HEADER CELL CYCLE 15-JUL-03 1Q0B
TITLE CRYSTAL STRUCTURE OF THE MOTOR PROTEIN KSP IN COMPLEX WITH ADP AND
TITLE 2 MONASTROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINESIN-LIKE PROTEIN KIF11;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 2-368;
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 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 OR KNSL1 OR EG5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PRSETA
KEYWDS CELL CYCLE, MOTOR PROTEIN, MONASTROL
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.YAN,V.SARDANA,B.XU,W.HALCZENKO,C.HOMNICK,C.A.BUSER,G.D.HARTMAN,
AUTHOR 2 H.E.HUBER,L.C.KUO
REVDAT 3 16-AUG-23 1Q0B 1 REMARK LINK
REVDAT 2 24-FEB-09 1Q0B 1 VERSN
REVDAT 1 13-JAN-04 1Q0B 0
JRNL AUTH Y.YAN,V.SARDANA,B.XU,C.HOMNICK,W.HALCZENKO,C.A.BUSER,
JRNL AUTH 2 M.SCHABER,G.D.HARTMAN,H.E.HUBER,L.C.KUO
JRNL TITL INHIBITION OF A MITOTIC MOTOR PROTEIN: WHERE, HOW, AND
JRNL TITL 2 CONFORMATIONAL CONSEQUENCES
JRNL REF J.MOL.BIOL. V. 335 547 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 14672662
JRNL DOI 10.1016/J.JMB.2003.10.074
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 70259
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 7000
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5229
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 96
REMARK 3 SOLVENT ATOMS : 500
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) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.270
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 1Q0B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-03.
REMARK 100 THE DEPOSITION ID IS D_1000019755.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 70259
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.24000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1II6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, POTASSIUM PHOSPHATE, PH 8,
REMARK 280 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 34.65000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.60000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.60000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.65000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.75000
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 LYS A 15
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 PRO A 363
REMARK 465 GLU A 364
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: 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 VAL A 178 1.97 -63.82
REMARK 500 PRO A 310 42.47 -68.30
REMARK 500 ASP B 149 48.14 -158.90
REMARK 500 ARG B 189 -70.59 -56.16
REMARK 500 ASN B 190 -169.58 -69.57
REMARK 500 PRO B 310 40.38 -67.71
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 603 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 112 OG1
REMARK 620 2 ADP A 601 O3B 92.8
REMARK 620 3 HOH A 606 O 89.3 93.5
REMARK 620 4 HOH A 610 O 93.2 88.6 176.6
REMARK 620 5 HOH A 702 O 89.8 177.0 88.0 89.8
REMARK 620 6 HOH A 789 O 175.0 90.1 86.5 90.9 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 602 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 112 OG1
REMARK 620 2 ADP B 600 O3B 92.2
REMARK 620 3 HOH B 609 O 90.1 177.4
REMARK 620 4 HOH B 615 O 85.8 90.3 88.5
REMARK 620 5 HOH B 628 O 173.0 89.3 88.3 87.3
REMARK 620 6 HOH B 795 O 93.9 88.2 92.9 178.5 93.0
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAT A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAT B 605
DBREF 1Q0B A 2 368 UNP P52732 KIF11_HUMAN 2 368
DBREF 1Q0B 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 603 1
HET ADP A 601 27
HET NAT A 604 20
HET MG B 602 1
HET ADP B 600 27
HET NAT B 605 20
HETNAM MG MAGNESIUM ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM NAT ETHYL 4-(3-HYDROXYPHENYL)-6-METHYL-2-THIOXO-1,2,3,4-
HETNAM 2 NAT TETRAHYDROPYRIMIDINE-5-CARBOXYLATE
HETSYN NAT MONASTROL
FORMUL 3 MG 2(MG 2+)
FORMUL 4 ADP 2(C10 H15 N5 O10 P2)
FORMUL 5 NAT 2(C14 H16 N2 O3 S)
FORMUL 9 HOH *500(H2 O)
HELIX 1 1 ASN A 29 ALA A 35 1 7
HELIX 2 2 PRO A 45 ARG A 47 5 3
HELIX 3 3 LYS A 77 VAL A 85 1 9
HELIX 4 4 VAL A 85 MET A 95 1 11
HELIX 5 5 GLY A 110 GLU A 116 1 7
HELIX 6 6 SER A 120 GLU A 124 5 5
HELIX 7 7 GLY A 134 ASN A 150 1 17
HELIX 8 8 ASN A 206 ASP A 208 5 3
HELIX 9 9 GLU A 209 MET A 228 1 20
HELIX 10 10 ALA A 230 SER A 235 1 6
HELIX 11 11 ASN A 289 GLU A 304 1 16
HELIX 12 12 PRO A 310 GLU A 313 5 4
HELIX 13 13 SER A 314 LEU A 320 1 7
HELIX 14 14 GLN A 321 LEU A 324 5 4
HELIX 15 15 ALA A 339 LEU A 341 5 3
HELIX 16 16 ASN A 342 LYS A 357 1 16
HELIX 17 17 ASN B 29 LYS B 34 1 6
HELIX 18 18 LYS B 77 MET B 95 1 19
HELIX 19 19 GLY B 110 GLU B 116 1 7
HELIX 20 20 SER B 120 GLU B 124 5 5
HELIX 21 21 THR B 126 ASP B 130 5 5
HELIX 22 22 GLY B 134 LEU B 147 1 14
HELIX 23 23 ASN B 206 ASP B 208 5 3
HELIX 24 24 GLU B 209 MET B 228 1 20
HELIX 25 25 ALA B 230 SER B 235 1 6
HELIX 26 26 ASN B 289 GLU B 304 1 16
HELIX 27 27 PRO B 310 GLU B 313 5 4
HELIX 28 28 SER B 314 LEU B 320 1 7
HELIX 29 29 GLN B 321 LEU B 324 5 4
HELIX 30 30 ALA B 339 LEU B 341 5 3
HELIX 31 31 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 GLY A 105 1 N PHE A 102 O ILE A 333
SHEET 5 B 8 GLU A 254 ASP A 265 1 O VAL A 264 N ILE A 101
SHEET 6 B 8 HIS A 236 THR A 248 -1 N GLU A 247 O LEU A 255
SHEET 7 B 8 THR A 152 TYR A 164 -1 N GLU A 153 O LYS A 246
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 GLY A 105 1 N PHE A 102 O ILE A 333
SHEET 5 C 8 GLU A 254 ASP A 265 1 O VAL A 264 N ILE A 101
SHEET 6 C 8 HIS A 236 THR A 248 -1 N GLU A 247 O LEU A 255
SHEET 7 C 8 THR A 152 TYR A 164 -1 N GLU A 153 O LYS A 246
SHEET 8 C 8 ILE A 202 THR A 203 -1 O ILE A 202 N VAL A 158
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 GLY B 105 1 N PHE B 102 O ILE B 333
SHEET 5 G 8 GLU B 254 ASP B 265 1 O VAL B 264 N ILE B 101
SHEET 6 G 8 HIS B 236 THR B 248 -1 N GLU B 247 O LEU B 255
SHEET 7 G 8 THR B 152 TYR B 164 -1 N LEU B 161 O VAL B 238
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 GLY B 105 1 N PHE B 102 O ILE B 333
SHEET 5 H 8 GLU B 254 ASP B 265 1 O VAL B 264 N ILE B 101
SHEET 6 H 8 HIS B 236 THR B 248 -1 N GLU B 247 O LEU B 255
SHEET 7 H 8 THR B 152 TYR B 164 -1 N LEU B 161 O VAL B 238
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 603 1555 1555 2.22
LINK O3B ADP A 601 MG MG A 603 1555 1555 2.21
LINK MG MG A 603 O HOH A 606 1555 1555 2.21
LINK MG MG A 603 O HOH A 610 1555 1555 2.28
LINK MG MG A 603 O HOH A 702 1555 1555 2.31
LINK MG MG A 603 O HOH A 789 1555 1555 2.28
LINK OG1 THR B 112 MG MG B 602 1555 1555 2.19
LINK O3B ADP B 600 MG MG B 602 1555 1555 2.21
LINK MG MG B 602 O HOH B 609 1555 1555 2.28
LINK MG MG B 602 O HOH B 615 1555 1555 2.27
LINK MG MG B 602 O HOH B 628 1555 1555 2.33
LINK MG MG B 602 O HOH B 795 1555 1555 2.22
SITE 1 AC1 6 THR B 112 ADP B 600 HOH B 609 HOH B 615
SITE 2 AC1 6 HOH B 628 HOH B 795
SITE 1 AC2 6 THR A 112 ADP A 601 HOH A 606 HOH A 610
SITE 2 AC2 6 HOH A 702 HOH A 789
SITE 1 AC3 19 ARG A 24 ARG A 26 PRO A 27 GLN A 106
SITE 2 AC3 19 THR A 107 GLY A 108 THR A 109 GLY A 110
SITE 3 AC3 19 LYS A 111 THR A 112 PHE A 113 GLU A 118
SITE 4 AC3 19 MG A 603 HOH A 610 HOH A 625 HOH A 636
SITE 5 AC3 19 HOH A 784 HOH A 789 HOH A 797
SITE 1 AC4 20 ARG B 24 ARG B 26 PRO B 27 GLN B 106
SITE 2 AC4 20 THR B 107 GLY B 108 THR B 109 GLY B 110
SITE 3 AC4 20 LYS B 111 THR B 112 PHE B 113 GLU B 118
SITE 4 AC4 20 MG B 602 HOH B 628 HOH B 633 HOH B 635
SITE 5 AC4 20 HOH B 653 HOH B 695 HOH B 766 HOH B 795
SITE 1 AC5 12 GLU A 116 GLU A 118 ARG A 119 TRP A 127
SITE 2 AC5 12 ASP A 130 ALA A 133 ILE A 136 PRO A 137
SITE 3 AC5 12 TYR A 211 LEU A 214 ALA A 218 HOH A 609
SITE 1 AC6 12 HOH A 730 GLU B 116 GLU B 118 ARG B 119
SITE 2 AC6 12 TRP B 127 ASP B 130 ALA B 133 ILE B 136
SITE 3 AC6 12 PRO B 137 TYR B 211 LEU B 214 HOH B 617
CRYST1 69.300 79.500 159.200 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 0.014430 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012579 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006281 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
