HEADER HYDROLASE 11-FEB-18 6CEC
TITLE CRYSTAL STRUCTURE OF FRAGMENT 3-(3-METHOXY-2-QUINOXALINYL)PROPANOIC
TITLE 2 ACID BOUND IN THE UBIQUITIN BINDING POCKET OF THE HDAC6 ZINC-FINGER
TITLE 3 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE 6;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: HD6;
COMPND 5 EC: 3.5.1.98;
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: HDAC6, KIAA0901, JM21;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) CODON PLUS;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28-LIC
KEYWDS HISTONE DEACETYLASE, HDAC, HDAC6, UBIQUITIN, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.HARDING,L.HALABELIAN,R.FERREIRA DE FREITAS,I.FRANZONI,
AUTHOR 2 M.RAVICHANDRAN,M.LAUTENS,V.SANTHAKUMAR,M.SCHAPIRA,C.BOUNTRA,
AUTHOR 3 A.M.EDWARDS,C.M.ARROWSMITH,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 04-OCT-23 6CEC 1 REMARK
REVDAT 3 30-MAY-18 6CEC 1 JRNL
REVDAT 2 16-MAY-18 6CEC 1 JRNL
REVDAT 1 28-FEB-18 6CEC 0
JRNL AUTH R.FERREIRA DE FREITAS,R.J.HARDING,I.FRANZONI,M.RAVICHANDRAN,
JRNL AUTH 2 M.K.MANN,H.OUYANG,M.LAUTENS,V.SANTHAKUMAR,C.H.ARROWSMITH,
JRNL AUTH 3 M.SCHAPIRA
JRNL TITL IDENTIFICATION AND STRUCTURE-ACTIVITY RELATIONSHIP OF HDAC6
JRNL TITL 2 ZINC-FINGER UBIQUITIN BINDING DOMAIN INHIBITORS.
JRNL REF J. MED. CHEM. V. 61 4517 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 29741882
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00258
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 14256
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) : 0.163
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.186
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 723
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) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1008
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.61
REMARK 3 BIN R VALUE (WORKING SET) : 0.1740
REMARK 3 BIN FREE R VALUE SET COUNT : 53
REMARK 3 BIN FREE R VALUE : 0.1780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 778
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 69
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.41000
REMARK 3 B22 (A**2) : 2.01000
REMARK 3 B33 (A**2) : -1.60000
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): 0.074
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.073
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.045
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.232
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 854 ; 0.024 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 705 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1174 ; 1.742 ; 1.916
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1635 ; 1.188 ; 3.010
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 103 ; 6.449 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 38 ;34.413 ;24.474
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 111 ;11.835 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 1 ;16.330 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 119 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1026 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 171 ; 0.002 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 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: USERS OF THIS CRYSTAL STRUCTURE: VERIFY
REMARK 3 OUR INTEPRETION OF THE ELECTRON DENSITY. AMPLITUDES AND UNMERGED
REMARK 3 INTENSITIES ARE INCLUDED WITH THIS DEPOSITION. DIFFRACTION
REMARK 3 IMAGES WILL BE DEPOSITED AT A LATER DATE IN A PUBLIC REPOSITORY.
REMARK 3 GEOMETRY RESTRAINTS FOR THE LIGAND WERE PREPARED WITH GRADE.
REMARK 4
REMARK 4 6CEC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-18.
REMARK 100 THE DEPOSITION ID IS D_1000232613.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-FEB-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN A200
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.6.2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 15017
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
REMARK 200 RESOLUTION RANGE LOW (A) : 32.920
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.03600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.22600
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDBID 5KH3
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M NA-FORMATE, 0.2 M NA-ACETATE
REMARK 280 PH4.6, 5 % ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 20.39000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 27.90000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.92000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 27.90000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 20.39000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.92000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 5870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 1107
REMARK 465 GLY A 1208
REMARK 465 GLU A 1209
REMARK 465 ASP A 1210
REMARK 465 MET A 1211
REMARK 465 PRO A 1212
REMARK 465 HIS A 1213
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 LEU A1196 CG CD1 CD2
REMARK 470 GLN A1204 CD OE1 NE2
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 A1135 -71.90 -88.19
REMARK 500 ILE A1157 -99.48 -100.16
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 A1303 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1113 SG
REMARK 620 2 HIS A1115 ND1 111.5
REMARK 620 3 CYS A1183 SG 115.9 97.7
REMARK 620 4 CYS A1186 SG 113.6 104.0 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1302 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1133 SG
REMARK 620 2 CYS A1136 SG 109.9
REMARK 620 3 CYS A1153 SG 112.7 115.2
REMARK 620 4 HIS A1160 ND1 106.6 109.9 101.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1145 SG
REMARK 620 2 CYS A1148 SG 120.0
REMARK 620 3 HIS A1164 NE2 117.2 98.1
REMARK 620 4 HIS A1170 ND1 110.3 99.7 109.7
REMARK 620 N 1 2 3
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 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EY7 A 1309
DBREF 6CEC A 1109 1213 UNP Q9UBN7 HDAC6_HUMAN 1109 1213
SEQADV 6CEC GLY A 1107 UNP Q9UBN7 EXPRESSION TAG
SEQADV 6CEC SER A 1108 UNP Q9UBN7 EXPRESSION TAG
SEQRES 1 A 107 GLY SER PRO LEU PRO TRP CYS PRO HIS LEU VAL ALA VAL
SEQRES 2 A 107 CYS PRO ILE PRO ALA ALA GLY LEU ASP VAL THR GLN PRO
SEQRES 3 A 107 CYS GLY ASP CYS GLY THR ILE GLN GLU ASN TRP VAL CYS
SEQRES 4 A 107 LEU SER CYS TYR GLN VAL TYR CYS GLY ARG TYR ILE ASN
SEQRES 5 A 107 GLY HIS MET LEU GLN HIS HIS GLY ASN SER GLY HIS PRO
SEQRES 6 A 107 LEU VAL LEU SER TYR ILE ASP LEU SER ALA TRP CYS TYR
SEQRES 7 A 107 TYR CYS GLN ALA TYR VAL HIS HIS GLN ALA LEU LEU ASP
SEQRES 8 A 107 VAL LYS ASN ILE ALA HIS GLN ASN LYS PHE GLY GLU ASP
SEQRES 9 A 107 MET PRO HIS
HET ZN A1301 1
HET ZN A1302 1
HET ZN A1303 1
HET UNX A1304 1
HET UNX A1305 1
HET UNX A1306 1
HET UNX A1307 1
HET UNX A1308 1
HET EY7 A1309 17
HETNAM ZN ZINC ION
HETNAM UNX UNKNOWN ATOM OR ION
HETNAM EY7 3-(3-METHOXYQUINOXALIN-2-YL)PROPANOIC ACID
FORMUL 2 ZN 3(ZN 2+)
FORMUL 5 UNX 5(X)
FORMUL 10 EY7 C12 H12 N2 O3
FORMUL 11 HOH *69(H2 O)
HELIX 1 AA1 HIS A 1115 VAL A 1119 5 5
HELIX 2 AA2 GLY A 1159 GLY A 1169 1 11
HELIX 3 AA3 HIS A 1192 ALA A 1194 5 3
HELIX 4 AA4 LEU A 1195 PHE A 1207 1 13
SHEET 1 AA1 5 VAL A1151 CYS A1153 0
SHEET 2 AA1 5 ASN A1142 CYS A1145 -1 N TRP A1143 O TYR A1152
SHEET 3 AA1 5 LEU A1172 SER A1175 -1 O LEU A1174 N VAL A1144
SHEET 4 AA1 5 ALA A1181 CYS A1183 -1 O TRP A1182 N VAL A1173
SHEET 5 AA1 5 ALA A1188 TYR A1189 -1 O ALA A1188 N CYS A1183
LINK SG CYS A1113 ZN ZN A1303 1555 1555 2.30
LINK ND1 HIS A1115 ZN ZN A1303 1555 1555 2.10
LINK SG CYS A1133 ZN ZN A1302 1555 1555 2.32
LINK SG CYS A1136 ZN ZN A1302 1555 1555 2.31
LINK SG CYS A1145 ZN ZN A1301 1555 1555 2.35
LINK SG CYS A1148 ZN ZN A1301 1555 1555 2.90
LINK SG CYS A1153 ZN ZN A1302 1555 1555 2.35
LINK ND1 HIS A1160 ZN ZN A1302 1555 1555 2.05
LINK NE2 HIS A1164 ZN ZN A1301 1555 1555 2.02
LINK ND1 HIS A1170 ZN ZN A1301 1555 1555 2.03
LINK SG CYS A1183 ZN ZN A1303 1555 1555 2.32
LINK SG CYS A1186 ZN ZN A1303 1555 1555 2.39
SITE 1 AC1 4 CYS A1145 CYS A1148 HIS A1164 HIS A1170
SITE 1 AC2 4 CYS A1133 CYS A1136 CYS A1153 HIS A1160
SITE 1 AC3 4 CYS A1113 HIS A1115 CYS A1183 CYS A1186
SITE 1 AC4 9 TRP A1143 GLY A1154 ARG A1155 TRP A1182
SITE 2 AC4 9 TYR A1184 TYR A1189 HIS A1203 HOH A1415
SITE 3 AC4 9 HOH A1448
CRYST1 40.780 43.840 55.800 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 0.024522 0.000000 0.000000 0.00000
SCALE2 0.000000 0.022810 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017921 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
