HEADER TRANSFERASE/INHIBITOR 20-FEB-13 3ZO1
TITLE THE SYNTHESIS AND EVALUATION OF DIAZASPIROCYCLIC PROTEIN KINASE
TITLE 2 INHIBITORS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PKA C-ALPHA;
COMPND 5 EC: 2.7.11.11;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CAMP-DEPENDENT PROTEIN KINASE INHIBITOR ALPHA;
COMPND 9 CHAIN: I;
COMPND 10 FRAGMENT: RESIDUES 6-23;
COMPND 11 SYNONYM: PKI-ALPHA;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: BOVINE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 11 ORGANISM_COMMON: BOVINE;
SOURCE 12 ORGANISM_TAXID: 9913
KEYWDS TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.E.ALLEN,C.L.CHOW,J.J.CALDWELL,I.M.WESTWOOD,R.L.VAN MONTFORT,
AUTHOR 2 I.COLLINS
REVDAT 6 20-DEC-23 3ZO1 1 REMARK LINK
REVDAT 5 03-APR-19 3ZO1 1 REMARK LINK
REVDAT 4 28-MAR-18 3ZO1 1 JRNL
REVDAT 3 28-AUG-13 3ZO1 1 JRNL
REVDAT 2 21-AUG-13 3ZO1 1 JRNL
REVDAT 1 06-MAR-13 3ZO1 0
JRNL AUTH C.E.ALLEN,C.L.CHOW,J.J.CALDWELL,I.M.WESTWOOD,
JRNL AUTH 2 R.L.VAN MONTFORT,I.COLLINS
JRNL TITL SYNTHESIS AND EVALUATION OF HETEROARYL SUBSTITUTED
JRNL TITL 2 DIAZASPIROCYCLES AS SCAFFOLDS TO PROBE THE ATP-BINDING SITE
JRNL TITL 3 OF PROTEIN KINASES.
JRNL REF BIOORG. MED. CHEM. V. 21 5707 2013
JRNL REFN ESSN 1464-3391
JRNL PMID 23920481
JRNL DOI 10.1016/J.BMC.2013.07.021
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 31013
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 1564
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 16
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.78
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2831
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1951
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2684
REMARK 3 BIN R VALUE (WORKING SET) : 0.1934
REMARK 3 BIN FREE R VALUE : 0.2261
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.19
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 147
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 : 2891
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 398
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.59
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.63100
REMARK 3 B22 (A**2) : -3.24330
REMARK 3 B33 (A**2) : 3.87430
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) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.153
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.130
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.140
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.124
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 3030 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 4102 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1044 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 70 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 453 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 3030 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 378 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 3843 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.96
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.10
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.11
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -27.3651 -1.9689 2.7837
REMARK 3 T TENSOR
REMARK 3 T11: -0.0894 T22: -0.0472
REMARK 3 T33: -0.1055 T12: 0.0091
REMARK 3 T13: 0.0025 T23: -0.0191
REMARK 3 L TENSOR
REMARK 3 L11: 0.8937 L22: 1.0222
REMARK 3 L33: 1.2725 L12: 0.2188
REMARK 3 L13: -0.0354 L23: -0.3822
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: 0.0555 S13: 0.0368
REMARK 3 S21: -0.0287 S22: 0.0392 S23: 0.0895
REMARK 3 S31: -0.0723 S32: -0.1194 S33: -0.0251
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN I
REMARK 3 ORIGIN FOR THE GROUP (A): -14.1389 1.7971 -10.6790
REMARK 3 T TENSOR
REMARK 3 T11: 0.0346 T22: 0.0089
REMARK 3 T33: -0.0785 T12: -0.0063
REMARK 3 T13: 0.0265 T23: -0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 1.2391 L22: 1.4507
REMARK 3 L33: 1.1126 L12: 0.7946
REMARK 3 L13: -1.3146 L23: -1.4555
REMARK 3 S TENSOR
REMARK 3 S11: -0.0458 S12: 0.1150 S13: -0.1294
REMARK 3 S21: 0.0763 S22: -0.0568 S23: 0.0316
REMARK 3 S31: 0.0607 S32: 0.0606 S33: 0.1026
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IDEAL-DIST CONTACT TERM CONTACT SETUP.
REMARK 3 ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY
REMARK 4
REMARK 4 3ZO1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-FEB-13.
REMARK 100 THE DEPOSITION ID IS D_1290055876.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97630
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31064
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 55.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.0000
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.56000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 2GFC
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM MES-BISTRIS PH6.5, 75MM LICL, 1MM
REMARK 280 DTT, 0.1MM EDTA, 1.5MM MEGA8; 4 DEGREE CELSIUS, TEMPERATURE 277K
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 36.47000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.28500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.17500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 40.28500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.47000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.17500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.3 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
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 0
REMARK 465 GLY A 1
REMARK 465 ASN A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 ALA A 5
REMARK 465 ALA A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
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 SER A 10 OG
REMARK 470 GLU A 11 CG CD OE1 OE2
REMARK 470 GLN A 12 CG CD OE1 NE2
REMARK 470 LYS A 16 CD CE NZ
REMARK 470 GLU A 17 CG CD OE1 OE2
REMARK 470 LYS A 21 CG CD CE NZ
REMARK 470 GLU A 64 CG CD OE1 OE2
REMARK 470 LYS A 81 NZ
REMARK 470 LYS A 83 CE NZ
REMARK 470 LYS A 105 CE NZ
REMARK 470 GLN A 177 OE1 NE2
REMARK 470 LYS A 217 NZ
REMARK 470 ILE A 244 CD1
REMARK 470 LYS A 285 CG CD CE NZ
REMARK 470 LYS A 295 CD CE NZ
REMARK 470 LYS A 309 CD CE NZ
REMARK 470 GLU A 311 CD OE1 OE2
REMARK 470 LYS A 317 CD CE NZ
REMARK 470 PHE A 318 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 319 CB CG CD CE NZ
REMARK 470 GLU A 331 CB CG CD OE1 OE2
REMARK 470 GLU A 333 CB CG CD OE1 OE2
REMARK 470 ILE A 335 CD1
REMARK 470 LYS A 345 CD CE NZ
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 ASN A 99 108.41 -165.07
REMARK 500 ASP A 166 42.61 -145.63
REMARK 500 ASP A 184 74.63 63.83
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2184 DISTANCE = 6.55 ANGSTROMS
REMARK 525 HOH A2369 DISTANCE = 6.02 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIJ A 1351
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1352
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1353
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1355
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ZO2 RELATED DB: PDB
REMARK 900 THE SYNTHESIS AND EVALUATION OF DIAZASPIROCYCLIC PROTEIN KINASE
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 3ZO3 RELATED DB: PDB
REMARK 900 THE SYNTHESIS AND EVALUATION OF DIAZASPIROCYCLIC PROTEIN KINASE
REMARK 900 INHIBITORS
REMARK 900 RELATED ID: 3ZO4 RELATED DB: PDB
REMARK 900 THE SYNTHESIS AND EVALUATION OF DIAZASPIROCYCLIC PROTEIN KINASE
REMARK 900 INHIBITORS
DBREF 3ZO1 A 0 350 UNP P00517 KAPCA_BOVIN 1 351
DBREF 3ZO1 I 5 22 UNP Q3SX13 IPKA_BOVIN 6 23
SEQRES 1 A 351 MET GLY ASN ALA ALA ALA ALA LYS LYS GLY SER GLU GLN
SEQRES 2 A 351 GLU SER VAL LYS GLU PHE LEU ALA LYS ALA LYS GLU ASP
SEQRES 3 A 351 PHE LEU LYS LYS TRP GLU ASN PRO ALA GLN ASN THR ALA
SEQRES 4 A 351 HIS LEU ASP GLN PHE GLU ARG ILE LYS THR LEU GLY THR
SEQRES 5 A 351 GLY SER PHE GLY ARG VAL MET LEU VAL LYS HIS MET GLU
SEQRES 6 A 351 THR GLY ASN HIS TYR ALA MET LYS ILE LEU ASP LYS GLN
SEQRES 7 A 351 LYS VAL VAL LYS LEU LYS GLN ILE GLU HIS THR LEU ASN
SEQRES 8 A 351 GLU LYS ARG ILE LEU GLN ALA VAL ASN PHE PRO PHE LEU
SEQRES 9 A 351 VAL LYS LEU GLU PHE SER PHE LYS ASP ASN SER ASN LEU
SEQRES 10 A 351 TYR MET VAL MET GLU TYR VAL PRO GLY GLY GLU MET PHE
SEQRES 11 A 351 SER HIS LEU ARG ARG ILE GLY ARG PHE SEP GLU PRO HIS
SEQRES 12 A 351 ALA ARG PHE TYR ALA ALA GLN ILE VAL LEU THR PHE GLU
SEQRES 13 A 351 TYR LEU HIS SER LEU ASP LEU ILE TYR ARG ASP LEU LYS
SEQRES 14 A 351 PRO GLU ASN LEU LEU ILE ASP GLN GLN GLY TYR ILE GLN
SEQRES 15 A 351 VAL THR ASP PHE GLY PHE ALA LYS ARG VAL LYS GLY ARG
SEQRES 16 A 351 THR TRP TPO LEU CYS GLY THR PRO GLU TYR LEU ALA PRO
SEQRES 17 A 351 GLU ILE ILE LEU SER LYS GLY TYR ASN LYS ALA VAL ASP
SEQRES 18 A 351 TRP TRP ALA LEU GLY VAL LEU ILE TYR GLU MET ALA ALA
SEQRES 19 A 351 GLY TYR PRO PRO PHE PHE ALA ASP GLN PRO ILE GLN ILE
SEQRES 20 A 351 TYR GLU LYS ILE VAL SER GLY LYS VAL ARG PHE PRO SER
SEQRES 21 A 351 HIS PHE SER SER ASP LEU LYS ASP LEU LEU ARG ASN LEU
SEQRES 22 A 351 LEU GLN VAL ASP LEU THR LYS ARG PHE GLY ASN LEU LYS
SEQRES 23 A 351 ASN GLY VAL ASN ASP ILE LYS ASN HIS LYS TRP PHE ALA
SEQRES 24 A 351 THR THR ASP TRP ILE ALA ILE TYR GLN ARG LYS VAL GLU
SEQRES 25 A 351 ALA PRO PHE ILE PRO LYS PHE LYS GLY PRO GLY ASP THR
SEQRES 26 A 351 SER ASN PHE ASP ASP TYR GLU GLU GLU GLU ILE ARG VAL
SEQRES 27 A 351 SEP ILE ASN GLU LYS CYS GLY LYS GLU PHE SER GLU PHE
SEQRES 1 I 18 THR THR TYR ALA ASP PHE ILE ALA SER GLY ARG THR GLY
SEQRES 2 I 18 ARG ARG ASN ALA ILE
MODRES 3ZO1 SEP A 139 SER PHOSPHOSERINE
MODRES 3ZO1 TPO A 197 THR PHOSPHOTHREONINE
MODRES 3ZO1 SEP A 338 SER PHOSPHOSERINE
HET SEP A 139 10
HET TPO A 197 11
HET SEP A 338 10
HET SIJ A1351 20
HET GOL A1352 6
HET GOL A1353 6
HET GOL A1354 6
HET GOL A1355 6
HET MOH A1356 2
HET MOH A1357 2
HETNAM SEP PHOSPHOSERINE
HETNAM TPO PHOSPHOTHREONINE
HETNAM SIJ 6-(1,9-DIAZASPIRO[5.5]UNDECAN-9-YL)-9H-PURINE
HETNAM GOL GLYCEROL
HETNAM MOH METHANOL
HETSYN SEP PHOSPHONOSERINE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 SIJ C14 H20 N6
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 8 MOH 2(C H4 O)
FORMUL 10 HOH *398(H2 O)
HELIX 1 1 SER A 10 ASN A 32 1 23
HELIX 2 2 HIS A 39 ASP A 41 5 3
HELIX 3 3 LYS A 76 LEU A 82 1 7
HELIX 4 4 GLN A 84 VAL A 98 1 15
HELIX 5 5 GLU A 127 GLY A 136 1 10
HELIX 6 6 SEP A 139 LEU A 160 1 22
HELIX 7 7 LYS A 168 GLU A 170 5 3
HELIX 8 8 THR A 201 LEU A 205 5 5
HELIX 9 9 ALA A 206 LEU A 211 1 6
HELIX 10 10 LYS A 217 GLY A 234 1 18
HELIX 11 11 GLN A 242 SER A 252 1 11
HELIX 12 12 SER A 262 LEU A 273 1 12
HELIX 13 13 VAL A 288 ASN A 293 1 6
HELIX 14 14 HIS A 294 ALA A 298 5 5
HELIX 15 15 ASP A 301 GLN A 307 1 7
HELIX 16 16 THR I 5 ALA I 12 1 8
SHEET 1 AA 5 PHE A 43 THR A 51 0
SHEET 2 AA 5 ARG A 56 HIS A 62 -1 O VAL A 57 N LEU A 49
SHEET 3 AA 5 ASN A 67 ASP A 75 -1 O ASN A 67 N HIS A 62
SHEET 4 AA 5 ASN A 115 GLU A 121 -1 O LEU A 116 N LEU A 74
SHEET 5 AA 5 LEU A 106 LYS A 111 -1 N GLU A 107 O VAL A 119
SHEET 1 AB 2 LEU A 162 ILE A 163 0
SHEET 2 AB 2 LYS A 189 ARG A 190 -1 O LYS A 189 N ILE A 163
SHEET 1 AC 2 LEU A 172 ILE A 174 0
SHEET 2 AC 2 ILE A 180 VAL A 182 -1 O GLN A 181 N LEU A 173
LINK C PHE A 138 N SEP A 139 1555 1555 1.36
LINK C SEP A 139 N GLU A 140 1555 1555 1.34
LINK C TRP A 196 N TPO A 197 1555 1555 1.32
LINK C TPO A 197 N LEU A 198 1555 1555 1.33
LINK C VAL A 337 N SEP A 338 1555 1555 1.34
LINK C SEP A 338 N ILE A 339 1555 1555 1.35
SITE 1 AC1 14 VAL A 57 ALA A 70 VAL A 104 GLU A 121
SITE 2 AC1 14 TYR A 122 VAL A 123 GLU A 127 GLU A 170
SITE 3 AC1 14 ASN A 171 LEU A 173 ASP A 184 PHE A 327
SITE 4 AC1 14 HOH A2224 HOH A2366
SITE 1 AC2 3 ARG A 134 ILE A 135 HOH A2245
SITE 1 AC3 5 VAL A 15 PHE A 18 GLU A 155 HOH A2326
SITE 2 AC3 5 HOH A2367
SITE 1 AC4 4 SER A 263 LYS A 266 ARG A 270 HOH A2300
SITE 1 AC5 3 HIS A 131 ARG A 134 HOH A2185
CRYST1 72.940 76.350 80.570 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 0.013710 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013098 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012412 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
