HEADER TRANSFERASE/TRANSFERASE INHIBITOR 20-JAN-12 4DEA
TITLE AURORA A IN COMPLEX WITH YL1-038-18
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AURORA KINASE A;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AURORA 2, AURORA/IPL1-RELATED KINASE 1, ARK-1, AURORA-
COMPND 5 RELATED KINASE 1, HARK1, BREAST TUMOR-AMPLIFIED KINASE,
COMPND 6 SERINE/THREONINE-PROTEIN KINASE 15, SERINE/THREONINE-PROTEIN KINASE
COMPND 7 6, SERINE/THREONINE-PROTEIN KINASE AURORA-A;
COMPND 8 EC: 2.7.11.1;
COMPND 9 ENGINEERED: YES;
COMPND 10 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: AIK, AIRK1, ARK1, AURA, AURKA, AYK1, BTAK, IAK1, STK15, STK6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: TUNER(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-MBP
KEYWDS PROTEIN KINASE, AURORA A, INHIBITOR, DFG-IN, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.P.MARTIN,J.-Y.ZHU,E.SCHONBRUNN
REVDAT 4 13-SEP-23 4DEA 1 REMARK SEQADV
REVDAT 3 26-SEP-12 4DEA 1 JRNL
REVDAT 2 12-SEP-12 4DEA 1 JRNL
REVDAT 1 22-AUG-12 4DEA 0
JRNL AUTH H.R.LAWRENCE,M.P.MARTIN,Y.LUO,R.PIREDDU,H.YANG,H.GEVARIYA,
JRNL AUTH 2 S.OZCAN,J.Y.ZHU,R.KENDIG,M.RODRIGUEZ,R.ELIAS,J.Q.CHENG,
JRNL AUTH 3 S.M.SEBTI,E.SCHONBRUNN,N.J.LAWRENCE
JRNL TITL DEVELOPMENT OF O-CHLOROPHENYL SUBSTITUTED PYRIMIDINES AS
JRNL TITL 2 EXCEPTIONALLY POTENT AURORA KINASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 55 7392 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22803810
JRNL DOI 10.1021/JM300334D
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.3
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) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2839472.400
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 13477
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) : 0.218
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 674
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.010
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.60
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2066
REMARK 3 BIN R VALUE (WORKING SET) : 0.3050
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 108
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2187
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 102
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 44.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.42000
REMARK 3 B22 (A**2) : -3.42000
REMARK 3 B33 (A**2) : 6.84000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.29
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) : 0.40
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.70
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.050
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.350 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.380 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.740 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.710 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 52.05
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : CARBOHYDRATE.PARAM
REMARK 3 PARAMETER FILE 6 : INH.PAR
REMARK 3 PARAMETER FILE 7 : EDO.PAR
REMARK 3 PARAMETER FILE 8 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : CARBOHYDRATE.TOP
REMARK 3 TOPOLOGY FILE 6 : INH.TOP
REMARK 3 TOPOLOGY FILE 7 : EDO.TOP
REMARK 3 TOPOLOGY FILE 8 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 4DEA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070220.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 7.0
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13477
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 3.50000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.28300
REMARK 200 R SYM FOR SHELL (I) : 25.2000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.300
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: PDB ENTRY 3FDN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10 MG/ML AURORA A PROTEIN, 1 MM YL1
REMARK 280 -038-18, 10 % (V/V) PEG 3350, 25 MM PHOSPHATE(NA/K PH 7.4), 100
REMARK 280 MM SODIUM TARTRATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K, PH 7.0
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 58.03333
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 116.06667
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 87.05000
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 145.08333
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 29.01667
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 58.03333
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 116.06667
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 145.08333
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 87.05000
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 29.01667
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 SER A 123
REMARK 465 PRO A 390
REMARK 465 SER A 391
REMARK 465 ASN A 392
REMARK 465 CYS A 393
REMARK 465 GLN A 394
REMARK 465 ASN A 395
REMARK 465 LYS A 396
REMARK 465 GLU A 397
REMARK 465 SER A 398
REMARK 465 ALA A 399
REMARK 465 SER A 400
REMARK 465 LYS A 401
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 125 -66.04 -161.33
REMARK 500 LYS A 166 -62.33 78.40
REMARK 500 ALA A 172 -7.29 83.92
REMARK 500 ASP A 202 -158.77 -135.29
REMARK 500 SER A 226 -49.58 82.46
REMARK 500 ASP A 256 36.29 -140.44
REMARK 500 ASP A 294 -36.82 -35.68
REMARK 500 ASP A 307 -156.84 -130.70
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 EDO A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHI A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DEB RELATED DB: PDB
REMARK 900 RELATED ID: 4DED RELATED DB: PDB
REMARK 900 RELATED ID: 4DEE RELATED DB: PDB
DBREF 4DEA A 123 401 UNP O14965 AURKA_HUMAN 123 401
SEQADV 4DEA ASP A 287 UNP O14965 THR 287 ENGINEERED MUTATION
SEQRES 1 A 279 SER LYS LYS ARG GLN TRP ALA LEU GLU ASP PHE GLU ILE
SEQRES 2 A 279 GLY ARG PRO LEU GLY LYS GLY LYS PHE GLY ASN VAL TYR
SEQRES 3 A 279 LEU ALA ARG GLU LYS GLN SER LYS PHE ILE LEU ALA LEU
SEQRES 4 A 279 LYS VAL LEU PHE LYS ALA GLN LEU GLU LYS ALA GLY VAL
SEQRES 5 A 279 GLU HIS GLN LEU ARG ARG GLU VAL GLU ILE GLN SER HIS
SEQRES 6 A 279 LEU ARG HIS PRO ASN ILE LEU ARG LEU TYR GLY TYR PHE
SEQRES 7 A 279 HIS ASP ALA THR ARG VAL TYR LEU ILE LEU GLU TYR ALA
SEQRES 8 A 279 PRO LEU GLY THR VAL TYR ARG GLU LEU GLN LYS LEU SER
SEQRES 9 A 279 LYS PHE ASP GLU GLN ARG THR ALA THR TYR ILE THR GLU
SEQRES 10 A 279 LEU ALA ASN ALA LEU SER TYR CYS HIS SER LYS ARG VAL
SEQRES 11 A 279 ILE HIS ARG ASP ILE LYS PRO GLU ASN LEU LEU LEU GLY
SEQRES 12 A 279 SER ALA GLY GLU LEU LYS ILE ALA ASP PHE GLY TRP SER
SEQRES 13 A 279 VAL HIS ALA PRO SER SER ARG ARG ASP THR LEU CYS GLY
SEQRES 14 A 279 THR LEU ASP TYR LEU PRO PRO GLU MET ILE GLU GLY ARG
SEQRES 15 A 279 MET HIS ASP GLU LYS VAL ASP LEU TRP SER LEU GLY VAL
SEQRES 16 A 279 LEU CYS TYR GLU PHE LEU VAL GLY LYS PRO PRO PHE GLU
SEQRES 17 A 279 ALA ASN THR TYR GLN GLU THR TYR LYS ARG ILE SER ARG
SEQRES 18 A 279 VAL GLU PHE THR PHE PRO ASP PHE VAL THR GLU GLY ALA
SEQRES 19 A 279 ARG ASP LEU ILE SER ARG LEU LEU LYS HIS ASN PRO SER
SEQRES 20 A 279 GLN ARG PRO MET LEU ARG GLU VAL LEU GLU HIS PRO TRP
SEQRES 21 A 279 ILE THR ALA ASN SER SER LYS PRO SER ASN CYS GLN ASN
SEQRES 22 A 279 LYS GLU SER ALA SER LYS
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET NHI A 504 26
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NHI 4,4'-(PYRIMIDINE-2,4-DIYLDIIMINO)DIBENZOIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 3(C2 H6 O2)
FORMUL 5 NHI C18 H14 N4 O4
FORMUL 6 HOH *102(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 HIS A 187 1 14
HELIX 4 4 THR A 217 SER A 226 1 10
HELIX 5 5 ASP A 229 SER A 249 1 21
HELIX 6 6 LYS A 258 GLU A 260 5 3
HELIX 7 7 PRO A 297 GLU A 302 1 6
HELIX 8 8 GLU A 308 GLY A 325 1 18
HELIX 9 9 THR A 333 ARG A 343 1 11
HELIX 10 10 THR A 353 LEU A 364 1 12
HELIX 11 11 ASN A 367 ARG A 371 5 5
HELIX 12 12 MET A 373 GLU A 379 1 7
HELIX 13 13 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 PHE A 157 LEU A 164 -1 O LEU A 161 N TYR A 148
SHEET 4 A 5 VAL A 206 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 VAL A 252 ILE A 253 0
SHEET 2 B 2 VAL A 279 HIS A 280 -1 O VAL A 279 N ILE A 253
SHEET 1 C 2 LEU A 262 LEU A 264 0
SHEET 2 C 2 LEU A 270 ILE A 272 -1 O LYS A 271 N LEU A 263
CISPEP 1 ALA A 281 PRO A 282 0 -0.40
SITE 1 AC1 2 TYR A 197 HOH A 683
SITE 1 AC2 5 GLU A 321 GLY A 325 LYS A 326 PRO A 327
SITE 2 AC2 5 GLU A 330
SITE 1 AC3 3 GLN A 127 GLY A 198 TYR A 199
SITE 1 AC4 14 ARG A 137 LEU A 139 GLY A 140 VAL A 147
SITE 2 AC4 14 ALA A 160 GLU A 211 ALA A 213 GLY A 216
SITE 3 AC4 14 ARG A 220 LEU A 263 HOH A 624 HOH A 643
SITE 4 AC4 14 HOH A 659 HOH A 670
CRYST1 82.420 82.420 174.100 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 0.012133 0.007005 0.000000 0.00000
SCALE2 0.000000 0.014010 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005744 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
