HEADER TRANSFERASE/TRANSFERASE INHIBITOR 02-JAN-12 3VBW
TITLE EXPLOITATION OF HYDROGEN BONDING CONSTRAINTS AND FLAT HYDROPHOBIC
TITLE 2 ENERGY LANDSCAPES IN PIM-1 KINASE NEEDLE SCREENING AND INHIBITOR
TITLE 3 DESIGN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PIM-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 120-404;
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: PIM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PIM1, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LIU
REVDAT 3 28-FEB-24 3VBW 1 REMARK SEQADV
REVDAT 2 16-MAY-12 3VBW 1 JRNL
REVDAT 1 21-MAR-12 3VBW 0
JRNL AUTH A.C.GOOD,J.LIU,B.HIRTH,G.ASMUSSEN,Y.XIANG,H.P.BIEMANN,
JRNL AUTH 2 K.A.BISHOP,T.FREMGEN,M.FITZGERALD,T.GLADYSHEVA,A.JAIN,
JRNL AUTH 3 K.JANCSICS,M.METZ,A.PAPOULIS,R.SKERLJ,J.D.STEPP,R.R.WEI
JRNL TITL IMPLICATIONS OF PROMISCUOUS PIM-1 KINASE FRAGMENT INHIBITOR
JRNL TITL 2 HYDROPHOBIC INTERACTIONS FOR FRAGMENT-BASED DRUG DESIGN.
JRNL REF J.MED.CHEM. V. 55 2641 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22339127
JRNL DOI 10.1021/JM2014698
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 84.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 14366
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.229
REMARK 3 FREE R VALUE : 0.299
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 757
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) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 797
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 54
REMARK 3 BIN FREE R VALUE : 0.3520
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2165
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 73
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.66000
REMARK 3 B22 (A**2) : 0.66000
REMARK 3 B33 (A**2) : -0.99000
REMARK 3 B12 (A**2) : 0.33000
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): 0.377
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.301
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.188
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.363
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2234 ; 0.017 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3030 ; 1.931 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 261 ; 6.797 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 116 ;36.299 ;23.103
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 375 ;16.680 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 21 ;23.257 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 325 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1728 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 35 A 305
REMARK 3 RESIDUE RANGE : A 1 A 1
REMARK 3 RESIDUE RANGE : A 2 A 27
REMARK 3 RESIDUE RANGE : A 327 A 375
REMARK 3 ORIGIN FOR THE GROUP (A): 31.0465 27.0644 0.4279
REMARK 3 T TENSOR
REMARK 3 T11: 0.0297 T22: 0.0237
REMARK 3 T33: 0.0219 T12: 0.0111
REMARK 3 T13: -0.0085 T23: 0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 1.4192 L22: 1.1386
REMARK 3 L33: 1.4480 L12: -0.2552
REMARK 3 L13: -0.4011 L23: -0.0999
REMARK 3 S TENSOR
REMARK 3 S11: -0.0341 S12: -0.0229 S13: 0.0189
REMARK 3 S21: -0.0378 S22: 0.0492 S23: 0.0251
REMARK 3 S31: 0.0162 S32: -0.1345 S33: -0.0151
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 USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3VBW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000069850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14366
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 84.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE, 1M NA ACETATE, PH 6.4,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 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 54.00000
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 27.00000
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 40.50000
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 13.50000
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 67.50000
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 28
REMARK 465 LYS A 29
REMARK 465 GLU A 30
REMARK 465 LYS A 31
REMARK 465 GLU A 32
REMARK 465 PRO A 33
REMARK 465 LEU A 34
REMARK 465 SER A 46
REMARK 465 GLY A 47
REMARK 465 GLY A 48
REMARK 465 PHE A 49
REMARK 465 PRO A 81
REMARK 465 ASN A 82
REMARK 465 GLY A 83
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 LYS A 313
REMARK 465 ALA A 314
REMARK 465 ALA A 315
REMARK 465 ALA A 316
REMARK 465 LEU A 317
REMARK 465 GLU A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
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 PRO A 241 O HOH A 359 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 HIS A 159 CG HIS A 159 CD2 0.054
REMARK 500 TRP A 212 CE2 TRP A 212 CD2 0.073
REMARK 500 HIS A 216 CG HIS A 216 CD2 0.061
REMARK 500 HIS A 219 CG HIS A 219 CD2 0.054
REMARK 500 HIS A 265 CG HIS A 265 CD2 0.058
REMARK 500 TRP A 269 CE2 TRP A 269 CD2 0.073
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 A 60 21.15 -146.16
REMARK 500 GLU A 79 -176.41 -175.61
REMARK 500 SER A 101 -161.85 -179.96
REMARK 500 GLU A 124 109.92 -163.29
REMARK 500 ARG A 166 -4.45 81.06
REMARK 500 ASP A 167 44.19 -140.14
REMARK 500 ASP A 186 79.40 67.98
REMARK 500 ASP A 202 33.12 -142.47
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 0FN A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VBQ RELATED DB: PDB
REMARK 900 RELATED ID: 3VBT RELATED DB: PDB
REMARK 900 RELATED ID: 3VBV RELATED DB: PDB
REMARK 900 RELATED ID: 3VBX RELATED DB: PDB
REMARK 900 RELATED ID: 3VBY RELATED DB: PDB
REMARK 900 RELATED ID: 3VC4 RELATED DB: PDB
DBREF 3VBW A 29 313 UNP P11309 PIM1_HUMAN 120 404
SEQADV 3VBW MET A 28 UNP P11309 INITIATING METHIONINE
SEQADV 3VBW ALA A 314 UNP P11309 EXPRESSION TAG
SEQADV 3VBW ALA A 315 UNP P11309 EXPRESSION TAG
SEQADV 3VBW ALA A 316 UNP P11309 EXPRESSION TAG
SEQADV 3VBW LEU A 317 UNP P11309 EXPRESSION TAG
SEQADV 3VBW GLU A 318 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 319 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 320 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 321 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 322 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 323 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 324 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 325 UNP P11309 EXPRESSION TAG
SEQADV 3VBW HIS A 326 UNP P11309 EXPRESSION TAG
SEQRES 1 A 299 MET LYS GLU LYS GLU PRO LEU GLU SER GLN TYR GLN VAL
SEQRES 2 A 299 GLY PRO LEU LEU GLY SER GLY GLY PHE GLY SER VAL TYR
SEQRES 3 A 299 SER GLY ILE ARG VAL SER ASP ASN LEU PRO VAL ALA ILE
SEQRES 4 A 299 LYS HIS VAL GLU LYS ASP ARG ILE SER ASP TRP GLY GLU
SEQRES 5 A 299 LEU PRO ASN GLY THR ARG VAL PRO MET GLU VAL VAL LEU
SEQRES 6 A 299 LEU LYS LYS VAL SER SER GLY PHE SER GLY VAL ILE ARG
SEQRES 7 A 299 LEU LEU ASP TRP PHE GLU ARG PRO ASP SER PHE VAL LEU
SEQRES 8 A 299 ILE LEU GLU ARG PRO GLU PRO VAL GLN ASP LEU PHE ASP
SEQRES 9 A 299 PHE ILE THR GLU ARG GLY ALA LEU GLN GLU GLU LEU ALA
SEQRES 10 A 299 ARG SER PHE PHE TRP GLN VAL LEU GLU ALA VAL ARG HIS
SEQRES 11 A 299 CYS HIS ASN CYS GLY VAL LEU HIS ARG ASP ILE LYS ASP
SEQRES 12 A 299 GLU ASN ILE LEU ILE ASP LEU ASN ARG GLY GLU LEU LYS
SEQRES 13 A 299 LEU ILE ASP PHE GLY SER GLY ALA LEU LEU LYS ASP THR
SEQRES 14 A 299 VAL TYR THR ASP PHE ASP GLY THR ARG VAL TYR SER PRO
SEQRES 15 A 299 PRO GLU TRP ILE ARG TYR HIS ARG TYR HIS GLY ARG SER
SEQRES 16 A 299 ALA ALA VAL TRP SER LEU GLY ILE LEU LEU TYR ASP MET
SEQRES 17 A 299 VAL CYS GLY ASP ILE PRO PHE GLU HIS ASP GLU GLU ILE
SEQRES 18 A 299 ILE ARG GLY GLN VAL PHE PHE ARG GLN ARG VAL SER SER
SEQRES 19 A 299 GLU CYS GLN HIS LEU ILE ARG TRP CYS LEU ALA LEU ARG
SEQRES 20 A 299 PRO SER ASP ARG PRO THR PHE GLU GLU ILE GLN ASN HIS
SEQRES 21 A 299 PRO TRP MET GLN ASP VAL LEU LEU PRO GLN GLU THR ALA
SEQRES 22 A 299 GLU ILE HIS LEU HIS SER LEU SER PRO GLY PRO SER LYS
SEQRES 23 A 299 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS
HET 0FN A 1 13
HETNAM 0FN 1,3-DIOXO-2,3-DIHYDRO-1H-INDENE-2-CARBONITRILE
FORMUL 2 0FN C10 H5 N O2
FORMUL 3 HOH *73(H2 O)
HELIX 1 1 ASP A 72 ILE A 74 5 3
HELIX 2 2 MET A 88 SER A 97 1 10
HELIX 3 3 LEU A 129 GLY A 137 1 9
HELIX 4 4 GLN A 140 CYS A 161 1 22
HELIX 5 5 LYS A 169 GLU A 171 5 3
HELIX 6 6 THR A 204 SER A 208 5 5
HELIX 7 7 PRO A 209 HIS A 216 1 8
HELIX 8 8 HIS A 219 GLY A 238 1 20
HELIX 9 9 HIS A 244 GLY A 251 1 8
HELIX 10 10 SER A 260 LEU A 271 1 12
HELIX 11 11 ARG A 274 ARG A 278 5 5
HELIX 12 12 THR A 280 ASN A 286 1 7
HELIX 13 13 HIS A 287 GLN A 291 5 5
HELIX 14 14 LEU A 295 LEU A 304 1 10
SHEET 1 A 5 TYR A 38 GLY A 45 0
SHEET 2 A 5 SER A 51 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 118 N LYS A 67
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 GLY A 78 0
SHEET 2 B 2 VAL A 86 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 LYS A 183 N LEU A 174
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 PHE A 100 SER A 101 0 -11.29
CISPEP 2 GLU A 124 PRO A 125 0 2.76
SITE 1 AC1 11 HOH A 21 LEU A 44 VAL A 52 ALA A 65
SITE 2 AC1 11 LYS A 67 ILE A 104 LEU A 120 GLU A 121
SITE 3 AC1 11 LEU A 174 ILE A 185 ASP A 186
CRYST1 97.000 97.000 81.000 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 0.010309 0.005952 0.000000 0.00000
SCALE2 0.000000 0.011904 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012346 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
