HEADER HYDROLASE 23-MAR-16 5IX0
TITLE HDAC2 WITH LIGAND BRD7232
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE 2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: UNP RESIDUES 7-375;
COMPND 5 SYNONYM: HD2;
COMPND 6 EC: 3.5.1.98;
COMPND 7 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: HDAC2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HDAC HISTONE DEACETYLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.STEINBACHER
REVDAT 2 06-MAR-24 5IX0 1 REMARK LINK
REVDAT 1 31-AUG-16 5IX0 0
JRNL AUTH F.F.WAGNER,M.WEIWER,S.STEINBACHER,A.SCHOMBURG,P.REINEMER,
JRNL AUTH 2 J.P.GALE,A.J.CAMPBELL,S.L.FISHER,W.N.ZHAO,S.A.REIS,
JRNL AUTH 3 K.M.HENNIG,M.THOMAS,P.MULLER,M.R.JEFSON,D.M.FASS,
JRNL AUTH 4 S.J.HAGGARTY,Y.L.ZHANG,E.B.HOLSON
JRNL TITL KINETIC AND STRUCTURAL INSIGHTS INTO THE BINDING OF HISTONE
JRNL TITL 2 DEACETYLASE 1 AND 2 (HDAC1, 2) INHIBITORS.
JRNL REF BIOORG.MED.CHEM. V. 24 4008 2016
JRNL REFN ESSN 1464-3391
JRNL PMID 27377864
JRNL DOI 10.1016/J.BMC.2016.06.040
REMARK 2
REMARK 2 RESOLUTION. 1.72 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.72
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 132391
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) : 0.180
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.700
REMARK 3 FREE R VALUE TEST SET COUNT : 998
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) : 1.72
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9683
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.2990
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8870
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 279
REMARK 3 SOLVENT ATOMS : 839
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.53000
REMARK 3 B22 (A**2) : 1.51000
REMARK 3 B33 (A**2) : -0.98000
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): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.095
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.784
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9378 ; 0.010 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8760 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12590 ; 1.395 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20195 ; 1.182 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1102 ; 6.316 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 454 ;36.805 ;23.767
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1551 ;11.221 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 51 ;17.925 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1272 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10486 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2255 ; 0.003 ; 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): 4411 ; 0.664 ; 1.514
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4410 ; 0.661 ; 1.513
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5512 ; 1.109 ; 2.548
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5513 ; 1.109 ; 2.549
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4967 ; 1.225 ; 1.942
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 4967 ; 1.224 ; 1.942
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7079 ; 1.950 ; 3.060
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11129 ; 6.641 ; 8.080
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 10715 ; 6.377 ; 7.495
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 11 A 379
REMARK 3 ORIGIN FOR THE GROUP (A): 58.9980 26.1060 -1.4250
REMARK 3 T TENSOR
REMARK 3 T11: 0.0753 T22: 0.0587
REMARK 3 T33: 0.0537 T12: -0.0240
REMARK 3 T13: 0.0266 T23: -0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.8026 L22: 1.2298
REMARK 3 L33: 1.3639 L12: -0.2326
REMARK 3 L13: -0.3733 L23: 0.0734
REMARK 3 S TENSOR
REMARK 3 S11: -0.0243 S12: -0.0377 S13: -0.0233
REMARK 3 S21: -0.0680 S22: -0.0165 S23: -0.0196
REMARK 3 S31: 0.0423 S32: 0.0360 S33: 0.0409
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 14 B 379
REMARK 3 ORIGIN FOR THE GROUP (A): 93.0430 38.3780 -36.5450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0334 T22: 0.0172
REMARK 3 T33: 0.0378 T12: 0.0180
REMARK 3 T13: -0.0024 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 1.5043 L22: 0.8546
REMARK 3 L33: 1.1956 L12: 0.3893
REMARK 3 L13: -0.0617 L23: -0.0743
REMARK 3 S TENSOR
REMARK 3 S11: 0.0009 S12: 0.0536 S13: 0.0059
REMARK 3 S21: 0.0177 S22: -0.0039 S23: -0.0514
REMARK 3 S31: -0.0216 S32: 0.0539 S33: 0.0030
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 14 C 379
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4390 23.3290 -47.4170
REMARK 3 T TENSOR
REMARK 3 T11: 0.0970 T22: 0.1242
REMARK 3 T33: 0.1233 T12: 0.0308
REMARK 3 T13: -0.0249 T23: -0.0319
REMARK 3 L TENSOR
REMARK 3 L11: 2.0425 L22: 1.4774
REMARK 3 L33: 1.0935 L12: -0.1956
REMARK 3 L13: 0.2697 L23: 0.2886
REMARK 3 S TENSOR
REMARK 3 S11: 0.0630 S12: 0.1930 S13: -0.0960
REMARK 3 S21: -0.1839 S22: -0.1038 S23: 0.1731
REMARK 3 S31: -0.0356 S32: -0.0576 S33: 0.0409
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5IX0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1000219564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : LN2 COOLED FIXED-EXIT SI(111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : DYNAMICALLY BENDABLE MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133389
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.720
REMARK 200 RESOLUTION RANGE LOW (A) : 79.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.8100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.72
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.76
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.40
REMARK 200 R MERGE FOR SHELL (I) : 0.93400
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, POTASSIUM PHOSPHATE, PH 5.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 46.09750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.62700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.73650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.62700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.09750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.73650
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 57.0 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 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: 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: 4
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 B 11
REMARK 465 GLY B 12
REMARK 465 LYS B 13
REMARK 465 GLY C 11
REMARK 465 GLY C 12
REMARK 465 LYS C 13
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 31 CD OE1 NE2
REMARK 480 ARG A 54 NE CZ NH1 NH2
REMARK 480 LYS A 55 CE NZ
REMARK 480 GLU A 76 CG CD OE1 OE2
REMARK 480 LYS A 79 CD CE NZ
REMARK 480 LYS A 148 CE NZ
REMARK 480 GLU A 208 CG CD OE1 OE2
REMARK 480 LYS A 223 CE NZ
REMARK 480 LYS A 288 CE NZ
REMARK 480 LYS B 15 CE NZ
REMARK 480 GLN B 31 CD OE1 NE2
REMARK 480 ARG B 54 CZ NH1 NH2
REMARK 480 LYS B 55 CE NZ
REMARK 480 LYS B 63 CE NZ
REMARK 480 GLU B 76 CG CD OE1 OE2
REMARK 480 LYS B 223 CD CE NZ
REMARK 480 ARG C 54 CG CD NE CZ NH1 NH2
REMARK 480 ARG C 60 CZ NH1 NH2
REMARK 480 GLU C 103 CG CD OE1 OE2
REMARK 480 ASP C 104 CG OD1 OD2
REMARK 480 ASP C 345 CG OD1 OD2
REMARK 480 LYS C 347 CE NZ
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 ARG B 234 NE - CZ - NH1 ANGL. DEV. = 3.2 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 GLU A 103 -94.96 -111.05
REMARK 500 CYS A 105 79.01 -108.31
REMARK 500 PHE A 155 -1.50 77.78
REMARK 500 CYS A 266 44.55 -107.85
REMARK 500 GLU B 103 -103.12 -113.23
REMARK 500 PHE B 155 -0.16 78.19
REMARK 500 ASN B 159 82.50 -68.88
REMARK 500 CYS B 266 45.15 -108.53
REMARK 500 GLU C 103 -94.40 -109.77
REMARK 500 PHE C 155 -0.81 75.45
REMARK 500 ASN C 159 84.79 -67.55
REMARK 500 CYS C 266 46.77 -108.04
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 789 DISTANCE = 7.11 ANGSTROMS
REMARK 525 HOH B 797 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH B 798 DISTANCE = 6.11 ANGSTROMS
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 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 179 O
REMARK 620 2 ASP A 179 OD1 70.7
REMARK 620 3 ASP A 181 O 104.1 101.5
REMARK 620 4 HIS A 183 O 164.9 94.5 81.5
REMARK 620 5 SER A 202 OG 87.6 99.8 158.2 91.9
REMARK 620 6 PHE A 203 O 76.6 144.8 73.9 118.5 91.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 181 OD1
REMARK 620 2 HIS A 183 ND1 97.4
REMARK 620 3 ASP A 269 OD2 106.4 96.7
REMARK 620 4 6EZ A 404 O13 173.5 84.7 79.4
REMARK 620 5 6EZ A 404 N23 101.5 112.4 136.4 72.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 192 O
REMARK 620 2 THR A 195 O 84.2
REMARK 620 3 VAL A 198 O 120.7 83.2
REMARK 620 4 TYR A 227 O 150.0 121.7 80.3
REMARK 620 5 HOH A 570 O 71.7 154.7 115.4 80.1
REMARK 620 6 HOH A 575 O 91.5 98.1 147.6 71.5 75.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 179 O
REMARK 620 2 ASP B 179 OD1 72.8
REMARK 620 3 ASP B 181 O 106.0 102.9
REMARK 620 4 HIS B 183 O 164.7 92.8 82.0
REMARK 620 5 SER B 202 OG 86.2 99.9 156.5 91.1
REMARK 620 6 PHE B 203 O 76.8 147.0 73.5 118.4 90.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 181 OD1
REMARK 620 2 HIS B 183 ND1 96.9
REMARK 620 3 ASP B 269 OD2 105.8 99.9
REMARK 620 4 6EZ B 404 N23 101.2 111.9 135.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 192 O
REMARK 620 2 THR B 195 O 83.9
REMARK 620 3 VAL B 198 O 121.0 86.9
REMARK 620 4 TYR B 227 O 148.3 123.1 80.1
REMARK 620 5 HOH B 578 O 72.2 154.9 111.9 78.0
REMARK 620 6 HOH B 590 O 90.7 95.9 148.3 71.9 77.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 179 O
REMARK 620 2 ASP C 179 OD1 72.3
REMARK 620 3 ASP C 181 O 103.8 102.9
REMARK 620 4 HIS C 183 O 165.8 94.3 83.7
REMARK 620 5 SER C 202 OG 85.4 99.0 158.0 92.0
REMARK 620 6 PHE C 203 O 75.7 145.9 73.3 118.4 90.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 181 OD1
REMARK 620 2 HIS C 183 ND1 97.0
REMARK 620 3 ASP C 269 OD2 106.9 95.0
REMARK 620 4 6EZ C 404 O13 173.2 83.9 79.8
REMARK 620 5 6EZ C 404 N23 100.4 113.5 137.5 73.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 192 O
REMARK 620 2 THR C 195 O 88.5
REMARK 620 3 VAL C 198 O 118.3 83.0
REMARK 620 4 HOH C 537 O 70.2 157.8 112.1
REMARK 620 5 HOH C 591 O 89.3 99.8 152.4 74.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6EZ A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG5 A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6EZ B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG5 B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG5 B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 6EZ C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 C 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 409
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5IWG RELATED DB: PDB
DBREF 5IX0 A 11 379 UNP Q92769 HDAC2_HUMAN 7 375
DBREF 5IX0 B 11 379 UNP Q92769 HDAC2_HUMAN 7 375
DBREF 5IX0 C 11 379 UNP Q92769 HDAC2_HUMAN 7 375
SEQRES 1 A 369 GLY GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP
SEQRES 2 A 369 ILE GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS
SEQRES 3 A 369 PRO HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN
SEQRES 4 A 369 TYR GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS
SEQRES 5 A 369 LYS ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP
SEQRES 6 A 369 GLU TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN
SEQRES 7 A 369 MET SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL
SEQRES 8 A 369 GLY GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE
SEQRES 9 A 369 CYS GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL
SEQRES 10 A 369 LYS LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP
SEQRES 11 A 369 ALA GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER
SEQRES 12 A 369 GLY PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU
SEQRES 13 A 369 GLU LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP
SEQRES 14 A 369 ILE ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE
SEQRES 15 A 369 TYR THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS
SEQRES 16 A 369 TYR GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP
SEQRES 17 A 369 ILE GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE
SEQRES 18 A 369 PRO MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN
SEQRES 19 A 369 ILE PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR
SEQRES 20 A 369 GLN PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER
SEQRES 21 A 369 LEU SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL
SEQRES 22 A 369 LYS GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE
SEQRES 23 A 369 ASN LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR
SEQRES 24 A 369 ILE ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA
SEQRES 25 A 369 VAL ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR
SEQRES 26 A 369 ASN ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU
SEQRES 27 A 369 HIS ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO
SEQRES 28 A 369 GLU TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN
SEQRES 29 A 369 LEU ARG MET LEU PRO
SEQRES 1 B 369 GLY GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP
SEQRES 2 B 369 ILE GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS
SEQRES 3 B 369 PRO HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN
SEQRES 4 B 369 TYR GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS
SEQRES 5 B 369 LYS ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP
SEQRES 6 B 369 GLU TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN
SEQRES 7 B 369 MET SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL
SEQRES 8 B 369 GLY GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE
SEQRES 9 B 369 CYS GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL
SEQRES 10 B 369 LYS LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP
SEQRES 11 B 369 ALA GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER
SEQRES 12 B 369 GLY PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU
SEQRES 13 B 369 GLU LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP
SEQRES 14 B 369 ILE ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE
SEQRES 15 B 369 TYR THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS
SEQRES 16 B 369 TYR GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP
SEQRES 17 B 369 ILE GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE
SEQRES 18 B 369 PRO MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN
SEQRES 19 B 369 ILE PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR
SEQRES 20 B 369 GLN PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER
SEQRES 21 B 369 LEU SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL
SEQRES 22 B 369 LYS GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE
SEQRES 23 B 369 ASN LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR
SEQRES 24 B 369 ILE ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA
SEQRES 25 B 369 VAL ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR
SEQRES 26 B 369 ASN ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU
SEQRES 27 B 369 HIS ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO
SEQRES 28 B 369 GLU TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN
SEQRES 29 B 369 LEU ARG MET LEU PRO
SEQRES 1 C 369 GLY GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP
SEQRES 2 C 369 ILE GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS
SEQRES 3 C 369 PRO HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN
SEQRES 4 C 369 TYR GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS
SEQRES 5 C 369 LYS ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP
SEQRES 6 C 369 GLU TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN
SEQRES 7 C 369 MET SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL
SEQRES 8 C 369 GLY GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE
SEQRES 9 C 369 CYS GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL
SEQRES 10 C 369 LYS LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP
SEQRES 11 C 369 ALA GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER
SEQRES 12 C 369 GLY PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU
SEQRES 13 C 369 GLU LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP
SEQRES 14 C 369 ILE ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE
SEQRES 15 C 369 TYR THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS
SEQRES 16 C 369 TYR GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP
SEQRES 17 C 369 ILE GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE
SEQRES 18 C 369 PRO MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN
SEQRES 19 C 369 ILE PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR
SEQRES 20 C 369 GLN PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER
SEQRES 21 C 369 LEU SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL
SEQRES 22 C 369 LYS GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE
SEQRES 23 C 369 ASN LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR
SEQRES 24 C 369 ILE ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA
SEQRES 25 C 369 VAL ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR
SEQRES 26 C 369 ASN ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU
SEQRES 27 C 369 HIS ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO
SEQRES 28 C 369 GLU TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN
SEQRES 29 C 369 LEU ARG MET LEU PRO
HET ZN A 401 1
HET CA A 402 1
HET CA A 403 1
HET 6EZ A 404 25
HET PEG A 405 7
HET PEG A 406 7
HET PG4 A 407 13
HET PG5 A 408 12
HET PGE A 409 10
HET PGE A 410 10
HET ZN B 401 1
HET CA B 402 1
HET CA B 403 1
HET 6EZ B 404 25
HET EDO B 405 4
HET PEG B 406 7
HET PEG B 407 7
HET PG5 B 408 12
HET PG5 B 409 12
HET PGE B 410 10
HET PGE B 411 10
HET PGE B 412 10
HET PGE B 413 10
HET PGE B 414 10
HET ZN C 401 1
HET CA C 402 1
HET CA C 403 1
HET 6EZ C 404 25
HET EDO C 405 4
HET PEG C 406 7
HET PG4 C 407 13
HET PGE C 408 10
HET PGE C 409 10
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM 6EZ (3-EXO)-N-(4-AMINO-4'-FLUORO[1,1'-BIPHENYL]-3-YL)-8-
HETNAM 2 6EZ OXABICYCLO[3.2.1]OCTANE-3-CARBOXAMIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM PG5 1-METHOXY-2-[2-(2-METHOXY-ETHOXY]-ETHANE
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 CA 6(CA 2+)
FORMUL 7 6EZ 3(C20 H21 F N2 O2)
FORMUL 8 PEG 5(C4 H10 O3)
FORMUL 10 PG4 2(C8 H18 O5)
FORMUL 11 PG5 3(C8 H18 O4)
FORMUL 12 PGE 9(C6 H14 O4)
FORMUL 18 EDO 2(C2 H6 O2)
FORMUL 37 HOH *839(H2 O)
HELIX 1 AA1 ASP A 23 TYR A 27 5 5
HELIX 2 AA2 PRO A 37 TYR A 50 1 14
HELIX 3 AA3 GLY A 51 MET A 56 5 6
HELIX 4 AA4 THR A 65 THR A 70 1 6
HELIX 5 AA5 SER A 74 ILE A 84 1 11
HELIX 6 AA6 ARG A 85 GLU A 91 5 7
HELIX 7 AA7 TYR A 92 PHE A 99 1 8
HELIX 8 AA8 GLY A 110 ARG A 131 1 22
HELIX 9 AA9 ASN A 159 LEU A 169 1 11
HELIX 10 AB1 GLY A 185 PHE A 192 1 8
HELIX 11 AB2 ALA A 221 LYS A 225 5 5
HELIX 12 AB3 ASP A 238 GLN A 258 1 21
HELIX 13 AB4 GLY A 267 LEU A 271 5 5
HELIX 14 AB5 THR A 282 THR A 295 1 14
HELIX 15 AB6 THR A 309 LEU A 325 1 17
HELIX 16 AB7 TYR A 338 GLY A 343 5 6
HELIX 17 AB8 THR A 360 ARG A 376 1 17
HELIX 18 AB9 ASP B 23 TYR B 27 5 5
HELIX 19 AC1 PRO B 37 TYR B 50 1 14
HELIX 20 AC2 GLY B 51 MET B 56 5 6
HELIX 21 AC3 THR B 65 THR B 70 1 6
HELIX 22 AC4 SER B 74 ILE B 84 1 11
HELIX 23 AC5 ARG B 85 MET B 89 5 5
HELIX 24 AC6 TYR B 92 PHE B 99 1 8
HELIX 25 AC7 GLY B 110 ARG B 131 1 22
HELIX 26 AC8 ASN B 159 LEU B 169 1 11
HELIX 27 AC9 GLY B 185 PHE B 192 1 8
HELIX 28 AD1 ALA B 221 LYS B 225 5 5
HELIX 29 AD2 ASP B 238 GLN B 258 1 21
HELIX 30 AD3 GLY B 267 LEU B 271 5 5
HELIX 31 AD4 THR B 282 THR B 295 1 14
HELIX 32 AD5 THR B 309 LEU B 325 1 17
HELIX 33 AD6 TYR B 338 GLY B 343 5 6
HELIX 34 AD7 THR B 360 ARG B 376 1 17
HELIX 35 AD8 ASP C 23 TYR C 27 5 5
HELIX 36 AD9 PRO C 37 TYR C 50 1 14
HELIX 37 AE1 GLY C 51 MET C 56 5 6
HELIX 38 AE2 THR C 65 THR C 70 1 6
HELIX 39 AE3 SER C 74 ILE C 84 1 11
HELIX 40 AE4 ARG C 85 MET C 89 5 5
HELIX 41 AE5 TYR C 92 ASN C 100 1 9
HELIX 42 AE6 GLY C 110 ARG C 131 1 22
HELIX 43 AE7 ASN C 159 LEU C 169 1 11
HELIX 44 AE8 GLY C 185 PHE C 192 1 8
HELIX 45 AE9 ALA C 221 LYS C 225 5 5
HELIX 46 AF1 ASP C 238 GLN C 258 1 21
HELIX 47 AF2 GLY C 267 LEU C 271 5 5
HELIX 48 AF3 THR C 282 THR C 295 1 14
HELIX 49 AF4 THR C 309 ASP C 326 1 18
HELIX 50 AF5 TYR C 338 GLY C 343 5 6
HELIX 51 AF6 THR C 360 ARG C 376 1 17
SHEET 1 AA1 8 GLU A 57 TYR A 59 0
SHEET 2 AA1 8 VAL A 16 TYR A 19 1 N TYR A 18 O TYR A 59
SHEET 3 AA1 8 MET A 136 ASN A 139 1 O VAL A 138 N TYR A 19
SHEET 4 AA1 8 LEU A 300 LEU A 303 1 O MET A 302 N ALA A 137
SHEET 5 AA1 8 ALA A 261 GLN A 265 1 N LEU A 264 O LEU A 301
SHEET 6 AA1 8 VAL A 175 ASP A 179 1 N ILE A 178 O GLN A 265
SHEET 7 AA1 8 VAL A 198 LYS A 205 1 O MET A 199 N TYR A 177
SHEET 8 AA1 8 ALA A 228 MET A 233 1 O VAL A 229 N THR A 200
SHEET 1 AA2 8 GLU B 57 TYR B 59 0
SHEET 2 AA2 8 VAL B 16 TYR B 19 1 N TYR B 18 O TYR B 59
SHEET 3 AA2 8 MET B 136 ASN B 139 1 O VAL B 138 N TYR B 19
SHEET 4 AA2 8 LEU B 300 LEU B 303 1 O MET B 302 N ALA B 137
SHEET 5 AA2 8 ALA B 261 GLN B 265 1 N LEU B 264 O LEU B 301
SHEET 6 AA2 8 VAL B 175 ASP B 179 1 N ILE B 178 O GLN B 265
SHEET 7 AA2 8 VAL B 198 LYS B 205 1 O MET B 199 N TYR B 177
SHEET 8 AA2 8 ALA B 228 MET B 233 1 O VAL B 229 N THR B 200
SHEET 1 AA3 8 GLU C 57 TYR C 59 0
SHEET 2 AA3 8 VAL C 16 TYR C 19 1 N TYR C 18 O TYR C 59
SHEET 3 AA3 8 MET C 136 ASN C 139 1 O VAL C 138 N TYR C 19
SHEET 4 AA3 8 LEU C 300 LEU C 303 1 O MET C 302 N ALA C 137
SHEET 5 AA3 8 ALA C 261 GLN C 265 1 N LEU C 264 O LEU C 301
SHEET 6 AA3 8 VAL C 175 ASP C 179 1 N LEU C 176 O VAL C 263
SHEET 7 AA3 8 VAL C 198 LYS C 205 1 O MET C 199 N TYR C 177
SHEET 8 AA3 8 ALA C 228 MET C 233 1 O PHE C 231 N SER C 202
LINK O ASP A 179 CA CA A 402 1555 1555 2.93
LINK OD1 ASP A 179 CA CA A 402 1555 1555 2.53
LINK OD1 ASP A 181 ZN ZN A 401 1555 1555 2.00
LINK O ASP A 181 CA CA A 402 1555 1555 2.48
LINK ND1 HIS A 183 ZN ZN A 401 1555 1555 2.30
LINK O HIS A 183 CA CA A 402 1555 1555 2.61
LINK O PHE A 192 CA CA A 403 1555 1555 2.41
LINK O THR A 195 CA CA A 403 1555 1555 2.69
LINK O VAL A 198 CA CA A 403 1555 1555 2.46
LINK OG SER A 202 CA CA A 402 1555 1555 3.01
LINK O PHE A 203 CA CA A 402 1555 1555 2.47
LINK O TYR A 227 CA CA A 403 1555 1555 3.16
LINK OD2 ASP A 269 ZN ZN A 401 1555 1555 1.96
LINK ZN ZN A 401 O13 6EZ A 404 1555 1555 2.69
LINK ZN ZN A 401 N23 6EZ A 404 1555 1555 2.16
LINK CA CA A 403 O HOH A 570 1555 1555 2.99
LINK CA CA A 403 O HOH A 575 1555 1555 2.38
LINK O ASP B 179 CA CA B 402 1555 1555 2.94
LINK OD1 ASP B 179 CA CA B 402 1555 1555 2.51
LINK OD1 ASP B 181 ZN ZN B 401 1555 1555 2.02
LINK O ASP B 181 CA CA B 402 1555 1555 2.48
LINK ND1 HIS B 183 ZN ZN B 401 1555 1555 2.21
LINK O HIS B 183 CA CA B 402 1555 1555 2.67
LINK O PHE B 192 CA CA B 403 1555 1555 2.43
LINK O THR B 195 CA CA B 403 1555 1555 2.63
LINK O VAL B 198 CA CA B 403 1555 1555 2.42
LINK OG SER B 202 CA CA B 402 1555 1555 2.92
LINK O PHE B 203 CA CA B 402 1555 1555 2.48
LINK O TYR B 227 CA CA B 403 1555 1555 3.10
LINK OD2 ASP B 269 ZN ZN B 401 1555 1555 1.94
LINK ZN ZN B 401 N23 6EZ B 404 1555 1555 2.19
LINK CA CA B 403 O HOH B 578 1555 1555 2.88
LINK CA CA B 403 O HOH B 590 1555 1555 2.34
LINK O ASP C 179 CA CA C 402 1555 1555 3.01
LINK OD1 ASP C 179 CA CA C 402 1555 1555 2.51
LINK OD1 ASP C 181 ZN ZN C 401 1555 1555 2.03
LINK O ASP C 181 CA CA C 402 1555 1555 2.42
LINK ND1 HIS C 183 ZN ZN C 401 1555 1555 2.42
LINK O HIS C 183 CA CA C 402 1555 1555 2.64
LINK O PHE C 192 CA CA C 403 1555 1555 2.37
LINK O THR C 195 CA CA C 403 1555 1555 2.63
LINK O VAL C 198 CA CA C 403 1555 1555 2.40
LINK OG SER C 202 CA CA C 402 1555 1555 2.97
LINK O PHE C 203 CA CA C 402 1555 1555 2.53
LINK OD2 ASP C 269 ZN ZN C 401 1555 1555 1.95
LINK ZN ZN C 401 O13 6EZ C 404 1555 1555 2.68
LINK ZN ZN C 401 N23 6EZ C 404 1555 1555 2.20
LINK CA CA C 403 O HOH C 537 1555 1555 3.00
LINK CA CA C 403 O HOH C 591 1555 1555 2.32
CISPEP 1 PHE A 210 PRO A 211 0 -3.72
CISPEP 2 GLY A 343 PRO A 344 0 0.82
CISPEP 3 PHE B 210 PRO B 211 0 -4.22
CISPEP 4 GLY B 343 PRO B 344 0 3.72
CISPEP 5 PHE C 210 PRO C 211 0 -6.02
CISPEP 6 GLY C 343 PRO C 344 0 1.70
SITE 1 AC1 4 ASP A 181 HIS A 183 ASP A 269 6EZ A 404
SITE 1 AC2 5 ASP A 179 ASP A 181 HIS A 183 SER A 202
SITE 2 AC2 5 PHE A 203
SITE 1 AC3 6 PHE A 192 THR A 195 VAL A 198 TYR A 227
SITE 2 AC3 6 HOH A 570 HOH A 575
SITE 1 AC4 20 TYR A 29 MET A 35 ARG A 39 PHE A 114
SITE 2 AC4 20 GLY A 143 LEU A 144 HIS A 145 HIS A 146
SITE 3 AC4 20 GLY A 154 PHE A 155 CYS A 156 ASP A 181
SITE 4 AC4 20 HIS A 183 PHE A 210 ASP A 269 GLY A 305
SITE 5 AC4 20 GLY A 306 TYR A 308 ZN A 401 HOH A 610
SITE 1 AC5 3 LYS A 170 GLN A 173 HOH A 546
SITE 1 AC6 4 ARG A 311 GLU A 340 TYR A 341 GLY A 343
SITE 1 AC7 2 ASN A 26 ASP A 109
SITE 1 AC8 4 LYS A 71 TYR A 72 ALA A 191 HOH A 678
SITE 1 AC9 6 GLN A 173 ARG A 174 ASP A 196 TYR A 227
SITE 2 AC9 6 TYR A 257 PRO A 379
SITE 1 AD1 4 ASP B 181 HIS B 183 ASP B 269 6EZ B 404
SITE 1 AD2 5 ASP B 179 ASP B 181 HIS B 183 SER B 202
SITE 2 AD2 5 PHE B 203
SITE 1 AD3 6 PHE B 192 THR B 195 VAL B 198 TYR B 227
SITE 2 AD3 6 HOH B 578 HOH B 590
SITE 1 AD4 20 TYR B 29 MET B 35 ARG B 39 PHE B 114
SITE 2 AD4 20 GLY B 143 LEU B 144 HIS B 145 HIS B 146
SITE 3 AD4 20 GLY B 154 PHE B 155 CYS B 156 ASP B 181
SITE 4 AD4 20 HIS B 183 PHE B 210 ASP B 269 GLY B 305
SITE 5 AD4 20 GLY B 306 TYR B 308 ZN B 401 HOH B 615
SITE 1 AD5 1 MET B 56
SITE 1 AD6 1 HOH B 652
SITE 1 AD7 4 ARG B 98 GLU B 328 HOH B 571 HOH C 526
SITE 1 AD8 4 HOH A 657 ARG B 311 GLU B 340 GLY B 343
SITE 1 AD9 3 LYS B 284 GLU C 67 THR C 70
SITE 1 AE1 3 ARG A 131 ASP B 23 TYR B 27
SITE 1 AE2 7 TYR A 59 LYS A 128 HOH A 515 ASP B 21
SITE 2 AE2 7 ASP B 23 ARG B 60 GLU B 113
SITE 1 AE3 4 ARG B 174 ASP B 196 TYR B 227 GLU C 240
SITE 1 AE4 6 SER B 272 GLY B 273 ARG B 275 ARG B 311
SITE 2 AE4 6 ASN B 312 HOH B 508
SITE 1 AE5 6 LYS B 14 ASP B 135 MET B 136 LYS B 294
SITE 2 AE5 6 ASN B 297 LEU B 298
SITE 1 AE6 4 ASP C 181 HIS C 183 ASP C 269 6EZ C 404
SITE 1 AE7 5 ASP C 179 ASP C 181 HIS C 183 SER C 202
SITE 2 AE7 5 PHE C 203
SITE 1 AE8 6 PHE C 192 THR C 195 VAL C 198 TYR C 227
SITE 2 AE8 6 HOH C 537 HOH C 591
SITE 1 AE9 20 TYR C 29 MET C 35 ARG C 39 PHE C 114
SITE 2 AE9 20 GLY C 143 LEU C 144 HIS C 145 HIS C 146
SITE 3 AE9 20 GLY C 154 PHE C 155 CYS C 156 ASP C 181
SITE 4 AE9 20 HIS C 183 PHE C 210 ASP C 269 GLY C 305
SITE 5 AE9 20 GLY C 306 TYR C 308 ZN C 401 HOH C 642
SITE 1 AF1 1 ILE C 58
SITE 1 AF2 2 GLN C 132 ASP C 135
SITE 1 AF3 6 ASN B 354 LEU C 169 TYR C 171 GLN C 173
SITE 2 AF3 6 ARG C 197 HOH C 678
SITE 1 AF4 7 TYR C 72 ALA C 191 ARG C 197 HOH C 525
SITE 2 AF4 7 HOH C 556 HOH C 573 HOH C 663
SITE 1 AF5 3 ASP C 23 ASN C 26 ASP C 109
CRYST1 92.195 97.473 139.254 90.00 90.00 90.00 P 21 21 21 12
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 0.010847 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010259 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007181 0.00000
(ATOM LINES ARE NOT SHOWN.)
END