 10.1038/NSB870
REMARK 2
REMARK 2 RESOLUTION. 1.7 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1566941.48
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 76.4
REMARK 3 NUMBER OF REFLECTIONS : 30601
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 1517
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 0.1
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4
REMARK 3 BIN R VALUE (WORKING SET) : 0.122
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 : 2657
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 281
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.1
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.04
REMARK 3 B22 (A**2) : -3.02
REMARK 3 B33 (A**2) : 7.0
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : 0.00
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.14
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.14
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.5
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.6
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.44
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.27 ; 1.50
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.01 ; 2.00
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.89 ; 2.00
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.87 ; 2.50
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.337772
REMARK 3 BSOL : 17.395
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 : PARAM19X.PRO
REMARK 3 PARAMETER FILE 2 : ANP.PAR
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1O6K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-OCT-02.
REMARK 100 THE PDBE ID CODE IS EBI-11497.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 116971
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 82.4
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 63.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.18600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: CDK1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.6
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML PROTEIN
REMARK 280 20 PEG 4K, 10% ISOPROPONAL, 5 MM DTT
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 22.45300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.70500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.49900
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.70500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.45300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.49900
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 300
REMARK 300 DETAILS:CHAIN A IS A MONOMER, BUT THIS ENTRY IS
REMARK 300 CLASSIFIEDAS A DIMER AS CHAIN A IS IN COMPLEX
REMARK 300 WITH A PEPTIDE(CHAIN C), FORMING A DIMERIC
REMARK 300 ASSOCIATION.
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 PROTEIN KINASE KNOWN TO PHOSPHORYLATE SEVERAL PROTEINS.
REMARK 400
REMARK 400 ENGINEERED MUTATION IN CHAIN A SER 474 ASP
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 ILE A 450
REMARK 465 THR A 451
REMARK 465 PRO A 452
REMARK 465 PRO A 453
REMARK 465 ASP A 454
REMARK 465 ARG A 455
REMARK 465 TYR A 456
REMARK 465 ASP A 457
REMARK 465 SER A 458
REMARK 465 LEU A 459
REMARK 465 GLY A 460
REMARK 465 LEU A 461
REMARK 465 LEU A 462
REMARK 465 GLU A 463
REMARK 465 LEU A 464
REMARK 465 ASP A 465
REMARK 465 ARG A 480
REMARK 465 GLU A 481
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 THR A 449 OG1 CG2
REMARK 470 GLN A 466 CG CD OE1 NE2
REMARK 470 ARG A 467 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 479 CG1 CG2 CD1
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 221 -162.90 -117.93
REMARK 500 ARG A 245 -44.99 67.42
REMARK 500 ARG A 274 -9.20 65.54
REMARK 500 ASP A 293 82.90 56.87
REMARK 500 ASN A 325 -142.99 70.02
REMARK 500 ASP A 399 -111.74 51.86
REMARK 500 GLN A 429 49.22 -87.16
REMARK 500 PHE A 473 -152.66 -105.99
REMARK 500 ARG C 4 110.34 61.79
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 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 MN A1481 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A1480 O2G
REMARK 620 2 ASP A 293 OD2 88.8
REMARK 620 3 ANP A1480 O2A 133.4 90.6
REMARK 620 4 HOH A2265 O 88.4 176.4 89.8
REMARK 620 5 ASN A 280 OD1 121.1 89.5 105.5 93.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1482 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A1480 O1G
REMARK 620 2 ASP A 293 OD1 150.5
REMARK 620 3 HOH A2266 O 99.3 93.5
REMARK 620 4 HOH A2267 O 106.3 98.7 95.6
REMARK 620 5 ASP A 293 OD2 97.8 56.6 85.4 155.3
REMARK 620 6 ANP A1480 O2B 82.3 82.6 174.1 89.3 88.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1481
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A1482
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A1480
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GZK RELATED DB: PDB
REMARK 900 MOLECULAR MECHANISM FOR THE REGULATION OF
REMARK 900 PROTEIN KINASE B/AKT BY HYDROPHOBIC MOTIF
REMARK 900 PHOSPHORYLATION
REMARK 900 RELATED ID: 1GZN RELATED DB: PDB
REMARK 900 STRUCTURE OF PKB KINASE DOMAIN
REMARK 900 RELATED ID: 1GZO RELATED DB: PDB
REMARK 900 STRUCTURE OF PROTEIN KINASE B UNPHOSPHORYLATED
REMARK 900 RELATED ID: 1O6L RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN ACTIVATED AKT/PROTEIN KINASE B
REMARK 900 (PKB-PIF CHIMERA) TERNARY COMPLEX WITH AMP-PNP AND GSK3
REMARK 900 PEPTIDESTRUCTURE OF PROTEIN KINASE B UNPHOSPHORYLATED
DBREF 1O6K A 146 481 UNP P31751 AKT2_HUMAN 146 481
DBREF 1O6K C 3 12 UNP P49841 KG3B_HUMAN 3 12
SEQADV 1O6K ASP A 474 UNP P31751 SER 474 ENGINEERED MUTATION
SEQRES 1 A 336 LYS VAL THR MET ASN ASP PHE ASP TYR LEU LYS LEU LEU
SEQRES 2 A 336 GLY LYS GLY THR PHE GLY LYS VAL ILE LEU VAL ARG GLU
SEQRES 3 A 336 LYS ALA THR GLY ARG TYR TYR ALA MET LYS ILE LEU ARG
SEQRES 4 A 336 LYS GLU VAL ILE ILE ALA LYS ASP GLU VAL ALA HIS THR
SEQRES 5 A 336 VAL THR GLU SER ARG VAL LEU GLN ASN THR ARG HIS PRO
SEQRES 6 A 336 PHE LEU THR ALA LEU LYS TYR ALA PHE GLN THR HIS ASP
SEQRES 7 A 336 ARG LEU CYS PHE VAL MET GLU TYR ALA ASN GLY GLY GLU
SEQRES 8 A 336 LEU PHE PHE HIS LEU SER ARG GLU ARG VAL PHE THR GLU
SEQRES 9 A 336 GLU ARG ALA ARG PHE TYR GLY ALA GLU ILE VAL SER ALA
SEQRES 10 A 336 LEU GLU TYR LEU HIS SER ARG ASP VAL VAL TYR ARG ASP
SEQRES 11 A 336 ILE LYS LEU GLU ASN LEU MET LEU ASP LYS ASP GLY HIS
SEQRES 12 A 336 ILE LYS ILE THR ASP PHE GLY LEU CYS LYS GLU GLY ILE
SEQRES 13 A 336 SER ASP GLY ALA THR MET LYS TPO PHE CYS GLY THR PRO
SEQRES 14 A 336 GLU TYR LEU ALA PRO GLU VAL LEU GLU ASP ASN ASP TYR
SEQRES 15 A 336 GLY ARG ALA VAL ASP TRP TRP GLY LEU GLY VAL VAL MET
SEQRES 16 A 336 TYR GLU MET MET CYS GLY ARG LEU PRO PHE TYR ASN GLN
SEQRES 17 A 336 ASP HIS GLU ARG LEU PHE GLU LEU ILE LEU MET GLU GLU
SEQRES 18 A 336 ILE ARG PHE PRO ARG THR LEU SER PRO GLU ALA LYS SER
SEQRES 19 A 336 LEU LEU ALA GLY LEU LEU LYS LYS ASP PRO LYS GLN ARG
SEQRES 20 A 336 LEU GLY GLY GLY PRO SER ASP ALA LYS GLU VAL MET GLU
SEQRES 21 A 336 HIS ARG PHE PHE LEU SER ILE ASN TRP GLN ASP VAL VAL
SEQRES 22 A 336 GLN LYS LYS LEU LEU PRO PRO PHE LYS PRO GLN VAL THR
SEQRES 23 A 336 SER GLU VAL ASP THR ARG TYR PHE ASP ASP GLU PHE THR
SEQRES 24 A 336 ALA GLN SER ILE THR ILE THR PRO PRO ASP ARG TYR ASP
SEQRES 25 A 336 SER LEU GLY LEU LEU GLU LEU ASP GLN ARG THR HIS PHE
SEQRES 26 A 336 PRO GLN PHE ASP TYR SER ALA SER ILE ARG GLU
SEQRES 1 C 10 GLY ARG PRO ARG THR THR SER PHE ALA GLU
MODRES 1O6K TPO A 309 THR PHOSPHOTHREONINE
HET TPO A 309 11
HET MN A1481 1
HET MN A1482 1
HET ANP A1480 31
HETNAM TPO PHOSPHOTHREONINE
HETNAM MN MANGANESE (II) ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 MN 2(MN 2+)
FORMUL 5 ANP C10 H17 N6 O12 P3
FORMUL 6 HOH *281(H2 O1)
HELIX 1 1 THR A 148 ASN A 150 5 3
HELIX 2 2 LYS A 185 LYS A 191 1 7
HELIX 3 3 GLU A 193 THR A 207 1 15
HELIX 4 4 GLU A 236 ARG A 245 1 10
HELIX 5 5 THR A 248 ARG A 269 1 22
HELIX 6 6 THR A 313 LEU A 317 5 5
HELIX 7 7 ALA A 330 GLY A 346 1 17
HELIX 8 8 ASP A 354 GLU A 365 1 12
HELIX 9 9 SER A 374 LEU A 385 1 12
HELIX 10 10 ASP A 399 GLU A 405 1 7
HELIX 11 11 HIS A 406 LEU A 410 5 5
HELIX 12 12 ASN A 413 GLN A 419 1 7
HELIX 13 13 ASP A 440 ALA A 445 1 6
SHEET 1 AA 6 PHE A 152 LYS A 160 0
SHEET 2 AA 6 GLY A 164 GLU A 171 -1 O VAL A 166 N LEU A 158
SHEET 3 AA 6 TYR A 177 ARG A 184 -1 O TYR A 178 N VAL A 169
SHEET 4 AA 6 ARG A 224 GLU A 230 -1 O LEU A 225 N LEU A 183
SHEET 5 AA 6 LEU A 215 GLN A 220 -1 N LYS A 216 O VAL A 228
SHEET 6 AA 6 TYR A 475 SER A 476 -1 O TYR A 475 N ALA A 218
SHEET 1 AB 2 LEU A 281 LEU A 283 0
SHEET 2 AB 2 ILE A 289 ILE A 291 -1 O LYS A 290 N MET A 282
SHEET 1 AC 2 CYS A 311 GLY A 312 0
SHEET 2 AC 2 PHE C 10 ALA C 11 -1 O PHE C 10 N GLY A 312
LINK C LYS A 308 N TPO A 309 1555 1555 1.34
LINK C TPO A 309 N PHE A 310 1555 1555 1.33
LINK O2A ANP A1480 MN MN A1481 1555 1555 2.04
LINK MN MN A1481 OD2 ASP A 293 1555 1555 2.26
LINK MN MN A1481 O HOH A2265 1555 1555 2.21
LINK MN MN A1481 OD1 ASN A 280 1555 1555 2.17
LINK MN MN A1481 O2G ANP A1480 1555 1555 2.13
LINK MN MN A1482 O HOH A2266 1555 1555 2.25
LINK MN MN A1482 O HOH A2267 1555 1555 2.18
LINK MN MN A1482 OD2 ASP A 293 1555 1555 2.34
LINK MN MN A1482 O2B ANP A1480 1555 1555 2.17
LINK MN MN A1482 OD1 ASP A 293 1555 1555 2.28
LINK MN MN A1482 O1G ANP A1480 1555 1555 2.16
SITE 1 AC1 4 ASN A 280 ASP A 293 ANP A1480 HOH A2265
SITE 1 AC2 4 ASP A 293 ANP A1480 HOH A2266 HOH A2267
SITE 1 AC3 28 GLY A 159 GLY A 161 VAL A 166 ALA A 179
SITE 2 AC3 28 LYS A 181 THR A 213 MET A 229 GLU A 230
SITE 3 AC3 28 ALA A 232 GLU A 236 LYS A 277 GLU A 279
SITE 4 AC3 28 ASN A 280 MET A 282 THR A 292 ASP A 293
SITE 5 AC3 28 PHE A 439 MN A1481 MN A1482 HOH A2008
SITE 6 AC3 28 HOH A2013 HOH A2264 HOH A2265 HOH A2267
SITE 7 AC3 28 ARG C 6 THR C 8 SER C 9 HOH C2008
CRYST1 44.906 60.998 129.410 90.00 90.00 90.00 P 21 21 21 4
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 0.022269 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016394 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007727 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
