HEADER TRANSCRIPTION 19-AUG-15 5AD3
TITLE BIVALENT BINDING TO BET BROMODOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BROMODOMAIN 1, RESIDUES 44-168;
COMPND 5 SYNONYM: PROTEIN HUNK1, BRD4;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.WARING,H.CHEN,A.A.RABOW,G.WALKER,R.BOBBY,S.BOIKO,R.H.BRADBURY,
AUTHOR 2 R.CALLIS,I.DALE,D.DANIELS,L.FLAVELL,G.HOLDGATE,T.A.JOWITT,A.KIKHNEY,
AUTHOR 3 M.MCALISTER,D.OGG,J.PATEL,P.PETTERUTI,G.R.ROBB,M.ROBERS,N.STRATTON,
AUTHOR 4 D.I.SVERGUN,W.WANG,D.WHITTAKER
REVDAT 5 10-JAN-24 5AD3 1 REMARK
REVDAT 4 30-NOV-16 5AD3 1 JRNL
REVDAT 3 09-NOV-16 5AD3 1 JRNL
REVDAT 2 26-OCT-16 5AD3 1 JRNL
REVDAT 1 28-SEP-16 5AD3 0
JRNL AUTH M.J.WARING,H.CHEN,A.A.RABOW,G.WALKER,R.BOBBY,S.BOIKO,
JRNL AUTH 2 R.H.BRADBURY,R.CALLIS,E.CLARK,I.DALE,D.L.DANIELS,A.DULAK,
JRNL AUTH 3 L.FLAVELL,G.HOLDGATE,T.A.JOWITT,A.KIKHNEY,M.MCALISTER,D.OGG,
JRNL AUTH 4 J.PATEL,P.PETTERUTI,G.R.ROBB,M.B.ROBERS,S.SAIF,N.STRATTON,
JRNL AUTH 5 D.I.SVERGUN,W.WANG,D.WHITTAKER,D.M.WILSON,Y.YAO
JRNL TITL POTENT AND SELECTIVE BIVALENT INHIBITORS OF BET BROMODOMAINS
JRNL REF NAT.CHEM.BIOL. V. 12 1097 2016
JRNL REFN ISSN 1552-4450
JRNL PMID 27775716
JRNL DOI 10.1038/NCHEMBIO.2210
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 45179
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) : 0.271
REMARK 3 R VALUE (WORKING SET) : 0.269
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040
REMARK 3 FREE R VALUE TEST SET COUNT : 2278
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 : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.53
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.37
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3271
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3748
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3122
REMARK 3 BIN R VALUE (WORKING SET) : 0.3754
REMARK 3 BIN FREE R VALUE : 0.3617
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.56
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149
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 : 2118
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 237
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.34430
REMARK 3 B22 (A**2) : -5.71960
REMARK 3 B33 (A**2) : 10.06390
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) : 0.329
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.110
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.110
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.119
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.106
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 : 0.869
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.833
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4340 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7876 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 943 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 72 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 577 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4340 ; 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 : 283 ; 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 : 4637 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.99
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.94
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.88
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 122.5050 -32.5522 2.0687
REMARK 3 T TENSOR
REMARK 3 T11: -0.2240 T22: -0.1720
REMARK 3 T33: 0.1328 T12: 0.0140
REMARK 3 T13: -0.0768 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 1.5011 L22: 0.7616
REMARK 3 L33: 0.8744 L12: 0.0570
REMARK 3 L13: 0.2299 L23: -0.0065
REMARK 3 S TENSOR
REMARK 3 S11: 0.0737 S12: 0.0682 S13: 0.0133
REMARK 3 S21: 0.0045 S22: 0.0329 S23: -0.0795
REMARK 3 S31: -0.0096 S32: -0.0190 S33: -0.1066
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: NULL
REMARK 3 ORIGIN FOR THE GROUP (A): 152.5510 -49.7280 2.6483
REMARK 3 T TENSOR
REMARK 3 T11: -0.2010 T22: -0.1715
REMARK 3 T33: 0.1024 T12: 0.0045
REMARK 3 T13: 0.0553 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.0400 L22: 0.4345
REMARK 3 L33: 1.0632 L12: -0.0821
REMARK 3 L13: -0.3579 L23: -0.0926
REMARK 3 S TENSOR
REMARK 3 S11: 0.0036 S12: 0.0559 S13: -0.0864
REMARK 3 S21: -0.0287 S22: 0.0025 S23: -0.1067
REMARK 3 S31: 0.0771 S32: -0.0109 S33: -0.0060
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5AD3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1290064738.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-14
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 : 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) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45639
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.490
REMARK 200 RESOLUTION RANGE LOW (A) : 52.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.900
REMARK 200 R MERGE (I) : 0.10000
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) : 1.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.66000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OSS
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4K 20%W/V, (NH4)2HPO4 0.2M
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 54.82000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.79550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.91300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 29.79550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 54.82000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 20.91300
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 SER B 42
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 ASN B 93 66.20 63.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2048 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A2054 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A2057 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH B2039 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH B2116 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH B2118 DISTANCE = 6.18 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K6K B 1169
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AD2 RELATED DB: PDB
REMARK 900 BIVALENT BINDING TO BET BROMODOMAINS
DBREF 5AD3 A 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 5AD3 B 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 5AD3 SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 5AD3 MET A 43 UNP O60885 EXPRESSION TAG
SEQADV 5AD3 SER B 42 UNP O60885 EXPRESSION TAG
SEQADV 5AD3 MET B 43 UNP O60885 EXPRESSION TAG
SEQRES 1 A 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 A 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 A 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 A 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 A 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 A 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 A 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 A 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 A 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 A 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 B 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 B 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 B 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 B 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 B 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 B 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 B 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 B 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 B 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 B 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
HET K6K B1169 39
HETNAM K6K 3-METHOXY-N-[2-[4-[1-(3-METHOXY-[1,2,4]TRIAZOLO[4,3-
HETNAM 2 K6K B]PYRIDAZIN-6-YL)-4-PIPERIDYL]PHENOXY]ETHYL]-N-METHYL-
HETNAM 3 K6K [1,2,4]TRIAZOLO[4,3-B]PYRIDAZIN-6-AMINE
FORMUL 3 K6K C26 H30 N10 O3
FORMUL 4 HOH *237(H2 O)
HELIX 1 1 THR A 60 VAL A 69 1 10
HELIX 2 2 VAL A 69 HIS A 77 1 9
HELIX 3 3 ALA A 80 GLN A 84 5 5
HELIX 4 4 ASP A 96 ILE A 101 1 6
HELIX 5 5 ASP A 106 ASN A 116 1 11
HELIX 6 6 ALA A 122 ASN A 140 1 19
HELIX 7 7 ASP A 144 GLU A 163 1 20
HELIX 8 8 THR B 60 VAL B 69 1 10
HELIX 9 9 VAL B 69 HIS B 77 1 9
HELIX 10 10 ALA B 80 GLN B 84 5 5
HELIX 11 11 ASP B 88 ASN B 93 1 6
HELIX 12 12 ASP B 96 ILE B 101 1 6
HELIX 13 13 ASP B 106 ASN B 116 1 11
HELIX 14 14 ASN B 121 ASN B 140 1 20
HELIX 15 15 ASP B 144 GLU B 163 1 20
SITE 1 AC1 14 TRP A 81 PRO A 82 PHE A 83 TYR A 139
SITE 2 AC1 14 ASN A 140 ILE A 146 HOH A2058 TRP B 81
SITE 3 AC1 14 PRO B 82 VAL B 87 ASN B 140 ASP B 145
SITE 4 AC1 14 HOH B2047 HOH B2066
CRYST1 109.640 41.826 59.591 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 0.009121 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023909 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016781 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
