HEADER HYDROLASE 04-DEC-06 2O4Q
TITLE STRUCTURE OF PHOSPHOTRIESTERASE MUTANT G60A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PARATHION HYDROLASE;
COMPND 3 CHAIN: A, B, K, P;
COMPND 4 FRAGMENT: RESIDUES 34-364;
COMPND 5 SYNONYM: PHOSPHOTRIESTERASE, PTE;
COMPND 6 EC: 3.1.8.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BREVUNDIMONAS DIMINUTA;
SOURCE 3 ORGANISM_TAXID: 293;
SOURCE 4 GENE: OPD;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS METALLOENZYME, TIM BARREL, NERVE AGENTS, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KIM,U.A.RAMAGOPAL,P.C.TSAI,F.M.RAUSHEL,S.C.ALMO
REVDAT 9 15-NOV-23 2O4Q 1 REMARK
REVDAT 8 30-AUG-23 2O4Q 1 REMARK
REVDAT 7 20-OCT-21 2O4Q 1 REMARK SEQADV LINK
REVDAT 6 18-OCT-17 2O4Q 1 REMARK
REVDAT 5 13-JUL-11 2O4Q 1 VERSN
REVDAT 4 23-JUN-09 2O4Q 1 HET HETATM HETNAM
REVDAT 3 24-FEB-09 2O4Q 1 VERSN
REVDAT 2 14-OCT-08 2O4Q 1 JRNL
REVDAT 1 18-DEC-07 2O4Q 0
JRNL AUTH J.KIM,P.C.TSAI,S.L.CHEN,F.HIMO,S.C.ALMO,F.M.RAUSHEL
JRNL TITL STRUCTURE OF DIETHYL PHOSPHATE BOUND TO THE BINUCLEAR METAL
JRNL TITL 2 CENTER OF PHOSPHOTRIESTERASE.
JRNL REF BIOCHEMISTRY V. 47 9497 2008
JRNL REFN ISSN 0006-2960
JRNL PMID 18702530
JRNL DOI 10.1021/BI800971V
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 3 NUMBER OF REFLECTIONS : 91514
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4597
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5644
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.18
REMARK 3 BIN R VALUE (WORKING SET) : 0.1790
REMARK 3 BIN FREE R VALUE SET COUNT : 291
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10110
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 28
REMARK 3 SOLVENT ATOMS : 1026
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.74
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.94000
REMARK 3 B22 (A**2) : -0.90000
REMARK 3 B33 (A**2) : -0.95000
REMARK 3 B12 (A**2) : 0.03000
REMARK 3 B13 (A**2) : 0.25000
REMARK 3 B23 (A**2) : -0.60000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.170
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.106
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.626
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10377 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14109 ; 1.424 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1334 ; 7.409 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 433 ;33.183 ;22.333
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1677 ;15.812 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 104 ;19.103 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1646 ; 0.120 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7840 ; 0.017 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5387 ; 0.219 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7286 ; 0.316 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1001 ; 0.153 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 10 ; 0.047 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 66 ; 0.208 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 27 ; 0.154 ; 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): 6774 ; 1.825 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10637 ; 2.503 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4018 ; 4.145 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3472 ; 5.978 ; 4.500
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2O4Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-DEC-06.
REMARK 100 THE DEPOSITION ID IS D_1000040684.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97904
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91515
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 31.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : 0.24200
REMARK 200 R SYM FOR SHELL (I) : 0.28600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.390
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: PDB ENTRY 1P6B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M MG ACETATE, 0.1M NA-CACODYLATE,
REMARK 280 20% PEG 8000, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23170 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 3650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23190 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -161.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, P
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 364
REMARK 465 ALA P 364
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 356 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG K 89 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG K 225 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG K 225 NE - CZ - NH2 ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 61 -142.29 -141.16
REMARK 500 TRP A 69 57.94 -150.58
REMARK 500 THR A 128 -168.66 -110.16
REMARK 500 TRP A 131 -151.19 -100.19
REMARK 500 GLU A 159 -130.99 56.45
REMARK 500 ALA A 259 52.71 -66.38
REMARK 500 LEU A 262 20.48 -155.27
REMARK 500 LEU A 272 -71.21 -94.60
REMARK 500 PHE A 306 83.35 -153.65
REMARK 500 SER B 61 -138.76 -143.91
REMARK 500 VAL B 101 31.84 -96.84
REMARK 500 ARG B 108 127.88 -36.79
REMARK 500 THR B 128 -167.20 -113.42
REMARK 500 TRP B 131 -158.19 -99.47
REMARK 500 GLU B 159 -125.37 50.04
REMARK 500 ASP B 236 81.12 -69.12
REMARK 500 SER B 308 31.10 -95.72
REMARK 500 VAL B 351 -51.60 -120.08
REMARK 500 SER K 61 -147.35 -140.72
REMARK 500 TRP K 69 57.03 -145.80
REMARK 500 THR K 128 -168.02 -113.01
REMARK 500 TRP K 131 -149.76 -102.19
REMARK 500 GLU K 159 -128.31 57.44
REMARK 500 ASP K 236 86.98 -67.72
REMARK 500 ALA K 259 64.35 -62.16
REMARK 500 LEU K 262 37.09 -146.91
REMARK 500 LEU K 272 -78.36 -88.52
REMARK 500 PHE K 306 83.47 -152.25
REMARK 500 GLN K 343 -54.42 -25.30
REMARK 500 SER P 61 -143.71 -141.14
REMARK 500 TRP P 69 59.96 -145.68
REMARK 500 VAL P 101 30.73 -94.00
REMARK 500 ARG P 108 126.58 -37.89
REMARK 500 THR P 128 -166.24 -117.48
REMARK 500 TRP P 131 -155.52 -100.43
REMARK 500 GLU P 159 -125.32 48.26
REMARK 500 PHE P 306 88.05 -154.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 THR A 202 ALA A 203 146.64
REMARK 500 ARG A 363 ALA A 364 147.16
REMARK 500 THR B 202 ALA B 203 146.36
REMARK 500 THR K 202 ALA K 203 147.88
REMARK 500 THR P 202 ALA P 203 147.88
REMARK 500 LEU P 362 ARG P 363 149.32
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 A2401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC A 1 O1
REMARK 620 2 HIS A 55 NE2 138.5
REMARK 620 3 HIS A 57 NE2 103.7 117.6
REMARK 620 4 KCX A 169 OQ1 94.5 91.3 87.4
REMARK 620 5 ASP A 301 OD1 85.9 86.3 95.6 176.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A2402 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC A 1 O2
REMARK 620 2 KCX A 169 OQ2 104.7
REMARK 620 3 HIS A 201 ND1 100.4 108.3
REMARK 620 4 HIS A 230 NE2 140.1 105.9 93.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2403 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC B 2 O2
REMARK 620 2 HIS B 55 NE2 137.1
REMARK 620 3 HIS B 57 NE2 104.7 117.6
REMARK 620 4 KCX B 169 OQ2 96.2 92.1 88.5
REMARK 620 5 ASP B 301 OD1 86.7 84.7 92.3 176.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2404 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC B 2 O1
REMARK 620 2 KCX B 169 OQ1 105.0
REMARK 620 3 HIS B 201 ND1 95.5 107.8
REMARK 620 4 HIS B 230 NE2 144.8 102.4 96.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K2405 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC K 3 O2
REMARK 620 2 HIS K 55 NE2 137.4
REMARK 620 3 HIS K 57 NE2 105.4 116.9
REMARK 620 4 KCX K 169 OQ1 92.5 91.5 90.4
REMARK 620 5 ASP K 301 OD1 88.1 84.3 94.8 174.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN K2406 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC K 3 O1
REMARK 620 2 KCX K 169 OQ2 105.7
REMARK 620 3 HIS K 201 ND1 98.7 106.1
REMARK 620 4 HIS K 230 NE2 138.0 105.9 98.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN P2407 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC P 4 O2
REMARK 620 2 HIS P 55 NE2 134.3
REMARK 620 3 HIS P 57 NE2 105.8 119.9
REMARK 620 4 KCX P 169 OQ2 91.8 94.1 84.7
REMARK 620 5 ASP P 301 OD1 90.1 82.7 97.3 176.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN P2408 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CAC P 4 O1
REMARK 620 2 KCX P 169 OQ1 104.9
REMARK 620 3 HIS P 201 ND1 93.4 106.8
REMARK 620 4 HIS P 230 NE2 147.8 101.8 95.8
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 2401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 2405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 2406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC K 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 2407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 2408
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC P 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2O4M RELATED DB: PDB
REMARK 900 STRUCTURE OF PHOSPHOTRIESTERASE MUTANT I106G/F132G/H257Y
DBREF 2O4Q A 34 364 UNP P0A434 OPD_BREDI 34 364
DBREF 2O4Q B 34 364 UNP P0A434 OPD_BREDI 34 364
DBREF 2O4Q K 34 364 UNP P0A434 OPD_BREDI 34 364
DBREF 2O4Q P 34 364 UNP P0A434 OPD_BREDI 34 364
SEQADV 2O4Q ALA A 60 UNP P0A434 GLY 60 ENGINEERED MUTATION
SEQADV 2O4Q ALA B 60 UNP P0A434 GLY 60 ENGINEERED MUTATION
SEQADV 2O4Q ALA K 60 UNP P0A434 GLY 60 ENGINEERED MUTATION
SEQADV 2O4Q ALA P 60 UNP P0A434 GLY 60 ENGINEERED MUTATION
SEQRES 1 A 331 GLY ASP ARG ILE ASN THR VAL ARG GLY PRO ILE THR ILE
SEQRES 2 A 331 SER GLU ALA GLY PHE THR LEU THR HIS GLU HIS ILE CYS
SEQRES 3 A 331 ALA SER SER ALA GLY PHE LEU ARG ALA TRP PRO GLU PHE
SEQRES 4 A 331 PHE GLY SER ARG LYS ALA LEU ALA GLU LYS ALA VAL ARG
SEQRES 5 A 331 GLY LEU ARG ARG ALA ARG ALA ALA GLY VAL ARG THR ILE
SEQRES 6 A 331 VAL ASP VAL SER THR PHE ASP ILE GLY ARG ASP VAL SER
SEQRES 7 A 331 LEU LEU ALA GLU VAL SER ARG ALA ALA ASP VAL HIS ILE
SEQRES 8 A 331 VAL ALA ALA THR GLY LEU TRP PHE ASP PRO PRO LEU SER
SEQRES 9 A 331 MET ARG LEU ARG SER VAL GLU GLU LEU THR GLN PHE PHE
SEQRES 10 A 331 LEU ARG GLU ILE GLN TYR GLY ILE GLU ASP THR GLY ILE
SEQRES 11 A 331 ARG ALA GLY ILE ILE KCX VAL ALA THR THR GLY LYS ALA
SEQRES 12 A 331 THR PRO PHE GLN GLU LEU VAL LEU LYS ALA ALA ALA ARG
SEQRES 13 A 331 ALA SER LEU ALA THR GLY VAL PRO VAL THR THR HIS THR
SEQRES 14 A 331 ALA ALA SER GLN ARG ASP GLY GLU GLN GLN ALA ALA ILE
SEQRES 15 A 331 PHE GLU SER GLU GLY LEU SER PRO SER ARG VAL CYS ILE
SEQRES 16 A 331 GLY HIS SER ASP ASP THR ASP ASP LEU SER TYR LEU THR
SEQRES 17 A 331 ALA LEU ALA ALA ARG GLY TYR LEU ILE GLY LEU ASP HIS
SEQRES 18 A 331 ILE PRO HIS SER ALA ILE GLY LEU GLU ASP ASN ALA SER
SEQRES 19 A 331 ALA SER ALA LEU LEU GLY ILE ARG SER TRP GLN THR ARG
SEQRES 20 A 331 ALA LEU LEU ILE LYS ALA LEU ILE ASP GLN GLY TYR MET
SEQRES 21 A 331 LYS GLN ILE LEU VAL SER ASN ASP TRP LEU PHE GLY PHE
SEQRES 22 A 331 SER SER TYR VAL THR ASN ILE MET ASP VAL MET ASP ARG
SEQRES 23 A 331 VAL ASN PRO ASP GLY MET ALA PHE ILE PRO LEU ARG VAL
SEQRES 24 A 331 ILE PRO PHE LEU ARG GLU LYS GLY VAL PRO GLN GLU THR
SEQRES 25 A 331 LEU ALA GLY ILE THR VAL THR ASN PRO ALA ARG PHE LEU
SEQRES 26 A 331 SER PRO THR LEU ARG ALA
SEQRES 1 B 331 GLY ASP ARG ILE ASN THR VAL ARG GLY PRO ILE THR ILE
SEQRES 2 B 331 SER GLU ALA GLY PHE THR LEU THR HIS GLU HIS ILE CYS
SEQRES 3 B 331 ALA SER SER ALA GLY PHE LEU ARG ALA TRP PRO GLU PHE
SEQRES 4 B 331 PHE GLY SER ARG LYS ALA LEU ALA GLU LYS ALA VAL ARG
SEQRES 5 B 331 GLY LEU ARG ARG ALA ARG ALA ALA GLY VAL ARG THR ILE
SEQRES 6 B 331 VAL ASP VAL SER THR PHE ASP ILE GLY ARG ASP VAL SER
SEQRES 7 B 331 LEU LEU ALA GLU VAL SER ARG ALA ALA ASP VAL HIS ILE
SEQRES 8 B 331 VAL ALA ALA THR GLY LEU TRP PHE ASP PRO PRO LEU SER
SEQRES 9 B 331 MET ARG LEU ARG SER VAL GLU GLU LEU THR GLN PHE PHE
SEQRES 10 B 331 LEU ARG GLU ILE GLN TYR GLY ILE GLU ASP THR GLY ILE
SEQRES 11 B 331 ARG ALA GLY ILE ILE KCX VAL ALA THR THR GLY LYS ALA
SEQRES 12 B 331 THR PRO PHE GLN GLU LEU VAL LEU LYS ALA ALA ALA ARG
SEQRES 13 B 331 ALA SER LEU ALA THR GLY VAL PRO VAL THR THR HIS THR
SEQRES 14 B 331 ALA ALA SER GLN ARG ASP GLY GLU GLN GLN ALA ALA ILE
SEQRES 15 B 331 PHE GLU SER GLU GLY LEU SER PRO SER ARG VAL CYS ILE
SEQRES 16 B 331 GLY HIS SER ASP ASP THR ASP ASP LEU SER TYR LEU THR
SEQRES 17 B 331 ALA LEU ALA ALA ARG GLY TYR LEU ILE GLY LEU ASP HIS
SEQRES 18 B 331 ILE PRO HIS SER ALA ILE GLY LEU GLU ASP ASN ALA SER
SEQRES 19 B 331 ALA SER ALA LEU LEU GLY ILE ARG SER TRP GLN THR ARG
SEQRES 20 B 331 ALA LEU LEU ILE LYS ALA LEU ILE ASP GLN GLY TYR MET
SEQRES 21 B 331 LYS GLN ILE LEU VAL SER ASN ASP TRP LEU PHE GLY PHE
SEQRES 22 B 331 SER SER TYR VAL THR ASN ILE MET ASP VAL MET ASP ARG
SEQRES 23 B 331 VAL ASN PRO ASP GLY MET ALA PHE ILE PRO LEU ARG VAL
SEQRES 24 B 331 ILE PRO PHE LEU ARG GLU LYS GLY VAL PRO GLN GLU THR
SEQRES 25 B 331 LEU ALA GLY ILE THR VAL THR ASN PRO ALA ARG PHE LEU
SEQRES 26 B 331 SER PRO THR LEU ARG ALA
SEQRES 1 K 331 GLY ASP ARG ILE ASN THR VAL ARG GLY PRO ILE THR ILE
SEQRES 2 K 331 SER GLU ALA GLY PHE THR LEU THR HIS GLU HIS ILE CYS
SEQRES 3 K 331 ALA SER SER ALA GLY PHE LEU ARG ALA TRP PRO GLU PHE
SEQRES 4 K 331 PHE GLY SER ARG LYS ALA LEU ALA GLU LYS ALA VAL ARG
SEQRES 5 K 331 GLY LEU ARG ARG ALA ARG ALA ALA GLY VAL ARG THR ILE
SEQRES 6 K 331 VAL ASP VAL SER THR PHE ASP ILE GLY ARG ASP VAL SER
SEQRES 7 K 331 LEU LEU ALA GLU VAL SER ARG ALA ALA ASP VAL HIS ILE
SEQRES 8 K 331 VAL ALA ALA THR GLY LEU TRP PHE ASP PRO PRO LEU SER
SEQRES 9 K 331 MET ARG LEU ARG SER VAL GLU GLU LEU THR GLN PHE PHE
SEQRES 10 K 331 LEU ARG GLU ILE GLN TYR GLY ILE GLU ASP THR GLY ILE
SEQRES 11 K 331 ARG ALA GLY ILE ILE KCX VAL ALA THR THR GLY LYS ALA
SEQRES 12 K 331 THR PRO PHE GLN GLU LEU VAL LEU LYS ALA ALA ALA ARG
SEQRES 13 K 331 ALA SER LEU ALA THR GLY VAL PRO VAL THR THR HIS THR
SEQRES 14 K 331 ALA ALA SER GLN ARG ASP GLY GLU GLN GLN ALA ALA ILE
SEQRES 15 K 331 PHE GLU SER GLU GLY LEU SER PRO SER ARG VAL CYS ILE
SEQRES 16 K 331 GLY HIS SER ASP ASP THR ASP ASP LEU SER TYR LEU THR
SEQRES 17 K 331 ALA LEU ALA ALA ARG GLY TYR LEU ILE GLY LEU ASP HIS
SEQRES 18 K 331 ILE PRO HIS SER ALA ILE GLY LEU GLU ASP ASN ALA SER
SEQRES 19 K 331 ALA SER ALA LEU LEU GLY ILE ARG SER TRP GLN THR ARG
SEQRES 20 K 331 ALA LEU LEU ILE LYS ALA LEU ILE ASP GLN GLY TYR MET
SEQRES 21 K 331 LYS GLN ILE LEU VAL SER ASN ASP TRP LEU PHE GLY PHE
SEQRES 22 K 331 SER SER TYR VAL THR ASN ILE MET ASP VAL MET ASP ARG
SEQRES 23 K 331 VAL ASN PRO ASP GLY MET ALA PHE ILE PRO LEU ARG VAL
SEQRES 24 K 331 ILE PRO PHE LEU ARG GLU LYS GLY VAL PRO GLN GLU THR
SEQRES 25 K 331 LEU ALA GLY ILE THR VAL THR ASN PRO ALA ARG PHE LEU
SEQRES 26 K 331 SER PRO THR LEU ARG ALA
SEQRES 1 P 331 GLY ASP ARG ILE ASN THR VAL ARG GLY PRO ILE THR ILE
SEQRES 2 P 331 SER GLU ALA GLY PHE THR LEU THR HIS GLU HIS ILE CYS
SEQRES 3 P 331 ALA SER SER ALA GLY PHE LEU ARG ALA TRP PRO GLU PHE
SEQRES 4 P 331 PHE GLY SER ARG LYS ALA LEU ALA GLU LYS ALA VAL ARG
SEQRES 5 P 331 GLY LEU ARG ARG ALA ARG ALA ALA GLY VAL ARG THR ILE
SEQRES 6 P 331 VAL ASP VAL SER THR PHE ASP ILE GLY ARG ASP VAL SER
SEQRES 7 P 331 LEU LEU ALA GLU VAL SER ARG ALA ALA ASP VAL HIS ILE
SEQRES 8 P 331 VAL ALA ALA THR GLY LEU TRP PHE ASP PRO PRO LEU SER
SEQRES 9 P 331 MET ARG LEU ARG SER VAL GLU GLU LEU THR GLN PHE PHE
SEQRES 10 P 331 LEU ARG GLU ILE GLN TYR GLY ILE GLU ASP THR GLY ILE
SEQRES 11 P 331 ARG ALA GLY ILE ILE KCX VAL ALA THR THR GLY LYS ALA
SEQRES 12 P 331 THR PRO PHE GLN GLU LEU VAL LEU LYS ALA ALA ALA ARG
SEQRES 13 P 331 ALA SER LEU ALA THR GLY VAL PRO VAL THR THR HIS THR
SEQRES 14 P 331 ALA ALA SER GLN ARG ASP GLY GLU GLN GLN ALA ALA ILE
SEQRES 15 P 331 PHE GLU SER GLU GLY LEU SER PRO SER ARG VAL CYS ILE
SEQRES 16 P 331 GLY HIS SER ASP ASP THR ASP ASP LEU SER TYR LEU THR
SEQRES 17 P 331 ALA LEU ALA ALA ARG GLY TYR LEU ILE GLY LEU ASP HIS
SEQRES 18 P 331 ILE PRO HIS SER ALA ILE GLY LEU GLU ASP ASN ALA SER
SEQRES 19 P 331 ALA SER ALA LEU LEU GLY ILE ARG SER TRP GLN THR ARG
SEQRES 20 P 331 ALA LEU LEU ILE LYS ALA LEU ILE ASP GLN GLY TYR MET
SEQRES 21 P 331 LYS GLN ILE LEU VAL SER ASN ASP TRP LEU PHE GLY PHE
SEQRES 22 P 331 SER SER TYR VAL THR ASN ILE MET ASP VAL MET ASP ARG
SEQRES 23 P 331 VAL ASN PRO ASP GLY MET ALA PHE ILE PRO LEU ARG VAL
SEQRES 24 P 331 ILE PRO PHE LEU ARG GLU LYS GLY VAL PRO GLN GLU THR
SEQRES 25 P 331 LEU ALA GLY ILE THR VAL THR ASN PRO ALA ARG PHE LEU
SEQRES 26 P 331 SER PRO THR LEU ARG ALA
MODRES 2O4Q KCX A 169 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2O4Q KCX B 169 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2O4Q KCX K 169 LYS LYSINE NZ-CARBOXYLIC ACID
MODRES 2O4Q KCX P 169 LYS LYSINE NZ-CARBOXYLIC ACID
HET KCX A 169 12
HET KCX B 169 12
HET KCX K 169 12
HET KCX P 169 12
HET ZN A2401 1
HET ZN A2402 1
HET CAC A 1 5
HET ZN B2403 1
HET ZN B2404 1
HET CAC B 2 5
HET ZN K2405 1
HET ZN K2406 1
HET CAC K 3 5
HET ZN P2407 1
HET ZN P2408 1
HET CAC P 4 5
HETNAM KCX LYSINE NZ-CARBOXYLIC ACID
HETNAM ZN ZINC ION
HETNAM CAC CACODYLATE ION
HETSYN CAC DIMETHYLARSINATE
FORMUL 1 KCX 4(C7 H14 N2 O4)
FORMUL 5 ZN 8(ZN 2+)
FORMUL 7 CAC 4(C2 H6 AS O2 1-)
FORMUL 17 HOH *1026(H2 O)
HELIX 1 1 ILE A 46 GLY A 50 1 5
HELIX 2 2 GLY A 64 TRP A 69 1 6
HELIX 3 3 PRO A 70 GLY A 74 5 5
HELIX 4 4 SER A 75 ALA A 93 1 19
HELIX 5 5 THR A 103 GLY A 107 5 5
HELIX 6 6 ASP A 109 ASP A 121 1 13
HELIX 7 7 PRO A 135 LEU A 140 1 6
HELIX 8 8 SER A 142 TYR A 156 1 15
HELIX 9 9 THR A 177 GLY A 195 1 19
HELIX 10 10 ALA A 203 GLN A 206 5 4
HELIX 11 11 ARG A 207 GLU A 219 1 13
HELIX 12 12 SER A 222 SER A 224 5 3
HELIX 13 13 HIS A 230 THR A 234 5 5
HELIX 14 14 ASP A 236 GLY A 247 1 12
HELIX 15 15 ASN A 265 LEU A 272 1 8
HELIX 16 16 SER A 276 GLN A 290 1 15
HELIX 17 17 TYR A 292 LYS A 294 5 3
HELIX 18 18 ASN A 312 ASN A 321 1 10
HELIX 19 19 ASP A 323 MET A 325 5 3
HELIX 20 20 ALA A 326 ARG A 331 1 6
HELIX 21 21 ARG A 331 LYS A 339 1 9
HELIX 22 22 PRO A 342 VAL A 351 1 10
HELIX 23 23 VAL A 351 SER A 359 1 9
HELIX 24 24 ILE B 46 GLY B 50 1 5
HELIX 25 25 GLY B 64 TRP B 69 1 6
HELIX 26 26 PRO B 70 GLY B 74 5 5
HELIX 27 27 SER B 75 ALA B 93 1 19
HELIX 28 28 THR B 103 GLY B 107 5 5
HELIX 29 29 ASP B 109 ASP B 121 1 13
HELIX 30 30 PRO B 135 LEU B 140 1 6
HELIX 31 31 SER B 142 TYR B 156 1 15
HELIX 32 32 THR B 177 GLY B 195 1 19
HELIX 33 33 ALA B 203 GLN B 206 5 4
HELIX 34 34 ARG B 207 GLU B 219 1 13
HELIX 35 35 SER B 222 SER B 224 5 3
HELIX 36 36 HIS B 230 THR B 234 5 5
HELIX 37 37 ASP B 236 ARG B 246 1 11
HELIX 38 38 ASN B 265 GLY B 273 1 9
HELIX 39 39 SER B 276 GLN B 290 1 15
HELIX 40 40 TYR B 292 LYS B 294 5 3
HELIX 41 41 ASN B 312 ASN B 321 1 10
HELIX 42 42 ASP B 323 MET B 325 5 3
HELIX 43 43 ALA B 326 ARG B 331 1 6
HELIX 44 44 ARG B 331 LYS B 339 1 9
HELIX 45 45 PRO B 342 VAL B 351 1 10
HELIX 46 46 VAL B 351 SER B 359 1 9
HELIX 47 47 ILE K 46 GLY K 50 1 5
HELIX 48 48 GLY K 64 TRP K 69 1 6
HELIX 49 49 PRO K 70 GLY K 74 5 5
HELIX 50 50 SER K 75 ALA K 93 1 19
HELIX 51 51 THR K 103 GLY K 107 5 5
HELIX 52 52 ASP K 109 ASP K 121 1 13
HELIX 53 53 PRO K 135 LEU K 140 1 6
HELIX 54 54 SER K 142 TYR K 156 1 15
HELIX 55 55 THR K 177 GLY K 195 1 19
HELIX 56 56 ALA K 203 GLN K 206 5 4
HELIX 57 57 ARG K 207 GLU K 219 1 13
HELIX 58 58 SER K 222 SER K 224 5 3
HELIX 59 59 HIS K 230 THR K 234 5 5
HELIX 60 60 ASP K 236 GLY K 247 1 12
HELIX 61 61 ASN K 265 LEU K 272 1 8
HELIX 62 62 SER K 276 GLN K 290 1 15
HELIX 63 63 TYR K 292 LYS K 294 5 3
HELIX 64 64 ASN K 312 ASN K 321 1 10
HELIX 65 65 ASP K 323 MET K 325 5 3
HELIX 66 66 ALA K 326 ARG K 331 1 6
HELIX 67 67 ARG K 331 LYS K 339 1 9
HELIX 68 68 PRO K 342 VAL K 351 1 10
HELIX 69 69 VAL K 351 SER K 359 1 9
HELIX 70 70 SER P 47 ALA P 49 5 3
HELIX 71 71 GLY P 64 TRP P 69 1 6
HELIX 72 72 PRO P 70 GLY P 74 5 5
HELIX 73 73 SER P 75 ALA P 93 1 19
HELIX 74 74 THR P 103 GLY P 107 5 5
HELIX 75 75 ASP P 109 ASP P 121 1 13
HELIX 76 76 PRO P 135 LEU P 140 1 6
HELIX 77 77 SER P 142 TYR P 156 1 15
HELIX 78 78 THR P 177 GLY P 195 1 19
HELIX 79 79 ALA P 203 GLN P 206 5 4
HELIX 80 80 ARG P 207 GLU P 219 1 13
HELIX 81 81 SER P 222 SER P 224 5 3
HELIX 82 82 HIS P 230 THR P 234 5 5
HELIX 83 83 ASP P 236 GLY P 247 1 12
HELIX 84 84 ASN P 265 GLY P 273 1 9
HELIX 85 85 SER P 276 GLN P 290 1 15
HELIX 86 86 GLY P 291 LYS P 294 5 4
HELIX 87 87 ASN P 312 ASN P 321 1 10
HELIX 88 88 ASP P 323 MET P 325 5 3
HELIX 89 89 ALA P 326 ARG P 331 1 6
HELIX 90 90 ARG P 331 LYS P 339 1 9
HELIX 91 91 PRO P 342 VAL P 351 1 10
HELIX 92 92 VAL P 351 SER P 359 1 9
SHEET 1 A 2 ARG A 36 THR A 39 0
SHEET 2 A 2 GLY A 42 THR A 45 -1 O ILE A 44 N ILE A 37
SHEET 1 B 3 THR A 52 GLU A 56 0
SHEET 2 B 3 THR A 97 ASP A 100 1 O THR A 97 N LEU A 53
SHEET 3 B 3 HIS A 123 VAL A 125 1 O VAL A 125 N ASP A 100
SHEET 1 C 2 CYS A 59 ALA A 60 0
SHEET 2 C 2 GLY A 305 PHE A 306 1 O GLY A 305 N ALA A 60
SHEET 1 D 6 ALA A 127 LEU A 130 0
SHEET 2 D 6 ILE A 167 ALA A 171 1 O KCX A 169 N THR A 128
SHEET 3 D 6 VAL A 198 HIS A 201 1 O THR A 199 N ILE A 168
SHEET 4 D 6 VAL A 226 ILE A 228 1 O CYS A 227 N VAL A 198
SHEET 5 D 6 LEU A 249 LEU A 252 1 O LEU A 249 N ILE A 228
SHEET 6 D 6 ILE A 296 VAL A 298 1 O LEU A 297 N LEU A 252
SHEET 1 E 2 ARG B 36 THR B 39 0
SHEET 2 E 2 GLY B 42 THR B 45 -1 O ILE B 44 N ILE B 37
SHEET 1 F 3 THR B 52 GLU B 56 0
SHEET 2 F 3 THR B 97 ASP B 100 1 O VAL B 99 N LEU B 53
SHEET 3 F 3 HIS B 123 VAL B 125 1 O VAL B 125 N ASP B 100
SHEET 1 G 2 CYS B 59 ALA B 60 0
SHEET 2 G 2 GLY B 305 PHE B 306 1 O GLY B 305 N ALA B 60
SHEET 1 H 6 ALA B 127 GLY B 129 0
SHEET 2 H 6 ILE B 167 ALA B 171 1 O KCX B 169 N THR B 128
SHEET 3 H 6 VAL B 198 HIS B 201 1 O THR B 199 N ILE B 168
SHEET 4 H 6 VAL B 226 ILE B 228 1 O CYS B 227 N THR B 200
SHEET 5 H 6 LEU B 249 LEU B 252 1 O LEU B 249 N ILE B 228
SHEET 6 H 6 ILE B 296 VAL B 298 1 O LEU B 297 N LEU B 252
SHEET 1 I 2 ARG K 36 THR K 39 0
SHEET 2 I 2 GLY K 42 THR K 45 -1 O ILE K 44 N ILE K 37
SHEET 1 J 3 THR K 52 GLU K 56 0
SHEET 2 J 3 THR K 97 ASP K 100 1 O THR K 97 N LEU K 53
SHEET 3 J 3 HIS K 123 VAL K 125 1 O VAL K 125 N ASP K 100
SHEET 1 K 2 CYS K 59 ALA K 60 0
SHEET 2 K 2 GLY K 305 PHE K 306 1 O GLY K 305 N ALA K 60
SHEET 1 L 6 ALA K 127 LEU K 130 0
SHEET 2 L 6 ILE K 167 ALA K 171 1 O KCX K 169 N THR K 128
SHEET 3 L 6 VAL K 198 HIS K 201 1 O THR K 199 N ILE K 168
SHEET 4 L 6 VAL K 226 ILE K 228 1 O CYS K 227 N VAL K 198
SHEET 5 L 6 LEU K 249 LEU K 252 1 O LEU K 249 N ILE K 228
SHEET 6 L 6 ILE K 296 VAL K 298 1 O LEU K 297 N LEU K 252
SHEET 1 M 2 ARG P 36 THR P 39 0
SHEET 2 M 2 GLY P 42 THR P 45 -1 O ILE P 44 N ILE P 37
SHEET 1 N 3 THR P 52 GLU P 56 0
SHEET 2 N 3 THR P 97 ASP P 100 1 O VAL P 99 N LEU P 53
SHEET 3 N 3 HIS P 123 VAL P 125 1 O VAL P 125 N ASP P 100
SHEET 1 O 2 CYS P 59 ALA P 60 0
SHEET 2 O 2 GLY P 305 PHE P 306 1 O GLY P 305 N ALA P 60
SHEET 1 P 6 ALA P 127 GLY P 129 0
SHEET 2 P 6 ILE P 167 ALA P 171 1 O KCX P 169 N THR P 128
SHEET 3 P 6 VAL P 198 HIS P 201 1 O THR P 199 N ILE P 168
SHEET 4 P 6 VAL P 226 ILE P 228 1 O CYS P 227 N VAL P 198
SHEET 5 P 6 LEU P 249 LEU P 252 1 O LEU P 249 N ILE P 228
SHEET 6 P 6 ILE P 296 VAL P 298 1 O LEU P 297 N LEU P 252
LINK C ILE A 168 N KCX A 169 1555 1555 1.33
LINK C KCX A 169 N VAL A 170 1555 1555 1.33
LINK C ILE B 168 N KCX B 169 1555 1555 1.34
LINK C KCX B 169 N VAL B 170 1555 1555 1.33
LINK C ILE K 168 N KCX K 169 1555 1555 1.33
LINK C KCX K 169 N VAL K 170 1555 1555 1.33
LINK C ILE P 168 N KCX P 169 1555 1555 1.34
LINK C KCX P 169 N VAL P 170 1555 1555 1.33
LINK O1 CAC A 1 ZN ZN A2401 1555 1555 1.97
LINK O2 CAC A 1 ZN ZN A2402 1555 1555 2.05
LINK NE2 HIS A 55 ZN ZN A2401 1555 1555 2.01
LINK NE2 HIS A 57 ZN ZN A2401 1555 1555 2.11
LINK OQ1 KCX A 169 ZN ZN A2401 1555 1555 2.09
LINK OQ2 KCX A 169 ZN ZN A2402 1555 1555 1.94
LINK ND1 HIS A 201 ZN ZN A2402 1555 1555 2.16
LINK NE2 HIS A 230 ZN ZN A2402 1555 1555 2.10
LINK OD1 ASP A 301 ZN ZN A2401 1555 1555 2.14
LINK O2 CAC B 2 ZN ZN B2403 1555 1555 2.08
LINK O1 CAC B 2 ZN ZN B2404 1555 1555 2.13
LINK NE2 HIS B 55 ZN ZN B2403 1555 1555 2.16
LINK NE2 HIS B 57 ZN ZN B2403 1555 1555 2.12
LINK OQ2 KCX B 169 ZN ZN B2403 1555 1555 2.10
LINK OQ1 KCX B 169 ZN ZN B2404 1555 1555 2.01
LINK ND1 HIS B 201 ZN ZN B2404 1555 1555 2.17
LINK NE2 HIS B 230 ZN ZN B2404 1555 1555 2.12
LINK OD1 ASP B 301 ZN ZN B2403 1555 1555 2.19
LINK O2 CAC K 3 ZN ZN K2405 1555 1555 1.95
LINK O1 CAC K 3 ZN ZN K2406 1555 1555 2.07
LINK NE2 HIS K 55 ZN ZN K2405 1555 1555 2.04
LINK NE2 HIS K 57 ZN ZN K2405 1555 1555 2.06
LINK OQ1 KCX K 169 ZN ZN K2405 1555 1555 2.02
LINK OQ2 KCX K 169 ZN ZN K2406 1555 1555 2.00
LINK ND1 HIS K 201 ZN ZN K2406 1555 1555 2.17
LINK NE2 HIS K 230 ZN ZN K2406 1555 1555 2.15
LINK OD1 ASP K 301 ZN ZN K2405 1555 1555 2.09
LINK O2 CAC P 4 ZN ZN P2407 1555 1555 2.00
LINK O1 CAC P 4 ZN ZN P2408 1555 1555 2.10
LINK NE2 HIS P 55 ZN ZN P2407 1555 1555 2.14
LINK NE2 HIS P 57 ZN ZN P2407 1555 1555 2.13
LINK OQ2 KCX P 169 ZN ZN P2407 1555 1555 2.20
LINK OQ1 KCX P 169 ZN ZN P2408 1555 1555 1.96
LINK ND1 HIS P 201 ZN ZN P2408 1555 1555 2.09
LINK NE2 HIS P 230 ZN ZN P2408 1555 1555 2.12
LINK OD1 ASP P 301 ZN ZN P2407 1555 1555 2.11
SITE 1 AC1 5 CAC A 1 HIS A 55 HIS A 57 KCX A 169
SITE 2 AC1 5 ASP A 301
SITE 1 AC2 4 CAC A 1 KCX A 169 HIS A 201 HIS A 230
SITE 1 AC3 9 HIS A 57 TRP A 131 KCX A 169 HIS A 201
SITE 2 AC3 9 ASP A 301 ZN A2401 ZN A2402 HOH A2488
SITE 3 AC3 9 HOH A2593
SITE 1 AC4 5 CAC B 2 HIS B 55 HIS B 57 KCX B 169
SITE 2 AC4 5 ASP B 301
SITE 1 AC5 4 CAC B 2 KCX B 169 HIS B 201 HIS B 230
SITE 1 AC6 9 HIS B 57 ILE B 106 TRP B 131 KCX B 169
SITE 2 AC6 9 HIS B 201 ASP B 301 ZN B2403 ZN B2404
SITE 3 AC6 9 HOH B2469
SITE 1 AC7 5 CAC K 3 HIS K 55 HIS K 57 KCX K 169
SITE 2 AC7 5 ASP K 301
SITE 1 AC8 4 CAC K 3 KCX K 169 HIS K 201 HIS K 230
SITE 1 AC9 9 HIS K 57 ILE K 106 TRP K 131 KCX K 169
SITE 2 AC9 9 HIS K 201 ASP K 301 ZN K2405 ZN K2406
SITE 3 AC9 9 HOH K2672
SITE 1 BC1 5 CAC P 4 HIS P 55 HIS P 57 KCX P 169
SITE 2 BC1 5 ASP P 301
SITE 1 BC2 4 CAC P 4 KCX P 169 HIS P 201 HIS P 230
SITE 1 BC3 10 HIS P 57 ILE P 106 TRP P 131 KCX P 169
SITE 2 BC3 10 HIS P 201 ASP P 301 ZN P2407 ZN P2408
SITE 3 BC3 10 HOH P2516 HOH P2566
CRYST1 55.295 68.299 90.030 90.05 100.42 89.96 P 1 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018085 -0.000013 0.003326 0.00000
SCALE2 0.000000 0.014642 0.000011 0.00000
SCALE3 0.000000 0.000000 0.011294 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
