HEADER TRANSFERASE 26-JUL-10 2XM9
TITLE STRUCTURE OF A SMALL MOLECULE INHIBITOR WITH THE KINASE DOMAIN OF CHK2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE CHK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 210-531;
COMPND 5 SYNONYM: CDS1, CHECKPOINT KINASE 2;
COMPND 6 EC: 2.7.11.1;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ROSETTA2 DE3(PLYSS);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTHREE-E
KEYWDS TRANSFERASE, CANCER
EXPDTA X-RAY DIFFRACTION
AUTHOR J.J.CALDWELL,E.J.WELSH,C.MATIJSSEN,V.E.ANDERSON,L.ANTONI,K.BOXALL,
AUTHOR 2 F.URBAN,A.HAYES,F.I.RAYNAUD,L.J.RIGOREAU,T.RAYNHAM,G.W.AHERNE,
AUTHOR 3 L.H.PEARL,A.W.OLIVER,M.D.GARRETT,I.COLLINS
REVDAT 3 20-DEC-23 2XM9 1 REMARK
REVDAT 2 16-FEB-11 2XM9 1 AUTHOR JRNL
REVDAT 1 12-JAN-11 2XM9 0
JRNL AUTH J.J.CALDWELL,E.J.WELSH,C.MATIJSSEN,V.E.ANDERSON,L.ANTONI,
JRNL AUTH 2 K.BOXALL,F.URBAN,A.HAYES,F.I.RAYNAUD,L.J.RIGOREAU,T.RAYNHAM,
JRNL AUTH 3 G.W.AHERNE,L.H.PEARL,A.W.OLIVER,M.D.GARRETT,I.COLLINS
JRNL TITL STRUCTURE-BASED DESIGN OF POTENT AND SELECTIVE
JRNL TITL 2 2-(QUINAZOLIN-2-YL)PHENOL INHIBITORS OF CHECKPOINT KINASE 2.
JRNL REF J.MED.CHEM. V. 54 580 2011
JRNL REFN ISSN 0022-2623
JRNL PMID 21186793
JRNL DOI 10.1021/JM101150B
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.07
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 15900
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 792
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 40.0782 - 4.5421 0.99 2618 131 0.1666 0.1961
REMARK 3 2 4.5421 - 3.6059 1.00 2528 128 0.1498 0.2014
REMARK 3 3 3.6059 - 3.1503 1.00 2498 143 0.1832 0.2571
REMARK 3 4 3.1503 - 2.8624 1.00 2489 143 0.2112 0.2549
REMARK 3 5 2.8624 - 2.6573 1.00 2469 125 0.2291 0.3035
REMARK 3 6 2.6573 - 2.5006 1.00 2506 122 0.2484 0.3087
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 51.58
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.090
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 49.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.25140
REMARK 3 B22 (A**2) : 0.25140
REMARK 3 B33 (A**2) : -0.50280
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 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 : 0.008 2329
REMARK 3 ANGLE : 1.071 3154
REMARK 3 CHIRALITY : 0.066 363
REMARK 3 PLANARITY : 0.004 393
REMARK 3 DIHEDRAL : 19.234 851
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 2XM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-10.
REMARK 100 THE DEPOSITION ID IS D_1290044790.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15926
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.320
REMARK 200 RESOLUTION RANGE LOW (A) : 41.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.350
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.43
REMARK 200 R MERGE FOR SHELL (I) : 0.52000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.450
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: PDB ENTRY 2CN5
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 0.2 M MAGNESIUM
REMARK 280 NITRATE, 8-16% (W/V) PEG 3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 61.96667
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 30.98333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 30.98333
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 61.96667
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.6 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -61.96667
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 203
REMARK 465 PRO A 204
REMARK 465 LEU A 205
REMARK 465 GLY A 206
REMARK 465 SER A 207
REMARK 465 HIS A 208
REMARK 465 MET A 209
REMARK 465 SER A 210
REMARK 465 GLY A 229
REMARK 465 ALA A 230
REMARK 465 CYS A 231
REMARK 465 ARG A 254
REMARK 465 LYS A 255
REMARK 465 PHE A 256
REMARK 465 ALA A 257
REMARK 465 ILE A 258
REMARK 465 GLY A 259
REMARK 465 SER A 260
REMARK 465 ALA A 261
REMARK 465 ARG A 262
REMARK 465 GLU A 263
REMARK 465 ALA A 264
REMARK 465 ASP A 265
REMARK 465 ALA A 513
REMARK 465 GLN A 514
REMARK 465 PRO A 515
REMARK 465 SER A 516
REMARK 465 THR A 517
REMARK 465 SER A 518
REMARK 465 ARG A 519
REMARK 465 LYS A 520
REMARK 465 ARG A 521
REMARK 465 PRO A 522
REMARK 465 ARG A 523
REMARK 465 GLU A 524
REMARK 465 GLY A 525
REMARK 465 GLU A 526
REMARK 465 ALA A 527
REMARK 465 GLU A 528
REMARK 465 GLY A 529
REMARK 465 ALA A 530
REMARK 465 GLU A 531
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 224 CG CD CE NZ
REMARK 470 SER A 252 OG
REMARK 470 LEU A 268 CG CD1 CD2
REMARK 470 GLU A 271 CG CD OE1 OE2
REMARK 470 GLU A 275 CG CD OE1 OE2
REMARK 470 LYS A 279 CD CE NZ
REMARK 470 GLU A 295 CG CD OE1 OE2
REMARK 470 LYS A 373 CG CD CE NZ
REMARK 470 GLU A 377 CG CD OE1 OE2
REMARK 470 MET A 381 CG SD CE
REMARK 470 ARG A 382 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 450 CG CD OE1 OE2
REMARK 470 LYS A 494 CD CE NZ
REMARK 470 THR A 506 OG1 CG2
REMARK 470 GLN A 510 CG CD OE1 NE2
REMARK 470 VAL A 511 CG1 CG2
REMARK 470 LEU A 512 CG CD1 CD2
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 SER A 223 -158.97 -141.02
REMARK 500 ALA A 294 -145.20 -138.42
REMARK 500 ASN A 316 17.43 55.18
REMARK 500 ARG A 346 -8.38 78.98
REMARK 500 ASP A 368 67.11 60.76
REMARK 500 GLU A 377 108.30 -57.63
REMARK 500 LEU A 467 48.16 -86.99
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 LWH A 1513
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 1514
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WTI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2XBJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2CN8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH
REMARK 900 DEBROMOHYMENIALDISINE
REMARK 900 RELATED ID: 2W0J RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH NSC 109555 , A SPECIFIC
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 2WTC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2WTJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
REMARK 900 RELATED ID: 2W7X RELATED DB: PDB
REMARK 900 CELLULAR INHIBITION OF CHECKPOINT KINASE 2 AND POTENTIATION OF
REMARK 900 CYTOTOXIC DRUGS BY NOVEL CHK2 INHIBITOR PV1019
REMARK 900 RELATED ID: 1GXC RELATED DB: PDB
REMARK 900 FHA DOMAIN FROM HUMAN CHK2 KINASE IN COMPLEX WITH A SYNTHETIC
REMARK 900 PHOSPHOPEPTIDE
REMARK 900 RELATED ID: 2CN5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN CHK2 IN COMPLEX WITH ADP
REMARK 900 RELATED ID: 2XM8 RELATED DB: PDB
REMARK 900 CO-CRYSTAL STRUCTURE OF A SMALL MOLECULE INHIBITOR BOUND TO THE
REMARK 900 KINASE DOMAIN OF CHK2
REMARK 900 RELATED ID: 2WTD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CHK2 IN COMPLEX WITH AN INHIBITOR
DBREF 2XM9 A 210 531 UNP O96017 CHK2_HUMAN 210 531
SEQADV 2XM9 GLY A 203 UNP O96017 EXPRESSION TAG
SEQADV 2XM9 PRO A 204 UNP O96017 EXPRESSION TAG
SEQADV 2XM9 LEU A 205 UNP O96017 EXPRESSION TAG
SEQADV 2XM9 GLY A 206 UNP O96017 EXPRESSION TAG
SEQADV 2XM9 SER A 207 UNP O96017 EXPRESSION TAG
SEQADV 2XM9 HIS A 208 UNP O96017 EXPRESSION TAG
SEQADV 2XM9 MET A 209 UNP O96017 EXPRESSION TAG
SEQRES 1 A 329 GLY PRO LEU GLY SER HIS MET SER VAL TYR PRO LYS ALA
SEQRES 2 A 329 LEU ARG ASP GLU TYR ILE MET SER LYS THR LEU GLY SER
SEQRES 3 A 329 GLY ALA CYS GLY GLU VAL LYS LEU ALA PHE GLU ARG LYS
SEQRES 4 A 329 THR CYS LYS LYS VAL ALA ILE LYS ILE ILE SER LYS ARG
SEQRES 5 A 329 LYS PHE ALA ILE GLY SER ALA ARG GLU ALA ASP PRO ALA
SEQRES 6 A 329 LEU ASN VAL GLU THR GLU ILE GLU ILE LEU LYS LYS LEU
SEQRES 7 A 329 ASN HIS PRO CYS ILE ILE LYS ILE LYS ASN PHE PHE ASP
SEQRES 8 A 329 ALA GLU ASP TYR TYR ILE VAL LEU GLU LEU MET GLU GLY
SEQRES 9 A 329 GLY GLU LEU PHE ASP LYS VAL VAL GLY ASN LYS ARG LEU
SEQRES 10 A 329 LYS GLU ALA THR CYS LYS LEU TYR PHE TYR GLN MET LEU
SEQRES 11 A 329 LEU ALA VAL GLN TYR LEU HIS GLU ASN GLY ILE ILE HIS
SEQRES 12 A 329 ARG ASP LEU LYS PRO GLU ASN VAL LEU LEU SER SER GLN
SEQRES 13 A 329 GLU GLU ASP CYS LEU ILE LYS ILE THR ASP PHE GLY HIS
SEQRES 14 A 329 SER LYS ILE LEU GLY GLU THR SER LEU MET ARG THR LEU
SEQRES 15 A 329 CYS GLY THR PRO THR TYR LEU ALA PRO GLU VAL LEU VAL
SEQRES 16 A 329 SER VAL GLY THR ALA GLY TYR ASN ARG ALA VAL ASP CYS
SEQRES 17 A 329 TRP SER LEU GLY VAL ILE LEU PHE ILE CYS LEU SER GLY
SEQRES 18 A 329 TYR PRO PRO PHE SER GLU HIS ARG THR GLN VAL SER LEU
SEQRES 19 A 329 LYS ASP GLN ILE THR SER GLY LYS TYR ASN PHE ILE PRO
SEQRES 20 A 329 GLU VAL TRP ALA GLU VAL SER GLU LYS ALA LEU ASP LEU
SEQRES 21 A 329 VAL LYS LYS LEU LEU VAL VAL ASP PRO LYS ALA ARG PHE
SEQRES 22 A 329 THR THR GLU GLU ALA LEU ARG HIS PRO TRP LEU GLN ASP
SEQRES 23 A 329 GLU ASP MET LYS ARG LYS PHE GLN ASP LEU LEU SER GLU
SEQRES 24 A 329 GLU ASN GLU SER THR ALA LEU PRO GLN VAL LEU ALA GLN
SEQRES 25 A 329 PRO SER THR SER ARG LYS ARG PRO ARG GLU GLY GLU ALA
SEQRES 26 A 329 GLU GLY ALA GLU
HET LWH A1513 28
HET NO3 A1514 4
HETNAM LWH 4-(1H-PYRAZOL-5-YL)-2-{4-[(3S)-PYRROLIDIN-3-
HETNAM 2 LWH YLAMINO]QUINAZOLIN-2-YL}PHENOL
HETNAM NO3 NITRATE ION
FORMUL 2 LWH C21 H20 N6 O
FORMUL 3 NO3 N O3 1-
FORMUL 4 HOH *153(H2 O)
HELIX 1 1 PRO A 213 GLU A 219 1 7
HELIX 2 2 PRO A 266 LEU A 280 1 15
HELIX 3 3 PHE A 310 VAL A 313 5 4
HELIX 4 4 LYS A 320 ASN A 341 1 22
HELIX 5 5 LYS A 349 GLU A 351 5 3
HELIX 6 6 THR A 378 LEU A 384 1 7
HELIX 7 7 THR A 387 LEU A 391 5 5
HELIX 8 8 ALA A 392 VAL A 399 1 8
HELIX 9 9 ARG A 406 GLY A 423 1 18
HELIX 10 10 SER A 435 GLY A 443 1 9
HELIX 11 11 ILE A 448 GLU A 454 1 7
HELIX 12 12 SER A 456 LEU A 467 1 12
HELIX 13 13 THR A 476 ARG A 482 1 7
HELIX 14 14 HIS A 483 GLN A 487 5 5
HELIX 15 15 ASP A 488 GLU A 504 1 17
SHEET 1 AA 5 TYR A 220 GLY A 227 0
SHEET 2 AA 5 GLU A 233 GLU A 239 -1 O VAL A 234 N LEU A 226
SHEET 3 AA 5 LYS A 245 ILE A 251 -1 O VAL A 246 N ALA A 237
SHEET 4 AA 5 TYR A 297 GLU A 302 -1 O TYR A 297 N ILE A 251
SHEET 5 AA 5 ILE A 288 ASP A 293 -1 N LYS A 289 O VAL A 300
SHEET 1 AB 3 GLY A 307 GLU A 308 0
SHEET 2 AB 3 VAL A 353 LEU A 355 -1 N LEU A 355 O GLY A 307
SHEET 3 AB 3 ILE A 364 ILE A 366 -1 O LYS A 365 N LEU A 354
SHEET 1 AC 2 ILE A 343 ILE A 344 0
SHEET 2 AC 2 LYS A 373 ILE A 374 -1 O LYS A 373 N ILE A 344
SITE 1 AC1 17 LEU A 226 SER A 228 LYS A 249 GLU A 273
SITE 2 AC1 17 ILE A 286 LEU A 301 GLU A 302 LEU A 303
SITE 3 AC1 17 MET A 304 GLY A 307 GLU A 308 GLU A 351
SITE 4 AC1 17 ASN A 352 LEU A 354 THR A 367 ASP A 368
SITE 5 AC1 17 HOH A2153
SITE 1 AC2 5 LEU A 375 GLY A 403 TYR A 404 ASN A 405
SITE 2 AC2 5 ARG A 406
CRYST1 91.360 91.360 92.950 90.00 90.00 120.00 P 32 2 1 6
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 0.010946 0.006320 0.000000 0.00000
SCALE2 0.000000 0.012639 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010758 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
