HEADER TRANSCRIPTION 19-DEC-15 5FFV
TITLE CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BRPF1 IN COMPLEX WITH
TITLE 2 H3K14AC HISTONE PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEREGRIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 626-740;
COMPND 5 SYNONYM: BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1,PROTEIN
COMPND 6 BR140;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE H3;
COMPND 10 CHAIN: C, D;
COMPND 11 FRAGMENT: UNP RESIDUES 10-20;
COMPND 12 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: BRPF1, BR140;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
SOURCE 10 MOL_ID: 2;
SOURCE 11 SYNTHETIC: YES;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606
KEYWDS PEREGRIN, MOZ-MORF COMPLEX, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR C.TALLANT,G.NUNEZ-ALONSO,P.SAVITSKY,T.KROJER,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP
REVDAT 2 10-JAN-24 5FFV 1 REMARK
REVDAT 1 30-DEC-15 5FFV 0
JRNL AUTH C.TALLANT,G.NUNEZ-ALONSO,P.SAVITSKY,T.KROJER,F.VON DELFT,
JRNL AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP
JRNL TITL CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN BRPF1 IN
JRNL TITL 2 COMPLEX WITH H3K14AC HISTONE PEPTIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 63980
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3307
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3938
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.62
REMARK 3 BIN R VALUE (WORKING SET) : 0.2260
REMARK 3 BIN FREE R VALUE SET COUNT : 247
REMARK 3 BIN FREE R VALUE : 0.2420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1938
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 274
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.47000
REMARK 3 B22 (A**2) : -0.34000
REMARK 3 B33 (A**2) : -0.13000
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): 0.051
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.051
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.032
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.364
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2005 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1946 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2693 ; 1.333 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4470 ; 0.776 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 235 ; 5.076 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;34.336 ;23.832
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 360 ;10.483 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;12.259 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 287 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2256 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 479 ; 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): 946 ; 1.046 ; 1.435
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 945 ; 1.043 ; 1.433
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1179 ; 1.642 ; 2.137
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1180 ; 1.642 ; 2.139
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1059 ; 1.731 ; 1.624
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1059 ; 1.731 ; 1.624
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1515 ; 2.716 ; 2.366
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2619 ; 4.799 ;12.518
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2443 ; 4.597 ;11.832
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 : 2
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 630 A 737
REMARK 3 ORIGIN FOR THE GROUP (A): 62.4105 10.5696 31.3339
REMARK 3 T TENSOR
REMARK 3 T11: 0.0163 T22: 0.0203
REMARK 3 T33: 0.0139 T12: 0.0052
REMARK 3 T13: 0.0145 T23: 0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.7360 L22: 0.6890
REMARK 3 L33: 0.1151 L12: 0.2550
REMARK 3 L13: -0.0261 L23: 0.0176
REMARK 3 S TENSOR
REMARK 3 S11: -0.0128 S12: 0.0309 S13: -0.0254
REMARK 3 S21: -0.0263 S22: -0.0219 S23: -0.0421
REMARK 3 S31: 0.0380 S32: 0.0250 S33: 0.0347
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 630 B 737
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6834 23.9518 43.1319
REMARK 3 T TENSOR
REMARK 3 T11: 0.0063 T22: 0.0360
REMARK 3 T33: 0.0164 T12: 0.0113
REMARK 3 T13: -0.0072 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 0.6174 L22: 0.6094
REMARK 3 L33: 0.1389 L12: -0.1631
REMARK 3 L13: -0.1269 L23: 0.0909
REMARK 3 S TENSOR
REMARK 3 S11: -0.0299 S12: -0.0149 S13: 0.0894
REMARK 3 S21: 0.0452 S22: 0.0296 S23: -0.0261
REMARK 3 S31: -0.0058 S32: -0.0550 S33: 0.0003
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 5FFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216513.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67343
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.730
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : 0.02700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.3
REMARK 200 DATA REDUNDANCY IN SHELL : 8.30
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
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: 4LC2
REMARK 200
REMARK 200 REMARK: ROD
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG3350, 0.2 M MGCL2, 0.1 M BIS
REMARK 280 -TRIS PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 37.13300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.17700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.13300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.17700
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 7480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 625
REMARK 465 MET A 626
REMARK 465 GLU A 627
REMARK 465 MET A 628
REMARK 465 GLY A 740
REMARK 465 SER B 625
REMARK 465 MET B 626
REMARK 465 GLU B 627
REMARK 465 MET B 628
REMARK 465 GLN B 629
REMARK 465 LYS B 738
REMARK 465 MET B 739
REMARK 465 GLY B 740
REMARK 465 LYS C 9
REMARK 465 LYS C 18
REMARK 465 GLN C 19
REMARK 465 LYS D 9
REMARK 465 LYS D 18
REMARK 465 GLN D 19
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 OE2 GLU B 723 O HOH B 901 1.49
REMARK 500 OE2 GLU A 723 O HOH A 901 1.81
REMARK 500 O HOH B 901 O HOH B 967 1.94
REMARK 500
REMARK 500 REMARK: NULL
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 ASP B 648 55.97 -144.11
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 EDO A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 801
DBREF 5FFV A 626 740 UNP P55201 BRPF1_HUMAN 626 740
DBREF 5FFV B 626 740 UNP P55201 BRPF1_HUMAN 626 740
DBREF 5FFV C 9 19 UNP K7EMV3 K7EMV3_HUMAN 10 20
DBREF 5FFV D 9 19 UNP K7EMV3 K7EMV3_HUMAN 10 20
SEQADV 5FFV SER A 625 UNP P55201 EXPRESSION TAG
SEQADV 5FFV SER B 625 UNP P55201 EXPRESSION TAG
SEQRES 1 A 116 SER MET GLU MET GLN LEU THR PRO PHE LEU ILE LEU LEU
SEQRES 2 A 116 ARG LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY
SEQRES 3 A 116 ASN ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO
SEQRES 4 A 116 ASP TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE
SEQRES 5 A 116 THR MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN
SEQRES 6 A 116 PHE ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER
SEQRES 7 A 116 ASN CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR
SEQRES 8 A 116 ARG ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL
SEQRES 9 A 116 LEU ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY
SEQRES 1 B 116 SER MET GLU MET GLN LEU THR PRO PHE LEU ILE LEU LEU
SEQRES 2 B 116 ARG LYS THR LEU GLU GLN LEU GLN GLU LYS ASP THR GLY
SEQRES 3 B 116 ASN ILE PHE SER GLU PRO VAL PRO LEU SER GLU VAL PRO
SEQRES 4 B 116 ASP TYR LEU ASP HIS ILE LYS LYS PRO MET ASP PHE PHE
SEQRES 5 B 116 THR MET LYS GLN ASN LEU GLU ALA TYR ARG TYR LEU ASN
SEQRES 6 B 116 PHE ASP ASP PHE GLU GLU ASP PHE ASN LEU ILE VAL SER
SEQRES 7 B 116 ASN CYS LEU LYS TYR ASN ALA LYS ASP THR ILE PHE TYR
SEQRES 8 B 116 ARG ALA ALA VAL ARG LEU ARG GLU GLN GLY GLY ALA VAL
SEQRES 9 B 116 LEU ARG GLN ALA ARG ARG GLN ALA GLU LYS MET GLY
SEQRES 1 C 11 LYS SER THR GLY GLY ALY ALA PRO ARG LYS GLN
SEQRES 1 D 11 LYS SER THR GLY GLY ALY ALA PRO ARG LYS GLN
MODRES 5FFV ALY C 14 LYS MODIFIED RESIDUE
MODRES 5FFV ALY D 14 LYS MODIFIED RESIDUE
HET ALY C 14 12
HET ALY D 14 12
HET EDO A 801 4
HET EDO A 802 4
HET EDO B 801 4
HETNAM ALY N(6)-ACETYLLYSINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 ALY 2(C8 H16 N2 O3)
FORMUL 5 EDO 3(C2 H6 O2)
FORMUL 8 HOH *274(H2 O)
HELIX 1 AA1 GLN A 629 LYS A 647 1 19
HELIX 2 AA2 ASP A 664 ILE A 669 1 6
HELIX 3 AA3 ASP A 674 ALA A 684 1 11
HELIX 4 AA4 ASN A 689 ASN A 708 1 20
HELIX 5 AA5 THR A 712 GLU A 737 1 26
HELIX 6 AA6 THR B 631 LYS B 647 1 17
HELIX 7 AA7 PRO B 658 VAL B 662 5 5
HELIX 8 AA8 ASP B 664 ILE B 669 1 6
HELIX 9 AA9 ASP B 674 ALA B 684 1 11
HELIX 10 AB1 ASN B 689 ASN B 708 1 20
HELIX 11 AB2 THR B 712 GLU B 737 1 26
LINK C GLY C 13 N ALY C 14 1555 1555 1.32
LINK C ALY C 14 N ALA C 15 1555 1555 1.33
LINK C GLY D 13 N ALY D 14 1555 1555 1.33
LINK C ALY D 14 N ALA D 15 1555 1555 1.33
SITE 1 AC1 9 PRO A 663 ASP A 691 ARG A 733 GLU A 737
SITE 2 AC1 9 HOH A 977 ARG B 730 ARG B 734 HOH B 938
SITE 3 AC1 9 HOH B 995
SITE 1 AC2 3 THR A 712 ILE A 713 HOH A 911
SITE 1 AC3 4 THR B 677 ASN B 681 HOH B 902 HOH B 910
CRYST1 74.266 74.354 49.509 90.00 90.00 90.00 P 21 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 0.013465 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013449 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
