HEADER TRANSFERASE 07-JAN-09 3FQH
TITLE CRYSTAL STRUCTURE OF SPLEEN TYROSINE KINASE COMPLEXED WITH A 2-
TITLE 2 SUBSTITUTED 7-AZAINDOLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE SYK;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 365-635, PROTEIN KINASE DOMAIN;
COMPND 5 SYNONYM: SPLEEN TYROSINE KINASE;
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;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS SYK, SPLEEN TYPROSINE KINASE, KINASE INHIBITOR, 7-AZAINDOLE,
KEYWDS 2 ALTERNATIVE SPLICING, ATP-BINDING, HOST-VIRUS INTERACTION, KINASE,
KEYWDS 3 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, POLYMORPHISM, SH2 DOMAIN,
KEYWDS 4 TRANSFERASE, TYROSINE-PROTEIN KINASE, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KUGLSTATTER,A.G.VILLASENOR
REVDAT 4 06-SEP-23 3FQH 1 REMARK SEQADV
REVDAT 3 24-JUL-19 3FQH 1 REMARK
REVDAT 2 31-MAR-09 3FQH 1 JRNL
REVDAT 1 10-MAR-09 3FQH 0
JRNL AUTH A.G.VILLASENOR,R.KONDRU,H.HO,S.WANG,E.PAPP,D.SHAW,
JRNL AUTH 2 J.W.BARNETT,M.F.BROWNER,A.KUGLSTATTER
JRNL TITL STRUCTURAL INSIGHTS FOR DESIGN OF POTENT SPLEEN TYROSINE
JRNL TITL 2 KINASE INHIBITORS FROM CRYSTALLOGRAPHIC ANALYSIS OF THREE
JRNL TITL 3 INHIBITOR COMPLEXES.
JRNL REF CHEM.BIOL.DRUG DES. V. 73 466 2009
JRNL REFN ISSN 1747-0277
JRNL PMID 19220318
JRNL DOI 10.1111/J.1747-0285.2009.00785.X
REMARK 2
REMARK 2 RESOLUTION. 2.26 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.26
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 3 NUMBER OF REFLECTIONS : 22847
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.259
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1222
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) : 2.26
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1056
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.3360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4247
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 54
REMARK 3 SOLVENT ATOMS : 108
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.26000
REMARK 3 B22 (A**2) : 3.51000
REMARK 3 B33 (A**2) : -2.08000
REMARK 3 B12 (A**2) : -0.02000
REMARK 3 B13 (A**2) : -0.13000
REMARK 3 B23 (A**2) : -0.50000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.464
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.268
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.195
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4401 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5934 ; 1.317 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 513 ; 5.714 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 200 ;36.801 ;24.050
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 811 ;15.924 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;22.750 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 620 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3272 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1907 ; 0.189 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2948 ; 0.301 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 180 ; 0.145 ; 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): 45 ; 0.188 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 13 ; 0.122 ; 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): 2675 ; 0.680 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4140 ; 1.206 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2088 ; 1.289 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1794 ; 2.021 ; 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3FQH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000050915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ALS
REMARK 200 BEAMLINE : 5.0.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24069
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
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 (%) : 92.4
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.04700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.28000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1XBB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 4000, 0.2M AMMONIUM SULFATE,
REMARK 280 0.1M HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 283K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: B
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 353
REMARK 465 ALA A 354
REMARK 465 LEU 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 SER A 379
REMARK 465 GLY A 380
REMARK 465 ASN A 381
REMARK 465 PHE A 382
REMARK 465 GLY A 383
REMARK 465 ASN A 406
REMARK 465 GLU A 407
REMARK 465 ALA A 408
REMARK 465 ASN A 409
REMARK 465 ASP A 410
REMARK 465 ASN A 635
REMARK 465 GLU A 636
REMARK 465 GLY A 637
REMARK 465 HIS A 638
REMARK 465 HIS A 639
REMARK 465 HIS A 640
REMARK 465 HIS A 641
REMARK 465 HIS A 642
REMARK 465 HIS A 643
REMARK 465 MET B 353
REMARK 465 ALA B 354
REMARK 465 LEU B 355
REMARK 465 GLU B 356
REMARK 465 GLU B 357
REMARK 465 ILE B 358
REMARK 465 ARG B 359
REMARK 465 PRO B 360
REMARK 465 LYS B 361
REMARK 465 GLU B 362
REMARK 465 GLY B 380
REMARK 465 ASN B 381
REMARK 465 PHE B 382
REMARK 465 GLY B 383
REMARK 465 ASN B 406
REMARK 465 GLU B 407
REMARK 465 ALA B 408
REMARK 465 ASN B 409
REMARK 465 ASP B 410
REMARK 465 GLN B 529
REMARK 465 THR B 530
REMARK 465 HIS B 531
REMARK 465 GLY B 532
REMARK 465 VAL B 634
REMARK 465 ASN B 635
REMARK 465 GLU B 636
REMARK 465 GLY B 637
REMARK 465 HIS B 638
REMARK 465 HIS B 639
REMARK 465 HIS B 640
REMARK 465 HIS B 641
REMARK 465 HIS B 642
REMARK 465 HIS B 643
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 THR A 530 OG1 CG2
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 MET A 392 -147.49 -99.49
REMARK 500 LYS A 394 -25.45 -145.47
REMARK 500 ALA A 441 -132.26 -142.31
REMARK 500 ASP A 494 35.47 -147.33
REMARK 500 ASP A 512 83.39 56.01
REMARK 500 THR A 530 133.65 60.36
REMARK 500 LYS B 394 -50.83 -152.67
REMARK 500 ALA B 441 -129.94 -158.58
REMARK 500 ASP B 494 37.10 -148.69
REMARK 500 ASP B 512 83.05 61.05
REMARK 500 TRP B 609 30.31 -92.90
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 057 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 057 B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FQE RELATED DB: PDB
REMARK 900 RELATED ID: 3FQS RELATED DB: PDB
DBREF 3FQH A 356 635 UNP P43405 KSYK_HUMAN 356 635
DBREF 3FQH B 356 635 UNP P43405 KSYK_HUMAN 356 635
SEQADV 3FQH MET A 353 UNP P43405 EXPRESSION TAG
SEQADV 3FQH ALA A 354 UNP P43405 EXPRESSION TAG
SEQADV 3FQH LEU A 355 UNP P43405 EXPRESSION TAG
SEQADV 3FQH GLU A 636 UNP P43405 EXPRESSION TAG
SEQADV 3FQH GLY A 637 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS A 638 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS A 639 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS A 640 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS A 641 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS A 642 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS A 643 UNP P43405 EXPRESSION TAG
SEQADV 3FQH MET B 353 UNP P43405 EXPRESSION TAG
SEQADV 3FQH ALA B 354 UNP P43405 EXPRESSION TAG
SEQADV 3FQH LEU B 355 UNP P43405 EXPRESSION TAG
SEQADV 3FQH GLU B 636 UNP P43405 EXPRESSION TAG
SEQADV 3FQH GLY B 637 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS B 638 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS B 639 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS B 640 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS B 641 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS B 642 UNP P43405 EXPRESSION TAG
SEQADV 3FQH HIS B 643 UNP P43405 EXPRESSION TAG
SEQRES 1 A 291 MET ALA LEU GLU GLU ILE ARG PRO LYS GLU VAL TYR LEU
SEQRES 2 A 291 ASP ARG LYS LEU LEU THR LEU GLU ASP LYS GLU LEU GLY
SEQRES 3 A 291 SER GLY ASN PHE GLY THR VAL LYS LYS GLY TYR TYR GLN
SEQRES 4 A 291 MET LYS LYS VAL VAL LYS THR VAL ALA VAL LYS ILE LEU
SEQRES 5 A 291 LYS ASN GLU ALA ASN ASP PRO ALA LEU LYS ASP GLU LEU
SEQRES 6 A 291 LEU ALA GLU ALA ASN VAL MET GLN GLN LEU ASP ASN PRO
SEQRES 7 A 291 TYR ILE VAL ARG MET ILE GLY ILE CYS GLU ALA GLU SER
SEQRES 8 A 291 TRP MET LEU VAL MET GLU MET ALA GLU LEU GLY PRO LEU
SEQRES 9 A 291 ASN LYS TYR LEU GLN GLN ASN ARG HIS VAL LYS ASP LYS
SEQRES 10 A 291 ASN ILE ILE GLU LEU VAL HIS GLN VAL SER MET GLY MET
SEQRES 11 A 291 LYS TYR LEU GLU GLU SER ASN PHE VAL HIS ARG ASP LEU
SEQRES 12 A 291 ALA ALA ARG ASN VAL LEU LEU VAL THR GLN HIS TYR ALA
SEQRES 13 A 291 LYS ILE SER ASP PHE GLY LEU SER LYS ALA LEU ARG ALA
SEQRES 14 A 291 ASP GLU ASN TYR TYR LYS ALA GLN THR HIS GLY LYS TRP
SEQRES 15 A 291 PRO VAL LYS TRP TYR ALA PRO GLU CYS ILE ASN TYR TYR
SEQRES 16 A 291 LYS PHE SER SER LYS SER ASP VAL TRP SER PHE GLY VAL
SEQRES 17 A 291 LEU MET TRP GLU ALA PHE SER TYR GLY GLN LYS PRO TYR
SEQRES 18 A 291 ARG GLY MET LYS GLY SER GLU VAL THR ALA MET LEU GLU
SEQRES 19 A 291 LYS GLY GLU ARG MET GLY CYS PRO ALA GLY CYS PRO ARG
SEQRES 20 A 291 GLU MET TYR ASP LEU MET ASN LEU CYS TRP THR TYR ASP
SEQRES 21 A 291 VAL GLU ASN ARG PRO GLY PHE ALA ALA VAL GLU LEU ARG
SEQRES 22 A 291 LEU ARG ASN TYR TYR TYR ASP VAL VAL ASN GLU GLY HIS
SEQRES 23 A 291 HIS HIS HIS HIS HIS
SEQRES 1 B 291 MET ALA LEU GLU GLU ILE ARG PRO LYS GLU VAL TYR LEU
SEQRES 2 B 291 ASP ARG LYS LEU LEU THR LEU GLU ASP LYS GLU LEU GLY
SEQRES 3 B 291 SER GLY ASN PHE GLY THR VAL LYS LYS GLY TYR TYR GLN
SEQRES 4 B 291 MET LYS LYS VAL VAL LYS THR VAL ALA VAL LYS ILE LEU
SEQRES 5 B 291 LYS ASN GLU ALA ASN ASP PRO ALA LEU LYS ASP GLU LEU
SEQRES 6 B 291 LEU ALA GLU ALA ASN VAL MET GLN GLN LEU ASP ASN PRO
SEQRES 7 B 291 TYR ILE VAL ARG MET ILE GLY ILE CYS GLU ALA GLU SER
SEQRES 8 B 291 TRP MET LEU VAL MET GLU MET ALA GLU LEU GLY PRO LEU
SEQRES 9 B 291 ASN LYS TYR LEU GLN GLN ASN ARG HIS VAL LYS ASP LYS
SEQRES 10 B 291 ASN ILE ILE GLU LEU VAL HIS GLN VAL SER MET GLY MET
SEQRES 11 B 291 LYS TYR LEU GLU GLU SER ASN PHE VAL HIS ARG ASP LEU
SEQRES 12 B 291 ALA ALA ARG ASN VAL LEU LEU VAL THR GLN HIS TYR ALA
SEQRES 13 B 291 LYS ILE SER ASP PHE GLY LEU SER LYS ALA LEU ARG ALA
SEQRES 14 B 291 ASP GLU ASN TYR TYR LYS ALA GLN THR HIS GLY LYS TRP
SEQRES 15 B 291 PRO VAL LYS TRP TYR ALA PRO GLU CYS ILE ASN TYR TYR
SEQRES 16 B 291 LYS PHE SER SER LYS SER ASP VAL TRP SER PHE GLY VAL
SEQRES 17 B 291 LEU MET TRP GLU ALA PHE SER TYR GLY GLN LYS PRO TYR
SEQRES 18 B 291 ARG GLY MET LYS GLY SER GLU VAL THR ALA MET LEU GLU
SEQRES 19 B 291 LYS GLY GLU ARG MET GLY CYS PRO ALA GLY CYS PRO ARG
SEQRES 20 B 291 GLU MET TYR ASP LEU MET ASN LEU CYS TRP THR TYR ASP
SEQRES 21 B 291 VAL GLU ASN ARG PRO GLY PHE ALA ALA VAL GLU LEU ARG
SEQRES 22 B 291 LEU ARG ASN TYR TYR TYR ASP VAL VAL ASN GLU GLY HIS
SEQRES 23 B 291 HIS HIS HIS HIS HIS
HET 057 A 1 27
HET 057 B 2 27
HETNAM 057 N-(2-HYDROXY-1,1-DIMETHYLETHYL)-1-METHYL-3-(1H-
HETNAM 2 057 PYRROLO[2,3-B]PYRIDIN-2-YL)-1H-INDOLE-5-CARBOXAMIDE
FORMUL 3 057 2(C21 H22 N4 O2)
FORMUL 5 HOH *108(H2 O)
HELIX 1 1 ASP A 366 LYS A 368 5 3
HELIX 2 2 PRO A 411 GLN A 426 1 16
HELIX 3 3 LEU A 456 ASN A 463 1 8
HELIX 4 4 LYS A 467 SER A 488 1 22
HELIX 5 5 ALA A 496 ARG A 498 5 3
HELIX 6 6 PRO A 535 TYR A 539 5 5
HELIX 7 7 ALA A 540 TYR A 547 1 8
HELIX 8 8 SER A 551 SER A 567 1 17
HELIX 9 9 LYS A 577 LYS A 587 1 11
HELIX 10 10 PRO A 598 TRP A 609 1 12
HELIX 11 11 ASP A 612 ARG A 616 5 5
HELIX 12 12 GLY A 618 VAL A 634 1 17
HELIX 13 13 PRO B 411 LEU B 427 1 17
HELIX 14 14 LEU B 456 ASN B 463 1 8
HELIX 15 15 LYS B 467 SER B 488 1 22
HELIX 16 16 ALA B 496 ARG B 498 5 3
HELIX 17 17 PRO B 535 TYR B 539 5 5
HELIX 18 18 ALA B 540 TYR B 547 1 8
HELIX 19 19 SER B 550 SER B 567 1 18
HELIX 20 20 LYS B 577 LYS B 587 1 11
HELIX 21 21 PRO B 598 TRP B 609 1 12
HELIX 22 22 GLY B 618 TYR B 631 1 14
SHEET 1 A 5 LEU A 370 GLU A 376 0
SHEET 2 A 5 VAL A 385 GLN A 391 -1 O TYR A 389 N THR A 371
SHEET 3 A 5 VAL A 396 ILE A 403 -1 O VAL A 401 N LYS A 386
SHEET 4 A 5 TRP A 444 GLU A 449 -1 O LEU A 446 N LYS A 402
SHEET 5 A 5 MET A 435 GLU A 440 -1 N GLY A 437 O VAL A 447
SHEET 1 B 4 LEU A 370 GLU A 376 0
SHEET 2 B 4 VAL A 385 GLN A 391 -1 O TYR A 389 N THR A 371
SHEET 3 B 4 VAL A 396 ILE A 403 -1 O VAL A 401 N LYS A 386
SHEET 4 B 4 GLU B 589 ARG B 590 -1 O ARG B 590 N VAL A 396
SHEET 1 C 3 GLY A 454 PRO A 455 0
SHEET 2 C 3 VAL A 500 THR A 504 -1 O LEU A 502 N GLY A 454
SHEET 3 C 3 TYR A 507 ILE A 510 -1 O LYS A 509 N LEU A 501
SHEET 1 D 2 PHE A 490 VAL A 491 0
SHEET 2 D 2 LYS A 517 ALA A 518 -1 O LYS A 517 N VAL A 491
SHEET 1 E 2 TYR A 525 LYS A 527 0
SHEET 2 E 2 LYS A 548 SER A 550 -1 O PHE A 549 N TYR A 526
SHEET 1 F 5 LEU B 370 GLY B 378 0
SHEET 2 F 5 VAL B 385 GLN B 391 -1 O VAL B 385 N GLY B 378
SHEET 3 F 5 VAL B 396 ILE B 403 -1 O LYS B 397 N TYR B 390
SHEET 4 F 5 MET B 445 GLU B 449 -1 O MET B 448 N ALA B 400
SHEET 5 F 5 MET B 435 CYS B 439 -1 N ILE B 436 O VAL B 447
SHEET 1 G 3 GLY B 454 PRO B 455 0
SHEET 2 G 3 VAL B 500 THR B 504 -1 O LEU B 502 N GLY B 454
SHEET 3 G 3 TYR B 507 ILE B 510 -1 O LYS B 509 N LEU B 501
SHEET 1 H 2 PHE B 490 VAL B 491 0
SHEET 2 H 2 LYS B 517 ALA B 518 -1 O LYS B 517 N VAL B 491
SHEET 1 I 2 TYR B 526 LYS B 527 0
SHEET 2 I 2 LYS B 548 PHE B 549 -1 O PHE B 549 N TYR B 526
SITE 1 AC1 11 LEU A 377 GLY A 378 ALA A 400 GLU A 449
SITE 2 AC1 11 ALA A 451 GLU A 452 GLY A 454 PRO A 455
SITE 3 AC1 11 LYS A 458 LEU A 501 HOH A1043
SITE 1 AC2 10 GLY B 378 SER B 379 ALA B 400 GLU B 449
SITE 2 AC2 10 ALA B 451 GLU B 452 GLY B 454 PRO B 455
SITE 3 AC2 10 LYS B 458 LEU B 501
CRYST1 40.156 41.949 87.604 80.78 90.78 79.59 P 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 0.024903 -0.004576 0.001111 0.00000
SCALE2 0.000000 0.024238 -0.004064 0.00000
SCALE3 0.000000 0.000000 0.011575 0.00000
(ATOM LINES ARE NOT SHOWN.)
END