HEADER TRANSFERASE 05-MAR-12 4ALU
TITLE BENZOFUROPYRIMIDINONE INHIBITORS OF PIM-1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PIM-1 KINASE;
COMPND 5 EC: 2.7.1.37, 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS PROTO-ONCOGENE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.STOUT,L.ADAMS
REVDAT 2 28-JUN-17 4ALU 1 REMARK
REVDAT 1 16-JAN-13 4ALU 0
JRNL AUTH A.L.TSUHAKO,D.S.BROWN,E.S.KOLTUN,N.AAY,A.ARCALAS,V.CHAN,
JRNL AUTH 2 H.DU,S.ENGST,M.FRANZINI,A.GALAN,P.HUANG,S.JOHNSTON,B.KANE,
JRNL AUTH 3 M.H.KIM,A.D.LAIRD,R.LIN,L.MOCK,I.NGAN,M.PACK,G.STOTT,
JRNL AUTH 4 T.J.STOUT,P.YU,C.ZAHARIA,W.ZHANG,P.ZHOU,J.M.NUSS,
JRNL AUTH 5 P.C.KEARNEY,W.XU
JRNL TITL THE DESIGN, SYNTHESIS, AND BIOLOGICAL EVALUATION OF PIM
JRNL TITL 2 KINASE INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 22 3732 2012
JRNL REFN ISSN 0960-894X
JRNL PMID 22542012
JRNL DOI 10.1016/J.BMCL.2012.04.025
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 12791
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 + TEST SET) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 679
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 946
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2225
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 91
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : 0.02000
REMARK 3 B33 (A**2) : -0.03000
REMARK 3 B12 (A**2) : 0.01000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.400
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.281
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.189
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.685
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.884
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2328 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3160 ; 1.780 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 7.252 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 119 ;33.440 ;23.109
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 388 ;18.053 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;21.187 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 334 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1806 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1144 ; 0.243 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1578 ; 0.337 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 128 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 30 ; 0.176 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 7 ; 0.201 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1392 ; 1.027 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2217 ; 1.805 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1104 ; 2.392 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 943 ; 3.797 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 4ALU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1290051565.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-06
REMARK 200 TEMPERATURE (KELVIN) : 155
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS-IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12791
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 26.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.160
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.15
REMARK 200 R MERGE FOR SHELL (I) : 0.22000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.250
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: IN-HOUSE STRUCTURE OF PIM1
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.2
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 54.03533
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 27.01767
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 40.52650
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 13.50883
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 67.54417
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 MET A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 GLY A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 GLY A 0
REMARK 465 SER A 1
REMARK 465 LEU A 2
REMARK 465 LEU A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 ILE A 6
REMARK 465 ASN A 7
REMARK 465 SER A 8
REMARK 465 LEU A 9
REMARK 465 ALA A 10
REMARK 465 HIS A 11
REMARK 465 LEU A 12
REMARK 465 ARG A 13
REMARK 465 ALA A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 CYS A 17
REMARK 465 ASN A 18
REMARK 465 ASP A 19
REMARK 465 LEU A 20
REMARK 465 HIS A 21
REMARK 465 ALA A 22
REMARK 465 THR A 23
REMARK 465 LYS A 24
REMARK 465 LEU A 25
REMARK 465 ALA A 26
REMARK 465 PRO A 27
REMARK 465 GLY A 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 LYS A 31
REMARK 465 GLU A 32
REMARK 465 LEU A 307
REMARK 465 SER A 308
REMARK 465 PRO A 309
REMARK 465 GLY A 310
REMARK 465 PRO A 311
REMARK 465 SER A 312
REMARK 465 LYS A 313
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 LEU A 34 152.19 93.64
REMARK 500 GLU A 35 44.40 -83.97
REMARK 500 ASP A 60 12.90 -148.89
REMARK 500 PRO A 81 37.69 -39.40
REMARK 500 ASN A 82 -26.26 -152.97
REMARK 500 SER A 98 -174.50 -172.42
REMARK 500 ARG A 166 -3.97 78.28
REMARK 500 ASP A 167 41.00 -141.80
REMARK 500 LYS A 169 161.45 179.44
REMARK 500 ASP A 186 87.87 71.61
REMARK 500 ASP A 202 41.36 -146.43
REMARK 500 HIS A 305 70.86 48.91
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 35 SER A 36 148.09
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 IMD A 1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 79O A 1308
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XQZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HPIM-1 KINASE AT 2.1 A RESOLUTION
REMARK 900 RELATED ID: 1XR1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HPIM-1 KINASE IN COMPLEX WITH AMP-PNPAT 2.1 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1XWS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN PIM1 KINASE DOMAIN
REMARK 900 RELATED ID: 1YHS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PIM-1 BOUND TO STAUROSPORINE
REMARK 900 RELATED ID: 1YI3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PIM-1 BOUND TO LY294002
REMARK 900 RELATED ID: 1YI4 RELATED DB: PDB
REMARK 900 STRUCTURE OF PIM-1 BOUND TO ADENOSINE
REMARK 900 RELATED ID: 1YWV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURES OF PROTO-ONCOGENE KINASE PIM1: A TARGETOF
REMARK 900 ABERRANT SOMATIC HYPERMUTATIONS IN DIFFUSE LARGE CELLLYMPHOMA
REMARK 900 RELATED ID: 1YXS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KINASE PIM1 WITH P123M MUTATION
REMARK 900 RELATED ID: 1YXT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH AMPPNP
REMARK 900 RELATED ID: 1YXU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH AMP
REMARK 900 RELATED ID: 1YXV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH 3,4 -DIHYDROXY-1-
REMARK 900 METHYLQUINOLIN-2(1H)-ONE
REMARK 900 RELATED ID: 1YXX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF KINASE PIM1 IN COMPLEX WITH (3E )-3-[(4-
REMARK 900 HYDROXYPHENYL)IMINO]-1H-INDOL-2(3H)-ONE
REMARK 900 RELATED ID: 2BIK RELATED DB: PDB
REMARK 900 HUMAN PIM1 PHOSPHORYLATED ON SER261
REMARK 900 RELATED ID: 2BIL RELATED DB: PDB
REMARK 900 THE HUMAN PROTEIN KINASE PIM1 IN COMPLEX WITH ITS CONSENSUS PEPTIDE
REMARK 900 PIMTIDE
REMARK 900 RELATED ID: 2BZH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH A RUTHENIUM
REMARK 900 ORGANOMETALLIC LIGAND RU1
REMARK 900 RELATED ID: 2BZI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH A RUTHENIUM
REMARK 900 ORGANOMETALLIC LIGAND RU2
REMARK 900 RELATED ID: 2BZJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH A RUTHENIUM
REMARK 900 ORGANOMETALLIC LIGAND RU3
REMARK 900 RELATED ID: 2BZK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN PIM1 IN COMPLEX WITH AMPPNP AND
REMARK 900 PIMTIDE
REMARK 900 RELATED ID: 2C3I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PIM1 IN COMPLEX WITH IMIDAZOPYRIDAZIN I
REMARK 900 RELATED ID: 2J2I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAB PIM1 IN COMPLEX WITH LY333531
REMARK 900 RELATED ID: 2XIX RELATED DB: PDB
REMARK 900 PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-1 FROM
REMARK 900 CRYSTALLOGRAPHIC FRAGMENT SCREEN
REMARK 900 RELATED ID: 2XIY RELATED DB: PDB
REMARK 900 PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-2 FROM
REMARK 900 CRYSTALLOGRAPHIC FRAGMENT SCREEN
REMARK 900 RELATED ID: 2XIZ RELATED DB: PDB
REMARK 900 PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-3 FROM
REMARK 900 CRYSTALLOGRAPHIC FRAGMENT SCREEN
REMARK 900 RELATED ID: 2XJ0 RELATED DB: PDB
REMARK 900 PROTEIN KINASE PIM-1 IN COMPLEX WITH FRAGMENT-4 FROM
REMARK 900 CRYSTALLOGRAPHIC FRAGMENT SCREEN
REMARK 900 RELATED ID: 2XJ1 RELATED DB: PDB
REMARK 900 PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INIBITOR
REMARK 900 RELATED ID: 2XJ2 RELATED DB: PDB
REMARK 900 PROTEIN KINASE PIM-1 IN COMPLEX WITH SMALL MOLECULE INHIBITOR
REMARK 900 RELATED ID: 4A7C RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PIM1 KINASE WITH ETP46546
REMARK 900 RELATED ID: 4ALV RELATED DB: PDB
REMARK 900 BENZOFUROPYRIMIDINONE INHIBITORS OF PIM-1
REMARK 900 RELATED ID: 4ALW RELATED DB: PDB
REMARK 900 BENZOFUROPYRIMIDINONE INHIBITORS OF PIM-1
DBREF 4ALU A 2 313 UNP P11309 PIM1_HUMAN 2 313
SEQADV 4ALU MET A -14 UNP P11309 EXPRESSION TAG
SEQADV 4ALU HIS A -13 UNP P11309 EXPRESSION TAG
SEQADV 4ALU HIS A -12 UNP P11309 EXPRESSION TAG
SEQADV 4ALU HIS A -11 UNP P11309 EXPRESSION TAG
SEQADV 4ALU HIS A -10 UNP P11309 EXPRESSION TAG
SEQADV 4ALU HIS A -9 UNP P11309 EXPRESSION TAG
SEQADV 4ALU HIS A -8 UNP P11309 EXPRESSION TAG
SEQADV 4ALU GLY A -7 UNP P11309 EXPRESSION TAG
SEQADV 4ALU GLU A -6 UNP P11309 EXPRESSION TAG
SEQADV 4ALU ASN A -5 UNP P11309 EXPRESSION TAG
SEQADV 4ALU LEU A -4 UNP P11309 EXPRESSION TAG
SEQADV 4ALU TYR A -3 UNP P11309 EXPRESSION TAG
SEQADV 4ALU PHE A -2 UNP P11309 EXPRESSION TAG
SEQADV 4ALU GLN A -1 UNP P11309 EXPRESSION TAG
SEQADV 4ALU GLY A 0 UNP P11309 EXPRESSION TAG
SEQADV 4ALU SER A 1 UNP P11309 EXPRESSION TAG
SEQADV 4ALU SER A 49 UNP P11309 PHE 49 CONFLICT
SEQRES 1 A 328 MET HIS HIS HIS HIS HIS HIS GLY GLU ASN LEU TYR PHE
SEQRES 2 A 328 GLN GLY SER LEU LEU SER LYS ILE ASN SER LEU ALA HIS
SEQRES 3 A 328 LEU ARG ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS
SEQRES 4 A 328 LEU ALA PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN
SEQRES 5 A 328 TYR GLN VAL GLY PRO LEU LEU GLY SER GLY GLY SER GLY
SEQRES 6 A 328 SER VAL TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO
SEQRES 7 A 328 VAL ALA ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP
SEQRES 8 A 328 TRP GLY GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU
SEQRES 9 A 328 VAL VAL LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY
SEQRES 10 A 328 VAL ILE ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER
SEQRES 11 A 328 PHE VAL LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP
SEQRES 12 A 328 LEU PHE ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU
SEQRES 13 A 328 GLU LEU ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA
SEQRES 14 A 328 VAL ARG HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP
SEQRES 15 A 328 ILE LYS ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY
SEQRES 16 A 328 GLU LEU LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU
SEQRES 17 A 328 LYS ASP THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL
SEQRES 18 A 328 TYR SER PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS
SEQRES 19 A 328 GLY ARG SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU
SEQRES 20 A 328 TYR ASP MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP
SEQRES 21 A 328 GLU GLU ILE ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG
SEQRES 22 A 328 VAL SER SER GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU
SEQRES 23 A 328 ALA LEU ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE
SEQRES 24 A 328 GLN ASN HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN
SEQRES 25 A 328 GLU THR ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY
SEQRES 26 A 328 PRO SER LYS
HET IMD A1307 5
HET 79O A1308 22
HETNAM IMD IMIDAZOLE
HETNAM 79O 8-BROMO-2-(2-CHLOROPHENYL)[1]BENZOFURO[3,2-D]PYRIMIDIN-
HETNAM 2 79O 4(3H)-ONE
FORMUL 2 IMD C3 H5 N2 1+
FORMUL 3 79O C16 H8 BR CL N2 O2
FORMUL 4 HOH *91(H2 O)
HELIX 1 1 MET A 88 SER A 97 1 10
HELIX 2 2 LEU A 129 GLY A 137 1 9
HELIX 3 3 GLN A 140 CYS A 161 1 22
HELIX 4 4 LYS A 169 GLU A 171 5 3
HELIX 5 5 THR A 204 SER A 208 5 5
HELIX 6 6 PRO A 209 HIS A 216 1 8
HELIX 7 7 HIS A 219 GLY A 238 1 20
HELIX 8 8 HIS A 244 GLY A 251 1 8
HELIX 9 9 SER A 260 LEU A 271 1 12
HELIX 10 10 ARG A 274 ARG A 278 5 5
HELIX 11 11 THR A 280 ASN A 286 1 7
HELIX 12 12 HIS A 287 GLN A 291 5 5
HELIX 13 13 LEU A 295 LEU A 304 1 10
SHEET 1 AA 5 LEU A 43 SER A 46 0
SHEET 2 AA 5 SER A 51 ILE A 56 -1 O VAL A 52 N LEU A 44
SHEET 3 AA 5 PRO A 63 GLU A 70 -1 O VAL A 64 N GLY A 55
SHEET 4 AA 5 SER A 115 GLU A 121 -1 O PHE A 116 N VAL A 69
SHEET 5 AA 5 LEU A 106 GLU A 111 -1 N LEU A 107 O ILE A 119
SHEET 1 AB 2 TRP A 77 GLU A 79 0
SHEET 2 AB 2 ARG A 85 PRO A 87 -1 O VAL A 86 N GLY A 78
SHEET 1 AC 3 VAL A 126 ASP A 128 0
SHEET 2 AC 3 ILE A 173 ASP A 176 -1 O ILE A 175 N GLN A 127
SHEET 3 AC 3 GLU A 181 LEU A 184 -1 O GLU A 181 N ASP A 176
SHEET 1 AD 2 VAL A 163 LEU A 164 0
SHEET 2 AD 2 ALA A 191 LEU A 192 -1 O ALA A 191 N LEU A 164
CISPEP 1 GLU A 124 PRO A 125 0 -6.21
SITE 1 AC1 7 PHE A 130 ILE A 133 THR A 134 ASP A 170
SITE 2 AC1 7 ASP A 234 GLY A 238 ASP A 239
SITE 1 AC2 12 GLY A 45 SER A 46 SER A 49 VAL A 52
SITE 2 AC2 12 ALA A 65 LYS A 67 GLU A 121 LEU A 174
SITE 3 AC2 12 ILE A 185 ASP A 186 HOH A2050 HOH A2091
CRYST1 97.162 97.162 81.053 90.00 90.00 120.00 P 65 6
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 0.010292 0.005942 0.000000 0.00000
SCALE2 0.000000 0.011884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012338 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
