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HEADER HYDROLASE 27-MAY-17 5XO8
TITLE CRYSTAL STRUCTURE OF A NOVEL ZEN LACTONASE MUTANT WITH LIGAND Z
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LACTONASE FOR PROTEIN;
COMPND 3 CHAIN: A, B, C, D, E, F, G, H;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHINOCLADIELLA MACKENZIEI CBS 650.93;
SOURCE 3 ORGANISM_TAXID: 1442369;
SOURCE 4 GENE: Z518_04590;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-46 EK/LIC
KEYWDS ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Y.ZHENG,W.T.LIU,W.D.LIU,C.C.CHEN,R.T.GUO
REVDAT 1 02-MAY-18 5XO8 0
JRNL AUTH Y.Y.ZHENG,W.T.LIU,C.C.CHEN,X.Y.HU,W.D.LIU,T.P.KO,X.K.TANG,
JRNL AUTH 2 H.L.WEI,J.W.HUANG,R.T.GUO
JRNL TITL CRYSTAL STRUCTURE OF A MYCOESTROGEN-DETOXIFYING LACTONASE
JRNL TITL 2 FROM RHINOCLADIELLA MACKENZIEI: MOLECULAR INSIGHT INTO ZHD
JRNL TITL 3 SUBSTRATE SELECTIVITY
JRNL REF ACS CATALYSIS V. 8 4294 2018
JRNL REFN ESSN 2155-5435
JRNL DOI 10.1021/ACSCATAL.8B00464
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 222748
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) : 0.146
REMARK 3 R VALUE (WORKING SET) : 0.145
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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) : 1.88
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.93
REMARK 3 REFLECTION IN BIN (WORKING SET) : 16092
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.20
REMARK 3 BIN R VALUE (WORKING SET) : 0.2070
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.2510
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 16430
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 184
REMARK 3 SOLVENT ATOMS : 2594
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.83
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): 0.100
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.072
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.443
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.958
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 17106 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 15762 ; 0.004 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 23368 ; 2.085 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 36464 ; 1.267 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2100 ; 6.700 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 738 ;31.779 ;23.604
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2610 ;12.164 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 104 ;12.775 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2530 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19282 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3774 ; 0.002 ; 0.020
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): 8412 ; 2.529 ; 2.483
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 8411 ; 2.527 ; 2.483
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10502 ; 3.124 ; 3.711
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 10503 ; 3.125 ; 3.711
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 8694 ; 3.521 ; 2.820
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 8695 ; 3.522 ; 2.820
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 12865 ; 5.105 ; 4.094
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 22664 ; 7.131 ;22.827
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 22422 ; 7.071 ;22.663
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 : 1.20
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 5XO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1300003872.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-17
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 : NSRRC
REMARK 200 BEAMLINE : TPS 05A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9998
REMARK 200 MONOCHROMATOR : LN2 COOLED SI(111) DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 224832
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.30200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: PHASER
REMARK 200 STARTING MODEL: 3WZL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.085 M SODIUM
REMARK 280 CACODYLATE PH 6.5, 25-28% W/V POLYETHYLENE GLYCOL 8000 AND 15% V/
REMARK 280 V GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, G
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 ALA B 3
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ALA C 3
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 ALA E 3
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 ALA F 3
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 ALA G 3
REMARK 465 LYS G 266
REMARK 465 MET H 1
REMARK 465 ALA H 2
REMARK 465 LYS H 266
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 OG SER G 196 O HOH G 401 1.94
REMARK 500 OD1 ASN H 242 O HOH H 401 1.95
REMARK 500 O GLN F 76 NZ LYS F 82 1.99
REMARK 500 OG SER B 196 O HOH B 401 2.01
REMARK 500 O HOH H 522 O HOH H 661 2.02
REMARK 500 O HOH E 442 O HOH E 625 2.02
REMARK 500 O LEU F 265 O HOH F 401 2.03
REMARK 500 O HOH B 495 O HOH B 652 2.04
REMARK 500 OD1 ASP F 145 OG1 THR F 148 2.05
REMARK 500 O HOH G 588 O HOH G 604 2.06
REMARK 500 O HOH G 416 O HOH G 623 2.06
REMARK 500 O HOH E 581 O HOH H 626 2.07
REMARK 500 O HOH F 548 O HOH F 561 2.08
REMARK 500 O HOH B 482 O HOH B 742 2.08
REMARK 500 O HOH B 731 O HOH B 745 2.09
REMARK 500 O HOH C 461 O HOH C 528 2.12
REMARK 500 O GLU F 202 O HOH F 402 2.12
REMARK 500 O HOH E 444 O HOH E 562 2.14
REMARK 500 O HOH A 683 O HOH A 750 2.14
REMARK 500 O HOH H 405 O HOH H 621 2.15
REMARK 500 O HOH G 516 O HOH G 663 2.16
REMARK 500 O HOH H 662 O HOH H 728 2.16
REMARK 500 CB ASP A 95 O HOH A 663 2.16
REMARK 500 O HOH G 565 O HOH G 664 2.17
REMARK 500 O HOH E 581 O HOH H 495 2.17
REMARK 500 O HOH C 580 O HOH C 640 2.17
REMARK 500 O HOH H 623 O HOH H 669 2.17
REMARK 500 OD1 ASN B 242 O HOH B 402 2.19
REMARK 500 O HOH H 412 O HOH H 609 2.19
REMARK 500 OH TYR D 9 O HOH D 401 2.19
REMARK 500 NZ LYS D 255 OE2 GLU D 259 2.19
REMARK 500 O HOH C 653 O HOH C 662 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 572 O HOH E 611 1455 2.11
REMARK 500 O HOH D 466 O HOH H 559 1464 2.16
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 65 -123.77 46.08
REMARK 500 ALA A 105 -117.96 58.08
REMARK 500 ASN A 163 94.39 -176.29
REMARK 500 ASN A 242 -107.42 -130.67
REMARK 500 SER B 65 -124.53 44.76
REMARK 500 ALA B 105 -118.19 57.82
REMARK 500 GLU B 129 71.86 51.26
REMARK 500 ASN B 163 93.22 -175.05
REMARK 500 TYR B 189 -61.13 -106.11
REMARK 500 ASN B 242 -110.55 -131.89
REMARK 500 ASN B 242 -108.50 -126.32
REMARK 500 SER C 65 -124.25 45.79
REMARK 500 ALA C 105 -117.32 54.75
REMARK 500 GLU C 129 70.30 50.35
REMARK 500 ASN C 163 93.34 -173.62
REMARK 500 ASN C 242 -107.45 -125.60
REMARK 500 SER D 65 -122.14 47.07
REMARK 500 ALA D 105 -117.62 56.23
REMARK 500 GLU D 129 70.34 50.77
REMARK 500 ASN D 163 88.15 -177.88
REMARK 500 ASN D 242 -105.60 -123.95
REMARK 500 SER E 65 -124.28 43.43
REMARK 500 ALA E 105 -114.48 55.99
REMARK 500 GLU E 129 71.48 50.74
REMARK 500 ASN E 163 97.56 -177.15
REMARK 500 ASN E 242 -107.35 -125.23
REMARK 500 SER F 65 -124.24 46.73
REMARK 500 TYR F 75 33.14 -140.62
REMARK 500 ALA F 105 -117.73 57.21
REMARK 500 GLU F 133 118.41 -167.16
REMARK 500 PRO F 146 84.52 -67.21
REMARK 500 ALA F 147 -41.49 170.89
REMARK 500 ASN F 163 95.11 -174.43
REMARK 500 ASN F 242 -113.94 -122.87
REMARK 500 SER G 65 -122.77 44.26
REMARK 500 ALA G 105 -119.70 56.49
REMARK 500 TYR G 118 51.65 -141.59
REMARK 500 ASN G 163 92.14 -178.74
REMARK 500 ASN G 242 -115.53 -125.51
REMARK 500 SER H 65 -125.59 46.11
REMARK 500 ALA H 105 -116.44 58.02
REMARK 500 ASN H 163 97.92 -173.38
REMARK 500 ASN H 242 -106.29 -124.83
REMARK 500 ASN H 242 -108.61 -128.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 797 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B 790 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH C 723 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH C 724 DISTANCE = 6.25 ANGSTROMS
REMARK 525 HOH D 713 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH D 714 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH D 715 DISTANCE = 7.17 ANGSTROMS
REMARK 525 HOH D 716 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH F 609 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH G 711 DISTANCE = 6.78 ANGSTROMS
REMARK 525 HOH H 754 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH H 755 DISTANCE = 6.66 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER E 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER F 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER G 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZER H 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5XO6 RELATED DB: PDB
REMARK 900 RELATED ID: 5XO7 RELATED DB: PDB
DBREF1 5XO8 A 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 A A0A0D2ILK1 1 266
DBREF1 5XO8 B 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 B A0A0D2ILK1 1 266
DBREF1 5XO8 C 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 C A0A0D2ILK1 1 266
DBREF1 5XO8 D 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 D A0A0D2ILK1 1 266
DBREF1 5XO8 E 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 E A0A0D2ILK1 1 266
DBREF1 5XO8 F 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 F A0A0D2ILK1 1 266
DBREF1 5XO8 G 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 G A0A0D2ILK1 1 266
DBREF1 5XO8 H 1 266 UNP A0A0D2ILK1_9EURO
DBREF2 5XO8 H A0A0D2ILK1 1 266
SEQADV 5XO8 ALA A 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5XO8 ALA B 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5XO8 ALA C 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5XO8 ALA D 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5XO8 ALA E 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5XO8 ALA F 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5XO8 ALA G 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQADV 5XO8 ALA H 105 UNP A0A0D2ILK SER 105 ENGINEERED MUTATION
SEQRES 1 A 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 A 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 A 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 A 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 A 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 A 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 A 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 A 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 A 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 A 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 A 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 A 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 A 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 A 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 A 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 A 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 A 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 A 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 A 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 A 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 A 266 SER ARG LYS TYR LEU LYS
SEQRES 1 B 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 B 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 B 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 B 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 B 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 B 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 B 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 B 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 B 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 B 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 B 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 B 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 B 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 B 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 B 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 B 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 B 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 B 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 B 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 B 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 B 266 SER ARG LYS TYR LEU LYS
SEQRES 1 C 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 C 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 C 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 C 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 C 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 C 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 C 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 C 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 C 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 C 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 C 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 C 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 C 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 C 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 C 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 C 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 C 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 C 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 C 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 C 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 C 266 SER ARG LYS TYR LEU LYS
SEQRES 1 D 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 D 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 D 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 D 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 D 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 D 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 D 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 D 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 D 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 D 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 D 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 D 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 D 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 D 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 D 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 D 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 D 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 D 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 D 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 D 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 D 266 SER ARG LYS TYR LEU LYS
SEQRES 1 E 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 E 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 E 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 E 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 E 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 E 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 E 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 E 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 E 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 E 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 E 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 E 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 E 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 E 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 E 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 E 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 E 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 E 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 E 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 E 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 E 266 SER ARG LYS TYR LEU LYS
SEQRES 1 F 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 F 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 F 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 F 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 F 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 F 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 F 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 F 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 F 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 F 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 F 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 F 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 F 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 F 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 F 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 F 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 F 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 F 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 F 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 F 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 F 266 SER ARG LYS TYR LEU LYS
SEQRES 1 G 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 G 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 G 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 G 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 G 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 G 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 G 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 G 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 G 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 G 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 G 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 G 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 G 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 G 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 G 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 G 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 G 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 G 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 G 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 G 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 G 266 SER ARG LYS TYR LEU LYS
SEQRES 1 H 266 MET ALA ALA THR ARG THR ARG GLY TYR VAL THR THR LYS
SEQRES 2 H 266 ASP GLY ILE LYS TRP TYR TYR GLU GLN GLU GLY SER GLY
SEQRES 3 H 266 PRO ASP VAL VAL LEU ILE PRO ASP GLY LEU GLY GLU CYS
SEQRES 4 H 266 GLN MET PHE ASP LYS PRO MET SER LEU ILE ALA SER ASN
SEQRES 5 H 266 GLY PHE ARG VAL THR THR PHE ASP MET PRO GLY MET SER
SEQRES 6 H 266 ARG SER SER ASP ALA PRO PRO GLU THR TYR GLN ASP ILE
SEQRES 7 H 266 THR GLY ARG LYS LEU ALA GLY TYR ILE ILE THR LEU LEU
SEQRES 8 H 266 ASP THR LEU ASP ILE LYS ILE ALA SER VAL TRP GLY CYS
SEQRES 9 H 266 ALA SER GLY ALA SER THR VAL LEU ALA LEU CYS SER ASP
SEQRES 10 H 266 TYR PRO GLU ARG VAL ARG ASN GLY MET PRO HIS GLU VAL
SEQRES 11 H 266 PRO THR GLU ASN PRO ASP ILE LEU LEU HIS ILE HIS GLU
SEQRES 12 H 266 VAL ASP PRO ALA THR ILE SER GLN GLU MET ALA ALA ASN
SEQRES 13 H 266 SER ARG ALA TYR SER GLY ASN VAL GLU ALA TRP ASP ALA
SEQRES 14 H 266 LEU GLY PRO GLU VAL HIS ALA ARG LEU HIS ASP ASN TYR
SEQRES 15 H 266 PRO ARG TRP ALA TYR GLY TYR PRO ARG THR ILE PRO PRO
SEQRES 16 H 266 SER ALA PRO VAL LYS THR GLU ASP LEU HIS LYS VAL PRO
SEQRES 17 H 266 ILE ASP TRP THR VAL GLY ALA SER THR PRO THR LYS LEU
SEQRES 18 H 266 PHE PHE GLU ASN ILE VAL ILE ALA ALA ARG GLU GLY ILE
SEQRES 19 H 266 ASN ILE GLY THR LEU PRO GLY ASN HIS PHE PRO TYR VAL
SEQRES 20 H 266 SER HIS PRO GLU GLU PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 21 H 266 SER ARG LYS TYR LEU LYS
HET ZER A 301 23
HET ZER B 301 23
HET ZER C 301 23
HET ZER D 301 23
HET ZER E 301 23
HET ZER F 301 23
HET ZER G 301 23
HET ZER H 301 23
HETNAM ZER (3S,11E)-14,16-DIHYDROXY-3-METHYL-3,4,5,6,9,10-
HETNAM 2 ZER HEXAHYDRO-1H-2-BENZOXACYCLOTETRADECINE-1,7(8H)-DIONE
HETSYN ZER ZEARALENONE
FORMUL 9 ZER 8(C18 H22 O5)
FORMUL 17 HOH *2594(H2 O)
HELIX 1 AA1 GLU A 38 MET A 41 5 4
HELIX 2 AA2 PHE A 42 SER A 51 1 10
HELIX 3 AA3 MET A 64 SER A 68 5 5
HELIX 4 AA4 PRO A 71 GLN A 76 5 6
HELIX 5 AA5 THR A 79 LEU A 94 1 16
HELIX 6 AA6 ALA A 105 TYR A 118 1 14
HELIX 7 AA7 PRO A 135 LEU A 139 5 5
HELIX 8 AA8 HIS A 140 VAL A 144 5 5
HELIX 9 AA9 ASP A 145 TYR A 160 1 16
HELIX 10 AB1 ASN A 163 ALA A 169 1 7
HELIX 11 AB2 GLY A 171 TYR A 189 1 19
HELIX 12 AB3 ILE A 193 ALA A 197 5 5
HELIX 13 AB4 LYS A 200 LEU A 204 5 5
HELIX 14 AB5 PRO A 218 GLU A 232 1 15
HELIX 15 AB6 PHE A 244 HIS A 249 1 6
HELIX 16 AB7 HIS A 249 LYS A 263 1 15
HELIX 17 AB8 GLU B 38 MET B 41 5 4
HELIX 18 AB9 PHE B 42 SER B 51 1 10
HELIX 19 AC1 MET B 64 SER B 68 5 5
HELIX 20 AC2 PRO B 71 GLN B 76 5 6
HELIX 21 AC3 THR B 79 LEU B 94 1 16
HELIX 22 AC4 ALA B 105 TYR B 118 1 14
HELIX 23 AC5 PRO B 135 LEU B 139 5 5
HELIX 24 AC6 HIS B 140 VAL B 144 5 5
HELIX 25 AC7 ASP B 145 TYR B 160 1 16
HELIX 26 AC8 ASN B 163 ALA B 169 1 7
HELIX 27 AC9 GLY B 171 TYR B 189 1 19
HELIX 28 AD1 ILE B 193 ALA B 197 5 5
HELIX 29 AD2 LYS B 200 LEU B 204 5 5
HELIX 30 AD3 PRO B 218 GLU B 232 1 15
HELIX 31 AD4 PHE B 244 HIS B 249 1 6
HELIX 32 AD5 HIS B 249 LYS B 263 1 15
HELIX 33 AD6 GLU C 38 MET C 41 5 4
HELIX 34 AD7 PHE C 42 SER C 51 1 10
HELIX 35 AD8 MET C 64 SER C 68 5 5
HELIX 36 AD9 PRO C 71 GLN C 76 5 6
HELIX 37 AE1 THR C 79 LEU C 94 1 16
HELIX 38 AE2 ALA C 105 TYR C 118 1 14
HELIX 39 AE3 PRO C 135 LEU C 139 5 5
HELIX 40 AE4 HIS C 140 VAL C 144 5 5
HELIX 41 AE5 ASP C 145 TYR C 160 1 16
HELIX 42 AE6 ASN C 163 ALA C 169 1 7
HELIX 43 AE7 GLY C 171 TYR C 189 1 19
HELIX 44 AE8 ILE C 193 ALA C 197 5 5
HELIX 45 AE9 LYS C 200 LEU C 204 5 5
HELIX 46 AF1 PHE C 222 GLU C 232 1 11
HELIX 47 AF2 PHE C 244 HIS C 249 1 6
HELIX 48 AF3 HIS C 249 LYS C 263 1 15
HELIX 49 AF4 GLU D 38 MET D 41 5 4
HELIX 50 AF5 PHE D 42 SER D 51 1 10
HELIX 51 AF6 MET D 64 SER D 68 5 5
HELIX 52 AF7 PRO D 71 GLN D 76 5 6
HELIX 53 AF8 THR D 79 LEU D 94 1 16
HELIX 54 AF9 ALA D 105 TYR D 118 1 14
HELIX 55 AG1 PRO D 135 LEU D 139 5 5
HELIX 56 AG2 HIS D 140 VAL D 144 5 5
HELIX 57 AG3 ASP D 145 TYR D 160 1 16
HELIX 58 AG4 ASN D 163 ALA D 169 1 7
HELIX 59 AG5 GLY D 171 TYR D 189 1 19
HELIX 60 AG6 ILE D 193 ALA D 197 5 5
HELIX 61 AG7 LYS D 200 LEU D 204 5 5
HELIX 62 AG8 PRO D 218 GLY D 233 1 16
HELIX 63 AG9 PHE D 244 HIS D 249 1 6
HELIX 64 AH1 HIS D 249 LYS D 263 1 15
HELIX 65 AH2 GLU E 38 MET E 41 5 4
HELIX 66 AH3 PHE E 42 SER E 51 1 10
HELIX 67 AH4 MET E 64 SER E 68 5 5
HELIX 68 AH5 PRO E 71 GLN E 76 5 6
HELIX 69 AH6 THR E 79 LEU E 94 1 16
HELIX 70 AH7 ALA E 105 TYR E 118 1 14
HELIX 71 AH8 PRO E 135 LEU E 139 5 5
HELIX 72 AH9 HIS E 140 VAL E 144 5 5
HELIX 73 AI1 ASP E 145 TYR E 160 1 16
HELIX 74 AI2 ASN E 163 ALA E 169 1 7
HELIX 75 AI3 GLY E 171 TYR E 189 1 19
HELIX 76 AI4 ILE E 193 ALA E 197 5 5
HELIX 77 AI5 LYS E 200 LEU E 204 5 5
HELIX 78 AI6 PRO E 218 GLY E 233 1 16
HELIX 79 AI7 PHE E 244 HIS E 249 1 6
HELIX 80 AI8 HIS E 249 LYS E 263 1 15
HELIX 81 AI9 GLU F 38 MET F 41 5 4
HELIX 82 AJ1 PHE F 42 SER F 51 1 10
HELIX 83 AJ2 MET F 64 SER F 68 5 5
HELIX 84 AJ3 PRO F 71 GLN F 76 5 6
HELIX 85 AJ4 THR F 79 LEU F 94 1 16
HELIX 86 AJ5 ALA F 105 TYR F 118 1 14
HELIX 87 AJ6 PRO F 135 LEU F 139 5 5
HELIX 88 AJ7 HIS F 140 VAL F 144 5 5
HELIX 89 AJ8 ALA F 147 TYR F 160 1 14
HELIX 90 AJ9 ASN F 163 ALA F 169 1 7
HELIX 91 AK1 GLY F 171 TYR F 189 1 19
HELIX 92 AK2 ILE F 193 ALA F 197 5 5
HELIX 93 AK3 PRO F 218 GLY F 233 1 16
HELIX 94 AK4 PHE F 244 HIS F 249 1 6
HELIX 95 AK5 HIS F 249 LYS F 263 1 15
HELIX 96 AK6 GLU G 38 MET G 41 5 4
HELIX 97 AK7 PHE G 42 SER G 51 1 10
HELIX 98 AK8 MET G 64 SER G 68 5 5
HELIX 99 AK9 PRO G 71 GLN G 76 5 6
HELIX 100 AL1 THR G 79 ASP G 95 1 17
HELIX 101 AL2 ALA G 105 TYR G 118 1 14
HELIX 102 AL3 PRO G 135 LEU G 139 5 5
HELIX 103 AL4 HIS G 140 VAL G 144 5 5
HELIX 104 AL5 ASP G 145 TYR G 160 1 16
HELIX 105 AL6 ASN G 163 ALA G 169 1 7
HELIX 106 AL7 GLY G 171 TYR G 189 1 19
HELIX 107 AL8 ILE G 193 ALA G 197 5 5
HELIX 108 AL9 LYS G 200 LEU G 204 5 5
HELIX 109 AM1 PHE G 222 GLY G 233 1 12
HELIX 110 AM2 PHE G 244 HIS G 249 1 6
HELIX 111 AM3 HIS G 249 LYS G 263 1 15
HELIX 112 AM4 GLU H 38 MET H 41 5 4
HELIX 113 AM5 PHE H 42 SER H 51 1 10
HELIX 114 AM6 MET H 64 SER H 68 5 5
HELIX 115 AM7 PRO H 71 GLN H 76 5 6
HELIX 116 AM8 THR H 79 LEU H 94 1 16
HELIX 117 AM9 ALA H 105 TYR H 118 1 14
HELIX 118 AN1 PRO H 135 LEU H 139 5 5
HELIX 119 AN2 ASP H 145 TYR H 160 1 16
HELIX 120 AN3 ASN H 163 ALA H 169 1 7
HELIX 121 AN4 GLY H 171 TYR H 189 1 19
HELIX 122 AN5 ILE H 193 ALA H 197 5 5
HELIX 123 AN6 LYS H 200 LEU H 204 5 5
HELIX 124 AN7 PHE H 222 GLY H 233 1 12
HELIX 125 AN8 PHE H 244 HIS H 249 1 6
HELIX 126 AN9 HIS H 249 LYS H 263 1 15
SHEET 1 AA1 6 THR A 6 THR A 11 0
SHEET 2 AA1 6 LYS A 17 GLU A 23 -1 O GLN A 22 N THR A 6
SHEET 3 AA1 6 ARG A 55 PHE A 59 -1 O VAL A 56 N GLU A 23
SHEET 4 AA1 6 ASP A 28 ILE A 32 1 N VAL A 29 O ARG A 55
SHEET 5 AA1 6 ALA A 99 CYS A 104 1 O TRP A 102 N ILE A 32
SHEET 6 AA1 6 VAL A 122 HIS A 128 1 O MET A 126 N VAL A 101
SHEET 1 AA2 2 ASP A 210 GLY A 214 0
SHEET 2 AA2 2 ASN A 235 LEU A 239 1 O ASN A 235 N TRP A 211
SHEET 1 AA3 6 THR B 6 THR B 11 0
SHEET 2 AA3 6 LYS B 17 GLU B 23 -1 O GLN B 22 N THR B 6
SHEET 3 AA3 6 ARG B 55 PHE B 59 -1 O VAL B 56 N GLU B 23
SHEET 4 AA3 6 ASP B 28 ILE B 32 1 N LEU B 31 O THR B 57
SHEET 5 AA3 6 ALA B 99 CYS B 104 1 O TRP B 102 N VAL B 30
SHEET 6 AA3 6 VAL B 122 HIS B 128 1 O MET B 126 N VAL B 101
SHEET 1 AA4 2 ASP B 210 GLY B 214 0
SHEET 2 AA4 2 ASN B 235 LEU B 239 1 O ASN B 235 N TRP B 211
SHEET 1 AA5 6 ARG C 5 THR C 11 0
SHEET 2 AA5 6 LYS C 17 GLU C 23 -1 O GLN C 22 N THR C 6
SHEET 3 AA5 6 ARG C 55 PHE C 59 -1 O VAL C 56 N GLU C 23
SHEET 4 AA5 6 ASP C 28 ILE C 32 1 N VAL C 29 O THR C 57
SHEET 5 AA5 6 ALA C 99 CYS C 104 1 O TRP C 102 N VAL C 30
SHEET 6 AA5 6 VAL C 122 HIS C 128 1 O MET C 126 N VAL C 101
SHEET 1 AA6 2 ASP C 210 GLY C 214 0
SHEET 2 AA6 2 ASN C 235 LEU C 239 1 O ASN C 235 N TRP C 211
SHEET 1 AA7 6 THR D 6 THR D 11 0
SHEET 2 AA7 6 LYS D 17 GLU D 23 -1 O GLN D 22 N THR D 6
SHEET 3 AA7 6 ARG D 55 PHE D 59 -1 O VAL D 56 N GLU D 23
SHEET 4 AA7 6 ASP D 28 ILE D 32 1 N VAL D 29 O THR D 57
SHEET 5 AA7 6 ALA D 99 CYS D 104 1 O TRP D 102 N VAL D 30
SHEET 6 AA7 6 VAL D 122 HIS D 128 1 O MET D 126 N VAL D 101
SHEET 1 AA8 2 ASP D 210 GLY D 214 0
SHEET 2 AA8 2 ASN D 235 LEU D 239 1 O ASN D 235 N TRP D 211
SHEET 1 AA9 6 THR E 6 THR E 11 0
SHEET 2 AA9 6 LYS E 17 GLU E 23 -1 O TYR E 20 N GLY E 8
SHEET 3 AA9 6 ARG E 55 PHE E 59 -1 O VAL E 56 N GLU E 23
SHEET 4 AA9 6 ASP E 28 ILE E 32 1 N LEU E 31 O THR E 57
SHEET 5 AA9 6 ALA E 99 CYS E 104 1 O TRP E 102 N ILE E 32
SHEET 6 AA9 6 VAL E 122 HIS E 128 1 O MET E 126 N VAL E 101
SHEET 1 AB1 2 ASP E 210 GLY E 214 0
SHEET 2 AB1 2 ASN E 235 LEU E 239 1 O ASN E 235 N TRP E 211
SHEET 1 AB2 6 THR F 6 THR F 11 0
SHEET 2 AB2 6 LYS F 17 GLU F 23 -1 O GLN F 22 N THR F 6
SHEET 3 AB2 6 ARG F 55 PHE F 59 -1 O VAL F 56 N GLU F 23
SHEET 4 AB2 6 ASP F 28 ILE F 32 1 N LEU F 31 O THR F 57
SHEET 5 AB2 6 ALA F 99 CYS F 104 1 O SER F 100 N VAL F 30
SHEET 6 AB2 6 VAL F 122 HIS F 128 1 O MET F 126 N VAL F 101
SHEET 1 AB3 2 ASP F 210 GLY F 214 0
SHEET 2 AB3 2 ASN F 235 LEU F 239 1 O ASN F 235 N TRP F 211
SHEET 1 AB4 6 THR G 6 THR G 11 0
SHEET 2 AB4 6 LYS G 17 GLU G 23 -1 O TYR G 20 N GLY G 8
SHEET 3 AB4 6 ARG G 55 PHE G 59 -1 O VAL G 56 N GLU G 23
SHEET 4 AB4 6 ASP G 28 ILE G 32 1 N VAL G 29 O ARG G 55
SHEET 5 AB4 6 ALA G 99 CYS G 104 1 O SER G 100 N VAL G 30
SHEET 6 AB4 6 VAL G 122 HIS G 128 1 O MET G 126 N VAL G 101
SHEET 1 AB5 2 ASP G 210 GLY G 214 0
SHEET 2 AB5 2 ASN G 235 LEU G 239 1 O ASN G 235 N TRP G 211
SHEET 1 AB6 6 THR H 6 THR H 11 0
SHEET 2 AB6 6 LYS H 17 GLU H 23 -1 O GLN H 22 N THR H 6
SHEET 3 AB6 6 ARG H 55 PHE H 59 -1 O VAL H 56 N GLU H 23
SHEET 4 AB6 6 ASP H 28 ILE H 32 1 N VAL H 29 O THR H 57
SHEET 5 AB6 6 ALA H 99 CYS H 104 1 O TRP H 102 N ILE H 32
SHEET 6 AB6 6 VAL H 122 HIS H 128 1 O MET H 126 N VAL H 101
SHEET 1 AB7 2 ASP H 210 GLY H 214 0
SHEET 2 AB7 2 ASN H 235 LEU H 239 1 O ASN H 235 N TRP H 211
SITE 1 AC1 15 GLY A 35 LEU A 36 ALA A 105 SER A 106
SITE 2 AC1 15 ASN A 134 LEU A 138 SER A 157 TYR A 160
SITE 3 AC1 15 TRP A 185 TYR A 189 PRO A 190 ILE A 193
SITE 4 AC1 15 PRO A 194 HIS A 243 PHE A 244
SITE 1 AC2 14 ASP B 34 GLY B 35 ALA B 105 SER B 106
SITE 2 AC2 14 ASN B 134 ILE B 137 TYR B 160 TRP B 185
SITE 3 AC2 14 TYR B 189 PRO B 190 ILE B 193 PRO B 194
SITE 4 AC2 14 HIS B 243 PHE B 244
SITE 1 AC3 12 GLY C 35 ALA C 105 SER C 106 ASN C 134
SITE 2 AC3 12 SER C 157 TYR C 160 TRP C 185 TYR C 189
SITE 3 AC3 12 PRO C 190 PRO C 194 HIS C 243 PHE C 244
SITE 1 AC4 15 ASP D 34 GLY D 35 ALA D 105 SER D 106
SITE 2 AC4 15 ASN D 134 MET D 153 ASN D 156 SER D 157
SITE 3 AC4 15 TYR D 160 TRP D 185 TYR D 189 PRO D 190
SITE 4 AC4 15 PRO D 194 HIS D 243 PHE D 244
SITE 1 AC5 14 ASP E 34 GLY E 35 ALA E 105 SER E 106
SITE 2 AC5 14 ASN E 134 MET E 153 SER E 157 TRP E 185
SITE 3 AC5 14 TYR E 189 PRO E 190 ILE E 193 PRO E 194
SITE 4 AC5 14 HIS E 243 PHE E 244
SITE 1 AC6 15 ASP F 34 GLY F 35 ALA F 105 SER F 106
SITE 2 AC6 15 ASN F 134 MET F 153 SER F 157 TYR F 160
SITE 3 AC6 15 TRP F 185 TYR F 189 PRO F 190 ILE F 193
SITE 4 AC6 15 PRO F 194 HIS F 243 PHE F 244
SITE 1 AC7 13 ASP G 34 GLY G 35 ALA G 105 SER G 106
SITE 2 AC7 13 ASN G 134 LEU G 138 SER G 157 TRP G 185
SITE 3 AC7 13 TYR G 189 PRO G 190 PRO G 194 HIS G 243
SITE 4 AC7 13 PHE G 244
SITE 1 AC8 14 ASP H 34 GLY H 35 ALA H 105 SER H 106
SITE 2 AC8 14 ASN H 134 LEU H 138 SER H 157 TYR H 160
SITE 3 AC8 14 TRP H 185 TYR H 189 PRO H 190 PRO H 194
SITE 4 AC8 14 HIS H 243 PHE H 244
CRYST1 75.470 95.196 101.663 90.21 92.34 91.48 P 1 8
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 0.013250 0.000342 0.000543 0.00000
SCALE2 0.000000 0.010508 0.000050 0.00000
SCALE3 0.000000 0.000000 0.009845 0.00000
TER 2056 LYS A 266
TER 4120 LYS B 266
TER 6176 LYS C 266
TER 8237 LYS D 266
TER 10293 LYS E 266
TER 12349 LYS F 266
TER 14395 LEU G 265
TER 16454 LEU H 265
MASTER 479 0 8 126 64 0 31 619208 8 184 168
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