HEADER TRANSFERASE 25-JUL-16 5LKZ
TITLE CRYSTAL STRUCTURE OF THE P300 ACETYLTRANSFERASE CATALYTIC CORE WITH
TITLE 2 CROTONYL-COENZYME A.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE P300,HISTONE ACETYLTRANSFERASE
COMPND 3 P300;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: UNP RESIDUES 1043-1519,UNP RESIDUES 1581-1666,UNP RESIDUES
COMPND 6 1043-1519,UNP RESIDUES 1581-1666;
COMPND 7 SYNONYM: P300 HAT,E1A-ASSOCIATED PROTEIN P300,P300 HAT,E1A-ASSOCIATED
COMPND 8 PROTEIN P300;
COMPND 9 EC: 2.3.1.48,2.3.1.48;
COMPND 10 ENGINEERED: YES;
COMPND 11 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: EP300, P300;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE
KEYWDS P300 ACETYLTRANSFERASE, CROTONYL-COA, CHROMATIN MODIFICATION,
KEYWDS 2 ACYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.KACZMARSKA,E.ORTEGA,J.A.MARQUEZ,D.PANNE
REVDAT 5 10-JAN-24 5LKZ 1 REMARK
REVDAT 4 03-APR-19 5LKZ 1 SOURCE
REVDAT 3 28-DEC-16 5LKZ 1 JRNL
REVDAT 2 16-NOV-16 5LKZ 1 JRNL
REVDAT 1 02-NOV-16 5LKZ 0
JRNL AUTH Z.KACZMARSKA,E.ORTEGA,A.GOUDARZI,H.HUANG,S.KIM,J.A.MARQUEZ,
JRNL AUTH 2 Y.ZHAO,S.KHOCHBIN,D.PANNE
JRNL TITL STRUCTURE OF P300 IN COMPLEX WITH ACYL-COA VARIANTS.
JRNL REF NAT. CHEM. BIOL. V. 13 21 2017
JRNL REFN ESSN 1552-4469
JRNL PMID 27820805
JRNL DOI 10.1038/NCHEMBIO.2217
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 26845
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1336
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.57
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1952
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4474
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 158
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.20000
REMARK 3 B22 (A**2) : -0.76000
REMARK 3 B33 (A**2) : -1.44000
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): 0.387
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.249
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.192
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.905
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.942
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4683 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4346 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6328 ; 1.349 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10036 ; 0.948 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 548 ; 5.786 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 222 ;33.961 ;23.514
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 802 ;13.871 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 32 ;13.193 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 662 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5219 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1083 ; 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): 2198 ; 2.218 ; 4.843
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2197 ; 2.215 ; 4.841
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2741 ; 3.799 ; 7.238
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2742 ; 3.799 ; 7.241
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2484 ; 2.222 ; 4.974
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2484 ; 2.221 ; 4.974
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3585 ; 3.813 ; 7.353
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 9668 ; 6.600 ;40.178
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 9632 ; 6.575 ;40.196
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 : 1.20
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 5LKZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1200000915.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.872600
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28182
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.9300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.810
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: 4BHW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, PEG MME 2000, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 55.04500
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 55.04500
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 46.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 77.95500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 77.95500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 55.04500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.80000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 77.95500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 55.04500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.80000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 77.95500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
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 A1953 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1958 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 1033
REMARK 465 ALA A 1034
REMARK 465 MET A 1035
REMARK 465 ALA A 1036
REMARK 465 GLY A 1037
REMARK 465 LYS A 1038
REMARK 465 ALA A 1039
REMARK 465 VAL A 1040
REMARK 465 PRO A 1041
REMARK 465 MET A 1042
REMARK 465 GLN A 1043
REMARK 465 SER A 1044
REMARK 465 LYS A 1045
REMARK 465 LYS A 1180
REMARK 465 GLN A 1181
REMARK 465 ILE A 1208
REMARK 465 GLN A 1209
REMARK 465 GLY A 1210
REMARK 465 ASP A 1217
REMARK 465 ASP A 1218
REMARK 465 PRO A 1219
REMARK 465 SER A 1220
REMARK 465 GLN A 1221
REMARK 465 PRO A 1222
REMARK 465 GLN A 1663
REMARK 465 ASP A 1664
REMARK 465 ARG A 1665
REMARK 465 PHE A 1666
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 ARG A1055 CG CD NE CZ NH1 NH2
REMARK 470 GLN A1082 CG CD OE1 NE2
REMARK 470 LEU A1083 CG CD1 CD2
REMARK 470 ILE A1086 CG1 CG2 CD1
REMARK 470 GLU A1229 CG CD OE1 OE2
REMARK 470 LYS A1233 CG CD CE NZ
REMARK 470 ASN A1607 CG OD1 ND2
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 O LEU A 1065 OG SER A 1072 2.08
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 O HOH A 1928 O HOH A 1928 3554 1.62
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 A1188 -5.30 68.92
REMARK 500 ARG A1197 -47.28 -132.47
REMARK 500 GLU A1249 -69.70 -91.73
REMARK 500 PHE A1288 50.53 -93.56
REMARK 500 HIS A1402 30.71 -75.53
REMARK 500 ILE A1447 -48.22 -131.06
REMARK 500 CYS A1450 80.16 63.89
REMARK 500 CYS A1621 95.58 -165.21
REMARK 500
REMARK 500 REMARK: NULL
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 ZN A1703 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1163 SG
REMARK 620 2 CYS A1164 SG 124.0
REMARK 620 3 HIS A1255 ND1 108.3 97.0
REMARK 620 4 CYS A1258 SG 109.9 107.3 109.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1177 SG
REMARK 620 2 CYS A1183 SG 84.0
REMARK 620 3 CYS A1201 SG 108.1 111.6
REMARK 620 4 CYS A1204 SG 132.3 143.6 61.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1702 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1247 SG
REMARK 620 2 CYS A1250 SG 104.5
REMARK 620 3 CYS A1272 SG 115.6 115.9
REMARK 620 4 CYS A1275 SG 106.4 106.8 106.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1704 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1315 NE2
REMARK 620 2 CYS A1408 SG 74.2
REMARK 620 3 CYS A1408 SG 127.2 54.0
REMARK 620 4 CYS A1408 SG 74.2 0.0 54.0
REMARK 620 5 CYS A1408 SG 127.2 54.0 0.0 54.0
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 ZN A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue COO A 1705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1708
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BHW RELATED DB: PDB
REMARK 900 4BHW CONTAINS THE SAME PROTEIN COMPLEXED WITH LYSYL-COENZYME A.
DBREF 5LKZ A 1043 1519 UNP Q09472 EP300_HUMAN 1043 1519
DBREF 5LKZ A 1581 1666 UNP Q09472 EP300_HUMAN 1581 1666
SEQADV 5LKZ GLY A 1033 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ ALA A 1034 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ MET A 1035 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ ALA A 1036 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ GLY A 1037 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ LYS A 1038 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ ALA A 1039 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ VAL A 1040 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ PRO A 1041 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ MET A 1042 UNP Q09472 EXPRESSION TAG
SEQADV 5LKZ PHE A 1467 UNP Q09472 TYR 1467 ENGINEERED MUTATION
SEQADV 5LKZ SER A 1520 UNP Q09472 LINKER
SEQADV 5LKZ GLY A 1521 UNP Q09472 LINKER
SEQADV 5LKZ GLY A 1522 UNP Q09472 LINKER
SEQADV 5LKZ SER A 1523 UNP Q09472 LINKER
SEQADV 5LKZ GLY A 1524 UNP Q09472 LINKER
SEQRES 1 A 578 GLY ALA MET ALA GLY LYS ALA VAL PRO MET GLN SER LYS
SEQRES 2 A 578 LYS LYS ILE PHE LYS PRO GLU GLU LEU ARG GLN ALA LEU
SEQRES 3 A 578 MET PRO THR LEU GLU ALA LEU TYR ARG GLN ASP PRO GLU
SEQRES 4 A 578 SER LEU PRO PHE ARG GLN PRO VAL ASP PRO GLN LEU LEU
SEQRES 5 A 578 GLY ILE PRO ASP TYR PHE ASP ILE VAL LYS SER PRO MET
SEQRES 6 A 578 ASP LEU SER THR ILE LYS ARG LYS LEU ASP THR GLY GLN
SEQRES 7 A 578 TYR GLN GLU PRO TRP GLN TYR VAL ASP ASP ILE TRP LEU
SEQRES 8 A 578 MET PHE ASN ASN ALA TRP LEU TYR ASN ARG LYS THR SER
SEQRES 9 A 578 ARG VAL TYR LYS TYR CYS SER LYS LEU SER GLU VAL PHE
SEQRES 10 A 578 GLU GLN GLU ILE ASP PRO VAL MET GLN SER LEU GLY TYR
SEQRES 11 A 578 CYS CYS GLY ARG LYS LEU GLU PHE SER PRO GLN THR LEU
SEQRES 12 A 578 CYS CYS TYR GLY LYS GLN LEU CYS THR ILE PRO ARG ASP
SEQRES 13 A 578 ALA THR TYR TYR SER TYR GLN ASN ARG TYR HIS PHE CYS
SEQRES 14 A 578 GLU LYS CYS PHE ASN GLU ILE GLN GLY GLU SER VAL SER
SEQRES 15 A 578 LEU GLY ASP ASP PRO SER GLN PRO GLN THR THR ILE ASN
SEQRES 16 A 578 LYS GLU GLN PHE SER LYS ARG LYS ASN ASP THR LEU ASP
SEQRES 17 A 578 PRO GLU LEU PHE VAL GLU CYS THR GLU CYS GLY ARG LYS
SEQRES 18 A 578 MET HIS GLN ILE CYS VAL LEU HIS HIS GLU ILE ILE TRP
SEQRES 19 A 578 PRO ALA GLY PHE VAL CYS ASP GLY CYS LEU LYS LYS SER
SEQRES 20 A 578 ALA ARG THR ARG LYS GLU ASN LYS PHE SER ALA LYS ARG
SEQRES 21 A 578 LEU PRO SER THR ARG LEU GLY THR PHE LEU GLU ASN ARG
SEQRES 22 A 578 VAL ASN ASP PHE LEU ARG ARG GLN ASN HIS PRO GLU SER
SEQRES 23 A 578 GLY GLU VAL THR VAL ARG VAL VAL HIS ALA SER ASP LYS
SEQRES 24 A 578 THR VAL GLU VAL LYS PRO GLY MET LYS ALA ARG PHE VAL
SEQRES 25 A 578 ASP SER GLY GLU MET ALA GLU SER PHE PRO TYR ARG THR
SEQRES 26 A 578 LYS ALA LEU PHE ALA PHE GLU GLU ILE ASP GLY VAL ASP
SEQRES 27 A 578 LEU CYS PHE PHE GLY MET HIS VAL GLN GLU TYR GLY SER
SEQRES 28 A 578 ASP CYS PRO PRO PRO ASN GLN ARG ARG VAL TYR ILE SER
SEQRES 29 A 578 TYR LEU ASP SER VAL HIS PHE PHE ARG PRO LYS CYS LEU
SEQRES 30 A 578 ARG THR ALA VAL TYR HIS GLU ILE LEU ILE GLY TYR LEU
SEQRES 31 A 578 GLU TYR VAL LYS LYS LEU GLY TYR THR THR GLY HIS ILE
SEQRES 32 A 578 TRP ALA CYS PRO PRO SER GLU GLY ASP ASP TYR ILE PHE
SEQRES 33 A 578 HIS CYS HIS PRO PRO ASP GLN LYS ILE PRO LYS PRO LYS
SEQRES 34 A 578 ARG LEU GLN GLU TRP PHE LYS LYS MET LEU ASP LYS ALA
SEQRES 35 A 578 VAL SER GLU ARG ILE VAL HIS ASP TYR LYS ASP ILE PHE
SEQRES 36 A 578 LYS GLN ALA THR GLU ASP ARG LEU THR SER ALA LYS GLU
SEQRES 37 A 578 LEU PRO TYR PHE GLU GLY ASP PHE TRP PRO ASN VAL LEU
SEQRES 38 A 578 GLU GLU SER ILE LYS GLU SER GLY GLY SER GLY SER GLN
SEQRES 39 A 578 LYS LEU TYR ALA THR MET GLU LYS HIS LYS GLU VAL PHE
SEQRES 40 A 578 PHE VAL ILE ARG LEU ILE ALA GLY PRO ALA ALA ASN SER
SEQRES 41 A 578 LEU PRO PRO ILE VAL ASP PRO ASP PRO LEU ILE PRO CYS
SEQRES 42 A 578 ASP LEU MET ASP GLY ARG ASP ALA PHE LEU THR LEU ALA
SEQRES 43 A 578 ARG ASP LYS HIS LEU GLU PHE SER SER LEU ARG ARG ALA
SEQRES 44 A 578 GLN TRP SER THR MET CYS MET LEU VAL GLU LEU HIS THR
SEQRES 45 A 578 GLN SER GLN ASP ARG PHE
HET ZN A1701 1
HET ZN A1702 1
HET ZN A1703 1
HET ZN A1704 1
HET COO A1705 53
HET GOL A1706 6
HET GOL A1707 6
HET GOL A1708 6
HETNAM ZN ZINC ION
HETNAM COO CROTONYL COENZYME A
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN 4(ZN 2+)
FORMUL 6 COO C25 H40 N7 O17 P3 S
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 10 HOH *158(H2 O)
HELIX 1 AA1 LYS A 1050 ARG A 1067 1 18
HELIX 2 AA2 SER A 1072 ARG A 1076 5 5
HELIX 3 AA3 ASP A 1080 GLY A 1085 1 6
HELIX 4 AA4 ASP A 1088 VAL A 1093 1 6
HELIX 5 AA5 ASP A 1098 THR A 1108 1 11
HELIX 6 AA6 GLU A 1113 ASN A 1132 1 20
HELIX 7 AA7 SER A 1136 LEU A 1160 1 25
HELIX 8 AA8 GLU A 1202 ASN A 1206 1 5
HELIX 9 AA9 GLU A 1229 PHE A 1231 5 3
HELIX 10 AB1 GLN A 1256 LEU A 1260 1 5
HELIX 11 AB2 CYS A 1272 SER A 1279 1 8
HELIX 12 AB3 THR A 1296 ASN A 1314 1 19
HELIX 13 AB4 LYS A 1336 VAL A 1344 1 9
HELIX 14 AB5 PRO A 1406 CYS A 1408 5 3
HELIX 15 AB6 LEU A 1409 GLY A 1429 1 21
HELIX 16 AB7 LYS A 1459 GLU A 1477 1 19
HELIX 17 AB8 ILE A 1486 ASP A 1493 1 8
HELIX 18 AB9 SER A 1497 LEU A 1501 5 5
HELIX 19 AC1 ASP A 1507 SER A 1520 1 14
HELIX 20 AC2 LYS A 1583 HIS A 1591 1 9
HELIX 21 AC3 ALA A 1602 SER A 1608 5 7
HELIX 22 AC4 CYS A 1621 ASP A 1625 5 5
HELIX 23 AC5 ARG A 1627 LYS A 1637 1 11
HELIX 24 AC6 SER A 1643 SER A 1662 1 20
SHEET 1 AA1 2 LEU A1175 CYS A1176 0
SHEET 2 AA1 2 THR A1184 ILE A1185 -1 O ILE A1185 N LEU A1175
SHEET 1 AA2 3 TYR A1198 CYS A1201 0
SHEET 2 AA2 3 THR A1190 TYR A1194 -1 N TYR A1192 O PHE A1200
SHEET 3 AA2 3 SER A1232 LYS A1235 -1 O SER A1232 N SER A1193
SHEET 1 AA3 2 SER A1212 LEU A1215 0
SHEET 2 AA3 2 THR A1224 ASN A1227 -1 O ILE A1226 N VAL A1213
SHEET 1 AA4 2 PHE A1244 GLU A1246 0
SHEET 2 AA4 2 LYS A1253 HIS A1255 -1 O MET A1254 N VAL A1245
SHEET 1 AA5 7 VAL A1321 GLU A1334 0
SHEET 2 AA5 7 SER A1352 ILE A1366 -1 O TYR A1355 N LYS A1331
SHEET 3 AA5 7 VAL A1369 TYR A1381 -1 O VAL A1369 N ILE A1366
SHEET 4 AA5 7 ARG A1392 SER A1400 -1 O ARG A1392 N TYR A1381
SHEET 5 AA5 7 THR A1432 TRP A1436 1 O THR A1432 N VAL A1393
SHEET 6 AA5 7 PHE A1595 ARG A1599 -1 O ILE A1598 N GLY A1433
SHEET 7 AA5 7 ASP A1482 ASP A1485 -1 N LYS A1484 O VAL A1597
SSBOND 1 CYS A 1201 CYS A 1204 1555 1555 2.40
LINK SG CYS A1163 ZN ZN A1703 1555 1555 2.32
LINK SG CYS A1164 ZN ZN A1703 1555 1555 2.31
LINK SG CYS A1177 ZN ZN A1701 1555 1555 2.36
LINK SG CYS A1183 ZN ZN A1701 1555 1555 2.35
LINK SG CYS A1201 ZN ZN A1701 1555 1555 2.35
LINK SG CYS A1204 ZN ZN A1701 1555 1555 2.35
LINK SG CYS A1247 ZN ZN A1702 1555 1555 2.33
LINK SG CYS A1250 ZN ZN A1702 1555 1555 2.32
LINK ND1 HIS A1255 ZN ZN A1703 1555 1555 2.08
LINK SG CYS A1258 ZN ZN A1703 1555 1555 2.37
LINK SG CYS A1272 ZN ZN A1702 1555 1555 2.34
LINK SG CYS A1275 ZN ZN A1702 1555 1555 2.34
LINK NE2 HIS A1315 ZN ZN A1704 1555 1555 2.19
LINK SG ACYS A1408 ZN ZN A1704 1555 1555 2.35
LINK SG BCYS A1408 ZN ZN A1704 1555 1555 2.33
LINK SG ACYS A1408 ZN ZN A1704 1555 3554 2.17
LINK SG BCYS A1408 ZN ZN A1704 1555 3554 2.61
CISPEP 1 ASP A 1069 PRO A 1070 0 1.55
CISPEP 2 PRO A 1387 PRO A 1388 0 5.44
CISPEP 3 ARG A 1405 PRO A 1406 0 2.75
SITE 1 AC1 4 CYS A1177 CYS A1183 CYS A1201 CYS A1204
SITE 1 AC2 4 CYS A1247 CYS A1250 CYS A1272 CYS A1275
SITE 1 AC3 4 CYS A1163 CYS A1164 HIS A1255 CYS A1258
SITE 1 AC4 2 HIS A1315 CYS A1408
SITE 1 AC5 23 SER A1396 TYR A1397 LEU A1398 ASP A1399
SITE 2 AC5 23 SER A1400 LYS A1407 ARG A1410 THR A1411
SITE 3 AC5 23 TYR A1414 TRP A1436 PRO A1440 LYS A1456
SITE 4 AC5 23 ILE A1457 PRO A1458 ARG A1462 TRP A1466
SITE 5 AC5 23 HOH A1810 HOH A1816 HOH A1831 HOH A1851
SITE 6 AC5 23 HOH A1863 HOH A1867 HOH A1881
SITE 1 AC6 6 ILE A1092 LYS A1094 SER A1095 ASN A1127
SITE 2 AC6 6 LEU A1130 GLY A1347
SITE 1 AC7 4 LYS A1331 TYR A1355 THR A1357 SER A1396
SITE 1 AC8 6 HIS A1434 ASP A1507 TRP A1509 PHE A1596
SITE 2 AC8 6 VAL A1597 HOH A1828
CRYST1 93.600 155.910 110.090 90.00 90.00 90.00 C 2 2 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 0.010684 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009083 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
