HEADER TRANSFERASE 03-MAR-15 4YJO
TITLE THE KINASE DOMAIN OF HUMAN SPLEEN TYROSINE (SYK) IN COMPLEX WITH
TITLE 2 GTC000222
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE SYK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 355-635;
COMPND 5 SYNONYM: SPLEEN TYROSINE KINASE,P72-SYK;
COMPND 6 EC: 2.7.10.2;
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: SYK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: SF9
KEYWDS SYK, NON-RECEPTOR TYROSINE KINASE, SPLEEN TYROSINE KINASE,
KEYWDS 2 TRANSFERASE, PHOSPHORYLATION, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.O.SOMERS,M.NEU
REVDAT 1 30-SEP-15 4YJO 0
JRNL AUTH J.LIDDLE,F.L.ATKINSON,M.D.BARKER,P.S.CARTER,N.R.CURTIS,
JRNL AUTH 2 R.P.DAVIS,C.DOUAULT,M.C.DICKSON,D.ELWES,N.S.GARTON,M.GRAY,
JRNL AUTH 3 T.G.HAYHOW,C.I.HOBBS,E.JONES,S.LEACH,K.LEAVENS,H.D.LEWIS,
JRNL AUTH 4 S.MCCLEARY,M.NEU,V.K.PATEL,A.G.PRESTON,C.RAMIREZ-MOLINA,
JRNL AUTH 5 T.J.SHIPLEY,P.A.SKONE,N.SMITHERS,D.O.SOMERS,A.L.WALKER,
JRNL AUTH 6 R.J.WATSON,G.G.WEINGARTEN
JRNL TITL DISCOVERY OF GSK143, A HIGHLY POTENT, SELECTIVE AND ORALLY
JRNL TITL 2 EFFICACIOUS SPLEEN TYROSINE KINASE INHIBITOR.
JRNL REF BIOORG. MED. CHEM. LETT. V. 21 6188 2011
JRNL REFN ESSN 1464-3405
JRNL PMID 21903390
JRNL DOI 10.1016/J.BMCL.2011.07.082
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 28936
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1539
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1968
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3770
REMARK 3 BIN FREE R VALUE SET COUNT : 116
REMARK 3 BIN FREE R VALUE : 0.4110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2171
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 37
REMARK 3 SOLVENT ATOMS : 235
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.35000
REMARK 3 B22 (A**2) : -2.93000
REMARK 3 B33 (A**2) : 4.99000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.88000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.113
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.114
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.542
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2281 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1573 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3079 ; 1.458 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 3825 ; 1.241 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 269 ; 4.507 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;32.168 ;24.393
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 415 ;11.888 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;18.882 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 315 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2501 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 472 ; 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 : NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4YJO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 6.2.4
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.5
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30502
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 28.784
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : 0.04800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.48800
REMARK 200 R SYM FOR SHELL (I) : 0.48800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600
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: IN-HOUSE SYK MODEL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% JEFFAMINE ED-2001, 10% GLYCEROL,
REMARK 280 0.1M MES PH6.8, 5MM TCEP, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 42.41050
REMARK 290 SMTRY3 2 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 TOTAL BURIED SURFACE AREA: 190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
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 355
REMARK 465 GLU A 356
REMARK 465 GLU A 357
REMARK 465 ILE A 358
REMARK 465 ARG A 359
REMARK 465 PRO A 360
REMARK 465 LYS A 361
REMARK 465 GLU A 362
REMARK 465 GLN A 529
REMARK 465 THR A 530
REMARK 465 HIS A 531
REMARK 465 VAL A 633
REMARK 465 VAL A 634
REMARK 465 ASN A 635
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1034 O HOH A 1035 2.01
REMARK 500 OH TYR A 525 O HOH A 1008 2.07
REMARK 500 OE2 GLU A 473 O HOH A 1004 2.11
REMARK 500
REMARK 500 REMARK: NULL
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 616 NE - CZ - NH2 ANGL. DEV. = -3.0 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 LYS A 394 -52.94 -139.35
REMARK 500 GLU A 407 43.41 38.97
REMARK 500 ALA A 441 -136.19 -128.65
REMARK 500 ASP A 494 41.25 -151.29
REMARK 500 ASP A 512 80.70 59.58
REMARK 500 TRP A 609 31.41 -91.53
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 4DF A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 702
DBREF 4YJO A 355 635 UNP P43405 KSYK_HUMAN 355 635
SEQRES 1 A 281 PRO GLU GLU ILE ARG PRO LYS GLU VAL TYR LEU ASP ARG
SEQRES 2 A 281 LYS LEU LEU THR LEU GLU ASP LYS GLU LEU GLY SER GLY
SEQRES 3 A 281 ASN PHE GLY THR VAL LYS LYS GLY TYR TYR GLN MET LYS
SEQRES 4 A 281 LYS VAL VAL LYS THR VAL ALA VAL LYS ILE LEU LYS ASN
SEQRES 5 A 281 GLU ALA ASN ASP PRO ALA LEU LYS ASP GLU LEU LEU ALA
SEQRES 6 A 281 GLU ALA ASN VAL MET GLN GLN LEU ASP ASN PRO TYR ILE
SEQRES 7 A 281 VAL ARG MET ILE GLY ILE CYS GLU ALA GLU SER TRP MET
SEQRES 8 A 281 LEU VAL MET GLU MET ALA GLU LEU GLY PRO LEU ASN LYS
SEQRES 9 A 281 TYR LEU GLN GLN ASN ARG HIS VAL LYS ASP LYS ASN ILE
SEQRES 10 A 281 ILE GLU LEU VAL HIS GLN VAL SER MET GLY MET LYS TYR
SEQRES 11 A 281 LEU GLU GLU SER ASN PHE VAL HIS ARG ASP LEU ALA ALA
SEQRES 12 A 281 ARG ASN VAL LEU LEU VAL THR GLN HIS TYR ALA LYS ILE
SEQRES 13 A 281 SER ASP PHE GLY LEU SER LYS ALA LEU ARG ALA ASP GLU
SEQRES 14 A 281 ASN TYR TYR LYS ALA GLN THR HIS GLY LYS TRP PRO VAL
SEQRES 15 A 281 LYS TRP TYR ALA PRO GLU CYS ILE ASN TYR TYR LYS PHE
SEQRES 16 A 281 SER SER LYS SER ASP VAL TRP SER PHE GLY VAL LEU MET
SEQRES 17 A 281 TRP GLU ALA PHE SER TYR GLY GLN LYS PRO TYR ARG GLY
SEQRES 18 A 281 MET LYS GLY SER GLU VAL THR ALA MET LEU GLU LYS GLY
SEQRES 19 A 281 GLU ARG MET GLY CYS PRO ALA GLY CYS PRO ARG GLU MET
SEQRES 20 A 281 TYR ASP LEU MET ASN LEU CYS TRP THR TYR ASP VAL GLU
SEQRES 21 A 281 ASN ARG PRO GLY PHE ALA ALA VAL GLU LEU ARG LEU ARG
SEQRES 22 A 281 ASN TYR TYR TYR ASP VAL VAL ASN
HET 4DF A 701 31
HET GOL A 702 6
HETNAM 4DF 5-CHLORO-N~2~-(1,1-DIOXIDO-2,3-DIHYDRO-1,2-
HETNAM 2 4DF BENZOTHIAZOL-6-YL)-N~4~-ETHYL-N~4~-(1H-INDAZOL-4-YL)
HETNAM 3 4DF PYRIMIDINE-2,4-DIAMINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 4DF C20 H18 CL N7 O2 S
FORMUL 3 GOL C3 H8 O3
FORMUL 4 HOH *235(H2 O)
HELIX 1 AA1 ASP A 366 LYS A 368 5 3
HELIX 2 AA2 ASN A 406 ASN A 409 5 4
HELIX 3 AA3 ASP A 410 LEU A 427 1 18
HELIX 4 AA4 LEU A 456 ASN A 463 1 8
HELIX 5 AA5 LYS A 467 SER A 488 1 22
HELIX 6 AA6 ALA A 496 ARG A 498 5 3
HELIX 7 AA7 PRO A 535 TYR A 539 5 5
HELIX 8 AA8 ALA A 540 TYR A 547 1 8
HELIX 9 AA9 SER A 550 SER A 567 1 18
HELIX 10 AB1 LYS A 577 LYS A 587 1 11
HELIX 11 AB2 PRO A 598 TRP A 609 1 12
HELIX 12 AB3 ASP A 612 ARG A 616 5 5
HELIX 13 AB4 GLY A 618 ASP A 632 1 15
SHEET 1 AA1 5 LEU A 370 GLY A 380 0
SHEET 2 AA1 5 GLY A 383 GLN A 391 -1 O LYS A 387 N GLU A 373
SHEET 3 AA1 5 VAL A 396 LEU A 404 -1 O ILE A 403 N THR A 384
SHEET 4 AA1 5 TRP A 444 GLU A 449 -1 O LEU A 446 N LYS A 402
SHEET 5 AA1 5 MET A 435 GLU A 440 -1 N GLY A 437 O VAL A 447
SHEET 1 AA2 3 GLY A 454 PRO A 455 0
SHEET 2 AA2 3 VAL A 500 THR A 504 -1 O LEU A 502 N GLY A 454
SHEET 3 AA2 3 TYR A 507 ILE A 510 -1 O LYS A 509 N LEU A 501
SHEET 1 AA3 2 PHE A 490 VAL A 491 0
SHEET 2 AA3 2 LYS A 517 ALA A 518 -1 O LYS A 517 N VAL A 491
SHEET 1 AA4 2 TYR A 526 LYS A 527 0
SHEET 2 AA4 2 LYS A 548 PHE A 549 -1 O PHE A 549 N TYR A 526
SITE 1 AC1 14 LEU A 377 GLY A 378 ALA A 400 LYS A 402
SITE 2 AC1 14 GLU A 420 VAL A 433 MET A 448 GLU A 449
SITE 3 AC1 14 MET A 450 ALA A 451 GLY A 454 PRO A 455
SITE 4 AC1 14 LEU A 501 ASP A 512
SITE 1 AC2 4 ASN A 406 GLN A 477 HIS A 506 HOH A 810
CRYST1 39.936 84.821 40.412 90.00 99.24 90.00 P 1 21 1 2
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 0.025040 0.000000 0.004072 0.00000
SCALE2 0.000000 0.011790 0.000000 0.00000
SCALE3 0.000000 0.000000 0.025070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
