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HEADER HYDROLASE 30-JUN-17 5XWZ
TITLE CRYSTAL STRUCTURE OF A LACTONASE FROM CLADOPHIALOPHORA BANTIANA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNPLACED GENOMIC SCAFFOLD SUPERCONT1.36, WHOLE GENOME
COMPND 3 SHOTGUN SEQUENCE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLADOPHIALOPHORA BANTIANA CBS 173.52;
SOURCE 3 ORGANISM_TAXID: 1442370;
SOURCE 4 GENE: Z519_12792;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-46 EK/LIC
KEYWDS ALPHA/BETA-HYDROLASE, LACTONASE, ZEARALENONE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.Y.ZHENG,W.T.LIU,W.D.LIU,C.C.CHEN,R.T.GUO
REVDAT 1 02-MAY-18 5XWZ 0
JRNL AUTH R.HUI,X.HU,W.LIU,W.LIU,Y.ZHENG,Y.CHEN,R.T.GUO,J.JIN,C.C.CHEN
JRNL TITL CHARACTERIZATION AND CRYSTAL STRUCTURE OF A NOVEL
JRNL TITL 2 ZEARALENONE HYDROLASE FROM CLADOPHIALOPHORA BANTIANA
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 73 515 2017
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 28876230
JRNL DOI 10.1107/S2053230X17011840
REMARK 2
REMARK 2 RESOLUTION. 1.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 141307
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7478
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10303
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.2370
REMARK 3 BIN FREE R VALUE SET COUNT : 533
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8096
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 1061
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.68
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.13000
REMARK 3 B22 (A**2) : 0.78000
REMARK 3 B33 (A**2) : -0.91000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.082
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.057
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.811
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.964
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8356 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7526 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11392 ; 1.485 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17509 ; 0.851 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1046 ; 7.068 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 360 ;38.173 ;23.778
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1292 ;14.419 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;13.514 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1249 ; 0.132 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9363 ; 0.015 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1681 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5XWZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1300004284.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-OCT-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : BL15A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 148988
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.48000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3WZL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM MALONATE, 0.1M BIS-TRIS
REMARK 280 PROPANE PH 7.0, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 60.43150
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.19950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 60.43150
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.19950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 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: 2090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 PRO A 3
REMARK 465 ASN A 137
REMARK 465 LEU A 138
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 PRO C 3
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 PRO D 3
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 HOH C 569 O HOH C 634 1.62
REMARK 500 O HOH C 423 O HOH C 620 1.68
REMARK 500 O HOH C 410 O HOH C 634 1.74
REMARK 500 O HOH A 580 O HOH A 616 1.85
REMARK 500 O HOH D 515 O HOH D 540 1.86
REMARK 500 O HOH C 490 O HOH D 544 1.87
REMARK 500 O HOH B 560 O HOH B 596 1.94
REMARK 500 O HOH C 565 O HOH C 574 1.96
REMARK 500 O HOH C 619 O HOH C 667 1.97
REMARK 500 O HOH D 507 O HOH D 547 1.99
REMARK 500 O HOH B 472 O HOH B 601 2.02
REMARK 500 O HOH A 638 O HOH A 666 2.02
REMARK 500 O HOH D 425 O HOH D 509 2.03
REMARK 500 O HOH B 531 O HOH B 615 2.05
REMARK 500 O HOH C 604 O HOH C 667 2.08
REMARK 500 OD2 ASP D 14 O HOH D 401 2.10
REMARK 500 O HOH C 598 O HOH D 536 2.12
REMARK 500 O HOH C 525 O HOH C 581 2.12
REMARK 500 O HOH A 645 O HOH C 637 2.14
REMARK 500 NE ARG A 7 O HOH A 401 2.14
REMARK 500 O HOH D 465 O HOH D 511 2.16
REMARK 500 O HOH D 510 O HOH D 567 2.16
REMARK 500 O HOH A 490 O HOH A 642 2.19
REMARK 500 O HOH C 611 O HOH C 620 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 470 O HOH B 470 2755 1.48
REMARK 500 O HOH A 605 O HOH D 512 2755 2.08
REMARK 500 O HOH A 599 O HOH C 526 4556 2.14
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 191 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 THR B 132 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 PRO C 135 C - N - CA ANGL. DEV. = 12.0 DEGREES
REMARK 500 PRO C 135 C - N - CD ANGL. DEV. = -14.8 DEGREES
REMARK 500 ARG C 151 NE - CZ - NH2 ANGL. DEV. = 3.3 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 SER A 65 -126.48 49.69
REMARK 500 SER A 105 -130.43 65.97
REMARK 500 ASP A 143 42.86 -96.92
REMARK 500 ASN A 163 83.70 -151.35
REMARK 500 PHE A 242 -113.45 -143.82
REMARK 500 ASP B 34 -179.65 -60.57
REMARK 500 SER B 65 -124.96 52.25
REMARK 500 SER B 105 -127.61 62.48
REMARK 500 ALA B 162 9.63 57.26
REMARK 500 ASN B 163 81.73 -155.25
REMARK 500 PHE B 242 -105.99 -132.46
REMARK 500 ASP C 34 -179.73 -66.15
REMARK 500 SER C 65 -124.46 49.21
REMARK 500 SER C 105 -129.38 66.63
REMARK 500 PRO C 135 -16.58 -32.63
REMARK 500 GLU C 136 -69.50 65.12
REMARK 500 ALA C 162 14.42 56.65
REMARK 500 ASN C 163 88.92 -157.75
REMARK 500 PHE C 242 -103.77 -134.53
REMARK 500 SER D 65 -123.90 48.74
REMARK 500 SER D 105 -126.04 62.29
REMARK 500 GLU D 129 70.64 47.98
REMARK 500 ALA D 162 11.30 55.80
REMARK 500 ASN D 163 80.16 -157.36
REMARK 500 PHE D 242 -106.01 -134.71
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 B 682 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH C 696 DISTANCE = 5.96 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO A 119 O
REMARK 620 2 VAL A 122 O 90.1
REMARK 620 3 HOH A 552 O 155.4 87.5
REMARK 620 4 HOH A 581 O 79.2 169.2 102.7
REMARK 620 5 HOH A 621 O 92.3 107.1 111.8 72.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 303 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO B 119 O
REMARK 620 2 VAL B 122 O 87.2
REMARK 620 3 HOH B 614 O 91.6 167.9
REMARK 620 4 HOH B 622 O 103.1 91.4 100.7
REMARK 620 5 HOH B 620 O 154.9 88.5 87.5 101.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA C 301 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PRO C 119 O
REMARK 620 2 VAL C 122 O 91.2
REMARK 620 3 HOH C 552 O 159.1 84.2
REMARK 620 4 HOH C 581 O 81.2 172.0 102.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA D 302 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER D 65 O
REMARK 620 2 SER D 68 OG 80.8
REMARK 620 3 HOH D 563 O 89.7 84.9
REMARK 620 4 HOH D 552 O 164.1 84.3 94.3
REMARK 620 5 HOH D 538 O 83.6 162.1 86.3 112.0
REMARK 620 6 HOH D 550 O 90.5 90.1 174.9 84.2 98.7
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA D 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MLI D 303
DBREF1 5XWZ A 1 265 UNP A0A0D2H023_XYLBA
DBREF2 5XWZ A A0A0D2H023 1 265
DBREF1 5XWZ B 1 265 UNP A0A0D2H023_XYLBA
DBREF2 5XWZ B A0A0D2H023 1 265
DBREF1 5XWZ C 1 265 UNP A0A0D2H023_XYLBA
DBREF2 5XWZ C A0A0D2H023 1 265
DBREF1 5XWZ D 1 265 UNP A0A0D2H023_XYLBA
DBREF2 5XWZ D A0A0D2H023 1 265
SEQADV 5XWZ HIS A -5 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS A -4 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS A -3 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS A -2 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS A -1 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS A 0 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS B -5 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS B -4 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS B -3 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS B -2 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS B -1 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS B 0 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS C -5 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS C -4 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS C -3 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS C -2 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS C -1 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS C 0 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS D -5 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS D -4 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS D -3 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS D -2 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS D -1 UNP A0A0D2H02 EXPRESSION TAG
SEQADV 5XWZ HIS D 0 UNP A0A0D2H02 EXPRESSION TAG
SEQRES 1 A 271 HIS HIS HIS HIS HIS HIS MET ALA PRO GLU ARG LEU ARG
SEQRES 2 A 271 SER THR ILE LEU THR LYS ASP GLY ILE ASN TRP TYR TYR
SEQRES 3 A 271 GLU GLN GLU GLY SER GLY PRO ASP VAL VAL LEU ILE PRO
SEQRES 4 A 271 ASP GLY LEU GLY ASP CYS GLN MET PHE ASP LYS PRO MET
SEQRES 5 A 271 SER ILE ILE GLY SER SER GLY PHE LYS VAL THR THR PHE
SEQRES 6 A 271 ASP MET PRO GLY MET SER ARG SER SER SER ALA PRO PRO
SEQRES 7 A 271 GLU THR TYR GLN ASP VAL THR GLY GLN LYS LEU ALA ASN
SEQRES 8 A 271 TYR ILE VAL THR VAL MET ASP GLN LEU GLY ILE LYS THR
SEQRES 9 A 271 ALA SER VAL TRP GLY CYS SER SER GLY ALA SER THR VAL
SEQRES 10 A 271 LEU ALA LEU CYS SER GLY PHE PRO GLU ARG VAL ARG ASN
SEQRES 11 A 271 GLY MET PRO HIS GLU VAL PRO THR ALA ASN PRO GLU ASN
SEQRES 12 A 271 LEU GLN ASN ILE HIS ASP ALA ASP PRO ALA THR ILE SER
SEQRES 13 A 271 ARG ASP MET ALA ALA VAL SER ARG ALA MET SER ALA ASN
SEQRES 14 A 271 GLU GLU ALA TRP ASP ALA LEU GLY PRO GLU VAL HIS GLU
SEQRES 15 A 271 ARG LEU ARG ASP ASN TYR VAL ARG TRP ALA TYR GLY TYR
SEQRES 16 A 271 PRO ARG THR ILE PRO GLY SER ALA ALA THR LYS THR GLU
SEQRES 17 A 271 ASP LEU HIS LYS VAL PRO ILE ASP TRP THR VAL GLY ALA
SEQRES 18 A 271 ALA GLY PRO THR GLN VAL PHE PHE GLU ASN VAL VAL ILE
SEQRES 19 A 271 ALA THR ARG GLU SER ILE PRO ILE LYS THR LEU PRO GLY
SEQRES 20 A 271 PHE HIS PHE PRO TYR VAL SER HIS PRO GLU ALA PHE ALA
SEQRES 21 A 271 LYS TYR VAL VAL GLU THR THR ARG LYS TYR LEU
SEQRES 1 B 271 HIS HIS HIS HIS HIS HIS MET ALA PRO GLU ARG LEU ARG
SEQRES 2 B 271 SER THR ILE LEU THR LYS ASP GLY ILE ASN TRP TYR TYR
SEQRES 3 B 271 GLU GLN GLU GLY SER GLY PRO ASP VAL VAL LEU ILE PRO
SEQRES 4 B 271 ASP GLY LEU GLY ASP CYS GLN MET PHE ASP LYS PRO MET
SEQRES 5 B 271 SER ILE ILE GLY SER SER GLY PHE LYS VAL THR THR PHE
SEQRES 6 B 271 ASP MET PRO GLY MET SER ARG SER SER SER ALA PRO PRO
SEQRES 7 B 271 GLU THR TYR GLN ASP VAL THR GLY GLN LYS LEU ALA ASN
SEQRES 8 B 271 TYR ILE VAL THR VAL MET ASP GLN LEU GLY ILE LYS THR
SEQRES 9 B 271 ALA SER VAL TRP GLY CYS SER SER GLY ALA SER THR VAL
SEQRES 10 B 271 LEU ALA LEU CYS SER GLY PHE PRO GLU ARG VAL ARG ASN
SEQRES 11 B 271 GLY MET PRO HIS GLU VAL PRO THR ALA ASN PRO GLU ASN
SEQRES 12 B 271 LEU GLN ASN ILE HIS ASP ALA ASP PRO ALA THR ILE SER
SEQRES 13 B 271 ARG ASP MET ALA ALA VAL SER ARG ALA MET SER ALA ASN
SEQRES 14 B 271 GLU GLU ALA TRP ASP ALA LEU GLY PRO GLU VAL HIS GLU
SEQRES 15 B 271 ARG LEU ARG ASP ASN TYR VAL ARG TRP ALA TYR GLY TYR
SEQRES 16 B 271 PRO ARG THR ILE PRO GLY SER ALA ALA THR LYS THR GLU
SEQRES 17 B 271 ASP LEU HIS LYS VAL PRO ILE ASP TRP THR VAL GLY ALA
SEQRES 18 B 271 ALA GLY PRO THR GLN VAL PHE PHE GLU ASN VAL VAL ILE
SEQRES 19 B 271 ALA THR ARG GLU SER ILE PRO ILE LYS THR LEU PRO GLY
SEQRES 20 B 271 PHE HIS PHE PRO TYR VAL SER HIS PRO GLU ALA PHE ALA
SEQRES 21 B 271 LYS TYR VAL VAL GLU THR THR ARG LYS TYR LEU
SEQRES 1 C 271 HIS HIS HIS HIS HIS HIS MET ALA PRO GLU ARG LEU ARG
SEQRES 2 C 271 SER THR ILE LEU THR LYS ASP GLY ILE ASN TRP TYR TYR
SEQRES 3 C 271 GLU GLN GLU GLY SER GLY PRO ASP VAL VAL LEU ILE PRO
SEQRES 4 C 271 ASP GLY LEU GLY ASP CYS GLN MET PHE ASP LYS PRO MET
SEQRES 5 C 271 SER ILE ILE GLY SER SER GLY PHE LYS VAL THR THR PHE
SEQRES 6 C 271 ASP MET PRO GLY MET SER ARG SER SER SER ALA PRO PRO
SEQRES 7 C 271 GLU THR TYR GLN ASP VAL THR GLY GLN LYS LEU ALA ASN
SEQRES 8 C 271 TYR ILE VAL THR VAL MET ASP GLN LEU GLY ILE LYS THR
SEQRES 9 C 271 ALA SER VAL TRP GLY CYS SER SER GLY ALA SER THR VAL
SEQRES 10 C 271 LEU ALA LEU CYS SER GLY PHE PRO GLU ARG VAL ARG ASN
SEQRES 11 C 271 GLY MET PRO HIS GLU VAL PRO THR ALA ASN PRO GLU ASN
SEQRES 12 C 271 LEU GLN ASN ILE HIS ASP ALA ASP PRO ALA THR ILE SER
SEQRES 13 C 271 ARG ASP MET ALA ALA VAL SER ARG ALA MET SER ALA ASN
SEQRES 14 C 271 GLU GLU ALA TRP ASP ALA LEU GLY PRO GLU VAL HIS GLU
SEQRES 15 C 271 ARG LEU ARG ASP ASN TYR VAL ARG TRP ALA TYR GLY TYR
SEQRES 16 C 271 PRO ARG THR ILE PRO GLY SER ALA ALA THR LYS THR GLU
SEQRES 17 C 271 ASP LEU HIS LYS VAL PRO ILE ASP TRP THR VAL GLY ALA
SEQRES 18 C 271 ALA GLY PRO THR GLN VAL PHE PHE GLU ASN VAL VAL ILE
SEQRES 19 C 271 ALA THR ARG GLU SER ILE PRO ILE LYS THR LEU PRO GLY
SEQRES 20 C 271 PHE HIS PHE PRO TYR VAL SER HIS PRO GLU ALA PHE ALA
SEQRES 21 C 271 LYS TYR VAL VAL GLU THR THR ARG LYS TYR LEU
SEQRES 1 D 271 HIS HIS HIS HIS HIS HIS MET ALA PRO GLU ARG LEU ARG
SEQRES 2 D 271 SER THR ILE LEU THR LYS ASP GLY ILE ASN TRP TYR TYR
SEQRES 3 D 271 GLU GLN GLU GLY SER GLY PRO ASP VAL VAL LEU ILE PRO
SEQRES 4 D 271 ASP GLY LEU GLY ASP CYS GLN MET PHE ASP LYS PRO MET
SEQRES 5 D 271 SER ILE ILE GLY SER SER GLY PHE LYS VAL THR THR PHE
SEQRES 6 D 271 ASP MET PRO GLY MET SER ARG SER SER SER ALA PRO PRO
SEQRES 7 D 271 GLU THR TYR GLN ASP VAL THR GLY GLN LYS LEU ALA ASN
SEQRES 8 D 271 TYR ILE VAL THR VAL MET ASP GLN LEU GLY ILE LYS THR
SEQRES 9 D 271 ALA SER VAL TRP GLY CYS SER SER GLY ALA SER THR VAL
SEQRES 10 D 271 LEU ALA LEU CYS SER GLY PHE PRO GLU ARG VAL ARG ASN
SEQRES 11 D 271 GLY MET PRO HIS GLU VAL PRO THR ALA ASN PRO GLU ASN
SEQRES 12 D 271 LEU GLN ASN ILE HIS ASP ALA ASP PRO ALA THR ILE SER
SEQRES 13 D 271 ARG ASP MET ALA ALA VAL SER ARG ALA MET SER ALA ASN
SEQRES 14 D 271 GLU GLU ALA TRP ASP ALA LEU GLY PRO GLU VAL HIS GLU
SEQRES 15 D 271 ARG LEU ARG ASP ASN TYR VAL ARG TRP ALA TYR GLY TYR
SEQRES 16 D 271 PRO ARG THR ILE PRO GLY SER ALA ALA THR LYS THR GLU
SEQRES 17 D 271 ASP LEU HIS LYS VAL PRO ILE ASP TRP THR VAL GLY ALA
SEQRES 18 D 271 ALA GLY PRO THR GLN VAL PHE PHE GLU ASN VAL VAL ILE
SEQRES 19 D 271 ALA THR ARG GLU SER ILE PRO ILE LYS THR LEU PRO GLY
SEQRES 20 D 271 PHE HIS PHE PRO TYR VAL SER HIS PRO GLU ALA PHE ALA
SEQRES 21 D 271 LYS TYR VAL VAL GLU THR THR ARG LYS TYR LEU
HET NA A 301 1
HET MLI A 302 7
HET GOL B 301 6
HET GOL B 302 6
HET NA B 303 1
HET NA C 301 1
HET GOL D 301 6
HET NA D 302 1
HET MLI D 303 7
HETNAM NA SODIUM ION
HETNAM MLI MALONATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 NA 4(NA 1+)
FORMUL 6 MLI 2(C3 H2 O4 2-)
FORMUL 7 GOL 3(C3 H8 O3)
FORMUL 14 HOH *1061(H2 O)
HELIX 1 AA1 ASP A 38 MET A 41 5 4
HELIX 2 AA2 PHE A 42 SER A 51 1 10
HELIX 3 AA3 MET A 64 SER A 68 5 5
HELIX 4 AA4 PRO A 71 TYR A 75 5 5
HELIX 5 AA5 THR A 79 GLY A 95 1 17
HELIX 6 AA6 SER A 105 PHE A 118 1 14
HELIX 7 AA7 GLN A 139 ASP A 143 5 5
HELIX 8 AA8 ASP A 145 SER A 161 1 17
HELIX 9 AA9 ASN A 163 LEU A 170 1 8
HELIX 10 AB1 GLY A 171 TYR A 189 1 19
HELIX 11 AB2 ILE A 193 ALA A 197 5 5
HELIX 12 AB3 LYS A 200 LEU A 204 5 5
HELIX 13 AB4 PHE A 222 GLU A 232 1 11
HELIX 14 AB5 PHE A 244 HIS A 249 1 6
HELIX 15 AB6 HIS A 249 LYS A 263 1 15
HELIX 16 AB7 ASP B 38 MET B 41 5 4
HELIX 17 AB8 PHE B 42 GLY B 50 1 9
HELIX 18 AB9 MET B 64 SER B 68 5 5
HELIX 19 AC1 PRO B 71 TYR B 75 5 5
HELIX 20 AC2 THR B 79 GLY B 95 1 17
HELIX 21 AC3 SER B 105 PHE B 118 1 14
HELIX 22 AC4 ASN B 140 ALA B 144 5 5
HELIX 23 AC5 ASP B 145 SER B 161 1 17
HELIX 24 AC6 ASN B 163 ALA B 169 1 7
HELIX 25 AC7 GLY B 171 TYR B 189 1 19
HELIX 26 AC8 ILE B 193 ALA B 197 5 5
HELIX 27 AC9 LYS B 200 LEU B 204 5 5
HELIX 28 AD1 PHE B 222 GLU B 232 1 11
HELIX 29 AD2 PHE B 244 HIS B 249 1 6
HELIX 30 AD3 HIS B 249 LYS B 263 1 15
HELIX 31 AD4 ASP C 38 MET C 41 5 4
HELIX 32 AD5 PHE C 42 SER C 51 1 10
HELIX 33 AD6 MET C 64 SER C 68 5 5
HELIX 34 AD7 PRO C 71 GLN C 76 5 6
HELIX 35 AD8 THR C 79 GLY C 95 1 17
HELIX 36 AD9 SER C 105 PHE C 118 1 14
HELIX 37 AE1 ASN C 140 ALA C 144 5 5
HELIX 38 AE2 ASP C 145 MET C 160 1 16
HELIX 39 AE3 ASN C 163 LEU C 170 1 8
HELIX 40 AE4 GLY C 171 TYR C 189 1 19
HELIX 41 AE5 ILE C 193 ALA C 197 5 5
HELIX 42 AE6 LYS C 200 LEU C 204 5 5
HELIX 43 AE7 PHE C 222 GLU C 232 1 11
HELIX 44 AE8 PHE C 244 HIS C 249 1 6
HELIX 45 AE9 HIS C 249 LYS C 263 1 15
HELIX 46 AF1 ASP D 38 MET D 41 5 4
HELIX 47 AF2 PHE D 42 SER D 51 1 10
HELIX 48 AF3 MET D 64 SER D 68 5 5
HELIX 49 AF4 PRO D 71 TYR D 75 5 5
HELIX 50 AF5 THR D 79 GLY D 95 1 17
HELIX 51 AF6 SER D 105 PHE D 118 1 14
HELIX 52 AF7 PRO D 135 GLN D 139 5 5
HELIX 53 AF8 ASN D 140 ALA D 144 5 5
HELIX 54 AF9 ASP D 145 MET D 160 1 16
HELIX 55 AG1 ASN D 163 ALA D 169 1 7
HELIX 56 AG2 GLY D 171 TYR D 189 1 19
HELIX 57 AG3 ILE D 193 ALA D 197 5 5
HELIX 58 AG4 LYS D 200 HIS D 205 1 6
HELIX 59 AG5 PHE D 222 GLU D 232 1 11
HELIX 60 AG6 PHE D 244 HIS D 249 1 6
HELIX 61 AG7 HIS D 249 LYS D 263 1 15
SHEET 1 AA1 6 ARG A 5 LEU A 11 0
SHEET 2 AA1 6 ASN A 17 GLU A 23 -1 O GLN A 22 N LEU A 6
SHEET 3 AA1 6 LYS A 55 PHE A 59 -1 O VAL A 56 N GLU A 23
SHEET 4 AA1 6 ASP A 28 ILE A 32 1 N VAL A 29 O LYS A 55
SHEET 5 AA1 6 ALA A 99 CYS A 104 1 O TRP A 102 N ILE A 32
SHEET 6 AA1 6 VAL A 122 HIS A 128 1 O MET A 126 N VAL A 101
SHEET 1 AA2 2 TRP A 211 GLY A 214 0
SHEET 2 AA2 2 ILE A 236 LEU A 239 1 O LEU A 239 N VAL A 213
SHEET 1 AA3 6 LEU B 6 LEU B 11 0
SHEET 2 AA3 6 ASN B 17 GLY B 24 -1 O GLN B 22 N LEU B 6
SHEET 3 AA3 6 LYS B 55 PHE B 59 -1 O VAL B 56 N GLU B 23
SHEET 4 AA3 6 ASP B 28 ILE B 32 1 N VAL B 29 O THR B 57
SHEET 5 AA3 6 ALA B 99 CYS B 104 1 O SER B 100 N VAL B 30
SHEET 6 AA3 6 VAL B 122 HIS B 128 1 O MET B 126 N VAL B 101
SHEET 1 AA4 2 TRP B 211 GLY B 214 0
SHEET 2 AA4 2 ILE B 236 LEU B 239 1 O LEU B 239 N VAL B 213
SHEET 1 AA5 6 ARG C 5 LEU C 11 0
SHEET 2 AA5 6 ASN C 17 GLU C 23 -1 O GLN C 22 N LEU C 6
SHEET 3 AA5 6 LYS C 55 PHE C 59 -1 O VAL C 56 N GLU C 23
SHEET 4 AA5 6 ASP C 28 ILE C 32 1 N LEU C 31 O THR C 57
SHEET 5 AA5 6 ALA C 99 CYS C 104 1 O SER C 100 N VAL C 30
SHEET 6 AA5 6 VAL C 122 HIS C 128 1 O MET C 126 N VAL C 101
SHEET 1 AA6 2 TRP C 211 GLY C 214 0
SHEET 2 AA6 2 ILE C 236 LEU C 239 1 O LEU C 239 N VAL C 213
SHEET 1 AA7 6 ARG D 5 LEU D 11 0
SHEET 2 AA7 6 ASN D 17 GLU D 23 -1 O TYR D 20 N SER D 8
SHEET 3 AA7 6 LYS D 55 PHE D 59 -1 O VAL D 56 N GLU D 23
SHEET 4 AA7 6 ASP D 28 ILE D 32 1 N VAL D 29 O LYS D 55
SHEET 5 AA7 6 ALA D 99 CYS D 104 1 O TRP D 102 N ILE D 32
SHEET 6 AA7 6 VAL D 122 HIS D 128 1 O MET D 126 N VAL D 101
SHEET 1 AA8 2 TRP D 211 GLY D 214 0
SHEET 2 AA8 2 ILE D 236 LEU D 239 1 O LEU D 239 N VAL D 213
LINK O PRO A 119 NA NA A 301 1555 1555 2.46
LINK O VAL A 122 NA NA A 301 1555 1555 2.22
LINK O PRO B 119 NA NA B 303 1555 1555 2.32
LINK O VAL B 122 NA NA B 303 1555 1555 2.44
LINK O PRO C 119 NA NA C 301 1555 1555 2.36
LINK O VAL C 122 NA NA C 301 1555 1555 2.25
LINK O SER D 65 NA NA D 302 1555 1555 2.34
LINK OG SER D 68 NA NA D 302 1555 1555 2.56
LINK NA NA A 301 O HOH A 552 1555 1555 2.45
LINK NA NA A 301 O HOH A 581 1555 1555 2.23
LINK NA NA A 301 O HOH A 621 1555 1555 2.11
LINK NA NA B 303 O HOH B 614 1555 1555 2.27
LINK NA NA B 303 O HOH B 622 1555 1555 2.28
LINK NA NA B 303 O HOH B 620 1555 1555 2.33
LINK NA NA C 301 O HOH C 552 1555 1555 2.60
LINK NA NA C 301 O HOH C 581 1555 1555 2.26
LINK NA NA D 302 O HOH D 563 1555 1555 2.67
LINK NA NA D 302 O HOH D 552 1555 1555 2.38
LINK NA NA D 302 O HOH D 538 1555 1555 2.39
LINK NA NA D 302 O HOH D 550 1555 1555 2.32
SITE 1 AC1 6 PRO A 119 VAL A 122 VAL A 207 HOH A 552
SITE 2 AC1 6 HOH A 581 HOH A 621
SITE 1 AC2 6 GLY A 35 LEU A 36 SER A 105 MET A 153
SITE 2 AC2 6 SER A 157 HIS A 243
SITE 1 AC3 6 SER A 150 ARG A 179 HOH A 513 THR B 12
SITE 2 AC3 6 GLY B 15 HOH B 439
SITE 1 AC4 4 GLY B 35 SER B 105 SER B 157 HIS B 243
SITE 1 AC5 6 PRO B 119 VAL B 122 VAL B 207 HOH B 614
SITE 2 AC5 6 HOH B 620 HOH B 622
SITE 1 AC6 5 PRO C 119 VAL C 122 VAL C 207 HOH C 552
SITE 2 AC6 5 HOH C 581
SITE 1 AC7 3 PRO D 131 PRO D 135 HOH D 525
SITE 1 AC8 6 SER D 65 SER D 68 HOH D 538 HOH D 550
SITE 2 AC8 6 HOH D 552 HOH D 563
SITE 1 AC9 8 ASP D 34 GLY D 35 LEU D 36 SER D 105
SITE 2 AC9 8 MET D 153 SER D 157 TRP D 185 HIS D 243
CRYST1 120.863 104.399 116.834 90.00 90.00 90.00 P 21 21 2 16
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 0.008274 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009579 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008559 0.00000
TER 2010 LEU A 265
TER 4048 LEU B 265
TER 6074 LEU C 265
TER 8100 LEU D 265
MASTER 509 0 9 61 32 0 16 6 9193 4 59 84
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