HEADER HYDROLASE 24-MAR-10 3MAX
TITLE CRYSTAL STRUCTURE OF HUMAN HDAC2 COMPLEXED WITH AN N-(2-AMINOPHENYL)
TITLE 2 BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEACETYLASE 2;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: HD2;
COMPND 5 EC: 3.5.1.98;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HDAC2;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PSXB19
KEYWDS CLASS 2, HDAC, FOOT POCKET, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.SKENE,A.J.JENNINGS
REVDAT 3 21-FEB-24 3MAX 1 REMARK SEQADV LINK
REVDAT 2 19-MAY-10 3MAX 1 JRNL
REVDAT 1 28-APR-10 3MAX 0
JRNL AUTH J.C.BRESSI,A.J.JENNINGS,R.SKENE,Y.WU,R.MELKUS,R.DE JONG,
JRNL AUTH 2 S.O'CONNELL,C.E.GRIMSHAW,M.NAVRE,A.R.GANGLOFF
JRNL TITL EXPLORATION OF THE HDAC2 FOOT POCKET: SYNTHESIS AND SAR OF
JRNL TITL 2 SUBSTITUTED N-(2-AMINOPHENYL)BENZAMIDES.
JRNL REF BIOORG.MED.CHEM.LETT. V. 20 3142 2010
JRNL REFN ISSN 0960-894X
JRNL PMID 20392638
JRNL DOI 10.1016/J.BMCL.2010.03.091
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 75270
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3973
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5480
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 244
REMARK 3 BIN FREE R VALUE : 0.2860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8842
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 624
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.11000
REMARK 3 B22 (A**2) : 3.56000
REMARK 3 B33 (A**2) : -1.45000
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): 0.174
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.152
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.101
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.053
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9185 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12400 ; 1.325 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1094 ; 5.136 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 454 ;37.752 ;23.744
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1558 ;13.240 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;18.269 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1270 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7111 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4539 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6302 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 601 ; 0.130 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 15 ; 0.096 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 73 ; 0.200 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.138 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 5438 ; 1.711 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8752 ; 2.668 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3867 ; 2.271 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3648 ; 3.312 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MAX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-10.
REMARK 100 THE DEPOSITION ID IS D_1000058325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-OCT-05
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 : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79353
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 79.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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 (%): 50.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% (V/V) PEG-600, 0.1 MM CHES, PH
REMARK 280 9.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 46.15550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.42450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.61350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.42450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 46.15550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.61350
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 ALA B 12
REMARK 465 LYS B 13
REMARK 465 LYS B 14
REMARK 465 ALA C 12
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 C 13 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 373 CD GLU A 373 OE2 0.077
REMARK 500 GLU B 373 CD GLU B 373 OE2 0.080
REMARK 500 GLU C 373 CD GLU C 373 OE2 0.079
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 -101.26 -136.82
REMARK 500 CYS A 105 78.17 -117.24
REMARK 500 PHE A 155 -3.86 75.40
REMARK 500 TYR A 226 -1.71 83.29
REMARK 500 CYS A 266 43.95 -108.89
REMARK 500 GLU B 103 -100.35 -110.82
REMARK 500 CYS B 105 79.60 -111.86
REMARK 500 PHE B 155 -1.66 80.56
REMARK 500 TYR B 226 0.87 81.88
REMARK 500 CYS B 266 44.72 -109.12
REMARK 500 TYR C 72 -52.61 -121.56
REMARK 500 GLU C 103 -98.61 -113.63
REMARK 500 CYS C 105 79.85 -114.43
REMARK 500 PHE C 155 -2.63 80.75
REMARK 500 TYR C 226 -0.49 80.61
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 380 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 100.2 103.3
REMARK 620 4 HIS A 183 O 90.1 162.0 79.1
REMARK 620 5 SER A 202 OG 102.8 88.6 156.5 95.8
REMARK 620 6 PHE A 203 O 144.2 76.2 71.7 121.0 92.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 379 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 181 OD2
REMARK 620 2 HIS A 183 ND1 105.3
REMARK 620 3 ASP A 269 OD2 104.7 102.4
REMARK 620 4 LLX A 400 N1 100.5 102.2 138.3
REMARK 620 5 LLX A 400 O10 167.8 83.7 80.9 69.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 381 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 192 O
REMARK 620 2 THR A 195 O 91.2
REMARK 620 3 VAL A 198 O 129.8 88.0
REMARK 620 4 HOH A 396 O 93.4 93.7 136.7
REMARK 620 5 HOH A 425 O 84.7 167.9 103.4 75.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 380 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 179 OD1
REMARK 620 2 ASP B 179 O 71.1
REMARK 620 3 ASP B 181 O 100.2 105.5
REMARK 620 4 HIS B 183 O 94.5 165.2 80.1
REMARK 620 5 SER B 202 OG 104.2 87.7 155.0 92.5
REMARK 620 6 PHE B 203 O 144.8 76.7 74.6 118.1 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 379 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 103.6 105.0
REMARK 620 4 LLX B 400 N1 102.0 103.3 137.3
REMARK 620 5 LLX B 400 O10 174.7 82.5 79.8 72.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 381 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE B 192 O
REMARK 620 2 THR B 195 O 90.5
REMARK 620 3 VAL B 198 O 124.7 88.0
REMARK 620 4 HOH B 385 O 91.6 94.2 143.7
REMARK 620 5 HOH B 441 O 78.5 164.5 107.3 75.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 380 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 179 OD1
REMARK 620 2 ASP C 179 O 71.0
REMARK 620 3 ASP C 181 O 100.5 103.2
REMARK 620 4 HIS C 183 O 91.7 162.4 82.4
REMARK 620 5 SER C 202 OG 102.5 87.0 156.8 94.1
REMARK 620 6 PHE C 203 O 144.7 78.6 69.3 118.9 93.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 379 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 181 OD2
REMARK 620 2 HIS C 183 ND1 101.2
REMARK 620 3 ASP C 269 OD2 102.8 103.1
REMARK 620 4 LLX C 400 N1 99.9 104.7 139.7
REMARK 620 5 LLX C 400 O10 173.0 85.0 78.9 75.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 381 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE C 192 O
REMARK 620 2 THR C 195 O 93.4
REMARK 620 3 VAL C 198 O 121.4 87.5
REMARK 620 4 HOH C 389 O 91.9 101.2 145.2
REMARK 620 5 HOH C 464 O 79.3 172.3 98.3 76.9
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 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LLX A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NHE A 383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LLX B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 379
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 380
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LLX C 400
DBREF 3MAX A 13 378 UNP Q92769 HDAC2_HUMAN 9 374
DBREF 3MAX B 13 378 UNP Q92769 HDAC2_HUMAN 9 374
DBREF 3MAX C 13 378 UNP Q92769 HDAC2_HUMAN 9 374
SEQADV 3MAX ALA A 12 UNP Q92769 EXPRESSION TAG
SEQADV 3MAX ALA B 12 UNP Q92769 EXPRESSION TAG
SEQADV 3MAX ALA C 12 UNP Q92769 EXPRESSION TAG
SEQRES 1 A 367 ALA LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE
SEQRES 2 A 367 GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO
SEQRES 3 A 367 HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR
SEQRES 4 A 367 GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS
SEQRES 5 A 367 ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU
SEQRES 6 A 367 TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET
SEQRES 7 A 367 SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY
SEQRES 8 A 367 GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS
SEQRES 9 A 367 GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS
SEQRES 10 A 367 LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA
SEQRES 11 A 367 GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY
SEQRES 12 A 367 PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU
SEQRES 13 A 367 LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE
SEQRES 14 A 367 ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR
SEQRES 15 A 367 THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR
SEQRES 16 A 367 GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE
SEQRES 17 A 367 GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO
SEQRES 18 A 367 MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE
SEQRES 19 A 367 PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN
SEQRES 20 A 367 PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU
SEQRES 21 A 367 SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS
SEQRES 22 A 367 GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN
SEQRES 23 A 367 LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE
SEQRES 24 A 367 ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL
SEQRES 25 A 367 ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN
SEQRES 26 A 367 ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS
SEQRES 27 A 367 ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU
SEQRES 28 A 367 TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU
SEQRES 29 A 367 ARG MET LEU
SEQRES 1 B 367 ALA LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE
SEQRES 2 B 367 GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO
SEQRES 3 B 367 HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR
SEQRES 4 B 367 GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS
SEQRES 5 B 367 ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU
SEQRES 6 B 367 TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET
SEQRES 7 B 367 SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY
SEQRES 8 B 367 GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS
SEQRES 9 B 367 GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS
SEQRES 10 B 367 LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA
SEQRES 11 B 367 GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY
SEQRES 12 B 367 PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU
SEQRES 13 B 367 LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE
SEQRES 14 B 367 ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR
SEQRES 15 B 367 THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR
SEQRES 16 B 367 GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE
SEQRES 17 B 367 GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO
SEQRES 18 B 367 MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE
SEQRES 19 B 367 PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN
SEQRES 20 B 367 PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU
SEQRES 21 B 367 SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS
SEQRES 22 B 367 GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN
SEQRES 23 B 367 LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE
SEQRES 24 B 367 ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL
SEQRES 25 B 367 ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN
SEQRES 26 B 367 ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS
SEQRES 27 B 367 ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU
SEQRES 28 B 367 TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU
SEQRES 29 B 367 ARG MET LEU
SEQRES 1 C 367 ALA LYS LYS LYS VAL CYS TYR TYR TYR ASP GLY ASP ILE
SEQRES 2 C 367 GLY ASN TYR TYR TYR GLY GLN GLY HIS PRO MET LYS PRO
SEQRES 3 C 367 HIS ARG ILE ARG MET THR HIS ASN LEU LEU LEU ASN TYR
SEQRES 4 C 367 GLY LEU TYR ARG LYS MET GLU ILE TYR ARG PRO HIS LYS
SEQRES 5 C 367 ALA THR ALA GLU GLU MET THR LYS TYR HIS SER ASP GLU
SEQRES 6 C 367 TYR ILE LYS PHE LEU ARG SER ILE ARG PRO ASP ASN MET
SEQRES 7 C 367 SER GLU TYR SER LYS GLN MET GLN ARG PHE ASN VAL GLY
SEQRES 8 C 367 GLU ASP CYS PRO VAL PHE ASP GLY LEU PHE GLU PHE CYS
SEQRES 9 C 367 GLN LEU SER THR GLY GLY SER VAL ALA GLY ALA VAL LYS
SEQRES 10 C 367 LEU ASN ARG GLN GLN THR ASP MET ALA VAL ASN TRP ALA
SEQRES 11 C 367 GLY GLY LEU HIS HIS ALA LYS LYS SER GLU ALA SER GLY
SEQRES 12 C 367 PHE CYS TYR VAL ASN ASP ILE VAL LEU ALA ILE LEU GLU
SEQRES 13 C 367 LEU LEU LYS TYR HIS GLN ARG VAL LEU TYR ILE ASP ILE
SEQRES 14 C 367 ASP ILE HIS HIS GLY ASP GLY VAL GLU GLU ALA PHE TYR
SEQRES 15 C 367 THR THR ASP ARG VAL MET THR VAL SER PHE HIS LYS TYR
SEQRES 16 C 367 GLY GLU TYR PHE PRO GLY THR GLY ASP LEU ARG ASP ILE
SEQRES 17 C 367 GLY ALA GLY LYS GLY LYS TYR TYR ALA VAL ASN PHE PRO
SEQRES 18 C 367 MET ARG ASP GLY ILE ASP ASP GLU SER TYR GLY GLN ILE
SEQRES 19 C 367 PHE LYS PRO ILE ILE SER LYS VAL MET GLU MET TYR GLN
SEQRES 20 C 367 PRO SER ALA VAL VAL LEU GLN CYS GLY ALA ASP SER LEU
SEQRES 21 C 367 SER GLY ASP ARG LEU GLY CYS PHE ASN LEU THR VAL LYS
SEQRES 22 C 367 GLY HIS ALA LYS CYS VAL GLU VAL VAL LYS THR PHE ASN
SEQRES 23 C 367 LEU PRO LEU LEU MET LEU GLY GLY GLY GLY TYR THR ILE
SEQRES 24 C 367 ARG ASN VAL ALA ARG CYS TRP THR TYR GLU THR ALA VAL
SEQRES 25 C 367 ALA LEU ASP CYS GLU ILE PRO ASN GLU LEU PRO TYR ASN
SEQRES 26 C 367 ASP TYR PHE GLU TYR PHE GLY PRO ASP PHE LYS LEU HIS
SEQRES 27 C 367 ILE SER PRO SER ASN MET THR ASN GLN ASN THR PRO GLU
SEQRES 28 C 367 TYR MET GLU LYS ILE LYS GLN ARG LEU PHE GLU ASN LEU
SEQRES 29 C 367 ARG MET LEU
HET ZN A 379 1
HET CA A 380 1
HET NA A 381 1
HET LLX A 400 22
HET NHE A 383 19
HET ZN B 379 1
HET CA B 380 1
HET NA B 381 1
HET LLX B 400 22
HET ZN C 379 1
HET CA C 380 1
HET NA C 381 1
HET LLX C 400 22
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
HETNAM NA SODIUM ION
HETNAM LLX N-(4-AMINOBIPHENYL-3-YL)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 LLX 3(C19 H16 N2 O)
FORMUL 8 NHE C8 H17 N O3 S
FORMUL 17 HOH *624(H2 O)
HELIX 1 1 ASP A 21 TYR A 27 5 7
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 ARG A 85 GLU A 91 5 7
HELIX 7 7 TYR A 92 PHE A 99 1 8
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 THR A 295 1 14
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 LYS B 55 5 5
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 LYS B 170 1 12
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 MET C 56 5 6
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 PHE C 99 1 8
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 LEU C 325 1 17
HELIX 50 50 TYR C 338 GLY C 343 5 6
HELIX 51 51 THR C 360 ARG C 376 1 17
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 PHE A 231 N SER A 202
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 LEU B 176 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 TYR C 59
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 VAL C 229 N THR C 200
LINK OD1 ASP A 179 CA CA A 380 1555 1555 2.66
LINK O ASP A 179 CA CA A 380 1555 1555 2.99
LINK OD2 ASP A 181 ZN ZN A 379 1555 1555 2.00
LINK O ASP A 181 CA CA A 380 1555 1555 2.62
LINK ND1 HIS A 183 ZN ZN A 379 1555 1555 2.19
LINK O HIS A 183 CA CA A 380 1555 1555 2.69
LINK O PHE A 192 NA NA A 381 1555 1555 2.18
LINK O THR A 195 NA NA A 381 1555 1555 2.50
LINK O VAL A 198 NA NA A 381 1555 1555 2.33
LINK OG SER A 202 CA CA A 380 1555 1555 2.84
LINK O PHE A 203 CA CA A 380 1555 1555 2.65
LINK OD2 ASP A 269 ZN ZN A 379 1555 1555 2.05
LINK ZN ZN A 379 N1 LLX A 400 1555 1555 2.13
LINK ZN ZN A 379 O10 LLX A 400 1555 1555 2.54
LINK NA NA A 381 O HOH A 396 1555 1555 2.41
LINK NA NA A 381 O HOH A 425 1555 1555 2.58
LINK OD1 ASP B 179 CA CA B 380 1555 1555 2.59
LINK O ASP B 179 CA CA B 380 1555 1555 2.90
LINK OD2 ASP B 181 ZN ZN B 379 1555 1555 1.95
LINK O ASP B 181 CA CA B 380 1555 1555 2.52
LINK ND1 HIS B 183 ZN ZN B 379 1555 1555 2.10
LINK O HIS B 183 CA CA B 380 1555 1555 2.64
LINK O PHE B 192 NA NA B 381 1555 1555 2.34
LINK O THR B 195 NA NA B 381 1555 1555 2.50
LINK O VAL B 198 NA NA B 381 1555 1555 2.34
LINK OG SER B 202 CA CA B 380 1555 1555 2.90
LINK O PHE B 203 CA CA B 380 1555 1555 2.58
LINK OD1 ASP B 269 ZN ZN B 379 1555 1555 1.91
LINK ZN ZN B 379 N1 LLX B 400 1555 1555 2.08
LINK ZN ZN B 379 O10 LLX B 400 1555 1555 2.67
LINK NA NA B 381 O HOH B 385 1555 1555 2.33
LINK NA NA B 381 O HOH B 441 1555 1555 2.52
LINK OD1 ASP C 179 CA CA C 380 1555 1555 2.63
LINK O ASP C 179 CA CA C 380 1555 1555 2.83
LINK OD2 ASP C 181 ZN ZN C 379 1555 1555 2.15
LINK O ASP C 181 CA CA C 380 1555 1555 2.57
LINK ND1 HIS C 183 ZN ZN C 379 1555 1555 2.04
LINK O HIS C 183 CA CA C 380 1555 1555 2.72
LINK O PHE C 192 NA NA C 381 1555 1555 2.30
LINK O THR C 195 NA NA C 381 1555 1555 2.38
LINK O VAL C 198 NA NA C 381 1555 1555 2.33
LINK OG SER C 202 CA CA C 380 1555 1555 2.86
LINK O PHE C 203 CA CA C 380 1555 1555 2.62
LINK OD2 ASP C 269 ZN ZN C 379 1555 1555 1.98
LINK ZN ZN C 379 N1 LLX C 400 1555 1555 2.13
LINK ZN ZN C 379 O10 LLX C 400 1555 1555 2.61
LINK NA NA C 381 O HOH C 389 1555 1555 2.26
LINK NA NA C 381 O HOH C 464 1555 1555 2.67
CISPEP 1 PHE A 210 PRO A 211 0 -3.60
CISPEP 2 GLY A 343 PRO A 344 0 4.13
CISPEP 3 PHE B 210 PRO B 211 0 -4.24
CISPEP 4 GLY B 343 PRO B 344 0 0.28
CISPEP 5 PHE C 210 PRO C 211 0 -4.99
CISPEP 6 GLY C 343 PRO C 344 0 2.58
SITE 1 AC1 4 ASP A 181 HIS A 183 ASP A 269 LLX A 400
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 396 HOH A 425
SITE 1 AC4 19 TYR A 29 MET A 35 ARG A 39 GLY A 143
SITE 2 AC4 19 LEU A 144 HIS A 145 HIS A 146 GLY A 154
SITE 3 AC4 19 PHE A 155 CYS A 156 ASP A 181 HIS A 183
SITE 4 AC4 19 PHE A 210 ASP A 269 LEU A 276 GLY A 305
SITE 5 AC4 19 GLY A 306 TYR A 308 ZN A 379
SITE 1 AC5 11 TYR A 59 LYS A 128 HOH A 537 HOH A 538
SITE 2 AC5 11 HOH A 539 ASP B 21 GLY B 22 ASP B 23
SITE 3 AC5 11 ARG B 60 GLU B 113 LEU B 117
SITE 1 AC6 4 ASP B 181 HIS B 183 ASP B 269 LLX B 400
SITE 1 AC7 5 ASP B 179 ASP B 181 HIS B 183 SER B 202
SITE 2 AC7 5 PHE B 203
SITE 1 AC8 6 PHE B 192 THR B 195 VAL B 198 TYR B 227
SITE 2 AC8 6 HOH B 385 HOH B 441
SITE 1 AC9 18 TYR B 29 MET B 35 ARG B 39 GLY B 143
SITE 2 AC9 18 LEU B 144 HIS B 145 HIS B 146 GLY B 154
SITE 3 AC9 18 PHE B 155 CYS B 156 ASP B 181 HIS B 183
SITE 4 AC9 18 PHE B 210 ASP B 269 GLY B 305 GLY B 306
SITE 5 AC9 18 TYR B 308 ZN B 379
SITE 1 BC1 4 ASP C 181 HIS C 183 ASP C 269 LLX C 400
SITE 1 BC2 5 ASP C 179 ASP C 181 HIS C 183 SER C 202
SITE 2 BC2 5 PHE C 203
SITE 1 BC3 6 PHE C 192 THR C 195 VAL C 198 TYR C 227
SITE 2 BC3 6 HOH C 389 HOH C 464
SITE 1 BC4 19 TYR C 29 MET C 35 ARG C 39 GLY C 143
SITE 2 BC4 19 LEU C 144 HIS C 145 HIS C 146 GLY C 154
SITE 3 BC4 19 PHE C 155 CYS C 156 ASP C 181 HIS C 183
SITE 4 BC4 19 PHE C 210 ASP C 269 LEU C 276 GLY C 305
SITE 5 BC4 19 GLY C 306 TYR C 308 ZN C 379
CRYST1 92.311 97.227 138.849 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 0.010833 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010285 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007202 0.00000
(ATOM LINES ARE NOT SHOWN.)
END