HEADER TRANSFERASE / TRANSFERASE INHIBITOR 04-SEP-09 3JPV
TITLE CRYSTAL STRUCTURE OF HUMAN PROTO-ONCOGENE SERINE THREONINE KINASE
TITLE 2 (PIM1) IN COMPLEX WITH A CONSENSUS PEPTIDE AND A PYRROLO[2,3-
TITLE 3 A]CARBAZOLE LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTO-ONCOGENE SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.11.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PEPTIDE (PIMTIDE) ARKRRRHPSGPPTA;
COMPND 8 CHAIN: B;
COMPND 9 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: PIM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS ONCOGENE, KINASE, SERINE-THREONINE, PIM1, PYRROLO[2, 3-A]CARBAZOLE,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC, ALTERNATIVE INITIATION, ATP-
KEYWDS 3 BINDING, CELL MEMBRANE, MANGANESE, MEMBRANE, METAL-BINDING,
KEYWDS 4 NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN, PROTO-ONCOGENE,
KEYWDS 5 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, TRANSFERASE -
KEYWDS 6 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,A.N.BULLOCK,O.FEDOROV,R.AKUE-GEDU,E.ROSSIGNOL,
AUTHOR 2 S.AZZARO,J.BAIN,P.COHEN,M.PRUDHOMME,P.MOREAU,F.AMIZON,F.VON DELFT,
AUTHOR 3 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,S.KNAPP,STRUCTURAL
AUTHOR 4 GENOMICS CONSORTIUM (SGC)
REVDAT 3 06-SEP-23 3JPV 1 REMARK DBREF
REVDAT 2 13-JUL-11 3JPV 1 VERSN
REVDAT 1 27-OCT-09 3JPV 0
JRNL AUTH R.AKUE-GEDU,E.ROSSIGNOL,S.AZZARO,S.KNAPP,P.FILIPPAKOPOULOS,
JRNL AUTH 2 A.N.BULLOCK,J.BAIN,P.COHEN,M.PRUDHOMME,F.ANIZON,P.MOREAU
JRNL TITL SYNTHESIS, KINASE INHIBITORY POTENCIES, AND IN VITRO
JRNL TITL 2 ANTIPROLIFERATIVE EVALUATION OF NEW PIM KINASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 52 6369 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 19788246
JRNL DOI 10.1021/JM901018F
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.58
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 18359
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.173
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 : 913
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1273
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.4190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2267
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 43.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -0.86000
REMARK 3 B12 (A**2) : 0.29000
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): 0.234
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.202
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.539
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2349 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 1636 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3188 ; 1.549 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3926 ; 0.914 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 278 ; 6.044 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 118 ;31.384 ;22.712
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 384 ;13.779 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;14.338 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 336 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2609 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 514 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1393 ; 3.779 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 566 ; 1.223 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2250 ; 5.274 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 956 ; 8.900 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 938 ;10.075 ;11.000
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 33 A 89
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3156 50.9767 7.2432
REMARK 3 T TENSOR
REMARK 3 T11: 0.1081 T22: 0.2866
REMARK 3 T33: 0.1640 T12: 0.0819
REMARK 3 T13: 0.0156 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 5.5190 L22: 5.6871
REMARK 3 L33: 5.0110 L12: 1.1059
REMARK 3 L13: 0.2355 L23: 1.1914
REMARK 3 S TENSOR
REMARK 3 S11: 0.0919 S12: -0.5215 S13: -0.0303
REMARK 3 S21: 0.4333 S22: -0.0449 S23: -0.2123
REMARK 3 S31: -0.0904 S32: 0.4285 S33: -0.0471
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 90 A 199
REMARK 3 ORIGIN FOR THE GROUP (A): 19.3118 53.6097 4.3653
REMARK 3 T TENSOR
REMARK 3 T11: 0.0955 T22: 0.0892
REMARK 3 T33: 0.0719 T12: 0.0343
REMARK 3 T13: 0.0189 T23: -0.0103
REMARK 3 L TENSOR
REMARK 3 L11: 2.1806 L22: 0.9433
REMARK 3 L33: 1.5606 L12: -0.0460
REMARK 3 L13: 0.5732 L23: 0.1018
REMARK 3 S TENSOR
REMARK 3 S11: 0.0275 S12: -0.1422 S13: -0.2436
REMARK 3 S21: 0.1179 S22: 0.0949 S23: -0.1114
REMARK 3 S31: 0.1835 S32: 0.2259 S33: -0.1224
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 200 A 305
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9489 64.2892 -4.0170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0499 T22: 0.0264
REMARK 3 T33: 0.0190 T12: 0.0082
REMARK 3 T13: 0.0014 T23: 0.0044
REMARK 3 L TENSOR
REMARK 3 L11: 2.6937 L22: 2.4378
REMARK 3 L33: 2.6338 L12: 0.5387
REMARK 3 L13: 0.2361 L23: 0.4469
REMARK 3 S TENSOR
REMARK 3 S11: -0.0549 S12: 0.0951 S13: 0.2132
REMARK 3 S21: -0.0805 S22: 0.0884 S23: 0.0493
REMARK 3 S31: -0.2430 S32: 0.0470 S33: -0.0336
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3JPV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1000055008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
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 FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18386
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 23.577
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.12700
REMARK 200 R SYM (I) : 0.12700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.76300
REMARK 200 R SYM FOR SHELL (I) : 0.76300
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 2.1.2
REMARK 200 STARTING MODEL: 2C3I
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.99
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NANO3 0.1M BTPROP PH 8.5 20%
REMARK 280 PEG3350 10% ETGLY, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
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 53.82867
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 26.91433
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 40.37150
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 13.45717
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 67.28583
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 SER A 0
REMARK 465 MET 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 SER A 306
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 ALA B -1
REMARK 465 ARG B 0
REMARK 465 GLY B 8
REMARK 465 PRO B 9
REMARK 465 PRO B 10
REMARK 465 THR B 11
REMARK 465 ALA B 12
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 35 CG CD OE1 OE2
REMARK 470 SER A 36 OG
REMARK 470 ILE A 56 CD1
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 ASN A 82 CG OD1 ND2
REMARK 470 THR A 84 OG1 CG2
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 ASP A 170 CB - CG - OD1 ANGL. DEV. = 6.4 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 61 13.92 58.08
REMARK 500 ASN A 82 41.28 -67.77
REMARK 500 SER A 101 -170.92 -178.25
REMARK 500 ASP A 167 47.46 -143.89
REMARK 500 ASP A 186 86.84 68.13
REMARK 500 LEU A 271 31.28 -98.62
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 1DR A 313
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHORS STATE THAT THE EXPRESSED PROTEIN HAS THE SEQUENCE FROM GI
REMARK 999 33304198 WHICH DIFFERS FROM GI 4505811 BY A SINGLE MUTATION R250G.
REMARK 999 AUTHORS CAN NO LONGER FIND GI|33304198 ON THE DATABASES. AUTHORS
REMARK 999 ARE NOT SURE IF THIS IS DUE TO POLYMORPHISM OR NOT. AUTHORS CONFIRM
REMARK 999 BY ESI THAT THE SEQUENCE WE HAVE CORRESPONDS TO THE R250G MUTANT
REMARK 999 AND ALSO IN OUR EXPERIMENTAL DENSITY WE SEE A G AND NOT A
REMARK 999 LARGERAMINOACID.
DBREF 3JPV A 1 312 UNP P11309 PIM1_HUMAN 92 403
DBREF 3JPV B -1 12 PDB 3JPV 3JPV -1 12
SEQADV 3JPV SER A 0 UNP P11309 EXPRESSION TAG
SEQADV 3JPV GLY A 250 UNP P11309 ARG 341 SEE REMARK 999
SEQRES 1 A 313 SER MET LEU LEU SER LYS ILE ASN SER LEU ALA HIS LEU
SEQRES 2 A 313 ARG ALA ALA PRO CYS ASN ASP LEU HIS ALA THR LYS LEU
SEQRES 3 A 313 ALA PRO GLY LYS GLU LYS GLU PRO LEU GLU SER GLN TYR
SEQRES 4 A 313 GLN VAL GLY PRO LEU LEU GLY SER GLY GLY PHE GLY SER
SEQRES 5 A 313 VAL TYR SER GLY ILE ARG VAL SER ASP ASN LEU PRO VAL
SEQRES 6 A 313 ALA ILE LYS HIS VAL GLU LYS ASP ARG ILE SER ASP TRP
SEQRES 7 A 313 GLY GLU LEU PRO ASN GLY THR ARG VAL PRO MET GLU VAL
SEQRES 8 A 313 VAL LEU LEU LYS LYS VAL SER SER GLY PHE SER GLY VAL
SEQRES 9 A 313 ILE ARG LEU LEU ASP TRP PHE GLU ARG PRO ASP SER PHE
SEQRES 10 A 313 VAL LEU ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP LEU
SEQRES 11 A 313 PHE ASP PHE ILE THR GLU ARG GLY ALA LEU GLN GLU GLU
SEQRES 12 A 313 LEU ALA ARG SER PHE PHE TRP GLN VAL LEU GLU ALA VAL
SEQRES 13 A 313 ARG HIS CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP ILE
SEQRES 14 A 313 LYS ASP GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY GLU
SEQRES 15 A 313 LEU LYS LEU ILE ASP PHE GLY SER GLY ALA LEU LEU LYS
SEQRES 16 A 313 ASP THR VAL TYR THR ASP PHE ASP GLY THR ARG VAL TYR
SEQRES 17 A 313 SER PRO PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS GLY
SEQRES 18 A 313 ARG SER ALA ALA VAL TRP SER LEU GLY ILE LEU LEU TYR
SEQRES 19 A 313 ASP MET VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP GLU
SEQRES 20 A 313 GLU ILE ILE GLY GLY GLN VAL PHE PHE ARG GLN ARG VAL
SEQRES 21 A 313 SER SER GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU ALA
SEQRES 22 A 313 LEU ARG PRO SER ASP ARG PRO THR PHE GLU GLU ILE GLN
SEQRES 23 A 313 ASN HIS PRO TRP MET GLN ASP VAL LEU LEU PRO GLN GLU
SEQRES 24 A 313 THR ALA GLU ILE HIS LEU HIS SER LEU SER PRO GLY PRO
SEQRES 25 A 313 SER
SEQRES 1 B 14 ALA ARG LYS ARG ARG ARG HIS PRO SER GLY PRO PRO THR
SEQRES 2 B 14 ALA
HET 1DR A 313 18
HETNAM 1DR 1,10-DIHYDROPYRROLO[2,3-A]CARBAZOLE-3-CARBALDEHYDE
FORMUL 3 1DR C15 H10 N2 O
FORMUL 4 HOH *161(H2 O)
HELIX 1 1 PRO A 33 GLN A 37 1 5
HELIX 2 2 ASP A 72 ILE A 74 5 3
HELIX 3 3 MET A 88 SER A 97 1 10
HELIX 4 4 LEU A 129 GLY A 137 1 9
HELIX 5 5 GLN A 140 CYS A 161 1 22
HELIX 6 6 LYS A 169 GLU A 171 5 3
HELIX 7 7 THR A 204 SER A 208 5 5
HELIX 8 8 PRO A 209 HIS A 216 1 8
HELIX 9 9 HIS A 219 GLY A 238 1 20
HELIX 10 10 HIS A 244 GLY A 251 1 8
HELIX 11 11 SER A 260 LEU A 271 1 12
HELIX 12 12 ARG A 274 ARG A 278 5 5
HELIX 13 13 THR A 280 HIS A 287 1 8
HELIX 14 14 PRO A 288 GLN A 291 5 4
HELIX 15 15 LEU A 295 LEU A 304 1 10
SHEET 1 A 5 TYR A 38 GLY A 47 0
SHEET 2 A 5 GLY A 50 ARG A 57 -1 O SER A 54 N GLY A 41
SHEET 3 A 5 PRO A 63 GLU A 70 -1 O VAL A 64 N GLY A 55
SHEET 4 A 5 SER A 115 GLU A 121 -1 O LEU A 120 N ALA A 65
SHEET 5 A 5 LEU A 106 GLU A 111 -1 N PHE A 110 O VAL A 117
SHEET 1 B 2 TRP A 77 GLU A 79 0
SHEET 2 B 2 ARG A 85 PRO A 87 -1 O VAL A 86 N GLY A 78
SHEET 1 C 3 VAL A 126 ASP A 128 0
SHEET 2 C 3 ILE A 173 ASP A 176 -1 O ILE A 175 N GLN A 127
SHEET 3 C 3 GLU A 181 LEU A 184 -1 O GLU A 181 N ASP A 176
SHEET 1 D 2 VAL A 163 LEU A 164 0
SHEET 2 D 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 -1.43
SITE 1 AC1 8 LEU A 44 PHE A 49 ALA A 65 LYS A 67
SITE 2 AC1 8 ARG A 122 LEU A 174 ILE A 185 ASP A 186
CRYST1 97.821 97.821 80.743 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 0.010223 0.005902 0.000000 0.00000
SCALE2 0.000000 0.011804 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012385 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
