HEADER TRANSFERASE 08-MAR-14 4PSW
TITLE CRYSTAL STRUCTURE OF HISTONE ACETYLTRANSFERASE COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE ACETYLTRANSFERASE TYPE B CATALYTIC SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 4-320;
COMPND 5 EC: 2.3.1.48;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE ACETYLTRANSFERASE TYPE B SUBUNIT 2;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: UNP RESIDUES 7-390;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: HISTONE H4 TYPE VIII;
COMPND 14 CHAIN: C;
COMPND 15 FRAGMENT: UNP RESIDUES 8-45;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: HAT1, YPL001W, LPA16W, YP8132.12;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 559292;
SOURCE 13 STRAIN: ATCC 204508 / S288C;
SOURCE 14 GENE: HAT2, YEL056W;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: OPHIOPHAGUS HANNAH;
SOURCE 19 ORGANISM_COMMON: KING COBRA;
SOURCE 20 ORGANISM_TAXID: 8665;
SOURCE 21 GENE: H4-VIII, L345_01081;
SOURCE 22 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 23 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HAT WD40, HISTONE ACETYLTRANSFERASE, ACCOA, PHOSPHORYLATION,
KEYWDS 2 CYTOPLASMATIC, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.YANG,Y.LI
REVDAT 1 09-JUL-14 4PSW 0
JRNL AUTH Y.LI,L.ZHANG,T.LIU,C.CHAI,Q.FANG,H.WU,P.A.AGUDELO GARCIA,
JRNL AUTH 2 Z.HAN,S.ZONG,Y.YU,X.ZHANG,M.R.PARTHUN,J.CHAI,R.M.XU,M.YANG
JRNL TITL HAT2P RECOGNIZES THE HISTONE H3 TAIL TO SPECIFY THE
JRNL TITL 2 ACETYLATION OF THE NEWLY SYNTHESIZED H3/H4 HETERODIMER BY
JRNL TITL 3 THE HAT1P/HAT2P COMPLEX
JRNL REF GENES DEV. V. 28 1217 2014
JRNL REFN ISSN 0890-9369
JRNL PMID 24835250
JRNL DOI 10.1101/GAD.240531.114
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.70
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 56511
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2868
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 29.7356 - 5.6898 0.99 2861 147 0.1720 0.1954
REMARK 3 2 5.6898 - 4.5213 1.00 2767 140 0.1434 0.1676
REMARK 3 3 4.5213 - 3.9512 0.99 2714 139 0.1386 0.1892
REMARK 3 4 3.9512 - 3.5906 0.99 2682 150 0.1481 0.2018
REMARK 3 5 3.5906 - 3.3337 1.00 2714 143 0.1573 0.1745
REMARK 3 6 3.3337 - 3.1373 1.00 2677 152 0.1668 0.2040
REMARK 3 7 3.1373 - 2.9804 1.00 2672 148 0.1747 0.2009
REMARK 3 8 2.9804 - 2.8507 1.00 2686 152 0.1758 0.2036
REMARK 3 9 2.8507 - 2.7411 1.00 2668 153 0.1750 0.2370
REMARK 3 10 2.7411 - 2.6465 1.00 2671 141 0.1888 0.2683
REMARK 3 11 2.6465 - 2.5638 1.00 2631 160 0.1850 0.2076
REMARK 3 12 2.5638 - 2.4906 1.00 2685 153 0.1898 0.2371
REMARK 3 13 2.4906 - 2.4251 1.00 2658 129 0.1880 0.2485
REMARK 3 14 2.4251 - 2.3659 1.00 2669 124 0.1918 0.2805
REMARK 3 15 2.3659 - 2.3122 1.00 2676 149 0.1954 0.2513
REMARK 3 16 2.3122 - 2.2630 1.00 2654 145 0.2084 0.2588
REMARK 3 17 2.2630 - 2.2177 1.00 2664 123 0.2033 0.2643
REMARK 3 18 2.2177 - 2.1759 1.00 2666 133 0.2129 0.2891
REMARK 3 19 2.1759 - 2.1370 1.00 2633 148 0.2050 0.2541
REMARK 3 20 2.1370 - 2.1000 0.99 2595 139 0.2232 0.2826
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.190
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 6010
REMARK 3 ANGLE : 1.188 8148
REMARK 3 CHIRALITY : 0.084 882
REMARK 3 PLANARITY : 0.005 1044
REMARK 3 DIHEDRAL : 16.369 2227
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 5:320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -3.4814 -37.5515 11.0169
REMARK 3 T TENSOR
REMARK 3 T11: 0.3221 T22: 0.1837
REMARK 3 T33: 0.2250 T12: 0.0042
REMARK 3 T13: 0.0536 T23: -0.0655
REMARK 3 L TENSOR
REMARK 3 L11: 1.1803 L22: 1.0725
REMARK 3 L33: 0.9880 L12: 0.6443
REMARK 3 L13: -0.4030 L23: -0.6627
REMARK 3 S TENSOR
REMARK 3 S11: -0.1368 S12: 0.1912 S13: -0.1913
REMARK 3 S21: -0.2861 S22: 0.0362 S23: -0.1466
REMARK 3 S31: 0.0870 S32: -0.0189 S33: 0.0863
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 7:390 )
REMARK 3 ORIGIN FOR THE GROUP (A): -22.0797 -23.0149 48.5177
REMARK 3 T TENSOR
REMARK 3 T11: 0.0922 T22: 0.1188
REMARK 3 T33: 0.1459 T12: -0.0232
REMARK 3 T13: 0.0103 T23: 0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 1.2328 L22: 0.6931
REMARK 3 L33: 1.2050 L12: -0.1405
REMARK 3 L13: -0.0558 L23: 0.1174
REMARK 3 S TENSOR
REMARK 3 S11: 0.0237 S12: 0.0624 S13: 0.1095
REMARK 3 S21: -0.0864 S22: -0.0094 S23: -0.0396
REMARK 3 S31: -0.0859 S32: -0.0422 S33: -0.0212
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PSW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAR-14.
REMARK 100 THE RCSB ID CODE IS RCSB085179.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9793
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56511
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.340
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 29.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASES
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM SODIUM TARTRATE AND 20%
REMARK 280 (W/V) POLYETHYLENE GLYCOL 3350, PH 7.0, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
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 38.99300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 62.37850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.22050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 62.37850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.99300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.22050
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 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 ASN A 4
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASN B 3
REMARK 465 GLN B 4
REMARK 465 GLU B 5
REMARK 465 LYS B 6
REMARK 465 ASN B 87
REMARK 465 GLU B 88
REMARK 465 ASP B 89
REMARK 465 PRO B 90
REMARK 465 GLN B 91
REMARK 465 GLU B 92
REMARK 465 GLU B 93
REMARK 465 ALA B 94
REMARK 465 GLY B 95
REMARK 465 GLU B 96
REMARK 465 GLU B 97
REMARK 465 TYR B 98
REMARK 465 GLN B 99
REMARK 465 SER B 100
REMARK 465 SER B 101
REMARK 465 LEU B 102
REMARK 465 PRO B 103
REMARK 465 ALA B 104
REMARK 465 GLY B 391
REMARK 465 PRO B 392
REMARK 465 PRO B 393
REMARK 465 LYS B 394
REMARK 465 VAL B 395
REMARK 465 ASN B 396
REMARK 465 LYS B 397
REMARK 465 ASP B 398
REMARK 465 ILE B 399
REMARK 465 ILE B 400
REMARK 465 SER B 401
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 HOH A 660 O HOH A 668 1.81
REMARK 500 O HOH B 809 O HOH B 812 1.81
REMARK 500 O HOH B 749 O HOH B 750 1.83
REMARK 500 O HOH B 756 O HOH B 806 1.87
REMARK 500 O HOH B 668 O HOH B 709 1.89
REMARK 500 O LYS C 46 O HOH C 108 1.95
REMARK 500 O HOH B 769 O HOH B 798 2.01
REMARK 500 O HOH A 520 O HOH B 679 2.01
REMARK 500 O HOH B 801 O HOH B 803 2.04
REMARK 500 OD1 ASP B 11 O HOH B 624 2.05
REMARK 500 O HOH B 763 O HOH B 793 2.05
REMARK 500 OH TYR B 115 O ARG B 148 2.06
REMARK 500 OH TYR A 137 O HOH A 610 2.07
REMARK 500 NE2 GLN A 154 O HOH A 506 2.10
REMARK 500 O HOH B 787 O HOH B 826 2.10
REMARK 500 O HOH B 758 O HOH B 784 2.13
REMARK 500 O HOH B 657 O HOH B 748 2.14
REMARK 500 OD1 ASP A 262 O HOH A 539 2.15
REMARK 500 O HOH A 634 O HOH A 642 2.17
REMARK 500 OE1 GLU B 229 O HOH B 791 2.17
REMARK 500 O ASP A 290 O HOH A 622 2.17
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 B 693 O HOH B 694 4446 1.96
REMARK 500 O HOH A 602 O HOH B 736 2444 2.01
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 ARG A 99 -46.61 65.20
REMARK 500 SER A 218 -74.82 -103.75
REMARK 500 ASP A 256 61.20 31.04
REMARK 500 GLU B 119 179.92 62.19
REMARK 500 ASP B 130 84.38 -155.66
REMARK 500 PHE B 158 -57.93 -138.71
REMARK 500 ASN B 162 132.41 -28.50
REMARK 500 HIS B 183 0.32 82.61
REMARK 500 SER B 192 -169.35 -67.51
REMARK 500 THR B 243 -64.69 70.75
REMARK 500 SER B 274 -9.93 85.68
REMARK 500 ASN B 283 75.26 -155.99
REMARK 500 TRP B 366 -1.84 80.42
REMARK 500 GLU B 374 54.60 -91.34
REMARK 500 ASN C 27 55.05 -119.74
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 639 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH B 785 DISTANCE = 5.22 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PSX RELATED DB: PDB
DBREF 4PSW A 4 320 UNP Q12341 HAT1_YEAST 4 320
DBREF 4PSW B 7 390 UNP P39984 HAT2_YEAST 7 390
DBREF 4PSW C 9 46 UNP V8PGJ1 V8PGJ1_OPHHA 8 45
SEQADV 4PSW MET B 1 UNP P39984 EXPRESSION TAG
SEQADV 4PSW GLU B 2 UNP P39984 EXPRESSION TAG
SEQADV 4PSW ASN B 3 UNP P39984 EXPRESSION TAG
SEQADV 4PSW GLN B 4 UNP P39984 EXPRESSION TAG
SEQADV 4PSW GLU B 5 UNP P39984 EXPRESSION TAG
SEQADV 4PSW LYS B 6 UNP P39984 EXPRESSION TAG
SEQADV 4PSW THR B 143 UNP P39984 VAL 143 ENGINEERED MUTATION
SEQADV 4PSW GLY B 391 UNP P39984 EXPRESSION TAG
SEQADV 4PSW PRO B 392 UNP P39984 EXPRESSION TAG
SEQADV 4PSW PRO B 393 UNP P39984 EXPRESSION TAG
SEQADV 4PSW LYS B 394 UNP P39984 EXPRESSION TAG
SEQADV 4PSW VAL B 395 UNP P39984 EXPRESSION TAG
SEQADV 4PSW ASN B 396 UNP P39984 EXPRESSION TAG
SEQADV 4PSW LYS B 397 UNP P39984 EXPRESSION TAG
SEQADV 4PSW ASP B 398 UNP P39984 EXPRESSION TAG
SEQADV 4PSW ILE B 399 UNP P39984 EXPRESSION TAG
SEQADV 4PSW ILE B 400 UNP P39984 EXPRESSION TAG
SEQADV 4PSW SER B 401 UNP P39984 EXPRESSION TAG
SEQRES 1 A 317 ASN ASP PHE LYS PRO GLU THR TRP THR SER SER ALA ASN
SEQRES 2 A 317 GLU ALA LEU ARG VAL SER ILE VAL GLY GLU ASN ALA VAL
SEQRES 3 A 317 GLN PHE SER PRO LEU PHE THR TYR PRO ILE TYR GLY ASP
SEQRES 4 A 317 SER GLU LYS ILE TYR GLY TYR LYS ASP LEU ILE ILE HIS
SEQRES 5 A 317 LEU ALA PHE ASP SER VAL THR PHE LYS PRO TYR VAL ASN
SEQRES 6 A 317 VAL LYS TYR SER ALA LYS LEU GLY ASP ASP ASN ILE VAL
SEQRES 7 A 317 ASP VAL GLU LYS LYS LEU LEU SER PHE LEU PRO LYS ASP
SEQRES 8 A 317 ASP VAL ILE VAL ARG ASP GLU ALA LYS TRP VAL ASP CYS
SEQRES 9 A 317 PHE ALA GLU GLU ARG LYS THR HIS ASN LEU SER ASP VAL
SEQRES 10 A 317 PHE GLU LYS VAL SER GLU TYR SER LEU ASN GLY GLU GLU
SEQRES 11 A 317 PHE VAL VAL TYR LYS SER SER LEU VAL ASP ASP PHE ALA
SEQRES 12 A 317 ARG ARG MET HIS ARG ARG VAL GLN ILE PHE SER LEU LEU
SEQRES 13 A 317 PHE ILE GLU ALA ALA ASN TYR ILE ASP GLU THR ASP PRO
SEQRES 14 A 317 SER TRP GLN ILE TYR TRP LEU LEU ASN LYS LYS THR LYS
SEQRES 15 A 317 GLU LEU ILE GLY PHE VAL THR THR TYR LYS TYR TRP HIS
SEQRES 16 A 317 TYR LEU GLY ALA LYS SER PHE ASP GLU ASP ILE ASP LYS
SEQRES 17 A 317 LYS PHE ARG ALA LYS ILE SER GLN PHE LEU ILE PHE PRO
SEQRES 18 A 317 PRO TYR GLN ASN LYS GLY HIS GLY SER CYS LEU TYR GLU
SEQRES 19 A 317 ALA ILE ILE GLN SER TRP LEU GLU ASP LYS SER ILE THR
SEQRES 20 A 317 GLU ILE THR VAL GLU ASP PRO ASN GLU ALA PHE ASP ASP
SEQRES 21 A 317 LEU ARG ASP ARG ASN ASP ILE GLN ARG LEU ARG LYS LEU
SEQRES 22 A 317 GLY TYR ASP ALA VAL PHE GLN LYS HIS SER ASP LEU SER
SEQRES 23 A 317 ASP GLU PHE LEU GLU SER SER ARG LYS SER LEU LYS LEU
SEQRES 24 A 317 GLU GLU ARG GLN PHE ASN ARG LEU VAL GLU MET LEU LEU
SEQRES 25 A 317 LEU LEU ASN ASN SER
SEQRES 1 B 401 MET GLU ASN GLN GLU LYS PRO LEU SER VAL ASP GLU GLU
SEQRES 2 B 401 TYR ASP LEU TRP LYS SER ASN VAL PRO LEU MET TYR ASP
SEQRES 3 B 401 PHE VAL SER GLU THR ARG LEU TPO TRP PRO SER LEU THR
SEQRES 4 B 401 VAL GLN TRP LEU PRO THR PRO VAL GLN GLU LEU ASP GLY
SEQRES 5 B 401 GLY PHE ILE LYS GLN GLU LEU ILE ILE GLY THR HIS THR
SEQRES 6 B 401 SER GLY GLU GLU GLU ASN TYR LEU LYS PHE ALA GLU ILE
SEQRES 7 B 401 ASN LEU PRO LYS GLU ILE LEU SER ASN GLU ASP PRO GLN
SEQRES 8 B 401 GLU GLU ALA GLY GLU GLU TYR GLN SER SER LEU PRO ALA
SEQRES 9 B 401 PRO ARG SER ASN ILE ARG ILE THR ALA LYS TYR GLU HIS
SEQRES 10 B 401 GLU GLU GLU ILE THR ARG ALA ARG TYR MET PRO GLN ASP
SEQRES 11 B 401 PRO ASN ILE VAL ALA THR ILE ASN GLY GLN GLY THR THR
SEQRES 12 B 401 PHE LEU TYR SER ARG SER GLU GLY LEU GLN SER THR LEU
SEQRES 13 B 401 LYS PHE HIS LYS ASP ASN GLY TYR ALA LEU SER PHE SER
SEQRES 14 B 401 THR LEU VAL LYS GLY ARG LEU LEU SER GLY SER ASP ASP
SEQRES 15 B 401 HIS THR VAL ALA LEU TRP GLU VAL GLY SER GLY GLY ASP
SEQRES 16 B 401 PRO THR LYS PRO VAL ARG THR TRP ASN ASP LEU HIS SER
SEQRES 17 B 401 ASP ILE ILE ASN ASP ASN LYS TRP HIS ASN PHE ASN LYS
SEQRES 18 B 401 ASP LEU PHE GLY THR VAL SER GLU ASP SER LEU LEU LYS
SEQRES 19 B 401 ILE ASN ASP VAL ARG ALA ASN ASN THR THR ILE ASP THR
SEQRES 20 B 401 VAL LYS CYS PRO GLN PRO PHE ASN THR LEU ALA PHE SER
SEQRES 21 B 401 HIS HIS SER SER ASN LEU LEU ALA ALA ALA GLY MET ASP
SEQRES 22 B 401 SER TYR VAL TYR LEU TYR ASP LEU ARG ASN MET LYS GLU
SEQRES 23 B 401 PRO LEU HIS HIS MET SER GLY HIS GLU ASP ALA VAL ASN
SEQRES 24 B 401 ASN LEU GLU PHE SER THR HIS VAL ASP GLY VAL VAL VAL
SEQRES 25 B 401 SER SER GLY SER ASP ASN ARG LEU MET MET TRP ASP LEU
SEQRES 26 B 401 LYS GLN ILE GLY ALA GLU GLN THR PRO ASP ASP ALA GLU
SEQRES 27 B 401 ASP GLY VAL PRO GLU LEU ILE MET VAL HIS ALA GLY HIS
SEQRES 28 B 401 ARG SER SER VAL ASN ASP PHE ASP LEU ASN PRO GLN ILE
SEQRES 29 B 401 PRO TRP LEU VAL ALA SER ALA GLU GLU GLU ASN ILE LEU
SEQRES 30 B 401 GLN VAL TRP LYS CYS SER HIS SER LEU PRO ILE VAL GLY
SEQRES 31 B 401 GLY PRO PRO LYS VAL ASN LYS ASP ILE ILE SER
SEQRES 1 C 38 GLY LYS GLY LEU GLY LYS GLY GLY ALA LYS ARG HIS ARG
SEQRES 2 C 38 LYS VAL LEU ARG ASP ASN ILE GLN GLY ILE THR LYS PRO
SEQRES 3 C 38 ALA ILE ARG ARG LEU ALA ARG ARG GLY GLY VAL LYS
MODRES 4PSW TPO B 34 THR PHOSPHOTHREONINE
HET TPO B 34 11
HET COA A 401 48
HETNAM TPO PHOSPHOTHREONINE
HETNAM COA COENZYME A
HETSYN TPO PHOSPHONOTHREONINE
FORMUL 2 TPO C4 H10 N O6 P
FORMUL 4 COA C21 H36 N7 O16 P3 S
FORMUL 5 HOH *526(H2 O)
HELIX 1 1 LYS A 7 THR A 10 5 4
HELIX 2 2 ALA A 15 ALA A 18 1 4
HELIX 3 3 THR A 36 GLY A 41 1 6
HELIX 4 4 ASP A 82 SER A 89 1 8
HELIX 5 5 ASP A 100 THR A 114 1 15
HELIX 6 6 ASN A 116 PHE A 121 1 6
HELIX 7 7 ASP A 143 GLN A 154 1 12
HELIX 8 8 GLN A 154 ILE A 161 1 8
HELIX 9 9 GLY A 201 ASP A 208 1 8
HELIX 10 10 PRO A 224 GLN A 227 5 4
HELIX 11 11 GLY A 230 GLU A 245 1 16
HELIX 12 12 ASN A 258 LEU A 276 1 19
HELIX 13 13 GLY A 277 PHE A 282 1 6
HELIX 14 14 SER A 289 LYS A 301 1 13
HELIX 15 15 GLU A 303 ASN A 319 1 17
HELIX 16 16 SER B 9 MET B 24 1 16
HELIX 17 17 GLU B 83 SER B 86 5 4
HELIX 18 18 LYS B 326 ILE B 328 5 3
HELIX 19 19 THR B 333 GLU B 338 1 6
HELIX 20 20 THR C 32 GLY C 43 1 12
SHEET 1 A 2 THR A 12 SER A 14 0
SHEET 2 A 2 LYS A 45 TYR A 47 -1 O ILE A 46 N SER A 13
SHEET 1 B 5 ALA A 28 PHE A 31 0
SHEET 2 B 5 LEU A 19 VAL A 24 -1 N ILE A 23 O VAL A 29
SHEET 3 B 5 ILE A 53 ASP A 59 1 O ILE A 54 N ARG A 20
SHEET 4 B 5 PRO A 65 LYS A 70 -1 O ASN A 68 N HIS A 55
SHEET 5 B 5 ILE A 97 VAL A 98 1 O ILE A 97 N VAL A 67
SHEET 1 C 2 TYR A 49 LYS A 50 0
SHEET 2 C 2 ALA A 73 LYS A 74 -1 O ALA A 73 N LYS A 50
SHEET 1 D 6 GLU A 122 SER A 128 0
SHEET 2 D 6 GLU A 133 SER A 140 -1 O VAL A 136 N VAL A 124
SHEET 3 D 6 GLN A 175 ASN A 181 -1 O TRP A 178 N TYR A 137
SHEET 4 D 6 LEU A 187 TRP A 197 -1 O ILE A 188 N LEU A 179
SHEET 5 D 6 PHE A 213 ILE A 222 -1 O LYS A 216 N TYR A 194
SHEET 6 D 6 ILE A 249 VAL A 254 1 O THR A 253 N ALA A 215
SHEET 1 E 4 TYR B 25 ARG B 32 0
SHEET 2 E 4 ILE B 376 CYS B 382 -1 O VAL B 379 N SER B 29
SHEET 3 E 4 LEU B 367 GLU B 372 -1 N SER B 370 O GLN B 378
SHEET 4 E 4 VAL B 355 LEU B 360 -1 N ASP B 357 O ALA B 371
SHEET 1 F 3 VAL B 40 TRP B 42 0
SHEET 2 F 3 PHE B 54 GLY B 62 -1 O ILE B 60 N GLN B 41
SHEET 3 F 3 GLN B 48 GLU B 49 -1 N GLN B 48 O LYS B 56
SHEET 1 G 4 VAL B 40 TRP B 42 0
SHEET 2 G 4 PHE B 54 GLY B 62 -1 O ILE B 60 N GLN B 41
SHEET 3 G 4 ASN B 71 PRO B 81 -1 O LEU B 80 N ILE B 55
SHEET 4 G 4 ASN B 108 HIS B 117 -1 O ARG B 110 N GLU B 77
SHEET 1 H 4 ILE B 121 MET B 127 0
SHEET 2 H 4 ASP B 130 ASN B 138 -1 O ALA B 135 N ARG B 125
SHEET 3 H 4 THR B 143 SER B 147 -1 O TYR B 146 N VAL B 134
SHEET 4 H 4 GLY B 151 LEU B 156 -1 O LEU B 156 N THR B 143
SHEET 1 I 4 ALA B 165 PHE B 168 0
SHEET 2 I 4 ARG B 175 GLY B 179 -1 O LEU B 177 N SER B 167
SHEET 3 I 4 VAL B 185 GLU B 189 -1 O TRP B 188 N LEU B 176
SHEET 4 I 4 ARG B 201 TRP B 203 -1 O ARG B 201 N LEU B 187
SHEET 1 J 4 ILE B 211 TRP B 216 0
SHEET 2 J 4 LEU B 223 SER B 228 -1 O GLY B 225 N LYS B 215
SHEET 3 J 4 LEU B 232 ASP B 237 -1 O ASN B 236 N PHE B 224
SHEET 4 J 4 THR B 244 LYS B 249 -1 O VAL B 248 N LEU B 233
SHEET 1 K 4 PHE B 254 PHE B 259 0
SHEET 2 K 4 LEU B 266 GLY B 271 -1 O ALA B 268 N ALA B 258
SHEET 3 K 4 VAL B 276 ASP B 280 -1 O TYR B 277 N ALA B 269
SHEET 4 K 4 HIS B 289 MET B 291 -1 O HIS B 289 N LEU B 278
SHEET 1 L 4 VAL B 298 PHE B 303 0
SHEET 2 L 4 VAL B 310 GLY B 315 -1 O SER B 314 N ASN B 299
SHEET 3 L 4 LEU B 320 ASP B 324 -1 O TRP B 323 N VAL B 311
SHEET 4 L 4 LEU B 344 HIS B 348 -1 O HIS B 348 N LEU B 320
LINK C LEU B 33 N TPO B 34 1555 1555 1.33
LINK C TPO B 34 N TRP B 35 1555 1555 1.33
SITE 1 AC1 13 SER A 218 PHE A 220 ILE A 222 GLN A 227
SITE 2 AC1 13 ASN A 228 LYS A 229 GLY A 230 GLY A 232
SITE 3 AC1 13 SER A 233 ASN A 258 ARG A 267 HOH A 529
SITE 4 AC1 13 LYS C 14
CRYST1 77.986 98.441 124.757 90.00 90.00 90.00 P 21 21 21 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 0.012823 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010158 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008016 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
