HEADER TRANSFERASE/TRANSFERASE INHIBITOR 24-AUG-12 4GRB
TITLE CASEIN KINASE 2 (CK2) BOUND TO INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TRANSFERASE;
COMPND 5 SYNONYM: CK II ALPHA;
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 GENE: CSNK2A1, CK2A1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, PROTEIN KINASE, CYTOSOL, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.A.LARSEN,J.E.DOWLING,A.D.FERGUSON
REVDAT 3 28-FEB-24 4GRB 1 REMARK
REVDAT 2 24-SEP-14 4GRB 1 JRNL
REVDAT 1 28-AUG-13 4GRB 0
JRNL AUTH J.E.DOWLING,M.ALIMZHANOV,L.BAO,M.H.BLOCK,C.CHUAQUI,
JRNL AUTH 2 E.L.COOKE,C.R.DENZ,A.HIRD,S.HUANG,N.A.LARSEN,B.PENG,
JRNL AUTH 3 T.W.PONTZ,C.RIVARD-COSTA,J.C.SAEH,K.THAKUR,Q.YE,T.ZHANG,
JRNL AUTH 4 P.D.LYNE
JRNL TITL STRUCTURE AND PROPERTY BASED DESIGN OF
JRNL TITL 2 PYRAZOLO[1,5-A]PYRIMIDINE INHIBITORS OF CK2 KINASE WITH
JRNL TITL 3 ACTIVITY IN VIVO.
JRNL REF ACS MED CHEM LETT V. 4 800 2013
JRNL REFN ISSN 1948-5875
JRNL PMID 24900749
JRNL DOI 10.1021/ML400197U
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 3 NUMBER OF REFLECTIONS : 16447
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 887
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 594
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 44.07
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 30
REMARK 3 BIN FREE R VALUE : 0.3960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2762
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 29
REMARK 3 SOLVENT ATOMS : 178
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : -0.20000
REMARK 3 B33 (A**2) : 0.74000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.399
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.245
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.148
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.598
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2867 ; 0.006 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1979 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3880 ; 1.002 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4769 ; 0.811 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 326 ; 4.926 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 154 ;32.067 ;23.052
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 501 ;14.932 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;20.185 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 399 ; 0.058 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3199 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 631 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 328
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4059 21.8272 19.2945
REMARK 3 T TENSOR
REMARK 3 T11: 0.0071 T22: 0.0139
REMARK 3 T33: 0.0032 T12: 0.0047
REMARK 3 T13: 0.0017 T23: 0.0020
REMARK 3 L TENSOR
REMARK 3 L11: 0.4245 L22: 0.7380
REMARK 3 L33: 0.7837 L12: -0.1350
REMARK 3 L13: -0.2468 L23: 0.2512
REMARK 3 S TENSOR
REMARK 3 S11: 0.0520 S12: 0.0159 S13: 0.0144
REMARK 3 S21: -0.0163 S22: -0.0439 S23: 0.0070
REMARK 3 S31: -0.0189 S32: 0.0240 S33: -0.0080
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4GRB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074539.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 6.5
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+ DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16447
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 29.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.4
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 46.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.16000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.900
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22-26% PEG 6K, 200 MM AMMONIUM
REMARK 280 SULFATE, 100 MM MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 296K
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 24.71550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.12050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.94850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.12050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.71550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.94850
REMARK 290 SMTRY3 4 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 MET A 1
REMARK 465 LYS A 329
REMARK 465 ASP A 330
REMARK 465 GLN A 331
REMARK 465 ALA A 332
REMARK 465 ARG A 333
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 316 NE - CZ - NH2 ANGL. DEV. = 3.6 DEGREES
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 ASP A 156 42.66 -153.36
REMARK 500 ASP A 175 81.77 54.06
REMARK 500 ALA A 193 176.11 64.24
REMARK 500 HIS A 234 68.47 -119.22
REMARK 500 VAL A 327 -99.15 -107.83
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 CL A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0XG A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U4U RELATED DB: PDB
DBREF 4GRB A 1 333 UNP P68400 CSK21_HUMAN 1 333
SEQRES 1 A 333 MET SER GLY PRO VAL PRO SER ARG ALA ARG VAL TYR THR
SEQRES 2 A 333 ASP VAL ASN THR HIS ARG PRO ARG GLU TYR TRP ASP TYR
SEQRES 3 A 333 GLU SER HIS VAL VAL GLU TRP GLY ASN GLN ASP ASP TYR
SEQRES 4 A 333 GLN LEU VAL ARG LYS LEU GLY ARG GLY LYS TYR SER GLU
SEQRES 5 A 333 VAL PHE GLU ALA ILE ASN ILE THR ASN ASN GLU LYS VAL
SEQRES 6 A 333 VAL VAL LYS ILE LEU LYS PRO VAL LYS LYS LYS LYS ILE
SEQRES 7 A 333 LYS ARG GLU ILE LYS ILE LEU GLU ASN LEU ARG GLY GLY
SEQRES 8 A 333 PRO ASN ILE ILE THR LEU ALA ASP ILE VAL LYS ASP PRO
SEQRES 9 A 333 VAL SER ARG THR PRO ALA LEU VAL PHE GLU HIS VAL ASN
SEQRES 10 A 333 ASN THR ASP PHE LYS GLN LEU TYR GLN THR LEU THR ASP
SEQRES 11 A 333 TYR ASP ILE ARG PHE TYR MET TYR GLU ILE LEU LYS ALA
SEQRES 12 A 333 LEU ASP TYR CYS HIS SER MET GLY ILE MET HIS ARG ASP
SEQRES 13 A 333 VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU HIS ARG
SEQRES 14 A 333 LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU PHE TYR
SEQRES 15 A 333 HIS PRO GLY GLN GLU TYR ASN VAL ARG VAL ALA SER ARG
SEQRES 16 A 333 TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP TYR GLN MET
SEQRES 17 A 333 TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY CYS MET
SEQRES 18 A 333 LEU ALA SER MET ILE PHE ARG LYS GLU PRO PHE PHE HIS
SEQRES 19 A 333 GLY HIS ASP ASN TYR ASP GLN LEU VAL ARG ILE ALA LYS
SEQRES 20 A 333 VAL LEU GLY THR GLU ASP LEU TYR ASP TYR ILE ASP LYS
SEQRES 21 A 333 TYR ASN ILE GLU LEU ASP PRO ARG PHE ASN ASP ILE LEU
SEQRES 22 A 333 GLY ARG HIS SER ARG LYS ARG TRP GLU ARG PHE VAL HIS
SEQRES 23 A 333 SER GLU ASN GLN HIS LEU VAL SER PRO GLU ALA LEU ASP
SEQRES 24 A 333 PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN SER ARG
SEQRES 25 A 333 LEU THR ALA ARG GLU ALA MET GLU HIS PRO TYR PHE TYR
SEQRES 26 A 333 THR VAL VAL LYS ASP GLN ALA ARG
HET CL A 401 1
HET 0XG A 402 28
HETNAM CL CHLORIDE ION
HETNAM 0XG 5-(2-{[4-(DIMETHYLCARBAMOYL)PHENYL]AMINO}-4-
HETNAM 2 0XG METHOXYPYRIMIDIN-5-YL)THIOPHENE-3-CARBOXYLIC ACID
FORMUL 2 CL CL 1-
FORMUL 3 0XG C19 H18 N4 O4 S
FORMUL 4 HOH *178(H2 O)
HELIX 1 1 PRO A 20 ASP A 25 1 6
HELIX 2 2 TYR A 26 HIS A 29 5 4
HELIX 3 3 LYS A 74 LEU A 88 1 15
HELIX 4 4 ASP A 120 LEU A 128 1 9
HELIX 5 5 THR A 129 MET A 150 1 22
HELIX 6 6 LYS A 158 HIS A 160 5 3
HELIX 7 7 SER A 194 LYS A 198 5 5
HELIX 8 8 GLY A 199 VAL A 204 1 6
HELIX 9 9 TYR A 211 ARG A 228 1 18
HELIX 10 10 ASP A 237 GLY A 250 1 14
HELIX 11 11 GLY A 250 TYR A 261 1 12
HELIX 12 12 ASP A 266 GLY A 274 1 9
HELIX 13 13 ARG A 280 VAL A 285 5 6
HELIX 14 14 ASN A 289 VAL A 293 5 5
HELIX 15 15 SER A 294 LYS A 303 1 10
HELIX 16 16 ASP A 308 ARG A 312 5 5
HELIX 17 17 THR A 314 GLU A 320 1 7
HELIX 18 18 HIS A 321 TYR A 325 5 5
SHEET 1 A 6 GLY A 34 ASN A 35 0
SHEET 2 A 6 LEU A 97 LYS A 102 1 O ILE A 100 N GLY A 34
SHEET 3 A 6 PRO A 109 GLU A 114 -1 O VAL A 112 N ASP A 99
SHEET 4 A 6 LYS A 64 LEU A 70 -1 N LYS A 68 O LEU A 111
SHEET 5 A 6 SER A 51 ASN A 58 -1 N ALA A 56 O VAL A 65
SHEET 6 A 6 TYR A 39 ARG A 47 -1 N ARG A 43 O GLU A 55
SHEET 1 B 2 ILE A 152 MET A 153 0
SHEET 2 B 2 GLU A 180 PHE A 181 -1 O GLU A 180 N MET A 153
SHEET 1 C 2 VAL A 162 ASP A 165 0
SHEET 2 C 2 LYS A 170 LEU A 173 -1 O LYS A 170 N ASP A 165
CISPEP 1 GLU A 230 PRO A 231 0 -3.20
SITE 1 AC1 2 ARG A 80 HOH A 619
SITE 1 AC2 11 ARG A 43 VAL A 53 VAL A 66 LYS A 68
SITE 2 AC2 11 PHE A 113 VAL A 116 ASN A 118 MET A 163
SITE 3 AC2 11 ILE A 174 ASP A 175 HOH A 525
CRYST1 49.431 61.897 116.241 90.00 90.00 90.00 P 21 21 21 4
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 0.020230 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016156 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008603 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
