HEADER TRANSFERASE 09-MAY-07 2PVM
TITLE STRUCTURE-BASED DESIGN OF PYRAZOLO[1,5-A][1,3,5]TRIAZINE DERIVATIVES
TITLE 2 AS POTENT INHIBITORS OF PROTEIN KINASE CK2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CASEIN KINASE II SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CK II, CK2-ALPHA, PROTEIN KINASE CK2 ALPHA;
COMPND 5 EC: 2.7.11.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_TAXID: 4577;
SOURCE 4 GENE: ACK2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-28A
KEYWDS STRUCTURE-BASED DRUG DESIGN, ENZYME-INHIBITOR COMPLEX, CASEIN KINASE
KEYWDS 2 II, PROTEIN KINASE CK2, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.NIE,C.PERRETTA,P.ERICKSON,S.MARGOSIAK,R.ALMASSY,J.LU,A.AVERILL,
AUTHOR 2 K.M.YAGER,S.CHU
REVDAT 5 15-NOV-23 2PVM 1 REMARK
REVDAT 4 30-AUG-23 2PVM 1 REMARK
REVDAT 3 20-OCT-21 2PVM 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2PVM 1 VERSN
REVDAT 1 13-MAY-08 2PVM 0
JRNL AUTH Z.NIE,C.PERRETTA,P.ERICKSON,S.MARGOSIAK,R.ALMASSY,J.LU,
JRNL AUTH 2 A.AVERILL,K.M.YAGER,S.CHU
JRNL TITL STRUCTURE-BASED DESIGN, SYNTHESIS, AND STUDY OF
JRNL TITL 2 PYRAZOLO[1,5-A][1,3,5]TRIAZINE DERIVATIVES AS POTENT
JRNL TITL 3 INHIBITORS OF PROTEIN KINASE CK2.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 4191 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17540560
JRNL DOI 10.1016/J.BMCL.2007.05.041
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 24747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2444
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 24747
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 48
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.01
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 309
REMARK 3 BIN R VALUE (WORKING SET) : 0.2950
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 32
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 : 2734
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 265
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.51300
REMARK 3 B22 (A**2) : -7.62200
REMARK 3 B33 (A**2) : 2.10900
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 2.11000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.14
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) : 0.26
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.19
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 20.83
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.740
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.230 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.800 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.040 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.980 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2PVM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAY-07.
REMARK 100 THE DEPOSITION ID IS D_1000042821.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 8.0
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 : ENRAF-NONIUS FR591
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL MAX-FLUX MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25306
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.07100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.2000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.60
REMARK 200 R MERGE FOR SHELL (I) : 0.28600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNX
REMARK 200 STARTING MODEL: PDB ENTRY 1OM1 PROTEIN MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 0.10M SODIUM ACETATE,
REMARK 280 0.10M TRISHCL, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 71.81900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.07250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 71.81900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.07250
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 751 LIES ON A SPECIAL POSITION.
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 -14
REMARK 465 GLY A -13
REMARK 465 SER A -12
REMARK 465 SER A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 SER A -4
REMARK 465 SER A -3
REMARK 465 GLY A -2
REMARK 465 LEU A -1
REMARK 465 VAL A 0
REMARK 465 PRO A 1
REMARK 465 ARG A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 HIS A 5
REMARK 465 ARG A 334
REMARK 465 THR A 335
REMARK 465 ARG A 336
REMARK 465 ALA A 337
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 705 O HOH A 705 2556 2.07
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 43 144.04 -174.68
REMARK 500 PRO A 72 124.82 -37.87
REMARK 500 ASP A 120 121.09 -37.96
REMARK 500 ASP A 156 42.80 -156.29
REMARK 500 ASP A 175 75.65 52.27
REMARK 500 ALA A 193 168.36 61.88
REMARK 500 ASP A 210 -159.89 -151.79
REMARK 500 HIS A 291 5.34 -69.40
REMARK 500 VAL A 293 50.71 -100.52
REMARK 500 ASN A 332 45.18 -79.17
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 P29 A 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PVH RELATED DB: PDB
REMARK 900 RELATED ID: 2PVJ RELATED DB: PDB
REMARK 900 RELATED ID: 2PVK RELATED DB: PDB
REMARK 900 RELATED ID: 2PVL RELATED DB: PDB
REMARK 900 RELATED ID: 2PVN RELATED DB: PDB
DBREF 2PVM A 6 337 UNP P28523 CSK2A_MAIZE 1 332
SEQADV 2PVM MET A -14 UNP P28523 EXPRESSION TAG
SEQADV 2PVM GLY A -13 UNP P28523 EXPRESSION TAG
SEQADV 2PVM SER A -12 UNP P28523 EXPRESSION TAG
SEQADV 2PVM SER A -11 UNP P28523 EXPRESSION TAG
SEQADV 2PVM HIS A -10 UNP P28523 EXPRESSION TAG
SEQADV 2PVM HIS A -9 UNP P28523 EXPRESSION TAG
SEQADV 2PVM HIS A -8 UNP P28523 EXPRESSION TAG
SEQADV 2PVM HIS A -7 UNP P28523 EXPRESSION TAG
SEQADV 2PVM HIS A -6 UNP P28523 EXPRESSION TAG
SEQADV 2PVM HIS A -5 UNP P28523 EXPRESSION TAG
SEQADV 2PVM SER A -4 UNP P28523 EXPRESSION TAG
SEQADV 2PVM SER A -3 UNP P28523 EXPRESSION TAG
SEQADV 2PVM GLY A -2 UNP P28523 EXPRESSION TAG
SEQADV 2PVM LEU A -1 UNP P28523 EXPRESSION TAG
SEQADV 2PVM VAL A 0 UNP P28523 EXPRESSION TAG
SEQADV 2PVM PRO A 1 UNP P28523 EXPRESSION TAG
SEQADV 2PVM ARG A 2 UNP P28523 EXPRESSION TAG
SEQADV 2PVM GLY A 3 UNP P28523 EXPRESSION TAG
SEQADV 2PVM SER A 4 UNP P28523 EXPRESSION TAG
SEQADV 2PVM HIS A 5 UNP P28523 EXPRESSION TAG
SEQADV 2PVM ALA A 256 UNP P28523 VAL 251 ENGINEERED MUTATION
SEQRES 1 A 352 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 352 LEU VAL PRO ARG GLY SER HIS MET SER LYS ALA ARG VAL
SEQRES 3 A 352 TYR ALA ASP VAL ASN VAL LEU ARG PRO LYS GLU TYR TRP
SEQRES 4 A 352 ASP TYR GLU ALA LEU THR VAL GLN TRP GLY GLU GLN ASP
SEQRES 5 A 352 ASP TYR GLU VAL VAL ARG LYS VAL GLY ARG GLY LYS TYR
SEQRES 6 A 352 SER GLU VAL PHE GLU GLY ILE ASN VAL ASN ASN ASN GLU
SEQRES 7 A 352 LYS CYS ILE ILE LYS ILE LEU LYS PRO VAL LYS LYS LYS
SEQRES 8 A 352 LYS ILE LYS ARG GLU ILE LYS ILE LEU GLN ASN LEU CSO
SEQRES 9 A 352 GLY GLY PRO ASN ILE VAL LYS LEU LEU ASP ILE VAL ARG
SEQRES 10 A 352 ASP GLN HIS SER LYS THR PRO SER LEU ILE PHE GLU TYR
SEQRES 11 A 352 VAL ASN ASN THR ASP PHE LYS VAL LEU TYR PRO THR LEU
SEQRES 12 A 352 THR ASP TYR ASP ILE ARG TYR TYR ILE TYR GLU LEU LEU
SEQRES 13 A 352 LYS ALA LEU ASP TYR CYS HIS SER GLN GLY ILE MET HIS
SEQRES 14 A 352 ARG ASP VAL LYS PRO HIS ASN VAL MET ILE ASP HIS GLU
SEQRES 15 A 352 LEU ARG LYS LEU ARG LEU ILE ASP TRP GLY LEU ALA GLU
SEQRES 16 A 352 PHE TYR HIS PRO GLY LYS GLU TYR ASN VAL ARG VAL ALA
SEQRES 17 A 352 SER ARG TYR PHE LYS GLY PRO GLU LEU LEU VAL ASP LEU
SEQRES 18 A 352 GLN ASP TYR ASP TYR SER LEU ASP MET TRP SER LEU GLY
SEQRES 19 A 352 CYS MET PHE ALA GLY MET ILE PHE ARG LYS GLU PRO PHE
SEQRES 20 A 352 PHE TYR GLY HIS ASP ASN HIS ASP GLN LEU VAL LYS ILE
SEQRES 21 A 352 ALA LYS VAL LEU GLY THR ASP GLY LEU ASN ALA TYR LEU
SEQRES 22 A 352 ASN LYS TYR ARG ILE GLU LEU ASP PRO GLN LEU GLU ALA
SEQRES 23 A 352 LEU VAL GLY ARG HIS SER ARG LYS PRO TRP LEU LYS PHE
SEQRES 24 A 352 MET ASN ALA ASP ASN GLN HIS LEU VAL SER PRO GLU ALA
SEQRES 25 A 352 ILE ASP PHE LEU ASP LYS LEU LEU ARG TYR ASP HIS GLN
SEQRES 26 A 352 GLU ARG LEU THR ALA LEU GLU ALA MET THR HIS PRO TYR
SEQRES 27 A 352 PHE GLN GLN VAL ARG ALA ALA GLU ASN SER ARG THR ARG
SEQRES 28 A 352 ALA
MODRES 2PVM CSO A 89 CYS S-HYDROXYCYSTEINE
HET CSO A 89 7
HET P29 A 501 26
HETNAM CSO S-HYDROXYCYSTEINE
HETNAM P29 4-(2-(1H-IMIDAZOL-4-YL)ETHYLAMINO)-2-(PHENYLAMINO)
HETNAM 2 P29 PYRAZOLO[1,5-A][1,3,5]TRIAZINE-8-CARBONITRILE
FORMUL 1 CSO C3 H7 N O3 S
FORMUL 2 P29 C17 H15 N9
FORMUL 3 HOH *265(H2 O)
HELIX 1 1 ASP A 14 ARG A 19 1 6
HELIX 2 2 PRO A 20 ASP A 25 1 6
HELIX 3 3 TYR A 26 LEU A 29 5 4
HELIX 4 4 GLU A 35 ASP A 37 5 3
HELIX 5 5 LYS A 74 CSO A 89 1 16
HELIX 6 6 ASP A 120 TYR A 125 1 6
HELIX 7 7 PRO A 126 LEU A 128 5 3
HELIX 8 8 THR A 129 GLN A 150 1 22
HELIX 9 9 LYS A 158 HIS A 160 5 3
HELIX 10 10 SER A 194 LYS A 198 5 5
HELIX 11 11 GLY A 199 VAL A 204 1 6
HELIX 12 12 TYR A 211 ARG A 228 1 18
HELIX 13 13 ASP A 237 GLY A 250 1 14
HELIX 14 14 GLY A 250 TYR A 261 1 12
HELIX 15 15 ASP A 266 GLY A 274 1 9
HELIX 16 16 PRO A 280 MET A 285 5 6
HELIX 17 17 ASN A 289 VAL A 293 5 5
HELIX 18 18 SER A 294 LYS A 303 1 10
HELIX 19 19 THR A 314 HIS A 321 1 8
HELIX 20 20 PHE A 324 ASN A 332 1 9
SHEET 1 A 5 TYR A 39 ARG A 47 0
SHEET 2 A 5 SER A 51 ASN A 58 -1 O GLU A 55 N ARG A 43
SHEET 3 A 5 LYS A 64 LEU A 70 -1 O CYS A 65 N GLY A 56
SHEET 4 A 5 PRO A 109 GLU A 114 -1 O PHE A 113 N ILE A 66
SHEET 5 A 5 LEU A 97 ARG A 102 -1 N VAL A 101 O SER A 110
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
LINK C LEU A 88 N CSO A 89 1555 1555 1.33
LINK C CSO A 89 N GLY A 90 1555 1555 1.33
CISPEP 1 GLU A 230 PRO A 231 0 -0.29
SITE 1 AC1 12 LYS A 21 GLU A 55 ILE A 66 PHE A 113
SITE 2 AC1 12 GLU A 114 TYR A 115 MET A 163 ILE A 174
SITE 3 AC1 12 ASP A 175 HOH A 506 HOH A 672 HOH A 723
CRYST1 143.638 60.145 44.984 90.00 102.90 90.00 C 1 2 1 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 0.006962 0.000000 0.001595 0.00000
SCALE2 0.000000 0.016626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022806 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
