HEADER TRANSFERASE/TRANSFERASE INHIBITOR 31-MAR-17 5VC6
TITLE CRYSTAL STRUCTURE OF HUMAN WEE1 KINASE DOMAIN IN COMPLEX WITH PHA-
TITLE 2 848125
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: WEE1-LIKE PROTEIN KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 291-575;
COMPND 5 SYNONYM: WEE1HU,WEE1A KINASE;
COMPND 6 EC: 2.7.10.2;
COMPND 7 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: WEE1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-RIPL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS KINASE DOMAIN, CELL CYCLE, WEE1, TRANSFERASE, INHIBITOR, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-Y.ZHU,E.SCHONBRUNN
REVDAT 4 04-OCT-23 5VC6 1 REMARK
REVDAT 3 11-DEC-19 5VC6 1 REMARK
REVDAT 2 11-OCT-17 5VC6 1 JRNL
REVDAT 1 23-AUG-17 5VC6 0
JRNL AUTH J.Y.ZHU,R.A.CUELLAR,N.BERNDT,H.E.LEE,S.H.OLESEN,M.P.MARTIN,
JRNL AUTH 2 J.T.JENSEN,G.I.GEORG,E.SCHONBRUNN
JRNL TITL STRUCTURAL BASIS OF WEE KINASES FUNCTIONALITY AND
JRNL TITL 2 INACTIVATION BY DIVERSE SMALL MOLECULE INHIBITORS.
JRNL REF J. MED. CHEM. V. 60 7863 2017
JRNL REFN ISSN 1520-4804
JRNL PMID 28792760
JRNL DOI 10.1021/ACS.JMEDCHEM.7B00996
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.16
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 18663
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 934
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 63.1940 - 3.8255 0.96 2596 137 0.1941 0.2484
REMARK 3 2 3.8255 - 3.0364 0.98 2578 136 0.2062 0.2415
REMARK 3 3 3.0364 - 2.6526 0.97 2541 134 0.2381 0.2848
REMARK 3 4 2.6526 - 2.4100 0.97 2522 132 0.2454 0.3041
REMARK 3 5 2.4100 - 2.2373 0.96 2513 133 0.2417 0.2954
REMARK 3 6 2.2373 - 2.1054 0.96 2489 131 0.2389 0.2699
REMARK 3 7 2.1054 - 1.9999 0.95 2490 131 0.2515 0.3022
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.410
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.49
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.67
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2146
REMARK 3 ANGLE : 1.014 2900
REMARK 3 CHIRALITY : 0.042 311
REMARK 3 PLANARITY : 0.005 372
REMARK 3 DIHEDRAL : 14.555 804
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 293 THROUGH 337 )
REMARK 3 ORIGIN FOR THE GROUP (A): 40.3654 -3.7687 8.4179
REMARK 3 T TENSOR
REMARK 3 T11: 0.2829 T22: 0.2658
REMARK 3 T33: 0.2895 T12: 0.0028
REMARK 3 T13: 0.0173 T23: 0.1093
REMARK 3 L TENSOR
REMARK 3 L11: 2.8444 L22: 1.3959
REMARK 3 L33: 2.2844 L12: -1.4347
REMARK 3 L13: 0.8146 L23: 0.7744
REMARK 3 S TENSOR
REMARK 3 S11: -0.0445 S12: -0.1240 S13: -0.4432
REMARK 3 S21: -0.2009 S22: 0.0392 S23: 0.1468
REMARK 3 S31: 0.2441 S32: 0.2152 S33: 0.0054
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 352 )
REMARK 3 ORIGIN FOR THE GROUP (A): 56.4569 -9.2630 12.4383
REMARK 3 T TENSOR
REMARK 3 T11: 0.4653 T22: 0.1933
REMARK 3 T33: 0.5757 T12: 0.0270
REMARK 3 T13: -0.0988 T23: 0.0290
REMARK 3 L TENSOR
REMARK 3 L11: 5.1001 L22: 4.1908
REMARK 3 L33: 3.2448 L12: -1.8201
REMARK 3 L13: 0.4905 L23: 0.6981
REMARK 3 S TENSOR
REMARK 3 S11: 0.8977 S12: 0.5677 S13: -0.8106
REMARK 3 S21: -0.7400 S22: -0.0698 S23: 0.4648
REMARK 3 S31: -0.4121 S32: -0.1108 S33: 2.0312
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 353 THROUGH 461 )
REMARK 3 ORIGIN FOR THE GROUP (A): 50.7173 6.7203 18.2180
REMARK 3 T TENSOR
REMARK 3 T11: 0.2281 T22: 0.2061
REMARK 3 T33: 0.0989 T12: 0.0270
REMARK 3 T13: 0.0160 T23: 0.0534
REMARK 3 L TENSOR
REMARK 3 L11: 3.3150 L22: 2.1145
REMARK 3 L33: 2.4795 L12: -0.2428
REMARK 3 L13: 1.4312 L23: -0.6215
REMARK 3 S TENSOR
REMARK 3 S11: -0.1811 S12: -0.4725 S13: 0.1251
REMARK 3 S21: 0.1820 S22: 0.0944 S23: -0.0051
REMARK 3 S31: -0.1816 S32: -0.0616 S33: -0.0882
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 462 THROUGH 484 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.9642 -0.5257 13.3763
REMARK 3 T TENSOR
REMARK 3 T11: 0.3139 T22: 0.3272
REMARK 3 T33: 0.3185 T12: -0.0179
REMARK 3 T13: 0.0599 T23: 0.0416
REMARK 3 L TENSOR
REMARK 3 L11: 5.4974 L22: 1.5949
REMARK 3 L33: 2.8341 L12: 2.6539
REMARK 3 L13: -0.0010 L23: -0.9431
REMARK 3 S TENSOR
REMARK 3 S11: -0.2131 S12: 0.7268 S13: -0.9124
REMARK 3 S21: -0.4471 S22: 0.0144 S23: -0.5544
REMARK 3 S31: 0.4438 S32: -0.0366 S33: 0.0307
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 485 THROUGH 571 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.1309 14.0771 18.7489
REMARK 3 T TENSOR
REMARK 3 T11: 0.3605 T22: 0.2418
REMARK 3 T33: 0.4200 T12: -0.0451
REMARK 3 T13: -0.1222 T23: 0.0446
REMARK 3 L TENSOR
REMARK 3 L11: 3.4178 L22: 2.5097
REMARK 3 L33: 1.9438 L12: -0.4003
REMARK 3 L13: 0.0722 L23: 0.0470
REMARK 3 S TENSOR
REMARK 3 S11: -0.2058 S12: -0.1185 S13: 0.8901
REMARK 3 S21: 0.3784 S22: -0.1422 S23: -0.7625
REMARK 3 S31: -0.4421 S32: 0.4392 S33: -0.8358
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VC6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 6.9
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18665
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 63.163
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.716
REMARK 200 R MERGE (I) : 0.04500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.75
REMARK 200 R MERGE FOR SHELL (I) : 0.26500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.620
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5V5Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5.0 MG/ML WEE1, 25 MM NA/K PHOSPHATE,
REMARK 280 1 MM DTT, 0.05 M AMMONIUM SULFATE, 0.05 M BIS-TRIS (PH 5.5), 7.5
REMARK 280 % PEG 3350, 1 MM PHA-848125, PH 6.9, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
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 22.46000
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: 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 287
REMARK 465 ALA A 288
REMARK 465 GLY A 289
REMARK 465 SER A 290
REMARK 465 MET A 291
REMARK 465 LYS A 292
REMARK 465 THR A 437
REMARK 465 SER A 438
REMARK 465 ILE A 439
REMARK 465 PRO A 440
REMARK 465 ASN A 441
REMARK 465 ALA A 442
REMARK 465 ALA A 443
REMARK 465 SER A 444
REMARK 465 GLU A 445
REMARK 465 GLU A 446
REMARK 465 GLY A 447
REMARK 465 ASP A 448
REMARK 465 GLU A 449
REMARK 465 ASP A 450
REMARK 465 ASP A 451
REMARK 465 TRP A 452
REMARK 465 ALA A 453
REMARK 465 SER A 454
REMARK 465 ASN A 455
REMARK 465 LYS A 456
REMARK 465 ALA A 572
REMARK 465 SER A 573
REMARK 465 ARG A 574
REMARK 465 LYS A 575
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 H PHE A 398 O HOH A 704 1.45
REMARK 500 O HOH A 793 O HOH A 794 2.19
REMARK 500 O PRO A 552 O HOH A 701 2.19
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 ARG A 393 -62.72 -99.78
REMARK 500 SER A 396 -151.00 -100.19
REMARK 500 ASP A 426 41.49 -154.57
REMARK 500 ASP A 463 81.95 56.26
REMARK 500 SER A 472 68.82 -111.34
REMARK 500 ASN A 519 -168.97 179.38
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 P48 A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VC3 RELATED DB: PDB
REMARK 900 RELATED ID: 5VC4 RELATED DB: PDB
REMARK 900 RELATED ID: 5VC5 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD2 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD9 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD8 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD7 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD5 RELATED DB: PDB
REMARK 900 RELATED ID: 5VD4 RELATED DB: PDB
REMARK 900 RELATED ID: 5VDA RELATED DB: PDB
DBREF 5VC6 A 291 575 UNP P30291 WEE1_HUMAN 291 575
SEQADV 5VC6 GLY A 287 UNP P30291 EXPRESSION TAG
SEQADV 5VC6 ALA A 288 UNP P30291 EXPRESSION TAG
SEQADV 5VC6 GLY A 289 UNP P30291 EXPRESSION TAG
SEQADV 5VC6 SER A 290 UNP P30291 EXPRESSION TAG
SEQRES 1 A 289 GLY ALA GLY SER MET LYS SER ARG TYR THR THR GLU PHE
SEQRES 2 A 289 HIS GLU LEU GLU LYS ILE GLY SER GLY GLU PHE GLY SER
SEQRES 3 A 289 VAL PHE LYS CYS VAL LYS ARG LEU ASP GLY CYS ILE TYR
SEQRES 4 A 289 ALA ILE LYS ARG SER LYS LYS PRO LEU ALA GLY SER VAL
SEQRES 5 A 289 ASP GLU GLN ASN ALA LEU ARG GLU VAL TYR ALA HIS ALA
SEQRES 6 A 289 VAL LEU GLY GLN HIS SER HIS VAL VAL ARG TYR PHE SER
SEQRES 7 A 289 ALA TRP ALA GLU ASP ASP HIS MET LEU ILE GLN ASN GLU
SEQRES 8 A 289 TYR CYS ASN GLY GLY SER LEU ALA ASP ALA ILE SER GLU
SEQRES 9 A 289 ASN TYR ARG ILE MET SER TYR PHE LYS GLU ALA GLU LEU
SEQRES 10 A 289 LYS ASP LEU LEU LEU GLN VAL GLY ARG GLY LEU ARG TYR
SEQRES 11 A 289 ILE HIS SER MET SER LEU VAL HIS MET ASP ILE LYS PRO
SEQRES 12 A 289 SER ASN ILE PHE ILE SER ARG THR SER ILE PRO ASN ALA
SEQRES 13 A 289 ALA SER GLU GLU GLY ASP GLU ASP ASP TRP ALA SER ASN
SEQRES 14 A 289 LYS VAL MET PHE LYS ILE GLY ASP LEU GLY HIS VAL THR
SEQRES 15 A 289 ARG ILE SER SER PRO GLN VAL GLU GLU GLY ASP SER ARG
SEQRES 16 A 289 PHE LEU ALA ASN GLU VAL LEU GLN GLU ASN TYR THR HIS
SEQRES 17 A 289 LEU PRO LYS ALA ASP ILE PHE ALA LEU ALA LEU THR VAL
SEQRES 18 A 289 VAL CYS ALA ALA GLY ALA GLU PRO LEU PRO ARG ASN GLY
SEQRES 19 A 289 ASP GLN TRP HIS GLU ILE ARG GLN GLY ARG LEU PRO ARG
SEQRES 20 A 289 ILE PRO GLN VAL LEU SER GLN GLU PHE THR GLU LEU LEU
SEQRES 21 A 289 LYS VAL MET ILE HIS PRO ASP PRO GLU ARG ARG PRO SER
SEQRES 22 A 289 ALA MET ALA LEU VAL LYS HIS SER VAL LEU LEU SER ALA
SEQRES 23 A 289 SER ARG LYS
HET P48 A 601 66
HET EDO A 602 10
HETNAM P48 N,1,4,4-TETRAMETHYL-8-{[4-(4-METHYLPIPERAZIN-1-YL)
HETNAM 2 P48 PHENYL]AMINO}-4,5-DIHYDRO-1H-PYRAZOLO[4,3-
HETNAM 3 P48 H]QUINAZOLINE-3-CARBOXAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 P48 C25 H32 N8 O
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *94(H2 O)
HELIX 1 AA1 SER A 293 GLU A 298 1 6
HELIX 2 AA2 SER A 337 LEU A 353 1 17
HELIX 3 AA3 LEU A 384 MET A 395 1 12
HELIX 4 AA4 LYS A 399 MET A 420 1 22
HELIX 5 AA5 LYS A 428 SER A 430 5 3
HELIX 6 AA6 ASP A 479 LEU A 483 5 5
HELIX 7 AA7 ALA A 484 GLN A 489 1 6
HELIX 8 AA8 LEU A 495 ALA A 511 1 17
HELIX 9 AA9 GLY A 520 ARG A 527 1 8
HELIX 10 AB1 SER A 539 MET A 549 1 11
HELIX 11 AB2 ASP A 553 ARG A 557 5 5
HELIX 12 AB3 SER A 559 LYS A 565 1 7
SHEET 1 AA1 5 PHE A 299 GLY A 308 0
SHEET 2 AA1 5 GLY A 311 LYS A 318 -1 O LYS A 315 N GLU A 303
SHEET 3 AA1 5 ILE A 324 LYS A 331 -1 O ARG A 329 N SER A 312
SHEET 4 AA1 5 HIS A 371 GLU A 377 -1 O MET A 372 N SER A 330
SHEET 5 AA1 5 TYR A 362 GLU A 368 -1 N TRP A 366 O LEU A 373
SHEET 1 AA2 3 GLY A 382 SER A 383 0
SHEET 2 AA2 3 ILE A 432 SER A 435 -1 O ILE A 434 N GLY A 382
SHEET 3 AA2 3 MET A 458 ILE A 461 -1 O LYS A 460 N PHE A 433
SHEET 1 AA3 2 LEU A 422 VAL A 423 0
SHEET 2 AA3 2 THR A 468 ARG A 469 -1 O THR A 468 N VAL A 423
CISPEP 1 LEU A 570 SER A 571 0 -10.10
SITE 1 AC1 12 ILE A 305 PHE A 310 VAL A 313 ALA A 326
SITE 2 AC1 12 LYS A 328 ASN A 376 GLU A 377 TYR A 378
SITE 3 AC1 12 CYS A 379 GLY A 382 PHE A 433 ASP A 463
SITE 1 AC2 2 GLU A 301 HOH A 721
CRYST1 50.430 44.920 64.800 90.00 102.91 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 0.019829 0.000000 0.004544 0.00000
SCALE2 0.000000 0.022262 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015832 0.00000
(ATOM LINES ARE NOT SHOWN.)
END