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Original site: 5F9E
Chemical substance (2) PDB-CCD (2) Chemical reaction (1) KEGG ENZYME (1) Gene (1) KEGG GENES (1) Protein sequence (4) UniProt (1) SWISS-PROT (1) PDBSTR (2) DNA sequence (2) EMBL (2) Protein domain (12) InterPro (8) PROSITE (4) Literature (1) PubMed (1) All databases (23)
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HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-DEC-15 5F9E
TITLE STRUCTURE OF PROTEIN KINASE C THETA WITH COMPOUND 10: 2,2-DIMETHYL-7-
TITLE 2 (2-OXIDANYLIDENE-3~{H}-IMIDAZO[4,5-B]PYRIDIN-1-YL)-1-(PHENYLMETHYL)-
TITLE 3 3~{H}-QUINAZOLIN-4-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE C THETA TYPE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: NPKC-THETA;
COMPND 5 EC: 2.7.11.13;
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: PRKCQ, PRKCT;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS KINASE, INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KLEIN
REVDAT 1 11-MAY-16 5F9E 0
JRNL AUTH T.KATOH,T.TAKAI,T.YUKAWA,T.TSUKAMOTO,E.WATANABE,H.MOTOTANI,
JRNL AUTH 2 T.ARITA,H.HAYASHI,H.NAKAGAWA,M.G.KLEIN,H.ZOU,B.C.SANG,
JRNL AUTH 3 G.SNELL,Y.NAKADA
JRNL TITL DISCOVERY AND OPTIMIZATION OF
JRNL TITL 2 1,7-DISUBSTITUTED-2,2-DIMETHYL-2,3-DIHYDROQUINAZOLIN-4(1H)
JRNL TITL 3 -ONES AS POTENT AND SELECTIVE PKC THETA INHIBITORS.
JRNL REF BIOORG.MED.CHEM. V. 24 2466 2016
JRNL REFN ESSN 1464-3391
JRNL PMID 27117263
JRNL DOI 10.1016/J.BMC.2016.04.008
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0025
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 54956
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2929
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3328
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 82.17
REMARK 3 BIN R VALUE (WORKING SET) : 0.2990
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.3470
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5248
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 164
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 54.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.74000
REMARK 3 B22 (A**2) : -1.84000
REMARK 3 B33 (A**2) : -0.90000
REMARK 3 B12 (A**2) : 0.00000
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): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.108
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.979
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5499 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5180 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7417 ; 1.422 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11958 ; 0.784 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 641 ; 6.264 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 279 ;34.549 ;24.014
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1007 ;16.338 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;18.334 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 753 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6122 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1324 ; 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): 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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 374 A 709
REMARK 3 RESIDUE RANGE : A 1001 A 1001
REMARK 3 ORIGIN FOR THE GROUP (A): 32.6740 74.9240 30.2966
REMARK 3 T TENSOR
REMARK 3 T11: 0.1516 T22: 0.0199
REMARK 3 T33: 0.0934 T12: 0.0040
REMARK 3 T13: -0.0064 T23: 0.0192
REMARK 3 L TENSOR
REMARK 3 L11: 1.3098 L22: 1.7655
REMARK 3 L33: 1.6686 L12: 0.4868
REMARK 3 L13: -0.1754 L23: -0.0871
REMARK 3 S TENSOR
REMARK 3 S11: 0.0537 S12: 0.0250 S13: 0.0296
REMARK 3 S21: -0.1174 S22: -0.0178 S23: 0.1679
REMARK 3 S31: 0.0360 S32: -0.1571 S33: -0.0358
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 375 B 700
REMARK 3 RESIDUE RANGE : B 1001 B 1001
REMARK 3 ORIGIN FOR THE GROUP (A): 29.7446 84.1102 -8.8861
REMARK 3 T TENSOR
REMARK 3 T11: 0.2372 T22: 0.3061
REMARK 3 T33: 0.2570 T12: 0.1107
REMARK 3 T13: -0.0996 T23: 0.0356
REMARK 3 L TENSOR
REMARK 3 L11: 1.1108 L22: 2.9367
REMARK 3 L33: 2.9342 L12: -0.3965
REMARK 3 L13: 0.4318 L23: -1.0389
REMARK 3 S TENSOR
REMARK 3 S11: 0.0503 S12: 0.0362 S13: -0.0588
REMARK 3 S21: 0.0633 S22: -0.1405 S23: -0.4380
REMARK 3 S31: 0.4183 S32: 0.3618 S33: 0.0901
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
REMARK 4
REMARK 4 5F9E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216138.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59517
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.5000
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7, 0.2M LITHIUM CITRATE,
REMARK 280 AND 18% PEG M.W. 3,350, 1% HEXANEDIOL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 37.80150
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 74.65200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.39300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 74.65200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.80150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.39300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 MET A 360
REMARK 465 GLU A 361
REMARK 465 PRO A 362
REMARK 465 GLU A 363
REMARK 465 LEU A 364
REMARK 465 ASN A 365
REMARK 465 LYS A 366
REMARK 465 GLU A 367
REMARK 465 ARG A 368
REMARK 465 PRO A 369
REMARK 465 SER A 370
REMARK 465 LEU A 371
REMARK 465 GLN A 372
REMARK 465 ILE A 373
REMARK 465 HIS A 710
REMARK 465 HIS A 711
REMARK 465 HIS A 712
REMARK 465 MET B 360
REMARK 465 GLU B 361
REMARK 465 PRO B 362
REMARK 465 GLU B 363
REMARK 465 LEU B 364
REMARK 465 ASN B 365
REMARK 465 LYS B 366
REMARK 465 GLU B 367
REMARK 465 ARG B 368
REMARK 465 PRO B 369
REMARK 465 SER B 370
REMARK 465 LEU B 371
REMARK 465 GLN B 372
REMARK 465 ILE B 373
REMARK 465 LYS B 374
REMARK 465 SER B 657
REMARK 465 PRO B 658
REMARK 465 PHE B 659
REMARK 465 ASP B 660
REMARK 465 CYS B 661
REMARK 465 SER B 662
REMARK 465 ASN B 663
REMARK 465 PHE B 664
REMARK 465 ASP B 665
REMARK 465 LYS B 666
REMARK 465 GLU B 667
REMARK 465 PHE B 668
REMARK 465 LEU B 669
REMARK 465 ASN B 670
REMARK 465 GLU B 671
REMARK 465 LYS B 672
REMARK 465 PRO B 673
REMARK 465 ARG B 674
REMARK 465 LEU B 675
REMARK 465 SEP B 676
REMARK 465 PHE B 677
REMARK 465 ALA B 678
REMARK 465 ASP B 679
REMARK 465 ARG B 680
REMARK 465 ALA B 681
REMARK 465 LEU B 682
REMARK 465 ILE B 683
REMARK 465 ASN B 684
REMARK 465 SER B 685
REMARK 465 MET B 686
REMARK 465 ASP B 687
REMARK 465 GLN B 688
REMARK 465 MET B 701
REMARK 465 GLU B 702
REMARK 465 ARG B 703
REMARK 465 LEU B 704
REMARK 465 ILE B 705
REMARK 465 SER B 706
REMARK 465 HIS B 707
REMARK 465 HIS B 708
REMARK 465 HIS B 709
REMARK 465 HIS B 710
REMARK 465 HIS B 711
REMARK 465 HIS B 712
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 LYS A 400 -133.99 42.42
REMARK 500 THR A 402 166.01 -48.69
REMARK 500 ASN A 403 30.86 -90.86
REMARK 500 HIS A 474 -46.17 74.61
REMARK 500 ARG A 503 -5.11 73.24
REMARK 500 ASP A 522 90.67 72.18
REMARK 500 ASN A 537 17.26 -140.77
REMARK 500 ASN A 557 -150.69 -125.13
REMARK 500 PHE A 614 45.15 -89.66
REMARK 500 ASN A 689 -19.58 -45.03
REMARK 500 LYS B 400 -57.58 78.79
REMARK 500 LYS B 401 -79.60 -66.56
REMARK 500 HIS B 474 -55.55 70.97
REMARK 500 ARG B 503 -7.56 71.76
REMARK 500 ASP B 522 88.94 62.54
REMARK 500 ASN B 537 21.83 -145.44
REMARK 500 CYS B 540 135.47 -170.19
REMARK 500 ASN B 557 -153.91 -123.77
REMARK 500 PHE B 614 39.31 -81.90
REMARK 500 MET B 690 33.94 -86.26
REMARK 500 PHE B 691 42.11 -106.77
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 PHE B 539 CYS B 540 -147.91
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 5VS A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5VS B 1001
DBREF 5F9E A 361 706 UNP Q04759 KPCT_HUMAN 361 706
DBREF 5F9E B 361 706 UNP Q04759 KPCT_HUMAN 361 706
SEQADV 5F9E MET A 360 UNP Q04759 INITIATING METHIONINE
SEQADV 5F9E GLU A 381 UNP Q04759 ILE 381 CONFLICT
SEQADV 5F9E GLU A 538 UNP Q04759 THR 538 CONFLICT
SEQADV 5F9E HIS A 707 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS A 708 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS A 709 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS A 710 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS A 711 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS A 712 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E MET B 360 UNP Q04759 INITIATING METHIONINE
SEQADV 5F9E GLU B 381 UNP Q04759 ILE 381 CONFLICT
SEQADV 5F9E GLU B 538 UNP Q04759 THR 538 CONFLICT
SEQADV 5F9E HIS B 707 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS B 708 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS B 709 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS B 710 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS B 711 UNP Q04759 EXPRESSION TAG
SEQADV 5F9E HIS B 712 UNP Q04759 EXPRESSION TAG
SEQRES 1 A 353 MET GLU PRO GLU LEU ASN LYS GLU ARG PRO SER LEU GLN
SEQRES 2 A 353 ILE LYS LEU LYS ILE GLU ASP PHE GLU LEU HIS LYS MET
SEQRES 3 A 353 LEU GLY LYS GLY SER PHE GLY LYS VAL PHE LEU ALA GLU
SEQRES 4 A 353 PHE LYS LYS THR ASN GLN PHE PHE ALA ILE LYS ALA LEU
SEQRES 5 A 353 LYS LYS ASP VAL VAL LEU MET ASP ASP ASP VAL GLU CYS
SEQRES 6 A 353 THR MET VAL GLU LYS ARG VAL LEU SER LEU ALA TRP GLU
SEQRES 7 A 353 HIS PRO PHE LEU THR HIS MET PHE CYS THR PHE GLN THR
SEQRES 8 A 353 LYS GLU ASN LEU PHE PHE VAL MET GLU TYR LEU ASN GLY
SEQRES 9 A 353 GLY ASP LEU MET TYR HIS ILE GLN SER CYS HIS LYS PHE
SEQRES 10 A 353 ASP LEU SER ARG ALA THR PHE TYR ALA ALA GLU ILE ILE
SEQRES 11 A 353 LEU GLY LEU GLN PHE LEU HIS SER LYS GLY ILE VAL TYR
SEQRES 12 A 353 ARG ASP LEU LYS LEU ASP ASN ILE LEU LEU ASP LYS ASP
SEQRES 13 A 353 GLY HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS GLU
SEQRES 14 A 353 ASN MET LEU GLY ASP ALA LYS THR ASN GLU PHE CYS GLY
SEQRES 15 A 353 THR PRO ASP TYR ILE ALA PRO GLU ILE LEU LEU GLY GLN
SEQRES 16 A 353 LYS TYR ASN HIS SER VAL ASP TRP TRP SER PHE GLY VAL
SEQRES 17 A 353 LEU LEU TYR GLU MET LEU ILE GLY GLN SER PRO PHE HIS
SEQRES 18 A 353 GLY GLN ASP GLU GLU GLU LEU PHE HIS SER ILE ARG MET
SEQRES 19 A 353 ASP ASN PRO PHE TYR PRO ARG TRP LEU GLU LYS GLU ALA
SEQRES 20 A 353 LYS ASP LEU LEU VAL LYS LEU PHE VAL ARG GLU PRO GLU
SEQRES 21 A 353 LYS ARG LEU GLY VAL ARG GLY ASP ILE ARG GLN HIS PRO
SEQRES 22 A 353 LEU PHE ARG GLU ILE ASN TRP GLU GLU LEU GLU ARG LYS
SEQRES 23 A 353 GLU ILE ASP PRO PRO PHE ARG PRO LYS VAL LYS SER PRO
SEQRES 24 A 353 PHE ASP CYS SER ASN PHE ASP LYS GLU PHE LEU ASN GLU
SEQRES 25 A 353 LYS PRO ARG LEU SEP PHE ALA ASP ARG ALA LEU ILE ASN
SEQRES 26 A 353 SER MET ASP GLN ASN MET PHE ARG ASN PHE SEP PHE MET
SEQRES 27 A 353 ASN PRO GLY MET GLU ARG LEU ILE SER HIS HIS HIS HIS
SEQRES 28 A 353 HIS HIS
SEQRES 1 B 353 MET GLU PRO GLU LEU ASN LYS GLU ARG PRO SER LEU GLN
SEQRES 2 B 353 ILE LYS LEU LYS ILE GLU ASP PHE GLU LEU HIS LYS MET
SEQRES 3 B 353 LEU GLY LYS GLY SER PHE GLY LYS VAL PHE LEU ALA GLU
SEQRES 4 B 353 PHE LYS LYS THR ASN GLN PHE PHE ALA ILE LYS ALA LEU
SEQRES 5 B 353 LYS LYS ASP VAL VAL LEU MET ASP ASP ASP VAL GLU CYS
SEQRES 6 B 353 THR MET VAL GLU LYS ARG VAL LEU SER LEU ALA TRP GLU
SEQRES 7 B 353 HIS PRO PHE LEU THR HIS MET PHE CYS THR PHE GLN THR
SEQRES 8 B 353 LYS GLU ASN LEU PHE PHE VAL MET GLU TYR LEU ASN GLY
SEQRES 9 B 353 GLY ASP LEU MET TYR HIS ILE GLN SER CYS HIS LYS PHE
SEQRES 10 B 353 ASP LEU SER ARG ALA THR PHE TYR ALA ALA GLU ILE ILE
SEQRES 11 B 353 LEU GLY LEU GLN PHE LEU HIS SER LYS GLY ILE VAL TYR
SEQRES 12 B 353 ARG ASP LEU LYS LEU ASP ASN ILE LEU LEU ASP LYS ASP
SEQRES 13 B 353 GLY HIS ILE LYS ILE ALA ASP PHE GLY MET CYS LYS GLU
SEQRES 14 B 353 ASN MET LEU GLY ASP ALA LYS THR ASN GLU PHE CYS GLY
SEQRES 15 B 353 THR PRO ASP TYR ILE ALA PRO GLU ILE LEU LEU GLY GLN
SEQRES 16 B 353 LYS TYR ASN HIS SER VAL ASP TRP TRP SER PHE GLY VAL
SEQRES 17 B 353 LEU LEU TYR GLU MET LEU ILE GLY GLN SER PRO PHE HIS
SEQRES 18 B 353 GLY GLN ASP GLU GLU GLU LEU PHE HIS SER ILE ARG MET
SEQRES 19 B 353 ASP ASN PRO PHE TYR PRO ARG TRP LEU GLU LYS GLU ALA
SEQRES 20 B 353 LYS ASP LEU LEU VAL LYS LEU PHE VAL ARG GLU PRO GLU
SEQRES 21 B 353 LYS ARG LEU GLY VAL ARG GLY ASP ILE ARG GLN HIS PRO
SEQRES 22 B 353 LEU PHE ARG GLU ILE ASN TRP GLU GLU LEU GLU ARG LYS
SEQRES 23 B 353 GLU ILE ASP PRO PRO PHE ARG PRO LYS VAL LYS SER PRO
SEQRES 24 B 353 PHE ASP CYS SER ASN PHE ASP LYS GLU PHE LEU ASN GLU
SEQRES 25 B 353 LYS PRO ARG LEU SEP PHE ALA ASP ARG ALA LEU ILE ASN
SEQRES 26 B 353 SER MET ASP GLN ASN MET PHE ARG ASN PHE SEP PHE MET
SEQRES 27 B 353 ASN PRO GLY MET GLU ARG LEU ILE SER HIS HIS HIS HIS
SEQRES 28 B 353 HIS HIS
MODRES 5F9E SEP A 676 SER MODIFIED RESIDUE
MODRES 5F9E SEP A 695 SER MODIFIED RESIDUE
MODRES 5F9E SEP B 695 SER MODIFIED RESIDUE
HET SEP A 676 10
HET SEP A 695 10
HET SEP B 695 10
HET 5VS A1001 30
HET 5VS B1001 30
HETNAM SEP PHOSPHOSERINE
HETNAM 5VS 2,2-DIMETHYL-7-(2-OXIDANYLIDENE-3~{H}-IMIDAZO[4,5-
HETNAM 2 5VS B]PYRIDIN-1-YL)-1-(PHENYLMETHYL)-3~{H}-QUINAZOLIN-4-
HETNAM 3 5VS ONE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP 3(C3 H8 N O6 P)
FORMUL 3 5VS 2(C23 H21 N5 O2)
FORMUL 5 HOH *164(H2 O)
HELIX 1 AA1 LYS A 376 GLU A 378 5 3
HELIX 2 AA2 LYS A 413 ASP A 419 1 7
HELIX 3 AA3 ASP A 421 TRP A 436 1 16
HELIX 4 AA4 LEU A 466 HIS A 474 1 9
HELIX 5 AA5 ASP A 477 LYS A 498 1 22
HELIX 6 AA6 LYS A 506 ASP A 508 5 3
HELIX 7 AA7 THR A 542 ILE A 546 5 5
HELIX 8 AA8 ALA A 547 LEU A 552 1 6
HELIX 9 AA9 HIS A 558 GLY A 575 1 18
HELIX 10 AB1 ASP A 583 ASP A 594 1 12
HELIX 11 AB2 GLU A 603 PHE A 614 1 12
HELIX 12 AB3 GLU A 617 ARG A 621 5 5
HELIX 13 AB4 ASP A 627 ARG A 635 5 9
HELIX 14 AB5 ASN A 638 ARG A 644 1 7
HELIX 15 AB6 ASP A 665 ASN A 670 1 6
HELIX 16 AB7 ASP A 679 MET A 686 1 8
HELIX 17 AB8 ASP A 687 ARG A 692 5 6
HELIX 18 AB9 ASN A 698 HIS A 708 1 11
HELIX 19 AC1 LYS B 376 PHE B 380 5 5
HELIX 20 AC2 LYS B 413 ASP B 419 1 7
HELIX 21 AC3 ASP B 421 TRP B 436 1 16
HELIX 22 AC4 ASP B 465 HIS B 474 1 10
HELIX 23 AC5 ASP B 477 LYS B 498 1 22
HELIX 24 AC6 LYS B 506 ASP B 508 5 3
HELIX 25 AC7 THR B 542 ILE B 546 5 5
HELIX 26 AC8 ALA B 547 LEU B 552 1 6
HELIX 27 AC9 HIS B 558 GLY B 575 1 18
HELIX 28 AD1 ASP B 583 ASP B 594 1 12
HELIX 29 AD2 GLU B 603 PHE B 614 1 12
HELIX 30 AD3 GLU B 617 ARG B 621 5 5
HELIX 31 AD4 ASP B 627 ARG B 635 5 9
HELIX 32 AD5 ASN B 638 ARG B 644 1 7
SHEET 1 AA1 6 PHE A 380 GLY A 389 0
SHEET 2 AA1 6 GLY A 392 PHE A 399 -1 O VAL A 394 N GLY A 387
SHEET 3 AA1 6 PHE A 405 LYS A 412 -1 O ALA A 410 N LYS A 393
SHEET 4 AA1 6 ASN A 453 GLU A 459 -1 O MET A 458 N ALA A 407
SHEET 5 AA1 6 MET A 444 GLN A 449 -1 N CYS A 446 O VAL A 457
SHEET 6 AA1 6 PHE A 696 MET A 697 -1 O PHE A 696 N THR A 447
SHEET 1 AA2 3 GLY A 464 ASP A 465 0
SHEET 2 AA2 3 ILE A 510 LEU A 512 -1 O LEU A 512 N GLY A 464
SHEET 3 AA2 3 ILE A 518 ILE A 520 -1 O LYS A 519 N LEU A 511
SHEET 1 AA3 6 GLU B 381 GLY B 389 0
SHEET 2 AA3 6 GLY B 392 GLU B 398 -1 O LEU B 396 N HIS B 383
SHEET 3 AA3 6 PHE B 405 LYS B 412 -1 O ALA B 410 N LYS B 393
SHEET 4 AA3 6 ASN B 453 MET B 458 -1 O MET B 458 N ALA B 407
SHEET 5 AA3 6 MET B 444 GLN B 449 -1 N CYS B 446 O VAL B 457
SHEET 6 AA3 6 PHE B 696 MET B 697 -1 O PHE B 696 N THR B 447
SHEET 1 AA4 2 ILE B 510 LEU B 512 0
SHEET 2 AA4 2 ILE B 518 ILE B 520 -1 O LYS B 519 N LEU B 511
LINK C LEU A 675 N SEP A 676 1555 1555 1.32
LINK C SEP A 676 N PHE A 677 1555 1555 1.32
LINK C PHE A 694 N SEP A 695 1555 1555 1.33
LINK C SEP A 695 N PHE A 696 1555 1555 1.32
LINK C PHE B 694 N SEP B 695 1555 1555 1.33
LINK C SEP B 695 N PHE B 696 1555 1555 1.33
SITE 1 AC1 14 LEU A 386 GLY A 387 PHE A 391 VAL A 394
SITE 2 AC1 14 ALA A 407 LYS A 409 THR A 442 MET A 458
SITE 3 AC1 14 GLU A 459 LEU A 461 ASN A 509 LEU A 511
SITE 4 AC1 14 ASP A 522 PHE A 664
SITE 1 AC2 9 LEU B 386 PHE B 391 ALA B 407 LYS B 409
SITE 2 AC2 9 THR B 442 MET B 458 GLU B 459 LEU B 461
SITE 3 AC2 9 ASN B 509
CRYST1 75.603 76.786 149.304 90.00 90.00 90.00 P 21 21 21 8
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 0.013227 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013023 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006698 0.00000
(ATOM LINES ARE NOT SHOWN.)
END