HEADER TRANSFERASE 04-APR-17 5VEE
TITLE PAK4 KINASE DOMAIN IN COMPLEX WITH FRAX486
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 286-591;
COMPND 5 SYNONYM: P21-ACTIVATED KINASE 4,PAK-4;
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: PAK4, KIAA1142;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RILP;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PET VECTOR
KEYWDS KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.Y.ZHANG,B.H.HA,T.J.BOGGON
REVDAT 5 04-OCT-23 5VEE 1 REMARK
REVDAT 4 26-FEB-20 5VEE 1 REMARK
REVDAT 3 01-JAN-20 5VEE 1 REMARK
REVDAT 2 03-JAN-18 5VEE 1 JRNL
REVDAT 1 18-OCT-17 5VEE 0
JRNL AUTH E.Y.ZHANG,B.H.HA,T.J.BOGGON
JRNL TITL PAK4 CRYSTAL STRUCTURES SUGGEST UNUSUAL KINASE
JRNL TITL 2 CONFORMATIONAL MOVEMENTS.
JRNL REF BIOCHIM. BIOPHYS. ACTA V.1866 356 2018
JRNL REFN ISSN 0006-3002
JRNL PMID 28993291
JRNL DOI 10.1016/J.BBAPAP.2017.10.004
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 12529
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) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 704
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 864
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.71
REMARK 3 BIN R VALUE (WORKING SET) : 0.4680
REMARK 3 BIN FREE R VALUE SET COUNT : 45
REMARK 3 BIN FREE R VALUE : 0.4650
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2295
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 115.5
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.21000
REMARK 3 B22 (A**2) : 3.21000
REMARK 3 B33 (A**2) : -6.41000
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): 0.499
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.305
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.335
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.485
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2382 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2296 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3231 ; 1.691 ; 2.003
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5317 ; 1.027 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 289 ; 7.061 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 101 ;34.657 ;23.366
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 422 ;15.884 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;19.275 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 359 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2587 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 465 ; 0.002 ; 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): 1159 ; 9.372 ;11.122
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1158 ; 9.369 ;11.118
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1447 ;13.355 ;16.667
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1448 ;13.351 ;16.672
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1223 ; 9.791 ;12.079
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1224 ; 9.787 ;12.083
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1785 ;14.492 ;17.704
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2645 ;18.984 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2646 ;18.980 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 5VEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227224.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-NOV-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97919
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13760
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 20.10
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.1000
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) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
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: 4FIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL (PH 7.5) AND 1.5 - 2.0
REMARK 280 M NA ACETATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 91.75450
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.47750
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.47750
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 45.87725
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.47750
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.47750
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 137.63175
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.47750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.47750
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 45.87725
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.47750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.47750
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 137.63175
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 91.75450
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 273
REMARK 465 ALA A 274
REMARK 465 ARG A 275
REMARK 465 ALA A 276
REMARK 465 ARG A 277
REMARK 465 GLN A 278
REMARK 465 GLU A 279
REMARK 465 ASN A 280
REMARK 465 GLY A 281
REMARK 465 MET A 282
REMARK 465 PRO A 283
REMARK 465 GLU A 284
REMARK 465 LYS A 285
REMARK 465 PRO A 286
REMARK 465 PRO A 287
REMARK 465 GLY A 288
REMARK 465 PRO A 289
REMARK 465 ARG A 290
REMARK 465 SER A 291
REMARK 465 PRO A 292
REMARK 465 GLN A 293
REMARK 465 ARG A 294
REMARK 465 GLU A 295
REMARK 465 PRO A 296
REMARK 465 GLN A 297
REMARK 465 ARG A 298
REMARK 465 VAL A 299
REMARK 465 THR A 590
REMARK 465 ARG A 591
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 GLU A 329 140.44 -172.45
REMARK 500 SER A 331 -48.69 68.78
REMARK 500 ASP A 372 -1.68 83.13
REMARK 500 ASP A 389 30.15 -91.10
REMARK 500 ASP A 440 43.91 -150.65
REMARK 500 LYS A 442 167.14 177.19
REMARK 500 ASP A 458 64.40 63.61
REMARK 500 ASN A 537 51.94 -93.17
REMARK 500 PHE A 548 -57.85 -29.51
REMARK 500 LEU A 553 44.33 -95.28
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 981 A 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VED RELATED DB: PDB
REMARK 900 RELATED ID: 5VEE RELATED DB: PDB
DBREF 5VEE A 286 591 UNP O96013 PAK4_HUMAN 286 591
SEQADV 5VEE GLY A 273 UNP O96013 EXPRESSION TAG
SEQADV 5VEE ALA A 274 UNP O96013 EXPRESSION TAG
SEQADV 5VEE ARG A 275 UNP O96013 EXPRESSION TAG
SEQADV 5VEE ALA A 276 UNP O96013 EXPRESSION TAG
SEQADV 5VEE ARG A 277 UNP O96013 EXPRESSION TAG
SEQADV 5VEE GLN A 278 UNP O96013 EXPRESSION TAG
SEQADV 5VEE GLU A 279 UNP O96013 EXPRESSION TAG
SEQADV 5VEE ASN A 280 UNP O96013 EXPRESSION TAG
SEQADV 5VEE GLY A 281 UNP O96013 EXPRESSION TAG
SEQADV 5VEE MET A 282 UNP O96013 EXPRESSION TAG
SEQADV 5VEE PRO A 283 UNP O96013 EXPRESSION TAG
SEQADV 5VEE GLU A 284 UNP O96013 EXPRESSION TAG
SEQADV 5VEE LYS A 285 UNP O96013 EXPRESSION TAG
SEQRES 1 A 319 GLY ALA ARG ALA ARG GLN GLU ASN GLY MET PRO GLU LYS
SEQRES 2 A 319 PRO PRO GLY PRO ARG SER PRO GLN ARG GLU PRO GLN ARG
SEQRES 3 A 319 VAL SER HIS GLU GLN PHE ARG ALA ALA LEU GLN LEU VAL
SEQRES 4 A 319 VAL ASP PRO GLY ASP PRO ARG SER TYR LEU ASP ASN PHE
SEQRES 5 A 319 ILE LYS ILE GLY GLU GLY SER THR GLY ILE VAL CYS ILE
SEQRES 6 A 319 ALA THR VAL ARG SER SER GLY LYS LEU VAL ALA VAL LYS
SEQRES 7 A 319 LYS MET ASP LEU ARG LYS GLN GLN ARG ARG GLU LEU LEU
SEQRES 8 A 319 PHE ASN GLU VAL VAL ILE MET ARG ASP TYR GLN HIS GLU
SEQRES 9 A 319 ASN VAL VAL GLU MET TYR ASN SER TYR LEU VAL GLY ASP
SEQRES 10 A 319 GLU LEU TRP VAL VAL MET GLU PHE LEU GLU GLY GLY ALA
SEQRES 11 A 319 LEU THR ASP ILE VAL THR HIS THR ARG MET ASN GLU GLU
SEQRES 12 A 319 GLN ILE ALA ALA VAL CYS LEU ALA VAL LEU GLN ALA LEU
SEQRES 13 A 319 SER VAL LEU HIS ALA GLN GLY VAL ILE HIS ARG ASP ILE
SEQRES 14 A 319 LYS SER ASP SER ILE LEU LEU THR HIS ASP GLY ARG VAL
SEQRES 15 A 319 LYS LEU SER ASP PHE GLY PHE CYS ALA GLN VAL SER LYS
SEQRES 16 A 319 GLU VAL PRO ARG ARG LYS SEP LEU VAL GLY THR PRO TYR
SEQRES 17 A 319 TRP MET ALA PRO GLU LEU ILE SER ARG LEU PRO TYR GLY
SEQRES 18 A 319 PRO GLU VAL ASP ILE TRP SER LEU GLY ILE MET VAL ILE
SEQRES 19 A 319 GLU MET VAL ASP GLY GLU PRO PRO TYR PHE ASN GLU PRO
SEQRES 20 A 319 PRO LEU LYS ALA MET LYS MET ILE ARG ASP ASN LEU PRO
SEQRES 21 A 319 PRO ARG LEU LYS ASN LEU HIS LYS VAL SER PRO SER LEU
SEQRES 22 A 319 LYS GLY PHE LEU ASP ARG LEU LEU VAL ARG ASP PRO ALA
SEQRES 23 A 319 GLN ARG ALA THR ALA ALA GLU LEU LEU LYS HIS PRO PHE
SEQRES 24 A 319 LEU ALA LYS ALA GLY PRO PRO ALA SER ILE VAL PRO LEU
SEQRES 25 A 319 MET ARG GLN ASN ARG THR ARG
MODRES 5VEE SEP A 474 SER MODIFIED RESIDUE
HET SEP A 474 10
HET 981 A 601 35
HETNAM SEP PHOSPHOSERINE
HETNAM 981 6-(2,4-DICHLOROPHENYL)-8-ETHYL-2-{[3-FLUORO-4-
HETNAM 2 981 (PIPERAZIN-1-YL)PHENYL]AMINO}PYRIDO[2,3-D]PYRIMIDIN-
HETNAM 3 981 7(8H)-ONE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 SEP C3 H8 N O6 P
FORMUL 2 981 C25 H23 CL2 F N6 O
HELIX 1 AA1 HIS A 301 VAL A 312 1 12
HELIX 2 AA2 ASP A 316 SER A 319 5 4
HELIX 3 AA3 ARG A 359 ARG A 371 1 13
HELIX 4 AA4 LEU A 403 THR A 410 1 8
HELIX 5 AA5 ASN A 413 GLN A 434 1 22
HELIX 6 AA6 LYS A 442 ASP A 444 5 3
HELIX 7 AA7 THR A 478 MET A 482 5 5
HELIX 8 AA8 ALA A 483 SER A 488 1 6
HELIX 9 AA9 GLU A 495 GLY A 511 1 17
HELIX 10 AB1 PRO A 519 ASN A 530 1 12
HELIX 11 AB2 ASN A 537 VAL A 541 5 5
HELIX 12 AB3 SER A 542 ARG A 551 1 10
HELIX 13 AB4 THR A 562 LEU A 567 1 6
HELIX 14 AB5 LYS A 568 ALA A 575 5 8
HELIX 15 AB6 PRO A 577 MET A 585 5 9
SHEET 1 AA1 5 LEU A 321 GLU A 329 0
SHEET 2 AA1 5 ILE A 334 VAL A 340 -1 O THR A 339 N ASP A 322
SHEET 3 AA1 5 LEU A 346 ASP A 353 -1 O VAL A 349 N CYS A 336
SHEET 4 AA1 5 GLU A 390 GLU A 396 -1 O VAL A 393 N LYS A 350
SHEET 5 AA1 5 MET A 381 VAL A 387 -1 N TYR A 382 O VAL A 394
SHEET 1 AA2 3 GLY A 401 ALA A 402 0
SHEET 2 AA2 3 ILE A 446 LEU A 448 -1 O LEU A 448 N GLY A 401
SHEET 3 AA2 3 VAL A 454 LEU A 456 -1 O LYS A 455 N LEU A 447
SHEET 1 AA3 2 VAL A 436 ILE A 437 0
SHEET 2 AA3 2 ALA A 463 GLN A 464 -1 O ALA A 463 N ILE A 437
LINK C LYS A 473 N SEP A 474 1555 1555 1.34
LINK C SEP A 474 N LEU A 475 1555 1555 1.33
SITE 1 AC1 10 VAL A 335 ALA A 348 VAL A 349 LYS A 350
SITE 2 AC1 10 GLU A 366 MET A 395 GLU A 396 LEU A 398
SITE 3 AC1 10 GLY A 401 ASP A 405
CRYST1 62.955 62.955 183.509 90.00 90.00 90.00 P 41 21 2 8
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 0.015884 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015884 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005449 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
