HEADER TRANSFERASE 11-MAR-14 4CT2
TITLE HUMAN PDK1-PKCZETA KINASE CHIMERA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 50-359;
COMPND 5 SYNONYM: HPDK1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC
KEYWDS TRANSFERASE, ALLOSTERIC REGULATION, ALLOSTERIC SITE, PHOSPHORYLATION,
KEYWDS 2 AGC PROTEIN KINASE, CHIMERIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.O.SCHULZE,H.ZHANG,L.A.LOPEZ-GARCIA,R.M.BIONDI
REVDAT 3 20-DEC-23 4CT2 1 REMARK LINK
REVDAT 2 02-JUL-14 4CT2 1 JRNL
REVDAT 1 28-MAY-14 4CT2 0
JRNL AUTH H.ZHANG,S.NEIMANIS,L.A.LOPEZ-GARCIA,J.M.ARENCIBIA,S.AMON,
JRNL AUTH 2 A.STROBA,S.ZEUZEM,E.PROSCHAK,H.STARK,A.F.BAUER,K.BUSSCHOTS,
JRNL AUTH 3 T.J.JORGENSEN,M.ENGEL,J.O.SCHULZE,R.M.BIONDI
JRNL TITL MOLECULAR MECHANISM OF REGULATION OF THE ATYPICAL PROTEIN
JRNL TITL 2 KINASE C BY N-TERMINAL DOMAINS AND AN ALLOSTERIC SMALL
JRNL TITL 3 COMPOUND.
JRNL REF CHEM.BIOL. V. 21 754 2014
JRNL REFN ISSN 1074-5521
JRNL PMID 24836908
JRNL DOI 10.1016/J.CHEMBIOL.2014.04.007
REMARK 2
REMARK 2 RESOLUTION. 1.25 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) : 1.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 84010
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4201
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 26.3151 - 3.8800 0.99 2763 145 0.1802 0.1809
REMARK 3 2 3.8800 - 3.0812 1.00 2716 143 0.1733 0.2108
REMARK 3 3 3.0812 - 2.6922 1.00 2698 142 0.1900 0.2093
REMARK 3 4 2.6922 - 2.4462 1.00 2680 141 0.1887 0.2223
REMARK 3 5 2.4462 - 2.2710 0.99 2658 140 0.1894 0.2318
REMARK 3 6 2.2710 - 2.1371 0.99 2668 141 0.1906 0.2232
REMARK 3 7 2.1371 - 2.0302 1.00 2645 139 0.1915 0.2076
REMARK 3 8 2.0302 - 1.9418 0.99 2669 140 0.1995 0.2593
REMARK 3 9 1.9418 - 1.8671 1.00 2662 140 0.2088 0.2646
REMARK 3 10 1.8671 - 1.8027 0.99 2645 140 0.2058 0.2247
REMARK 3 11 1.8027 - 1.7463 0.99 2668 140 0.1900 0.2500
REMARK 3 12 1.7463 - 1.6964 0.99 2638 139 0.1959 0.2625
REMARK 3 13 1.6964 - 1.6518 1.00 2645 139 0.2024 0.2589
REMARK 3 14 1.6518 - 1.6115 1.00 2674 141 0.2025 0.2892
REMARK 3 15 1.6115 - 1.5748 1.00 2634 138 0.2005 0.2515
REMARK 3 16 1.5748 - 1.5413 1.00 2621 138 0.2030 0.2607
REMARK 3 17 1.5413 - 1.5105 1.00 2665 141 0.2025 0.2473
REMARK 3 18 1.5105 - 1.4820 1.00 2634 138 0.2155 0.2647
REMARK 3 19 1.4820 - 1.4555 1.00 2685 142 0.2164 0.2786
REMARK 3 20 1.4555 - 1.4309 1.00 2661 140 0.2251 0.2991
REMARK 3 21 1.4309 - 1.4078 1.00 2634 139 0.2280 0.2680
REMARK 3 22 1.4078 - 1.3861 1.00 2655 139 0.2197 0.2938
REMARK 3 23 1.3861 - 1.3657 1.00 2662 140 0.2253 0.2717
REMARK 3 24 1.3657 - 1.3465 1.00 2664 141 0.2278 0.2807
REMARK 3 25 1.3465 - 1.3283 1.00 2620 138 0.2293 0.2522
REMARK 3 26 1.3283 - 1.3111 1.00 2656 139 0.2535 0.3205
REMARK 3 27 1.3111 - 1.2947 1.00 2670 141 0.2594 0.2938
REMARK 3 28 1.2947 - 1.2791 1.00 2606 137 0.2617 0.3206
REMARK 3 29 1.2791 - 1.2642 1.00 2686 142 0.2844 0.3690
REMARK 3 30 1.2642 - 1.2500 1.00 2627 138 0.2856 0.3563
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) : 0.160
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.020
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 19.23
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.00
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 : 0.010 2346
REMARK 3 ANGLE : 1.457 3201
REMARK 3 CHIRALITY : 0.082 359
REMARK 3 PLANARITY : 0.009 402
REMARK 3 DIHEDRAL : 13.037 878
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: RESIDUES 118-123 ARE DISORDERED
REMARK 4
REMARK 4 4CT2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-MAR-14.
REMARK 100 THE DEPOSITION ID IS D_1290059913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-09
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 : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99999
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 84028
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.250
REMARK 200 RESOLUTION RANGE LOW (A) : 26.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.90
REMARK 200 R MERGE FOR SHELL (I) : 0.74000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3HRC
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M NA CITRATE, 0.1 M HEPES PH 7.5,
REMARK 280 10 MM DTT
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 73.77500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 22.31500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.77500
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 22.31500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 GLY A 49
REMARK 465 ALA A 50
REMARK 465 MET A 51
REMARK 465 ASP A 52
REMARK 465 GLY A 53
REMARK 465 THR A 54
REMARK 465 ALA A 55
REMARK 465 ALA A 56
REMARK 465 GLU A 57
REMARK 465 PRO A 58
REMARK 465 ARG A 59
REMARK 465 PRO A 60
REMARK 465 GLY A 61
REMARK 465 ALA A 62
REMARK 465 GLY A 63
REMARK 465 SER A 64
REMARK 465 LEU A 65
REMARK 465 GLN A 66
REMARK 465 HIS A 67
REMARK 465 ALA A 68
REMARK 465 GLN A 69
REMARK 465 PRO A 70
REMARK 465 PRO A 71
REMARK 465 PRO A 72
REMARK 465 GLN A 73
REMARK 465 PRO A 74
REMARK 465 HIS A 119
REMARK 465 LYS A 120
REMARK 465 GLU A 121
REMARK 465 ASN A 122
REMARK 465 LYS A 123
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 ARG A 75 N CA O CB CG CD NE
REMARK 470 ARG A 75 CZ NH1 NH2
REMARK 470 LYS A 76 CE NZ
REMARK 470 ARG A 78 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 83 CD CE NZ
REMARK 470 PHE A 93 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 116 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 117 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 118 CA C O CB CG1 CG2
REMARK 470 ILE A 124 CG1 CG2 CD1
REMARK 470 TYR A 126 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 128 CD OE1 NE2
REMARK 470 ARG A 172 CZ NH1 NH2
REMARK 470 LYS A 173 CG CD CE NZ
REMARK 470 LYS A 199 CE NZ
REMARK 470 LYS A 235 NZ
REMARK 470 LYS A 261 NZ
REMARK 470 LYS A 296 NZ
REMARK 470 GLU A 303 CG CD OE1 OE2
REMARK 470 LYS A 304 CD CE NZ
REMARK 470 LYS A 323 CE NZ
REMARK 470 GLU A 348 CG CD OE1 OE2
REMARK 470 ASN A 349 CG OD1 ND2
REMARK 470 GLN A 352 CG CD OE1 NE2
REMARK 470 LYS A 357 CD CE NZ
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 HH TYR A 108 O HOH A 2020 1.53
REMARK 500 O LYS A 304 O HOH A 2231 2.17
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 76 126.24 -30.08
REMARK 500 PHE A 93 39.86 -148.89
REMARK 500 HIS A 117 -77.24 -69.26
REMARK 500 ASP A 138 68.27 -160.03
REMARK 500 ARG A 204 -9.78 77.37
REMARK 500 ASP A 223 70.07 70.54
REMARK 500 ASP A 223 69.06 71.76
REMARK 500 GLU A 348 -77.98 -48.42
REMARK 500 ASN A 349 58.50 -108.30
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 A2032 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH A2135 DISTANCE = 7.10 ANGSTROMS
REMARK 525 HOH A2311 DISTANCE = 7.71 ANGSTROMS
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 NA A 700 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 223 OD2
REMARK 620 2 ASP A 223 OD2 5.8
REMARK 620 3 ATP A 500 O2B 81.5 86.5
REMARK 620 4 ATP A 500 O1G 140.7 141.0 74.5
REMARK 620 5 HOH A2172 O 68.7 67.1 128.0 149.8
REMARK 620 6 HOH A2173 O 102.0 96.3 154.3 87.9 75.6
REMARK 620 7 HOH A2176 O 66.3 64.6 75.9 77.7 123.6 82.2
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTD A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CT1 RELATED DB: PDB
REMARK 900 HUMAN PDK1-PKCZETA KINASE CHIMERA IN COMPLEX WITH ALLOSTERIC
REMARK 900 COMPOUND PS315 BOUND TO THE PIF-POCKET
DBREF 4CT2 A 50 359 UNP O15530 PDPK1_HUMAN 50 359
SEQADV 4CT2 GLY A 49 UNP O15530 EXPRESSION TAG
SEQADV 4CT2 VAL A 113 UNP O15530 LEU 113 ENGINEERED MUTATION
SEQADV 4CT2 VAL A 118 UNP O15530 ILE 118 ENGINEERED MUTATION
SEQADV 4CT2 HIS A 119 UNP O15530 ILE 119 ENGINEERED MUTATION
SEQADV 4CT2 ILE A 124 UNP O15530 VAL 124 ENGINEERED MUTATION
SEQADV 4CT2 GLN A 128 UNP O15530 THR 128 ENGINEERED MUTATION
SEQADV 4CT2 LYS A 131 UNP O15530 ARG 131 ENGINEERED MUTATION
SEQADV 4CT2 CYS A 148 UNP O15530 THR 148 ENGINEERED MUTATION
SEQADV 4CT2 LEU A 157 UNP O15530 PHE 157 ENGINEERED MUTATION
SEQADV 4CT2 GLY A 288 UNP O15530 TYR 288 ENGINEERED MUTATION
SEQADV 4CT2 ALA A 292 UNP O15530 GLN 292 ENGINEERED MUTATION
SEQRES 1 A 311 GLY ALA MET ASP GLY THR ALA ALA GLU PRO ARG PRO GLY
SEQRES 2 A 311 ALA GLY SER LEU GLN HIS ALA GLN PRO PRO PRO GLN PRO
SEQRES 3 A 311 ARG LYS LYS ARG PRO GLU ASP PHE LYS PHE GLY LYS ILE
SEQRES 4 A 311 LEU GLY GLU GLY SER PHE SER THR VAL VAL LEU ALA ARG
SEQRES 5 A 311 GLU LEU ALA THR SER ARG GLU TYR ALA ILE LYS ILE VAL
SEQRES 6 A 311 GLU LYS ARG HIS VAL HIS LYS GLU ASN LYS ILE PRO TYR
SEQRES 7 A 311 VAL GLN ARG GLU LYS ASP VAL MET SER ARG LEU ASP HIS
SEQRES 8 A 311 PRO PHE PHE VAL LYS LEU TYR PHE CYS PHE GLN ASP ASP
SEQRES 9 A 311 GLU LYS LEU TYR LEU GLY LEU SER TYR ALA LYS ASN GLY
SEQRES 10 A 311 GLU LEU LEU LYS TYR ILE ARG LYS ILE GLY SER PHE ASP
SEQRES 11 A 311 GLU THR CYS THR ARG PHE TYR THR ALA GLU ILE VAL SER
SEQRES 12 A 311 ALA LEU GLU TYR LEU HIS GLY LYS GLY ILE ILE HIS ARG
SEQRES 13 A 311 ASP LEU LYS PRO GLU ASN ILE LEU LEU ASN GLU ASP MET
SEQRES 14 A 311 HIS ILE GLN ILE THR ASP PHE GLY THR ALA LYS VAL LEU
SEQRES 15 A 311 SER PRO GLU SER LYS GLN ALA ARG ALA ASN SEP PHE VAL
SEQRES 16 A 311 GLY THR ALA GLN TYR VAL SER PRO GLU LEU LEU THR GLU
SEQRES 17 A 311 LYS SER ALA CYS LYS SER SER ASP LEU TRP ALA LEU GLY
SEQRES 18 A 311 CYS ILE ILE TYR GLN LEU VAL ALA GLY LEU PRO PRO PHE
SEQRES 19 A 311 ARG ALA GLY ASN GLU GLY LEU ILE PHE ALA LYS ILE ILE
SEQRES 20 A 311 LYS LEU GLU TYR ASP PHE PRO GLU LYS PHE PHE PRO LYS
SEQRES 21 A 311 ALA ARG ASP LEU VAL GLU LYS LEU LEU VAL LEU ASP ALA
SEQRES 22 A 311 THR LYS ARG LEU GLY CYS GLU GLU MET GLU GLY TYR GLY
SEQRES 23 A 311 PRO LEU LYS ALA HIS PRO PHE PHE GLU SER VAL THR TRP
SEQRES 24 A 311 GLU ASN LEU HIS GLN GLN THR PRO PRO LYS LEU THR
MODRES 4CT2 SEP A 241 SER PHOSPHOSERINE
HET SEP A 241 14
HET ATP A 500 42
HET DTD A 600 16
HET NA A 700 1
HETNAM SEP PHOSPHOSERINE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM DTD DITHIANE DIOL
HETNAM NA SODIUM ION
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 ATP C10 H16 N5 O13 P3
FORMUL 3 DTD C4 H8 O2 S2
FORMUL 4 NA NA 1+
FORMUL 5 HOH *311(H2 O)
HELIX 1 2 ILE A 124 SER A 135 1 12
HELIX 2 3 LEU A 167 ILE A 174 1 8
HELIX 3 4 GLU A 179 LYS A 199 1 21
HELIX 4 7 PRO A 251 GLU A 256 1 6
HELIX 5 8 SER A 262 ALA A 277 1 16
HELIX 6 9 GLU A 287 ILE A 295 1 9
HELIX 7 10 PRO A 307 LEU A 316 1 10
HELIX 8 13 TYR A 333 ALA A 338 1 6
SHEET 1 AA 5 PHE A 82 GLY A 91 0
SHEET 2 AA 5 SER A 94 GLU A 101 -1 O VAL A 96 N LEU A 88
SHEET 3 AA 5 ARG A 106 GLU A 114 -1 O TYR A 108 N ALA A 99
SHEET 4 AA 5 LYS A 154 LEU A 159 -1 O LEU A 155 N VAL A 113
SHEET 5 AA 5 PHE A 147 ASP A 151 -1 O PHE A 147 N GLY A 158
SHEET 1 AB 3 GLY A 165 GLU A 166 0
SHEET 2 AB 3 ILE A 211 ASN A 214 -1 N LEU A 213 O GLY A 165
SHEET 3 AB 3 HIS A 218 ILE A 221 -1 O GLN A 220 N LEU A 212
SHEET 1 AC 2 ILE A 201 ILE A 202 0
SHEET 2 AC 2 LYS A 228 VAL A 229 -1 O LYS A 228 N ILE A 202
LINK C ASN A 240 N SEP A 241 1555 1555 1.33
LINK C SEP A 241 N PHE A 242 1555 1555 1.33
LINK OD2BASP A 223 NA NA A 700 1555 1555 2.46
LINK OD2AASP A 223 NA NA A 700 1555 1555 2.49
LINK O2B ATP A 500 NA NA A 700 1555 1555 2.75
LINK O1G ATP A 500 NA NA A 700 1555 1555 2.35
LINK NA NA A 700 O HOH A2172 1555 1555 3.12
LINK NA NA A 700 O HOH A2173 1555 1555 2.57
LINK NA NA A 700 O HOH A2176 1555 1555 3.19
SITE 1 AC1 20 GLY A 89 GLY A 91 SER A 92 SER A 94
SITE 2 AC1 20 VAL A 96 ALA A 109 LYS A 111 SER A 160
SITE 3 AC1 20 ALA A 162 GLU A 166 LEU A 212 ASP A 223
SITE 4 AC1 20 NA A 700 HOH A2016 HOH A2034 HOH A2174
SITE 5 AC1 20 HOH A2176 HOH A2182 HOH A2308 HOH A2309
SITE 1 AC2 6 PHE A 242 VAL A 243 GLY A 244 ALA A 246
SITE 2 AC2 6 ARG A 283 GLU A 287
SITE 1 AC3 3 ASP A 223 ATP A 500 HOH A2173
CRYST1 147.550 44.630 47.610 90.00 100.96 90.00 C 1 2 1 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 0.006777 0.000000 0.001312 0.00000
SCALE2 0.000000 0.022406 0.000000 0.00000
SCALE3 0.000000 0.000000 0.021394 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
