HEADER TRANSFERASE 22-JAN-05 2BIK
TITLE HUMAN PIM1 PHOSPHORYLATED ON SER261
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: B;
COMPND 4 SYNONYM: PIM1;
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: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P11-TORONTO
KEYWDS KINASE, CANCER, LEUKEMIA, TRANSFERASE, ATP-BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR S.KNAPP,J.DEBRECZENI,A.BULLOCK,F.VON DELFT,M.SUNDSTROM,C.ARROWSMITH,
AUTHOR 2 A.EDWARDS,K.GUO
REVDAT 7 13-DEC-23 2BIK 1 REMARK
REVDAT 6 23-OCT-19 2BIK 1 SEQADV
REVDAT 5 08-MAY-19 2BIK 1 REMARK
REVDAT 4 06-MAR-19 2BIK 1 REMARK LINK
REVDAT 3 24-JAN-18 2BIK 1 AUTHOR JRNL
REVDAT 2 24-FEB-09 2BIK 1 VERSN
REVDAT 1 07-FEB-05 2BIK 0
JRNL AUTH S.KNAPP,J.DEBRECZENI,A.BULLOCK,F.VON DELFT,M.SUNDSTROM,
JRNL AUTH 2 C.ARROWSMITH,A.EDWARDS,K.GUO
JRNL TITL HUMAN PIM1 PHOSPHORYLATED ON SER261
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.07
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 39487
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.183
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2128
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2889
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2140
REMARK 3 BIN FREE R VALUE SET COUNT : 166
REMARK 3 BIN FREE R VALUE : 0.3010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2214
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.15000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : -0.23000
REMARK 3 B12 (A**2) : 0.08000
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): 0.115
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.029
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2354 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2146 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3204 ; 1.602 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4965 ; 0.818 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 272 ; 5.158 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 120 ;33.455 ;23.083
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 391 ;11.900 ;15.038
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;16.683 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 343 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2588 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 514 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 454 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2248 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1120 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1367 ; 0.078 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 223 ; 0.149 ; 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): 10 ; 0.225 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 44 ; 0.334 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 25 ; 0.262 ; 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): 1470 ; 2.522 ; 4.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2226 ; 3.298 ; 6.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1107 ; 5.166 ;10.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 978 ; 5.890 ;13.000
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 2BIK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1290022594.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41795
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 49.740
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.640
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.91
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.050
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 1XWS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA2SO4, 0.1 M BIS-TRIS-PROPANE
REMARK 280 PH 7.5, 20% PEG3350, 10% ETHYLENE-GLYCOL, 0.5% DMSO, SITTING
REMARK 280 DROP, VAPOR DIFFUSION, 277 K, VAPOR DIFFUSION, SITTING DROP
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 53.41533
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 26.70767
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 40.06150
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 13.35383
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 66.76917
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: PQS
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 MET B 1
REMARK 465 LEU B 2
REMARK 465 LEU B 3
REMARK 465 SER B 4
REMARK 465 LYS B 5
REMARK 465 ILE B 6
REMARK 465 ASN B 7
REMARK 465 SER B 8
REMARK 465 LEU B 9
REMARK 465 ALA B 10
REMARK 465 HIS B 11
REMARK 465 LEU B 12
REMARK 465 ARG B 13
REMARK 465 ALA B 14
REMARK 465 ALA B 15
REMARK 465 PRO B 16
REMARK 465 CYS B 17
REMARK 465 ASN B 18
REMARK 465 ASP B 19
REMARK 465 LEU B 20
REMARK 465 HIS B 21
REMARK 465 ALA B 22
REMARK 465 THR B 23
REMARK 465 LYS B 24
REMARK 465 LEU B 25
REMARK 465 ALA B 26
REMARK 465 PRO B 27
REMARK 465 GLY B 28
REMARK 465 LYS B 29
REMARK 465 GLU B 30
REMARK 465 LYS B 31
REMARK 465 GLU B 32
REMARK 465 SER B 306
REMARK 465 LEU B 307
REMARK 465 SER B 308
REMARK 465 PRO B 309
REMARK 465 GLY B 310
REMARK 465 PRO B 311
REMARK 465 SER B 312
REMARK 465 LYS B 313
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 B 79 CG CD OE1 OE2
REMARK 470 GLU B 243 CD OE1 OE2
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 O HOH B 2256 O HOH B 2257 2.08
REMARK 500 O HOH B 2239 O HOH B 2243 2.09
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 ASP B 60 18.95 -144.25
REMARK 500 ASP B 167 43.57 -145.22
REMARK 500 ASP B 186 82.30 65.31
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 CL B1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BI1 B1306
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: 2BIL RELATED DB: PDB
REMARK 900 HUMAN PIM1 WITH ITS CONSENSUS PEPTIDE PIMTIDE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE VARIANT DESCRIBED IN THE SEQADV RECORDS BELOW HAS NOT
REMARK 999 BEEN ANNOTATED IN THE UNIPROT SEQUENCE DATABASE ENTRY
REMARK 999 P11309. 261 SER IS PHOSPHORYLATED
DBREF 2BIK B 1 313 UNP P11309 PIM1_HUMAN 1 313
SEQADV 2BIK GLY B 250 UNP P11309 ARG 250 VARIANT
SEQRES 1 B 313 MET LEU LEU SER LYS ILE ASN SER LEU ALA HIS LEU ARG
SEQRES 2 B 313 ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS LEU ALA
SEQRES 3 B 313 PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN TYR GLN
SEQRES 4 B 313 VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY SER VAL
SEQRES 5 B 313 TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO VAL ALA
SEQRES 6 B 313 ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP TRP GLY
SEQRES 7 B 313 GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU VAL VAL
SEQRES 8 B 313 LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY VAL ILE
SEQRES 9 B 313 ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER PHE VAL
SEQRES 10 B 313 LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP LEU PHE
SEQRES 11 B 313 ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU GLU LEU
SEQRES 12 B 313 ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA VAL ARG
SEQRES 13 B 313 HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP ILE LYS
SEQRES 14 B 313 ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY GLU LEU
SEQRES 15 B 313 LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU LYS ASP
SEQRES 16 B 313 THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL TYR SER
SEQRES 17 B 313 PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS GLY ARG
SEQRES 18 B 313 SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU TYR ASP
SEQRES 19 B 313 MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP GLU GLU
SEQRES 20 B 313 ILE ILE GLY GLY GLN VAL PHE PHE ARG GLN ARG VAL SER
SEQRES 21 B 313 SEP GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU ALA LEU
SEQRES 22 B 313 ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE GLN ASN
SEQRES 23 B 313 HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN GLU THR
SEQRES 24 B 313 ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY PRO SER
SEQRES 25 B 313 LYS
MODRES 2BIK SEP B 261 SER PHOSPHOSERINE
HET SEP B 261 10
HET BI1 B1306 31
HET CL B1307 1
HET CL B1308 1
HETNAM SEP PHOSPHOSERINE
HETNAM BI1 3-{1-[3-(DIMETHYLAMINO)PROPYL]-1H-INDOL-3-YL}-4-(1H-
HETNAM 2 BI1 INDOL-3-YL)-1H-PYRROLE-2,5-DIONE
HETNAM CL CHLORIDE ION
HETSYN SEP PHOSPHONOSERINE
HETSYN BI1 RBT205 INHIBITOR
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 BI1 C25 H24 N4 O2
FORMUL 3 CL 2(CL 1-)
FORMUL 5 HOH *290(H2 O)
HELIX 1 1 PRO B 33 GLN B 37 1 5
HELIX 2 2 ASP B 72 ILE B 74 5 3
HELIX 3 3 MET B 88 SER B 97 1 10
HELIX 4 4 LEU B 129 GLY B 137 1 9
HELIX 5 5 GLN B 140 CYS B 161 1 22
HELIX 6 6 LYS B 169 GLU B 171 5 3
HELIX 7 7 THR B 204 SER B 208 5 5
HELIX 8 8 PRO B 209 HIS B 216 1 8
HELIX 9 9 HIS B 219 GLY B 238 1 20
HELIX 10 10 HIS B 244 GLY B 251 1 8
HELIX 11 11 SER B 260 LEU B 271 1 12
HELIX 12 12 ARG B 274 ARG B 278 5 5
HELIX 13 13 THR B 280 ASN B 286 1 7
HELIX 14 14 HIS B 287 GLN B 291 5 5
HELIX 15 15 LEU B 295 LEU B 304 1 10
SHEET 1 BA 5 TYR B 38 GLY B 47 0
SHEET 2 BA 5 GLY B 50 ARG B 57 -1 O GLY B 50 N GLY B 47
SHEET 3 BA 5 PRO B 63 GLU B 70 -1 O VAL B 64 N GLY B 55
SHEET 4 BA 5 SER B 115 GLU B 121 -1 O PHE B 116 N VAL B 69
SHEET 5 BA 5 LEU B 106 GLU B 111 -1 N LEU B 107 O ILE B 119
SHEET 1 BB 2 TRP B 77 GLU B 79 0
SHEET 2 BB 2 ARG B 85 PRO B 87 -1 O VAL B 86 N GLY B 78
SHEET 1 BC 3 VAL B 126 ASP B 128 0
SHEET 2 BC 3 ILE B 173 ASP B 176 -1 O ILE B 175 N GLN B 127
SHEET 3 BC 3 GLU B 181 LEU B 184 -1 O GLU B 181 N ASP B 176
SHEET 1 BD 2 VAL B 163 LEU B 164 0
SHEET 2 BD 2 ALA B 191 LEU B 192 -1 O ALA B 191 N LEU B 164
LINK C SER B 260 N SEP B 261 1555 1555 1.33
LINK C SEP B 261 N GLU B 262 1555 1555 1.33
CISPEP 1 GLU B 124 PRO B 125 0 -4.65
SITE 1 AC1 4 GLU B 70 ARG B 73 THR B 196 HOH B2017
SITE 1 AC2 7 GLU B 153 ARG B 156 GLN B 257 ARG B 258
SITE 2 AC2 7 VAL B 259 GLN B 264 HOH B2133
SITE 1 AC3 15 LEU B 44 GLY B 45 PHE B 49 VAL B 52
SITE 2 AC3 15 ALA B 65 ILE B 104 LEU B 120 GLU B 121
SITE 3 AC3 15 ARG B 122 GLU B 171 LEU B 174 ILE B 185
SITE 4 AC3 15 ASP B 186 HOH B2156 HOH B2290
CRYST1 99.321 99.321 80.123 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 0.010068 0.005813 0.000000 0.00000
SCALE2 0.000000 0.011626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012481 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
