HEADER TRANSCRIPTION 07-JUN-06 2H8N
TITLE STRUCTURE OF A GLUTAMINE-RICH DOMAIN FROM HISTONE DEACETYLASE 4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: N-TERMINAL GLUTAMINE-RICH DOMAIN, RESIDUES 62-129;
COMPND 5 SYNONYM: HD4;
COMPND 6 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: HDAC4, KIAA0288;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA HELIX, POLAR ZIPPER, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR L.GUO,A.HAN,D.L.BATES,L.CHEN
REVDAT 4 14-FEB-24 2H8N 1 SEQADV
REVDAT 3 24-FEB-09 2H8N 1 VERSN
REVDAT 2 03-APR-07 2H8N 1 JRNL
REVDAT 1 27-FEB-07 2H8N 0
JRNL AUTH L.GUO,A.HAN,D.L.BATES,J.CAO,L.CHEN
JRNL TITL CRYSTAL STRUCTURE OF A CONSERVED N-TERMINAL DOMAIN OF
JRNL TITL 2 HISTONE DEACETYLASE 4 REVEALS FUNCTIONAL INSIGHTS INTO
JRNL TITL 3 GLUTAMINE-RICH DOMAINS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 4297 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17360518
JRNL DOI 10.1073/PNAS.0608041104
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 6.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 16845
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.281
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1702
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2324
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 42.39200
REMARK 3 B22 (A**2) : -24.86500
REMARK 3 B33 (A**2) : -17.52800
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 7.49400
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 2.801 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.822 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 4.797 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 8.211 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038067.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.12710
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : ADSC
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19701
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 6.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
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) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
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: SAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: THE REFLECTIONS IN THE STRUCTURE FACTOR FILE WERE SCALED
REMARK 200 TO 2.3A, THE STRUCTURE WAS REFINED TO 2.6A. ALTHOUGH THE
REMARK 200 DIFFRACTION WENT TO 2.3A, DUE TO SEVERE ANISOTROPIC EFFECT,
REMARK 200 USEFUL DATA WAS ONLY TO 2.6A.
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.825M LITHIUM SULFATE, 55MM HEPES PH
REMARK 280 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 7.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 93.69900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.22550
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 93.69900
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 30.22550
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 300 REMARK: THE TETRAMER IN THE ASYMMETRIC UNIT IS THE BIOLOGICAL
REMARK 300 ASSEMBLY, NO CRYSTALLOGRAPHIC SYMMETRY IS INVOVLED IN THE TETRAMER
REMARK 300 FORMATION.
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -69.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 GLY A 42
REMARK 465 SER A 43
REMARK 465 SER A 44
REMARK 465 HIS A 45
REMARK 465 HIS A 46
REMARK 465 HIS A 47
REMARK 465 HIS A 48
REMARK 465 HIS A 49
REMARK 465 HIS A 50
REMARK 465 SER A 51
REMARK 465 SER A 52
REMARK 465 GLY A 53
REMARK 465 LEU A 54
REMARK 465 VAL A 55
REMARK 465 PRO A 56
REMARK 465 ARG A 57
REMARK 465 GLY A 58
REMARK 465 SER A 59
REMARK 465 HIS A 60
REMARK 465 MET A 61
REMARK 465 HIS A 130
REMARK 465 GLN A 131
REMARK 465 ARG A 132
REMARK 465 LYS A 133
REMARK 465 LEU A 134
REMARK 465 GLU A 135
REMARK 465 ARG A 136
REMARK 465 HIS A 137
REMARK 465 ARG A 138
REMARK 465 GLN A 139
REMARK 465 GLU A 140
REMARK 465 GLN A 141
REMARK 465 GLU A 142
REMARK 465 LEU A 143
REMARK 465 GLU A 144
REMARK 465 LYS A 145
REMARK 465 GLN A 146
REMARK 465 HIS A 147
REMARK 465 ARG A 148
REMARK 465 GLU A 149
REMARK 465 GLN A 150
REMARK 465 LYS A 151
REMARK 465 LEU A 152
REMARK 465 GLN A 153
REMARK 465 GLY B 42
REMARK 465 SER B 43
REMARK 465 SER B 44
REMARK 465 HIS B 45
REMARK 465 HIS B 46
REMARK 465 HIS B 47
REMARK 465 HIS B 48
REMARK 465 HIS B 49
REMARK 465 HIS B 50
REMARK 465 SER B 51
REMARK 465 SER B 52
REMARK 465 GLY B 53
REMARK 465 LEU B 54
REMARK 465 VAL B 55
REMARK 465 PRO B 56
REMARK 465 ARG B 57
REMARK 465 GLY B 58
REMARK 465 SER B 59
REMARK 465 HIS B 60
REMARK 465 MET B 61
REMARK 465 HIS B 130
REMARK 465 GLN B 131
REMARK 465 ARG B 132
REMARK 465 LYS B 133
REMARK 465 LEU B 134
REMARK 465 GLU B 135
REMARK 465 ARG B 136
REMARK 465 HIS B 137
REMARK 465 ARG B 138
REMARK 465 GLN B 139
REMARK 465 GLU B 140
REMARK 465 GLN B 141
REMARK 465 GLU B 142
REMARK 465 LEU B 143
REMARK 465 GLU B 144
REMARK 465 LYS B 145
REMARK 465 GLN B 146
REMARK 465 HIS B 147
REMARK 465 ARG B 148
REMARK 465 GLU B 149
REMARK 465 GLN B 150
REMARK 465 LYS B 151
REMARK 465 LEU B 152
REMARK 465 GLN B 153
REMARK 465 GLY C 42
REMARK 465 SER C 43
REMARK 465 SER C 44
REMARK 465 HIS C 45
REMARK 465 HIS C 46
REMARK 465 HIS C 47
REMARK 465 HIS C 48
REMARK 465 HIS C 49
REMARK 465 HIS C 50
REMARK 465 SER C 51
REMARK 465 SER C 52
REMARK 465 GLY C 53
REMARK 465 LEU C 54
REMARK 465 VAL C 55
REMARK 465 PRO C 56
REMARK 465 ARG C 57
REMARK 465 GLY C 58
REMARK 465 SER C 59
REMARK 465 HIS C 60
REMARK 465 MET C 61
REMARK 465 HIS C 130
REMARK 465 GLN C 131
REMARK 465 ARG C 132
REMARK 465 LYS C 133
REMARK 465 LEU C 134
REMARK 465 GLU C 135
REMARK 465 ARG C 136
REMARK 465 HIS C 137
REMARK 465 ARG C 138
REMARK 465 GLN C 139
REMARK 465 GLU C 140
REMARK 465 GLN C 141
REMARK 465 GLU C 142
REMARK 465 LEU C 143
REMARK 465 GLU C 144
REMARK 465 LYS C 145
REMARK 465 GLN C 146
REMARK 465 HIS C 147
REMARK 465 ARG C 148
REMARK 465 GLU C 149
REMARK 465 GLN C 150
REMARK 465 LYS C 151
REMARK 465 LEU C 152
REMARK 465 GLN C 153
REMARK 465 GLY D 42
REMARK 465 SER D 43
REMARK 465 SER D 44
REMARK 465 HIS D 45
REMARK 465 HIS D 46
REMARK 465 HIS D 47
REMARK 465 HIS D 48
REMARK 465 HIS D 49
REMARK 465 HIS D 50
REMARK 465 SER D 51
REMARK 465 SER D 52
REMARK 465 GLY D 53
REMARK 465 LEU D 54
REMARK 465 VAL D 55
REMARK 465 PRO D 56
REMARK 465 ARG D 57
REMARK 465 GLY D 58
REMARK 465 SER D 59
REMARK 465 HIS D 60
REMARK 465 MET D 61
REMARK 465 HIS D 130
REMARK 465 GLN D 131
REMARK 465 ARG D 132
REMARK 465 LYS D 133
REMARK 465 LEU D 134
REMARK 465 GLU D 135
REMARK 465 ARG D 136
REMARK 465 HIS D 137
REMARK 465 ARG D 138
REMARK 465 GLN D 139
REMARK 465 GLU D 140
REMARK 465 GLN D 141
REMARK 465 GLU D 142
REMARK 465 LEU D 143
REMARK 465 GLU D 144
REMARK 465 LYS D 145
REMARK 465 GLN D 146
REMARK 465 HIS D 147
REMARK 465 ARG D 148
REMARK 465 GLU D 149
REMARK 465 GLN D 150
REMARK 465 LYS D 151
REMARK 465 LEU D 152
REMARK 465 GLN D 153
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 GLU A 63 -72.58 -165.96
REMARK 500 GLN A 114 -25.77 -150.07
REMARK 500 HIS A 123 -36.84 -142.15
REMARK 500 GLU B 63 -68.14 -160.05
REMARK 500 ALA B 120 -73.65 -68.94
REMARK 500 MET B 121 -5.50 -57.52
REMARK 500 GLU C 63 -65.01 -171.17
REMARK 500 ALA C 120 -76.41 -64.05
REMARK 500 MET C 121 -5.45 -58.69
REMARK 500 GLU D 63 -68.95 -172.27
REMARK 500 GLN D 116 -74.71 -76.98
REMARK 500 ALA D 120 -72.79 -72.35
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2H8N A 62 153 UNP P56524 HDAC4_HUMAN 62 153
DBREF 2H8N B 62 153 UNP P56524 HDAC4_HUMAN 62 153
DBREF 2H8N C 62 153 UNP P56524 HDAC4_HUMAN 62 153
DBREF 2H8N D 62 153 UNP P56524 HDAC4_HUMAN 62 153
SEQADV 2H8N GLY A 42 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER A 43 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER A 44 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS A 45 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS A 46 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS A 47 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS A 48 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS A 49 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS A 50 UNP P56524 EXPRESSION TAG
SEQADV 2H8N SER A 51 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER A 52 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY A 53 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N LEU A 54 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N VAL A 55 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N PRO A 56 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N ARG A 57 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY A 58 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER A 59 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS A 60 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N MET A 61 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY B 42 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER B 43 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER B 44 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS B 45 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS B 46 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS B 47 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS B 48 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS B 49 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS B 50 UNP P56524 EXPRESSION TAG
SEQADV 2H8N SER B 51 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER B 52 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY B 53 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N LEU B 54 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N VAL B 55 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N PRO B 56 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N ARG B 57 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY B 58 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER B 59 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS B 60 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N MET B 61 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY C 42 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER C 43 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER C 44 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS C 45 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS C 46 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS C 47 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS C 48 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS C 49 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS C 50 UNP P56524 EXPRESSION TAG
SEQADV 2H8N SER C 51 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER C 52 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY C 53 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N LEU C 54 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N VAL C 55 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N PRO C 56 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N ARG C 57 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY C 58 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER C 59 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS C 60 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N MET C 61 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY D 42 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER D 43 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER D 44 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS D 45 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS D 46 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS D 47 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS D 48 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS D 49 UNP P56524 EXPRESSION TAG
SEQADV 2H8N HIS D 50 UNP P56524 EXPRESSION TAG
SEQADV 2H8N SER D 51 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER D 52 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY D 53 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N LEU D 54 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N VAL D 55 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N PRO D 56 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N ARG D 57 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N GLY D 58 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N SER D 59 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N HIS D 60 UNP P56524 CLONING ARTIFACT
SEQADV 2H8N MET D 61 UNP P56524 CLONING ARTIFACT
SEQRES 1 A 112 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 A 112 VAL PRO ARG GLY SER HIS MET ALA GLU PRO ALA LEU ARG
SEQRES 3 A 112 GLU GLN GLN LEU GLN GLN GLU LEU LEU ALA LEU LYS GLN
SEQRES 4 A 112 LYS GLN GLN ILE GLN ARG GLN ILE LEU ILE ALA GLU PHE
SEQRES 5 A 112 GLN ARG GLN HIS GLU GLN LEU SER ARG GLN HIS GLU ALA
SEQRES 6 A 112 GLN LEU HIS GLU HIS ILE LYS GLN GLN GLN GLU MET LEU
SEQRES 7 A 112 ALA MET LYS HIS GLN GLN GLU LEU LEU GLU HIS GLN ARG
SEQRES 8 A 112 LYS LEU GLU ARG HIS ARG GLN GLU GLN GLU LEU GLU LYS
SEQRES 9 A 112 GLN HIS ARG GLU GLN LYS LEU GLN
SEQRES 1 B 112 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 B 112 VAL PRO ARG GLY SER HIS MET ALA GLU PRO ALA LEU ARG
SEQRES 3 B 112 GLU GLN GLN LEU GLN GLN GLU LEU LEU ALA LEU LYS GLN
SEQRES 4 B 112 LYS GLN GLN ILE GLN ARG GLN ILE LEU ILE ALA GLU PHE
SEQRES 5 B 112 GLN ARG GLN HIS GLU GLN LEU SER ARG GLN HIS GLU ALA
SEQRES 6 B 112 GLN LEU HIS GLU HIS ILE LYS GLN GLN GLN GLU MET LEU
SEQRES 7 B 112 ALA MET LYS HIS GLN GLN GLU LEU LEU GLU HIS GLN ARG
SEQRES 8 B 112 LYS LEU GLU ARG HIS ARG GLN GLU GLN GLU LEU GLU LYS
SEQRES 9 B 112 GLN HIS ARG GLU GLN LYS LEU GLN
SEQRES 1 C 112 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 C 112 VAL PRO ARG GLY SER HIS MET ALA GLU PRO ALA LEU ARG
SEQRES 3 C 112 GLU GLN GLN LEU GLN GLN GLU LEU LEU ALA LEU LYS GLN
SEQRES 4 C 112 LYS GLN GLN ILE GLN ARG GLN ILE LEU ILE ALA GLU PHE
SEQRES 5 C 112 GLN ARG GLN HIS GLU GLN LEU SER ARG GLN HIS GLU ALA
SEQRES 6 C 112 GLN LEU HIS GLU HIS ILE LYS GLN GLN GLN GLU MET LEU
SEQRES 7 C 112 ALA MET LYS HIS GLN GLN GLU LEU LEU GLU HIS GLN ARG
SEQRES 8 C 112 LYS LEU GLU ARG HIS ARG GLN GLU GLN GLU LEU GLU LYS
SEQRES 9 C 112 GLN HIS ARG GLU GLN LYS LEU GLN
SEQRES 1 D 112 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU
SEQRES 2 D 112 VAL PRO ARG GLY SER HIS MET ALA GLU PRO ALA LEU ARG
SEQRES 3 D 112 GLU GLN GLN LEU GLN GLN GLU LEU LEU ALA LEU LYS GLN
SEQRES 4 D 112 LYS GLN GLN ILE GLN ARG GLN ILE LEU ILE ALA GLU PHE
SEQRES 5 D 112 GLN ARG GLN HIS GLU GLN LEU SER ARG GLN HIS GLU ALA
SEQRES 6 D 112 GLN LEU HIS GLU HIS ILE LYS GLN GLN GLN GLU MET LEU
SEQRES 7 D 112 ALA MET LYS HIS GLN GLN GLU LEU LEU GLU HIS GLN ARG
SEQRES 8 D 112 LYS LEU GLU ARG HIS ARG GLN GLU GLN GLU LEU GLU LYS
SEQRES 9 D 112 GLN HIS ARG GLU GLN LYS LEU GLN
HELIX 1 1 GLU A 63 LYS A 122 1 60
HELIX 2 2 GLN A 124 GLU A 129 5 6
HELIX 3 3 GLU B 63 LYS B 122 1 60
HELIX 4 4 GLN B 124 GLU B 129 5 6
HELIX 5 5 GLU C 63 LYS C 122 1 60
HELIX 6 6 GLN C 124 GLU C 129 5 6
HELIX 7 7 GLU D 63 LYS D 122 1 60
HELIX 8 8 GLN D 124 GLU D 129 5 6
CRYST1 187.398 60.451 60.450 90.00 108.74 90.00 C 1 2 1 16
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 0.005336 0.000000 0.001810 0.00000
SCALE2 0.000000 0.016542 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017469 0.00000
(ATOM LINES ARE NOT SHOWN.)
END