HEADER HYDROLASE/HYDROLASE INHIBITOR 28-APR-11 3RQD
TITLE IDEAL THIOLATE-ZINC COORDINATION GEOMETRY IN DEPSIPEPTIDE BINDING TO
TITLE 2 HISTONE DEACETYLASE 8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE 8;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HD8;
COMPND 5 EC: 3.5.1.98;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: LARGAZOLE;
COMPND 9 CHAIN: C, D;
COMPND 10 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: HDAC8, HDACL1, CDA07;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYMPLOCA;
SOURCE 11 ORGANISM_TAXID: 105591
KEYWDS HISTONE DEACETYLASE, LARGAZOLE, HISTONE DEACETYLATION, HYDROLASE-
KEYWDS 2 HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.COLE,D.P.DOWLING,D.W.CHRISTIANSON
REVDAT 5 15-NOV-23 3RQD 1 LINK ATOM
REVDAT 4 13-SEP-23 3RQD 1 REMARK SEQADV LINK
REVDAT 3 24-JAN-18 3RQD 1 AUTHOR REMARK
REVDAT 2 21-MAR-12 3RQD 1 JRNL
REVDAT 1 24-AUG-11 3RQD 0
JRNL AUTH K.E.COLE,D.P.DOWLING,M.A.BOONE,A.J.PHILLIPS,D.W.CHRISTIANSON
JRNL TITL STRUCTURAL BASIS OF THE ANTIPROLIFERATIVE ACTIVITY OF
JRNL TITL 2 LARGAZOLE, A DEPSIPEPTIDE INHIBITOR OF THE HISTONE
JRNL TITL 3 DEACETYLASES.
JRNL REF J.AM.CHEM.SOC. V. 133 12474 2011
JRNL REFN ISSN 0002-7863
JRNL PMID 21790156
JRNL DOI 10.1021/JA205972N
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.78
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.080
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 44332
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 2213
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.7904 - 5.3949 0.99 2860 157 0.1885 0.1891
REMARK 3 2 5.3949 - 4.2837 0.99 2825 150 0.1709 0.1914
REMARK 3 3 4.2837 - 3.7427 0.99 2830 139 0.1758 0.2406
REMARK 3 4 3.7427 - 3.4007 0.99 2778 133 0.1907 0.2215
REMARK 3 5 3.4007 - 3.1571 0.98 2761 154 0.2103 0.2586
REMARK 3 6 3.1571 - 2.9710 0.96 2710 153 0.2146 0.2933
REMARK 3 7 2.9710 - 2.8222 0.95 2687 134 0.2103 0.2534
REMARK 3 8 2.8222 - 2.6994 0.93 2627 124 0.2101 0.2605
REMARK 3 9 2.6994 - 2.5955 0.92 2562 145 0.2123 0.2712
REMARK 3 10 2.5955 - 2.5060 0.91 2604 132 0.2094 0.2908
REMARK 3 11 2.5060 - 2.4276 0.91 2540 125 0.2055 0.2539
REMARK 3 12 2.4276 - 2.3582 0.88 2463 137 0.2080 0.2449
REMARK 3 13 2.3582 - 2.2962 0.90 2516 143 0.2113 0.2692
REMARK 3 14 2.2962 - 2.2401 0.88 2495 126 0.2221 0.3195
REMARK 3 15 2.2401 - 2.1892 0.88 2479 133 0.2291 0.2566
REMARK 3 16 2.1892 - 2.1426 0.86 2382 128 0.2361 0.3074
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 40.63
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 5.02810
REMARK 3 B22 (A**2) : -2.06410
REMARK 3 B33 (A**2) : -2.96400
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.38570
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 5759
REMARK 3 ANGLE : 1.098 7815
REMARK 3 CHIRALITY : 0.072 856
REMARK 3 PLANARITY : 0.006 992
REMARK 3 DIHEDRAL : 19.719 2061
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN A AND (RESSEQ 14:83 OR RESSEQ
REMARK 3 96:376 )
REMARK 3 SELECTION : CHAIN B AND (RESSEQ 14:83 OR RESSEQ
REMARK 3 96:376 )
REMARK 3 ATOM PAIRS NUMBER : 2724
REMARK 3 RMSD : 0.124
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3RQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000065248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : DOUBLE SILICON(111) CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46258
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.140
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.12700
REMARK 200 R SYM (I) : 0.12700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.54300
REMARK 200 R SYM FOR SHELL (I) : 0.54300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER (CCP4)
REMARK 200 STARTING MODEL: 3WEF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M 2-(N-MORPHOLINO)ETHANESULFONIC
REMARK 280 ACID (MES, PH 5.3), 4 MM TRIS(2-CARBOXYETHYL)PHOSPHINE (TCEP), 1-
REMARK 280 6% PEG 35000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K,
REMARK 280 PH 6.6
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 44.15100
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 26260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE LARGAZOLE IS CYCLIC DEPSIPEPTIDE, A MEMBER OF INHIBITOR CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: LARGAZOLE
REMARK 400 CHAIN: C, D
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
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 MET A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 3
REMARK 465 PRO A 4
REMARK 465 GLU A 5
REMARK 465 GLU A 6
REMARK 465 PRO A 7
REMARK 465 ALA A 8
REMARK 465 ASP A 9
REMARK 465 SER A 10
REMARK 465 GLY A 11
REMARK 465 GLN A 12
REMARK 465 SER A 13
REMARK 465 GLU A 85
REMARK 465 GLY A 86
REMARK 465 ASP A 87
REMARK 465 ASP A 88
REMARK 465 ASP A 89
REMARK 465 HIS A 90
REMARK 465 PRO A 91
REMARK 465 ASP A 92
REMARK 465 SER A 93
REMARK 465 ILE A 94
REMARK 465 ILE A 378
REMARK 465 GLU A 379
REMARK 465 GLY A 380
REMARK 465 ARG A 381
REMARK 465 GLY A 382
REMARK 465 SER A 383
REMARK 465 HIS A 384
REMARK 465 HIS A 385
REMARK 465 HIS A 386
REMARK 465 HIS A 387
REMARK 465 HIS A 388
REMARK 465 HIS A 389
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 PRO B 4
REMARK 465 GLU B 5
REMARK 465 GLU B 6
REMARK 465 PRO B 7
REMARK 465 ALA B 8
REMARK 465 ASP B 9
REMARK 465 SER B 10
REMARK 465 GLY B 11
REMARK 465 GLN B 12
REMARK 465 GLN B 84
REMARK 465 GLU B 85
REMARK 465 GLY B 86
REMARK 465 ASP B 87
REMARK 465 ASP B 88
REMARK 465 ASP B 89
REMARK 465 HIS B 90
REMARK 465 PRO B 91
REMARK 465 ASP B 92
REMARK 465 SER B 93
REMARK 465 GLU B 379
REMARK 465 GLY B 380
REMARK 465 ARG B 381
REMARK 465 GLY B 382
REMARK 465 SER B 383
REMARK 465 HIS B 384
REMARK 465 HIS B 385
REMARK 465 HIS B 386
REMARK 465 HIS B 387
REMARK 465 HIS B 388
REMARK 465 HIS B 389
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 GLU A 65 CD
REMARK 480 GLU A 95 CD
REMARK 480 GLU A 170 CD
REMARK 480 GLN A 253 CD
REMARK 480 ASP A 343 CG OD2
REMARK 480 GLU B 65 CD
REMARK 480 GLU B 170 CG
REMARK 480 GLN B 253 CD
REMARK 480 ASP B 343 CG
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 02G C 1 CA - C - N ANGL. DEV. = 23.6 DEGREES
REMARK 500 02G D 1 CA - C - N ANGL. DEV. = 26.9 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 SER A 21 145.05 -170.10
REMARK 500 PHE A 70 -58.58 -122.07
REMARK 500 TYR A 100 -92.66 69.33
REMARK 500 SER A 150 139.27 -170.69
REMARK 500 ASP A 178 157.48 -45.34
REMARK 500 TYR A 224 -5.78 89.16
REMARK 500 ALA A 270 134.24 -39.29
REMARK 500 CYS A 275 54.64 33.82
REMARK 500 SER A 276 -57.80 -121.58
REMARK 500 HIS A 334 -177.88 -171.62
REMARK 500 LEU B 14 43.57 -64.23
REMARK 500 SER B 21 145.36 -170.49
REMARK 500 PHE B 70 -58.97 -120.80
REMARK 500 TYR B 100 -93.44 70.95
REMARK 500 SER B 150 140.27 -170.47
REMARK 500 ASP B 178 159.99 -47.47
REMARK 500 TYR B 224 -7.01 89.97
REMARK 500 ALA B 270 133.32 -38.65
REMARK 500 CYS B 275 54.77 35.95
REMARK 500 SER B 276 -59.04 -123.51
REMARK 500 HIS B 360 -70.05 -65.03
REMARK 500 03Y C 4 18.00 102.89
REMARK 500 03Y D 4 17.82 106.03
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 02G C 1 24.46
REMARK 500 02G D 1 19.43
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 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 176 O
REMARK 620 2 ASP A 176 OD1 69.9
REMARK 620 3 ASP A 178 O 101.1 99.0
REMARK 620 4 HIS A 180 O 159.3 90.0 86.4
REMARK 620 5 SER A 199 OG 85.4 103.0 158.0 94.9
REMARK 620 6 LEU A 200 O 77.3 143.9 72.4 123.4 88.8
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 178 OD2
REMARK 620 2 HIS A 180 ND1 111.2
REMARK 620 3 ASP A 267 OD2 110.9 99.1
REMARK 620 4 02G C 1 S 117.3 108.9 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 189 O
REMARK 620 2 THR A 192 O 72.0
REMARK 620 3 VAL A 195 O 113.3 87.3
REMARK 620 4 TYR A 225 O 159.5 122.6 83.6
REMARK 620 5 HOH A 511 O 74.8 146.4 110.5 88.6
REMARK 620 6 HOH A 563 O 87.1 99.8 159.7 76.6 73.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 176 O
REMARK 620 2 ASP B 176 OD1 71.7
REMARK 620 3 ASP B 178 O 106.1 102.0
REMARK 620 4 HIS B 180 O 155.9 85.9 86.8
REMARK 620 5 SER B 199 OG 84.9 99.6 158.0 90.2
REMARK 620 6 LEU B 200 O 80.7 150.3 75.1 122.9 88.3
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 178 OD2
REMARK 620 2 HIS B 180 ND1 110.5
REMARK 620 3 ASP B 267 OD2 112.4 100.0
REMARK 620 4 02G D 1 S 113.6 112.0 107.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 189 O
REMARK 620 2 THR B 192 O 69.8
REMARK 620 3 VAL B 195 O 114.2 86.6
REMARK 620 4 TYR B 225 O 159.5 120.5 85.1
REMARK 620 5 HOH B 527 O 82.4 91.8 161.3 79.7
REMARK 620 6 HOH B 537 O 75.4 144.9 112.2 91.4 79.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 390
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 391
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 392
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 392
DBREF 3RQD A 1 377 UNP Q9BY41 HDAC8_HUMAN 1 377
DBREF 3RQD B 1 377 UNP Q9BY41 HDAC8_HUMAN 1 377
DBREF 3RQD C 1 5 PDB 3RQD 3RQD 1 5
DBREF 3RQD D 1 5 PDB 3RQD 3RQD 1 5
SEQADV 3RQD ILE A 378 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD GLU A 379 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD GLY A 380 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD ARG A 381 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD GLY A 382 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD SER A 383 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS A 384 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS A 385 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS A 386 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS A 387 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS A 388 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS A 389 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD ILE B 378 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD GLU B 379 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD GLY B 380 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD ARG B 381 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD GLY B 382 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD SER B 383 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS B 384 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS B 385 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS B 386 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS B 387 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS B 388 UNP Q9BY41 EXPRESSION TAG
SEQADV 3RQD HIS B 389 UNP Q9BY41 EXPRESSION TAG
SEQRES 1 A 389 MET GLU GLU PRO GLU GLU PRO ALA ASP SER GLY GLN SER
SEQRES 2 A 389 LEU VAL PRO VAL TYR ILE TYR SER PRO GLU TYR VAL SER
SEQRES 3 A 389 MET CYS ASP SER LEU ALA LYS ILE PRO LYS ARG ALA SER
SEQRES 4 A 389 MET VAL HIS SER LEU ILE GLU ALA TYR ALA LEU HIS LYS
SEQRES 5 A 389 GLN MET ARG ILE VAL LYS PRO LYS VAL ALA SER MET GLU
SEQRES 6 A 389 GLU MET ALA THR PHE HIS THR ASP ALA TYR LEU GLN HIS
SEQRES 7 A 389 LEU GLN LYS VAL SER GLN GLU GLY ASP ASP ASP HIS PRO
SEQRES 8 A 389 ASP SER ILE GLU TYR GLY LEU GLY TYR ASP CYS PRO ALA
SEQRES 9 A 389 THR GLU GLY ILE PHE ASP TYR ALA ALA ALA ILE GLY GLY
SEQRES 10 A 389 ALA THR ILE THR ALA ALA GLN CYS LEU ILE ASP GLY MET
SEQRES 11 A 389 CYS LYS VAL ALA ILE ASN TRP SER GLY GLY TRP HIS HIS
SEQRES 12 A 389 ALA LYS LYS ASP GLU ALA SER GLY PHE CYS TYR LEU ASN
SEQRES 13 A 389 ASP ALA VAL LEU GLY ILE LEU ARG LEU ARG ARG LYS PHE
SEQRES 14 A 389 GLU ARG ILE LEU TYR VAL ASP LEU ASP LEU HIS HIS GLY
SEQRES 15 A 389 ASP GLY VAL GLU ASP ALA PHE SER PHE THR SER LYS VAL
SEQRES 16 A 389 MET THR VAL SER LEU HIS LYS PHE SER PRO GLY PHE PHE
SEQRES 17 A 389 PRO GLY THR GLY ASP VAL SER ASP VAL GLY LEU GLY LYS
SEQRES 18 A 389 GLY ARG TYR TYR SER VAL ASN VAL PRO ILE GLN ASP GLY
SEQRES 19 A 389 ILE GLN ASP GLU LYS TYR TYR GLN ILE CYS GLU SER VAL
SEQRES 20 A 389 LEU LYS GLU VAL TYR GLN ALA PHE ASN PRO LYS ALA VAL
SEQRES 21 A 389 VAL LEU GLN LEU GLY ALA ASP THR ILE ALA GLY ASP PRO
SEQRES 22 A 389 MET CYS SER PHE ASN MET THR PRO VAL GLY ILE GLY LYS
SEQRES 23 A 389 CYS LEU LYS TYR ILE LEU GLN TRP GLN LEU ALA THR LEU
SEQRES 24 A 389 ILE LEU GLY GLY GLY GLY TYR ASN LEU ALA ASN THR ALA
SEQRES 25 A 389 ARG CYS TRP THR TYR LEU THR GLY VAL ILE LEU GLY LYS
SEQRES 26 A 389 THR LEU SER SER GLU ILE PRO ASP HIS GLU PHE PHE THR
SEQRES 27 A 389 ALA TYR GLY PRO ASP TYR VAL LEU GLU ILE THR PRO SER
SEQRES 28 A 389 CYS ARG PRO ASP ARG ASN GLU PRO HIS ARG ILE GLN GLN
SEQRES 29 A 389 ILE LEU ASN TYR ILE LYS GLY ASN LEU LYS HIS VAL VAL
SEQRES 30 A 389 ILE GLU GLY ARG GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 B 389 MET GLU GLU PRO GLU GLU PRO ALA ASP SER GLY GLN SER
SEQRES 2 B 389 LEU VAL PRO VAL TYR ILE TYR SER PRO GLU TYR VAL SER
SEQRES 3 B 389 MET CYS ASP SER LEU ALA LYS ILE PRO LYS ARG ALA SER
SEQRES 4 B 389 MET VAL HIS SER LEU ILE GLU ALA TYR ALA LEU HIS LYS
SEQRES 5 B 389 GLN MET ARG ILE VAL LYS PRO LYS VAL ALA SER MET GLU
SEQRES 6 B 389 GLU MET ALA THR PHE HIS THR ASP ALA TYR LEU GLN HIS
SEQRES 7 B 389 LEU GLN LYS VAL SER GLN GLU GLY ASP ASP ASP HIS PRO
SEQRES 8 B 389 ASP SER ILE GLU TYR GLY LEU GLY TYR ASP CYS PRO ALA
SEQRES 9 B 389 THR GLU GLY ILE PHE ASP TYR ALA ALA ALA ILE GLY GLY
SEQRES 10 B 389 ALA THR ILE THR ALA ALA GLN CYS LEU ILE ASP GLY MET
SEQRES 11 B 389 CYS LYS VAL ALA ILE ASN TRP SER GLY GLY TRP HIS HIS
SEQRES 12 B 389 ALA LYS LYS ASP GLU ALA SER GLY PHE CYS TYR LEU ASN
SEQRES 13 B 389 ASP ALA VAL LEU GLY ILE LEU ARG LEU ARG ARG LYS PHE
SEQRES 14 B 389 GLU ARG ILE LEU TYR VAL ASP LEU ASP LEU HIS HIS GLY
SEQRES 15 B 389 ASP GLY VAL GLU ASP ALA PHE SER PHE THR SER LYS VAL
SEQRES 16 B 389 MET THR VAL SER LEU HIS LYS PHE SER PRO GLY PHE PHE
SEQRES 17 B 389 PRO GLY THR GLY ASP VAL SER ASP VAL GLY LEU GLY LYS
SEQRES 18 B 389 GLY ARG TYR TYR SER VAL ASN VAL PRO ILE GLN ASP GLY
SEQRES 19 B 389 ILE GLN ASP GLU LYS TYR TYR GLN ILE CYS GLU SER VAL
SEQRES 20 B 389 LEU LYS GLU VAL TYR GLN ALA PHE ASN PRO LYS ALA VAL
SEQRES 21 B 389 VAL LEU GLN LEU GLY ALA ASP THR ILE ALA GLY ASP PRO
SEQRES 22 B 389 MET CYS SER PHE ASN MET THR PRO VAL GLY ILE GLY LYS
SEQRES 23 B 389 CYS LEU LYS TYR ILE LEU GLN TRP GLN LEU ALA THR LEU
SEQRES 24 B 389 ILE LEU GLY GLY GLY GLY TYR ASN LEU ALA ASN THR ALA
SEQRES 25 B 389 ARG CYS TRP THR TYR LEU THR GLY VAL ILE LEU GLY LYS
SEQRES 26 B 389 THR LEU SER SER GLU ILE PRO ASP HIS GLU PHE PHE THR
SEQRES 27 B 389 ALA TYR GLY PRO ASP TYR VAL LEU GLU ILE THR PRO SER
SEQRES 28 B 389 CYS ARG PRO ASP ARG ASN GLU PRO HIS ARG ILE GLN GLN
SEQRES 29 B 389 ILE LEU ASN TYR ILE LYS GLY ASN LEU LYS HIS VAL VAL
SEQRES 30 B 389 ILE GLU GLY ARG GLY SER HIS HIS HIS HIS HIS HIS
SEQRES 1 C 5 02G GLY BB9 03Y VAL
SEQRES 1 D 5 02G GLY BB9 03Y VAL
MODRES 3RQD BB9 C 3 CYS
MODRES 3RQD 03Y C 4 CYS 2-METHYL-L-CYSTEINE
MODRES 3RQD BB9 D 3 CYS
MODRES 3RQD 03Y D 4 CYS 2-METHYL-L-CYSTEINE
HET 02G C 1 10
HET BB9 C 3 5
HET 03Y C 4 7
HET 02G D 1 10
HET BB9 D 3 5
HET 03Y D 4 7
HET ZN A 401 1
HET K A 402 1
HET K A 403 1
HET ZN B 401 1
HET K B 402 1
HET K B 403 1
HETNAM 02G (3S,4E)-3-HYDROXY-7-SULFANYLHEPT-4-ENOIC ACID
HETNAM BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID
HETNAM 03Y 2-METHYL-L-CYSTEINE
HETNAM ZN ZINC ION
HETNAM K POTASSIUM ION
FORMUL 3 02G 2(C7 H12 O3 S)
FORMUL 3 BB9 2(C3 H5 N O2 S)
FORMUL 3 03Y 2(C4 H9 N O2 S)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 K 4(K 1+)
FORMUL 11 HOH *504(H2 O)
HELIX 1 1 SER A 21 SER A 30 1 10
HELIX 2 2 LYS A 36 TYR A 48 1 13
HELIX 3 3 ALA A 49 MET A 54 5 6
HELIX 4 4 SER A 63 ALA A 68 1 6
HELIX 5 5 THR A 72 GLN A 84 1 13
HELIX 6 6 GLY A 107 ASP A 128 1 22
HELIX 7 7 ASN A 156 ARG A 166 1 11
HELIX 8 8 GLY A 182 SER A 190 1 9
HELIX 9 9 LEU A 219 ARG A 223 5 5
HELIX 10 10 GLN A 236 ASN A 256 1 21
HELIX 11 11 THR A 280 GLN A 293 1 14
HELIX 12 12 ASN A 307 GLY A 324 1 18
HELIX 13 13 PHE A 336 GLY A 341 5 6
HELIX 14 14 GLU A 358 HIS A 375 1 18
HELIX 15 15 SER B 21 SER B 30 1 10
HELIX 16 16 LYS B 36 TYR B 48 1 13
HELIX 17 17 ALA B 49 MET B 54 5 6
HELIX 18 18 SER B 63 ALA B 68 1 6
HELIX 19 19 THR B 72 SER B 83 1 12
HELIX 20 20 GLY B 107 ASP B 128 1 22
HELIX 21 21 ASN B 156 ARG B 166 1 11
HELIX 22 22 GLY B 182 SER B 190 1 9
HELIX 23 23 LEU B 219 ARG B 223 5 5
HELIX 24 24 GLN B 236 ASN B 256 1 21
HELIX 25 25 THR B 280 GLN B 293 1 14
HELIX 26 26 ASN B 307 GLY B 324 1 18
HELIX 27 27 PHE B 336 GLY B 341 5 6
HELIX 28 28 GLU B 358 HIS B 375 1 18
SHEET 1 A 8 ARG A 55 VAL A 57 0
SHEET 2 A 8 VAL A 17 ILE A 19 1 N TYR A 18 O ARG A 55
SHEET 3 A 8 VAL A 133 ASN A 136 1 O VAL A 133 N VAL A 17
SHEET 4 A 8 ALA A 297 LEU A 301 1 O ILE A 300 N ASN A 136
SHEET 5 A 8 ALA A 259 GLN A 263 1 N LEU A 262 O LEU A 299
SHEET 6 A 8 ILE A 172 ASP A 176 1 N LEU A 173 O ALA A 259
SHEET 7 A 8 VAL A 195 LYS A 202 1 O MET A 196 N TYR A 174
SHEET 8 A 8 SER A 226 ILE A 231 1 O VAL A 227 N THR A 197
SHEET 1 B 8 ARG B 55 VAL B 57 0
SHEET 2 B 8 VAL B 17 ILE B 19 1 N TYR B 18 O ARG B 55
SHEET 3 B 8 VAL B 133 ASN B 136 1 O VAL B 133 N VAL B 17
SHEET 4 B 8 ALA B 297 LEU B 301 1 O ILE B 300 N ASN B 136
SHEET 5 B 8 ALA B 259 GLN B 263 1 N LEU B 262 O LEU B 299
SHEET 6 B 8 ILE B 172 ASP B 176 1 N VAL B 175 O GLN B 263
SHEET 7 B 8 VAL B 195 LYS B 202 1 O MET B 196 N TYR B 174
SHEET 8 B 8 SER B 226 ILE B 231 1 O VAL B 227 N THR B 197
LINK C 02G C 1 N GLY C 2 1555 1555 1.36
LINK O2 02G C 1 C VAL C 5 1555 1555 1.37
LINK C GLY C 2 N BB9 C 3 1555 1555 1.32
LINK C GLY C 2 SG BB9 C 3 1555 1555 1.70
LINK C BB9 C 3 N 03Y C 4 1555 1555 1.31
LINK C BB9 C 3 SG 03Y C 4 1555 1555 1.73
LINK C 03Y C 4 N VAL C 5 1555 1555 1.36
LINK C 02G D 1 N GLY D 2 1555 1555 1.37
LINK O2 02G D 1 C VAL D 5 1555 1555 1.37
LINK C GLY D 2 N BB9 D 3 1555 1555 1.31
LINK C GLY D 2 SG BB9 D 3 1555 1555 1.70
LINK C BB9 D 3 N 03Y D 4 1555 1555 1.30
LINK C BB9 D 3 SG 03Y D 4 1555 1555 1.73
LINK C 03Y D 4 N VAL D 5 1555 1555 1.37
LINK O ASP A 176 K K A 402 1555 1555 2.98
LINK OD1 ASP A 176 K K A 402 1555 1555 3.05
LINK OD2 ASP A 178 ZN ZN A 401 1555 1555 1.96
LINK O ASP A 178 K K A 402 1555 1555 2.92
LINK ND1 HIS A 180 ZN ZN A 401 1555 1555 2.18
LINK O HIS A 180 K K A 402 1555 1555 2.88
LINK O PHE A 189 K K A 403 1555 1555 2.87
LINK O THR A 192 K K A 403 1555 1555 2.96
LINK O VAL A 195 K K A 403 1555 1555 2.82
LINK OG SER A 199 K K A 402 1555 1555 3.08
LINK O LEU A 200 K K A 402 1555 1555 2.77
LINK O TYR A 225 K K A 403 1555 1555 3.22
LINK OD2 ASP A 267 ZN ZN A 401 1555 1555 2.00
LINK ZN ZN A 401 S 02G C 1 1555 1555 2.30
LINK K K A 403 O HOH A 511 1555 1555 3.12
LINK K K A 403 O HOH A 563 1555 1555 3.21
LINK O ASP B 176 K K B 402 1555 1555 2.97
LINK OD1 ASP B 176 K K B 402 1555 1555 3.02
LINK OD2 ASP B 178 ZN ZN B 401 1555 1555 1.99
LINK O ASP B 178 K K B 402 1555 1555 2.83
LINK ND1 HIS B 180 ZN ZN B 401 1555 1555 2.16
LINK O HIS B 180 K K B 402 1555 1555 2.99
LINK O PHE B 189 K K B 403 1555 1555 2.93
LINK O THR B 192 K K B 403 1555 1555 3.03
LINK O VAL B 195 K K B 403 1555 1555 2.80
LINK OG SER B 199 K K B 402 1555 1555 3.21
LINK O LEU B 200 K K B 402 1555 1555 2.68
LINK O TYR B 225 K K B 403 1555 1555 3.12
LINK OD2 ASP B 267 ZN ZN B 401 1555 1555 2.02
LINK ZN ZN B 401 S 02G D 1 1555 1555 2.31
LINK K K B 403 O HOH B 527 1555 1555 3.17
LINK K K B 403 O HOH B 537 1555 1555 2.89
CISPEP 1 PHE A 208 PRO A 209 0 0.55
CISPEP 2 GLY A 341 PRO A 342 0 5.05
CISPEP 3 PHE B 208 PRO B 209 0 2.53
CISPEP 4 GLY B 341 PRO B 342 0 4.74
SITE 1 AC1 4 ASP B 178 HIS B 180 ASP B 267 02G D 1
SITE 1 AC2 4 ASP A 178 HIS A 180 ASP A 267 02G C 1
SITE 1 AC3 5 ASP B 176 ASP B 178 HIS B 180 SER B 199
SITE 2 AC3 5 LEU B 200
SITE 1 AC4 5 ASP A 176 ASP A 178 HIS A 180 SER A 199
SITE 2 AC4 5 LEU A 200
SITE 1 AC5 4 PHE A 189 THR A 192 VAL A 195 TYR A 225
SITE 1 AC6 4 PHE B 189 THR B 192 VAL B 195 TYR B 225
CRYST1 54.059 88.302 93.660 90.00 101.62 90.00 P 1 21 1 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 0.018498 0.000000 0.003804 0.00000
SCALE2 0.000000 0.011325 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010900 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
