HEADER TRANSCRIPTION 22-AUG-17 5Y93
TITLE CRYSTAL STRUCTURE ANALYSIS OF THE BRD4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 44-168;
COMPND 5 SYNONYM: PROTEIN HUNK1;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: SEQUENCE FROM 28-43 ARE TAGS. MKKGHHHHHHLVPRGS
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS BRD4(1), BROMODOMAIN, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XU,Y.ZHANG,M.SONG,C.WANG
REVDAT 2 04-DEC-19 5Y93 1 REMARK
REVDAT 1 13-JUN-18 5Y93 0
JRNL AUTH M.ZHANG,Y.ZHANG,M.SONG,X.XUE,J.WANG,C.WANG,C.ZHANG,C.LI,
JRNL AUTH 2 Q.XIANG,L.ZOU,X.WU,C.WU,B.DONG,W.XUE,Y.ZHOU,H.CHEN,D.WU,
JRNL AUTH 3 K.DING,Y.XU
JRNL TITL STRUCTURE-BASED DISCOVERY AND OPTIMIZATION OF BENZO[
JRNL TITL 2 D]ISOXAZOLE DERIVATIVES AS POTENT AND SELECTIVE BET
JRNL TITL 3 INHIBITORS FOR POTENTIAL TREATMENT OF CASTRATION-RESISTANT
JRNL TITL 4 PROSTATE CANCER (CRPC)
JRNL REF J. MED. CHEM. V. 61 3037 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29566488
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00103
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 16206
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 877
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) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1178
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 66
REMARK 3 BIN FREE R VALUE : 0.2080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1115
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 60
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.48000
REMARK 3 B22 (A**2) : -1.17000
REMARK 3 B33 (A**2) : -1.31000
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): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.097
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.063
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.822
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1246 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1181 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1695 ; 1.557 ; 1.996
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2729 ; 1.194 ; 3.012
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 140 ; 5.699 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 59 ;33.552 ;25.085
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 210 ;14.794 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 4 ; 7.658 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 172 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1384 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 288 ; 0.002 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 5Y93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1300004856.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 8.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL19U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97853
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 : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.14
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17128
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 78.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.30700
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: MERLOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 35.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2M NANO3, 0.1M HEPES,
REMARK 280 10% ETGHLY,PH8.3, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
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 17.52000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 39.01500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.56000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 39.01500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 17.52000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 23.56000
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: 120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 28
REMARK 465 LYS A 29
REMARK 465 LYS A 30
REMARK 465 GLY A 31
REMARK 465 HIS A 32
REMARK 465 THR A 166
REMARK 465 GLU A 167
REMARK 465 GLU A 168
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 A 52 96.66 -161.79
REMARK 500 ASN A 140 -169.57 -106.42
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 8Q9 A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 206
DBREF 5Y93 A 44 168 UNP O60885 BRD4_HUMAN 44 168
SEQADV 5Y93 MET A 28 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 LYS A 29 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 LYS A 30 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 GLY A 31 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 HIS A 32 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 HIS A 33 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 HIS A 34 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 HIS A 35 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 HIS A 36 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 HIS A 37 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 LEU A 38 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 VAL A 39 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 PRO A 40 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 ARG A 41 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 GLY A 42 UNP O60885 EXPRESSION TAG
SEQADV 5Y93 SER A 43 UNP O60885 EXPRESSION TAG
SEQRES 1 A 141 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS LEU VAL PRO
SEQRES 2 A 141 ARG GLY SER ASN PRO PRO PRO PRO GLU THR SER ASN PRO
SEQRES 3 A 141 ASN LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU
SEQRES 4 A 141 LEU ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE
SEQRES 5 A 141 ALA TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU
SEQRES 6 A 141 ASN LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET
SEQRES 7 A 141 ASP MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR
SEQRES 8 A 141 TYR TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR
SEQRES 9 A 141 MET PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP
SEQRES 10 A 141 ASP ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE
SEQRES 11 A 141 LEU GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
HET 8Q9 A 201 36
HET NO3 A 202 4
HET NO3 A 203 4
HET EDO A 204 4
HET GOL A 205 6
HET GOL A 206 6
HETNAM 8Q9 2-[[5-[(5-BROMANYL-2-METHOXY-PHENYL)SULFONYLAMINO]-3-
HETNAM 2 8Q9 METHYL-1,2-BENZOXAZOL-6-YL]OXY]-N-(2-MORPHOLIN-4-
HETNAM 3 8Q9 YLETHYL)ETHANAMIDE
HETNAM NO3 NITRATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 8Q9 C23 H27 BR N4 O7 S
FORMUL 3 NO3 2(N O3 1-)
FORMUL 5 EDO C2 H6 O2
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 8 HOH *66(H2 O)
HELIX 1 AA1 THR A 60 VAL A 69 1 10
HELIX 2 AA2 VAL A 69 LYS A 76 1 8
HELIX 3 AA3 ALA A 80 GLN A 84 5 5
HELIX 4 AA4 ASP A 96 ILE A 101 1 6
HELIX 5 AA5 ASP A 106 ASN A 116 1 11
HELIX 6 AA6 ASN A 121 ASN A 140 1 20
HELIX 7 AA7 ASP A 144 ASN A 162 1 19
CISPEP 1 VAL A 39 PRO A 40 0 -5.25
SITE 1 AC1 11 TRP A 81 PRO A 82 VAL A 87 LEU A 92
SITE 2 AC1 11 LEU A 94 LYS A 99 ASN A 140 MET A 149
SITE 3 AC1 11 HOH A 312 HOH A 323 HOH A 338
SITE 1 AC2 5 LYS A 57 TYR A 98 LYS A 99 LYS A 102
SITE 2 AC2 5 ASP A 145
SITE 1 AC3 9 HIS A 34 HIS A 35 HIS A 36 HIS A 37
SITE 2 AC3 9 LEU A 38 VAL A 39 GLN A 123 ILE A 126
SITE 3 AC3 9 ASN A 130
SITE 1 AC4 5 ILE A 100 ILE A 101 LYS A 102 THR A 103
SITE 2 AC4 5 ASN A 135
SITE 1 AC5 6 TYR A 65 TYR A 137 GLU A 151 LYS A 160
SITE 2 AC5 6 GLU A 163 HOH A 313
SITE 1 AC6 6 PRO A 46 PRO A 48 ARG A 58 TRP A 120
SITE 2 AC6 6 ASN A 121 HOH A 311
CRYST1 35.040 47.120 78.030 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 0.028539 0.000000 0.000000 0.00000
SCALE2 0.000000 0.021222 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012816 0.00000
(ATOM LINES ARE NOT SHOWN.)
END