HEADER HYDROLASE 01-JUL-13 3WE7
TITLE CRYSTAL STRUCTURE OF DIACETYLCHITOBIOSE DEACETYLASE FROM PYROCOCCUS
TITLE 2 HORIKOSHII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN PH0499;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROCOCCUS HORIKOSHII OT3;
SOURCE 3 ORGANISM_TAXID: 70601;
SOURCE 4 STRAIN: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
SOURCE 5 GENE: PH0499;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROSSMANN FOLD, HYDROLASE, ZINC BINDING, DEACETYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MINE,T.NAKAMURA,Y.FUKUDA,T.INOUE,K.UEGAKI,T.SATO
REVDAT 2 20-AUG-14 3WE7 1 JRNL
REVDAT 1 07-MAY-14 3WE7 0
JRNL AUTH S.MINE,M.NIIYAMA,W.HASHIMOTO,T.IKEGAMI,D.KOMA,T.OHMOTO,
JRNL AUTH 2 Y.FUKUDA,T.INOUE,Y.ABE,T.UEDA,J.MORITA,K.UEGAKI,T.NAKAMURA
JRNL TITL EXPRESSION FROM ENGINEERED ESCHERICHIA COLI CHROMOSOME AND
JRNL TITL 2 CRYSTALLOGRAPHIC STUDY OF ARCHAEAL N,N'-DIACETYLCHITOBIOSE
JRNL TITL 3 DEACETYLASE
JRNL REF FEBS J. V. 281 2584 2014
JRNL REFN ISSN 1742-464X
JRNL PMID 24702737
JRNL DOI 10.1111/FEBS.12805
REMARK 2
REMARK 2 RESOLUTION. 1.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.62
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 109668
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5792
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 REFLECTION IN BIN (WORKING SET) : 7495
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 383
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6570
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 73
REMARK 3 SOLVENT ATOMS : 547
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.25
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.083
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.060
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.686
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6917 ; 0.024 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9363 ; 2.346 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 822 ; 6.423 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 340 ;34.189 ;23.824
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1187 ;14.469 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 45 ;18.033 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 987 ; 0.179 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5327 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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): 3 ; 8.302 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN
REMARK 3 THE INPUT
REMARK 4
REMARK 4 3WE7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUL-13.
REMARK 100 THE RCSB ID CODE IS RCSB096223.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97895, 0.97926, 0.99498
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 115813
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M COBALTOUS CHLORIDE HEXAHYDRATE,
REMARK 280 0.1M SODIUM ACETATE TRIHYDRATE, 1.0M 1,6 HEXANEDIOL, PH 4.6,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 153.48200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 76.74100
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 76.74100
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 153.48200
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 35430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 52590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -201.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, 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 BIOMT1 2 -0.500000 -0.866025 0.000000 116.05800
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 67.00612
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 153.48200
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 VAL A 2
REMARK 465 VAL A 3
REMARK 465 ASN A 4
REMARK 465 MET A 5
REMARK 465 MET B 1
REMARK 465 VAL B 2
REMARK 465 VAL B 3
REMARK 465 ASN B 4
REMARK 465 MET B 5
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 VAL C 3
REMARK 465 ASN C 4
REMARK 465 MET C 5
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 O3 GOL B 303 O HOH B 459 1.63
REMARK 500 OD1 ASP C 208 O HOH C 527 2.14
REMARK 500 OD1 ASP B 227 O HOH B 562 2.18
REMARK 500 O HOH B 468 O HOH B 474 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 HIS A 44 CG HIS A 44 CD2 0.066
REMARK 500 GLY A 104 N GLY A 104 CA 0.118
REMARK 500 HIS A 152 CG HIS A 152 CD2 0.059
REMARK 500 HIS B 198 CG HIS B 198 CD2 0.069
REMARK 500 ASP B 208 CB ASP B 208 CG 0.127
REMARK 500 HIS B 220 CG HIS B 220 CD2 0.058
REMARK 500 HIS B 264 CG HIS B 264 CD2 0.055
REMARK 500 HIS C 220 CG HIS C 220 CD2 0.058
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 47 CB - CG - OD2 ANGL. DEV. = -6.2 DEGREES
REMARK 500 LEU A 103 O - C - N ANGL. DEV. = -10.3 DEGREES
REMARK 500 GLY A 104 C - N - CA ANGL. DEV. = -25.1 DEGREES
REMARK 500 ASP A 115 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 125 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP A 205 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ARG B 101 NE - CZ - NH1 ANGL. DEV. = 5.3 DEGREES
REMARK 500 ASP B 115 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG B 218 NE - CZ - NH1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP C 61 CB - CG - OD2 ANGL. DEV. = -11.5 DEGREES
REMARK 500 ASP C 80 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG C 125 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG C 125 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG C 157 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 LEU C 212 CB - CG - CD2 ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG C 256 NE - CZ - NH1 ANGL. DEV. = 3.4 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 ASP A 46 -13.90 112.89
REMARK 500 MET A 52 27.48 -142.61
REMARK 500 THR A 116 -5.29 85.65
REMARK 500 ASN A 187 10.31 -149.66
REMARK 500 ILE A 265 15.96 54.99
REMARK 500 ASP B 34 -5.84 67.05
REMARK 500 ASP B 46 -20.53 113.11
REMARK 500 MET B 52 26.94 -146.12
REMARK 500 ASN C 30 64.84 -151.45
REMARK 500 ASP C 46 -13.35 118.50
REMARK 500 MET C 52 27.66 -149.99
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 125 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ARG A 21 21.9 L L OUTSIDE RANGE
REMARK 500 THR A 207 22.1 L L OUTSIDE RANGE
REMARK 500 ASN C 112 24.2 L L OUTSIDE RANGE
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 ZN A 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACY A 303 OXT
REMARK 620 2 HIS A 44 ND1 112.3
REMARK 620 3 HIS A 155 NE2 99.8 104.4
REMARK 620 4 ASP A 47 OD2 138.9 99.3 96.8
REMARK 620 5 ACY A 303 O 57.4 97.2 153.7 94.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACY C 302 OXT
REMARK 620 2 ASP C 47 OD2 133.1
REMARK 620 3 HIS C 155 NE2 98.6 102.2
REMARK 620 4 HIS C 44 ND1 115.5 99.5 104.0
REMARK 620 5 ACY C 302 O 57.5 90.0 154.1 96.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ACY B 304 OXT
REMARK 620 2 ASP B 47 OD2 131.9
REMARK 620 3 HIS B 155 NE2 96.1 100.2
REMARK 620 4 HIS B 44 ND1 120.0 98.6 105.4
REMARK 620 5 ACY B 304 O 59.2 90.4 152.9 97.5
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 304 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 138 OD1
REMARK 620 2 HOH C 567 O 168.5
REMARK 620 3 HOH C 564 O 79.9 89.3
REMARK 620 4 HOH C 565 O 92.4 93.7 103.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEZ C 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WL4 RELATED DB: PDB
REMARK 900 RELATED ID: 3WL3 RELATED DB: PDB
DBREF 3WE7 A 1 272 UNP O58235 O58235_PYRHO 1 272
DBREF 3WE7 B 1 272 UNP O58235 O58235_PYRHO 1 272
DBREF 3WE7 C 1 272 UNP O58235 O58235_PYRHO 1 272
SEQRES 1 A 272 MET VAL VAL ASN MET PHE GLU ASP ILE ASP THR PHE GLU
SEQRES 2 A 272 GLU ALA PHE ASN LYS LEU LEU ARG GLU VAL LEU GLU PHE
SEQRES 3 A 272 ASP LEU GLN ASN PRO PHE LYS ASP ALA LYS LYS VAL LEU
SEQRES 4 A 272 CYS ILE GLU PRO HIS PRO ASP ASP CYS VAL ILE GLY MET
SEQRES 5 A 272 GLY GLY THR ILE LYS LYS LEU SER ASP MET GLY VAL GLU
SEQRES 6 A 272 VAL ILE TYR VAL CYS MET THR ASP GLY TYR MET GLY THR
SEQRES 7 A 272 THR ASP GLU SER LEU SER GLY HIS GLU LEU ALA ALA ILE
SEQRES 8 A 272 ARG ARG LYS GLU GLU GLU GLU SER ALA ARG LEU LEU GLY
SEQRES 9 A 272 VAL LYS LYS ILE TYR TRP LEU ASN TYR ARG ASP THR GLU
SEQRES 10 A 272 LEU PRO TYR SER ARG GLU VAL ARG LYS ASP LEU THR LYS
SEQRES 11 A 272 ILE LEU ARG LYS GLU GLN PRO ASP GLY VAL PHE ALA PRO
SEQRES 12 A 272 ASP PRO TRP LEU PRO TYR GLU SER HIS PRO ASP HIS ARG
SEQRES 13 A 272 ARG THR GLY PHE LEU ALA ILE GLU SER VAL ALA PHE SER
SEQRES 14 A 272 GLN LEU PRO ASN PHE SER ASN THR ASP LEU ASP ILE GLY
SEQRES 15 A 272 LEU ASN PRO TYR ASN SER GLY SER PHE ILE ALA LEU TYR
SEQRES 16 A 272 TYR THR HIS LYS PRO ASN TYR ILE VAL ASP ILE THR ASP
SEQRES 17 A 272 LEU MET GLU LEU LYS LEU LYS ALA ILE ARG VAL HIS ARG
SEQRES 18 A 272 SER GLN PHE PRO ASP ASP ILE TRP GLU LYS TRP GLU PRO
SEQRES 19 A 272 PHE LEU ARG THR ILE ALA MET PHE TYR GLY GLU LYS ILE
SEQRES 20 A 272 GLY VAL ARG TYR GLY GLU GLY PHE ARG ILE MET PRO GLY
SEQRES 21 A 272 LEU PHE TYR HIS ILE THR PRO PHE THR ASP LEU ILE
SEQRES 1 B 272 MET VAL VAL ASN MET PHE GLU ASP ILE ASP THR PHE GLU
SEQRES 2 B 272 GLU ALA PHE ASN LYS LEU LEU ARG GLU VAL LEU GLU PHE
SEQRES 3 B 272 ASP LEU GLN ASN PRO PHE LYS ASP ALA LYS LYS VAL LEU
SEQRES 4 B 272 CYS ILE GLU PRO HIS PRO ASP ASP CYS VAL ILE GLY MET
SEQRES 5 B 272 GLY GLY THR ILE LYS LYS LEU SER ASP MET GLY VAL GLU
SEQRES 6 B 272 VAL ILE TYR VAL CYS MET THR ASP GLY TYR MET GLY THR
SEQRES 7 B 272 THR ASP GLU SER LEU SER GLY HIS GLU LEU ALA ALA ILE
SEQRES 8 B 272 ARG ARG LYS GLU GLU GLU GLU SER ALA ARG LEU LEU GLY
SEQRES 9 B 272 VAL LYS LYS ILE TYR TRP LEU ASN TYR ARG ASP THR GLU
SEQRES 10 B 272 LEU PRO TYR SER ARG GLU VAL ARG LYS ASP LEU THR LYS
SEQRES 11 B 272 ILE LEU ARG LYS GLU GLN PRO ASP GLY VAL PHE ALA PRO
SEQRES 12 B 272 ASP PRO TRP LEU PRO TYR GLU SER HIS PRO ASP HIS ARG
SEQRES 13 B 272 ARG THR GLY PHE LEU ALA ILE GLU SER VAL ALA PHE SER
SEQRES 14 B 272 GLN LEU PRO ASN PHE SER ASN THR ASP LEU ASP ILE GLY
SEQRES 15 B 272 LEU ASN PRO TYR ASN SER GLY SER PHE ILE ALA LEU TYR
SEQRES 16 B 272 TYR THR HIS LYS PRO ASN TYR ILE VAL ASP ILE THR ASP
SEQRES 17 B 272 LEU MET GLU LEU LYS LEU LYS ALA ILE ARG VAL HIS ARG
SEQRES 18 B 272 SER GLN PHE PRO ASP ASP ILE TRP GLU LYS TRP GLU PRO
SEQRES 19 B 272 PHE LEU ARG THR ILE ALA MET PHE TYR GLY GLU LYS ILE
SEQRES 20 B 272 GLY VAL ARG TYR GLY GLU GLY PHE ARG ILE MET PRO GLY
SEQRES 21 B 272 LEU PHE TYR HIS ILE THR PRO PHE THR ASP LEU ILE
SEQRES 1 C 272 MET VAL VAL ASN MET PHE GLU ASP ILE ASP THR PHE GLU
SEQRES 2 C 272 GLU ALA PHE ASN LYS LEU LEU ARG GLU VAL LEU GLU PHE
SEQRES 3 C 272 ASP LEU GLN ASN PRO PHE LYS ASP ALA LYS LYS VAL LEU
SEQRES 4 C 272 CYS ILE GLU PRO HIS PRO ASP ASP CYS VAL ILE GLY MET
SEQRES 5 C 272 GLY GLY THR ILE LYS LYS LEU SER ASP MET GLY VAL GLU
SEQRES 6 C 272 VAL ILE TYR VAL CYS MET THR ASP GLY TYR MET GLY THR
SEQRES 7 C 272 THR ASP GLU SER LEU SER GLY HIS GLU LEU ALA ALA ILE
SEQRES 8 C 272 ARG ARG LYS GLU GLU GLU GLU SER ALA ARG LEU LEU GLY
SEQRES 9 C 272 VAL LYS LYS ILE TYR TRP LEU ASN TYR ARG ASP THR GLU
SEQRES 10 C 272 LEU PRO TYR SER ARG GLU VAL ARG LYS ASP LEU THR LYS
SEQRES 11 C 272 ILE LEU ARG LYS GLU GLN PRO ASP GLY VAL PHE ALA PRO
SEQRES 12 C 272 ASP PRO TRP LEU PRO TYR GLU SER HIS PRO ASP HIS ARG
SEQRES 13 C 272 ARG THR GLY PHE LEU ALA ILE GLU SER VAL ALA PHE SER
SEQRES 14 C 272 GLN LEU PRO ASN PHE SER ASN THR ASP LEU ASP ILE GLY
SEQRES 15 C 272 LEU ASN PRO TYR ASN SER GLY SER PHE ILE ALA LEU TYR
SEQRES 16 C 272 TYR THR HIS LYS PRO ASN TYR ILE VAL ASP ILE THR ASP
SEQRES 17 C 272 LEU MET GLU LEU LYS LEU LYS ALA ILE ARG VAL HIS ARG
SEQRES 18 C 272 SER GLN PHE PRO ASP ASP ILE TRP GLU LYS TRP GLU PRO
SEQRES 19 C 272 PHE LEU ARG THR ILE ALA MET PHE TYR GLY GLU LYS ILE
SEQRES 20 C 272 GLY VAL ARG TYR GLY GLU GLY PHE ARG ILE MET PRO GLY
SEQRES 21 C 272 LEU PHE TYR HIS ILE THR PRO PHE THR ASP LEU ILE
HET ZN A 301 1
HET GOL A 302 6
HET ACY A 303 4
HET ZN B 301 1
HET GOL B 302 6
HET GOL B 303 18
HET ACY B 304 4
HET NA B 305 1
HET HEZ B 306 8
HET HEZ B 307 8
HET ZN C 301 1
HET ACY C 302 4
HET GOL C 303 6
HET NA C 304 1
HET HEZ C 305 8
HET HEZ C 306 8
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM ACY ACETIC ACID
HETNAM NA SODIUM ION
HETNAM HEZ HEXANE-1,6-DIOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 6 ACY 3(C2 H4 O2)
FORMUL 11 NA 2(NA 1+)
FORMUL 12 HEZ 4(C6 H14 O2)
FORMUL 20 HOH *547(H2 O)
HELIX 1 1 THR A 11 GLU A 22 1 12
HELIX 2 2 ASP A 46 MET A 62 1 17
HELIX 3 3 SER A 84 LEU A 103 1 20
HELIX 4 4 SER A 121 GLN A 136 1 16
HELIX 5 5 HIS A 152 SER A 169 1 18
HELIX 6 6 ASN A 176 ILE A 181 1 6
HELIX 7 7 LEU A 209 VAL A 219 1 11
HELIX 8 8 PRO A 225 LYS A 246 1 22
HELIX 9 9 PRO A 259 HIS A 264 5 6
HELIX 10 10 PHE A 268 ILE A 272 5 5
HELIX 11 11 THR B 11 GLU B 22 1 12
HELIX 12 12 ASP B 46 MET B 62 1 17
HELIX 13 13 SER B 84 LEU B 103 1 20
HELIX 14 14 SER B 121 GLN B 136 1 16
HELIX 15 15 HIS B 152 SER B 169 1 18
HELIX 16 16 ASN B 176 ILE B 181 1 6
HELIX 17 17 LEU B 209 VAL B 219 1 11
HELIX 18 18 HIS B 220 PHE B 224 5 5
HELIX 19 19 PRO B 225 LYS B 246 1 22
HELIX 20 20 PRO B 259 HIS B 264 5 6
HELIX 21 21 PHE B 268 ILE B 272 5 5
HELIX 22 22 THR C 11 GLU C 22 1 12
HELIX 23 23 ASP C 46 MET C 62 1 17
HELIX 24 24 SER C 84 LEU C 103 1 20
HELIX 25 25 SER C 121 GLN C 136 1 16
HELIX 26 26 HIS C 152 SER C 169 1 18
HELIX 27 27 ASN C 176 ILE C 181 1 6
HELIX 28 28 LEU C 209 VAL C 219 1 11
HELIX 29 29 PRO C 225 LYS C 246 1 22
HELIX 30 30 PRO C 259 HIS C 264 5 6
HELIX 31 31 PHE C 268 ILE C 272 5 5
SHEET 1 A 5 LYS A 107 TYR A 113 0
SHEET 2 A 5 GLU A 65 THR A 72 1 N CYS A 70 O TYR A 109
SHEET 3 A 5 LYS A 37 GLU A 42 1 N CYS A 40 O VAL A 69
SHEET 4 A 5 GLY A 139 PRO A 143 1 O PHE A 141 N LEU A 39
SHEET 5 A 5 PHE A 191 TYR A 195 1 O ALA A 193 N VAL A 140
SHEET 1 B 2 TYR A 202 ASP A 205 0
SHEET 2 B 2 GLY A 252 PHE A 255 -1 O GLU A 253 N VAL A 204
SHEET 1 C 5 LYS B 107 TYR B 113 0
SHEET 2 C 5 GLU B 65 THR B 72 1 N CYS B 70 O LEU B 111
SHEET 3 C 5 LYS B 37 GLU B 42 1 N GLU B 42 O MET B 71
SHEET 4 C 5 GLY B 139 PRO B 143 1 O PHE B 141 N ILE B 41
SHEET 5 C 5 PHE B 191 TYR B 195 1 O ALA B 193 N VAL B 140
SHEET 1 D 2 TYR B 202 ASP B 205 0
SHEET 2 D 2 GLY B 252 PHE B 255 -1 O PHE B 255 N TYR B 202
SHEET 1 E 5 LYS C 107 TYR C 113 0
SHEET 2 E 5 GLU C 65 THR C 72 1 N CYS C 70 O TYR C 109
SHEET 3 E 5 LYS C 37 GLU C 42 1 N GLU C 42 O VAL C 69
SHEET 4 E 5 GLY C 139 PRO C 143 1 O PHE C 141 N ILE C 41
SHEET 5 E 5 PHE C 191 TYR C 195 1 O ALA C 193 N VAL C 140
SHEET 1 F 2 TYR C 202 ASP C 205 0
SHEET 2 F 2 GLY C 252 PHE C 255 -1 O GLU C 253 N VAL C 204
SSBOND 1 CYS A 40 CYS A 48 1555 1555 2.11
SSBOND 2 CYS B 40 CYS B 48 1555 1555 2.09
SSBOND 3 CYS C 40 CYS C 48 1555 1555 2.10
LINK ZN ZN A 301 OXT ACY A 303 1555 1555 1.88
LINK ZN ZN C 301 OXT ACY C 302 1555 1555 1.90
LINK ZN ZN B 301 OXT ACY B 304 1555 1555 1.95
LINK OD2 ASP C 47 ZN ZN C 301 1555 1555 1.98
LINK OD2 ASP B 47 ZN ZN B 301 1555 1555 1.99
LINK NE2 HIS B 155 ZN ZN B 301 1555 1555 2.02
LINK NE2 HIS C 155 ZN ZN C 301 1555 1555 2.04
LINK ND1 HIS C 44 ZN ZN C 301 1555 1555 2.06
LINK ND1 HIS B 44 ZN ZN B 301 1555 1555 2.07
LINK ND1 HIS A 44 ZN ZN A 301 1555 1555 2.07
LINK NE2 HIS A 155 ZN ZN A 301 1555 1555 2.09
LINK OD2 ASP A 47 ZN ZN A 301 1555 1555 2.12
LINK OD1 ASP C 138 NA NA C 304 1555 1555 2.16
LINK OD1 ASP B 138 NA NA B 305 1555 1555 2.17
LINK ZN ZN B 301 O ACY B 304 1555 1555 2.43
LINK ZN ZN C 301 O ACY C 302 1555 1555 2.45
LINK ZN ZN A 301 O ACY A 303 1555 1555 2.53
LINK NA NA C 304 O HOH C 567 1555 1555 2.12
LINK NA NA C 304 O HOH C 564 1555 1555 2.15
LINK NA NA C 304 O HOH C 565 1555 1555 2.43
SITE 1 AC1 4 HIS A 44 ASP A 47 HIS A 155 ACY A 303
SITE 1 AC2 7 HIS A 44 MET A 76 GLY A 77 ARG A 92
SITE 2 AC2 7 ASP A 115 HIS A 152 ACY A 303
SITE 1 AC3 7 HIS A 44 ASP A 46 ASP A 47 HIS A 155
SITE 2 AC3 7 ZN A 301 GOL A 302 HIS B 264
SITE 1 AC4 4 HIS B 44 ASP B 47 HIS B 155 ACY B 304
SITE 1 AC5 8 HIS B 44 GLY B 74 GLY B 77 ARG B 92
SITE 2 AC5 8 ASP B 115 HIS B 152 ACY B 304 HOH B 534
SITE 1 AC6 8 TYR A 120 ARG A 157 TYR B 120 ARG B 157
SITE 2 AC6 8 HOH B 459 HOH B 498 HOH B 574 ARG C 157
SITE 1 AC7 7 HIS B 44 ASP B 46 ASP B 47 HIS B 155
SITE 2 AC7 7 ZN B 301 GOL B 302 HIS C 264
SITE 1 AC8 1 ASP B 138
SITE 1 AC9 6 SER B 151 HIS B 152 HOH B 566 ALA C 167
SITE 2 AC9 6 ILE C 192 TYR C 263
SITE 1 BC1 5 ALA B 167 ILE B 192 TYR B 263 HOH B 444
SITE 2 BC1 5 HOH B 474
SITE 1 BC2 4 HIS C 44 ASP C 47 HIS C 155 ACY C 302
SITE 1 BC3 7 HIS A 264 HIS C 44 ASP C 46 ASP C 47
SITE 2 BC3 7 HIS C 155 ZN C 301 GOL C 303
SITE 1 BC4 8 HIS C 44 MET C 76 GLY C 77 ARG C 92
SITE 2 BC4 8 ASP C 115 HIS C 152 ACY C 302 HOH C 457
SITE 1 BC5 5 ASP C 138 HOH C 564 HOH C 565 HOH C 566
SITE 2 BC5 5 HOH C 567
SITE 1 BC6 6 GLU C 97 VAL C 105 LYS C 107 ILE C 108
SITE 2 BC6 6 HOH C 441 HOH C 476
SITE 1 BC7 3 PHE C 32 LYS C 33 MET C 62
CRYST1 77.372 77.372 230.223 90.00 90.00 120.00 P 32 2 1 18
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 0.012925 0.007462 0.000000 0.00000
SCALE2 0.000000 0.014924 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004344 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
