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HEADER HYDROLASE 01-OCT-14 3WZM
TITLE ZEN LACTONASE MUTANT COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLONOSTACHYS ROSEA;
SOURCE 3 ORGANISM_TAXID: 29856;
SOURCE 4 GENE: ZHD101;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-46 EK/LIC
KEYWDS ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.P.KO,C.H.HUANG,J.R.LIU,R.T.GUO
REVDAT 1 26-NOV-14 3WZM 0
JRNL AUTH W.PENG,T.P.KO,Y.YANG,Y.ZHENG,C.C.CHEN,Z.ZHU,C.H.HUANG,
JRNL AUTH 2 Y.F.ZENG,J.W.HUANG,A.H.-J.WAND,J.R.LIU,R.T.GUO
JRNL TITL CRYSTAL STRUCTURE AND SUBSTRATE-BINDING MODE OF THE
JRNL TITL 2 MYCOESTROGEN-DETOXIFYING LACTONASE ZHD FROM CLONOSTACHYS
JRNL TITL 3 ROSEA
JRNL REF RSC ADV V. 4 62321 2014
JRNL REFN ESSN 2046-2069
JRNL DOI 10.1039/C4RA12111B
REMARK 2
REMARK 2 RESOLUTION. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.3
REMARK 3 NUMBER OF REFLECTIONS : 35113
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1848
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.61
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4628
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 257
REMARK 3 BIN FREE R VALUE : 0.3110
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6063
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 426
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.31000
REMARK 3 B22 (A**2) : 2.31000
REMARK 3 B33 (A**2) : -3.47000
REMARK 3 B12 (A**2) : 1.16000
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): 0.443
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.292
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 17.529
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6288 ; 0.019 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8589 ; 1.763 ; 1.969
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 789 ; 6.814 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;36.621 ;24.096
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 975 ;17.159 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;12.484 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 975 ; 0.112 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4785 ; 0.009 ; 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): 3957 ; 0.870 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6420 ; 1.604 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2331 ; 2.347 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2169 ; 3.758 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : C A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 264 5
REMARK 3 1 A 1 A 264 5
REMARK 3 1 B 1 B 264 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1056 ; 0.320 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1056 ; 0.180 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1056 ; 0.220 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 C (A): 988 ; 0.550 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 A (A): 988 ; 0.380 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 988 ; 0.480 ; 5.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1056 ;27.130 ; 2.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1056 ;14.890 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1056 ;13.000 ; 2.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 988 ;26.210 ;10.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 988 ;14.340 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 988 ;12.760 ;10.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 300 C 300 1
REMARK 3 1 A 300 A 300 1
REMARK 3 1 B 300 B 300 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 C (A): 23 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 A (A): 23 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 2 B (A): 23 ; 0.030 ; 0.050
REMARK 3 TIGHT THERMAL 2 C (A**2): 23 ; 3.900 ; 0.500
REMARK 3 TIGHT THERMAL 2 A (A**2): 23 ; 2.010 ; 0.500
REMARK 3 TIGHT THERMAL 2 B (A**2): 23 ; 1.910 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 300
REMARK 3 ORIGIN FOR THE GROUP (A): -17.8905 18.2956 11.0766
REMARK 3 T TENSOR
REMARK 3 T11: 0.3572 T22: 0.1672
REMARK 3 T33: 0.2432 T12: 0.0340
REMARK 3 T13: 0.0202 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.8340 L22: 0.6581
REMARK 3 L33: 2.1814 L12: 0.2496
REMARK 3 L13: -0.1344 L23: -0.0080
REMARK 3 S TENSOR
REMARK 3 S11: -0.1210 S12: 0.0665 S13: -0.0033
REMARK 3 S21: 0.1339 S22: 0.1979 S23: -0.0138
REMARK 3 S31: -0.0833 S32: 0.0792 S33: -0.0769
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 300
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9443 26.3094 -27.3866
REMARK 3 T TENSOR
REMARK 3 T11: 0.3023 T22: 0.2102
REMARK 3 T33: 0.2311 T12: -0.1300
REMARK 3 T13: 0.0233 T23: -0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.9298 L22: 0.6643
REMARK 3 L33: 2.7931 L12: 0.3216
REMARK 3 L13: -0.7241 L23: -0.4066
REMARK 3 S TENSOR
REMARK 3 S11: -0.0155 S12: 0.1008 S13: 0.0203
REMARK 3 S21: 0.0515 S22: 0.1017 S23: -0.0735
REMARK 3 S31: -0.0885 S32: -0.1098 S33: -0.0862
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 300
REMARK 3 ORIGIN FOR THE GROUP (A): -48.9973 3.4387 -19.9495
REMARK 3 T TENSOR
REMARK 3 T11: 0.0767 T22: 0.3250
REMARK 3 T33: 0.6359 T12: -0.1433
REMARK 3 T13: -0.1346 T23: 0.1820
REMARK 3 L TENSOR
REMARK 3 L11: 2.0824 L22: 0.8982
REMARK 3 L33: 4.4659 L12: -1.1274
REMARK 3 L13: -0.2518 L23: 0.9842
REMARK 3 S TENSOR
REMARK 3 S11: -0.0263 S12: 0.1160 S13: -0.3881
REMARK 3 S21: -0.0488 S22: 0.0092 S23: 0.2780
REMARK 3 S31: 0.0776 S32: -0.6039 S33: 0.0171
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 3WZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-OCT-14.
REMARK 100 THE RCSB ID CODE IS RCSB096992.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-13
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 : BL13B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38626
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 34.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 0.34500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB 3WZL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 2000 MME, 0.1M BIS-TRIS PH
REMARK 280 6.5, SOAKING WITH RESERVOIR + 10MM ZEARALENONE) , VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 157.26133
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 314.52267
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 235.89200
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 393.15333
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 78.63067
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 157.26133
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 314.52267
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 393.15333
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 235.89200
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 78.63067
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
REMARK 350 TOTAL BURIED SURFACE AREA: 1270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 424 LIES ON A SPECIAL POSITION.
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 -13
REMARK 465 ALA A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 VAL A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 LYS A 0
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 VAL B -5
REMARK 465 ASP B -4
REMARK 465 ASP B -3
REMARK 465 ASP B -2
REMARK 465 ASP B -1
REMARK 465 LYS B 0
REMARK 465 MET C -13
REMARK 465 ALA C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 HIS C -9
REMARK 465 HIS C -8
REMARK 465 HIS C -7
REMARK 465 HIS C -6
REMARK 465 VAL C -5
REMARK 465 ASP C -4
REMARK 465 ASP C -3
REMARK 465 ASP C -2
REMARK 465 ASP C -1
REMARK 465 LYS C 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O GLU B 201 O HOH B 562 2.01
REMARK 500 OE2 GLU C 163 O HOH C 415 2.16
REMARK 500 OD2 ASP A 25 O HOH A 637 2.16
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 A 668 O HOH C 430 8555 1.94
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 ARG A 2 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 185 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 2 NE - CZ - NH1 ANGL. DEV. = -3.1 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 62 -128.30 41.44
REMARK 500 TYR A 72 12.25 -144.72
REMARK 500 ALA A 102 -124.82 56.75
REMARK 500 GLU A 126 70.31 48.53
REMARK 500 PRO A 196 29.54 -78.64
REMARK 500 MET A 241 -115.80 -139.96
REMARK 500 ASP B 31 -170.79 -68.92
REMARK 500 SER B 62 -134.19 47.09
REMARK 500 ALA B 102 -122.26 53.50
REMARK 500 TYR B 115 54.77 -141.12
REMARK 500 GLU B 126 71.55 50.03
REMARK 500 HIS B 134 0.30 -65.34
REMARK 500 ASP B 143 -52.09 -29.74
REMARK 500 PRO B 196 44.82 -82.90
REMARK 500 MET B 241 -109.55 -143.32
REMARK 500 PRO C 30 174.21 -53.24
REMARK 500 ASP C 31 -159.82 -84.59
REMARK 500 ASP C 40 -74.59 -21.48
REMARK 500 SER C 62 -116.81 48.32
REMARK 500 ASP C 92 54.28 33.87
REMARK 500 ALA C 102 -110.75 50.34
REMARK 500 GLU C 126 68.15 64.26
REMARK 500 ASP C 157 -65.47 -101.21
REMARK 500 ALA C 195 113.97 -34.89
REMARK 500 PRO C 196 31.69 -76.09
REMARK 500 PRO C 217 153.94 -43.72
REMARK 500 ALA C 228 -71.79 -56.33
REMARK 500 MET C 241 -94.80 -119.39
REMARK 500 TYR C 245 -7.63 -56.39
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 THR A 138 24.3 L L OUTSIDE RANGE
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 514 DISTANCE = 5.60 ANGSTROMS
REMARK 525 HOH A 526 DISTANCE = 7.57 ANGSTROMS
REMARK 525 HOH A 533 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH A 543 DISTANCE = 5.02 ANGSTROMS
REMARK 525 HOH A 561 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH A 573 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH A 591 DISTANCE = 7.25 ANGSTROMS
REMARK 525 HOH A 596 DISTANCE = 5.55 ANGSTROMS
REMARK 525 HOH A 604 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 611 DISTANCE = 5.95 ANGSTROMS
REMARK 525 HOH A 631 DISTANCE = 5.30 ANGSTROMS
REMARK 525 HOH A 634 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH A 635 DISTANCE = 8.09 ANGSTROMS
REMARK 525 HOH A 639 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A 640 DISTANCE = 7.63 ANGSTROMS
REMARK 525 HOH A 655 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A 660 DISTANCE = 7.43 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A 675 DISTANCE = 5.52 ANGSTROMS
REMARK 525 HOH A 684 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH B 416 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH B 422 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH B 433 DISTANCE = 7.07 ANGSTROMS
REMARK 525 HOH B 448 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH B 449 DISTANCE = 7.26 ANGSTROMS
REMARK 525 HOH B 451 DISTANCE = 7.70 ANGSTROMS
REMARK 525 HOH B 452 DISTANCE = 6.94 ANGSTROMS
REMARK 525 HOH B 461 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH B 467 DISTANCE = 5.35 ANGSTROMS
REMARK 525 HOH B 469 DISTANCE = 5.71 ANGSTROMS
REMARK 525 HOH B 481 DISTANCE = 5.75 ANGSTROMS
REMARK 525 HOH B 486 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH B 508 DISTANCE = 7.00 ANGSTROMS
REMARK 525 HOH B 518 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B 523 DISTANCE = 5.96 ANGSTROMS
REMARK 525 HOH B 531 DISTANCE = 8.00 ANGSTROMS
REMARK 525 HOH B 539 DISTANCE = 5.90 ANGSTROMS
REMARK 525 HOH B 542 DISTANCE = 7.29 ANGSTROMS
REMARK 525 HOH B 543 DISTANCE = 6.87 ANGSTROMS
REMARK 525 HOH B 549 DISTANCE = 7.14 ANGSTROMS
REMARK 525 HOH B 550 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH B 551 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH B 554 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH B 556 DISTANCE = 5.07 ANGSTROMS
REMARK 525 HOH B 559 DISTANCE = 7.91 ANGSTROMS
REMARK 525 HOH C 404 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH C 405 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH C 420 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH C 433 DISTANCE = 7.83 ANGSTROMS
REMARK 525 HOH C 435 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH C 439 DISTANCE = 7.42 ANGSTROMS
REMARK 525 HOH C 447 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH C 449 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH C 451 DISTANCE = 5.14 ANGSTROMS
REMARK 525 HOH C 455 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH C 456 DISTANCE = 5.47 ANGSTROMS
REMARK 525 HOH C 459 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH C 461 DISTANCE = 6.20 ANGSTROMS
REMARK 525 HOH C 465 DISTANCE = 5.48 ANGSTROMS
REMARK 525 HOH C 467 DISTANCE = 7.31 ANGSTROMS
REMARK 525 HOH C 468 DISTANCE = 6.67 ANGSTROMS
REMARK 525 HOH C 470 DISTANCE = 7.26 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 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZER B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZER C 300
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WZL RELATED DB: PDB
REMARK 900 NATIVE PROTEIN
DBREF 3WZM A 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 3WZM B 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 3WZM C 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
SEQADV 3WZM MET A -13 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ALA A -12 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS A -11 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS A -10 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS A -9 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS A -8 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS A -7 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS A -6 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM VAL A -5 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP A -4 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP A -3 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP A -2 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP A -1 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM LYS A 0 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ALA A 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 3WZM MET B -13 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ALA B -12 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS B -11 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS B -10 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS B -9 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS B -8 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS B -7 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS B -6 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM VAL B -5 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP B -4 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP B -3 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP B -2 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP B -1 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM LYS B 0 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ALA B 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQADV 3WZM MET C -13 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ALA C -12 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS C -11 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS C -10 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS C -9 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS C -8 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS C -7 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM HIS C -6 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM VAL C -5 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP C -4 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP C -3 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP C -2 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ASP C -1 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM LYS C 0 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZM ALA C 102 UNP Q8NKB0 SER 102 ENGINEERED MUTATION
SEQRES 1 A 278 MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP
SEQRES 2 A 278 LYS MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY
SEQRES 3 A 278 ILE THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP
SEQRES 4 A 278 VAL VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 5 A 278 PHE ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE
SEQRES 6 A 278 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 7 A 278 ALA LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA
SEQRES 8 A 278 GLN LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA
SEQRES 9 A 278 LEU ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER
SEQRES 10 A 278 GLY ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO
SEQRES 11 A 278 ASP ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR
SEQRES 12 A 278 LYS LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU
SEQRES 13 A 278 ASP GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU
SEQRES 14 A 278 ASN ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET
SEQRES 15 A 278 GLY ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO
SEQRES 16 A 278 VAL TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER
SEQRES 17 A 278 ALA PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO
SEQRES 18 A 278 LEU ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER
SEQRES 19 A 278 PHE PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL
SEQRES 20 A 278 ASN ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL
SEQRES 21 A 278 SER HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 22 A 278 THR GLN LYS HIS LEU
SEQRES 1 B 278 MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP
SEQRES 2 B 278 LYS MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY
SEQRES 3 B 278 ILE THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP
SEQRES 4 B 278 VAL VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 5 B 278 PHE ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE
SEQRES 6 B 278 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 7 B 278 ALA LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA
SEQRES 8 B 278 GLN LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA
SEQRES 9 B 278 LEU ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER
SEQRES 10 B 278 GLY ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO
SEQRES 11 B 278 ASP ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR
SEQRES 12 B 278 LYS LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU
SEQRES 13 B 278 ASP GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU
SEQRES 14 B 278 ASN ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET
SEQRES 15 B 278 GLY ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO
SEQRES 16 B 278 VAL TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER
SEQRES 17 B 278 ALA PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO
SEQRES 18 B 278 LEU ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER
SEQRES 19 B 278 PHE PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL
SEQRES 20 B 278 ASN ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL
SEQRES 21 B 278 SER HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 22 B 278 THR GLN LYS HIS LEU
SEQRES 1 C 278 MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP
SEQRES 2 C 278 LYS MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY
SEQRES 3 C 278 ILE THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP
SEQRES 4 C 278 VAL VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET
SEQRES 5 C 278 PHE ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE
SEQRES 6 C 278 ARG VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER
SEQRES 7 C 278 ALA LYS ALA PRO PRO GLU THR TYR THR GLU VAL THR ALA
SEQRES 8 C 278 GLN LYS LEU ALA SER TYR VAL ILE SER VAL LEU ASP ALA
SEQRES 9 C 278 LEU ASP ILE LYS HIS ALA THR VAL TRP GLY CYS ALA SER
SEQRES 10 C 278 GLY ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO
SEQRES 11 C 278 ASP ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR
SEQRES 12 C 278 LYS LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU
SEQRES 13 C 278 ASP GLU GLU ILE SER LYS ILE LEU ALA ASN VAL MET LEU
SEQRES 14 C 278 ASN ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA MET
SEQRES 15 C 278 GLY ASP GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO
SEQRES 16 C 278 VAL TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER
SEQRES 17 C 278 ALA PRO VAL LYS ASP LEU GLU ALA LEU ARG GLY LYS PRO
SEQRES 18 C 278 LEU ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER
SEQRES 19 C 278 PHE PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL
SEQRES 20 C 278 ASN ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL
SEQRES 21 C 278 SER HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR
SEQRES 22 C 278 THR GLN LYS HIS LEU
HET ZER A 300 23
HET ZER B 300 23
HET ZER C 300 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 4 ZER 3(C18 H22 O5)
FORMUL 7 HOH *426(H2 O)
HELIX 1 1 GLU A 35 MET A 38 5 4
HELIX 2 2 PHE A 39 ALA A 48 1 10
HELIX 3 3 MET A 61 ALA A 65 5 5
HELIX 4 4 PRO A 68 TYR A 72 5 5
HELIX 5 5 THR A 76 ASP A 92 1 17
HELIX 6 6 ALA A 102 TYR A 115 1 14
HELIX 7 7 LEU A 132 ASN A 137 1 6
HELIX 8 8 THR A 138 LEU A 141 5 4
HELIX 9 9 GLU A 142 ASP A 157 1 16
HELIX 10 10 GLY A 161 ALA A 167 1 7
HELIX 11 11 GLY A 169 TYR A 187 1 19
HELIX 12 12 ILE A 191 ALA A 195 5 5
HELIX 13 13 ASP A 199 ARG A 204 1 6
HELIX 14 14 PRO A 217 GLY A 232 1 16
HELIX 15 15 PHE A 243 HIS A 248 1 6
HELIX 16 16 HIS A 248 LEU A 264 1 17
HELIX 17 17 GLU B 35 MET B 38 5 4
HELIX 18 18 PHE B 39 GLN B 49 1 11
HELIX 19 19 MET B 61 ALA B 65 5 5
HELIX 20 20 PRO B 68 TYR B 72 5 5
HELIX 21 21 THR B 76 LEU B 91 1 16
HELIX 22 22 ALA B 102 TYR B 115 1 14
HELIX 23 23 LEU B 132 ASN B 137 1 6
HELIX 24 24 THR B 138 LEU B 141 5 4
HELIX 25 25 GLU B 142 ASP B 157 1 16
HELIX 26 26 GLY B 161 ALA B 167 1 7
HELIX 27 27 GLY B 169 TYR B 187 1 19
HELIX 28 28 ILE B 191 ALA B 195 5 5
HELIX 29 29 ASP B 199 ARG B 204 1 6
HELIX 30 30 PRO B 217 ALA B 231 1 15
HELIX 31 31 PHE B 243 HIS B 248 1 6
HELIX 32 32 HIS B 248 LYS B 262 1 15
HELIX 33 33 GLU C 35 MET C 38 5 4
HELIX 34 34 PHE C 39 ILE C 46 1 8
HELIX 35 35 ALA C 47 GLY C 50 5 4
HELIX 36 36 PRO C 68 THR C 73 5 6
HELIX 37 37 THR C 76 LEU C 91 1 16
HELIX 38 38 ALA C 102 TYR C 115 1 14
HELIX 39 39 LEU C 132 ASN C 137 1 6
HELIX 40 40 GLU C 142 ASP C 157 1 16
HELIX 41 41 GLY C 161 ALA C 167 1 7
HELIX 42 42 MET C 168 TYR C 187 1 20
HELIX 43 43 THR C 190 ALA C 195 1 6
HELIX 44 44 ASP C 199 ARG C 204 1 6
HELIX 45 45 PHE C 221 GLY C 232 1 12
HELIX 46 46 PHE C 243 HIS C 248 1 6
HELIX 47 47 HIS C 248 LYS C 262 1 15
SHEET 1 A 8 THR A 3 THR A 9 0
SHEET 2 A 8 ILE A 13 GLU A 20 -1 O TRP A 15 N ILE A 7
SHEET 3 A 8 ARG A 52 PHE A 56 -1 O VAL A 53 N GLU A 20
SHEET 4 A 8 ASP A 25 VAL A 29 1 N LEU A 28 O THR A 54
SHEET 5 A 8 ALA A 96 CYS A 101 1 O THR A 97 N VAL A 27
SHEET 6 A 8 ILE A 119 HIS A 125 1 O MET A 123 N VAL A 98
SHEET 7 A 8 LEU A 208 GLY A 213 1 O ASP A 209 N CYS A 124
SHEET 8 A 8 ASN A 234 LEU A 238 1 O ASN A 234 N TRP A 210
SHEET 1 B 8 THR B 3 SER B 8 0
SHEET 2 B 8 THR B 14 GLU B 20 -1 O GLN B 19 N THR B 3
SHEET 3 B 8 ARG B 52 PHE B 56 -1 O VAL B 53 N GLU B 20
SHEET 4 B 8 ASP B 25 VAL B 29 1 N VAL B 26 O ARG B 52
SHEET 5 B 8 ALA B 96 CYS B 101 1 O THR B 97 N VAL B 27
SHEET 6 B 8 ILE B 119 HIS B 125 1 O HIS B 125 N GLY B 100
SHEET 7 B 8 LEU B 208 GLY B 213 1 O ASP B 209 N ALA B 122
SHEET 8 B 8 ASN B 234 LEU B 238 1 O ASN B 234 N TRP B 210
SHEET 1 C 8 THR C 3 SER C 8 0
SHEET 2 C 8 THR C 14 GLY C 21 -1 O TRP C 15 N ILE C 7
SHEET 3 C 8 ARG C 52 PHE C 56 -1 O VAL C 53 N GLU C 20
SHEET 4 C 8 ASP C 25 VAL C 29 1 N VAL C 26 O ARG C 52
SHEET 5 C 8 ALA C 96 CYS C 101 1 O TRP C 99 N VAL C 29
SHEET 6 C 8 ILE C 119 HIS C 125 1 O ASN C 121 N VAL C 98
SHEET 7 C 8 LEU C 208 GLY C 213 1 O THR C 211 N CYS C 124
SHEET 8 C 8 ASN C 234 LEU C 238 1 O ASN C 234 N TRP C 210
SITE 1 AC1 13 GLY A 32 LEU A 33 ALA A 102 SER A 103
SITE 2 AC1 13 PRO A 128 MET A 154 TRP A 183 TYR A 187
SITE 3 AC1 13 ILE A 191 PRO A 192 PHE A 221 HIS A 242
SITE 4 AC1 13 HOH A 601
SITE 1 AC2 11 GLY B 32 LEU B 33 ALA B 102 SER B 103
SITE 2 AC2 11 PRO B 128 MET B 154 TRP B 183 TYR B 187
SITE 3 AC2 11 ILE B 191 PRO B 192 HIS B 242
SITE 1 AC3 14 ASP C 31 GLY C 32 ALA C 102 SER C 103
SITE 2 AC3 14 PRO C 128 LEU C 135 MET C 154 TRP C 183
SITE 3 AC3 14 TYR C 187 PRO C 188 ILE C 191 PRO C 192
SITE 4 AC3 14 PHE C 221 HOH C 421
CRYST1 86.842 86.842 471.784 90.00 90.00 120.00 P 61 2 2 36
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 0.011515 0.006648 0.000000 0.00000
SCALE2 0.000000 0.013297 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002120 0.00000
TER 2022 LEU A 264
TER 4044 LEU B 264
TER 6066 LEU C 264
MASTER 636 0 3 47 24 0 11 6 6558 3 69 66
END |