HEADER TRANSFERASE/TRANSFERASE INHIBITOR 19-OCT-12 4HNI
TITLE CRYSTAL STRUCTURE OF CK1E IN COMPLEX WITH PF4800567
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE I ISOFORM EPSILON;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CKI-EPSILON, CKIE;
COMPND 5 EC: 2.7.11.1;
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 GENE: CSNK1E;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CK1E, KINASE, INHIBITOR, PF4800567, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HUANG,A.M.LONG,H.ZHAO
REVDAT 4 28-FEB-24 4HNI 1 REMARK SEQADV
REVDAT 3 07-NOV-18 4HNI 1 REMARK
REVDAT 2 02-JAN-13 4HNI 1 JRNL
REVDAT 1 14-NOV-12 4HNI 0
JRNL AUTH A.M.LONG,H.ZHAO,X.HUANG
JRNL TITL STRUCTURAL BASIS FOR THE POTENT AND SELECTIVE INHIBITION OF
JRNL TITL 2 CASEIN KINASE 1 EPSILON.
JRNL REF J.MED.CHEM. V. 55 10307 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 23106386
JRNL DOI 10.1021/JM301336N
REMARK 2
REMARK 2 RESOLUTION. 2.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
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 : 26156
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) : 0.237
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1331
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 : 4597
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 95
REMARK 3 SOLVENT ATOMS : 63
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) : NULL
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 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 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 4HNI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-225
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26206
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.740
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.14600
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) : 2.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.68500
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, 3% ETHANOL, 1.1-1.6 M
REMARK 280 (NH4)2SO4, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 77.71300
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 55.55400
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 55.55400
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 116.56950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 55.55400
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 55.55400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 38.85650
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 55.55400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.55400
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 116.56950
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 55.55400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.55400
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 38.85650
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 77.71300
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 GLU A 2
REMARK 465 LYS A 43
REMARK 465 THR A 44
REMARK 465 LYS A 45
REMARK 465 HIS A 46
REMARK 465 PRO A 47
REMARK 465 GLN A 48
REMARK 465 LEU A 49
REMARK 465 LYS A 294
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 LYS B 43
REMARK 465 THR B 44
REMARK 465 LYS B 45
REMARK 465 HIS B 46
REMARK 465 PRO B 47
REMARK 465 GLN B 48
REMARK 465 LEU B 49
REMARK 465 HIS B 50
REMARK 465 ILE B 51
REMARK 465 LYS B 294
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 GLU A 52 CG CD OE1 OE2
REMARK 470 ARG A 160 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 52 CG CD OE1 OE2
REMARK 470 ARG B 160 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 217 CG CD CE NZ
REMARK 470 TYR B 225 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 HIS B 278 CG ND1 CD2 CE1 NE2
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 OE1 GLU A 117 NH2 ARG A 270 2.14
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 GLU B 247 CB GLU B 247 CG 0.156
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 GLY B 6 N - CA - C ANGL. DEV. = -18.6 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 ASN A 7 -36.01 59.22
REMARK 500 ALA A 30 -78.53 -62.50
REMARK 500 TRP A 70 131.75 -174.35
REMARK 500 ASP A 76 -6.08 -55.31
REMARK 500 ASP A 128 53.37 -152.76
REMARK 500 ARG A 160 -76.58 -78.26
REMARK 500 SER A 210 145.10 176.53
REMARK 500 LYS A 217 103.00 -57.59
REMARK 500 LYS A 221 -69.39 -26.36
REMARK 500 ASN B 7 31.42 -140.50
REMARK 500 TRP B 70 129.72 -177.30
REMARK 500 ARG B 127 -1.34 66.30
REMARK 500 ASP B 128 54.75 -151.64
REMARK 500 ALA B 219 -82.99 -47.87
REMARK 500 THR B 220 -175.94 -62.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16W A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 16W B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4HNK RELATED DB: PDB
REMARK 900 RELATED ID: 4HOK RELATED DB: PDB
DBREF 4HNI A 1 294 UNP P49674 KC1E_HUMAN 1 294
DBREF 4HNI B 1 294 UNP P49674 KC1E_HUMAN 1 294
SEQADV 4HNI GLY A -1 UNP P49674 EXPRESSION TAG
SEQADV 4HNI SER A 0 UNP P49674 EXPRESSION TAG
SEQADV 4HNI GLY B -1 UNP P49674 EXPRESSION TAG
SEQADV 4HNI SER B 0 UNP P49674 EXPRESSION TAG
SEQRES 1 A 296 GLY SER MET GLU LEU ARG VAL GLY ASN LYS TYR ARG LEU
SEQRES 2 A 296 GLY ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR
SEQRES 3 A 296 LEU GLY ALA ASN ILE ALA SER GLY GLU GLU VAL ALA ILE
SEQRES 4 A 296 LYS LEU GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS
SEQRES 5 A 296 ILE GLU SER LYS PHE TYR LYS MET MET GLN GLY GLY VAL
SEQRES 6 A 296 GLY ILE PRO SER ILE LYS TRP CYS GLY ALA GLU GLY ASP
SEQRES 7 A 296 TYR ASN VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU
SEQRES 8 A 296 GLU ASP LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU
SEQRES 9 A 296 LYS THR VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG
SEQRES 10 A 296 ILE GLU TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP
SEQRES 11 A 296 VAL LYS PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS
SEQRES 12 A 296 GLY ASN LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS
SEQRES 13 A 296 LYS TYR ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR
SEQRES 14 A 296 ARG GLU ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA
SEQRES 15 A 296 SER ILE ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG
SEQRES 16 A 296 ASP ASP LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE
SEQRES 17 A 296 ASN LEU GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA
SEQRES 18 A 296 THR LYS ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS
SEQRES 19 A 296 MET SER THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO
SEQRES 20 A 296 SER GLU PHE SER THR TYR LEU ASN PHE CYS ARG SER LEU
SEQRES 21 A 296 ARG PHE ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN
SEQRES 22 A 296 LEU PHE ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR
SEQRES 23 A 296 ASP TYR VAL PHE ASP TRP ASN MET LEU LYS
SEQRES 1 B 296 GLY SER MET GLU LEU ARG VAL GLY ASN LYS TYR ARG LEU
SEQRES 2 B 296 GLY ARG LYS ILE GLY SER GLY SER PHE GLY ASP ILE TYR
SEQRES 3 B 296 LEU GLY ALA ASN ILE ALA SER GLY GLU GLU VAL ALA ILE
SEQRES 4 B 296 LYS LEU GLU CYS VAL LYS THR LYS HIS PRO GLN LEU HIS
SEQRES 5 B 296 ILE GLU SER LYS PHE TYR LYS MET MET GLN GLY GLY VAL
SEQRES 6 B 296 GLY ILE PRO SER ILE LYS TRP CYS GLY ALA GLU GLY ASP
SEQRES 7 B 296 TYR ASN VAL MET VAL MET GLU LEU LEU GLY PRO SER LEU
SEQRES 8 B 296 GLU ASP LEU PHE ASN PHE CYS SER ARG LYS PHE SER LEU
SEQRES 9 B 296 LYS THR VAL LEU LEU LEU ALA ASP GLN MET ILE SER ARG
SEQRES 10 B 296 ILE GLU TYR ILE HIS SER LYS ASN PHE ILE HIS ARG ASP
SEQRES 11 B 296 VAL LYS PRO ASP ASN PHE LEU MET GLY LEU GLY LYS LYS
SEQRES 12 B 296 GLY ASN LEU VAL TYR ILE ILE ASP PHE GLY LEU ALA LYS
SEQRES 13 B 296 LYS TYR ARG ASP ALA ARG THR HIS GLN HIS ILE PRO TYR
SEQRES 14 B 296 ARG GLU ASN LYS ASN LEU THR GLY THR ALA ARG TYR ALA
SEQRES 15 B 296 SER ILE ASN THR HIS LEU GLY ILE GLU GLN SER ARG ARG
SEQRES 16 B 296 ASP ASP LEU GLU SER LEU GLY TYR VAL LEU MET TYR PHE
SEQRES 17 B 296 ASN LEU GLY SER LEU PRO TRP GLN GLY LEU LYS ALA ALA
SEQRES 18 B 296 THR LYS ARG GLN LYS TYR GLU ARG ILE SER GLU LYS LYS
SEQRES 19 B 296 MET SER THR PRO ILE GLU VAL LEU CYS LYS GLY TYR PRO
SEQRES 20 B 296 SER GLU PHE SER THR TYR LEU ASN PHE CYS ARG SER LEU
SEQRES 21 B 296 ARG PHE ASP ASP LYS PRO ASP TYR SER TYR LEU ARG GLN
SEQRES 22 B 296 LEU PHE ARG ASN LEU PHE HIS ARG GLN GLY PHE SER TYR
SEQRES 23 B 296 ASP TYR VAL PHE ASP TRP ASN MET LEU LYS
HET 16W A 301 25
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HET 16W B 301 25
HET SO4 B 302 5
HET SO4 B 303 5
HET SO4 B 304 5
HET SO4 B 305 5
HETNAM 16W 3-[(3-CHLOROPHENOXY)METHYL]-1-(TETRAHYDRO-2H-PYRAN-4-
HETNAM 2 16W YL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-4-AMINE
HETNAM SO4 SULFATE ION
FORMUL 3 16W 2(C17 H18 CL N5 O2)
FORMUL 4 SO4 9(O4 S 2-)
FORMUL 14 HOH *63(H2 O)
HELIX 1 1 ILE A 51 LYS A 57 1 7
HELIX 2 2 SER A 88 CYS A 96 1 9
HELIX 3 3 SER A 101 SER A 121 1 21
HELIX 4 4 LYS A 130 ASP A 132 5 3
HELIX 5 5 LEU A 138 GLY A 142 5 5
HELIX 6 6 THR A 176 ALA A 180 5 5
HELIX 7 7 SER A 181 LEU A 186 1 6
HELIX 8 8 SER A 191 GLY A 209 1 19
HELIX 9 9 THR A 220 THR A 235 1 16
HELIX 10 10 PRO A 236 CYS A 241 1 6
HELIX 11 11 PRO A 245 ARG A 256 1 12
HELIX 12 12 ASP A 265 GLY A 281 1 17
HELIX 13 13 PHE A 288 MET A 292 5 5
HELIX 14 14 SER B 53 GLN B 60 1 8
HELIX 15 15 SER B 88 CYS B 96 1 9
HELIX 16 16 SER B 101 LYS B 122 1 22
HELIX 17 17 LYS B 130 ASP B 132 5 3
HELIX 18 18 LEU B 138 GLY B 142 5 5
HELIX 19 19 SER B 181 LEU B 186 1 6
HELIX 20 20 SER B 191 GLY B 209 1 19
HELIX 21 21 LYS B 221 THR B 235 1 15
HELIX 22 22 PRO B 236 CYS B 241 1 6
HELIX 23 23 SER B 246 SER B 257 1 12
HELIX 24 24 ASP B 265 GLY B 281 1 17
HELIX 25 25 PHE B 288 MET B 292 5 5
SHEET 1 A 4 ARG A 4 VAL A 5 0
SHEET 2 A 4 TYR A 9 ARG A 10 -1 O TYR A 9 N VAL A 5
SHEET 3 A 4 ASP A 22 ASN A 28 -1 O ALA A 27 N ARG A 10
SHEET 4 A 4 LYS A 14 GLY A 16 -1 N GLY A 16 O ILE A 23
SHEET 1 B 6 ARG A 4 VAL A 5 0
SHEET 2 B 6 TYR A 9 ARG A 10 -1 O TYR A 9 N VAL A 5
SHEET 3 B 6 ASP A 22 ASN A 28 -1 O ALA A 27 N ARG A 10
SHEET 4 B 6 VAL A 35 CYS A 41 -1 O ILE A 37 N TYR A 24
SHEET 5 B 6 TYR A 77 GLU A 83 -1 O ASN A 78 N GLU A 40
SHEET 6 B 6 ILE A 68 GLU A 74 -1 N LYS A 69 O VAL A 81
SHEET 1 C 2 PHE A 124 ILE A 125 0
SHEET 2 C 2 LYS A 154 LYS A 155 -1 O LYS A 154 N ILE A 125
SHEET 1 D 2 PHE A 134 MET A 136 0
SHEET 2 D 2 VAL A 145 ILE A 147 -1 O TYR A 146 N LEU A 135
SHEET 1 E 6 ARG B 4 VAL B 5 0
SHEET 2 E 6 TYR B 9 GLY B 18 -1 O TYR B 9 N VAL B 5
SHEET 3 E 6 GLY B 21 ASN B 28 -1 O ILE B 23 N ILE B 15
SHEET 4 E 6 GLU B 34 CYS B 41 -1 O VAL B 35 N GLY B 26
SHEET 5 E 6 TYR B 77 GLU B 83 -1 O MET B 82 N ALA B 36
SHEET 6 E 6 ILE B 68 GLU B 74 -1 N LYS B 69 O VAL B 81
SHEET 1 F 2 PHE B 124 ILE B 125 0
SHEET 2 F 2 LYS B 154 LYS B 155 -1 O LYS B 154 N ILE B 125
SHEET 1 G 2 PHE B 134 MET B 136 0
SHEET 2 G 2 VAL B 145 ILE B 147 -1 O TYR B 146 N LEU B 135
SITE 1 AC1 9 ILE A 15 ALA A 36 MET A 80 MET A 82
SITE 2 AC1 9 GLU A 83 LEU A 84 LEU A 85 ASP A 149
SITE 3 AC1 9 PHE A 150
SITE 1 AC2 3 ARG A 127 LYS A 154 LYS A 171
SITE 1 AC3 3 THR A 176 ALA A 177 TYR A 225
SITE 1 AC4 4 ARG A 157 ARG A 192 LYS A 263 LYS B 140
SITE 1 AC5 5 ARG A 178 GLN A 214 GLY A 215 LYS A 224
SITE 2 AC5 5 ILE A 228
SITE 1 AC6 3 LYS A 155 ASP A 158 ALA A 159
SITE 1 AC7 11 ARG A 13 ILE B 15 ALA B 36 LYS B 38
SITE 2 AC7 11 MET B 80 MET B 82 GLU B 83 LEU B 84
SITE 3 AC7 11 LEU B 85 LEU B 135 ASP B 149
SITE 1 AC8 5 ARG B 178 GLN B 214 GLY B 215 LYS B 224
SITE 2 AC8 5 ILE B 228
SITE 1 AC9 3 ARG B 127 LYS B 154 LYS B 171
SITE 1 BC1 4 LYS A 140 ARG B 157 ARG B 192 LYS B 263
SITE 1 BC2 2 THR B 176 ALA B 177
CRYST1 111.108 111.108 155.426 90.00 90.00 90.00 P 43 21 2 16
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 0.009000 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009000 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006434 0.00000
(ATOM LINES ARE NOT SHOWN.)
END