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HEADER HYDROLASE 01-OCT-14 3WZL
TITLE ZEN LACTONASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: 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 3WZL 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. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 31238
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) : 0.213
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.266
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1635
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3907
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE SET COUNT : 186
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6066
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 235
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 74.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.05000
REMARK 3 B22 (A**2) : 4.05000
REMARK 3 B33 (A**2) : -6.07000
REMARK 3 B12 (A**2) : 2.02000
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): 0.567
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.316
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.229
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.924
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.897
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6219 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8496 ; 1.677 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 789 ; 6.660 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 249 ;37.783 ;24.096
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 978 ;17.559 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;14.409 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 972 ; 0.110 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4719 ; 0.007 ; 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 ; 0.860 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6423 ; 1.640 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2262 ; 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): 2073 ; 3.904 ; 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 : 1
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 ; 0.390 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1056 ; 0.230 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1056 ; 0.240 ; 0.500
REMARK 3 LOOSE POSITIONAL 1 C (A): 966 ; 0.690 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 A (A): 966 ; 0.460 ; 5.000
REMARK 3 LOOSE POSITIONAL 1 B (A): 966 ; 0.530 ; 5.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1056 ;32.400 ; 2.000
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1056 ;16.790 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1056 ;16.360 ; 2.000
REMARK 3 LOOSE THERMAL 1 C (A**2): 966 ;31.510 ;10.000
REMARK 3 LOOSE THERMAL 1 A (A**2): 966 ;16.340 ;10.000
REMARK 3 LOOSE THERMAL 1 B (A**2): 966 ;16.050 ;10.000
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 264
REMARK 3 ORIGIN FOR THE GROUP (A): -17.7091 18.1579 11.3335
REMARK 3 T TENSOR
REMARK 3 T11: 0.5409 T22: 0.2679
REMARK 3 T33: 0.2894 T12: 0.0727
REMARK 3 T13: 0.0336 T23: -0.0223
REMARK 3 L TENSOR
REMARK 3 L11: 0.6505 L22: 0.1260
REMARK 3 L33: 1.8377 L12: -0.0109
REMARK 3 L13: -0.1785 L23: -0.0097
REMARK 3 S TENSOR
REMARK 3 S11: -0.1611 S12: 0.1100 S13: -0.0209
REMARK 3 S21: 0.1356 S22: 0.1847 S23: 0.0033
REMARK 3 S31: -0.0553 S32: 0.0357 S33: -0.0235
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 264
REMARK 3 ORIGIN FOR THE GROUP (A): -7.9615 26.1668 -27.5081
REMARK 3 T TENSOR
REMARK 3 T11: 0.4443 T22: 0.3221
REMARK 3 T33: 0.3051 T12: -0.2347
REMARK 3 T13: 0.0458 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 0.3172 L22: 0.3318
REMARK 3 L33: 1.8870 L12: 0.2870
REMARK 3 L13: -0.4779 L23: -0.1908
REMARK 3 S TENSOR
REMARK 3 S11: 0.0191 S12: 0.0852 S13: -0.0502
REMARK 3 S21: 0.0360 S22: 0.1162 S23: -0.0384
REMARK 3 S31: -0.1346 S32: -0.0468 S33: -0.1353
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 264
REMARK 3 ORIGIN FOR THE GROUP (A): -49.1470 3.5492 -19.8835
REMARK 3 T TENSOR
REMARK 3 T11: 0.1065 T22: 0.4426
REMARK 3 T33: 1.2370 T12: -0.1850
REMARK 3 T13: -0.2009 T23: 0.4156
REMARK 3 L TENSOR
REMARK 3 L11: 1.3652 L22: 1.1768
REMARK 3 L33: 4.8260 L12: -1.2193
REMARK 3 L13: -0.9869 L23: 0.4614
REMARK 3 S TENSOR
REMARK 3 S11: 0.0607 S12: 0.0251 S13: -0.4938
REMARK 3 S21: -0.1371 S22: 0.1288 S23: 0.4718
REMARK 3 S31: 0.1113 S32: -0.9287 S33: -0.1895
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 3WZL 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 RCSB096991.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-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 : 33747
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 9.100
REMARK 200 R MERGE (I) : 0.06500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 37.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.24200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.17
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, VAPOR DIFFUSION, SITTING DROP
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 158.00533
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 316.01067
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 237.00800
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 395.01333
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 79.00267
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 158.00533
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 316.01067
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 395.01333
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 237.00800
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 79.00267
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: 1240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20480 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL
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 A 387 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 316 LIES ON A SPECIAL POSITION.
REMARK 375 HOH C 309 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 N MET A 1 O HOH A 333 2.13
REMARK 500 O HOH B 354 O HOH B 368 2.18
REMARK 500 OD2 ASP A 25 O HOH A 343 2.18
REMARK 500 O HOH B 348 O HOH B 399 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS B 124 CB CYS B 124 SG -0.099
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. = -3.1 DEGREES
REMARK 500 PRO C 24 C - N - CA ANGL. DEV. = 9.3 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 ALA A 48 14.22 -62.36
REMARK 500 PHE A 56 142.41 -171.50
REMARK 500 SER A 62 -132.42 36.71
REMARK 500 GLU A 74 52.63 36.01
REMARK 500 SER A 102 -138.11 63.09
REMARK 500 ALA A 167 0.28 -69.95
REMARK 500 PRO A 196 34.36 -79.55
REMARK 500 MET A 241 -118.00 -143.73
REMARK 500 ASP B 31 -169.84 -76.06
REMARK 500 SER B 62 -124.12 39.78
REMARK 500 SER B 102 -120.50 61.12
REMARK 500 MET B 241 -112.73 -132.83
REMARK 500 ARG C 4 77.23 -112.43
REMARK 500 ASP C 31 -158.73 -72.86
REMARK 500 LEU C 33 -6.10 -54.33
REMARK 500 ALA C 48 3.24 -67.76
REMARK 500 SER C 62 -116.92 43.29
REMARK 500 TYR C 72 10.17 -150.39
REMARK 500 ALA C 81 -35.67 -38.90
REMARK 500 ASP C 92 46.08 39.17
REMARK 500 SER C 102 -103.30 35.65
REMARK 500 GLU C 126 65.62 71.81
REMARK 500 LEU C 131 92.87 -68.97
REMARK 500 ASN C 137 36.37 -67.51
REMARK 500 THR C 138 -45.38 -130.69
REMARK 500 SER C 147 35.83 -83.13
REMARK 500 LYS C 148 -36.87 -145.65
REMARK 500 SER C 159 -91.94 -78.68
REMARK 500 PRO C 196 19.35 -63.37
REMARK 500 VAL C 197 57.51 -117.02
REMARK 500 ARG C 204 107.53 -59.59
REMARK 500 PRO C 207 84.68 -63.75
REMARK 500 ALA C 214 -73.47 -18.33
REMARK 500 PHE C 221 44.47 -141.08
REMARK 500 THR C 227 -40.93 -136.38
REMARK 500 ALA C 228 -72.05 -46.15
REMARK 500 MET C 241 -105.51 -123.83
REMARK 500 VAL C 246 -42.93 -136.88
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 316 DISTANCE = 5.19 ANGSTROMS
REMARK 525 HOH A 328 DISTANCE = 5.42 ANGSTROMS
REMARK 525 HOH A 371 DISTANCE = 6.60 ANGSTROMS
REMARK 525 HOH A 372 DISTANCE = 7.87 ANGSTROMS
REMARK 525 HOH A 378 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 381 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH A 382 DISTANCE = 6.43 ANGSTROMS
REMARK 525 HOH A 383 DISTANCE = 6.31 ANGSTROMS
REMARK 525 HOH A 388 DISTANCE = 5.10 ANGSTROMS
REMARK 525 HOH A 399 DISTANCE = 5.38 ANGSTROMS
REMARK 525 HOH A 403 DISTANCE = 6.24 ANGSTROMS
REMARK 525 HOH B 339 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH B 362 DISTANCE = 5.74 ANGSTROMS
REMARK 525 HOH B 376 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 377 DISTANCE = 7.94 ANGSTROMS
REMARK 525 HOH B 379 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B 389 DISTANCE = 7.58 ANGSTROMS
REMARK 525 HOH B 396 DISTANCE = 7.69 ANGSTROMS
REMARK 525 HOH C 303 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH C 316 DISTANCE = 8.74 ANGSTROMS
REMARK 525 HOH C 317 DISTANCE = 8.86 ANGSTROMS
REMARK 525 HOH C 319 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH C 320 DISTANCE = 6.51 ANGSTROMS
REMARK 525 HOH C 321 DISTANCE = 5.25 ANGSTROMS
REMARK 525 HOH C 325 DISTANCE = 5.41 ANGSTROMS
REMARK 525 HOH C 326 DISTANCE = 5.39 ANGSTROMS
REMARK 525 HOH C 327 DISTANCE = 6.79 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WZM RELATED DB: PDB
DBREF 3WZL A 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 3WZL B 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 3WZL C 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
SEQADV 3WZL MET A -13 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ALA A -12 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS A -11 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS A -10 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS A -9 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS A -8 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS A -7 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS A -6 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL VAL A -5 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP A -4 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP A -3 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP A -2 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP A -1 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL LYS A 0 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL MET B -13 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ALA B -12 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS B -11 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS B -10 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS B -9 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS B -8 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS B -7 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS B -6 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL VAL B -5 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP B -4 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP B -3 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP B -2 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP B -1 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL LYS B 0 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL MET C -13 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ALA C -12 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS C -11 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS C -10 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS C -9 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS C -8 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS C -7 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL HIS C -6 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL VAL C -5 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP C -4 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP C -3 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP C -2 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL ASP C -1 UNP Q8NKB0 EXPRESSION TAG
SEQADV 3WZL LYS C 0 UNP Q8NKB0 EXPRESSION TAG
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 SER 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 SER 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 SER 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
FORMUL 4 HOH *235(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 LEU A 91 1 16
HELIX 6 6 SER 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 HIS A 263 1 16
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 SER 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 VAL B 158 1 17
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 LEU B 264 1 17
HELIX 33 33 PHE C 39 ALA C 48 1 10
HELIX 34 34 PRO C 68 TYR C 72 5 5
HELIX 35 35 THR C 76 ALA C 90 1 15
HELIX 36 36 SER C 102 TYR C 115 1 14
HELIX 37 37 LEU C 132 ASN C 137 1 6
HELIX 38 38 GLU C 145 ASP C 157 1 13
HELIX 39 39 TRP C 165 MET C 168 5 4
HELIX 40 40 GLY C 169 TYR C 187 1 19
HELIX 41 41 ASP C 199 ARG C 204 1 6
HELIX 42 42 PRO C 217 PHE C 222 1 6
HELIX 43 43 ASN C 224 THR C 229 1 6
HELIX 44 44 LYS C 230 GLY C 232 5 3
HELIX 45 45 PHE C 243 HIS C 248 1 6
HELIX 46 46 PRO C 249 LYS C 262 1 14
SHEET 1 A 8 THR A 3 SER A 8 0
SHEET 2 A 8 THR A 14 GLU A 20 -1 O TYR A 17 N SER A 5
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 VAL A 26 O ARG A 52
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 ARG B 2 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 THR B 54
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 MET B 123 N VAL B 98
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 5 TYR C 17 GLU C 20 0
SHEET 2 C 5 ARG C 52 PHE C 56 -1 O THR C 55 N GLU C 18
SHEET 3 C 5 ASP C 25 VAL C 29 1 N VAL C 26 O THR C 54
SHEET 4 C 5 ALA C 96 CYS C 101 1 O TRP C 99 N VAL C 29
SHEET 5 C 5 CYS C 124 HIS C 125 1 O HIS C 125 N GLY C 100
SHEET 1 D 2 ASP C 209 VAL C 212 0
SHEET 2 D 2 ASN C 234 LEU C 237 1 O ASN C 234 N TRP C 210
CRYST1 86.637 86.637 474.016 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 0.011542 0.006664 0.000000 0.00000
SCALE2 0.000000 0.013328 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002110 0.00000
TER 2023 LEU A 264
TER 4046 LEU B 264
TER 6069 LEU C 264
MASTER 568 0 0 46 23 0 0 6 6301 3 0 66
END |