HEADER HYDROLASE 19-SEP-06 2IEH
TITLE CRYSTAL STRUCTURE OF HUMAN KINESIN EG5 IN COMPLEX WITH (R)-MON97, A
TITLE 2 NEW MONASTROL-BASED INHIBITOR THAT BINDS AS (R)-ENANTIOMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINESIN-LIKE PROTEIN KIF11;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: MOTOR DOMAIN OF HUMAN KINESIN EG5;
COMPND 5 SYNONYM: KINESIN-RELATED MOTOR PROTEIN EG5, KINESIN-LIKE SPINDLE
COMPND 6 PROTEIN HKSP, THYROID RECEPTOR-INTERACTING PROTEIN 5, TRIP5, KINESIN-
COMPND 7 LIKE PROTEIN 1;
COMPND 8 EC: 3.6.4.4;
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: KIF11, EG5, KNSL1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS BETA-SHEET CORE, FLANKED BY THREE ALPHA-HELICES ON EACH SIDE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR I.GARCIA-SAEZ,F.KOZIELSKI
REVDAT 3 30-AUG-23 2IEH 1 REMARK LINK
REVDAT 2 13-MAY-08 2IEH 1 JRNL VERSN
REVDAT 1 23-JAN-07 2IEH 0
JRNL AUTH I.GARCIA-SAEZ,S.DEBONIS,R.LOPEZ,F.TRUCCO,B.ROUSSEAU,
JRNL AUTH 2 P.THUERY,F.KOZIELSKI
JRNL TITL STRUCTURE OF HUMAN EG5 IN COMPLEX WITH A NEW MONASTROL-BASED
JRNL TITL 2 INHIBITOR BOUND IN THE R CONFIGURATION.
JRNL REF J.BIOL.CHEM. V. 282 9740 2007
JRNL REFN ISSN 0021-9258
JRNL PMID 17251189
JRNL DOI 10.1074/JBC.M608883200
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 46815
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 SET) : 0.234
REMARK 3 FREE R VALUE : 0.281
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2362
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 394
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 119
REMARK 3 SOLVENT ATOMS : 214
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM SIGMAA (A) : 0.38
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.800
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2IEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-06.
REMARK 100 THE DEPOSITION ID IS D_1000039482.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979645
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51576
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.19000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.79000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.950
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1Q0B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG4000, 0.2M K2HPO4, 0.1M MES, PH
REMARK 280 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 34.68500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.93000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.95000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.93000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.68500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.95000
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 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 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 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 PRO A 5
REMARK 465 ASN A 6
REMARK 465 SER A 7
REMARK 465 SER A 8
REMARK 465 ALA A 9
REMARK 465 LYS A 10
REMARK 465 LYS A 11
REMARK 465 LYS A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 ILE A 272
REMARK 465 GLY A 273
REMARK 465 ARG A 274
REMARK 465 SER A 275
REMARK 465 GLY A 276
REMARK 465 ALA A 277
REMARK 465 VAL A 278
REMARK 465 ASP A 279
REMARK 465 LYS A 280
REMARK 465 ARG A 281
REMARK 465 ALA A 282
REMARK 465 ARG A 283
REMARK 465 GLU A 284
REMARK 465 ALA A 285
REMARK 465 GLY A 286
REMARK 465 ASN A 287
REMARK 465 VAL A 365
REMARK 465 ASN A 366
REMARK 465 GLN A 367
REMARK 465 LYS A 368
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 PRO B 5
REMARK 465 ASN B 6
REMARK 465 SER B 7
REMARK 465 SER B 8
REMARK 465 ALA B 9
REMARK 465 LYS B 10
REMARK 465 LYS B 11
REMARK 465 LYS B 12
REMARK 465 GLU B 13
REMARK 465 GLU B 14
REMARK 465 LYS B 15
REMARK 465 ILE B 272
REMARK 465 GLY B 273
REMARK 465 ARG B 274
REMARK 465 SER B 275
REMARK 465 GLY B 276
REMARK 465 ALA B 277
REMARK 465 VAL B 278
REMARK 465 ASP B 279
REMARK 465 LYS B 280
REMARK 465 ARG B 281
REMARK 465 ALA B 282
REMARK 465 ARG B 283
REMARK 465 GLU B 284
REMARK 465 ALA B 285
REMARK 465 GLY B 286
REMARK 465 ASN B 287
REMARK 465 GLN B 367
REMARK 465 LYS B 368
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 GLN A 183 O HOH A 717 1.84
REMARK 500 N LYS A 197 O HOH A 717 2.01
REMARK 500 O THR A 328 ND2 ASN A 361 2.02
REMARK 500 OE1 GLU A 162 O HOH A 714 2.04
REMARK 500 OD1 ASP A 177 OG SER A 179 2.05
REMARK 500 OG SER B 61 O HOH B 696 2.07
REMARK 500 NE ARG A 221 O HOH A 714 2.12
REMARK 500 OG1 THR A 107 OE2 GLU A 270 2.14
REMARK 500 OE1 GLU A 351 O HOH A 713 2.16
REMARK 500 CD ARG A 221 O HOH A 714 2.16
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 GLY A 16 CA GLY A 16 C 0.101
REMARK 500 PHE A 102 CB PHE A 102 CG -0.139
REMARK 500 PHE A 102 CD1 PHE A 102 CE1 -0.121
REMARK 500 ARG A 189 CB ARG A 189 CG 0.163
REMARK 500 ARG A 189 CG ARG A 189 CD 0.180
REMARK 500 SER B 36 C SER B 36 O 0.148
REMARK 500 ALA B 37 CA ALA B 37 CB -0.158
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 LYS A 15 CA - C - N ANGL. DEV. = -15.1 DEGREES
REMARK 500 GLY A 16 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 LEU A 182 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 ARG A 189 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 189 NE - CZ - NH2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ARG A 221 CG - CD - NE ANGL. DEV. = 23.2 DEGREES
REMARK 500 ARG A 221 CD - NE - CZ ANGL. DEV. = 12.8 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 221 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 LEU A 227 CB - CG - CD1 ANGL. DEV. = -10.9 DEGREES
REMARK 500 HIS B 38 C - N - CA ANGL. DEV. = 22.1 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 LYS A 17 134.13 173.88
REMARK 500 PRO A 121 176.72 -53.67
REMARK 500 GLU A 123 42.72 37.56
REMARK 500 ASP A 149 -79.57 -51.21
REMARK 500 ASN A 150 -169.10 -61.87
REMARK 500 ASN A 165 53.67 39.61
REMARK 500 LEU A 171 38.48 -96.63
REMARK 500 LEU A 172 16.33 -154.70
REMARK 500 ARG A 189 -73.01 -69.50
REMARK 500 ASP A 208 28.90 -77.91
REMARK 500 PRO A 310 32.16 -64.10
REMARK 500 SER A 314 145.74 -170.55
REMARK 500 LYS A 362 77.58 -114.30
REMARK 500 ASN B 29 -144.26 -87.57
REMARK 500 GLU B 118 -169.99 -121.70
REMARK 500 ASP B 149 57.15 -155.35
REMARK 500 VAL B 178 3.80 -59.45
REMARK 500 ASN B 190 -159.24 -88.86
REMARK 500 PRO B 310 34.15 -64.14
REMARK 500 SER B 314 149.38 -174.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 125 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 SER B 36 -12.22
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 112 OG1
REMARK 620 2 HOH A 613 O 65.7
REMARK 620 3 HOH A 616 O 81.9 95.6
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOY A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOY B 605
DBREF 2IEH A 2 368 UNP P52732 KIF11_HUMAN 2 368
DBREF 2IEH B 2 368 UNP P52732 KIF11_HUMAN 2 368
SEQRES 1 A 367 ALA SER GLN PRO ASN SER SER ALA LYS LYS LYS GLU GLU
SEQRES 2 A 367 LYS GLY LYS ASN ILE GLN VAL VAL VAL ARG CYS ARG PRO
SEQRES 3 A 367 PHE ASN LEU ALA GLU ARG LYS ALA SER ALA HIS SER ILE
SEQRES 4 A 367 VAL GLU CYS ASP PRO VAL ARG LYS GLU VAL SER VAL ARG
SEQRES 5 A 367 THR GLY GLY LEU ALA ASP LYS SER SER ARG LYS THR TYR
SEQRES 6 A 367 THR PHE ASP MET VAL PHE GLY ALA SER THR LYS GLN ILE
SEQRES 7 A 367 ASP VAL TYR ARG SER VAL VAL CYS PRO ILE LEU ASP GLU
SEQRES 8 A 367 VAL ILE MET GLY TYR ASN CYS THR ILE PHE ALA TYR GLY
SEQRES 9 A 367 GLN THR GLY THR GLY LYS THR PHE THR MET GLU GLY GLU
SEQRES 10 A 367 ARG SER PRO ASN GLU GLU TYR THR TRP GLU GLU ASP PRO
SEQRES 11 A 367 LEU ALA GLY ILE ILE PRO ARG THR LEU HIS GLN ILE PHE
SEQRES 12 A 367 GLU LYS LEU THR ASP ASN GLY THR GLU PHE SER VAL LYS
SEQRES 13 A 367 VAL SER LEU LEU GLU ILE TYR ASN GLU GLU LEU PHE ASP
SEQRES 14 A 367 LEU LEU ASN PRO SER SER ASP VAL SER GLU ARG LEU GLN
SEQRES 15 A 367 MET PHE ASP ASP PRO ARG ASN LYS ARG GLY VAL ILE ILE
SEQRES 16 A 367 LYS GLY LEU GLU GLU ILE THR VAL HIS ASN LYS ASP GLU
SEQRES 17 A 367 VAL TYR GLN ILE LEU GLU LYS GLY ALA ALA LYS ARG THR
SEQRES 18 A 367 THR ALA ALA THR LEU MET ASN ALA TYR SER SER ARG SER
SEQRES 19 A 367 HIS SER VAL PHE SER VAL THR ILE HIS MET LYS GLU THR
SEQRES 20 A 367 THR ILE ASP GLY GLU GLU LEU VAL LYS ILE GLY LYS LEU
SEQRES 21 A 367 ASN LEU VAL ASP LEU ALA GLY SER GLU ASN ILE GLY ARG
SEQRES 22 A 367 SER GLY ALA VAL ASP LYS ARG ALA ARG GLU ALA GLY ASN
SEQRES 23 A 367 ILE ASN GLN SER LEU LEU THR LEU GLY ARG VAL ILE THR
SEQRES 24 A 367 ALA LEU VAL GLU ARG THR PRO HIS VAL PRO TYR ARG GLU
SEQRES 25 A 367 SER LYS LEU THR ARG ILE LEU GLN ASP SER LEU GLY GLY
SEQRES 26 A 367 ARG THR ARG THR SER ILE ILE ALA THR ILE SER PRO ALA
SEQRES 27 A 367 SER LEU ASN LEU GLU GLU THR LEU SER THR LEU GLU TYR
SEQRES 28 A 367 ALA HIS ARG ALA LYS ASN ILE LEU ASN LYS PRO GLU VAL
SEQRES 29 A 367 ASN GLN LYS
SEQRES 1 B 367 ALA SER GLN PRO ASN SER SER ALA LYS LYS LYS GLU GLU
SEQRES 2 B 367 LYS GLY LYS ASN ILE GLN VAL VAL VAL ARG CYS ARG PRO
SEQRES 3 B 367 PHE ASN LEU ALA GLU ARG LYS ALA SER ALA HIS SER ILE
SEQRES 4 B 367 VAL GLU CYS ASP PRO VAL ARG LYS GLU VAL SER VAL ARG
SEQRES 5 B 367 THR GLY GLY LEU ALA ASP LYS SER SER ARG LYS THR TYR
SEQRES 6 B 367 THR PHE ASP MET VAL PHE GLY ALA SER THR LYS GLN ILE
SEQRES 7 B 367 ASP VAL TYR ARG SER VAL VAL CYS PRO ILE LEU ASP GLU
SEQRES 8 B 367 VAL ILE MET GLY TYR ASN CYS THR ILE PHE ALA TYR GLY
SEQRES 9 B 367 GLN THR GLY THR GLY LYS THR PHE THR MET GLU GLY GLU
SEQRES 10 B 367 ARG SER PRO ASN GLU GLU TYR THR TRP GLU GLU ASP PRO
SEQRES 11 B 367 LEU ALA GLY ILE ILE PRO ARG THR LEU HIS GLN ILE PHE
SEQRES 12 B 367 GLU LYS LEU THR ASP ASN GLY THR GLU PHE SER VAL LYS
SEQRES 13 B 367 VAL SER LEU LEU GLU ILE TYR ASN GLU GLU LEU PHE ASP
SEQRES 14 B 367 LEU LEU ASN PRO SER SER ASP VAL SER GLU ARG LEU GLN
SEQRES 15 B 367 MET PHE ASP ASP PRO ARG ASN LYS ARG GLY VAL ILE ILE
SEQRES 16 B 367 LYS GLY LEU GLU GLU ILE THR VAL HIS ASN LYS ASP GLU
SEQRES 17 B 367 VAL TYR GLN ILE LEU GLU LYS GLY ALA ALA LYS ARG THR
SEQRES 18 B 367 THR ALA ALA THR LEU MET ASN ALA TYR SER SER ARG SER
SEQRES 19 B 367 HIS SER VAL PHE SER VAL THR ILE HIS MET LYS GLU THR
SEQRES 20 B 367 THR ILE ASP GLY GLU GLU LEU VAL LYS ILE GLY LYS LEU
SEQRES 21 B 367 ASN LEU VAL ASP LEU ALA GLY SER GLU ASN ILE GLY ARG
SEQRES 22 B 367 SER GLY ALA VAL ASP LYS ARG ALA ARG GLU ALA GLY ASN
SEQRES 23 B 367 ILE ASN GLN SER LEU LEU THR LEU GLY ARG VAL ILE THR
SEQRES 24 B 367 ALA LEU VAL GLU ARG THR PRO HIS VAL PRO TYR ARG GLU
SEQRES 25 B 367 SER LYS LEU THR ARG ILE LEU GLN ASP SER LEU GLY GLY
SEQRES 26 B 367 ARG THR ARG THR SER ILE ILE ALA THR ILE SER PRO ALA
SEQRES 27 B 367 SER LEU ASN LEU GLU GLU THR LEU SER THR LEU GLU TYR
SEQRES 28 B 367 ALA HIS ARG ALA LYS ASN ILE LEU ASN LYS PRO GLU VAL
SEQRES 29 B 367 ASN GLN LYS
HET MG A 601 1
HET K A 607 1
HET CL A 608 1
HET ADP A 600 27
HET MOY A 602 24
HET PG4 A 606 13
HET MG B 604 1
HET ADP B 603 27
HET MOY B 605 24
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM CL CHLORIDE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MOY [(4R)-4-(3-HYDROXYPHENYL)-1,6-DIMETHYL-2-THIOXO-1,2,3,
HETNAM 2 MOY 4-TETRAHYDROPYRIMIDIN-5-YL](PHENYL)METHANONE
HETNAM PG4 TETRAETHYLENE GLYCOL
FORMUL 3 MG 2(MG 2+)
FORMUL 4 K K 1+
FORMUL 5 CL CL 1-
FORMUL 6 ADP 2(C10 H15 N5 O10 P2)
FORMUL 7 MOY 2(C19 H18 N2 O2 S)
FORMUL 8 PG4 C8 H18 O5
FORMUL 12 HOH *214(H2 O)
HELIX 1 1 LYS A 77 VAL A 85 1 9
HELIX 2 2 VAL A 85 MET A 95 1 11
HELIX 3 3 GLY A 110 GLU A 116 1 7
HELIX 4 4 GLY A 134 THR A 148 1 15
HELIX 5 5 ASN A 206 ASP A 208 5 3
HELIX 6 6 GLU A 209 THR A 223 1 15
HELIX 7 7 ALA A 230 SER A 235 1 6
HELIX 8 8 ASN A 289 GLU A 304 1 16
HELIX 9 9 PRO A 310 GLU A 313 5 4
HELIX 10 10 SER A 314 LEU A 320 1 7
HELIX 11 11 GLN A 321 LEU A 324 5 4
HELIX 12 12 ALA A 339 LEU A 341 5 3
HELIX 13 13 ASN A 342 LYS A 357 1 16
HELIX 14 14 ASN B 29 LYS B 34 1 6
HELIX 15 15 LYS B 77 VAL B 85 1 9
HELIX 16 16 VAL B 85 MET B 95 1 11
HELIX 17 17 GLY B 110 GLU B 116 1 7
HELIX 18 18 GLY B 134 LEU B 147 1 14
HELIX 19 19 ASN B 206 ASP B 208 5 3
HELIX 20 20 GLU B 209 MET B 228 1 20
HELIX 21 21 ALA B 230 SER B 235 1 6
HELIX 22 22 ASN B 289 GLU B 304 1 16
HELIX 23 23 PRO B 310 GLU B 313 5 4
HELIX 24 24 SER B 314 LEU B 320 1 7
HELIX 25 25 GLN B 321 LEU B 324 5 4
HELIX 26 26 ALA B 339 LEU B 341 5 3
HELIX 27 27 ASN B 342 LYS B 357 1 16
SHEET 1 A 2 LYS A 17 ASN A 18 0
SHEET 2 A 2 LEU A 360 ASN A 361 -1 O ASN A 361 N LYS A 17
SHEET 1 B 8 MET A 70 PHE A 72 0
SHEET 2 B 8 GLN A 20 CYS A 25 1 N VAL A 23 O PHE A 72
SHEET 3 B 8 ARG A 329 ILE A 336 1 O ALA A 334 N VAL A 22
SHEET 4 B 8 ASN A 98 TYR A 104 1 N ASN A 98 O ARG A 329
SHEET 5 B 8 LEU A 255 ASP A 265 1 O VAL A 264 N ILE A 101
SHEET 6 B 8 HIS A 236 GLU A 247 -1 N ILE A 243 O GLY A 259
SHEET 7 B 8 THR A 152 TYR A 164 -1 N LEU A 161 O VAL A 238
SHEET 8 B 8 GLU A 167 ASP A 170 -1 O PHE A 169 N GLU A 162
SHEET 1 C 8 MET A 70 PHE A 72 0
SHEET 2 C 8 GLN A 20 CYS A 25 1 N VAL A 23 O PHE A 72
SHEET 3 C 8 ARG A 329 ILE A 336 1 O ALA A 334 N VAL A 22
SHEET 4 C 8 ASN A 98 TYR A 104 1 N ASN A 98 O ARG A 329
SHEET 5 C 8 LEU A 255 ASP A 265 1 O VAL A 264 N ILE A 101
SHEET 6 C 8 HIS A 236 GLU A 247 -1 N ILE A 243 O GLY A 259
SHEET 7 C 8 THR A 152 TYR A 164 -1 N LEU A 161 O VAL A 238
SHEET 8 C 8 ILE A 202 VAL A 204 -1 O VAL A 204 N VAL A 156
SHEET 1 D 3 VAL A 41 ASP A 44 0
SHEET 2 D 3 GLU A 49 GLY A 56 -1 O SER A 51 N GLU A 42
SHEET 3 D 3 SER A 61 THR A 67 -1 O LYS A 64 N VAL A 52
SHEET 1 E 2 GLN A 183 ASP A 186 0
SHEET 2 E 2 VAL A 194 LYS A 197 -1 O ILE A 195 N PHE A 185
SHEET 1 F 2 LYS B 17 ASN B 18 0
SHEET 2 F 2 LEU B 360 ASN B 361 -1 O ASN B 361 N LYS B 17
SHEET 1 G 8 MET B 70 PHE B 72 0
SHEET 2 G 8 GLN B 20 CYS B 25 1 N VAL B 23 O PHE B 72
SHEET 3 G 8 ARG B 329 ILE B 336 1 O ALA B 334 N VAL B 22
SHEET 4 G 8 ASN B 98 TYR B 104 1 N PHE B 102 O ILE B 333
SHEET 5 G 8 GLU B 254 ASP B 265 1 O LYS B 260 N CYS B 99
SHEET 6 G 8 HIS B 236 THR B 248 -1 N ILE B 243 O GLY B 259
SHEET 7 G 8 GLU B 153 TYR B 164 -1 N GLU B 153 O LYS B 246
SHEET 8 G 8 GLU B 167 ASP B 170 -1 O PHE B 169 N GLU B 162
SHEET 1 H 8 MET B 70 PHE B 72 0
SHEET 2 H 8 GLN B 20 CYS B 25 1 N VAL B 23 O PHE B 72
SHEET 3 H 8 ARG B 329 ILE B 336 1 O ALA B 334 N VAL B 22
SHEET 4 H 8 ASN B 98 TYR B 104 1 N PHE B 102 O ILE B 333
SHEET 5 H 8 GLU B 254 ASP B 265 1 O LYS B 260 N CYS B 99
SHEET 6 H 8 HIS B 236 THR B 248 -1 N ILE B 243 O GLY B 259
SHEET 7 H 8 GLU B 153 TYR B 164 -1 N GLU B 153 O LYS B 246
SHEET 8 H 8 ILE B 202 VAL B 204 -1 O VAL B 204 N VAL B 156
SHEET 1 I 3 VAL B 41 ASP B 44 0
SHEET 2 I 3 GLU B 49 GLY B 56 -1 O GLU B 49 N ASP B 44
SHEET 3 I 3 SER B 61 THR B 67 -1 O LYS B 64 N VAL B 52
SHEET 1 J 2 GLN B 183 ASP B 186 0
SHEET 2 J 2 VAL B 194 LYS B 197 -1 O ILE B 195 N PHE B 185
LINK OG1 THR A 112 MG MG A 601 1555 1555 2.38
LINK MG MG A 601 O HOH A 613 1555 1555 2.36
LINK MG MG A 601 O HOH A 616 1555 1555 2.46
LINK OG1 THR B 112 MG MG B 604 1555 1555 2.41
SITE 1 AC1 5 THR A 112 ADP A 600 HOH A 612 HOH A 613
SITE 2 AC1 5 HOH A 616
SITE 1 AC2 6 ARG A 24 CYS A 25 GLY A 73 ALA A 74
SITE 2 AC2 6 THR A 76 ADP A 600
SITE 1 AC3 2 ARG A 138 PG4 A 606
SITE 1 AC4 5 THR B 112 ADP B 603 HOH B 609 HOH B 610
SITE 2 AC4 5 HOH B 612
SITE 1 AC5 18 ARG A 24 ARG A 26 PRO A 27 GLN A 106
SITE 2 AC5 18 THR A 107 GLY A 108 THR A 109 GLY A 110
SITE 3 AC5 18 LYS A 111 THR A 112 PHE A 113 GLU A 118
SITE 4 AC5 18 MG A 601 PG4 A 606 K A 607 HOH A 612
SITE 5 AC5 18 HOH A 613 HOH A 621
SITE 1 AC6 12 GLU A 116 GLY A 117 GLU A 118 ARG A 119
SITE 2 AC6 12 TRP A 127 ASP A 130 ALA A 133 PRO A 137
SITE 3 AC6 12 LEU A 160 TYR A 211 GLU A 215 ARG A 221
SITE 1 AC7 11 ARG A 24 PRO A 27 ALA A 74 THR A 76
SITE 2 AC7 11 LYS A 77 GLN A 78 ILE A 79 PRO A 131
SITE 3 AC7 11 ARG A 138 ADP A 600 CL A 608
SITE 1 AC8 17 ARG B 24 ARG B 26 PRO B 27 GLN B 106
SITE 2 AC8 17 THR B 107 GLY B 108 THR B 109 GLY B 110
SITE 3 AC8 17 LYS B 111 THR B 112 PHE B 113 GLU B 118
SITE 4 AC8 17 MG B 604 HOH B 610 HOH B 619 HOH B 625
SITE 5 AC8 17 HOH B 702
SITE 1 AC9 10 GLU B 116 GLY B 117 GLU B 118 ARG B 119
SITE 2 AC9 10 ASP B 130 ALA B 133 PRO B 137 TYR B 211
SITE 3 AC9 10 LEU B 214 ARG B 221
CRYST1 69.370 79.900 159.860 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 0.014415 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012516 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006255 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
