HEADER GENE REGULATION 07-FEB-17 5PSP
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF BRD1 AFTER
TITLE 2 INITIAL REFINEMENT WITH NO LIGAND MODELLED (STRUCTURE 133)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BR140-LIKE PROTEIN,BROMODOMAIN AND PHD FINGER-CONTAINING
COMPND 5 PROTEIN 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BRD1, BRL, BRPF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PANDDA, SGC - DIAMOND I04-1 FRAGMENT SCREENING, BROMODOMAIN,
KEYWDS 2 EPIGENETICS, XCHEMEXPLORER, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.PEARCE,T.KROJER,R.TALON,A.R.BRADLEY,M.FAIRHEAD,R.SETHI,N.WRIGHT,
AUTHOR 2 E.MACLEAN,P.COLLINS,J.BRANDAO-NETO,A.DOUANGAMATH,Z.RENJIE,A.DIAS,
AUTHOR 3 J.NG,P.E.BRENNAN,O.COX,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,F.VON
AUTHOR 4 DELFT
REVDAT 4 06-MAR-24 5PSP 1 LINK
REVDAT 3 04-OCT-17 5PSP 1 REMARK
REVDAT 2 27-SEP-17 5PSP 1 JRNL REMARK
REVDAT 1 29-MAR-17 5PSP 0
JRNL AUTH N.M.PEARCE,T.KROJER,A.R.BRADLEY,P.COLLINS,R.P.NOWAK,R.TALON,
JRNL AUTH 2 B.D.MARSDEN,S.KELM,J.SHI,C.M.DEANE,F.VON DELFT
JRNL TITL A MULTI-CRYSTAL METHOD FOR EXTRACTING OBSCURED
JRNL TITL 2 CRYSTALLOGRAPHIC STATES FROM CONVENTIONALLY UNINTERPRETABLE
JRNL TITL 3 ELECTRON DENSITY.
JRNL REF NAT COMMUN V. 8 15123 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 28436492
JRNL DOI 10.1038/NCOMMS15123
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0131
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) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.8
REMARK 3 NUMBER OF REFLECTIONS : 40581
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) : 0.182
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2092
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2906
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2590
REMARK 3 BIN FREE R VALUE SET COUNT : 145
REMARK 3 BIN FREE R VALUE : 0.3310
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1953
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 259
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.38000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : -1.04000
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): 0.080
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.083
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.709
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2083 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2008 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2815 ; 2.005 ; 1.975
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4599 ; 1.104 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 264 ; 4.606 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;34.825 ;23.509
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 380 ;13.539 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;13.147 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 311 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2388 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 493 ; 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): 1002 ; 2.185 ; 2.028
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1001 ; 2.172 ; 2.025
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1257 ; 2.938 ; 3.024
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 5PSP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1001401066.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9200
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.3.6
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42716
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 29.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.06400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : 0.78900
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 5AMF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 7.0 -- 30% PEG3350,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 27.68750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.90300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 28.21200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.90300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 27.68750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 28.21200
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 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 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 1
REMARK 465 HIS A 2
REMARK 465 HIS A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 GLY A 10
REMARK 465 VAL A 11
REMARK 465 ASP A 12
REMARK 465 LEU A 13
REMARK 465 GLY A 14
REMARK 465 THR A 15
REMARK 465 GLU A 16
REMARK 465 ASN A 17
REMARK 465 LEU A 18
REMARK 465 TYR A 19
REMARK 465 PHE A 20
REMARK 465 GLN A 21
REMARK 465 LEU A 143
REMARK 465 GLU A 144
REMARK 465 GLU A 145
REMARK 465 ALA A 146
REMARK 465 SER A 147
REMARK 465 GLY A 148
REMARK 465 MET A 149
REMARK 465 HIS A 150
REMARK 465 LEU A 151
REMARK 465 PRO A 152
REMARK 465 GLU A 153
REMARK 465 ARG A 154
REMARK 465 PRO A 155
REMARK 465 ALA A 156
REMARK 465 MET B 1
REMARK 465 HIS B 2
REMARK 465 HIS B 3
REMARK 465 HIS B 4
REMARK 465 HIS B 5
REMARK 465 HIS B 6
REMARK 465 HIS B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 GLY B 10
REMARK 465 VAL B 11
REMARK 465 ASP B 12
REMARK 465 LEU B 13
REMARK 465 GLY B 14
REMARK 465 THR B 15
REMARK 465 GLU B 16
REMARK 465 ASN B 17
REMARK 465 LEU B 18
REMARK 465 TYR B 19
REMARK 465 PHE B 20
REMARK 465 GLN B 21
REMARK 465 GLU B 145
REMARK 465 ALA B 146
REMARK 465 SER B 147
REMARK 465 GLY B 148
REMARK 465 MET B 149
REMARK 465 HIS B 150
REMARK 465 LEU B 151
REMARK 465 PRO B 152
REMARK 465 GLU B 153
REMARK 465 ARG B 154
REMARK 465 PRO B 155
REMARK 465 ALA B 156
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 24 CG CD OE1 OE2
REMARK 470 MET A 28 CE
REMARK 470 LEU A 30 CG CD1 CD2
REMARK 470 ARG A 31 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 37 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 62 CD CE NZ
REMARK 470 LYS A 82 CG CD CE NZ
REMARK 470 LYS A 90 CG CD CE NZ
REMARK 470 ARG A 132 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 141 CG1 CG2 CD1
REMARK 470 LYS B 62 CG CD CE NZ
REMARK 470 GLU B 63 CG CD OE1 OE2
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 ARG B 136 NE CZ NH1 NH2
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 O1 EDO B 202 O HOH B 301 2.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 SD MET A 23 O HOH B 317 1655 1.81
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 ASP B 125 CB ASP B 125 CG 0.138
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 MET A 23 CG - SD - CE ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG B 124 NE - CZ - NH1 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 132 NE - CZ - NH2 ANGL. DEV. = 3.2 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 411 DISTANCE = 5.92 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 B 201 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS A 108 O
REMARK 620 2 HOH A 339 O 99.8
REMARK 620 3 HOH A 364 O 74.6 86.0
REMARK 620 4 MET B 107 O 90.0 105.4 162.4
REMARK 620 5 ASN B 110 O 154.2 105.7 102.9 87.0
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 EDO A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 203
DBREF 5PSP A 23 156 UNP O95696 BRD1_HUMAN 555 688
DBREF 5PSP B 23 156 UNP O95696 BRD1_HUMAN 555 688
SEQADV 5PSP MET A 1 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS A 2 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS A 3 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS A 4 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS A 5 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS A 6 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS A 7 UNP O95696 EXPRESSION TAG
SEQADV 5PSP SER A 8 UNP O95696 EXPRESSION TAG
SEQADV 5PSP SER A 9 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLY A 10 UNP O95696 EXPRESSION TAG
SEQADV 5PSP VAL A 11 UNP O95696 EXPRESSION TAG
SEQADV 5PSP ASP A 12 UNP O95696 EXPRESSION TAG
SEQADV 5PSP LEU A 13 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLY A 14 UNP O95696 EXPRESSION TAG
SEQADV 5PSP THR A 15 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLU A 16 UNP O95696 EXPRESSION TAG
SEQADV 5PSP ASN A 17 UNP O95696 EXPRESSION TAG
SEQADV 5PSP LEU A 18 UNP O95696 EXPRESSION TAG
SEQADV 5PSP TYR A 19 UNP O95696 EXPRESSION TAG
SEQADV 5PSP PHE A 20 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLN A 21 UNP O95696 EXPRESSION TAG
SEQADV 5PSP SER A 22 UNP O95696 EXPRESSION TAG
SEQADV 5PSP MET A 23 UNP O95696 VAL 555 ENGINEERED MUTATION
SEQADV 5PSP GLU A 34 UNP O95696 PRO 566 ENGINEERED MUTATION
SEQADV 5PSP ARG A 37 UNP O95696 VAL 569 ENGINEERED MUTATION
SEQADV 5PSP MET B 1 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS B 2 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS B 3 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS B 4 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS B 5 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS B 6 UNP O95696 EXPRESSION TAG
SEQADV 5PSP HIS B 7 UNP O95696 EXPRESSION TAG
SEQADV 5PSP SER B 8 UNP O95696 EXPRESSION TAG
SEQADV 5PSP SER B 9 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLY B 10 UNP O95696 EXPRESSION TAG
SEQADV 5PSP VAL B 11 UNP O95696 EXPRESSION TAG
SEQADV 5PSP ASP B 12 UNP O95696 EXPRESSION TAG
SEQADV 5PSP LEU B 13 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLY B 14 UNP O95696 EXPRESSION TAG
SEQADV 5PSP THR B 15 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLU B 16 UNP O95696 EXPRESSION TAG
SEQADV 5PSP ASN B 17 UNP O95696 EXPRESSION TAG
SEQADV 5PSP LEU B 18 UNP O95696 EXPRESSION TAG
SEQADV 5PSP TYR B 19 UNP O95696 EXPRESSION TAG
SEQADV 5PSP PHE B 20 UNP O95696 EXPRESSION TAG
SEQADV 5PSP GLN B 21 UNP O95696 EXPRESSION TAG
SEQADV 5PSP SER B 22 UNP O95696 EXPRESSION TAG
SEQADV 5PSP MET B 23 UNP O95696 VAL 555 ENGINEERED MUTATION
SEQADV 5PSP GLU B 34 UNP O95696 PRO 566 ENGINEERED MUTATION
SEQADV 5PSP ARG B 37 UNP O95696 VAL 569 ENGINEERED MUTATION
SEQRES 1 A 156 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 156 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU GLN VAL
SEQRES 3 A 156 ALA MET GLU LEU ARG LEU THR GLU LEU THR ARG LEU LEU
SEQRES 4 A 156 ARG SER VAL LEU ASP GLN LEU GLN ASP LYS ASP PRO ALA
SEQRES 5 A 156 ARG ILE PHE ALA GLN PRO VAL SER LEU LYS GLU VAL PRO
SEQRES 6 A 156 ASP TYR LEU ASP HIS ILE LYS HIS PRO MET ASP PHE ALA
SEQRES 7 A 156 THR MET ARG LYS ARG LEU GLU ALA GLN GLY TYR LYS ASN
SEQRES 8 A 156 LEU HIS GLU PHE GLU GLU ASP PHE ASP LEU ILE ILE ASP
SEQRES 9 A 156 ASN CYS MET LYS TYR ASN ALA ARG ASP THR VAL PHE TYR
SEQRES 10 A 156 ARG ALA ALA VAL ARG LEU ARG ASP GLN GLY GLY VAL VAL
SEQRES 11 A 156 LEU ARG GLN ALA ARG ARG GLU VAL ASP SER ILE GLY LEU
SEQRES 12 A 156 GLU GLU ALA SER GLY MET HIS LEU PRO GLU ARG PRO ALA
SEQRES 1 B 156 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 156 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU GLN VAL
SEQRES 3 B 156 ALA MET GLU LEU ARG LEU THR GLU LEU THR ARG LEU LEU
SEQRES 4 B 156 ARG SER VAL LEU ASP GLN LEU GLN ASP LYS ASP PRO ALA
SEQRES 5 B 156 ARG ILE PHE ALA GLN PRO VAL SER LEU LYS GLU VAL PRO
SEQRES 6 B 156 ASP TYR LEU ASP HIS ILE LYS HIS PRO MET ASP PHE ALA
SEQRES 7 B 156 THR MET ARG LYS ARG LEU GLU ALA GLN GLY TYR LYS ASN
SEQRES 8 B 156 LEU HIS GLU PHE GLU GLU ASP PHE ASP LEU ILE ILE ASP
SEQRES 9 B 156 ASN CYS MET LYS TYR ASN ALA ARG ASP THR VAL PHE TYR
SEQRES 10 B 156 ARG ALA ALA VAL ARG LEU ARG ASP GLN GLY GLY VAL VAL
SEQRES 11 B 156 LEU ARG GLN ALA ARG ARG GLU VAL ASP SER ILE GLY LEU
SEQRES 12 B 156 GLU GLU ALA SER GLY MET HIS LEU PRO GLU ARG PRO ALA
HET EDO A 201 4
HET EDO A 202 8
HET NA B 201 1
HET EDO B 202 4
HET EDO B 203 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 4(C2 H6 O2)
FORMUL 5 NA NA 1+
FORMUL 8 HOH *259(H2 O)
HELIX 1 AA1 SER A 22 LYS A 49 1 28
HELIX 2 AA2 ASP A 66 ILE A 71 1 6
HELIX 3 AA3 ASP A 76 ALA A 86 1 11
HELIX 4 AA4 ASN A 91 ASN A 110 1 20
HELIX 5 AA5 THR A 114 GLY A 142 1 29
HELIX 6 AA6 MET B 23 LYS B 49 1 27
HELIX 7 AA7 ASP B 66 ILE B 71 1 6
HELIX 8 AA8 ASP B 76 ALA B 86 1 11
HELIX 9 AA9 ASN B 91 ASN B 110 1 20
HELIX 10 AB1 THR B 114 GLY B 142 1 29
LINK O LYS A 108 NA NA B 201 1555 1555 2.34
LINK O HOH A 339 NA NA B 201 1555 1555 2.40
LINK O HOH A 364 NA NA B 201 1555 1555 2.44
LINK O MET B 107 NA NA B 201 1555 1555 2.25
LINK O ASN B 110 NA NA B 201 1555 1555 2.31
SITE 1 AC1 5 TYR A 109 ASN A 110 EDO A 202 HOH A 301
SITE 2 AC1 5 HOH A 363
SITE 1 AC2 9 ILE A 54 VAL A 59 CYS A 106 ASN A 110
SITE 2 AC2 9 PHE A 116 EDO A 201 HOH A 301 HOH A 306
SITE 3 AC2 9 HOH A 312
SITE 1 AC3 6 LYS A 108 HOH A 339 HOH A 364 MET B 107
SITE 2 AC3 6 ASN B 110 TYR B 117
SITE 1 AC4 7 ILE B 54 TYR B 109 ASN B 110 PHE B 116
SITE 2 AC4 7 HOH B 301 HOH B 307 HOH B 406
SITE 1 AC5 5 LEU B 92 GLU B 96 LEU B 131 ARG B 135
SITE 2 AC5 5 HOH B 308
CRYST1 55.375 56.424 101.806 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 0.018059 0.000000 0.000000 0.00000
SCALE2 0.000000 0.017723 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009823 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
