HEADER TRANSFERASE 04-AUG-03 1Q4K
TITLE THE POLO-BOX DOMAIN OF PLK1 IN COMPLEX WITH A PHOSPHO-
TITLE 2 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK;
COMPND 3 CHAIN: B, A, C;
COMPND 4 FRAGMENT: POLO BOX DOMAIN OF HUMAN PLK1;
COMPND 5 SYNONYM: PLK-1, SERINE-THREONINE PROTEIN KINASE 13, STPK13;
COMPND 6 EC: 2.7.1.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: PHOSPHO-PEPTIDE SEQUENCE
COMPND 11 MET.GLN.SER.PTHR.PRO.LEU;
COMPND 12 CHAIN: D, E, F;
COMPND 13 FRAGMENT: PHOSPHO-PEPTIDE;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PLK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834 (DE3) PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P1;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: CHEMICAL SYNTHESIS
KEYWDS SIX-STRANDED ANTI-PARALLEL BETA SHEET WITH ONE ALPHA HELIX,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.CHENG,E.D.LOWE,J.SINCLAIR,E.A.NIGG,L.N.JOHNSON
REVDAT 2 24-FEB-09 1Q4K 1 VERSN
REVDAT 1 11-NOV-03 1Q4K 0
JRNL AUTH K.Y.CHENG,E.D.LOWE,J.SINCLAIR,E.A.NIGG,L.N.JOHNSON
JRNL TITL THE CRYSTAL STRUCTURE OF THE HUMAN POLO-LIKE
JRNL TITL 2 KINASE-1 POLO BOX DOMAIN AND ITS PHOSPHO-PEPTIDE
JRNL TITL 3 COMPLEX.
JRNL REF EMBO J. V. 22 5757 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 14592974
JRNL DOI 10.1093/EMBOJ/CDG558
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 36665
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1943
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2705
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2600
REMARK 3 BIN FREE R VALUE SET COUNT : 153
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 191
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.01000
REMARK 3 B12 (A**2) : 0.01000
REMARK 3 B13 (A**2) : -0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.373
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.291
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.791
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.861
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5628 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 5100 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7608 ; 1.591 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 11854 ; 1.269 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 671 ; 7.213 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 842 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6138 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1185 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1264 ; 0.201 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 6263 ; 0.229 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 3546 ; 0.094 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 199 ; 0.194 ; 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): 28 ; 0.238 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 95 ; 0.265 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.337 ; 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): 3377 ; 0.707 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5450 ; 1.341 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2251 ; 1.778 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2158 ; 3.048 ; 4.500
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 1Q4K COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-03.
REMARK 100 THE RCSB ID CODE IS RCSB019907.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37228
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.7
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.6
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.36400
REMARK 200 R SYM FOR SHELL (I) : 0.25800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: UNLIGANDED POLO BOX DOMAIN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, MES, PH 6.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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 LYS B 345
REMARK 465 GLY B 346
REMARK 465 LEU B 347
REMARK 465 GLU B 348
REMARK 465 ASN B 349
REMARK 465 PRO B 350
REMARK 465 LEU B 351
REMARK 465 PRO B 352
REMARK 465 GLU B 353
REMARK 465 ARG B 354
REMARK 465 PRO B 355
REMARK 465 ARG B 356
REMARK 465 GLU B 357
REMARK 465 LYS B 358
REMARK 465 GLU B 359
REMARK 465 GLU B 360
REMARK 465 PRO B 361
REMARK 465 VAL B 362
REMARK 465 VAL B 363
REMARK 465 ARG B 364
REMARK 465 GLU B 365
REMARK 465 THR B 366
REMARK 465 GLY B 367
REMARK 465 GLU B 368
REMARK 465 VAL B 369
REMARK 465 VAL B 370
REMARK 465 SER B 595
REMARK 465 ALA B 596
REMARK 465 SER B 597
REMARK 465 ASN B 598
REMARK 465 ARG B 599
REMARK 465 LEU B 600
REMARK 465 LYS B 601
REMARK 465 ALA B 602
REMARK 465 SER B 603
REMARK 465 LYS A 345
REMARK 465 GLY A 346
REMARK 465 LEU A 347
REMARK 465 GLU A 348
REMARK 465 ASN A 349
REMARK 465 PRO A 350
REMARK 465 LEU A 351
REMARK 465 PRO A 352
REMARK 465 GLU A 353
REMARK 465 ARG A 354
REMARK 465 PRO A 355
REMARK 465 ARG A 356
REMARK 465 GLU A 357
REMARK 465 LYS A 358
REMARK 465 GLU A 359
REMARK 465 GLU A 360
REMARK 465 PRO A 361
REMARK 465 VAL A 362
REMARK 465 VAL A 363
REMARK 465 ARG A 364
REMARK 465 GLU A 365
REMARK 465 THR A 366
REMARK 465 GLY A 367
REMARK 465 GLU A 368
REMARK 465 VAL A 369
REMARK 465 VAL A 370
REMARK 465 ASP A 371
REMARK 465 ARG A 594
REMARK 465 SER A 595
REMARK 465 ALA A 596
REMARK 465 SER A 597
REMARK 465 ASN A 598
REMARK 465 ARG A 599
REMARK 465 LEU A 600
REMARK 465 LYS A 601
REMARK 465 ALA A 602
REMARK 465 SER A 603
REMARK 465 LYS C 345
REMARK 465 GLY C 346
REMARK 465 LEU C 347
REMARK 465 GLU C 348
REMARK 465 ASN C 349
REMARK 465 PRO C 350
REMARK 465 LEU C 351
REMARK 465 PRO C 352
REMARK 465 GLU C 353
REMARK 465 ARG C 354
REMARK 465 PRO C 355
REMARK 465 ARG C 356
REMARK 465 GLU C 357
REMARK 465 LYS C 358
REMARK 465 GLU C 359
REMARK 465 GLU C 360
REMARK 465 PRO C 361
REMARK 465 VAL C 362
REMARK 465 VAL C 363
REMARK 465 ARG C 364
REMARK 465 GLU C 365
REMARK 465 THR C 366
REMARK 465 GLY C 367
REMARK 465 GLU C 368
REMARK 465 VAL C 369
REMARK 465 VAL C 370
REMARK 465 ASP C 371
REMARK 465 ALA C 495
REMARK 465 ASN C 496
REMARK 465 ILE C 497
REMARK 465 THR C 498
REMARK 465 PRO C 499
REMARK 465 ARG C 500
REMARK 465 GLU C 501
REMARK 465 GLY C 502
REMARK 465 ARG C 594
REMARK 465 SER C 595
REMARK 465 ALA C 596
REMARK 465 SER C 597
REMARK 465 ASN C 598
REMARK 465 ARG C 599
REMARK 465 LEU C 600
REMARK 465 LYS C 601
REMARK 465 ALA C 602
REMARK 465 SER C 603
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 ALA A 493 O HOH A 21 2.04
REMARK 500 C THR B 517 O HOH B 36 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS C 589 O HOH B 13 1554 1.91
REMARK 500 OD2 ASP B 419 OH TYR A 445 1455 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 B 537 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP B 554 CB - CG - OD2 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 537 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP C 376 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP C 416 CB - CG - OD2 ANGL. DEV. = 5.7 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 CYS B 372 -7.82 81.78
REMARK 500 GLU B 391 63.47 -113.26
REMARK 500 TYR B 417 51.71 -110.29
REMARK 500 LYS B 420 -1.97 -153.87
REMARK 500 ASN B 430 -2.80 74.34
REMARK 500 ASP B 438 22.14 -78.34
REMARK 500 ASP B 449 -45.30 -137.49
REMARK 500 ASN B 496 43.21 -94.91
REMARK 500 GLU B 504 114.16 61.51
REMARK 500 THR B 517 -106.62 -99.06
REMARK 500 HIS B 538 17.75 58.77
REMARK 500 GLU A 391 68.63 -101.49
REMARK 500 ARG A 396 56.45 -119.81
REMARK 500 TYR A 421 -61.88 -131.37
REMARK 500 ASN A 430 -1.67 81.50
REMARK 500 ASP A 449 -53.16 -146.58
REMARK 500 SER A 467 25.78 110.55
REMARK 500 GLU A 504 109.55 5.84
REMARK 500 THR A 517 -74.01 -108.33
REMARK 500 CYS A 573 136.11 -5.06
REMARK 500 TYR C 417 46.27 -108.94
REMARK 500 LYS C 420 -45.17 -146.88
REMARK 500 ASN C 430 -0.99 64.20
REMARK 500 ASP C 449 -65.87 -146.16
REMARK 500 GLU C 504 -43.26 50.75
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 THR A 517 ARG A 518 59.72
REMARK 500 CYS A 572 CYS A 573 149.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 109 DISTANCE = 6.29 ANGSTROMS
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NO SEQUENCE DATABASE REFERENCE FOUND FOR PHOSPHO-PEPTIDE
REMARK 999 (ENTITY 2, CHAINS D,E,F)AT THE TIME OF PROCESSING
DBREF 1Q4K A 345 603 UNP P53350 PLK1_HUMAN 345 603
DBREF 1Q4K B 345 603 UNP P53350 PLK1_HUMAN 345 603
DBREF 1Q4K C 345 603 UNP P53350 PLK1_HUMAN 345 603
DBREF 1Q4K D 1 6 PDB 1Q4K 1Q4K 1 6
DBREF 1Q4K E 1 6 PDB 1Q4K 1Q4K 1 6
DBREF 1Q4K F 1 6 PDB 1Q4K 1Q4K 1 6
SEQRES 1 B 259 LYS GLY LEU GLU ASN PRO LEU PRO GLU ARG PRO ARG GLU
SEQRES 2 B 259 LYS GLU GLU PRO VAL VAL ARG GLU THR GLY GLU VAL VAL
SEQRES 3 B 259 ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER
SEQRES 4 B 259 VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG
SEQRES 5 B 259 GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE
SEQRES 6 B 259 TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY
SEQRES 7 B 259 LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU
SEQRES 8 B 259 PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY
SEQRES 9 B 259 ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER
SEQRES 10 B 259 TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS
SEQRES 11 B 259 LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER
SEQRES 12 B 259 GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG
SEQRES 13 B 259 GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR
SEQRES 14 B 259 TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER
SEQRES 15 B 259 ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR
SEQRES 16 B 259 LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR
SEQRES 17 B 259 ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER
SEQRES 18 B 259 LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER
SEQRES 19 B 259 ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU
SEQRES 20 B 259 SER SER ARG SER ALA SER ASN ARG LEU LYS ALA SER
SEQRES 1 A 259 LYS GLY LEU GLU ASN PRO LEU PRO GLU ARG PRO ARG GLU
SEQRES 2 A 259 LYS GLU GLU PRO VAL VAL ARG GLU THR GLY GLU VAL VAL
SEQRES 3 A 259 ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER
SEQRES 4 A 259 VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG
SEQRES 5 A 259 GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE
SEQRES 6 A 259 TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY
SEQRES 7 A 259 LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU
SEQRES 8 A 259 PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY
SEQRES 9 A 259 ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER
SEQRES 10 A 259 TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS
SEQRES 11 A 259 LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER
SEQRES 12 A 259 GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG
SEQRES 13 A 259 GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR
SEQRES 14 A 259 TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER
SEQRES 15 A 259 ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR
SEQRES 16 A 259 LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR
SEQRES 17 A 259 ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER
SEQRES 18 A 259 LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER
SEQRES 19 A 259 ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU
SEQRES 20 A 259 SER SER ARG SER ALA SER ASN ARG LEU LYS ALA SER
SEQRES 1 C 259 LYS GLY LEU GLU ASN PRO LEU PRO GLU ARG PRO ARG GLU
SEQRES 2 C 259 LYS GLU GLU PRO VAL VAL ARG GLU THR GLY GLU VAL VAL
SEQRES 3 C 259 ASP CYS HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER
SEQRES 4 C 259 VAL ASN ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG
SEQRES 5 C 259 GLN GLU GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE
SEQRES 6 C 259 TRP VAL SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY
SEQRES 7 C 259 LEU GLY TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU
SEQRES 8 C 259 PHE ASN ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY
SEQRES 9 C 259 ASP SER LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER
SEQRES 10 C 259 TYR LEU THR VAL SER SER HIS PRO ASN SER LEU MET LYS
SEQRES 11 C 259 LYS ILE THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER
SEQRES 12 C 259 GLU HIS LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG
SEQRES 13 C 259 GLU GLY ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR
SEQRES 14 C 259 TRP PHE ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER
SEQRES 15 C 259 ASN GLY SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR
SEQRES 16 C 259 LYS LEU ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR
SEQRES 17 C 259 ILE ASP GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER
SEQRES 18 C 259 LEU LEU GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER
SEQRES 19 C 259 ARG LEU ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU
SEQRES 20 C 259 SER SER ARG SER ALA SER ASN ARG LEU LYS ALA SER
SEQRES 1 D 6 MET GLN SER TPO PRO LEU
SEQRES 1 E 6 MET GLN SER TPO PRO LEU
SEQRES 1 F 6 MET GLN SER TPO PRO LEU
MODRES 1Q4K TPO D 4 THR PHOSPHOTHREONINE
MODRES 1Q4K TPO E 4 THR PHOSPHOTHREONINE
MODRES 1Q4K TPO F 4 THR PHOSPHOTHREONINE
HET TPO D 4 11
HET TPO E 4 11
HET TPO F 4 11
HETNAM TPO PHOSPHOTHREONINE
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 4 TPO 3(C4 H10 N O6 P)
FORMUL 7 HOH *191(H2 O)
HELIX 1 1 CYS B 372 SER B 387 1 16
HELIX 2 2 ARG B 396 GLU B 401 5 6
HELIX 3 3 ASP B 402 ILE B 406 5 5
HELIX 4 4 PRO B 469 SER B 471 5 3
HELIX 5 5 LEU B 472 LEU B 490 1 19
HELIX 6 6 LEU B 564 GLY B 571 1 8
HELIX 7 7 CYS B 573 SER B 593 1 21
HELIX 8 8 CYS A 372 SER A 387 1 16
HELIX 9 9 ARG A 396 GLU A 401 5 6
HELIX 10 10 ASP A 402 ILE A 406 5 5
HELIX 11 11 PRO A 469 SER A 471 5 3
HELIX 12 12 LEU A 472 LEU A 490 1 19
HELIX 13 13 LEU A 564 GLY A 571 1 8
HELIX 14 14 CYS A 573 SER A 593 1 21
HELIX 15 15 CYS C 372 SER C 387 1 16
HELIX 16 16 ARG C 396 GLU C 401 5 6
HELIX 17 17 ASP C 402 ILE C 406 5 5
HELIX 18 18 LEU C 472 LEU C 490 1 19
HELIX 19 19 LEU C 564 GLY C 571 1 8
HELIX 20 20 CYS C 573 SER C 593 1 21
SHEET 1 A 6 VAL B 411 TYR B 417 0
SHEET 2 A 6 GLY B 422 LEU B 427 -1 O GLY B 424 N VAL B 415
SHEET 3 A 6 VAL B 432 PHE B 436 -1 O GLY B 433 N TYR B 425
SHEET 4 A 6 ARG B 441 LEU B 444 -1 O LEU B 444 N VAL B 432
SHEET 5 A 6 SER B 450 ILE B 454 -1 O ILE B 454 N ARG B 441
SHEET 6 A 6 GLU B 460 THR B 464 -1 O LEU B 463 N LEU B 451
SHEET 1 B 6 LEU B 511 ARG B 516 0
SHEET 2 B 6 ALA B 520 LEU B 525 -1 O HIS B 524 N THR B 513
SHEET 3 B 6 VAL B 530 PHE B 534 -1 O GLN B 531 N LEU B 523
SHEET 4 B 6 LYS B 540 CYS B 544 -1 O LEU B 543 N VAL B 530
SHEET 5 B 6 ALA B 549 ILE B 553 -1 O ILE B 553 N LYS B 540
SHEET 6 B 6 PHE B 559 ARG B 563 -1 O TYR B 562 N VAL B 550
SHEET 1 C 6 VAL A 411 ASP A 416 0
SHEET 2 C 6 GLY A 422 LEU A 427 -1 O GLY A 424 N VAL A 415
SHEET 3 C 6 VAL A 432 PHE A 436 -1 O LEU A 435 N LEU A 423
SHEET 4 C 6 ARG A 441 LEU A 444 -1 O LEU A 444 N VAL A 432
SHEET 5 C 6 SER A 450 ILE A 454 -1 O ILE A 454 N ARG A 441
SHEET 6 C 6 GLU A 460 THR A 464 -1 O SER A 461 N TYR A 453
SHEET 1 D 6 LEU A 511 ARG A 516 0
SHEET 2 D 6 ALA A 520 LEU A 525 -1 O ILE A 522 N PHE A 515
SHEET 3 D 6 VAL A 530 PHE A 534 -1 O GLN A 531 N LEU A 523
SHEET 4 D 6 LYS A 540 CYS A 544 -1 O LEU A 543 N VAL A 530
SHEET 5 D 6 ALA A 549 ILE A 553 -1 O ALA A 549 N CYS A 544
SHEET 6 D 6 PHE A 559 ARG A 563 -1 O TYR A 562 N VAL A 550
SHEET 1 E 6 VAL C 411 ASP C 416 0
SHEET 2 E 6 GLY C 422 LEU C 427 -1 O GLY C 424 N VAL C 415
SHEET 3 E 6 VAL C 432 PHE C 436 -1 O GLY C 433 N TYR C 425
SHEET 4 E 6 ARG C 441 LEU C 444 -1 O LEU C 444 N VAL C 432
SHEET 5 E 6 SER C 450 ILE C 454 -1 O GLN C 452 N ILE C 443
SHEET 6 E 6 SER C 461 THR C 464 -1 O LEU C 463 N LEU C 451
SHEET 1 F 6 LEU C 511 ARG C 516 0
SHEET 2 F 6 ALA C 520 LEU C 525 -1 O ILE C 522 N PHE C 515
SHEET 3 F 6 VAL C 530 PHE C 534 -1 O GLN C 531 N LEU C 523
SHEET 4 F 6 LYS C 540 CYS C 544 -1 O LEU C 543 N VAL C 530
SHEET 5 F 6 ALA C 549 ILE C 553 -1 O ILE C 553 N LYS C 540
SHEET 6 F 6 PHE C 559 ARG C 563 -1 O TYR C 562 N VAL C 550
LINK C SER D 3 N TPO D 4 1555 1555 1.33
LINK C TPO D 4 N PRO D 5 1555 1555 1.35
LINK C SER E 3 N TPO E 4 1555 1555 1.34
LINK C TPO E 4 N PRO E 5 1555 1555 1.34
LINK C SER F 3 N TPO F 4 1555 1555 1.34
LINK C TPO F 4 N PRO F 5 1555 1555 1.33
CRYST1 57.071 56.888 85.050 91.45 103.21 118.50 P 1 3
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 0.017522 0.009515 0.005679 0.00000
SCALE2 0.000000 0.020003 0.003183 0.00000
SCALE3 0.000000 0.000000 0.012229 0.00000
(ATOM LINES ARE NOT SHOWN.)
END