HEADER TRANSFERASE 10-MAY-10 3MYG
TITLE AURORA A KINASE COMPLEXED WITH SCH 1473759
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 6;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 126-391;
COMPND 5 SYNONYM: AURORA KINASE A, SERINE/THREONINE-PROTEIN KINASE AURORA-A,
COMPND 6 SERINE/THREONINE-PROTEIN KINASE 15, AURORA/IPL1-RELATED KINASE 1,
COMPND 7 AURORA-RELATED KINASE 1, ARK-1, HARK1, BREAST TUMOR-AMPLIFIED KINASE;
COMPND 8 EC: 2.7.11.1;
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: AURKA, AIK, ARK1, AURA, BTAK, STK15, STK6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PDEST14
KEYWDS KINASE, CELL CYCLE, INHIBITOR, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.HRUZA,W.PROSIS,L.RAMANATHAN
REVDAT 3 06-SEP-23 3MYG 1 REMARK SEQADV
REVDAT 2 18-APR-18 3MYG 1 JRNL
REVDAT 1 21-JUL-10 3MYG 0
JRNL AUTH T.YU,J.R.TAGAT,A.D.KEREKES,R.J.DOLL,Y.ZHANG,Y.XIAO,
JRNL AUTH 2 S.ESPOSITE,D.B.BELANGER,P.J.CURRAN,A.K.MANDAL,M.A.SIDDIQUI,
JRNL AUTH 3 N.Y.SHIH,A.D.BASSO,M.LIU,K.GRAY,S.TEVAR,J.JONES,S.LEE,
JRNL AUTH 4 L.LIANG,S.PONERY,E.B.SMITH,A.HRUZA,J.VOIGT,L.RAMANATHAN,
JRNL AUTH 5 W.PROSISE,M.HU
JRNL TITL DISCOVERY OF A POTENT, INJECTABLE INHIBITOR OF AURORA
JRNL TITL 2 KINASES BASED ON THE IMIDAZO-[1,2-A]-PYRAZINE CORE.
JRNL REF ACS MED CHEM LETT V. 1 214 2010
JRNL REFN ISSN 1948-5875
JRNL PMID 24900197
JRNL DOI 10.1021/ML100063W
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.3
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 13611
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) : 0.222
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.250
REMARK 3 FREE R VALUE TEST SET COUNT : 714
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 : 7
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.58
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.62
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2582
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2522
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2438
REMARK 3 BIN R VALUE (WORKING SET) : 0.2478
REMARK 3 BIN FREE R VALUE : 0.3306
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.58
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 144
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 : 2081
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 47
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 63.39
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 58.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.42770
REMARK 3 B22 (A**2) : 4.42770
REMARK 3 B33 (A**2) : -8.85540
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.343
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.375
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.237
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.235
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.352
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.929
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.919
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2178 ; 2.000 ; NULL
REMARK 3 BOND ANGLES : 2929 ; 2.000 ; NULL
REMARK 3 TORSION ANGLES : 756 ; 2.000 ; NULL
REMARK 3 TRIGONAL CARBON PLANES : 49 ; 2.000 ; NULL
REMARK 3 GENERAL PLANES : 311 ; 5.000 ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : 2178 ; 20.000 ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 261 ; 5.000 ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 2471 ; 4.000 ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.09
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.67
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.19
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MYG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059151.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-07
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC
REMARK 200 OPTICS : OSMIC
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS VII
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13705
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.65300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1MQ4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.2M LISO4, 33% PEG 400, PH
REMARK 280 8.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.09400
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 114.18800
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 85.64100
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 142.73500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 28.54700
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 57.09400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 114.18800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 142.73500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 85.64100
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 28.54700
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 120
REMARK 465 ALA A 121
REMARK 465 MET A 122
REMARK 465 GLY A 123
REMARK 465 SER A 124
REMARK 465 LYS A 125
REMARK 465 ALA A 281
REMARK 465 PRO A 282
REMARK 465 SER A 283
REMARK 465 SER A 284
REMARK 465 ARG A 285
REMARK 465 ARG A 286
REMARK 465 THR A 287
REMARK 465 THR A 288
REMARK 465 LEU A 289
REMARK 465 CYS A 290
REMARK 465 GLY A 291
REMARK 465 LYS A 389
REMARK 465 PRO A 390
REMARK 465 SER A 391
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 TRP A 128 124.73 58.52
REMARK 500 PHE A 144 -36.36 85.29
REMARK 500 ALA A 172 -19.91 -153.75
REMARK 500 ASP A 202 -143.35 -127.75
REMARK 500 SER A 226 -48.97 72.30
REMARK 500 ARG A 255 -15.04 66.41
REMARK 500 ASP A 307 -152.51 -138.48
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EML A 1
DBREF 3MYG A 125 391 UNP O14965 STK6_HUMAN 125 391
SEQADV 3MYG GLY A 120 UNP O14965 EXPRESSION TAG
SEQADV 3MYG ALA A 121 UNP O14965 EXPRESSION TAG
SEQADV 3MYG MET A 122 UNP O14965 EXPRESSION TAG
SEQADV 3MYG GLY A 123 UNP O14965 EXPRESSION TAG
SEQADV 3MYG SER A 124 UNP O14965 EXPRESSION TAG
SEQRES 1 A 272 GLY ALA MET GLY SER LYS ARG GLN TRP ALA LEU GLU ASP
SEQRES 2 A 272 PHE GLU ILE GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY
SEQRES 3 A 272 ASN VAL TYR LEU ALA ARG GLU LYS GLN SER LYS PHE ILE
SEQRES 4 A 272 LEU ALA LEU LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS
SEQRES 5 A 272 ALA GLY VAL GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE
SEQRES 6 A 272 GLN SER HIS LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR
SEQRES 7 A 272 GLY TYR PHE HIS ASP ALA THR ARG VAL TYR LEU ILE LEU
SEQRES 8 A 272 GLU TYR ALA PRO LEU GLY THR VAL TYR ARG GLU LEU GLN
SEQRES 9 A 272 LYS LEU SER LYS PHE ASP GLU GLN ARG THR ALA THR TYR
SEQRES 10 A 272 ILE THR GLU LEU ALA ASN ALA LEU SER TYR CYS HIS SER
SEQRES 11 A 272 LYS ARG VAL ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU
SEQRES 12 A 272 LEU LEU GLY SER ALA GLY GLU LEU LYS ILE ALA ASP PHE
SEQRES 13 A 272 GLY TRP SER VAL HIS ALA PRO SER SER ARG ARG THR THR
SEQRES 14 A 272 LEU CYS GLY THR LEU ASP TYR LEU PRO PRO GLU MET ILE
SEQRES 15 A 272 GLU GLY ARG MET HIS ASP GLU LYS VAL ASP LEU TRP SER
SEQRES 16 A 272 LEU GLY VAL LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO
SEQRES 17 A 272 PRO PHE GLU ALA ASN THR TYR GLN GLU THR TYR LYS ARG
SEQRES 18 A 272 ILE SER ARG VAL GLU PHE THR PHE PRO ASP PHE VAL THR
SEQRES 19 A 272 GLU GLY ALA ARG ASP LEU ILE SER ARG LEU LEU LYS HIS
SEQRES 20 A 272 ASN PRO SER GLN ARG PRO MET LEU ARG GLU VAL LEU GLU
SEQRES 21 A 272 HIS PRO TRP ILE THR ALA ASN SER SER LYS PRO SER
HET PG4 A 4 13
HET EML A 1 30
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM EML 2-{ETHYL[(5-{[6-METHYL-3-(1H-PYRAZOL-4-YL)IMIDAZO[1,2-
HETNAM 2 EML A]PYRAZIN-8-YL]AMINO}ISOTHIAZOL-3-YL)METHYL]AMINO}-2-
HETNAM 3 EML METHYLPROPAN-1-OL
HETSYN EML SCH 1473759
FORMUL 2 PG4 C8 H18 O5
FORMUL 3 EML C20 H26 N8 O S
FORMUL 4 HOH *47(H2 O)
HELIX 1 1 ALA A 129 GLU A 131 5 3
HELIX 2 2 LYS A 166 LYS A 171 1 6
HELIX 3 3 VAL A 174 LEU A 188 1 15
HELIX 4 4 THR A 217 SER A 226 1 10
HELIX 5 5 ASP A 229 LYS A 250 1 22
HELIX 6 6 LYS A 258 GLU A 260 5 3
HELIX 7 7 ASP A 274 SER A 278 5 5
HELIX 8 8 PRO A 297 GLU A 302 1 6
HELIX 9 9 GLU A 308 GLY A 325 1 18
HELIX 10 10 THR A 333 ARG A 343 1 11
HELIX 11 11 THR A 353 LEU A 364 1 12
HELIX 12 12 ASN A 367 ARG A 371 5 5
HELIX 13 13 MET A 373 GLU A 379 1 7
HELIX 14 14 HIS A 380 SER A 387 1 8
SHEET 1 A 5 PHE A 133 LYS A 141 0
SHEET 2 A 5 GLY A 145 GLU A 152 -1 O VAL A 147 N LEU A 139
SHEET 3 A 5 ILE A 158 PHE A 165 -1 O VAL A 163 N ASN A 146
SHEET 4 A 5 ARG A 205 LEU A 210 -1 O VAL A 206 N LEU A 164
SHEET 5 A 5 LEU A 196 HIS A 201 -1 N PHE A 200 O TYR A 207
SHEET 1 B 2 LEU A 262 LEU A 264 0
SHEET 2 B 2 LEU A 270 ILE A 272 -1 O LYS A 271 N LEU A 263
SITE 1 AC1 3 LEU A 225 SER A 226 LYS A 227
SITE 1 AC2 19 HOH A 13 ARG A 137 LEU A 139 ALA A 160
SITE 2 AC2 19 LYS A 162 LEU A 194 LEU A 210 GLU A 211
SITE 3 AC2 19 TYR A 212 ALA A 213 PRO A 214 LEU A 215
SITE 4 AC2 19 GLY A 216 LYS A 224 LEU A 263 ASP A 274
SITE 5 AC2 19 SER A 342 ARG A 343 VAL A 344
CRYST1 80.880 80.880 171.282 90.00 90.00 120.00 P 61 2 2 12
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 0.012364 0.007138 0.000000 0.00000
SCALE2 0.000000 0.014277 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005838 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
