HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-OCT-14 4WNM
TITLE SYK CATALYTIC DOMAIN IN COMPLEX WITH A POTENT TRIAZOLOPYRIDINE
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE SYK;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SPLEEN TYROSINE KINASE,P72-SYK;
COMPND 5 EC: 2.7.10.2;
COMPND 6 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
KEYWDS SYK CATALYTIC DOMAIN IN COMPLEX WITH A POTENT TRIAZOLOPYRIDINE BASED
KEYWDS 2 INHIBITOR, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR P.J.JACKSON
REVDAT 2 27-DEC-23 4WNM 1 REMARK
REVDAT 1 20-JAN-16 4WNM 0
JRNL AUTH G.D.FERGUSON,M.DELGADO,V.PLANTEVIN-KRENITSKY,
JRNL AUTH 2 K.JENSEN-PERGAKES,R.J.BATES,S.TORRES,M.CELERIDAD,H.BROWN,
JRNL AUTH 3 K.BURNETT,L.NADOLNY,L.TEHRANI,G.PACKARD,B.PAGARIGAN,
JRNL AUTH 4 J.HAELEWYN,T.NGUYEN,L.XU,Y.TANG,M.HICKMAN,F.BACULI,S.PIERCE,
JRNL AUTH 5 K.MIYAZAWA,P.JACKSON,P.CHAMBERLAIN,L.LEBRUN,W.XIE,B.BENNETT,
JRNL AUTH 6 K.BLEASE
JRNL TITL A NOVEL TRIAZOLOPYRIDINE-BASED SPLEEN TYROSINE KINASE
JRNL TITL 2 INHIBITOR THAT ARRESTS JOINT INFLAMMATION.
JRNL REF PLOS ONE V. 11 45705 2016
JRNL REFN ESSN 1932-6203
JRNL PMID 26756335
JRNL DOI 10.1371/JOURNAL.PONE.0145705
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.9
REMARK 3 NUMBER OF REFLECTIONS : 9503
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 475
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) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 653
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.01
REMARK 3 BIN R VALUE (WORKING SET) : 0.3260
REMARK 3 BIN FREE R VALUE SET COUNT : 37
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2172
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 38
REMARK 3 SOLVENT ATOMS : 16
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.03000
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): 1.041
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.332
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.272
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.091
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2265 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2105 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3066 ; 1.517 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4787 ; 0.819 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 270 ; 6.892 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 103 ;40.542 ;23.981
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 378 ;16.494 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;22.063 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 324 ; 0.085 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2543 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 530 ; 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): 1088 ; 3.285 ; 4.720
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1088 ; 3.281 ; 4.720
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1355 ; 5.021 ; 7.064
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 : 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 4WNM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000204120.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9994
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 (%) : 88.9
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
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) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.76000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
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 (%): 44.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 5.3, 150 MM AMMONIUM
REMARK 280 SULFATE, AND 22% PEG 3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 278K
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 19.93550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.31350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.41000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.31350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 19.93550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.41000
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 TOTAL BURIED SURFACE AREA: 220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12920 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 MET A 343
REMARK 465 ASP A 344
REMARK 465 THR A 345
REMARK 465 GLU A 346
REMARK 465 SER A 350
REMARK 465 PRO A 351
REMARK 465 TYR A 352
REMARK 465 ALA A 353
REMARK 465 ASP A 354
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 GLU A 407
REMARK 465 ALA A 408
REMARK 465 ASN A 409
REMARK 465 ASP A 410
REMARK 465 HIS A 637
REMARK 465 HIS A 638
REMARK 465 HIS A 639
REMARK 465 HIS A 640
REMARK 465 HIS A 641
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 VAL A 363 CG1 CG2
REMARK 470 LYS A 368 CG CD CE NZ
REMARK 470 LYS A 375 CG CD CE NZ
REMARK 470 LYS A 393 CG CD CE NZ
REMARK 470 LYS A 397 CG CD CE NZ
REMARK 470 LYS A 405 CG CD CE NZ
REMARK 470 LYS A 414 CG CD CE NZ
REMARK 470 HIS A 531 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 533 CG CD CE NZ
REMARK 470 LYS A 571 CG CD CE NZ
REMARK 470 GLU A 600 CG CD OE1 OE2
REMARK 470 ASP A 612 CG OD1 OD2
REMARK 470 GLU A 614 CG CD OE1 OE2
REMARK 470 ASN A 635 CG OD1 ND2
REMARK 470 HIS A 636 C O
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 367 -36.33 -35.86
REMARK 500 LEU A 369 40.63 -70.14
REMARK 500 LEU A 377 70.54 -108.72
REMARK 500 SER A 379 -148.20 -176.71
REMARK 500 GLN A 391 99.43 -67.32
REMARK 500 ASN A 429 146.15 -172.02
REMARK 500 ALA A 441 -154.77 -149.86
REMARK 500 GLU A 442 -37.55 -39.65
REMARK 500 ASP A 494 37.28 -156.36
REMARK 500 ASP A 512 74.20 75.28
REMARK 500 HIS A 531 93.35 -54.14
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 3RT A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 702
DBREF 4WNM A 343 635 UNP P43405 KSYK_HUMAN 343 635
SEQADV 4WNM HIS A 636 UNP P43405 EXPRESSION TAG
SEQADV 4WNM HIS A 637 UNP P43405 EXPRESSION TAG
SEQADV 4WNM HIS A 638 UNP P43405 EXPRESSION TAG
SEQADV 4WNM HIS A 639 UNP P43405 EXPRESSION TAG
SEQADV 4WNM HIS A 640 UNP P43405 EXPRESSION TAG
SEQADV 4WNM HIS A 641 UNP P43405 EXPRESSION TAG
SEQRES 1 A 299 MET ASP THR GLU VAL TYR GLU SER PRO TYR ALA ASP PRO
SEQRES 2 A 299 GLU GLU ILE ARG PRO LYS GLU VAL TYR LEU ASP ARG LYS
SEQRES 3 A 299 LEU LEU THR LEU GLU ASP LYS GLU LEU GLY SER GLY ASN
SEQRES 4 A 299 PHE GLY THR VAL LYS LYS GLY TYR TYR GLN MET LYS LYS
SEQRES 5 A 299 VAL VAL LYS THR VAL ALA VAL LYS ILE LEU LYS ASN GLU
SEQRES 6 A 299 ALA ASN ASP PRO ALA LEU LYS ASP GLU LEU LEU ALA GLU
SEQRES 7 A 299 ALA ASN VAL MET GLN GLN LEU ASP ASN PRO TYR ILE VAL
SEQRES 8 A 299 ARG MET ILE GLY ILE CYS GLU ALA GLU SER TRP MET LEU
SEQRES 9 A 299 VAL MET GLU MET ALA GLU LEU GLY PRO LEU ASN LYS TYR
SEQRES 10 A 299 LEU GLN GLN ASN ARG HIS VAL LYS ASP LYS ASN ILE ILE
SEQRES 11 A 299 GLU LEU VAL HIS GLN VAL SER MET GLY MET LYS TYR LEU
SEQRES 12 A 299 GLU GLU SER ASN PHE VAL HIS ARG ASP LEU ALA ALA ARG
SEQRES 13 A 299 ASN VAL LEU LEU VAL THR GLN HIS TYR ALA LYS ILE SER
SEQRES 14 A 299 ASP PHE GLY LEU SER LYS ALA LEU ARG ALA ASP GLU ASN
SEQRES 15 A 299 TYR TYR LYS ALA GLN THR HIS GLY LYS TRP PRO VAL LYS
SEQRES 16 A 299 TRP TYR ALA PRO GLU CYS ILE ASN TYR TYR LYS PHE SER
SEQRES 17 A 299 SER LYS SER ASP VAL TRP SER PHE GLY VAL LEU MET TRP
SEQRES 18 A 299 GLU ALA PHE SER TYR GLY GLN LYS PRO TYR ARG GLY MET
SEQRES 19 A 299 LYS GLY SER GLU VAL THR ALA MET LEU GLU LYS GLY GLU
SEQRES 20 A 299 ARG MET GLY CYS PRO ALA GLY CYS PRO ARG GLU MET TYR
SEQRES 21 A 299 ASP LEU MET ASN LEU CYS TRP THR TYR ASP VAL GLU ASN
SEQRES 22 A 299 ARG PRO GLY PHE ALA ALA VAL GLU LEU ARG LEU ARG ASN
SEQRES 23 A 299 TYR TYR TYR ASP VAL VAL ASN HIS HIS HIS HIS HIS HIS
HET 3RT A 701 33
HET SO4 A 702 5
HETNAM 3RT N~3~-(TETRAHYDRO-2H-PYRAN-4-YL)-N~6~-[5-(TETRAHYDRO-2H-
HETNAM 2 3RT PYRAN-4-YLMETHYL)[1,2,4]TRIAZOLO[1,5-A]PYRIDIN-2-YL]-
HETNAM 3 3RT 1H-INDAZOLE-3,6-DIAMINE
HETNAM SO4 SULFATE ION
FORMUL 2 3RT C24 H29 N7 O2
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *16(H2 O)
HELIX 1 AA1 ASP A 366 LYS A 368 5 3
HELIX 2 AA2 ALA A 412 GLN A 426 1 15
HELIX 3 AA3 LEU A 456 ASN A 463 1 8
HELIX 4 AA4 LYS A 467 ASN A 489 1 23
HELIX 5 AA5 ALA A 496 ARG A 498 5 3
HELIX 6 AA6 PRO A 535 TYR A 539 5 5
HELIX 7 AA7 ALA A 540 TYR A 547 1 8
HELIX 8 AA8 SER A 551 SER A 567 1 17
HELIX 9 AA9 LYS A 577 LYS A 587 1 11
HELIX 10 AB1 PRO A 598 TRP A 609 1 12
HELIX 11 AB2 GLY A 618 ASN A 635 1 18
SHEET 1 AA1 5 LEU A 370 SER A 379 0
SHEET 2 AA1 5 GLY A 383 GLN A 391 -1 O LYS A 387 N LYS A 375
SHEET 3 AA1 5 VAL A 396 LEU A 404 -1 O VAL A 399 N GLY A 388
SHEET 4 AA1 5 TRP A 444 GLU A 449 -1 O MET A 448 N ALA A 400
SHEET 5 AA1 5 MET A 435 GLU A 440 -1 N ILE A 436 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 TYR A 507 N VAL A 503
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 525 LYS A 527 0
SHEET 2 AA4 2 LYS A 548 SER A 550 -1 O PHE A 549 N TYR A 526
SITE 1 AC1 14 LEU A 377 ALA A 400 GLU A 449 MET A 450
SITE 2 AC1 14 ALA A 451 GLY A 454 PRO A 455 LYS A 458
SITE 3 AC1 14 GLN A 462 ARG A 498 ASN A 499 LEU A 501
SITE 4 AC1 14 SER A 511 ASP A 512
SITE 1 AC2 6 ARG A 493 LYS A 517 TYR A 526 ALA A 528
SITE 2 AC2 6 THR A 530 TRP A 534
CRYST1 39.871 84.820 90.627 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 0.025081 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011790 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011034 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
