HEADER PROTEIN BINDING/INHIBITOR 22-SEP-15 5DW1
TITLE X-RAY CRYSTAL STRUCTURE OF HUMAN BRD2(BD2) IN COMPLEX WITH RVX297 TO
TITLE 2 1.55 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: BD2 (UNP RESIDUES 345-455);
COMPND 5 SYNONYM: O27.1.1, REALLY INTERESTING NEW GENE 3 PROTEIN;
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: BRD2, KIAA9001, RING3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PJEXPRESS401
KEYWDS BROMODOMAIN, PROTEIN BINDING-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.WHITE,E.FONTANO,R.K.SUTO
REVDAT 3 06-MAR-24 5DW1 1 JRNL REMARK LINK
REVDAT 2 20-JUL-16 5DW1 1 JRNL
REVDAT 1 22-JUN-16 5DW1 0
JRNL AUTH O.A.KHARENKO,E.M.GESNER,R.G.PATEL,K.NOREK,A.WHITE,E.FONTANO,
JRNL AUTH 2 R.K.SUTO,P.R.YOUNG,K.G.MCLURE,H.C.HANSEN
JRNL TITL RVX-297- A NOVEL BD2 SELECTIVE INHIBITOR OF BET
JRNL TITL 2 BROMODOMAINS.
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 477 62 2016
JRNL REFN ESSN 1090-2104
JRNL PMID 27282480
JRNL DOI 10.1016/J.BBRC.2016.06.021
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 80774
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.195
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3641
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 583
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.59000
REMARK 3 B22 (A**2) : 0.28000
REMARK 3 B33 (A**2) : 0.09000
REMARK 3 B12 (A**2) : 0.23000
REMARK 3 B13 (A**2) : 0.13000
REMARK 3 B23 (A**2) : -0.34000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.068
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.386
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5DW1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213896.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.075
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : MIRRORS
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 85026
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 95.0
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.42600
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: 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 (%): 59.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.6 M SODIUM MALONATE, PH 7.0, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 A 343
REMARK 465 MET A 344
REMARK 465 SER B 343
REMARK 465 MET B 344
REMARK 465 LYS B 345
REMARK 465 SER C 343
REMARK 465 MET C 344
REMARK 465 LYS C 345
REMARK 465 SER D 343
REMARK 465 MET D 344
REMARK 465 LYS D 345
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 B 351 CG CD CE NZ
REMARK 470 GLU C 348 CG CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NZ LYS A 402 O HOH A 601 2.12
REMARK 500 NZ LYS D 400 O HOH D 601 2.14
REMARK 500 OE1 GLU D 413 O HOH D 602 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 447 CD GLU A 447 OE1 0.072
REMARK 500 PHE A 448 CG PHE A 448 CD1 0.104
REMARK 500 ASP B 444 CB ASP B 444 CG 0.129
REMARK 500 GLU B 447 CD GLU B 447 OE1 0.072
REMARK 500 GLU C 447 CD GLU C 447 OE1 0.090
REMARK 500 GLU D 447 CD GLU D 447 OE1 0.066
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 373 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ASP A 444 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 449 NE - CZ - NH1 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ARG A 449 NE - CZ - NH2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TYR B 373 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 TYR B 373 CZ - CE2 - CD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP B 385 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG B 409 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 409 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 PHE B 448 CB - CG - CD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 TYR C 373 CB - CG - CD1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG C 406 NE - CZ - NH2 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP C 417 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG C 419 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 MET C 438 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 ASP C 444 CB - CG - OD1 ANGL. DEV. = 9.5 DEGREES
REMARK 500 ASP C 444 CB - CG - OD2 ANGL. DEV. = -11.3 DEGREES
REMARK 500 PHE C 448 CB - CG - CD2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 TYR D 373 CB - CG - CD1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ARG D 406 NE - CZ - NH2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG D 419 NE - CZ - NH2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 ASP D 444 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ASP D 444 CB - CG - OD2 ANGL. DEV. = -7.8 DEGREES
REMARK 500 PHE D 448 CB - CG - CD2 ANGL. DEV. = -4.7 DEGREES
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 A 752 DISTANCE = 6.83 ANGSTROMS
REMARK 525 HOH C 754 DISTANCE = 6.03 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 661 O
REMARK 620 2 HOH A 671 O 73.3
REMARK 620 3 HOH A 699 O 77.8 71.6
REMARK 620 4 HOH B 646 O 113.6 167.1 98.6
REMARK 620 5 GLY D 382 O 85.5 85.1 154.4 105.9
REMARK 620 6 HOH D 683 O 160.4 92.1 110.5 83.5 80.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 502 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 377 OD1
REMARK 620 2 SER C 379 OG 80.5
REMARK 620 3 HOH C 679 O 93.9 83.2
REMARK 620 4 HOH C 712 O 173.8 93.8 87.8
REMARK 620 5 HOH C 719 O 101.9 175.5 92.8 84.0
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5GD A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5GD B 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5GD C 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5GD D 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DW2 RELATED DB: PDB
DBREF 5DW1 A 345 455 UNP P25440 BRD2_HUMAN 345 455
DBREF 5DW1 B 345 455 UNP P25440 BRD2_HUMAN 345 455
DBREF 5DW1 C 345 455 UNP P25440 BRD2_HUMAN 345 455
DBREF 5DW1 D 345 455 UNP P25440 BRD2_HUMAN 345 455
SEQADV 5DW1 SER A 343 UNP P25440 EXPRESSION TAG
SEQADV 5DW1 MET A 344 UNP P25440 EXPRESSION TAG
SEQADV 5DW1 SER B 343 UNP P25440 EXPRESSION TAG
SEQADV 5DW1 MET B 344 UNP P25440 EXPRESSION TAG
SEQADV 5DW1 SER C 343 UNP P25440 EXPRESSION TAG
SEQADV 5DW1 MET C 344 UNP P25440 EXPRESSION TAG
SEQADV 5DW1 SER D 343 UNP P25440 EXPRESSION TAG
SEQADV 5DW1 MET D 344 UNP P25440 EXPRESSION TAG
SEQRES 1 A 113 SER MET LYS LEU SER GLU GLN LEU LYS HIS CYS ASN GLY
SEQRES 2 A 113 ILE LEU LYS GLU LEU LEU SER LYS LYS HIS ALA ALA TYR
SEQRES 3 A 113 ALA TRP PRO PHE TYR LYS PRO VAL ASP ALA SER ALA LEU
SEQRES 4 A 113 GLY LEU HIS ASP TYR HIS ASP ILE ILE LYS HIS PRO MET
SEQRES 5 A 113 ASP LEU SER THR VAL LYS ARG LYS MET GLU ASN ARG ASP
SEQRES 6 A 113 TYR ARG ASP ALA GLN GLU PHE ALA ALA ASP VAL ARG LEU
SEQRES 7 A 113 MET PHE SER ASN CYS TYR LYS TYR ASN PRO PRO ASP HIS
SEQRES 8 A 113 ASP VAL VAL ALA MET ALA ARG LYS LEU GLN ASP VAL PHE
SEQRES 9 A 113 GLU PHE ARG TYR ALA LYS MET PRO ASP
SEQRES 1 B 113 SER MET LYS LEU SER GLU GLN LEU LYS HIS CYS ASN GLY
SEQRES 2 B 113 ILE LEU LYS GLU LEU LEU SER LYS LYS HIS ALA ALA TYR
SEQRES 3 B 113 ALA TRP PRO PHE TYR LYS PRO VAL ASP ALA SER ALA LEU
SEQRES 4 B 113 GLY LEU HIS ASP TYR HIS ASP ILE ILE LYS HIS PRO MET
SEQRES 5 B 113 ASP LEU SER THR VAL LYS ARG LYS MET GLU ASN ARG ASP
SEQRES 6 B 113 TYR ARG ASP ALA GLN GLU PHE ALA ALA ASP VAL ARG LEU
SEQRES 7 B 113 MET PHE SER ASN CYS TYR LYS TYR ASN PRO PRO ASP HIS
SEQRES 8 B 113 ASP VAL VAL ALA MET ALA ARG LYS LEU GLN ASP VAL PHE
SEQRES 9 B 113 GLU PHE ARG TYR ALA LYS MET PRO ASP
SEQRES 1 C 113 SER MET LYS LEU SER GLU GLN LEU LYS HIS CYS ASN GLY
SEQRES 2 C 113 ILE LEU LYS GLU LEU LEU SER LYS LYS HIS ALA ALA TYR
SEQRES 3 C 113 ALA TRP PRO PHE TYR LYS PRO VAL ASP ALA SER ALA LEU
SEQRES 4 C 113 GLY LEU HIS ASP TYR HIS ASP ILE ILE LYS HIS PRO MET
SEQRES 5 C 113 ASP LEU SER THR VAL LYS ARG LYS MET GLU ASN ARG ASP
SEQRES 6 C 113 TYR ARG ASP ALA GLN GLU PHE ALA ALA ASP VAL ARG LEU
SEQRES 7 C 113 MET PHE SER ASN CYS TYR LYS TYR ASN PRO PRO ASP HIS
SEQRES 8 C 113 ASP VAL VAL ALA MET ALA ARG LYS LEU GLN ASP VAL PHE
SEQRES 9 C 113 GLU PHE ARG TYR ALA LYS MET PRO ASP
SEQRES 1 D 113 SER MET LYS LEU SER GLU GLN LEU LYS HIS CYS ASN GLY
SEQRES 2 D 113 ILE LEU LYS GLU LEU LEU SER LYS LYS HIS ALA ALA TYR
SEQRES 3 D 113 ALA TRP PRO PHE TYR LYS PRO VAL ASP ALA SER ALA LEU
SEQRES 4 D 113 GLY LEU HIS ASP TYR HIS ASP ILE ILE LYS HIS PRO MET
SEQRES 5 D 113 ASP LEU SER THR VAL LYS ARG LYS MET GLU ASN ARG ASP
SEQRES 6 D 113 TYR ARG ASP ALA GLN GLU PHE ALA ALA ASP VAL ARG LEU
SEQRES 7 D 113 MET PHE SER ASN CYS TYR LYS TYR ASN PRO PRO ASP HIS
SEQRES 8 D 113 ASP VAL VAL ALA MET ALA ARG LYS LEU GLN ASP VAL PHE
SEQRES 9 D 113 GLU PHE ARG TYR ALA LYS MET PRO ASP
HET 5GD A 500 31
HET 5GD B 500 31
HET 5GD C 501 31
HET NA C 502 1
HET 5GD D 501 31
HET NA D 502 1
HETNAM 5GD 2-{3,5-DIMETHYL-4-[2-(PYRROLIDIN-1-YL)ETHOXY]PHENYL}-5,
HETNAM 2 5GD 7-DIMETHOXYQUINAZOLIN-4(3H)-ONE
HETNAM NA SODIUM ION
FORMUL 5 5GD 4(C24 H29 N3 O4)
FORMUL 8 NA 2(NA 1+)
FORMUL 11 HOH *583(H2 O)
HELIX 1 AA1 SER A 347 LEU A 361 1 15
HELIX 2 AA2 SER A 362 LYS A 364 5 3
HELIX 3 AA3 HIS A 365 TRP A 370 1 6
HELIX 4 AA4 PRO A 371 TYR A 373 5 3
HELIX 5 AA5 ASP A 377 GLY A 382 1 6
HELIX 6 AA6 ASP A 385 ILE A 390 1 6
HELIX 7 AA7 ASP A 395 ASN A 405 1 11
HELIX 8 AA8 ASP A 410 ASN A 429 1 20
HELIX 9 AA9 HIS A 433 LYS A 452 1 20
HELIX 10 AB1 SER B 347 LEU B 361 1 15
HELIX 11 AB2 SER B 362 LYS B 364 5 3
HELIX 12 AB3 HIS B 365 TRP B 370 1 6
HELIX 13 AB4 PRO B 371 TYR B 373 5 3
HELIX 14 AB5 ASP B 377 GLY B 382 1 6
HELIX 15 AB6 ASP B 385 ILE B 390 1 6
HELIX 16 AB7 ASP B 395 ASN B 405 1 11
HELIX 17 AB8 ASP B 410 ASN B 429 1 20
HELIX 18 AB9 HIS B 433 LYS B 452 1 20
HELIX 19 AC1 SER C 347 LEU C 361 1 15
HELIX 20 AC2 SER C 362 LYS C 364 5 3
HELIX 21 AC3 HIS C 365 TRP C 370 1 6
HELIX 22 AC4 PRO C 371 TYR C 373 5 3
HELIX 23 AC5 ASP C 385 ILE C 390 1 6
HELIX 24 AC6 ASP C 395 ASN C 405 1 11
HELIX 25 AC7 ASP C 410 ASN C 429 1 20
HELIX 26 AC8 HIS C 433 LYS C 452 1 20
HELIX 27 AC9 SER D 347 LEU D 361 1 15
HELIX 28 AD1 SER D 362 LYS D 364 5 3
HELIX 29 AD2 HIS D 365 TRP D 370 1 6
HELIX 30 AD3 PRO D 371 TYR D 373 5 3
HELIX 31 AD4 ASP D 377 GLY D 382 1 6
HELIX 32 AD5 ASP D 385 ILE D 390 1 6
HELIX 33 AD6 ASP D 395 ASN D 405 1 11
HELIX 34 AD7 ASP D 410 ASN D 429 1 20
HELIX 35 AD8 HIS D 433 LYS D 452 1 20
LINK O HOH A 661 NA NA D 502 1554 1555 2.42
LINK O HOH A 671 NA NA D 502 1554 1555 3.05
LINK O HOH A 699 NA NA D 502 1554 1555 2.56
LINK O HOH B 646 NA NA D 502 1545 1555 2.59
LINK OD1 ASP C 377 NA NA C 502 1555 1555 2.40
LINK OG SER C 379 NA NA C 502 1555 1555 2.49
LINK NA NA C 502 O HOH C 679 1555 1555 2.27
LINK NA NA C 502 O HOH C 712 1555 1555 2.28
LINK NA NA C 502 O HOH C 719 1555 1555 2.38
LINK O GLY D 382 NA NA D 502 1555 1555 2.38
LINK NA NA D 502 O HOH D 683 1555 1555 2.31
SITE 1 AC1 10 TRP A 370 PRO A 371 PHE A 372 VAL A 376
SITE 2 AC1 10 LEU A 381 LEU A 383 ASN A 429 HIS A 433
SITE 3 AC1 10 HOH A 626 HOH D 636
SITE 1 AC2 13 PRO B 371 PHE B 372 VAL B 376 LEU B 381
SITE 2 AC2 13 LEU B 383 ASN B 429 HIS B 433 VAL B 435
SITE 3 AC2 13 HOH B 616 HOH B 630 HOH C 629 HOH C 643
SITE 4 AC2 13 HOH C 689
SITE 1 AC3 14 TRP B 370 ALA B 380 TRP C 370 PRO C 371
SITE 2 AC3 14 PHE C 372 VAL C 376 LEU C 381 ASN C 429
SITE 3 AC3 14 HIS C 433 HOH C 625 HOH C 651 HOH C 672
SITE 4 AC3 14 HOH C 690 HIS D 384
SITE 1 AC4 5 ASP C 377 SER C 379 HOH C 679 HOH C 712
SITE 2 AC4 5 HOH C 719
SITE 1 AC5 14 TRP A 370 ALA A 380 SER B 379 HIS B 384
SITE 2 AC5 14 PRO D 371 PHE D 372 VAL D 376 LEU D 381
SITE 3 AC5 14 LEU D 383 ASN D 429 HIS D 433 HOH D 630
SITE 4 AC5 14 HOH D 678 HOH D 701
SITE 1 AC6 6 HOH A 661 HOH A 671 HOH A 699 HOH B 646
SITE 2 AC6 6 GLY D 382 HOH D 683
CRYST1 56.289 57.318 62.033 62.09 72.08 66.08 P 1 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 0.017765 -0.007880 -0.002867 0.00000
SCALE2 0.000000 0.019086 -0.008200 0.00000
SCALE3 0.000000 0.000000 0.018440 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
