HEADER TRANSCRIPTION 22-APR-10 3MO8
TITLE PWWP DOMAIN OF HUMAN BROMODOMAIN AND PHD FINGER-CONTAINING PROTEIN 1
TITLE 2 IN COMPLEX WITH TRIMETHYLATED H3K36 PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PEREGRIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1079-1207;
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 H3.2 TRIMETHYLATED H3K36 PEPTIDE;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUE 31-42;
COMPND 12 SYNONYM: HISTONE H3/M, HISTONE H3/O;
COMPND 13 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: BR140, BRPF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-(DE3)-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28-MHL;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606
KEYWDS PEREGRIN, PROTEIN BR140, HISTONE H3 ACETYLATION, TRANSCRIPTION,
KEYWDS 2 STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR R.LAM,H.ZENG,S.NI,C.BOUNTRA,J.WEIGELT,C.H.ARROWSMITH,A.M.EDWARDS,
AUTHOR 2 A.BOCHKAREV,J.MIN,H.WU,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 06-SEP-23 3MO8 1 SEQADV LINK
REVDAT 3 08-NOV-17 3MO8 1 REMARK
REVDAT 2 20-JUL-11 3MO8 1 JRNL
REVDAT 1 02-JUN-10 3MO8 0
JRNL AUTH H.WU,H.ZENG,R.LAM,W.TEMPEL,M.F.AMAYA,C.XU,L.DOMBROVSKI,
JRNL AUTH 2 W.QIU,Y.WANG,J.MIN
JRNL TITL STRUCTURAL AND HISTONE BINDING ABILITY CHARACTERIZATIONS OF
JRNL TITL 2 HUMAN PWWP DOMAINS.
JRNL REF PLOS ONE V. 6 18919 2011
JRNL REFN ESSN 1932-6203
JRNL PMID 21720545
JRNL DOI 10.1371/JOURNAL.PONE.0018919
REMARK 2
REMARK 2 RESOLUTION. 1.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC REFMAC_5.5.0109
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) : 1.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 18540
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1005
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) : 1.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1201
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1124
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 107
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24000
REMARK 3 B22 (A**2) : 2.40000
REMARK 3 B33 (A**2) : -2.16000
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): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.093
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.061
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.050
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1170 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1587 ; 1.214 ; 1.982
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 141 ; 4.969 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 52 ;27.124 ;22.500
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 205 ;13.057 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;12.200 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 167 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 886 ; 0.006 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 703 ; 0.770 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1138 ; 1.444 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 467 ; 2.111 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 447 ; 3.504 ; 4.500
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 : 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 1078 A 1204
REMARK 3 ORIGIN FOR THE GROUP (A): 18.9190 19.4870 18.6760
REMARK 3 T TENSOR
REMARK 3 T11: 0.0624 T22: 0.0121
REMARK 3 T33: 0.0926 T12: -0.0054
REMARK 3 T13: 0.0106 T23: 0.0000
REMARK 3 L TENSOR
REMARK 3 L11: 0.8213 L22: 0.6005
REMARK 3 L33: 1.7663 L12: 0.1870
REMARK 3 L13: -0.5033 L23: 0.0764
REMARK 3 S TENSOR
REMARK 3 S11: 0.0323 S12: -0.0180 S13: 0.0472
REMARK 3 S21: -0.0229 S22: 0.0287 S23: -0.0384
REMARK 3 S31: 0.0086 S32: 0.0080 S33: -0.0610
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 1 B 12
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4490 29.7360 13.3060
REMARK 3 T TENSOR
REMARK 3 T11: 0.1240 T22: 0.0177
REMARK 3 T33: 0.0984 T12: 0.0110
REMARK 3 T13: 0.0030 T23: 0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 1.5390 L22: 8.2628
REMARK 3 L33: 1.9003 L12: 0.4753
REMARK 3 L13: -0.2621 L23: 1.2125
REMARK 3 S TENSOR
REMARK 3 S11: -0.0626 S12: 0.0864 S13: 0.1270
REMARK 3 S21: -0.1429 S22: -0.0095 S23: 0.2037
REMARK 3 S31: -0.2913 S32: -0.0888 S33: 0.0721
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 : 1.40
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
REMARK 4
REMARK 4 3MO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058792.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97935
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK HIGH-RESOLUTION
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-3000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19545
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.690
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 (%) : 99.4
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.40700
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: PDB ENTRY 3L42
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM FORMATE, 0.1M TRIS-HCL
REMARK 280 PH8.5, H3K36ME3 PEPTIDE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 21.54300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.30250
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.76950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 21.54300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.30250
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 56.76950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 21.54300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 35.30250
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 56.76950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 21.54300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 35.30250
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 56.76950
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 300 REMARK: AS PER THE AUTHORS THE BIOLOGICAL ASSEMBLY IS A MONOMER
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: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8520 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 GLU A 1205
REMARK 465 GLN A 1206
REMARK 465 SER A 1207
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 A1079 CG CD OE1 OE2
REMARK 470 GLU A1126 CG CD OE1 OE2
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 PHE A1148 36.48 -85.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L42 RELATED DB: PDB
DBREF 3MO8 A 1079 1207 UNP P55201 BRPF1_HUMAN 1079 1207
DBREF 3MO8 B 1 12 UNP Q71DI3 H32_HUMAN 31 42
SEQADV 3MO8 GLY A 1078 UNP P55201 EXPRESSION TAG
SEQRES 1 A 130 GLY GLU ASP SER PRO LEU ASP ALA LEU ASP LEU VAL TRP
SEQRES 2 A 130 ALA LYS CYS ARG GLY TYR PRO SER TYR PRO ALA LEU ILE
SEQRES 3 A 130 ILE ASP PRO LYS MET PRO ARG GLU GLY MET PHE HIS HIS
SEQRES 4 A 130 GLY VAL PRO ILE PRO VAL PRO PRO LEU GLU VAL LEU LYS
SEQRES 5 A 130 LEU GLY GLU GLN MET THR GLN GLU ALA ARG GLU HIS LEU
SEQRES 6 A 130 TYR LEU VAL LEU PHE PHE ASP ASN LYS ARG THR TRP GLN
SEQRES 7 A 130 TRP LEU PRO ARG THR LYS LEU VAL PRO LEU GLY VAL ASN
SEQRES 8 A 130 GLN ASP LEU ASP LYS GLU LYS MET LEU GLU GLY ARG LYS
SEQRES 9 A 130 SER ASN ILE ARG LYS SER VAL GLN ILE ALA TYR HIS ARG
SEQRES 10 A 130 ALA LEU GLN HIS ARG SER LYS VAL GLN GLY GLU GLN SER
SEQRES 1 B 12 PRO ALA THR GLY GLY VAL M3L LYS PRO HIS ARG TYR
MODRES 3MO8 M3L B 7 LYS N-TRIMETHYLLYSINE
HET M3L B 7 12
HETNAM M3L N-TRIMETHYLLYSINE
FORMUL 2 M3L C9 H21 N2 O2 1+
FORMUL 3 HOH *107(H2 O)
HELIX 1 1 PRO A 1124 ALA A 1138 1 15
HELIX 2 2 PRO A 1158 THR A 1160 5 3
HELIX 3 3 ASN A 1168 LEU A 1177 1 10
HELIX 4 4 LYS A 1181 GLY A 1204 1 24
SHEET 1 A 5 TRP A1154 LEU A1157 0
SHEET 2 A 5 TYR A1143 PHE A1147 -1 N TYR A1143 O LEU A1157
SHEET 3 A 5 TYR A1099 ILE A1104 -1 N ILE A1104 O LEU A1144
SHEET 4 A 5 LEU A1088 ALA A1091 -1 N VAL A1089 O ALA A1101
SHEET 5 A 5 LEU A1162 PRO A1164 -1 O VAL A1163 N TRP A1090
SHEET 1 B 2 MET A1113 HIS A1115 0
SHEET 2 B 2 VAL A1118 ILE A1120 -1 O VAL A1118 N HIS A1115
LINK C VAL B 6 N M3L B 7 1555 1555 1.34
LINK C M3L B 7 N LYS B 8 1555 1555 1.33
CRYST1 43.086 70.605 113.539 90.00 90.00 90.00 I 2 2 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 0.023209 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014163 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008808 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
