HEADER HYDROLASE/HYDROLASE INHIBITOR 30-JUL-13 4LY1
TITLE STRUCTURE OF HUMAN HDAC2 IN COMPLEX WITH INHIBITOR 4-(ACETYLAMINO)-N-
TITLE 2 [2-AMINO-5-(THIOPHEN-2-YL)PHENYL]BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE 2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CORE DOMAIN (UNP RESIDUES 8-376);
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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS DEACETYLASE, HISTONE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR R.FONG,P.J.LUPARDUS
REVDAT 3 20-SEP-23 4LY1 1 REMARK LINK
REVDAT 2 02-OCT-13 4LY1 1 JRNL
REVDAT 1 21-AUG-13 4LY1 0
JRNL AUTH B.E.LAUFFER,R.MINTZER,R.FONG,S.MUKUND,C.TAM,I.ZILBERLEYB,
JRNL AUTH 2 B.FLICKE,A.RITSCHER,G.FEDOROWICZ,R.VALLERO,D.F.ORTWINE,
JRNL AUTH 3 J.GUNZNER,Z.MODRUSAN,L.NEUMANN,C.M.KOTH,P.J.LUPARDUS,
JRNL AUTH 4 J.S.KAMINKER,C.E.HEISE,P.STEINER
JRNL TITL HISTONE DEACETYLASE (HDAC) INHIBITOR KINETIC RATE CONSTANTS
JRNL TITL 2 CORRELATE WITH CELLULAR HISTONE ACETYLATION BUT NOT
JRNL TITL 3 TRANSCRIPTION AND CELL VIABILITY.
JRNL REF J.BIOL.CHEM. V. 288 26926 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23897821
JRNL DOI 10.1074/JBC.M113.490706
REMARK 2
REMARK 2 RESOLUTION. 1.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 174095
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) : 0.170
REMARK 3 R VALUE (WORKING SET) : 0.169
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8703
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.57
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.61
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 12661
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2179
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 12015
REMARK 3 BIN R VALUE (WORKING SET) : 0.2170
REMARK 3 BIN FREE R VALUE : 0.2347
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 646
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8869
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 201
REMARK 3 SOLVENT ATOMS : 846
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.36860
REMARK 3 B22 (A**2) : -6.58640
REMARK 3 B33 (A**2) : 3.21780
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.163
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.073
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 9480 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 12784 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 3329 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 227 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1389 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 9480 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 1117 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 12225 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.70
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.66
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4LY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1000081228.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-F
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 174095
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.570
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.58700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3MAX
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M CHES, PH 9.5, 40% PEG-600, VAPOR
REMARK 280 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 46.01700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.46100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.74500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.46100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.01700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.74500
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
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 HIS A 380
REMARK 465 GLY B 12
REMARK 465 HIS B 380
REMARK 465 GLY C 12
REMARK 465 PRO C 379
REMARK 465 HIS C 380
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 LYS B 13 CG CD CE NZ
REMARK 470 LYS C 13 CG CD CE NZ
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 HOH A 781 O HOH A 795 2.19
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 TYR A 72 -58.58 -129.39
REMARK 500 GLU A 103 -91.99 -114.11
REMARK 500 CYS A 105 75.59 -116.15
REMARK 500 PHE A 155 -3.25 79.61
REMARK 500 TYR A 226 2.78 87.73
REMARK 500 TYR B 72 -56.63 -126.85
REMARK 500 GLU B 103 -102.63 -110.45
REMARK 500 CYS B 105 78.52 -115.00
REMARK 500 TYR B 226 2.26 86.97
REMARK 500 TYR C 72 -53.78 -126.17
REMARK 500 GLU C 103 -102.36 -111.17
REMARK 500 CYS C 105 78.11 -115.64
REMARK 500 TYR C 226 5.77 82.05
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 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 179 OD1
REMARK 620 2 ASP A 179 O 71.9
REMARK 620 3 ASP A 181 O 100.3 104.2
REMARK 620 4 HIS A 183 O 91.8 163.1 82.9
REMARK 620 5 SER A 202 OG 101.1 88.0 157.9 90.7
REMARK 620 6 PHE A 203 O 145.9 78.1 71.6 118.8 93.5
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 OD2
REMARK 620 2 HIS A 183 ND1 100.4
REMARK 620 3 ASP A 269 OD2 106.7 104.2
REMARK 620 4 20Y A 407 N20 93.2 107.2 138.8
REMARK 620 5 20Y A 407 N20 96.1 103.8 139.6 4.1
REMARK 620 6 20Y A 407 O12 173.0 84.2 76.9 80.4 77.6
REMARK 620 7 20Y A 407 O12 167.1 86.5 81.8 74.3 71.6 6.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 192 O
REMARK 620 2 THR A 195 O 77.6
REMARK 620 3 VAL A 198 O 117.6 83.2
REMARK 620 4 TYR A 227 O 156.0 121.6 81.4
REMARK 620 5 HOH A 520 O 90.3 92.0 149.6 75.7
REMARK 620 6 HOH A 521 O 74.8 151.9 114.5 83.9 82.9
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 OD1
REMARK 620 2 ASP B 179 O 72.1
REMARK 620 3 ASP B 181 O 101.0 103.8
REMARK 620 4 HIS B 183 O 92.3 164.0 82.4
REMARK 620 5 SER B 202 OG 102.5 88.0 156.0 91.9
REMARK 620 6 PHE B 203 O 146.3 78.5 70.2 117.5 92.4
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 OD2
REMARK 620 2 HIS B 183 ND1 100.4
REMARK 620 3 ASP B 269 OD1 103.7 103.9
REMARK 620 4 20Y B 408 N20 97.5 105.7 139.5
REMARK 620 5 20Y B 408 N20 97.6 107.5 137.9 1.9
REMARK 620 6 20Y B 408 O12 171.3 85.0 81.3 74.4 74.2
REMARK 620 7 20Y B 408 O12 174.0 84.4 78.5 77.6 77.4 3.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 192 O
REMARK 620 2 THR B 195 O 79.5
REMARK 620 3 VAL B 198 O 119.6 83.7
REMARK 620 4 TYR B 227 O 155.8 120.0 79.2
REMARK 620 5 HOH B 514 O 89.8 91.9 148.6 76.2
REMARK 620 6 HOH B 535 O 72.8 151.5 115.5 85.7 81.9
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 OD1
REMARK 620 2 ASP C 179 O 70.9
REMARK 620 3 ASP C 181 O 100.7 103.8
REMARK 620 4 HIS C 183 O 93.3 163.7 82.6
REMARK 620 5 SER C 202 OG 103.2 89.2 155.5 90.6
REMARK 620 6 PHE C 203 O 145.5 78.6 71.0 117.7 91.8
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 OD2
REMARK 620 2 HIS C 183 ND1 100.2
REMARK 620 3 ASP C 269 OD2 104.2 103.0
REMARK 620 4 20Y C 406 N20 95.4 108.8 138.8
REMARK 620 5 20Y C 406 N20 100.5 103.0 140.0 7.0
REMARK 620 6 20Y C 406 O12 171.7 86.3 79.2 77.5 72.8
REMARK 620 7 20Y C 406 O12 172.5 83.6 81.1 77.2 72.2 3.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 403 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 192 O
REMARK 620 2 THR C 195 O 80.1
REMARK 620 3 VAL C 198 O 115.6 80.1
REMARK 620 4 TYR C 227 O 155.7 119.1 84.0
REMARK 620 5 HOH C 501 O 88.1 92.9 153.2 76.9
REMARK 620 6 HOH C 503 O 72.9 152.6 116.1 85.8 81.4
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 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 NA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20Y A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 B 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20Y B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 C 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 20Y C 406
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LXZ RELATED DB: PDB
DBREF 4LY1 A 12 380 UNP Q92769 HDAC2_HUMAN 8 376
DBREF 4LY1 B 12 380 UNP Q92769 HDAC2_HUMAN 8 376
DBREF 4LY1 C 12 380 UNP Q92769 HDAC2_HUMAN 8 376
SEQRES 1 A 369 GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE
SEQRES 2 A 369 GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO
SEQRES 3 A 369 HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR
SEQRES 4 A 369 GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS
SEQRES 5 A 369 ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU
SEQRES 6 A 369 TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET
SEQRES 7 A 369 SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY
SEQRES 8 A 369 GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS
SEQRES 9 A 369 GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS
SEQRES 10 A 369 LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA
SEQRES 11 A 369 GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY
SEQRES 12 A 369 PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU
SEQRES 13 A 369 LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE
SEQRES 14 A 369 ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR
SEQRES 15 A 369 THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR
SEQRES 16 A 369 GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE
SEQRES 17 A 369 GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO
SEQRES 18 A 369 MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE
SEQRES 19 A 369 PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN
SEQRES 20 A 369 PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU
SEQRES 21 A 369 SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS
SEQRES 22 A 369 GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN
SEQRES 23 A 369 LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE
SEQRES 24 A 369 ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL
SEQRES 25 A 369 ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN
SEQRES 26 A 369 ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS
SEQRES 27 A 369 ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU
SEQRES 28 A 369 TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU
SEQRES 29 A 369 ARG MET LEU PRO HIS
SEQRES 1 B 369 GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE
SEQRES 2 B 369 GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO
SEQRES 3 B 369 HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR
SEQRES 4 B 369 GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS
SEQRES 5 B 369 ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU
SEQRES 6 B 369 TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET
SEQRES 7 B 369 SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY
SEQRES 8 B 369 GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS
SEQRES 9 B 369 GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS
SEQRES 10 B 369 LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA
SEQRES 11 B 369 GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY
SEQRES 12 B 369 PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU
SEQRES 13 B 369 LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE
SEQRES 14 B 369 ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR
SEQRES 15 B 369 THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR
SEQRES 16 B 369 GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE
SEQRES 17 B 369 GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO
SEQRES 18 B 369 MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE
SEQRES 19 B 369 PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN
SEQRES 20 B 369 PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU
SEQRES 21 B 369 SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS
SEQRES 22 B 369 GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN
SEQRES 23 B 369 LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE
SEQRES 24 B 369 ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL
SEQRES 25 B 369 ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN
SEQRES 26 B 369 ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS
SEQRES 27 B 369 ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU
SEQRES 28 B 369 TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU
SEQRES 29 B 369 ARG MET LEU PRO HIS
SEQRES 1 C 369 GLY LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE
SEQRES 2 C 369 GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO
SEQRES 3 C 369 HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR
SEQRES 4 C 369 GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS
SEQRES 5 C 369 ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU
SEQRES 6 C 369 TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET
SEQRES 7 C 369 SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY
SEQRES 8 C 369 GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS
SEQRES 9 C 369 GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS
SEQRES 10 C 369 LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA
SEQRES 11 C 369 GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY
SEQRES 12 C 369 PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU
SEQRES 13 C 369 LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE
SEQRES 14 C 369 ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR
SEQRES 15 C 369 THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR
SEQRES 16 C 369 GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE
SEQRES 17 C 369 GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO
SEQRES 18 C 369 MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE
SEQRES 19 C 369 PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN
SEQRES 20 C 369 PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU
SEQRES 21 C 369 SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS
SEQRES 22 C 369 GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN
SEQRES 23 C 369 LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE
SEQRES 24 C 369 ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL
SEQRES 25 C 369 ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN
SEQRES 26 C 369 ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS
SEQRES 27 C 369 ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU
SEQRES 28 C 369 TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU
SEQRES 29 C 369 ARG MET LEU PRO HIS
HET ZN A 401 1
HET CA A 402 1
HET NA A 403 1
HET PG4 A 404 13
HET PG4 A 405 13
HET PG4 A 406 13
HET 20Y A 407 50
HET ZN B 401 1
HET CA B 402 1
HET NA B 403 1
HET NHE B 404 13
HET PG4 B 405 13
HET PG4 B 406 13
HET PG4 B 407 13
HET 20Y B 408 50
HET ZN C 401 1
HET CA C 402 1
HET NA C 403 1
HET PG4 C 404 13
HET PG4 C 405 13
HET 20Y C 406 50
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM PG4 TETRAETHYLENE GLYCOL
HETNAM 20Y 4-(ACETYLAMINO)-N-[2-AMINO-5-(THIOPHEN-2-YL)
HETNAM 2 20Y PHENYL]BENZAMIDE
HETNAM NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID
HETSYN NHE N-CYCLOHEXYLTAURINE; CHES
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 CA 3(CA 2+)
FORMUL 6 NA 3(NA 1+)
FORMUL 7 PG4 8(C8 H18 O5)
FORMUL 10 20Y 3(C19 H17 N3 O2 S)
FORMUL 14 NHE C8 H17 N O3 S
FORMUL 25 HOH *846(H2 O)
HELIX 1 1 ASP A 23 TYR A 27 5 5
HELIX 2 2 PRO A 37 TYR A 50 1 14
HELIX 3 3 GLY A 51 MET A 56 5 6
HELIX 4 4 THR A 65 THR A 70 1 6
HELIX 5 5 SER A 74 ILE A 84 1 11
HELIX 6 6 ASN A 88 GLU A 91 5 4
HELIX 7 7 TYR A 92 ASN A 100 1 9
HELIX 8 8 GLY A 110 ARG A 131 1 22
HELIX 9 9 ASN A 159 LEU A 169 1 11
HELIX 10 10 GLY A 185 PHE A 192 1 8
HELIX 11 11 ALA A 221 LYS A 225 5 5
HELIX 12 12 ASP A 238 GLN A 258 1 21
HELIX 13 13 GLY A 267 LEU A 271 5 5
HELIX 14 14 THR A 282 PHE A 296 1 15
HELIX 15 15 THR A 309 LEU A 325 1 17
HELIX 16 16 TYR A 338 GLY A 343 5 6
HELIX 17 17 THR A 360 ARG A 376 1 17
HELIX 18 18 ASP B 23 TYR B 27 5 5
HELIX 19 19 PRO B 37 TYR B 50 1 14
HELIX 20 20 GLY B 51 MET B 56 5 6
HELIX 21 21 THR B 65 THR B 70 1 6
HELIX 22 22 SER B 74 ILE B 84 1 11
HELIX 23 23 ARG B 85 MET B 89 5 5
HELIX 24 24 TYR B 92 ASN B 100 1 9
HELIX 25 25 GLY B 110 ARG B 131 1 22
HELIX 26 26 ASN B 159 LEU B 169 1 11
HELIX 27 27 GLY B 185 PHE B 192 1 8
HELIX 28 28 ALA B 221 LYS B 225 5 5
HELIX 29 29 ASP B 238 GLN B 258 1 21
HELIX 30 30 GLY B 267 LEU B 271 5 5
HELIX 31 31 THR B 282 THR B 295 1 14
HELIX 32 32 THR B 309 LEU B 325 1 17
HELIX 33 33 TYR B 338 GLY B 343 5 6
HELIX 34 34 THR B 360 ARG B 376 1 17
HELIX 35 35 ASP C 23 TYR C 27 5 5
HELIX 36 36 PRO C 37 TYR C 50 1 14
HELIX 37 37 GLY C 51 LYS C 55 5 5
HELIX 38 38 THR C 65 THR C 70 1 6
HELIX 39 39 SER C 74 ILE C 84 1 11
HELIX 40 40 ARG C 85 GLU C 91 5 7
HELIX 41 41 TYR C 92 ASN C 100 1 9
HELIX 42 42 GLY C 110 ARG C 131 1 22
HELIX 43 43 ASN C 159 LEU C 169 1 11
HELIX 44 44 GLY C 185 PHE C 192 1 8
HELIX 45 45 ALA C 221 LYS C 225 5 5
HELIX 46 46 ASP C 238 GLN C 258 1 21
HELIX 47 47 GLY C 267 LEU C 271 5 5
HELIX 48 48 THR C 282 THR C 295 1 14
HELIX 49 49 THR C 309 ASP C 326 1 18
HELIX 50 50 TYR C 338 GLY C 343 5 6
HELIX 51 51 THR C 360 MET C 377 1 18
SHEET 1 A 8 GLU A 57 TYR A 59 0
SHEET 2 A 8 VAL A 16 TYR A 19 1 N TYR A 18 O TYR A 59
SHEET 3 A 8 MET A 136 ASN A 139 1 O VAL A 138 N TYR A 19
SHEET 4 A 8 LEU A 300 LEU A 303 1 O MET A 302 N ALA A 137
SHEET 5 A 8 ALA A 261 GLN A 265 1 N LEU A 264 O LEU A 301
SHEET 6 A 8 VAL A 175 ASP A 179 1 N ILE A 178 O GLN A 265
SHEET 7 A 8 VAL A 198 LYS A 205 1 O MET A 199 N TYR A 177
SHEET 8 A 8 ALA A 228 MET A 233 1 O VAL A 229 N THR A 200
SHEET 1 B 8 GLU B 57 TYR B 59 0
SHEET 2 B 8 VAL B 16 TYR B 19 1 N TYR B 18 O TYR B 59
SHEET 3 B 8 MET B 136 ASN B 139 1 O VAL B 138 N TYR B 19
SHEET 4 B 8 LEU B 300 LEU B 303 1 O MET B 302 N ALA B 137
SHEET 5 B 8 ALA B 261 GLN B 265 1 N LEU B 264 O LEU B 301
SHEET 6 B 8 VAL B 175 ASP B 179 1 N ILE B 178 O VAL B 263
SHEET 7 B 8 VAL B 198 LYS B 205 1 O MET B 199 N TYR B 177
SHEET 8 B 8 ALA B 228 MET B 233 1 O PHE B 231 N SER B 202
SHEET 1 C 8 GLU C 57 TYR C 59 0
SHEET 2 C 8 VAL C 16 TYR C 19 1 N TYR C 18 O GLU C 57
SHEET 3 C 8 MET C 136 ASN C 139 1 O VAL C 138 N TYR C 19
SHEET 4 C 8 LEU C 300 LEU C 303 1 O MET C 302 N ALA C 137
SHEET 5 C 8 ALA C 261 GLN C 265 1 N LEU C 264 O LEU C 301
SHEET 6 C 8 VAL C 175 ASP C 179 1 N ILE C 178 O GLN C 265
SHEET 7 C 8 VAL C 198 LYS C 205 1 O MET C 199 N TYR C 177
SHEET 8 C 8 ALA C 228 MET C 233 1 O PHE C 231 N SER C 202
LINK OD1 ASP A 179 CA CA A 402 1555 1555 2.57
LINK O ASP A 179 CA CA A 402 1555 1555 2.91
LINK OD2 ASP A 181 ZN ZN A 401 1555 1555 2.03
LINK O ASP A 181 CA CA A 402 1555 1555 2.63
LINK ND1 HIS A 183 ZN ZN A 401 1555 1555 2.05
LINK O HIS A 183 CA CA A 402 1555 1555 2.70
LINK O PHE A 192 NA NA A 403 1555 1555 2.55
LINK O THR A 195 NA NA A 403 1555 1555 2.77
LINK O VAL A 198 NA NA A 403 1555 1555 2.53
LINK OG SER A 202 CA CA A 402 1555 1555 2.93
LINK O PHE A 203 CA CA A 402 1555 1555 2.61
LINK O TYR A 227 NA NA A 403 1555 1555 3.08
LINK OD2 ASP A 269 ZN ZN A 401 1555 1555 1.92
LINK ZN ZN A 401 N20A20Y A 407 1555 1555 1.91
LINK ZN ZN A 401 N20B20Y A 407 1555 1555 2.29
LINK ZN ZN A 401 O12A20Y A 407 1555 1555 2.56
LINK ZN ZN A 401 O12B20Y A 407 1555 1555 2.59
LINK NA NA A 403 O HOH A 520 1555 1555 2.50
LINK NA NA A 403 O HOH A 521 1555 1555 2.95
LINK OD1 ASP B 179 CA CA B 402 1555 1555 2.60
LINK O ASP B 179 CA CA B 402 1555 1555 2.94
LINK OD2 ASP B 181 ZN ZN B 401 1555 1555 1.98
LINK O ASP B 181 CA CA B 402 1555 1555 2.60
LINK ND1 HIS B 183 ZN ZN B 401 1555 1555 2.02
LINK O HIS B 183 CA CA B 402 1555 1555 2.68
LINK O PHE B 192 NA NA B 403 1555 1555 2.58
LINK O THR B 195 NA NA B 403 1555 1555 2.75
LINK O VAL B 198 NA NA B 403 1555 1555 2.52
LINK OG SER B 202 CA CA B 402 1555 1555 2.87
LINK O PHE B 203 CA CA B 402 1555 1555 2.60
LINK O TYR B 227 NA NA B 403 1555 1555 3.03
LINK OD1 ASP B 269 ZN ZN B 401 1555 1555 1.97
LINK ZN ZN B 401 N20B20Y B 408 1555 1555 2.03
LINK ZN ZN B 401 N20A20Y B 408 1555 1555 2.19
LINK ZN ZN B 401 O12A20Y B 408 1555 1555 2.58
LINK ZN ZN B 401 O12B20Y B 408 1555 1555 2.66
LINK NA NA B 403 O HOH B 514 1555 1555 2.55
LINK NA NA B 403 O HOH B 535 1555 1555 2.87
LINK OD1 ASP C 179 CA CA C 402 1555 1555 2.57
LINK O ASP C 179 CA CA C 402 1555 1555 2.89
LINK OD2 ASP C 181 ZN ZN C 401 1555 1555 2.05
LINK O ASP C 181 CA CA C 402 1555 1555 2.58
LINK ND1 HIS C 183 ZN ZN C 401 1555 1555 2.06
LINK O HIS C 183 CA CA C 402 1555 1555 2.70
LINK O PHE C 192 NA NA C 403 1555 1555 2.55
LINK O THR C 195 NA NA C 403 1555 1555 2.76
LINK O VAL C 198 NA NA C 403 1555 1555 2.49
LINK OG SER C 202 CA CA C 402 1555 1555 2.91
LINK O PHE C 203 CA CA C 402 1555 1555 2.61
LINK O TYR C 227 NA NA C 403 1555 1555 3.08
LINK OD2 ASP C 269 ZN ZN C 401 1555 1555 1.99
LINK ZN ZN C 401 N20B20Y C 406 1555 1555 2.04
LINK ZN ZN C 401 N20A20Y C 406 1555 1555 2.19
LINK ZN ZN C 401 O12B20Y C 406 1555 1555 2.50
LINK ZN ZN C 401 O12A20Y C 406 1555 1555 2.62
LINK NA NA C 403 O HOH C 501 1555 1555 2.53
LINK NA NA C 403 O HOH C 503 1555 1555 2.95
CISPEP 1 PHE A 210 PRO A 211 0 -3.99
CISPEP 2 GLY A 343 PRO A 344 0 1.28
CISPEP 3 PHE B 210 PRO B 211 0 -2.64
CISPEP 4 GLY B 343 PRO B 344 0 2.65
CISPEP 5 PHE C 210 PRO C 211 0 -4.18
CISPEP 6 GLY C 343 PRO C 344 0 2.91
SITE 1 AC1 4 ASP A 181 HIS A 183 ASP A 269 20Y A 407
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 520 HOH A 521
SITE 1 AC4 3 LYS A 71 ALA A 191 PHE A 192
SITE 1 AC5 5 ARG A 311 GLU A 340 TYR A 341 GLY A 343
SITE 2 AC5 5 HOH A 791
SITE 1 AC6 3 ASP A 23 ASN A 26 TYR A 27
SITE 1 AC7 20 TYR A 29 MET A 35 ARG A 39 GLY A 143
SITE 2 AC7 20 LEU A 144 HIS A 145 HIS A 146 GLY A 154
SITE 3 AC7 20 PHE A 155 CYS A 156 ASP A 181 HIS A 183
SITE 4 AC7 20 PHE A 210 ASP A 269 LEU A 276 GLY A 305
SITE 5 AC7 20 GLY A 306 TYR A 308 ZN A 401 HOH A 593
SITE 1 AC8 4 ASP B 181 HIS B 183 ASP B 269 20Y B 408
SITE 1 AC9 5 ASP B 179 ASP B 181 HIS B 183 SER B 202
SITE 2 AC9 5 PHE B 203
SITE 1 BC1 6 PHE B 192 THR B 195 VAL B 198 TYR B 227
SITE 2 BC1 6 HOH B 514 HOH B 535
SITE 1 BC2 10 TYR A 59 LYS A 128 HOH A 583 ASP B 21
SITE 2 BC2 10 ASP B 23 TYR B 27 ARG B 60 LYS B 63
SITE 3 BC2 10 GLU B 113 PG4 B 407
SITE 1 BC3 6 HOH A 783 ARG B 311 GLU B 340 TYR B 341
SITE 2 BC3 6 GLY B 343 HOH B 714
SITE 1 BC4 6 LYS B 284 GLU B 328 ASN B 331 HIS B 349
SITE 2 BC4 6 GLU C 67 THR C 70
SITE 1 BC5 10 ARG A 131 HOH A 631 ASP B 23 ASN B 26
SITE 2 BC5 10 TYR B 27 ASP B 109 NHE B 404 HOH B 736
SITE 3 BC5 10 HOH B 748 HOH B 822
SITE 1 BC6 21 TYR B 29 MET B 35 ARG B 39 GLY B 143
SITE 2 BC6 21 LEU B 144 HIS B 145 HIS B 146 GLY B 154
SITE 3 BC6 21 PHE B 155 CYS B 156 ASP B 181 HIS B 183
SITE 4 BC6 21 PHE B 210 ASP B 269 GLY B 305 GLY B 306
SITE 5 BC6 21 TYR B 308 ZN B 401 HOH B 602 HOH B 617
SITE 6 BC6 21 HOH B 639
SITE 1 BC7 4 ASP C 181 HIS C 183 ASP C 269 20Y C 406
SITE 1 BC8 5 ASP C 179 ASP C 181 HIS C 183 SER C 202
SITE 2 BC8 5 PHE C 203
SITE 1 BC9 6 PHE C 192 THR C 195 VAL C 198 TYR C 227
SITE 2 BC9 6 HOH C 501 HOH C 503
SITE 1 CC1 5 ASP B 345 ALA C 191 ARG C 197 HOH C 558
SITE 2 CC1 5 HOH C 576
SITE 1 CC2 7 ASN B 354 LEU C 169 LYS C 170 TYR C 171
SITE 2 CC2 7 GLN C 173 ARG C 197 HOH C 687
SITE 1 CC3 20 TYR C 29 MET C 35 ARG C 39 GLY C 143
SITE 2 CC3 20 LEU C 144 HIS C 145 HIS C 146 GLY C 154
SITE 3 CC3 20 PHE C 155 CYS C 156 ASP C 181 HIS C 183
SITE 4 CC3 20 PHE C 210 ASP C 269 GLY C 305 GLY C 306
SITE 5 CC3 20 TYR C 308 ZN C 401 HOH C 583 HOH C 586
CRYST1 92.034 97.490 138.922 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 0.010866 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010257 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007198 0.00000
(ATOM LINES ARE NOT SHOWN.)
END