HEADER TRANSCRIPTION 16-MAY-16 5G4S
TITLE BROMODOMAIN OF HUMAN BRPF1 WITH N-1,3-DIMETHYL-6-2R-2-
TITLE 2 METHYLPIPERAZIN-1-YL-2-OXO-2,3-DIHYDRO-1H-1,3-BENZODIAZOL-5-YL-N-
TITLE 3 ETHYL-2-METHOXYBENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEREGRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BROMODOMAIN OF BRPF1, UNP RESIDUES 624-738;
COMPND 5 SYNONYM: BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1, PROTEIN
COMPND 6 BR140,;
COMPND 7 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: 562
KEYWDS TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHUNG
REVDAT 2 16-MAY-18 5G4S 1 REMARK
REVDAT 1 06-JUL-16 5G4S 0
JRNL AUTH P.BAMBOROUGH,H.A.BARNETT,I.BECHER,M.J.BIRD,C.CHUNG,
JRNL AUTH 2 P.D.CRAGGS,E.H.DEMONT,H.DIALLO,D.J.FALLON,L.J.GORDON,
JRNL AUTH 3 P.GRANDI,C.I.HOBBS,E.HOOPER-GREENHILL,E.J.JONES,R.P.LAW,
JRNL AUTH 4 A.LE GALL,D.LUGO,A.MICHON,D.J.MITCHELL,R.K.PRINJHA,
JRNL AUTH 5 R.J.SHEPPARD,A.J.B.WATSON,R.J.WATSON
JRNL TITL GSK6853, A CHEMICAL PROBE FOR INHIBITION OF THE BRPF1
JRNL TITL 2 BROMODOMAIN.
JRNL REF ACS MED.CHEM.LETT. V. 7 552 2016
JRNL REFN ISSN 1948-5875
JRNL PMID 27326325
JRNL DOI 10.1021/ACSMEDCHEMLETT.6B00092
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 20440
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1105
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1314
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.2280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 957
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 229
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.15000
REMARK 3 B22 (A**2) : -0.15000
REMARK 3 B33 (A**2) : 0.29000
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): 0.087
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.053
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.848
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1048 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 720 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1418 ; 1.082 ; 1.940
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1742 ; 0.852 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 115 ; 4.986 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 53 ;33.633 ;24.340
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 180 ;11.709 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;12.162 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 145 ; 0.062 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1132 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 216 ; 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): 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 623 A 738
REMARK 3 ORIGIN FOR THE GROUP (A): 15.9435 34.5666 32.1697
REMARK 3 T TENSOR
REMARK 3 T11: 0.0262 T22: 0.0606
REMARK 3 T33: 0.0242 T12: 0.0066
REMARK 3 T13: 0.0087 T23: 0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 1.2999 L22: 0.7354
REMARK 3 L33: 0.3775 L12: -0.1126
REMARK 3 L13: -0.6943 L23: 0.1262
REMARK 3 S TENSOR
REMARK 3 S11: 0.0911 S12: -0.0331 S13: -0.1018
REMARK 3 S21: 0.0137 S22: -0.1597 S23: 0.0250
REMARK 3 S31: -0.0388 S32: 0.0028 S33: 0.0687
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 : 1.20
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.
REMARK 4
REMARK 4 5G4S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1290066866.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-SEP-14
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) : 0.97934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21557
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 49.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 12.60
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.30
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.000
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: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MORPHEUS BUFFER 1, PH 6.5 37.5%
REMARK 280 MPD_P1K_P3350 10% MORPHEUS NITRATE-PHOSPHATE-SULPHATE
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.57000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.26500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.26500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 63.85500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.26500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.26500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 21.28500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.26500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.26500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 63.85500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.26500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.26500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 21.28500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 42.57000
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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2036 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2112 LIES ON A SPECIAL POSITION.
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 621
REMARK 465 GLN A 622
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 GLU A 623 CG CD OE1 OE2
REMARK 470 LYS A 738 CG CD CE NZ
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 A2004 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A2006 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A2015 DISTANCE = 6.18 ANGSTROMS
REMARK 525 HOH A2050 DISTANCE = 6.84 ANGSTROMS
REMARK 525 HOH A2228 DISTANCE = 6.68 ANGSTROMS
REMARK 525 HOH A2229 DISTANCE = 9.79 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1800
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8VI A 1739
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5G4R RELATED DB: PDB
REMARK 900 BROMODOMAIN OF HUMAN BRPF1 WITH N-1,3-DIMETHYL-6- 2R-2-
REMARK 900 METHYLPIPERAZIN-1-YL-2-OXO-2,3-DIHYDRO-1H-1 ,3-BENZODIAZOL-5-YL-2-
REMARK 900 METHOXYBENZAMIDE
DBREF 5G4S A 624 738 UNP P55201 BRPF1_HUMAN 624 738
SEQADV 5G4S GLY A 621 UNP P55201 EXPRESSION TAG
SEQADV 5G4S GLN A 622 UNP P55201 EXPRESSION TAG
SEQADV 5G4S GLU A 623 UNP P55201 EXPRESSION TAG
SEQRES 1 A 118 GLY GLN GLU ILE ALA MET GLU MET GLN LEU THR PRO PHE
SEQRES 2 A 118 LEU ILE LEU LEU ARG LYS THR LEU GLU GLN LEU GLN GLU
SEQRES 3 A 118 LYS ASP THR GLY ASN ILE PHE SER GLU PRO VAL PRO LEU
SEQRES 4 A 118 SER GLU VAL PRO ASP TYR LEU ASP HIS ILE LYS LYS PRO
SEQRES 5 A 118 MET ASP PHE PHE THR MET LYS GLN ASN LEU GLU ALA TYR
SEQRES 6 A 118 ARG TYR LEU ASN PHE ASP ASP PHE GLU GLU ASP PHE ASN
SEQRES 7 A 118 LEU ILE VAL SER ASN CYS LEU LYS TYR ASN ALA LYS ASP
SEQRES 8 A 118 THR ILE PHE TYR ARG ALA ALA VAL ARG LEU ARG GLU GLN
SEQRES 9 A 118 GLY GLY ALA VAL LEU ARG GLN ALA ARG ARG GLN ALA GLU
SEQRES 10 A 118 LYS
HET 8VI A1739 64
HET EDO A1800 4
HETNAM 8VI N-[1,3-DIMETHYL-6-[(2R)-2-METHYLPIPERAZIN-1-YL]-2-
HETNAM 2 8VI OXIDANYLIDENE-BENZIMIDAZOL-5-YL]-N-ETHYL-2-METHOXY-
HETNAM 3 8VI BENZAMIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 8VI C24 H31 N5 O3
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *229(H2 O)
HELIX 1 1 ILE A 624 MET A 628 5 5
HELIX 2 2 GLN A 629 GLU A 646 1 18
HELIX 3 3 ASP A 664 ILE A 669 1 6
HELIX 4 4 ASP A 674 ALA A 684 1 11
HELIX 5 5 ASN A 689 ASN A 708 1 20
HELIX 6 6 THR A 712 GLU A 737 1 26
SITE 1 AC1 1 GLU A 695
SITE 1 AC2 14 ILE A 624 MET A 626 ASN A 651 ILE A 652
SITE 2 AC2 14 GLU A 655 VAL A 657 PRO A 658 VAL A 662
SITE 3 AC2 14 PHE A 676 TYR A 707 ASN A 708 PHE A 714
SITE 4 AC2 14 HOH A2057 HOH A2125
CRYST1 60.530 60.530 85.140 90.00 90.00 90.00 P 43 21 2 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 0.016521 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016521 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011745 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
