HEADER TRANSFERASE 26-JAN-09 3FZT
TITLE CRYSTAL STRUCTURE OF PYK2 COMPLEXED WITH PF-4618433
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE KINASE 2 BETA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 416-692, PROTEIN KINASE DOMAIN;
COMPND 5 SYNONYM: FOCAL ADHESION KINASE 2, FADK 2, PROLINE-RICH TYROSINE
COMPND 6 KINASE 2, CELL ADHESION KINASE BETA, CAK BETA, CALCIUM-DEPENDENT
COMPND 7 TYROSINE KINASE, CADTK, RELATED ADHESION FOCAL TYROSINE KINASE,
COMPND 8 RAFTK;
COMPND 9 EC: 2.7.10.2
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PYK2, KINASE, DFG, ALTERNATIVE SPLICING, ATP-BINDING, CELL MEMBRANE,
KEYWDS 2 CYTOPLASM, MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,
KEYWDS 3 POLYMORPHISM, TRANSFERASE, TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HAN
REVDAT 3 21-FEB-24 3FZT 1 REMARK
REVDAT 2 19-JAN-10 3FZT 1 JRNL
REVDAT 1 31-MAR-09 3FZT 0
JRNL AUTH S.HAN,A.MISTRY,J.S.CHANG,D.CUNNINGHAM,M.GRIFFOR,
JRNL AUTH 2 P.C.BONNETTE,H.WANG,B.A.CHRUNYK,G.E.ASPNES,D.P.WALKER,
JRNL AUTH 3 A.D.BROSIUS,L.BUCKBINDER
JRNL TITL STRUCTURAL CHARACTERIZATION OF PROLINE-RICH TYROSINE KINASE
JRNL TITL 2 2 (PYK2) REVEALS A UNIQUE (DFG-OUT) CONFORMATION AND ENABLES
JRNL TITL 3 INHIBITOR DESIGN.
JRNL REF J.BIOL.CHEM. V. 284 13193 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19244237
JRNL DOI 10.1074/JBC.M809038200
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.3.0008
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.1
REMARK 3 NUMBER OF REFLECTIONS : 18100
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 979
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1011
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 70.23
REMARK 3 BIN R VALUE (WORKING SET) : 0.1870
REMARK 3 BIN FREE R VALUE SET COUNT : 46
REMARK 3 BIN FREE R VALUE : 0.2080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2101
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 196
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.78000
REMARK 3 B22 (A**2) : -0.42000
REMARK 3 B33 (A**2) : 1.20000
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): 0.205
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.416
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.910
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2185 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2958 ; 1.385 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 256 ; 5.314 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 96 ;34.152 ;24.167
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 393 ;15.189 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.126 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 323 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1631 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1030 ; 0.198 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1506 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 166 ; 0.170 ; 0.200
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): 32 ; 0.171 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.189 ; 0.200
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): 1342 ; 0.863 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2103 ; 1.378 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 987 ; 2.142 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 855 ; 3.169 ; 4.500
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3FZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
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 : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19176
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.3
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 75.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.27000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, 0.2M MGCL2, 20-27%
REMARK 280 PEG3350, 1MM TCEP, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
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 18.85650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.22100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.45750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.22100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.85650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.45750
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 PRO A 416
REMARK 465 GLN A 417
REMARK 465 TYR A 418
REMARK 465 GLY A 419
REMARK 465 TYR A 573
REMARK 465 ILE A 574
REMARK 465 GLU A 575
REMARK 465 ASP A 578
REMARK 465 TYR A 579
REMARK 465 TYR A 580
REMARK 465 LYS A 581
REMARK 465 ALA A 582
REMARK 465 SER A 583
REMARK 465 VAL A 584
REMARK 465 THR A 585
REMARK 465 ARG A 586
REMARK 465 MET A 691
REMARK 465 GLU A 692
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 671 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 671 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 ARG A 548 -11.43 78.50
REMARK 500 ASP A 549 43.67 -142.89
REMARK 500 PHE A 568 17.05 -140.66
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 4JZ A 999
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FZO RELATED DB: PDB
REMARK 900 PYK2 APO
REMARK 900 RELATED ID: 3FZP RELATED DB: PDB
REMARK 900 PYK2 COMPLEXED WITH ATPGS
REMARK 900 RELATED ID: 3FZR RELATED DB: PDB
REMARK 900 PYK2 COMPLEXED WITH PF-431396
REMARK 900 RELATED ID: 3FZS RELATED DB: PDB
REMARK 900 PYK2 COMPLEXED WITH BIRB796
DBREF 3FZT A 416 692 UNP Q14289 FAK2_HUMAN 416 692
SEQRES 1 A 277 PRO GLN TYR GLY ILE ALA ARG GLU ASP VAL VAL LEU ASN
SEQRES 2 A 277 ARG ILE LEU GLY GLU GLY PHE PHE GLY GLU VAL TYR GLU
SEQRES 3 A 277 GLY VAL TYR THR ASN HIS LYS GLY GLU LYS ILE ASN VAL
SEQRES 4 A 277 ALA VAL LYS THR CYS LYS LYS ASP CYS THR LEU ASP ASN
SEQRES 5 A 277 LYS GLU LYS PHE MET SER GLU ALA VAL ILE MET LYS ASN
SEQRES 6 A 277 LEU ASP HIS PRO HIS ILE VAL LYS LEU ILE GLY ILE ILE
SEQRES 7 A 277 GLU GLU GLU PRO THR TRP ILE ILE MET GLU LEU TYR PRO
SEQRES 8 A 277 TYR GLY GLU LEU GLY HIS TYR LEU GLU ARG ASN LYS ASN
SEQRES 9 A 277 SER LEU LYS VAL LEU THR LEU VAL LEU TYR SER LEU GLN
SEQRES 10 A 277 ILE CYS LYS ALA MET ALA TYR LEU GLU SER ILE ASN CYS
SEQRES 11 A 277 VAL HIS ARG ASP ILE ALA VAL ARG ASN ILE LEU VAL ALA
SEQRES 12 A 277 SER PRO GLU CYS VAL LYS LEU GLY ASP PHE GLY LEU SER
SEQRES 13 A 277 ARG TYR ILE GLU ASP GLU ASP TYR TYR LYS ALA SER VAL
SEQRES 14 A 277 THR ARG LEU PRO ILE LYS TRP MET SER PRO GLU SER ILE
SEQRES 15 A 277 ASN PHE ARG ARG PHE THR THR ALA SER ASP VAL TRP MET
SEQRES 16 A 277 PHE ALA VAL CYS MET TRP GLU ILE LEU SER PHE GLY LYS
SEQRES 17 A 277 GLN PRO PHE PHE TRP LEU GLU ASN LYS ASP VAL ILE GLY
SEQRES 18 A 277 VAL LEU GLU LYS GLY ASP ARG LEU PRO LYS PRO ASP LEU
SEQRES 19 A 277 CYS PRO PRO VAL LEU TYR THR LEU MET THR ARG CYS TRP
SEQRES 20 A 277 ASP TYR ASP PRO SER ASP ARG PRO ARG PHE THR GLU LEU
SEQRES 21 A 277 VAL CYS SER LEU SER ASP VAL TYR GLN MET GLU LYS ASP
SEQRES 22 A 277 ILE ALA MET GLU
HET 4JZ A 999 33
HETNAM 4JZ 1-[5-TERT-BUTYL-2-(4-METHYLPHENYL)-1,2-DIHYDRO-3H-
HETNAM 2 4JZ PYRAZOL-3-YLIDENE]-3-{3-[(PYRIDIN-3-YLOXY)METHYL]-1H-
HETNAM 3 4JZ PYRAZOL-5-YL}UREA
FORMUL 2 4JZ C24 H27 N7 O2
FORMUL 3 HOH *196(H2 O)
HELIX 1 1 ALA A 421 GLU A 423 5 3
HELIX 2 2 THR A 464 LYS A 479 1 16
HELIX 3 3 GLU A 509 LYS A 518 1 10
HELIX 4 4 LYS A 522 ILE A 543 1 22
HELIX 5 5 ALA A 551 ARG A 553 5 3
HELIX 6 6 PRO A 588 MET A 592 5 5
HELIX 7 7 SER A 593 ARG A 600 1 8
HELIX 8 8 THR A 603 SER A 620 1 18
HELIX 9 9 GLU A 630 LYS A 632 5 3
HELIX 10 10 ASP A 633 LYS A 640 1 8
HELIX 11 11 PRO A 651 TRP A 662 1 12
HELIX 12 12 ASP A 665 ARG A 669 5 5
HELIX 13 13 ARG A 671 ALA A 690 1 20
SHEET 1 A 5 VAL A 425 GLU A 433 0
SHEET 2 A 5 GLU A 438 THR A 445 -1 O VAL A 439 N LEU A 431
SHEET 3 A 5 LYS A 451 LYS A 457 -1 O VAL A 456 N TYR A 440
SHEET 4 A 5 TRP A 499 GLU A 503 -1 O ILE A 500 N LYS A 457
SHEET 5 A 5 LEU A 489 ILE A 493 -1 N GLY A 491 O ILE A 501
SHEET 1 B 2 ILE A 555 SER A 559 0
SHEET 2 B 2 CYS A 562 LEU A 565 -1 O LYS A 564 N LEU A 556
CISPEP 1 GLU A 496 PRO A 497 0 -1.60
SITE 1 AC1 17 LYS A 457 SER A 473 GLU A 474 MET A 478
SITE 2 AC1 17 VAL A 487 MET A 502 GLU A 503 LEU A 504
SITE 3 AC1 17 TYR A 505 LEU A 556 LEU A 565 GLY A 566
SITE 4 AC1 17 ASP A 567 PHE A 568 ARG A 572 HOH A1011
SITE 5 AC1 17 HOH A1033
CRYST1 37.713 82.915 86.442 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 0.026516 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012061 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011568 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
