HEADER TRANSFERASE/TRANSFERASE INHIBITOR 07-JUL-11 3SRV
TITLE CRYSTAL STRUCTURE OF SPLEEN TYROSINE KINASE (SYK) IN COMPLEX WITH A
TITLE 2 DIAMINOPYRIMIDINE CARBOXAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE SYK;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 360-635);
COMPND 5 SYNONYM: SPLEEN TYROSINE KINASE;
COMPND 6 EC: 2.7.10.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: TYROSINE-PROTEIN KINASE SYK;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 360-635);
COMPND 12 SYNONYM: SPLEEN TYROSINE KINASE;
COMPND 13 EC: 2.7.10.2;
COMPND 14 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_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 GENE: SYK;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 17 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS SK363, 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 3 03-APR-24 3SRV 1 REMARK SEQADV LINK
REVDAT 2 12-OCT-11 3SRV 1 JRNL
REVDAT 1 21-SEP-11 3SRV 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 ISSN 0960-894X
JRNL PMID 21903390
JRNL DOI 10.1016/J.BMCL.2011.07.082
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 38566
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1929
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) : 2725
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4292
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 472
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.71000
REMARK 3 B22 (A**2) : 1.61000
REMARK 3 B33 (A**2) : -1.06000
REMARK 3 B12 (A**2) : -1.13000
REMARK 3 B13 (A**2) : 0.19000
REMARK 3 B23 (A**2) : 0.69000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.194
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.174
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.137
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.875
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4477 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3081 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6029 ; 1.378 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7488 ; 0.881 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 525 ; 4.399 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 207 ;36.250 ;24.010
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 813 ;13.965 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;16.990 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 621 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4916 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 909 ; 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): 2615 ; 1.218 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1068 ; 0.245 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4191 ; 2.187 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1862 ; 2.875 ; 4.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1836 ; 4.399 ; 6.000
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 : 1.40
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3SRV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066574.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUN-10
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 : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38589
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 39.470
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
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) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.40200
REMARK 200 R SYM FOR SHELL (I) : 0.40200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: OTHER IN-HOUSE COORDINATES
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M NA-K-PHOSPHATE, 0.1M
REMARK 280 BIS-TRIS-PROPANE PH 6.5, 5MM DTT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 GLY A 359
REMARK 465 PRO A 360
REMARK 465 LYS A 361
REMARK 465 GLU A 362
REMARK 465 VAL A 363
REMARK 465 SER A 379
REMARK 465 GLY A 380
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 PRO A 411
REMARK 465 ASN A 635
REMARK 465 GLY B 359
REMARK 465 PRO B 360
REMARK 465 LYS B 361
REMARK 465 GLU B 362
REMARK 465 VAL B 363
REMARK 465 LYS B 405
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 VAL B 633
REMARK 465 VAL B 634
REMARK 465 ASN B 635
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 LYS B 533 CG CD CE NZ
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 B 118 O HOH B 146 2.07
REMARK 500 O HOH B 15 O HOH B 16 2.11
REMARK 500 O HOH A 118 O HOH A 216 2.16
REMARK 500 OD1 ASP A 468 O HOH A 206 2.18
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 ASP B 554 CB - CG - OD1 ANGL. DEV. = 5.7 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 393 -109.45 59.46
REMARK 500 ALA A 441 -136.35 -145.28
REMARK 500 ASP A 494 43.01 -150.11
REMARK 500 ASP A 512 72.28 65.42
REMARK 500 HIS A 531 73.13 -111.34
REMARK 500 TRP A 609 34.43 -93.11
REMARK 500 LYS B 393 -113.19 62.83
REMARK 500 ALA B 412 -79.60 -59.54
REMARK 500 ALA B 441 -133.03 -121.30
REMARK 500 ASP B 494 44.45 -151.51
REMARK 500 ASP B 512 72.82 62.47
REMARK 500 HIS B 531 88.74 -67.53
REMARK 500 TRP B 609 34.79 -88.46
REMARK 500 TYR B 631 53.98 -63.40
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 S19 A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 636
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S19 B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 4
DBREF 3SRV A 360 635 UNP P43405 KSYK_HUMAN 360 635
DBREF 3SRV B 360 635 UNP P43405 KSYK_HUMAN 360 635
SEQADV 3SRV GLY A 359 UNP P43405 EXPRESSION TAG
SEQADV 3SRV GLY B 359 UNP P43405 EXPRESSION TAG
SEQRES 1 A 277 GLY PRO LYS GLU VAL TYR LEU ASP ARG LYS LEU LEU THR
SEQRES 2 A 277 LEU GLU ASP LYS GLU LEU GLY SER GLY ASN PHE GLY THR
SEQRES 3 A 277 VAL LYS LYS GLY TYR TYR GLN MET LYS LYS VAL VAL LYS
SEQRES 4 A 277 THR VAL ALA VAL LYS ILE LEU LYS ASN GLU ALA ASN ASP
SEQRES 5 A 277 PRO ALA LEU LYS ASP GLU LEU LEU ALA GLU ALA ASN VAL
SEQRES 6 A 277 MET GLN GLN LEU ASP ASN PRO TYR ILE VAL ARG MET ILE
SEQRES 7 A 277 GLY ILE CYS GLU ALA GLU SER TRP MET LEU VAL MET GLU
SEQRES 8 A 277 MET ALA GLU LEU GLY PRO LEU ASN LYS TYR LEU GLN GLN
SEQRES 9 A 277 ASN ARG HIS VAL LYS ASP LYS ASN ILE ILE GLU LEU VAL
SEQRES 10 A 277 HIS GLN VAL SER MET GLY MET LYS TYR LEU GLU GLU SER
SEQRES 11 A 277 ASN PHE VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU
SEQRES 12 A 277 LEU VAL THR GLN HIS TYR ALA LYS ILE SER ASP PHE GLY
SEQRES 13 A 277 LEU SER LYS ALA LEU ARG ALA ASP GLU ASN PTR TYR LYS
SEQRES 14 A 277 ALA GLN THR HIS GLY LYS TRP PRO VAL LYS TRP TYR ALA
SEQRES 15 A 277 PRO GLU CYS ILE ASN TYR TYR LYS PHE SER SER LYS SER
SEQRES 16 A 277 ASP VAL TRP SER PHE GLY VAL LEU MET TRP GLU ALA PHE
SEQRES 17 A 277 SER TYR GLY GLN LYS PRO TYR ARG GLY MET LYS GLY SER
SEQRES 18 A 277 GLU VAL THR ALA MET LEU GLU LYS GLY GLU ARG MET GLY
SEQRES 19 A 277 CYS PRO ALA GLY CYS PRO ARG GLU MET TYR ASP LEU MET
SEQRES 20 A 277 ASN LEU CYS TRP THR TYR ASP VAL GLU ASN ARG PRO GLY
SEQRES 21 A 277 PHE ALA ALA VAL GLU LEU ARG LEU ARG ASN TYR TYR TYR
SEQRES 22 A 277 ASP VAL VAL ASN
SEQRES 1 B 277 GLY PRO LYS GLU VAL TYR LEU ASP ARG LYS LEU LEU THR
SEQRES 2 B 277 LEU GLU ASP LYS GLU LEU GLY SER GLY ASN PHE GLY THR
SEQRES 3 B 277 VAL LYS LYS GLY TYR TYR GLN MET LYS LYS VAL VAL LYS
SEQRES 4 B 277 THR VAL ALA VAL LYS ILE LEU LYS ASN GLU ALA ASN ASP
SEQRES 5 B 277 PRO ALA LEU LYS ASP GLU LEU LEU ALA GLU ALA ASN VAL
SEQRES 6 B 277 MET GLN GLN LEU ASP ASN PRO TYR ILE VAL ARG MET ILE
SEQRES 7 B 277 GLY ILE CYS GLU ALA GLU SER TRP MET LEU VAL MET GLU
SEQRES 8 B 277 MET ALA GLU LEU GLY PRO LEU ASN LYS TYR LEU GLN GLN
SEQRES 9 B 277 ASN ARG HIS VAL LYS ASP LYS ASN ILE ILE GLU LEU VAL
SEQRES 10 B 277 HIS GLN VAL SER MET GLY MET LYS TYR LEU GLU GLU SER
SEQRES 11 B 277 ASN PHE VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU
SEQRES 12 B 277 LEU VAL THR GLN HIS TYR ALA LYS ILE SER ASP PHE GLY
SEQRES 13 B 277 LEU SER LYS ALA LEU ARG ALA ASP GLU ASN TYR TYR LYS
SEQRES 14 B 277 ALA GLN THR HIS GLY LYS TRP PRO VAL LYS TRP TYR ALA
SEQRES 15 B 277 PRO GLU CYS ILE ASN TYR TYR LYS PHE SER SER LYS SER
SEQRES 16 B 277 ASP VAL TRP SER PHE GLY VAL LEU MET TRP GLU ALA PHE
SEQRES 17 B 277 SER TYR GLY GLN LYS PRO TYR ARG GLY MET LYS GLY SER
SEQRES 18 B 277 GLU VAL THR ALA MET LEU GLU LYS GLY GLU ARG MET GLY
SEQRES 19 B 277 CYS PRO ALA GLY CYS PRO ARG GLU MET TYR ASP LEU MET
SEQRES 20 B 277 ASN LEU CYS TRP THR TYR ASP VAL GLU ASN ARG PRO GLY
SEQRES 21 B 277 PHE ALA ALA VAL GLU LEU ARG LEU ARG ASN TYR TYR TYR
SEQRES 22 B 277 ASP VAL VAL ASN
MODRES 3SRV PTR A 525 TYR O-PHOSPHOTYROSINE
HET PTR A 525 16
HET S19 A 1 25
HET GOL A 636 6
HET GOL A 2 6
HET GOL A 3 6
HET S19 B 2 25
HET GOL B 4 6
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM S19 2-{[(3R,4R)-3-AMINOTETRAHYDRO-2H-PYRAN-4-YL]AMINO}-4-
HETNAM 2 S19 [(4-METHYLPHENYL)AMINO]PYRIMIDINE-5-CARBOXAMIDE
HETNAM GOL GLYCEROL
HETSYN PTR PHOSPHONOTYROSINE
HETSYN S19 GSK143
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 3 S19 2(C17 H22 N6 O2)
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 9 HOH *472(H2 O)
HELIX 1 1 ASP A 366 LYS A 368 5 3
HELIX 2 2 ALA A 412 GLN A 426 1 15
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 550 SER A 567 1 18
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 633 1 16
HELIX 13 13 ASP B 366 LYS B 368 5 3
HELIX 14 14 PRO B 411 LEU B 427 1 17
HELIX 15 15 LEU B 456 ASN B 463 1 8
HELIX 16 16 LYS B 467 SER B 488 1 22
HELIX 17 17 ALA B 496 ARG B 498 5 3
HELIX 18 18 PRO B 535 TYR B 539 5 5
HELIX 19 19 ALA B 540 TYR B 547 1 8
HELIX 20 20 SER B 550 SER B 567 1 18
HELIX 21 21 LYS B 577 LYS B 587 1 11
HELIX 22 22 PRO B 598 TRP B 609 1 12
HELIX 23 23 GLY B 618 TYR B 631 1 14
SHEET 1 A 5 LEU A 370 GLY A 378 0
SHEET 2 A 5 GLY A 383 MET A 392 -1 O LYS A 387 N GLU A 373
SHEET 3 A 5 VAL A 395 LEU A 404 -1 O ILE A 403 N THR A 384
SHEET 4 A 5 TRP A 444 GLU A 449 -1 O MET A 448 N ALA A 400
SHEET 5 A 5 MET A 435 GLU A 440 -1 N ILE A 436 O VAL A 447
SHEET 1 B 4 LEU A 370 GLY A 378 0
SHEET 2 B 4 GLY A 383 MET A 392 -1 O LYS A 387 N GLU A 373
SHEET 3 B 4 VAL A 395 LEU A 404 -1 O ILE A 403 N THR A 384
SHEET 4 B 4 GLU B 589 MET B 591 -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 526 LYS A 527 0
SHEET 2 E 2 LYS A 548 PHE A 549 -1 O PHE A 549 N TYR A 526
SHEET 1 F 5 LEU B 370 GLY B 380 0
SHEET 2 F 5 GLY B 383 MET B 392 -1 O LYS B 387 N GLU B 373
SHEET 3 F 5 VAL B 395 ILE B 403 -1 O ILE B 403 N THR B 384
SHEET 4 F 5 TRP B 444 GLU B 449 -1 O MET B 448 N ALA B 400
SHEET 5 F 5 MET B 435 GLU B 440 -1 N GLY B 437 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
LINK C ASN A 524 N PTR A 525 1555 1555 1.33
LINK C PTR A 525 N TYR A 526 1555 1555 1.32
SITE 1 AC1 14 GOL A 2 HOH A 52 HOH A 235 ALA A 400
SITE 2 AC1 14 MET A 448 GLU A 449 ALA A 451 GLY A 454
SITE 3 AC1 14 PRO A 455 ARG A 498 ASN A 499 LEU A 501
SITE 4 AC1 14 SER A 511 ASP A 512
SITE 1 AC2 7 HOH A 76 HOH A 202 MET A 424 LEU A 427
SITE 2 AC2 7 ARG A 434 MET A 435 HOH A 637
SITE 1 AC3 6 S19 A 1 LYS A 402 ASP A 494 ARG A 498
SITE 2 AC3 6 ASN A 499 ASP A 512
SITE 1 AC4 1 LYS A 458
SITE 1 AC5 17 HOH B 52 HOH B 199 LEU B 377 SER B 379
SITE 2 AC5 17 ALA B 400 VAL B 433 MET B 448 GLU B 449
SITE 3 AC5 17 MET B 450 ALA B 451 GLY B 454 PRO B 455
SITE 4 AC5 17 ARG B 498 ASN B 499 LEU B 501 SER B 511
SITE 5 AC5 17 ASP B 512
SITE 1 AC6 3 HOH B 32 GLN B 461 LYS B 571
CRYST1 40.124 42.316 87.621 99.68 90.16 100.19 P 1 1
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 0.024923 0.004478 0.000852 0.00000
SCALE2 0.000000 0.024010 0.004178 0.00000
SCALE3 0.000000 0.000000 0.011584 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
