HEADER HYDROLASE 21-JAN-08 3C10
TITLE CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE DEACETYLASE
TITLE 2 HDAC7 IN COMPLEX WITH TRICHOSTATIN A (TSA)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE 7A;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN: RESIDUES 482-903;
COMPND 5 SYNONYM: HD7A, HDAC7;
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: HDAC7A, HDAC7;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-MHL
KEYWDS HDAC, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 ALTERNATIVE SPLICING, CHROMATIN REGULATOR, CYTOPLASM, HYDROLASE,
KEYWDS 3 NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, REPRESSOR, TRANSCRIPTION,
KEYWDS 4 TRANSCRIPTION REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MIN,A.SCHUETZ,P.LOPPNAU,J.WEIGELT,M.SUNDSTROM,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,A.BOCHKAREV,A.N.PLOTNIKOV,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (SGC)
REVDAT 4 30-AUG-23 3C10 1 REMARK SEQADV LINK
REVDAT 3 27-OCT-09 3C10 1 JRNL
REVDAT 2 24-FEB-09 3C10 1 VERSN
REVDAT 1 19-FEB-08 3C10 0
SPRSDE 19-FEB-08 3C10 2PQP
JRNL AUTH A.SCHUETZ,J.MIN,A.ALLALI-HASSANI,M.SCHAPIRA,M.SHUEN,
JRNL AUTH 2 P.LOPPNAU,R.MAZITSCHEK,N.P.KWIATKOWSKI,T.A.LEWIS,
JRNL AUTH 3 R.L.MAGLATHIN,T.H.MCLEAN,A.BOCHKAREV,A.N.PLOTNIKOV,M.VEDADI,
JRNL AUTH 4 C.H.ARROWSMITH
JRNL TITL HUMAN HDAC7 HARBORS A CLASS IIA HISTONE DEACETYLASE-SPECIFIC
JRNL TITL 2 ZINC BINDING MOTIF AND CRYPTIC DEACETYLASE ACTIVITY.
JRNL REF J.BIOL.CHEM. V. 283 11355 2008
JRNL REFN ISSN 0021-9258
JRNL PMID 18285338
JRNL DOI 10.1074/JBC.M707362200
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.42
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 69791
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3651
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3989
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2650
REMARK 3 BIN FREE R VALUE SET COUNT : 206
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8424
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 78
REMARK 3 SOLVENT ATOMS : 459
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.04000
REMARK 3 B22 (A**2) : 0.04000
REMARK 3 B33 (A**2) : -0.06000
REMARK 3 B12 (A**2) : 0.02000
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): 0.212
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.193
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.147
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.243
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8726 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11790 ; 1.689 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1104 ; 7.388 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 396 ;38.708 ;23.712
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1330 ;17.874 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 56 ;19.447 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1262 ; 0.124 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6790 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4203 ; 0.221 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5841 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 487 ; 0.166 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 12 ; 0.283 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 86 ; 0.226 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.184 ; 0.200
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): 5499 ; 1.001 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8714 ; 1.678 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3254 ; 2.656 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3076 ; 4.007 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3C10 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046205.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.10000
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73439
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.04100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 79.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.23800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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 2NVR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3350, 0.1 M HEPES PH 7.5, 10
REMARK 280 % ISOPROPANOL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 300K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 99.31333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 49.65667
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 GLY A 481
REMARK 465 SER A 482
REMARK 465 ARG A 483
REMARK 465 ALA A 484
REMARK 465 GLN A 485
REMARK 465 SER A 486
REMARK 465 SER A 487
REMARK 465 PRO A 488
REMARK 465 ALA A 489
REMARK 465 ALA A 490
REMARK 465 PRO A 491
REMARK 465 ALA A 492
REMARK 465 SER A 493
REMARK 465 LEU A 494
REMARK 465 SER A 495
REMARK 465 ALA A 496
REMARK 465 PRO A 497
REMARK 465 GLU A 498
REMARK 465 PRO A 499
REMARK 465 ALA A 500
REMARK 465 SER A 501
REMARK 465 GLN A 502
REMARK 465 ALA A 503
REMARK 465 ARG A 504
REMARK 465 VAL A 505
REMARK 465 LEU A 506
REMARK 465 SER A 507
REMARK 465 SER A 508
REMARK 465 SER A 509
REMARK 465 GLU A 510
REMARK 465 THR A 511
REMARK 465 PRO A 512
REMARK 465 ALA A 513
REMARK 465 ARG A 514
REMARK 465 ARG A 611
REMARK 465 MET A 612
REMARK 465 PHE A 613
REMARK 465 LEU A 901
REMARK 465 ALA A 902
REMARK 465 SER A 903
REMARK 465 GLY B 481
REMARK 465 SER B 482
REMARK 465 ARG B 483
REMARK 465 ALA B 484
REMARK 465 GLN B 485
REMARK 465 SER B 486
REMARK 465 SER B 487
REMARK 465 PRO B 488
REMARK 465 ALA B 489
REMARK 465 ALA B 490
REMARK 465 PRO B 491
REMARK 465 ALA B 492
REMARK 465 SER B 493
REMARK 465 LEU B 494
REMARK 465 SER B 495
REMARK 465 ALA B 496
REMARK 465 PRO B 497
REMARK 465 GLU B 498
REMARK 465 PRO B 499
REMARK 465 ALA B 500
REMARK 465 SER B 501
REMARK 465 GLN B 502
REMARK 465 ALA B 503
REMARK 465 ARG B 504
REMARK 465 VAL B 505
REMARK 465 LEU B 506
REMARK 465 SER B 507
REMARK 465 SER B 508
REMARK 465 SER B 509
REMARK 465 GLU B 510
REMARK 465 THR B 511
REMARK 465 PRO B 512
REMARK 465 ALA B 513
REMARK 465 ARG B 514
REMARK 465 THR B 515
REMARK 465 ARG B 596
REMARK 465 LEU B 597
REMARK 465 LYS B 598
REMARK 465 LEU B 599
REMARK 465 ASP B 600
REMARK 465 ASN B 601
REMARK 465 GLY B 602
REMARK 465 LYS B 603
REMARK 465 LEU B 604
REMARK 465 ALA B 605
REMARK 465 GLY B 606
REMARK 465 LEU B 607
REMARK 465 LEU B 608
REMARK 465 ALA B 609
REMARK 465 GLN B 610
REMARK 465 ARG B 611
REMARK 465 MET B 612
REMARK 465 PHE B 613
REMARK 465 ALA B 902
REMARK 465 SER B 903
REMARK 465 GLY C 481
REMARK 465 SER C 482
REMARK 465 ARG C 483
REMARK 465 ALA C 484
REMARK 465 GLN C 485
REMARK 465 SER C 486
REMARK 465 SER C 487
REMARK 465 PRO C 488
REMARK 465 ALA C 489
REMARK 465 ALA C 490
REMARK 465 PRO C 491
REMARK 465 ALA C 492
REMARK 465 SER C 493
REMARK 465 LEU C 494
REMARK 465 SER C 495
REMARK 465 ALA C 496
REMARK 465 PRO C 497
REMARK 465 GLU C 498
REMARK 465 PRO C 499
REMARK 465 ALA C 500
REMARK 465 SER C 501
REMARK 465 GLN C 502
REMARK 465 ALA C 503
REMARK 465 ARG C 504
REMARK 465 VAL C 505
REMARK 465 LEU C 506
REMARK 465 SER C 507
REMARK 465 SER C 508
REMARK 465 SER C 509
REMARK 465 GLU C 510
REMARK 465 THR C 511
REMARK 465 PRO C 512
REMARK 465 ALA C 513
REMARK 465 ARG C 514
REMARK 465 THR C 515
REMARK 465 LEU C 516
REMARK 465 PRO C 517
REMARK 465 PHE C 518
REMARK 465 LEU C 594
REMARK 465 SER C 595
REMARK 465 ARG C 596
REMARK 465 LEU C 597
REMARK 465 LYS C 598
REMARK 465 LEU C 599
REMARK 465 ASP C 600
REMARK 465 ASN C 601
REMARK 465 GLY C 602
REMARK 465 LYS C 603
REMARK 465 LEU C 604
REMARK 465 ALA C 605
REMARK 465 GLY C 606
REMARK 465 LEU C 607
REMARK 465 LEU C 608
REMARK 465 ALA C 609
REMARK 465 GLN C 610
REMARK 465 ARG C 611
REMARK 465 MET C 612
REMARK 465 PHE C 613
REMARK 465 VAL C 614
REMARK 465 MET C 615
REMARK 465 ARG C 900
REMARK 465 LEU C 901
REMARK 465 ALA C 902
REMARK 465 SER C 903
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 A 596 CB CG CD NE CZ NH1 NH2
REMARK 470 LYS A 598 CG CD CE NZ
REMARK 470 LEU B 867 CG CD1 CD2
REMARK 470 GLU B 870 CB CG CD OE1 OE2
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 GLY C 833 O HOH C 938 1.95
REMARK 500 OD1 ASP B 733 O HOH B 1035 2.04
REMARK 500 K K C 202 O HOH C 906 2.11
REMARK 500 O THR A 519 N LYS A 658 2.16
REMARK 500 O HOH B 940 O HOH B 1044 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MET A 769 CG - SD - CE ANGL. DEV. = 9.7 DEGREES
REMARK 500 ARG B 690 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
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 PHE A 679 -4.25 80.85
REMARK 500 SER A 790 67.35 64.77
REMARK 500 ALA A 798 75.05 -100.52
REMARK 500 GLU A 840 -110.70 -118.12
REMARK 500 PHE B 518 65.92 -63.15
REMARK 500 THR B 519 -164.61 -127.97
REMARK 500 HIS B 531 97.01 -66.01
REMARK 500 ASP B 733 53.97 34.43
REMARK 500 PRO B 809 30.11 -94.67
REMARK 500 GLU B 840 -119.89 -117.52
REMARK 500 LEU B 867 -18.45 79.11
REMARK 500 ASN C 592 -90.00 -72.45
REMARK 500 ARG C 655 -2.05 90.37
REMARK 500 ALA C 698 138.49 -175.67
REMARK 500 ALA C 808 -86.82 -11.12
REMARK 500 ALA C 831 18.80 56.22
REMARK 500 GLU C 840 -108.73 -113.67
REMARK 500 GLN C 874 150.06 -45.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 ALA C 808 PRO C 809 -115.56
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 K A 202 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 4 O
REMARK 620 2 HOH A 42 O 87.3
REMARK 620 3 PHE A 718 O 81.2 74.1
REMARK 620 4 ASP A 721 O 159.2 108.1 89.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TSN A 301 O1
REMARK 620 2 ASP A 707 OD1 96.3
REMARK 620 3 HIS A 709 ND1 96.2 104.5
REMARK 620 4 ASP A 801 OD2 152.3 103.4 97.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 533 SG
REMARK 620 2 CYS A 535 SG 109.5
REMARK 620 3 HIS A 541 NE2 106.9 97.2
REMARK 620 4 CYS A 618 SG 100.1 123.3 119.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 201 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 705 O
REMARK 620 2 ASP A 705 OD1 73.6
REMARK 620 3 ASP A 707 O 100.3 99.6
REMARK 620 4 HIS A 709 O 166.2 93.1 78.0
REMARK 620 5 SER A 728 OG 80.5 108.9 150.3 107.8
REMARK 620 6 LEU A 729 O 73.9 141.3 66.5 117.0 85.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TSN B 301 O1
REMARK 620 2 ASP B 707 OD1 84.0
REMARK 620 3 HIS B 709 ND1 113.5 101.9
REMARK 620 4 ASP B 801 OD2 146.2 107.5 95.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 533 SG
REMARK 620 2 CYS B 535 SG 110.9
REMARK 620 3 HIS B 541 NE2 107.7 95.7
REMARK 620 4 CYS B 618 SG 112.3 114.4 114.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 201 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 705 O
REMARK 620 2 ASP B 705 OD1 71.2
REMARK 620 3 ASP B 707 O 104.0 96.6
REMARK 620 4 HIS B 709 O 161.0 90.4 72.7
REMARK 620 5 SER B 728 OG 83.2 110.2 153.1 108.4
REMARK 620 6 LEU B 729 O 76.3 139.4 68.2 117.9 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 202 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 718 O
REMARK 620 2 ASP B 721 O 95.9
REMARK 620 3 VAL B 724 O 142.2 79.7
REMARK 620 4 HOH B 907 O 89.3 157.9 83.1
REMARK 620 5 HOH B 913 O 85.8 109.6 131.3 92.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 TSN C 301 O1
REMARK 620 2 ASP C 707 OD1 89.2
REMARK 620 3 HIS C 709 ND1 108.1 98.1
REMARK 620 4 ASP C 801 OD2 159.1 99.7 89.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 102 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C 533 SG
REMARK 620 2 CYS C 535 SG 113.9
REMARK 620 3 HIS C 541 NE2 102.2 97.1
REMARK 620 4 CYS C 618 SG 100.0 122.3 120.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 201 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 705 O
REMARK 620 2 ASP C 705 OD1 73.5
REMARK 620 3 ASP C 707 O 97.8 97.0
REMARK 620 4 HIS C 709 O 162.3 90.3 77.0
REMARK 620 5 SER C 728 OG 84.4 113.3 148.8 109.0
REMARK 620 6 LEU C 729 O 75.6 141.2 64.8 115.9 86.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K C 202 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 718 O
REMARK 620 2 ASP C 721 O 96.2
REMARK 620 3 VAL C 724 O 150.5 87.0
REMARK 620 4 HOH C 913 O 75.9 92.3 133.4
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 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TSN C 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2NVR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE DEACETYLASE
REMARK 900 HDAC7
REMARK 900 RELATED ID: 3C0Y RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE DEACETYLASE
REMARK 900 HDAC7
REMARK 900 RELATED ID: 3C0Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF HUMAN HISTONE DEACETYLASE
REMARK 900 HDAC7 IN COMPLEX WITH SAHA
DBREF 3C10 A 482 903 UNP Q8WUI4 HDAC7_HUMAN 482 903
DBREF 3C10 B 482 903 UNP Q8WUI4 HDAC7_HUMAN 482 903
DBREF 3C10 C 482 903 UNP Q8WUI4 HDAC7_HUMAN 482 903
SEQADV 3C10 GLY A 481 UNP Q8WUI4 EXPRESSION TAG
SEQADV 3C10 GLY B 481 UNP Q8WUI4 EXPRESSION TAG
SEQADV 3C10 GLY C 481 UNP Q8WUI4 EXPRESSION TAG
SEQRES 1 A 423 GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER
SEQRES 2 A 423 LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU
SEQRES 3 A 423 SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR
SEQRES 4 A 423 THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN
SEQRES 5 A 423 CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA
SEQRES 6 A 423 GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG
SEQRES 7 A 423 GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS
SEQRES 8 A 423 ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG
SEQRES 9 A 423 HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU
SEQRES 10 A 423 LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN
SEQRES 11 A 423 ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL
SEQRES 12 A 423 ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN
SEQRES 13 A 423 ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA
SEQRES 14 A 423 PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA
SEQRES 15 A 423 VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR
SEQRES 16 A 423 ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA
SEQRES 17 A 423 CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE
SEQRES 18 A 423 LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR
SEQRES 19 A 423 GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE
SEQRES 20 A 423 SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY
SEQRES 21 A 423 SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU
SEQRES 22 A 423 GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP
SEQRES 23 A 423 PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG
SEQRES 24 A 423 ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP
SEQRES 25 A 423 LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY
SEQRES 26 A 423 HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS
SEQRES 27 A 423 CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA
SEQRES 28 A 423 GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP
SEQRES 29 A 423 LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA
SEQRES 30 A 423 ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU
SEQRES 31 A 423 GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER
SEQRES 32 A 423 LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY
SEQRES 33 A 423 CYS MET GLN ARG LEU ALA SER
SEQRES 1 B 423 GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER
SEQRES 2 B 423 LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU
SEQRES 3 B 423 SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR
SEQRES 4 B 423 THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN
SEQRES 5 B 423 CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA
SEQRES 6 B 423 GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG
SEQRES 7 B 423 GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS
SEQRES 8 B 423 ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG
SEQRES 9 B 423 HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU
SEQRES 10 B 423 LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN
SEQRES 11 B 423 ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL
SEQRES 12 B 423 ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN
SEQRES 13 B 423 ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA
SEQRES 14 B 423 PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA
SEQRES 15 B 423 VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR
SEQRES 16 B 423 ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA
SEQRES 17 B 423 CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE
SEQRES 18 B 423 LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR
SEQRES 19 B 423 GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE
SEQRES 20 B 423 SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY
SEQRES 21 B 423 SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU
SEQRES 22 B 423 GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP
SEQRES 23 B 423 PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG
SEQRES 24 B 423 ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP
SEQRES 25 B 423 LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY
SEQRES 26 B 423 HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS
SEQRES 27 B 423 CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA
SEQRES 28 B 423 GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP
SEQRES 29 B 423 LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA
SEQRES 30 B 423 ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU
SEQRES 31 B 423 GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER
SEQRES 32 B 423 LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY
SEQRES 33 B 423 CYS MET GLN ARG LEU ALA SER
SEQRES 1 C 423 GLY SER ARG ALA GLN SER SER PRO ALA ALA PRO ALA SER
SEQRES 2 C 423 LEU SER ALA PRO GLU PRO ALA SER GLN ALA ARG VAL LEU
SEQRES 3 C 423 SER SER SER GLU THR PRO ALA ARG THR LEU PRO PHE THR
SEQRES 4 C 423 THR GLY LEU ILE TYR ASP SER VAL MET LEU LYS HIS GLN
SEQRES 5 C 423 CYS SER CYS GLY ASP ASN SER ARG HIS PRO GLU HIS ALA
SEQRES 6 C 423 GLY ARG ILE GLN SER ILE TRP SER ARG LEU GLN GLU ARG
SEQRES 7 C 423 GLY LEU ARG SER GLN CYS GLU CYS LEU ARG GLY ARG LYS
SEQRES 8 C 423 ALA SER LEU GLU GLU LEU GLN SER VAL HIS SER GLU ARG
SEQRES 9 C 423 HIS VAL LEU LEU TYR GLY THR ASN PRO LEU SER ARG LEU
SEQRES 10 C 423 LYS LEU ASP ASN GLY LYS LEU ALA GLY LEU LEU ALA GLN
SEQRES 11 C 423 ARG MET PHE VAL MET LEU PRO CYS GLY GLY VAL GLY VAL
SEQRES 12 C 423 ASP THR ASP THR ILE TRP ASN GLU LEU HIS SER SER ASN
SEQRES 13 C 423 ALA ALA ARG TRP ALA ALA GLY SER VAL THR ASP LEU ALA
SEQRES 14 C 423 PHE LYS VAL ALA SER ARG GLU LEU LYS ASN GLY PHE ALA
SEQRES 15 C 423 VAL VAL ARG PRO PRO GLY HIS HIS ALA ASP HIS SER THR
SEQRES 16 C 423 ALA MET GLY PHE CYS PHE PHE ASN SER VAL ALA ILE ALA
SEQRES 17 C 423 CYS ARG GLN LEU GLN GLN GLN SER LYS ALA SER LYS ILE
SEQRES 18 C 423 LEU ILE VAL ASP TRP ASP VAL HIS HIS GLY ASN GLY THR
SEQRES 19 C 423 GLN GLN THR PHE TYR GLN ASP PRO SER VAL LEU TYR ILE
SEQRES 20 C 423 SER LEU HIS ARG HIS ASP ASP GLY ASN PHE PHE PRO GLY
SEQRES 21 C 423 SER GLY ALA VAL ASP GLU VAL GLY ALA GLY SER GLY GLU
SEQRES 22 C 423 GLY PHE ASN VAL ASN VAL ALA TRP ALA GLY GLY LEU ASP
SEQRES 23 C 423 PRO PRO MET GLY ASP PRO GLU TYR LEU ALA ALA PHE ARG
SEQRES 24 C 423 ILE VAL VAL MET PRO ILE ALA ARG GLU PHE SER PRO ASP
SEQRES 25 C 423 LEU VAL LEU VAL SER ALA GLY PHE ASP ALA ALA GLU GLY
SEQRES 26 C 423 HIS PRO ALA PRO LEU GLY GLY TYR HIS VAL SER ALA LYS
SEQRES 27 C 423 CYS PHE GLY TYR MET THR GLN GLN LEU MET ASN LEU ALA
SEQRES 28 C 423 GLY GLY ALA VAL VAL LEU ALA LEU GLU GLY GLY HIS ASP
SEQRES 29 C 423 LEU THR ALA ILE CYS ASP ALA SER GLU ALA CYS VAL ALA
SEQRES 30 C 423 ALA LEU LEU GLY ASN ARG VAL ASP PRO LEU SER GLU GLU
SEQRES 31 C 423 GLY TRP LYS GLN LYS PRO ASN LEU ASN ALA ILE ARG SER
SEQRES 32 C 423 LEU GLU ALA VAL ILE ARG VAL HIS SER LYS TYR TRP GLY
SEQRES 33 C 423 CYS MET GLN ARG LEU ALA SER
HET ZN A 101 1
HET ZN A 102 1
HET K A 201 1
HET K A 202 1
HET TSN A 301 22
HET ZN B 101 1
HET ZN B 102 1
HET K B 201 1
HET K B 202 1
HET TSN B 301 22
HET ZN C 101 1
HET ZN C 102 1
HET K C 201 1
HET K C 202 1
HET TSN C 301 22
HETNAM ZN ZINC ION
HETNAM K POTASSIUM ION
HETNAM TSN TRICHOSTATIN A
HETSYN TSN 7-[4-(DIMETHYLAMINO)PHENYL]-N-HYDROXY-4,6-DIMETHYL-7-
HETSYN 2 TSN OXO-2,4-HEPTADIENAMIDE
FORMUL 4 ZN 6(ZN 2+)
FORMUL 6 K 6(K 1+)
FORMUL 8 TSN 3(C17 H22 N2 O3)
FORMUL 19 HOH *459(H2 O)
HELIX 1 1 ASP A 525 HIS A 531 5 7
HELIX 2 2 ASP A 537 HIS A 541 5 5
HELIX 3 3 ALA A 545 ARG A 558 1 14
HELIX 4 4 LEU A 560 CYS A 564 5 5
HELIX 5 5 SER A 573 GLN A 578 1 6
HELIX 6 6 SER A 582 THR A 591 1 10
HELIX 7 7 ASP A 600 GLN A 610 1 11
HELIX 8 8 HIS A 633 SER A 654 1 22
HELIX 9 9 ASN A 683 SER A 696 1 14
HELIX 10 10 GLY A 711 TYR A 719 1 9
HELIX 11 11 ALA A 749 GLU A 753 5 5
HELIX 12 12 GLY A 770 VAL A 781 1 12
HELIX 13 13 VAL A 781 SER A 790 1 10
HELIX 14 14 PRO A 807 GLY A 811 5 5
HELIX 15 15 SER A 816 MET A 828 1 13
HELIX 16 16 ASN A 829 GLY A 833 5 5
HELIX 17 17 ASP A 844 GLY A 861 1 18
HELIX 18 18 ASP A 865 GLU A 869 5 5
HELIX 19 19 GLU A 870 GLN A 874 5 5
HELIX 20 20 ASN A 877 SER A 892 1 16
HELIX 21 21 LYS A 893 TYR A 894 5 2
HELIX 22 22 TRP A 895 GLN A 899 5 5
HELIX 23 23 ASP B 525 HIS B 531 5 7
HELIX 24 24 ALA B 545 ARG B 558 1 14
HELIX 25 25 LEU B 560 CYS B 564 5 5
HELIX 26 26 SER B 573 SER B 579 1 7
HELIX 27 27 SER B 582 THR B 591 1 10
HELIX 28 28 HIS B 633 SER B 654 1 22
HELIX 29 29 ASN B 683 GLN B 695 1 13
HELIX 30 30 GLY B 711 TYR B 719 1 9
HELIX 31 31 ASP B 733 ASN B 736 5 4
HELIX 32 32 ALA B 749 GLU B 753 5 5
HELIX 33 33 GLY B 770 VAL B 781 1 12
HELIX 34 34 VAL B 781 SER B 790 1 10
HELIX 35 35 SER B 816 MET B 828 1 13
HELIX 36 36 ASN B 829 GLY B 833 5 5
HELIX 37 37 ASP B 844 LEU B 860 1 17
HELIX 38 38 ASN B 877 SER B 892 1 16
HELIX 39 39 LYS B 893 TYR B 894 5 2
HELIX 40 40 TRP B 895 GLN B 899 5 5
HELIX 41 41 ASP C 525 HIS C 531 5 7
HELIX 42 42 ALA C 545 ARG C 558 1 14
HELIX 43 43 LEU C 560 CYS C 564 5 5
HELIX 44 44 SER C 573 GLN C 578 1 6
HELIX 45 45 SER C 582 THR C 591 1 10
HELIX 46 46 HIS C 633 SER C 654 1 22
HELIX 47 47 ASN C 683 GLN C 695 1 13
HELIX 48 48 GLY C 711 PHE C 718 1 8
HELIX 49 49 ASP C 733 ASN C 736 5 4
HELIX 50 50 ALA C 749 GLU C 753 5 5
HELIX 51 51 GLY C 770 VAL C 781 1 12
HELIX 52 52 VAL C 781 SER C 790 1 10
HELIX 53 53 PRO C 807 GLY C 811 5 5
HELIX 54 54 SER C 816 MET C 828 1 13
HELIX 55 55 ASN C 829 GLY C 833 5 5
HELIX 56 56 ASP C 844 LEU C 860 1 17
HELIX 57 57 ASP C 865 GLU C 869 5 5
HELIX 58 58 GLU C 870 GLN C 874 5 5
HELIX 59 59 ASN C 877 SER C 892 1 16
HELIX 60 60 LYS C 893 TYR C 894 5 2
HELIX 61 61 TRP C 895 GLN C 899 5 5
SHEET 1 A 8 GLU A 565 LEU A 567 0
SHEET 2 A 8 THR A 520 ILE A 523 1 N LEU A 522 O LEU A 567
SHEET 3 A 8 ASN A 659 ALA A 662 1 O PHE A 661 N GLY A 521
SHEET 4 A 8 VAL A 835 LEU A 839 1 O LEU A 837 N ALA A 662
SHEET 5 A 8 LEU A 793 ALA A 798 1 N VAL A 796 O VAL A 836
SHEET 6 A 8 ILE A 701 ASP A 705 1 N LEU A 702 O LEU A 795
SHEET 7 A 8 VAL A 724 ARG A 731 1 O ILE A 727 N ILE A 703
SHEET 8 A 8 ASN A 756 TRP A 761 1 O VAL A 759 N SER A 728
SHEET 1 B 2 VAL A 621 GLY A 622 0
SHEET 2 B 2 ILE A 628 TRP A 629 -1 O TRP A 629 N VAL A 621
SHEET 1 C 8 GLU B 565 LEU B 567 0
SHEET 2 C 8 THR B 520 ILE B 523 1 N LEU B 522 O LEU B 567
SHEET 3 C 8 ASN B 659 ALA B 662 1 O ASN B 659 N GLY B 521
SHEET 4 C 8 VAL B 835 LEU B 839 1 O LEU B 837 N ALA B 662
SHEET 5 C 8 LEU B 793 ALA B 798 1 N VAL B 796 O VAL B 836
SHEET 6 C 8 ILE B 701 ASP B 705 1 N LEU B 702 O LEU B 795
SHEET 7 C 8 VAL B 724 ARG B 731 1 O LEU B 725 N ILE B 703
SHEET 8 C 8 ASN B 756 TRP B 761 1 O VAL B 759 N SER B 728
SHEET 1 D 2 VAL B 621 GLY B 622 0
SHEET 2 D 2 ILE B 628 TRP B 629 -1 O TRP B 629 N VAL B 621
SHEET 1 E 8 GLU C 565 LEU C 567 0
SHEET 2 E 8 THR C 520 ILE C 523 1 N LEU C 522 O LEU C 567
SHEET 3 E 8 ASN C 659 ALA C 662 1 O PHE C 661 N ILE C 523
SHEET 4 E 8 VAL C 835 LEU C 839 1 O LEU C 837 N ALA C 662
SHEET 5 E 8 LEU C 793 ALA C 798 1 N VAL C 796 O VAL C 836
SHEET 6 E 8 ILE C 701 ASP C 705 1 N LEU C 702 O LEU C 795
SHEET 7 E 8 VAL C 724 ARG C 731 1 O LEU C 725 N ILE C 703
SHEET 8 E 8 ASN C 756 TRP C 761 1 O VAL C 759 N SER C 728
LINK O HOH A 4 K K A 202 1555 1555 2.51
LINK O HOH A 42 K K A 202 1555 1555 2.38
LINK ZN ZN A 101 O1 TSN A 301 1555 1555 2.14
LINK ZN ZN A 101 OD1 ASP A 707 1555 1555 1.94
LINK ZN ZN A 101 ND1 HIS A 709 1555 1555 2.00
LINK ZN ZN A 101 OD2 ASP A 801 1555 1555 2.04
LINK ZN ZN A 102 SG CYS A 533 1555 1555 2.43
LINK ZN ZN A 102 SG CYS A 535 1555 1555 2.35
LINK ZN ZN A 102 NE2 HIS A 541 1555 1555 2.00
LINK ZN ZN A 102 SG CYS A 618 1555 1555 2.13
LINK K K A 201 O ASP A 705 1555 1555 2.78
LINK K K A 201 OD1 ASP A 705 1555 1555 2.71
LINK K K A 201 O ASP A 707 1555 1555 2.56
LINK K K A 201 O HIS A 709 1555 1555 2.75
LINK K K A 201 OG SER A 728 1555 1555 2.70
LINK K K A 201 O LEU A 729 1555 1555 2.74
LINK K K A 202 O PHE A 718 1555 1555 2.63
LINK K K A 202 O ASP A 721 1555 1555 2.54
LINK ZN ZN B 101 O1 TSN B 301 1555 1555 2.03
LINK ZN ZN B 101 OD1 ASP B 707 1555 1555 2.05
LINK ZN ZN B 101 ND1 HIS B 709 1555 1555 2.03
LINK ZN ZN B 101 OD2 ASP B 801 1555 1555 2.02
LINK ZN ZN B 102 SG CYS B 533 1555 1555 2.26
LINK ZN ZN B 102 SG CYS B 535 1555 1555 2.33
LINK ZN ZN B 102 NE2 HIS B 541 1555 1555 2.06
LINK ZN ZN B 102 SG CYS B 618 1555 1555 2.44
LINK K K B 201 O ASP B 705 1555 1555 2.69
LINK K K B 201 OD1 ASP B 705 1555 1555 2.67
LINK K K B 201 O ASP B 707 1555 1555 2.55
LINK K K B 201 O HIS B 709 1555 1555 2.67
LINK K K B 201 OG SER B 728 1555 1555 2.65
LINK K K B 201 O LEU B 729 1555 1555 2.65
LINK K K B 202 O PHE B 718 1555 1555 2.52
LINK K K B 202 O ASP B 721 1555 1555 2.47
LINK K K B 202 O VAL B 724 1555 1555 2.50
LINK K K B 202 O HOH B 907 1555 1555 2.48
LINK K K B 202 O HOH B 913 1555 1555 2.49
LINK ZN ZN C 101 O1 TSN C 301 1555 1555 1.99
LINK ZN ZN C 101 OD1 ASP C 707 1555 1555 2.07
LINK ZN ZN C 101 ND1 HIS C 709 1555 1555 2.12
LINK ZN ZN C 101 OD2 ASP C 801 1555 1555 1.95
LINK ZN ZN C 102 SG CYS C 533 1555 1555 2.48
LINK ZN ZN C 102 SG CYS C 535 1555 1555 2.26
LINK ZN ZN C 102 NE2 HIS C 541 1555 1555 2.06
LINK ZN ZN C 102 SG CYS C 618 1555 1555 2.11
LINK K K C 201 O ASP C 705 1555 1555 2.69
LINK K K C 201 OD1 ASP C 705 1555 1555 2.63
LINK K K C 201 O ASP C 707 1555 1555 2.62
LINK K K C 201 O HIS C 709 1555 1555 2.68
LINK K K C 201 OG SER C 728 1555 1555 2.62
LINK K K C 201 O LEU C 729 1555 1555 2.64
LINK K K C 202 O PHE C 718 1555 1555 2.54
LINK K K C 202 O ASP C 721 1555 1555 2.49
LINK K K C 202 O VAL C 724 1555 1555 2.48
LINK K K C 202 O HOH C 913 1555 1555 2.53
CISPEP 1 PRO A 593 LEU A 594 0 -5.66
CISPEP 2 ARG A 665 PRO A 666 0 -4.48
CISPEP 3 PHE A 738 PRO A 739 0 -1.63
CISPEP 4 ASP A 766 PRO A 767 0 7.78
CISPEP 5 ARG B 665 PRO B 666 0 -8.10
CISPEP 6 PHE B 738 PRO B 739 0 -1.38
CISPEP 7 ASP B 766 PRO B 767 0 -0.77
CISPEP 8 ALA B 808 PRO B 809 0 -6.81
CISPEP 9 ASN C 592 PRO C 593 0 -22.91
CISPEP 10 ARG C 665 PRO C 666 0 -1.28
CISPEP 11 PHE C 738 PRO C 739 0 -2.60
CISPEP 12 ASP C 766 PRO C 767 0 5.07
SITE 1 AC1 4 TSN A 301 ASP A 707 HIS A 709 ASP A 801
SITE 1 AC2 4 CYS A 533 CYS A 535 HIS A 541 CYS A 618
SITE 1 AC3 5 ASP A 705 ASP A 707 HIS A 709 SER A 728
SITE 2 AC3 5 LEU A 729
SITE 1 AC4 6 HOH A 4 HOH A 42 PHE A 718 ASP A 721
SITE 2 AC4 6 VAL A 724 PHE A 755
SITE 1 AC5 4 TSN B 301 ASP B 707 HIS B 709 ASP B 801
SITE 1 AC6 4 CYS B 533 CYS B 535 HIS B 541 CYS B 618
SITE 1 AC7 5 ASP B 705 ASP B 707 HIS B 709 SER B 728
SITE 2 AC7 5 LEU B 729
SITE 1 AC8 6 PHE B 718 ASP B 721 VAL B 724 PHE B 755
SITE 2 AC8 6 HOH B 907 HOH B 913
SITE 1 AC9 4 TSN C 301 ASP C 707 HIS C 709 ASP C 801
SITE 1 BC1 4 CYS C 533 CYS C 535 HIS C 541 CYS C 618
SITE 1 BC2 5 ASP C 705 ASP C 707 HIS C 709 SER C 728
SITE 2 BC2 5 LEU C 729
SITE 1 BC3 6 PHE C 718 ASP C 721 VAL C 724 PHE C 755
SITE 2 BC3 6 HOH C 906 HOH C 913
SITE 1 BC4 11 ZN A 101 HOH A 120 HOH A 260 HIS A 669
SITE 2 BC4 11 HIS A 670 PHE A 679 ASP A 707 HIS A 709
SITE 3 BC4 11 ASP A 801 PRO A 809 LEU A 810
SITE 1 BC5 13 ZN B 101 ARG B 540 ASP B 626 HIS B 669
SITE 2 BC5 13 HIS B 670 GLY B 678 PHE B 679 ASP B 707
SITE 3 BC5 13 HIS B 709 ASP B 801 LEU B 810 GLY B 841
SITE 4 BC5 13 HOH B 953
SITE 1 BC6 15 ZN C 101 ARG C 540 ASP C 626 HIS C 669
SITE 2 BC6 15 HIS C 670 PHE C 679 ASP C 707 HIS C 709
SITE 3 BC6 15 PHE C 738 ASP C 801 PRO C 809 LEU C 810
SITE 4 BC6 15 HOH C 971 HOH C 991 HOH C 999
CRYST1 81.827 81.827 148.970 90.00 90.00 120.00 P 32 9
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 0.012221 0.007056 0.000000 0.00000
SCALE2 0.000000 0.014111 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006713 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
