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HEADER HYDROLASE 10-JAN-19 6QGC
TITLE PETASE FROM IDEONELLA SAKAIENSIS WITHOUT LIGAND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PET DEGRADATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.J.PALM,L.REISKY,D.BOETTCHER,H.MUELLER,E.A.P.MICHELS,C.WALCZAK,
AUTHOR 2 L.BERNDT,M.S.WEISS,U.T.BORNSCHEUER,G.WEBER
REVDAT 1 03-APR-19 6QGC 0
JRNL AUTH G.J.PALM,L.REISKY,D.BOETTCHER,H.MUELLER,E.A.P.MICHELS,
JRNL AUTH 2 C.WALCZAK,L.BERNDT,M.S.WEISS,U.T.BORNSCHEUER,G.WEBER
JRNL TITL STRUCTURE OF THE PLASTIC-DEGRADING I. SAKAIENSIS MHETASE
JRNL TITL 2 BOUND TO A SUBSTRATE
JRNL REF NAT COMMUN 2019
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-019-09326-3
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0230
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 3 NUMBER OF REFLECTIONS : 69684
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.261
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3607
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4823
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.11
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 262
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7688
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 19
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.30000
REMARK 3 B22 (A**2) : -2.11000
REMARK 3 B33 (A**2) : 0.78000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.33000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.183
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.164
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.568
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.925
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7902 ; 0.016 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 6728 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10780 ; 1.817 ; 1.656
REMARK 3 BOND ANGLES OTHERS (DEGREES): 15832 ; 1.052 ; 1.634
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1048 ; 7.406 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 360 ;32.802 ;21.556
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1148 ;13.874 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;17.402 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1085 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9151 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1473 ; 0.001 ; 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): 4186 ; 0.385 ; 0.810
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4185 ; 0.385 ; 0.810
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5227 ; 0.658 ; 1.213
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 5228 ; 0.658 ; 1.213
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3716 ; 0.587 ; 0.884
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3703 ; 0.517 ; 0.872
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5532 ; 0.826 ; 1.287
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8831 ; 4.467 ;10.311
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8766 ; 4.401 ;10.061
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 : 4
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 29 A 290
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3550 -14.6180 194.0830
REMARK 3 T TENSOR
REMARK 3 T11: 0.0067 T22: 0.2332
REMARK 3 T33: 0.2518 T12: -0.0057
REMARK 3 T13: -0.0373 T23: -0.0071
REMARK 3 L TENSOR
REMARK 3 L11: 1.0663 L22: 0.6538
REMARK 3 L33: 0.4528 L12: -0.2222
REMARK 3 L13: -0.1487 L23: -0.0775
REMARK 3 S TENSOR
REMARK 3 S11: -0.0019 S12: 0.0574 S13: -0.0479
REMARK 3 S21: -0.0291 S22: 0.0073 S23: 0.0502
REMARK 3 S31: -0.0003 S32: 0.0275 S33: -0.0054
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 29 B 289
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6970 -12.4240 222.6240
REMARK 3 T TENSOR
REMARK 3 T11: 0.0129 T22: 0.2326
REMARK 3 T33: 0.2618 T12: -0.0040
REMARK 3 T13: -0.0315 T23: -0.0056
REMARK 3 L TENSOR
REMARK 3 L11: 0.6480 L22: 0.6553
REMARK 3 L33: 0.5254 L12: 0.1800
REMARK 3 L13: -0.2104 L23: -0.2132
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: -0.0691 S13: -0.0259
REMARK 3 S21: 0.0730 S22: -0.0054 S23: 0.0264
REMARK 3 S31: -0.0287 S32: 0.0303 S33: -0.0173
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 28 C 289
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8830 -29.5730 264.3110
REMARK 3 T TENSOR
REMARK 3 T11: 0.0127 T22: 0.2203
REMARK 3 T33: 0.2574 T12: 0.0054
REMARK 3 T13: -0.0370 T23: -0.0010
REMARK 3 L TENSOR
REMARK 3 L11: 1.0816 L22: 0.8037
REMARK 3 L33: 0.4828 L12: -0.3261
REMARK 3 L13: -0.0678 L23: 0.0640
REMARK 3 S TENSOR
REMARK 3 S11: 0.0343 S12: 0.0602 S13: 0.0458
REMARK 3 S21: -0.0509 S22: -0.0059 S23: -0.0301
REMARK 3 S31: -0.0398 S32: -0.0364 S33: -0.0284
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 29 D 289
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5640 7.4680 267.1450
REMARK 3 T TENSOR
REMARK 3 T11: 0.0164 T22: 0.2291
REMARK 3 T33: 0.2546 T12: 0.0040
REMARK 3 T13: -0.0473 T23: -0.0019
REMARK 3 L TENSOR
REMARK 3 L11: 0.6043 L22: 0.5982
REMARK 3 L33: 0.4821 L12: -0.0973
REMARK 3 L13: 0.2066 L23: -0.1374
REMARK 3 S TENSOR
REMARK 3 S11: 0.0111 S12: 0.0584 S13: -0.0148
REMARK 3 S21: -0.0695 S22: -0.0163 S23: 0.0212
REMARK 3 S31: 0.0259 S32: 0.0331 S33: 0.0052
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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 6QGC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JAN-19.
REMARK 100 THE DEPOSITION ID IS D_1292100076.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUL-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PETRA III, EMBL C/O DESY
REMARK 200 BEAMLINE : P13 (MX1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9799
REMARK 200 MONOCHROMATOR : MIRROR
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JUN 1, 2017
REMARK 200 DATA SCALING SOFTWARE : XDS JUN 1, 2017
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 73090
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13100
REMARK 200 FOR THE DATA SET : 8.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.71900
REMARK 200 FOR SHELL : 1.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4CG1
REMARK 200
REMARK 200 REMARK: PLATES
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN (10 MG/ML, 20 MM TRIS PH
REMARK 280 7.5, 150 MM NACL) + 1 UL RESERVOIR (0.1 M SODIUM CITRATE OR
REMARK 280 SODIUM ACETATE PH 5.0, 15% (V/V) PEG8000, 0.5 M LITHIUM SULFATE),
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.38450
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 ASN A 2
REMARK 465 PHE A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 MET A 10
REMARK 465 GLN A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 VAL A 14
REMARK 465 LEU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 17
REMARK 465 LEU A 18
REMARK 465 MET A 19
REMARK 465 ALA A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 THR A 26
REMARK 465 ALA A 27
REMARK 465 GLN A 28
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 PHE B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 LEU B 9
REMARK 465 MET B 10
REMARK 465 GLN B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 VAL B 14
REMARK 465 LEU B 15
REMARK 465 GLY B 16
REMARK 465 GLY B 17
REMARK 465 LEU B 18
REMARK 465 MET B 19
REMARK 465 ALA B 20
REMARK 465 VAL B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 THR B 26
REMARK 465 ALA B 27
REMARK 465 GLN B 28
REMARK 465 SER B 290
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 PHE C 3
REMARK 465 PRO C 4
REMARK 465 ARG C 5
REMARK 465 ALA C 6
REMARK 465 SER C 7
REMARK 465 ARG C 8
REMARK 465 LEU C 9
REMARK 465 MET C 10
REMARK 465 GLN C 11
REMARK 465 ALA C 12
REMARK 465 ALA C 13
REMARK 465 VAL C 14
REMARK 465 LEU C 15
REMARK 465 GLY C 16
REMARK 465 GLY C 17
REMARK 465 LEU C 18
REMARK 465 MET C 19
REMARK 465 ALA C 20
REMARK 465 VAL C 21
REMARK 465 SER C 22
REMARK 465 ALA C 23
REMARK 465 ALA C 24
REMARK 465 ALA C 25
REMARK 465 THR C 26
REMARK 465 ALA C 27
REMARK 465 SER C 290
REMARK 465 MET D 1
REMARK 465 ASN D 2
REMARK 465 PHE D 3
REMARK 465 PRO D 4
REMARK 465 ARG D 5
REMARK 465 ALA D 6
REMARK 465 SER D 7
REMARK 465 ARG D 8
REMARK 465 LEU D 9
REMARK 465 MET D 10
REMARK 465 GLN D 11
REMARK 465 ALA D 12
REMARK 465 ALA D 13
REMARK 465 VAL D 14
REMARK 465 LEU D 15
REMARK 465 GLY D 16
REMARK 465 GLY D 17
REMARK 465 LEU D 18
REMARK 465 MET D 19
REMARK 465 ALA D 20
REMARK 465 VAL D 21
REMARK 465 SER D 22
REMARK 465 ALA D 23
REMARK 465 ALA D 24
REMARK 465 ALA D 25
REMARK 465 THR D 26
REMARK 465 ALA D 27
REMARK 465 GLN D 28
REMARK 465 SER D 290
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN C 28 CG CD OE1 NE2
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 A 175 O HOH A 401 2.12
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 280 NE - CZ - NH2 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG D 132 NE - CZ - NH1 ANGL. DEV. = -3.9 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 ASN A 73 48.61 -140.87
REMARK 500 THR A 88 -8.66 72.99
REMARK 500 SER A 160 -122.13 61.66
REMARK 500 SER A 214 -92.58 -121.05
REMARK 500 THR B 88 -4.75 68.17
REMARK 500 SER B 160 -121.48 66.79
REMARK 500 SER B 214 -72.77 -135.38
REMARK 500 ASP B 283 149.73 -174.46
REMARK 500 ASN C 73 39.32 -147.23
REMARK 500 THR C 88 -9.63 69.34
REMARK 500 SER C 160 -118.73 65.54
REMARK 500 SER C 214 -85.28 -129.40
REMARK 500 SER C 214 -80.29 -132.79
REMARK 500 THR D 88 -9.43 74.07
REMARK 500 SER D 160 -120.91 66.02
REMARK 500 ALA D 180 69.56 -151.09
REMARK 500 SER D 214 -82.16 -132.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 53 0.08 SIDE CHAIN
REMARK 500 ARG A 123 0.10 SIDE CHAIN
REMARK 500 ARG A 132 0.09 SIDE CHAIN
REMARK 500 ARG A 285 0.17 SIDE CHAIN
REMARK 500 ARG B 123 0.09 SIDE CHAIN
REMARK 500 ARG B 280 0.09 SIDE CHAIN
REMARK 500 ARG C 59 0.23 SIDE CHAIN
REMARK 500 ARG C 90 0.16 SIDE CHAIN
REMARK 500 ARG C 123 0.14 SIDE CHAIN
REMARK 500 ARG C 224 0.14 SIDE CHAIN
REMARK 500 ARG C 280 0.23 SIDE CHAIN
REMARK 500 ARG C 285 0.10 SIDE CHAIN
REMARK 500 ARG D 34 0.08 SIDE CHAIN
REMARK 500 ARG D 132 0.09 SIDE CHAIN
REMARK 500 ARG D 267 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 301
DBREF1 6QGC A 1 290 UNP PETH_IDESA
DBREF2 6QGC A A0A0K8P6T7 1 290
DBREF1 6QGC B 1 290 UNP PETH_IDESA
DBREF2 6QGC B A0A0K8P6T7 1 290
DBREF1 6QGC C 1 290 UNP PETH_IDESA
DBREF2 6QGC C A0A0K8P6T7 1 290
DBREF1 6QGC D 1 290 UNP PETH_IDESA
DBREF2 6QGC D A0A0K8P6T7 1 290
SEQRES 1 A 290 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 A 290 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 A 290 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 A 290 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 A 290 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 A 290 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 A 290 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 A 290 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 A 290 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 A 290 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 A 290 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 A 290 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 A 290 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 A 290 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 A 290 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 A 290 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 A 290 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 A 290 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 A 290 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 A 290 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 A 290 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 A 290 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 A 290 ALA ASN CYS SER
SEQRES 1 B 290 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 B 290 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 B 290 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 B 290 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 B 290 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 B 290 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 B 290 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 B 290 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 B 290 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 B 290 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 B 290 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 B 290 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 B 290 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 B 290 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 B 290 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 B 290 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 B 290 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 B 290 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 B 290 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 B 290 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 B 290 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 B 290 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 B 290 ALA ASN CYS SER
SEQRES 1 C 290 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 C 290 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 C 290 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 C 290 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 C 290 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 C 290 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 C 290 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 C 290 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 C 290 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 C 290 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 C 290 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 C 290 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 C 290 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 C 290 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 C 290 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 C 290 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 C 290 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 C 290 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 C 290 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 C 290 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 C 290 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 C 290 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 C 290 ALA ASN CYS SER
SEQRES 1 D 290 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 D 290 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 D 290 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 D 290 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 D 290 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 D 290 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 D 290 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 D 290 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 D 290 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 D 290 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 D 290 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 D 290 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 D 290 MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 D 290 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 D 290 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 D 290 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 D 290 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 D 290 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 D 290 GLY SER HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 D 290 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 D 290 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 D 290 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 D 290 ALA ASN CYS SER
HET SO4 A 301 5
HET CL A 302 1
HET CL B 301 1
HET SO4 C 301 5
HET SO4 C 302 5
HET CL C 303 1
HET CL D 301 1
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
FORMUL 5 SO4 3(O4 S 2-)
FORMUL 6 CL 4(CL 1-)
FORMUL 12 HOH *454(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 SER A 221 1 8
HELIX 7 AA7 ASN A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
HELIX 10 AB1 THR B 39 ALA B 45 1 7
HELIX 11 AB2 ARG B 90 LYS B 95 5 6
HELIX 12 AB3 TRP B 96 PHE B 106 1 11
HELIX 13 AB4 GLN B 119 GLY B 139 1 21
HELIX 14 AB5 SER B 160 ASN B 173 1 14
HELIX 15 AB6 PRO B 210 SER B 213 5 4
HELIX 16 AB7 SER B 214 MET B 222 1 9
HELIX 17 AB8 ASN B 246 ASP B 263 1 18
HELIX 18 AB9 ASP B 265 ARG B 267 5 3
HELIX 19 AC1 TYR B 268 GLU B 274 1 7
HELIX 20 AC2 THR C 39 ALA C 45 1 7
HELIX 21 AC3 ARG C 90 LYS C 95 5 6
HELIX 22 AC4 TRP C 96 PHE C 106 1 11
HELIX 23 AC5 GLN C 119 GLY C 139 1 21
HELIX 24 AC6 SER C 160 ASN C 173 1 14
HELIX 25 AC7 SER C 214 MET C 222 1 9
HELIX 26 AC8 ASN C 246 ASP C 263 1 18
HELIX 27 AC9 ASP C 265 ARG C 267 5 3
HELIX 28 AD1 TYR C 268 GLU C 274 1 7
HELIX 29 AD2 THR D 39 ALA D 45 1 7
HELIX 30 AD3 ARG D 90 LYS D 95 5 6
HELIX 31 AD4 TRP D 96 SER D 103 1 8
HELIX 32 AD5 GLN D 119 GLY D 139 1 21
HELIX 33 AD6 SER D 160 ASN D 173 1 14
HELIX 34 AD7 PRO D 210 SER D 213 5 4
HELIX 35 AD8 SER D 214 MET D 222 1 9
HELIX 36 AD9 ASN D 246 ASP D 263 1 18
HELIX 37 AE1 ASP D 265 ARG D 267 5 3
HELIX 38 AE2 TYR D 268 GLU D 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N GLY A 79 O VAL A 107
SHEET 5 AA1 6 VAL A 149 GLY A 158 1 O ASP A 150 N VAL A 78
SHEET 6 AA1 6 ALA A 178 ALA A 179 1 O ALA A 178 N VAL A 156
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ASP A 283 N GLU A 231
SHEET 1 AA3 6 VAL B 52 THR B 56 0
SHEET 2 AA3 6 ALA B 65 PRO B 71 -1 O VAL B 68 N PHE B 55
SHEET 3 AA3 6 VAL B 107 ASP B 112 -1 O VAL B 108 N TYR B 69
SHEET 4 AA3 6 VAL B 78 VAL B 84 1 N ILE B 81 O ILE B 109
SHEET 5 AA3 6 VAL B 149 GLY B 158 1 O ASP B 150 N VAL B 78
SHEET 6 AA3 6 ALA B 178 ALA B 179 1 O ALA B 178 N VAL B 156
SHEET 1 AA4 3 THR B 198 CYS B 203 0
SHEET 2 AA4 3 LYS B 227 ILE B 232 1 O ILE B 232 N ALA B 202
SHEET 3 AA4 3 VAL B 281 ALA B 287 -1 O ASP B 283 N GLU B 231
SHEET 1 AA5 6 VAL C 52 THR C 56 0
SHEET 2 AA5 6 ALA C 65 PRO C 71 -1 O TYR C 70 N ARG C 53
SHEET 3 AA5 6 VAL C 107 ASP C 112 -1 O VAL C 108 N TYR C 69
SHEET 4 AA5 6 VAL C 78 VAL C 84 1 N ILE C 81 O VAL C 107
SHEET 5 AA5 6 VAL C 149 TRP C 159 1 O ASP C 150 N VAL C 78
SHEET 6 AA5 6 ALA C 178 GLN C 182 1 O GLN C 182 N GLY C 158
SHEET 1 AA6 3 THR C 198 CYS C 203 0
SHEET 2 AA6 3 LYS C 227 ILE C 232 1 O LEU C 230 N ALA C 202
SHEET 3 AA6 3 VAL C 281 ALA C 287 -1 O ASP C 283 N GLU C 231
SHEET 1 AA7 6 VAL D 52 THR D 56 0
SHEET 2 AA7 6 ALA D 65 PRO D 71 -1 O VAL D 68 N PHE D 55
SHEET 3 AA7 6 VAL D 107 ASP D 112 -1 O VAL D 108 N TYR D 69
SHEET 4 AA7 6 VAL D 78 VAL D 84 1 N ILE D 81 O VAL D 107
SHEET 5 AA7 6 VAL D 149 GLY D 158 1 O ASP D 150 N VAL D 78
SHEET 6 AA7 6 ALA D 178 ALA D 179 1 O ALA D 178 N VAL D 156
SHEET 1 AA8 3 THR D 198 CYS D 203 0
SHEET 2 AA8 3 LYS D 227 ILE D 232 1 O ILE D 232 N ALA D 202
SHEET 3 AA8 3 VAL D 281 ALA D 287 -1 O ASP D 283 N GLU D 231
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.04
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.10
SSBOND 3 CYS B 203 CYS B 239 1555 1555 2.10
SSBOND 4 CYS B 273 CYS B 289 1555 1555 2.12
SSBOND 5 CYS C 203 CYS C 239 1555 1555 2.05
SSBOND 6 CYS C 273 CYS C 289 1555 1555 2.10
SSBOND 7 CYS D 203 CYS D 239 1555 1555 2.10
SSBOND 8 CYS D 273 CYS D 289 1555 1555 2.13
SITE 1 AC1 7 GLN A 119 PRO A 120 SER A 121 HOH A 412
SITE 2 AC1 7 HOH A 414 HOH A 425 HOH A 483
SITE 1 AC2 4 TYR A 87 SER A 160 MET A 161 ARG B 132
SITE 1 AC3 4 TYR B 87 SER B 160 MET B 161 HOH B 450
SITE 1 AC4 6 GLN C 119 PRO C 120 SER C 121 HOH C 420
SITE 2 AC4 6 HOH C 436 HOH C 455
SITE 1 AC5 5 SER C 92 LYS C 95 HOH C 403 HOH C 494
SITE 2 AC5 5 ARG D 53
SITE 1 AC6 3 TYR C 87 SER C 160 MET C 161
SITE 1 AC7 4 TYR D 87 SER D 160 MET D 161 HOH D 428
CRYST1 51.121 78.769 140.121 90.00 92.56 90.00 P 1 21 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 0.019561 0.000000 0.000876 0.00000
SCALE2 0.000000 0.012695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007144 0.00000
TER 1927 SER A 290
TER 3851 CYS B 289
TER 5779 CYS C 289
TER 7702 CYS D 289
MASTER 572 0 7 38 36 0 10 6 8161 4 31 92
END |