HEADER TRANSFERASE/TRANSFERASE INHIBITOR 21-MAR-12 4E9C
TITLE THE STRUCTURE OF THE POLO-BOX DOMAIN (PBD) OF POLO-LIKE KINASE 1
TITLE 2 (PLK1) IN COMPLEX WITH LDPPLHSPTA PHOSPHOPEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-PROTEIN KINASE
COMPND 5 13, STPK13;
COMPND 6 EC: 2.7.11.21;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: LDPPLHSPTA PHOSPHOPEPTIDE;
COMPND 10 CHAIN: B;
COMPND 11 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: PLK1, PLK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS
KEYWDS SERINE/THREONINE KINASE, TRANSFERASE, PHOSPHOPROTEIN BINDING DOMAIN,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.SLEDZ,M.HYVONEN,S.LANG,C.J.STUBBS,C.ABELL
REVDAT 2 17-OCT-12 4E9C 1 JRNL
REVDAT 1 10-OCT-12 4E9C 0
JRNL AUTH S.LANG,C.J.STUBBS,C.ABELL
JRNL TITL HIGH-THROUGHPUT INTERROGATION OF LIGAND BINDING MODE USING A
JRNL TITL 2 FLUORESCENCE-BASED ASSAY.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 51 7680 2012
JRNL REFN ISSN 1433-7851
JRNL PMID 22730171
JRNL DOI 10.1002/ANIE.201202660
REMARK 2
REMARK 2 RESOLUTION. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 22978
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1235
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1581
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1844
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 22
REMARK 3 SOLVENT ATOMS : 170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.121
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.079
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.357
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1952 ; 0.007 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2648 ; 1.084 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 245 ; 5.337 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 87 ;32.417 ;22.644
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 339 ;15.554 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 17 ;20.620 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 295 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1454 ; 0.003 ; 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): 1176 ; 0.474 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1901 ; 0.927 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 776 ; 1.418 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 738 ; 2.439 ; 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 : 1
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 380 A 585
REMARK 3 ORIGIN FOR THE GROUP (A): 11.7300 0.4870 4.2080
REMARK 3 T TENSOR
REMARK 3 T11: 0.0127 T22: 0.0122
REMARK 3 T33: 0.0676 T12: 0.0091
REMARK 3 T13: 0.0240 T23: 0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.8038 L22: 0.8776
REMARK 3 L33: 1.5273 L12: 0.2856
REMARK 3 L13: 0.2650 L23: 0.4960
REMARK 3 S TENSOR
REMARK 3 S11: 0.0282 S12: 0.0217 S13: 0.0380
REMARK 3 S21: 0.0253 S22: -0.0279 S23: 0.0127
REMARK 3 S31: 0.0288 S32: 0.0432 S33: -0.0003
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: NULL
REMARK 4
REMARK 4 4E9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
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 : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24213
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 44.890
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
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: 3P35
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 30% PEG 300, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.89200
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
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 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE LDPPLHSPTA PHOSPHOPEPTIDE IS PEPTIDE-LIKE, A MEMBER OF ENZYME
REMARK 400 INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: LDPPLHSPTA PHOSPHOPEPTIDE
REMARK 400 CHAIN: B
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 GLY A 363
REMARK 465 PRO A 364
REMARK 465 LEU A 365
REMARK 465 GLY A 366
REMARK 465 SER A 367
REMARK 465 PRO A 368
REMARK 465 GLU A 369
REMARK 465 PHE A 370
REMARK 465 ASP A 371
REMARK 465 ACE B 70
REMARK 465 LEU B 71
REMARK 465 ASP B 72
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 CYS A 372 SG
REMARK 470 GLU A 398 CG CD OE1 OE2
REMARK 470 LYS A 420 CG CD CE NZ
REMARK 470 ARG A 456 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 503 CG OD1 OD2
REMARK 470 GLU A 504 CG CD OE1 OE2
REMARK 470 GLU A 555 CG CD OE1 OE2
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 420 -42.30 -137.60
REMARK 500 TYR A 421 -52.70 -123.04
REMARK 500 ASP A 449 -48.48 -141.91
REMARK 500 HIS A 468 67.33 61.05
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 A 860 DISTANCE = 5.20 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF LDPPLHSPTA
REMARK 800 PHOSPHOPEPTIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E9D RELATED DB: PDB
REMARK 900 RELATED ID: 4E67 RELATED DB: PDB
DBREF 4E9C A 371 594 UNP P53350 PLK1_HUMAN 371 594
DBREF 4E9C B 70 80 PDB 4E9C 4E9C 70 80
SEQADV 4E9C GLY A 363 UNP P53350 EXPRESSION TAG
SEQADV 4E9C PRO A 364 UNP P53350 EXPRESSION TAG
SEQADV 4E9C LEU A 365 UNP P53350 EXPRESSION TAG
SEQADV 4E9C GLY A 366 UNP P53350 EXPRESSION TAG
SEQADV 4E9C SER A 367 UNP P53350 EXPRESSION TAG
SEQADV 4E9C PRO A 368 UNP P53350 EXPRESSION TAG
SEQADV 4E9C GLU A 369 UNP P53350 EXPRESSION TAG
SEQADV 4E9C PHE A 370 UNP P53350 EXPRESSION TAG
SEQRES 1 A 232 GLY PRO LEU GLY SER PRO GLU PHE ASP CYS HIS LEU SER
SEQRES 2 A 232 ASP MET LEU GLN GLN LEU HIS SER VAL ASN ALA SER LYS
SEQRES 3 A 232 PRO SER GLU ARG GLY LEU VAL ARG GLN GLU GLU ALA GLU
SEQRES 4 A 232 ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL SER LYS TRP
SEQRES 5 A 232 VAL ASP TYR SER ASP LYS TYR GLY LEU GLY TYR GLN LEU
SEQRES 6 A 232 CYS ASP ASN SER VAL GLY VAL LEU PHE ASN ASP SER THR
SEQRES 7 A 232 ARG LEU ILE LEU TYR ASN ASP GLY ASP SER LEU GLN TYR
SEQRES 8 A 232 ILE GLU ARG ASP GLY THR GLU SER TYR LEU THR VAL SER
SEQRES 9 A 232 SER HIS PRO ASN SER LEU MET LYS LYS ILE THR LEU LEU
SEQRES 10 A 232 LYS TYR PHE ARG ASN TYR MET SER GLU HIS LEU LEU LYS
SEQRES 11 A 232 ALA GLY ALA ASN ILE THR PRO ARG GLU GLY ASP GLU LEU
SEQRES 12 A 232 ALA ARG LEU PRO TYR LEU ARG THR TRP PHE ARG THR ARG
SEQRES 13 A 232 SER ALA ILE ILE LEU HIS LEU SER ASN GLY SER VAL GLN
SEQRES 14 A 232 ILE ASN PHE PHE GLN ASP HIS THR LYS LEU ILE LEU CYS
SEQRES 15 A 232 PRO LEU MET ALA ALA VAL THR TYR ILE ASP GLU LYS ARG
SEQRES 16 A 232 ASP PHE ARG THR TYR ARG LEU SER LEU LEU GLU GLU TYR
SEQRES 17 A 232 GLY CYS CYS LYS GLU LEU ALA SER ARG LEU ARG TYR ALA
SEQRES 18 A 232 ARG THR MET VAL ASP LYS LEU LEU SER SER ARG
SEQRES 1 B 11 ACE LEU ASP PRO PRO LEU HIS SER TPO ALA NH2
MODRES 4E9C TPO B 78 THR PHOSPHOTHREONINE
HET TPO B 78 11
HET NH2 B 80 1
HET PG0 A 601 8
HET PG0 A 602 8
HET GOL B 101 6
HETNAM TPO PHOSPHOTHREONINE
HETNAM NH2 AMINO GROUP
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM GOL GLYCEROL
HETSYN TPO PHOSPHONOTHREONINE
HETSYN PG0 PEG 6000
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 TPO C4 H10 N O6 P
FORMUL 2 NH2 H2 N
FORMUL 3 PG0 2(C5 H12 O3)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *170(H2 O)
HELIX 1 1 HIS A 373 SER A 387 1 15
HELIX 2 2 LYS A 388 ARG A 392 5 5
HELIX 3 3 ARG A 396 GLU A 401 5 6
HELIX 4 4 ASP A 402 ILE A 406 5 5
HELIX 5 5 SER A 466 HIS A 468 5 3
HELIX 6 6 PRO A 469 SER A 471 5 3
HELIX 7 7 LEU A 472 LEU A 490 1 19
HELIX 8 8 LEU A 564 GLY A 571 1 8
HELIX 9 9 CYS A 573 SER A 593 1 21
SHEET 1 A 6 VAL A 411 ASP A 416 0
SHEET 2 A 6 GLY A 422 LEU A 427 -1 O GLY A 424 N VAL A 415
SHEET 3 A 6 VAL A 432 PHE A 436 -1 O LEU A 435 N LEU A 423
SHEET 4 A 6 ARG A 441 LEU A 444 -1 O LEU A 444 N VAL A 432
SHEET 5 A 6 SER A 450 ILE A 454 -1 O ILE A 454 N ARG A 441
SHEET 6 A 6 GLU A 460 THR A 464 -1 O LEU A 463 N LEU A 451
SHEET 1 B 6 LEU A 511 ARG A 516 0
SHEET 2 B 6 ALA A 520 LEU A 525 -1 O ILE A 522 N PHE A 515
SHEET 3 B 6 VAL A 530 PHE A 534 -1 O GLN A 531 N LEU A 523
SHEET 4 B 6 LYS A 540 CYS A 544 -1 O LEU A 543 N VAL A 530
SHEET 5 B 6 ALA A 549 ILE A 553 -1 O ILE A 553 N LYS A 540
SHEET 6 B 6 PHE A 559 ARG A 563 -1 O TYR A 562 N VAL A 550
LINK C SER B 77 N TPO B 78 1555 1555 1.33
LINK C TPO B 78 N ALA B 79 1555 1555 1.33
LINK C ALA B 79 N NH2 B 80 1555 1555 1.26
SITE 1 AC1 4 TYR A 417 TYR A 481 PHE A 482 TYR A 485
SITE 1 AC2 2 ASP A 376 GLN A 380
SITE 1 AC3 7 THR A 459 GLU A 460 PHE A 535 HIS A 538
SITE 2 AC3 7 PRO B 74 HIS B 76 TPO B 78
SITE 1 AC4 25 LYS A 413 TRP A 414 VAL A 415 ASP A 416
SITE 2 AC4 25 THR A 459 SER A 461 TYR A 462 TYR A 485
SITE 3 AC4 25 HIS A 489 LEU A 490 LEU A 491 ARG A 516
SITE 4 AC4 25 THR A 517 PHE A 535 HIS A 538 LYS A 540
SITE 5 AC4 25 HOH A 702 HOH A 738 GOL B 101 HOH B 201
SITE 6 AC4 25 HOH B 202 HOH B 203 HOH B 204 HOH B 205
SITE 7 AC4 25 HOH B 207
CRYST1 35.634 89.784 37.108 90.00 109.28 90.00 P 1 21 1 2
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 0.028063 0.000000 0.009818 0.00000
SCALE2 0.000000 0.011138 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028550 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
