HEADER TRANSFERASE/TRANSFERASE INHIBITOR 06-DEC-13 4NWM
TITLE CRYSTAL STRUCTURE OF BRUTON AGAMMAGLOBULINEMIA TYROSINE KINASE
TITLE 2 COMPLEXED WITH BMS-809959 AKA 4-TERT-BUTYL-N-[2-ME THYL-3-(6-{[4-
TITLE 3 (MORPHOLINE-4-CARBONYL)PHENYL]AMINO}-9H- PURIN-2-YL)PHENYL]BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE BTK;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 396-657;
COMPND 5 SYNONYM: AGAMMAGLOBULINEMIA TYROSINE KINASE, ATK, B-CELL PROGENITOR
COMPND 6 KINASE, BPK, BRUTON TYROSINE KINASE;
COMPND 7 EC: 2.7.10.2;
COMPND 8 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: BTK, AGMX1, ATK, BPK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS
KEYWDS KINASE, BTK, ATK, XLA, PSCTK1, AGMX1, AT, IMD1, MGC126261, MGC126262
KEYWDS 2 BPK, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.K.MUCKELBAUER
REVDAT 3 22-NOV-17 4NWM 1 REMARK
REVDAT 2 08-OCT-14 4NWM 1 JRNL
REVDAT 1 02-APR-14 4NWM 0
JRNL AUTH Q.SHI,A.TEBBEN,A.J.DYCKMAN,H.LI,C.LIU,J.LIN,S.SPERGEL,
JRNL AUTH 2 J.R.BURKE,K.W.MCINTYRE,G.C.OLINI,J.STRNAD,N.SURTI,
JRNL AUTH 3 J.K.MUCKELBAUER,C.CHANG,Y.AN,L.CHENG,Q.RUAN,K.LEFTHERIS,
JRNL AUTH 4 P.H.CARTER,J.TINO,G.V.DE LUCCA
JRNL TITL PURINE DERIVATIVES AS POTENT BRUTON'S TYROSINE KINASE (BTK)
JRNL TITL 2 INHIBITORS FOR AUTOIMMUNE DISEASES.
JRNL REF BIOORG.MED.CHEM.LETT. V. 24 2206 2014
JRNL REFN ISSN 0960-894X
JRNL PMID 24685542
JRNL DOI 10.1016/J.BMCL.2014.02.075
REMARK 2
REMARK 2 RESOLUTION. 2.03 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.11.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.24
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 33555
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1699
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.03
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.09
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.26
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2787
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1962
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2635
REMARK 3 BIN R VALUE (WORKING SET) : 0.1929
REMARK 3 BIN FREE R VALUE : 0.2546
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.45
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 152
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4064
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 182
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 25.32
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.67
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.79200
REMARK 3 B22 (A**2) : 0.91900
REMARK 3 B33 (A**2) : -5.71110
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.240
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.206
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4263 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5794 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1419 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 78 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 707 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4263 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 541 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5076 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.04
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.22
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.83
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4NWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000083747.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.25
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) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33694
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.4
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.09600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.07400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 28.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.25, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298K
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 22.45900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.56300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.25250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.56300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.45900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.25250
REMARK 290 SMTRY3 4 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 489
REMARK 465 MET B 489
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 A 400 CG CD CE NZ
REMARK 470 LYS A 406 CD CE NZ
REMARK 470 GLU A 407 OE1 OE2
REMARK 470 LYS A 420 CD CE NZ
REMARK 470 GLN A 424 CG CD OE1 NE2
REMARK 470 LYS A 433 NZ
REMARK 470 GLU A 434 CG CD OE1 OE2
REMARK 470 ASP A 440 CG OD1 OD2
REMARK 470 GLU A 441 CD OE1 OE2
REMARK 470 GLU A 444 CG CD OE1 OE2
REMARK 470 GLU A 445 CG CD OE1 OE2
REMARK 470 LYS A 447 CG CD CE NZ
REMARK 470 GLU A 455 CG CD OE1 OE2
REMARK 470 LYS A 466 CG CD CE NZ
REMARK 470 ARG A 468 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 490 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 492 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 494 CD OE1 NE2
REMARK 470 LYS A 573 CG CD CE NZ
REMARK 470 LYS A 595 CD CE NZ
REMARK 470 GLU A 608 CG CD OE1 OE2
REMARK 470 GLN A 612 CG CD OE1 NE2
REMARK 470 GLU A 624 CD OE1 OE2
REMARK 470 LYS A 625 CD CE NZ
REMARK 470 GLU A 636 CG CD OE1 OE2
REMARK 470 LYS A 637 CG CD CE NZ
REMARK 470 ASP A 656 CG OD1 OD2
REMARK 470 GLU A 657 CG CD OE1 OE2
REMARK 470 LYS B 400 CG CD CE NZ
REMARK 470 LYS B 406 CG CD CE NZ
REMARK 470 LYS B 417 CE NZ
REMARK 470 LYS B 420 CE NZ
REMARK 470 GLN B 424 CG CD OE1 NE2
REMARK 470 TYR B 425 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 433 CG CD CE NZ
REMARK 470 GLU B 441 CD OE1 OE2
REMARK 470 GLU B 444 OE1 OE2
REMARK 470 GLU B 445 CG CD OE1 OE2
REMARK 470 LYS B 447 CG CD CE NZ
REMARK 470 GLU B 455 CG CD OE1 OE2
REMARK 470 LYS B 466 CG CD CE NZ
REMARK 470 GLN B 467 CG CD OE1 NE2
REMARK 470 ARG B 468 CD NE CZ NH1 NH2
REMARK 470 GLU B 488 CG CD OE1 OE2
REMARK 470 ARG B 490 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 492 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 494 CG CD OE1 NE2
REMARK 470 LYS B 503 CE NZ
REMARK 470 LYS B 515 CE NZ
REMARK 470 ASP B 549 CG OD1 OD2
REMARK 470 GLU B 550 CD OE1 OE2
REMARK 470 LYS B 573 CD CE NZ
REMARK 470 LYS B 595 CD CE NZ
REMARK 470 GLU B 608 CG CD OE1 OE2
REMARK 470 GLN B 612 CG CD OE1 NE2
REMARK 470 LEU B 614 CG CD1 CD2
REMARK 470 LYS B 625 CG CD CE NZ
REMARK 470 GLU B 636 CG CD OE1 OE2
REMARK 470 LYS B 637 CG CD CE NZ
REMARK 470 ASP B 639 OD1 OD2
REMARK 470 GLU B 640 CG CD OE1 OE2
REMARK 470 LYS B 645 CG CD CE NZ
REMARK 470 ASP B 656 CG OD1 OD2
REMARK 470 GLU B 657 CG CD OE1 OE2
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 GLU A 445 -7.20 178.00
REMARK 500 LYS A 466 35.10 -90.82
REMARK 500 ARG A 520 -11.35 81.81
REMARK 500 ASP A 521 50.60 -146.57
REMARK 500 ASP A 548 107.84 -170.91
REMARK 500 GLU B 445 -111.10 -78.81
REMARK 500 ALA B 446 -53.96 54.23
REMARK 500 ARG B 520 -12.84 83.89
REMARK 500 ASP B 521 51.33 -146.36
REMARK 500 ASP B 548 104.41 -170.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 2P5 A 701
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2P5 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2P5 B 701
DBREF 4NWM A 396 657 UNP Q06187 BTK_HUMAN 396 657
DBREF 4NWM B 396 657 UNP Q06187 BTK_HUMAN 396 657
SEQADV 4NWM MET A 395 UNP Q06187 INITIATING METHIONINE
SEQADV 4NWM MET B 395 UNP Q06187 INITIATING METHIONINE
SEQRES 1 A 263 MET GLU ILE ASP PRO LYS ASP LEU THR PHE LEU LYS GLU
SEQRES 2 A 263 LEU GLY THR GLY GLN PHE GLY VAL VAL LYS TYR GLY LYS
SEQRES 3 A 263 TRP ARG GLY GLN TYR ASP VAL ALA ILE LYS MET ILE LYS
SEQRES 4 A 263 GLU GLY SER MET SER GLU ASP GLU PHE ILE GLU GLU ALA
SEQRES 5 A 263 LYS VAL MET MET ASN LEU SER HIS GLU LYS LEU VAL GLN
SEQRES 6 A 263 LEU TYR GLY VAL CYS THR LYS GLN ARG PRO ILE PHE ILE
SEQRES 7 A 263 ILE THR GLU TYR MET ALA ASN GLY OCS LEU LEU ASN TYR
SEQRES 8 A 263 LEU ARG GLU MET ARG HIS ARG PHE GLN THR GLN GLN LEU
SEQRES 9 A 263 LEU GLU MET CYS LYS ASP VAL CYS GLU ALA MET GLU TYR
SEQRES 10 A 263 LEU GLU SER LYS GLN PHE LEU HIS ARG ASP LEU ALA ALA
SEQRES 11 A 263 ARG ASN CYS LEU VAL ASN ASP GLN GLY VAL VAL LYS VAL
SEQRES 12 A 263 SER ASP PHE GLY LEU SER ARG TYR VAL LEU ASP ASP GLU
SEQRES 13 A 263 TYR THR SER SER VAL GLY SER LYS PHE PRO VAL ARG TRP
SEQRES 14 A 263 SER PRO PRO GLU VAL LEU MET TYR SER LYS PHE SER SER
SEQRES 15 A 263 LYS SER ASP ILE TRP ALA PHE GLY VAL LEU MET TRP GLU
SEQRES 16 A 263 ILE TYR SER LEU GLY LYS MET PRO TYR GLU ARG PHE THR
SEQRES 17 A 263 ASN SER GLU THR ALA GLU HIS ILE ALA GLN GLY LEU ARG
SEQRES 18 A 263 LEU TYR ARG PRO HIS LEU ALA SER GLU LYS VAL TYR THR
SEQRES 19 A 263 ILE MET TYR SER CYS TRP HIS GLU LYS ALA ASP GLU ARG
SEQRES 20 A 263 PRO THR PHE LYS ILE LEU LEU SER ASN ILE LEU ASP VAL
SEQRES 21 A 263 MET ASP GLU
SEQRES 1 B 263 MET GLU ILE ASP PRO LYS ASP LEU THR PHE LEU LYS GLU
SEQRES 2 B 263 LEU GLY THR GLY GLN PHE GLY VAL VAL LYS TYR GLY LYS
SEQRES 3 B 263 TRP ARG GLY GLN TYR ASP VAL ALA ILE LYS MET ILE LYS
SEQRES 4 B 263 GLU GLY SER MET SER GLU ASP GLU PHE ILE GLU GLU ALA
SEQRES 5 B 263 LYS VAL MET MET ASN LEU SER HIS GLU LYS LEU VAL GLN
SEQRES 6 B 263 LEU TYR GLY VAL CYS THR LYS GLN ARG PRO ILE PHE ILE
SEQRES 7 B 263 ILE THR GLU TYR MET ALA ASN GLY OCS LEU LEU ASN TYR
SEQRES 8 B 263 LEU ARG GLU MET ARG HIS ARG PHE GLN THR GLN GLN LEU
SEQRES 9 B 263 LEU GLU MET CYS LYS ASP VAL CYS GLU ALA MET GLU TYR
SEQRES 10 B 263 LEU GLU SER LYS GLN PHE LEU HIS ARG ASP LEU ALA ALA
SEQRES 11 B 263 ARG ASN CYS LEU VAL ASN ASP GLN GLY VAL VAL LYS VAL
SEQRES 12 B 263 SER ASP PHE GLY LEU SER ARG TYR VAL LEU ASP ASP GLU
SEQRES 13 B 263 TYR THR SER SER VAL GLY SER LYS PHE PRO VAL ARG TRP
SEQRES 14 B 263 SER PRO PRO GLU VAL LEU MET TYR SER LYS PHE SER SER
SEQRES 15 B 263 LYS SER ASP ILE TRP ALA PHE GLY VAL LEU MET TRP GLU
SEQRES 16 B 263 ILE TYR SER LEU GLY LYS MET PRO TYR GLU ARG PHE THR
SEQRES 17 B 263 ASN SER GLU THR ALA GLU HIS ILE ALA GLN GLY LEU ARG
SEQRES 18 B 263 LEU TYR ARG PRO HIS LEU ALA SER GLU LYS VAL TYR THR
SEQRES 19 B 263 ILE MET TYR SER CYS TRP HIS GLU LYS ALA ASP GLU ARG
SEQRES 20 B 263 PRO THR PHE LYS ILE LEU LEU SER ASN ILE LEU ASP VAL
SEQRES 21 B 263 MET ASP GLU
MODRES 4NWM OCS A 481 CYS CYSTEINESULFONIC ACID
MODRES 4NWM OCS B 481 CYS CYSTEINESULFONIC ACID
HET OCS A 481 9
HET OCS B 481 9
HET 2P5 A 701 44
HET 2P5 B 701 44
HETNAM OCS CYSTEINESULFONIC ACID
HETNAM 2P5 4-TERT-BUTYL-N-[2-METHYL-3-(6-{[4-(MORPHOLIN-4-
HETNAM 2 2P5 YLCARBONYL)PHENYL]AMINO}-7H-PURIN-2-YL)
HETNAM 3 2P5 PHENYL]BENZAMIDE
FORMUL 1 OCS 2(C3 H7 N O5 S)
FORMUL 3 2P5 2(C34 H35 N7 O3)
FORMUL 5 HOH *182(H2 O)
HELIX 1 1 ASP A 398 LYS A 400 5 3
HELIX 2 2 SER A 438 GLU A 444 1 7
HELIX 3 3 GLU A 445 ASN A 451 1 7
HELIX 4 4 OCS A 481 GLU A 488 1 8
HELIX 5 5 GLN A 494 LYS A 515 1 22
HELIX 6 6 ALA A 523 ARG A 525 5 3
HELIX 7 7 GLY A 541 VAL A 546 5 6
HELIX 8 8 ASP A 548 SER A 553 1 6
HELIX 9 9 PRO A 560 SER A 564 5 5
HELIX 10 10 PRO A 565 SER A 572 1 8
HELIX 11 11 SER A 575 SER A 592 1 18
HELIX 12 12 THR A 602 GLY A 613 1 12
HELIX 13 13 SER A 623 CYS A 633 1 11
HELIX 14 14 LYS A 637 ARG A 641 5 5
HELIX 15 15 THR A 643 GLU A 657 1 15
HELIX 16 16 ASP B 398 LYS B 400 5 3
HELIX 17 17 SER B 438 GLU B 445 1 8
HELIX 18 18 ALA B 446 ASN B 451 1 6
HELIX 19 19 OCS B 481 GLU B 488 1 8
HELIX 20 20 GLN B 494 LYS B 515 1 22
HELIX 21 21 ALA B 523 ARG B 525 5 3
HELIX 22 22 GLY B 541 VAL B 546 5 6
HELIX 23 23 ASP B 548 SER B 553 1 6
HELIX 24 24 PRO B 560 SER B 564 5 5
HELIX 25 25 PRO B 565 SER B 572 1 8
HELIX 26 26 SER B 575 SER B 592 1 18
HELIX 27 27 THR B 602 GLY B 613 1 12
HELIX 28 28 SER B 623 CYS B 633 1 11
HELIX 29 29 LYS B 637 ARG B 641 5 5
HELIX 30 30 THR B 643 GLU B 657 1 15
SHEET 1 A 5 LEU A 402 GLY A 411 0
SHEET 2 A 5 GLY A 414 TRP A 421 -1 O VAL A 416 N LEU A 408
SHEET 3 A 5 TYR A 425 MET A 431 -1 O MET A 431 N VAL A 415
SHEET 4 A 5 PHE A 471 GLU A 475 -1 O ILE A 472 N LYS A 430
SHEET 5 A 5 LEU A 460 CYS A 464 -1 N GLY A 462 O ILE A 473
SHEET 1 B 2 CYS A 527 VAL A 529 0
SHEET 2 B 2 VAL A 535 VAL A 537 -1 O LYS A 536 N LEU A 528
SHEET 1 C 5 LEU B 402 GLY B 411 0
SHEET 2 C 5 GLY B 414 TRP B 421 -1 O TYR B 418 N LYS B 406
SHEET 3 C 5 TYR B 425 MET B 431 -1 O ILE B 429 N LYS B 417
SHEET 4 C 5 PHE B 471 GLU B 475 -1 O ILE B 472 N LYS B 430
SHEET 5 C 5 LEU B 460 CYS B 464 -1 N GLY B 462 O ILE B 473
SHEET 1 D 2 CYS B 527 VAL B 529 0
SHEET 2 D 2 VAL B 535 VAL B 537 -1 O LYS B 536 N LEU B 528
LINK C GLY A 480 N OCS A 481 1555 1555 1.34
LINK C OCS A 481 N LEU A 482 1555 1555 1.33
LINK C GLY B 480 N OCS B 481 1555 1555 1.34
LINK C OCS B 481 N LEU B 482 1555 1555 1.33
CISPEP 1 ARG A 468 PRO A 469 0 7.58
CISPEP 2 ARG B 468 PRO B 469 0 3.80
SITE 1 AC1 19 THR A 410 PHE A 413 VAL A 416 ALA A 428
SITE 2 AC1 19 LYS A 430 GLU A 475 MET A 477 ALA A 478
SITE 3 AC1 19 GLY A 480 ASN A 526 LEU A 528 ASP A 539
SITE 4 AC1 19 SER A 543 TYR A 551 HOH A 804 HOH A 824
SITE 5 AC1 19 HOH A 846 HOH A 865 HOH A 886
SITE 1 AC2 19 THR B 410 PHE B 413 VAL B 416 ALA B 428
SITE 2 AC2 19 LYS B 430 GLU B 475 MET B 477 ALA B 478
SITE 3 AC2 19 ASN B 479 GLY B 480 ASN B 526 LEU B 528
SITE 4 AC2 19 ASP B 539 SER B 543 TYR B 551 HOH B 814
SITE 5 AC2 19 HOH B 821 HOH B 847 HOH B 885
CRYST1 44.918 86.505 135.126 90.00 90.00 90.00 P 21 21 21 8
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 0.022263 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007401 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
