HEADER HYDROLASE 20-OCT-09 2WVS
TITLE CRYSTAL STRUCTURE OF AN ALPHA-L-FUCOSIDASE GH29 TRAPPED COVALENT
TITLE 2 INTERMEDIATE FROM BACTEROIDES THETAIOTAOMICRON IN COMPLEX WITH 2-
TITLE 3 FLUORO-FUCOSYL FLUORIDE USING AN E288Q MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-L-FUCOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 31-473;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;
SOURCE 3 ORGANISM_TAXID: 226186;
SOURCE 4 STRAIN: VPI-5482;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS ALPHA-L-FUCOSE, HYDROLASE, GLYCOSIDE HYDROLASE FAMILY 29
EXPDTA X-RAY DIFFRACTION
AUTHOR A.LAMMERTS VAN BUEREN,A.ARDEVOL,J.FAYERS-KERR,B.LUO,Y.ZHANG,
AUTHOR 2 M.SOLLOGOUB,Y.BLERIOT,C.ROVIRA,G.J.DAVIES
REVDAT 3 29-JUL-20 2WVS 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE
REVDAT 2 15-JUN-11 2WVS 1 JRNL REMARK
REVDAT 1 02-FEB-10 2WVS 0
JRNL AUTH A.LAMMERTS VAN BUEREN,A.ARDEVOL,J.FAYERS-KERR,B.LUO,Y.ZHANG,
JRNL AUTH 2 M.SOLLOGOUB,Y.BLERIOT,C.ROVIRA,G.J.DAVIES
JRNL TITL ANALYSIS OF THE REACTION COORDINATE OF ALPHA-L-FUCOSIDASES:
JRNL TITL 2 A COMBINED STRUCTURAL AND QUANTUM MECHANICAL APPROACH
JRNL REF J.AM.CHEM.SOC. V. 132 1804 2010
JRNL REFN ISSN 0002-7863
JRNL PMID 20092273
JRNL DOI 10.1021/JA908908Q
REMARK 2
REMARK 2 RESOLUTION. 2.19 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 97.56
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 3 NUMBER OF REFLECTIONS : 91482
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) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.178
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4816
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) : 2.19
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5007
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2300
REMARK 3 BIN FREE R VALUE SET COUNT : 280
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14296
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 922
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.63
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.40000
REMARK 3 B22 (A**2) : 2.03000
REMARK 3 B33 (A**2) : -2.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.44000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.288
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.157
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.166
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14904 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20218 ; 1.413 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1770 ; 5.866 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 726 ;33.833 ;23.774
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2518 ;16.248 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 90 ;21.485 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2044 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11478 ; 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): 8741 ; 0.706 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14091 ; 1.299 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6163 ; 2.087 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6116 ; 3.267 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: U VALUES REFINED INDIVIDUALLY.
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
REMARK 4
REMARK 4 2WVS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-OCT-09.
REMARK 100 THE DEPOSITION ID IS D_1290041437.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-09
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.99
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 91280
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.190
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 92.58000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLU 288 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLU 288 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, GLU 288 TO GLN
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, GLU 288 TO GLN
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 GLU A 31
REMARK 465 ALA A 32
REMARK 465 LYS A 33
REMARK 465 LYS A 34
REMARK 465 GLU B 31
REMARK 465 ALA B 32
REMARK 465 LYS B 33
REMARK 465 LYS B 34
REMARK 465 ALA B 472
REMARK 465 LYS B 473
REMARK 465 GLU C 31
REMARK 465 ALA C 32
REMARK 465 LYS C 33
REMARK 465 LYS C 34
REMARK 465 LYS C 473
REMARK 465 GLU D 31
REMARK 465 ALA D 32
REMARK 465 LYS D 33
REMARK 465 LYS D 34
REMARK 465 LYS D 473
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 LYS A 421 CG CD CE NZ
REMARK 470 LYS A 424 CG CD CE NZ
REMARK 470 LYS B 421 CG CD CE NZ
REMARK 470 LYS B 424 CG CD CE NZ
REMARK 470 LYS C 421 CG CD CE NZ
REMARK 470 LYS C 424 CG CD CE NZ
REMARK 470 LYS D 421 CG CD CE NZ
REMARK 470 LYS D 424 CG CD CE NZ
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 CE LYS B 166 O HOH B 2075 1.94
REMARK 500 O HOH A 2149 O HOH A 2150 2.13
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 264 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 204 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG B 264 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 264 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG C 264 NE - CZ - NH2 ANGL. DEV. = -3.5 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 ARG A 60 -53.27 63.22
REMARK 500 ASN A 108 67.58 -159.36
REMARK 500 PRO A 109 77.65 -68.92
REMARK 500 TYR A 128 148.63 -170.07
REMARK 500 LYS A 157 -46.00 68.96
REMARK 500 LYS A 194 -70.42 -100.39
REMARK 500 TYR A 220 73.07 -119.45
REMARK 500 HIS A 272 -68.02 74.80
REMARK 500 PRO A 312 -168.54 -74.36
REMARK 500 ASN A 314 63.14 -150.60
REMARK 500 ARG A 360 150.22 -49.42
REMARK 500 VAL A 381 -56.51 -125.17
REMARK 500 THR A 446 -169.53 -160.40
REMARK 500 ILE B 36 125.03 -29.23
REMARK 500 GLU B 45 -74.58 -76.38
REMARK 500 ARG B 60 -52.71 62.43
REMARK 500 ASN B 108 69.64 -157.36
REMARK 500 ASN B 153 44.61 -98.84
REMARK 500 LYS B 157 -38.29 68.10
REMARK 500 HIS B 272 -65.96 69.85
REMARK 500 SER B 285 56.83 -142.45
REMARK 500 ARG B 289 -50.55 77.74
REMARK 500 ASN B 314 65.39 -153.52
REMARK 500 ASN B 402 38.77 -97.02
REMARK 500 THR B 446 -168.04 -160.45
REMARK 500 ARG C 60 -48.62 55.79
REMARK 500 ASN C 108 62.98 -152.51
REMARK 500 ASN C 153 40.04 -102.48
REMARK 500 LYS C 157 -33.61 64.28
REMARK 500 ASN C 239 55.74 -119.00
REMARK 500 HIS C 272 -68.49 73.39
REMARK 500 ASN C 314 68.67 -157.94
REMARK 500 VAL C 381 -59.80 -121.90
REMARK 500 ASN C 402 50.50 -113.63
REMARK 500 ARG C 447 120.68 -39.46
REMARK 500 ALA C 471 -141.08 -78.50
REMARK 500 GLU D 45 -88.15 -72.78
REMARK 500 ARG D 60 -51.08 60.60
REMARK 500 TRP D 107 93.71 -64.14
REMARK 500 ASN D 108 75.16 -150.86
REMARK 500 PRO D 109 62.69 -69.87
REMARK 500 THR D 110 -47.29 -21.30
REMARK 500 LYS D 157 -32.85 66.23
REMARK 500 PRO D 221 1.35 -67.74
REMARK 500 HIS D 272 -66.20 61.75
REMARK 500 ASP D 274 -165.39 -73.20
REMARK 500 ASN D 276 37.40 -93.98
REMARK 500 ARG D 290 137.53 158.12
REMARK 500 ASN D 314 59.86 -161.91
REMARK 500 VAL D 381 -62.54 -123.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 263 ARG A 264 -147.77
REMARK 500 LEU B 263 ARG B 264 -148.36
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WVT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN ALPHA-L-FUCOSIDASE GH29 FROM BACTEROIDES
REMARK 900 THETAIOTAOMICRON IN COMPLEX WITH A NOVEL IMINOSUGAR FUCOSIDASE
REMARK 900 INHIBITOR
REMARK 900 RELATED ID: 2WVV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF AN ALPHA-L-FUCOSIDASE GH29 FROM BACTEROIDES
REMARK 900 THETAIOTAOMICRON
REMARK 900 RELATED ID: 2WVU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A MICHAELIS COMPLEX OF ALPHA-L-FUCOSIDASE GH29
REMARK 900 FROM BACTEROIDES THETAIOTAOMICRON WITH THE SYNTHETIC SUBSTRATE 4-
REMARK 900 NITROPHENYL-ALPHA-L-FUCOSE
DBREF 2WVS A 31 473 UNP Q8A3I4 Q8A3I4_BACTN 31 473
DBREF 2WVS B 31 473 UNP Q8A3I4 Q8A3I4_BACTN 31 473
DBREF 2WVS C 31 473 UNP Q8A3I4 Q8A3I4_BACTN 31 473
DBREF 2WVS D 31 473 UNP Q8A3I4 Q8A3I4_BACTN 31 473
SEQADV 2WVS GLN A 288 UNP Q8A3I4 GLU 288 ENGINEERED MUTATION
SEQADV 2WVS GLN B 288 UNP Q8A3I4 GLU 288 ENGINEERED MUTATION
SEQADV 2WVS GLN C 288 UNP Q8A3I4 GLU 288 ENGINEERED MUTATION
SEQADV 2WVS GLN D 288 UNP Q8A3I4 GLU 288 ENGINEERED MUTATION
SEQRES 1 A 443 GLU ALA LYS LYS GLU ILE PRO LEU LYS TYR GLY ALA THR
SEQRES 2 A 443 ASN GLU GLY LYS ARG GLN ASP PRO ALA MET GLN LYS PHE
SEQRES 3 A 443 ARG ASP ASN ARG LEU GLY ALA PHE ILE HIS TRP GLY LEU
SEQRES 4 A 443 TYR ALA ILE PRO GLY GLY GLU TRP ASN GLY LYS VAL TYR
SEQRES 5 A 443 GLY GLY ALA ALA GLU TRP LEU LYS SER TRP ALA LYS VAL
SEQRES 6 A 443 PRO ALA ASP GLU TRP LEU LYS LEU MET ASP GLN TRP ASN
SEQRES 7 A 443 PRO THR LYS PHE ASP ALA LYS LYS TRP ALA LYS MET ALA
SEQRES 8 A 443 LYS GLU MET GLY THR LYS TYR VAL LYS ILE THR THR LYS
SEQRES 9 A 443 HIS HIS GLU GLY PHE CYS LEU TRP PRO SER LYS TYR THR
SEQRES 10 A 443 LYS TYR THR VAL ALA ASN THR PRO TYR LYS ARG ASP ILE
SEQRES 11 A 443 LEU GLY GLU LEU VAL LYS ALA TYR ASN ASP GLU GLY ILE
SEQRES 12 A 443 ASP VAL HIS PHE TYR PHE SER VAL MET ASP TRP SER ASN
SEQRES 13 A 443 PRO ASP TYR ARG TYR ASP ILE LYS SER LYS GLU ASP SER
SEQRES 14 A 443 ILE ALA PHE SER ARG PHE LEU GLU PHE THR ASP ASN GLN
SEQRES 15 A 443 LEU LYS GLU LEU ALA THR ARG TYR PRO THR VAL LYS ASP
SEQRES 16 A 443 PHE TRP PHE ASP GLY THR TRP ASP ALA SER VAL LYS LYS
SEQRES 17 A 443 ASN GLY TRP TRP THR ALA HIS ALA GLU GLN MET LEU LYS
SEQRES 18 A 443 GLU LEU VAL PRO GLY VAL ALA ILE ASN SER ARG LEU ARG
SEQRES 19 A 443 ALA ASP ASP LYS GLY LYS ARG HIS PHE ASP SER ASN GLY
SEQRES 20 A 443 ARG LEU MET GLY ASP TYR GLU SER GLY TYR GLN ARG ARG
SEQRES 21 A 443 LEU PRO ASP PRO VAL LYS ASP LEU LYS VAL THR GLN TRP
SEQRES 22 A 443 ASP TRP GLU ALA CYS MET THR ILE PRO GLU ASN GLN TRP
SEQRES 23 A 443 GLY TYR HIS LYS ASP TRP SER LEU SER TYR VAL LYS THR
SEQRES 24 A 443 PRO ILE GLU VAL ILE ASP ARG ILE VAL HIS ALA VAL SER
SEQRES 25 A 443 MET GLY GLY ASN MET VAL VAL ASN PHE GLY PRO GLN ALA
SEQRES 26 A 443 ASP GLY ASP PHE ARG PRO GLU GLU LYS ALA MET ALA THR
SEQRES 27 A 443 ALA ILE GLY LYS TRP MET ASN ARG TYR GLY LYS ALA VAL
SEQRES 28 A 443 TYR ALA CYS ASP TYR ALA GLY PHE GLU LYS GLN ASP TRP
SEQRES 29 A 443 GLY TYR TYR THR ARG GLY LYS ASN ASP GLU VAL TYR MET
SEQRES 30 A 443 VAL VAL PHE ASN GLN PRO TYR SER GLU ARG LEU ILE VAL
SEQRES 31 A 443 LYS THR PRO LYS GLY ILE THR VAL GLU LYS ALA THR LEU
SEQRES 32 A 443 LEU THR THR GLY GLU ASP ILE THR VAL VAL GLU THR THR
SEQRES 33 A 443 ARG ASN GLU TYR ASN VAL SER VAL PRO LYS LYS ASN PRO
SEQRES 34 A 443 GLY GLU PRO TYR VAL ILE GLN LEU LYS VAL ARG ALA ALA
SEQRES 35 A 443 LYS
SEQRES 1 B 443 GLU ALA LYS LYS GLU ILE PRO LEU LYS TYR GLY ALA THR
SEQRES 2 B 443 ASN GLU GLY LYS ARG GLN ASP PRO ALA MET GLN LYS PHE
SEQRES 3 B 443 ARG ASP ASN ARG LEU GLY ALA PHE ILE HIS TRP GLY LEU
SEQRES 4 B 443 TYR ALA ILE PRO GLY GLY GLU TRP ASN GLY LYS VAL TYR
SEQRES 5 B 443 GLY GLY ALA ALA GLU TRP LEU LYS SER TRP ALA LYS VAL
SEQRES 6 B 443 PRO ALA ASP GLU TRP LEU LYS LEU MET ASP GLN TRP ASN
SEQRES 7 B 443 PRO THR LYS PHE ASP ALA LYS LYS TRP ALA LYS MET ALA
SEQRES 8 B 443 LYS GLU MET GLY THR LYS TYR VAL LYS ILE THR THR LYS
SEQRES 9 B 443 HIS HIS GLU GLY PHE CYS LEU TRP PRO SER LYS TYR THR
SEQRES 10 B 443 LYS TYR THR VAL ALA ASN THR PRO TYR LYS ARG ASP ILE
SEQRES 11 B 443 LEU GLY GLU LEU VAL LYS ALA TYR ASN ASP GLU GLY ILE
SEQRES 12 B 443 ASP VAL HIS PHE TYR PHE SER VAL MET ASP TRP SER ASN
SEQRES 13 B 443 PRO ASP TYR ARG TYR ASP ILE LYS SER LYS GLU ASP SER
SEQRES 14 B 443 ILE ALA PHE SER ARG PHE LEU GLU PHE THR ASP ASN GLN
SEQRES 15 B 443 LEU LYS GLU LEU ALA THR ARG TYR PRO THR VAL LYS ASP
SEQRES 16 B 443 PHE TRP PHE ASP GLY THR TRP ASP ALA SER VAL LYS LYS
SEQRES 17 B 443 ASN GLY TRP TRP THR ALA HIS ALA GLU GLN MET LEU LYS
SEQRES 18 B 443 GLU LEU VAL PRO GLY VAL ALA ILE ASN SER ARG LEU ARG
SEQRES 19 B 443 ALA ASP ASP LYS GLY LYS ARG HIS PHE ASP SER ASN GLY
SEQRES 20 B 443 ARG LEU MET GLY ASP TYR GLU SER GLY TYR GLN ARG ARG
SEQRES 21 B 443 LEU PRO ASP PRO VAL LYS ASP LEU LYS VAL THR GLN TRP
SEQRES 22 B 443 ASP TRP GLU ALA CYS MET THR ILE PRO GLU ASN GLN TRP
SEQRES 23 B 443 GLY TYR HIS LYS ASP TRP SER LEU SER TYR VAL LYS THR
SEQRES 24 B 443 PRO ILE GLU VAL ILE ASP ARG ILE VAL HIS ALA VAL SER
SEQRES 25 B 443 MET GLY GLY ASN MET VAL VAL ASN PHE GLY PRO GLN ALA
SEQRES 26 B 443 ASP GLY ASP PHE ARG PRO GLU GLU LYS ALA MET ALA THR
SEQRES 27 B 443 ALA ILE GLY LYS TRP MET ASN ARG TYR GLY LYS ALA VAL
SEQRES 28 B 443 TYR ALA CYS ASP TYR ALA GLY PHE GLU LYS GLN ASP TRP
SEQRES 29 B 443 GLY TYR TYR THR ARG GLY LYS ASN ASP GLU VAL TYR MET
SEQRES 30 B 443 VAL VAL PHE ASN GLN PRO TYR SER GLU ARG LEU ILE VAL
SEQRES 31 B 443 LYS THR PRO LYS GLY ILE THR VAL GLU LYS ALA THR LEU
SEQRES 32 B 443 LEU THR THR GLY GLU ASP ILE THR VAL VAL GLU THR THR
SEQRES 33 B 443 ARG ASN GLU TYR ASN VAL SER VAL PRO LYS LYS ASN PRO
SEQRES 34 B 443 GLY GLU PRO TYR VAL ILE GLN LEU LYS VAL ARG ALA ALA
SEQRES 35 B 443 LYS
SEQRES 1 C 443 GLU ALA LYS LYS GLU ILE PRO LEU LYS TYR GLY ALA THR
SEQRES 2 C 443 ASN GLU GLY LYS ARG GLN ASP PRO ALA MET GLN LYS PHE
SEQRES 3 C 443 ARG ASP ASN ARG LEU GLY ALA PHE ILE HIS TRP GLY LEU
SEQRES 4 C 443 TYR ALA ILE PRO GLY GLY GLU TRP ASN GLY LYS VAL TYR
SEQRES 5 C 443 GLY GLY ALA ALA GLU TRP LEU LYS SER TRP ALA LYS VAL
SEQRES 6 C 443 PRO ALA ASP GLU TRP LEU LYS LEU MET ASP GLN TRP ASN
SEQRES 7 C 443 PRO THR LYS PHE ASP ALA LYS LYS TRP ALA LYS MET ALA
SEQRES 8 C 443 LYS GLU MET GLY THR LYS TYR VAL LYS ILE THR THR LYS
SEQRES 9 C 443 HIS HIS GLU GLY PHE CYS LEU TRP PRO SER LYS TYR THR
SEQRES 10 C 443 LYS TYR THR VAL ALA ASN THR PRO TYR LYS ARG ASP ILE
SEQRES 11 C 443 LEU GLY GLU LEU VAL LYS ALA TYR ASN ASP GLU GLY ILE
SEQRES 12 C 443 ASP VAL HIS PHE TYR PHE SER VAL MET ASP TRP SER ASN
SEQRES 13 C 443 PRO ASP TYR ARG TYR ASP ILE LYS SER LYS GLU ASP SER
SEQRES 14 C 443 ILE ALA PHE SER ARG PHE LEU GLU PHE THR ASP ASN GLN
SEQRES 15 C 443 LEU LYS GLU LEU ALA THR ARG TYR PRO THR VAL LYS ASP
SEQRES 16 C 443 PHE TRP PHE ASP GLY THR TRP ASP ALA SER VAL LYS LYS
SEQRES 17 C 443 ASN GLY TRP TRP THR ALA HIS ALA GLU GLN MET LEU LYS
SEQRES 18 C 443 GLU LEU VAL PRO GLY VAL ALA ILE ASN SER ARG LEU ARG
SEQRES 19 C 443 ALA ASP ASP LYS GLY LYS ARG HIS PHE ASP SER ASN GLY
SEQRES 20 C 443 ARG LEU MET GLY ASP TYR GLU SER GLY TYR GLN ARG ARG
SEQRES 21 C 443 LEU PRO ASP PRO VAL LYS ASP LEU LYS VAL THR GLN TRP
SEQRES 22 C 443 ASP TRP GLU ALA CYS MET THR ILE PRO GLU ASN GLN TRP
SEQRES 23 C 443 GLY TYR HIS LYS ASP TRP SER LEU SER TYR VAL LYS THR
SEQRES 24 C 443 PRO ILE GLU VAL ILE ASP ARG ILE VAL HIS ALA VAL SER
SEQRES 25 C 443 MET GLY GLY ASN MET VAL VAL ASN PHE GLY PRO GLN ALA
SEQRES 26 C 443 ASP GLY ASP PHE ARG PRO GLU GLU LYS ALA MET ALA THR
SEQRES 27 C 443 ALA ILE GLY LYS TRP MET ASN ARG TYR GLY LYS ALA VAL
SEQRES 28 C 443 TYR ALA CYS ASP TYR ALA GLY PHE GLU LYS GLN ASP TRP
SEQRES 29 C 443 GLY TYR TYR THR ARG GLY LYS ASN ASP GLU VAL TYR MET
SEQRES 30 C 443 VAL VAL PHE ASN GLN PRO TYR SER GLU ARG LEU ILE VAL
SEQRES 31 C 443 LYS THR PRO LYS GLY ILE THR VAL GLU LYS ALA THR LEU
SEQRES 32 C 443 LEU THR THR GLY GLU ASP ILE THR VAL VAL GLU THR THR
SEQRES 33 C 443 ARG ASN GLU TYR ASN VAL SER VAL PRO LYS LYS ASN PRO
SEQRES 34 C 443 GLY GLU PRO TYR VAL ILE GLN LEU LYS VAL ARG ALA ALA
SEQRES 35 C 443 LYS
SEQRES 1 D 443 GLU ALA LYS LYS GLU ILE PRO LEU LYS TYR GLY ALA THR
SEQRES 2 D 443 ASN GLU GLY LYS ARG GLN ASP PRO ALA MET GLN LYS PHE
SEQRES 3 D 443 ARG ASP ASN ARG LEU GLY ALA PHE ILE HIS TRP GLY LEU
SEQRES 4 D 443 TYR ALA ILE PRO GLY GLY GLU TRP ASN GLY LYS VAL TYR
SEQRES 5 D 443 GLY GLY ALA ALA GLU TRP LEU LYS SER TRP ALA LYS VAL
SEQRES 6 D 443 PRO ALA ASP GLU TRP LEU LYS LEU MET ASP GLN TRP ASN
SEQRES 7 D 443 PRO THR LYS PHE ASP ALA LYS LYS TRP ALA LYS MET ALA
SEQRES 8 D 443 LYS GLU MET GLY THR LYS TYR VAL LYS ILE THR THR LYS
SEQRES 9 D 443 HIS HIS GLU GLY PHE CYS LEU TRP PRO SER LYS TYR THR
SEQRES 10 D 443 LYS TYR THR VAL ALA ASN THR PRO TYR LYS ARG ASP ILE
SEQRES 11 D 443 LEU GLY GLU LEU VAL LYS ALA TYR ASN ASP GLU GLY ILE
SEQRES 12 D 443 ASP VAL HIS PHE TYR PHE SER VAL MET ASP TRP SER ASN
SEQRES 13 D 443 PRO ASP TYR ARG TYR ASP ILE LYS SER LYS GLU ASP SER
SEQRES 14 D 443 ILE ALA PHE SER ARG PHE LEU GLU PHE THR ASP ASN GLN
SEQRES 15 D 443 LEU LYS GLU LEU ALA THR ARG TYR PRO THR VAL LYS ASP
SEQRES 16 D 443 PHE TRP PHE ASP GLY THR TRP ASP ALA SER VAL LYS LYS
SEQRES 17 D 443 ASN GLY TRP TRP THR ALA HIS ALA GLU GLN MET LEU LYS
SEQRES 18 D 443 GLU LEU VAL PRO GLY VAL ALA ILE ASN SER ARG LEU ARG
SEQRES 19 D 443 ALA ASP ASP LYS GLY LYS ARG HIS PHE ASP SER ASN GLY
SEQRES 20 D 443 ARG LEU MET GLY ASP TYR GLU SER GLY TYR GLN ARG ARG
SEQRES 21 D 443 LEU PRO ASP PRO VAL LYS ASP LEU LYS VAL THR GLN TRP
SEQRES 22 D 443 ASP TRP GLU ALA CYS MET THR ILE PRO GLU ASN GLN TRP
SEQRES 23 D 443 GLY TYR HIS LYS ASP TRP SER LEU SER TYR VAL LYS THR
SEQRES 24 D 443 PRO ILE GLU VAL ILE ASP ARG ILE VAL HIS ALA VAL SER
SEQRES 25 D 443 MET GLY GLY ASN MET VAL VAL ASN PHE GLY PRO GLN ALA
SEQRES 26 D 443 ASP GLY ASP PHE ARG PRO GLU GLU LYS ALA MET ALA THR
SEQRES 27 D 443 ALA ILE GLY LYS TRP MET ASN ARG TYR GLY LYS ALA VAL
SEQRES 28 D 443 TYR ALA CYS ASP TYR ALA GLY PHE GLU LYS GLN ASP TRP
SEQRES 29 D 443 GLY TYR TYR THR ARG GLY LYS ASN ASP GLU VAL TYR MET
SEQRES 30 D 443 VAL VAL PHE ASN GLN PRO TYR SER GLU ARG LEU ILE VAL
SEQRES 31 D 443 LYS THR PRO LYS GLY ILE THR VAL GLU LYS ALA THR LEU
SEQRES 32 D 443 LEU THR THR GLY GLU ASP ILE THR VAL VAL GLU THR THR
SEQRES 33 D 443 ARG ASN GLU TYR ASN VAL SER VAL PRO LYS LYS ASN PRO
SEQRES 34 D 443 GLY GLU PRO TYR VAL ILE GLN LEU LYS VAL ARG ALA ALA
SEQRES 35 D 443 LYS
HET FUF A1449 10
HET FUF A1450 11
HET SO4 A1474 5
HET SO4 A1475 5
HET FUF B1449 10
HET SO4 B1472 5
HET FUF C1449 10
HET SO4 C1473 5
HET SO4 C1474 5
HET FUF D1449 10
HET SO4 D1473 5
HET SO4 D1474 5
HETNAM FUF 2-DEOXY-2-FLUORO-BETA-L-FUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETSYN FUF 2,6-DIDEOXY-2-FLUORO-BETA-L-LYXO-HEXOPYRANOSE
FORMUL 5 FUF 5(C6 H11 F O4)
FORMUL 7 SO4 7(O4 S 2-)
FORMUL 17 HOH *922(H2 O)
HELIX 1 1 ASP A 50 ARG A 60 1 11
HELIX 2 2 GLY A 68 ILE A 72 5 5
HELIX 3 3 ALA A 85 GLU A 87 5 3
HELIX 4 4 TRP A 88 ALA A 93 1 6
HELIX 5 5 PRO A 96 LYS A 102 1 7
HELIX 6 6 LEU A 103 TRP A 107 5 5
HELIX 7 7 ASP A 113 GLY A 125 1 13
HELIX 8 8 VAL A 151 THR A 154 5 4
HELIX 9 9 ASP A 159 GLU A 171 1 13
HELIX 10 10 SER A 195 TYR A 220 1 26
HELIX 11 11 ASP A 233 LYS A 238 1 6
HELIX 12 12 ASN A 239 VAL A 254 1 16
HELIX 13 13 SER A 261 ARG A 264 5 4
HELIX 14 14 ASP A 297 TRP A 303 5 7
HELIX 15 15 ASP A 321 SER A 325 5 5
HELIX 16 16 THR A 329 MET A 343 1 15
HELIX 17 17 ARG A 360 GLY A 378 1 19
HELIX 18 18 LYS A 379 VAL A 381 5 3
HELIX 19 19 ASP B 50 ARG B 60 1 11
HELIX 20 20 GLY B 68 ILE B 72 5 5
HELIX 21 21 ALA B 85 GLU B 87 5 3
HELIX 22 22 TRP B 88 ALA B 93 1 6
HELIX 23 23 PRO B 96 LYS B 102 1 7
HELIX 24 24 LEU B 103 TRP B 107 5 5
HELIX 25 25 ASP B 113 GLY B 125 1 13
HELIX 26 26 VAL B 151 THR B 154 5 4
HELIX 27 27 ASP B 159 GLU B 171 1 13
HELIX 28 28 SER B 195 TYR B 220 1 26
HELIX 29 29 ASP B 233 LYS B 238 1 6
HELIX 30 30 ASN B 239 VAL B 254 1 16
HELIX 31 31 SER B 261 ARG B 264 5 4
HELIX 32 32 ASP B 297 TRP B 303 5 7
HELIX 33 33 ASP B 321 SER B 325 5 5
HELIX 34 34 THR B 329 MET B 343 1 15
HELIX 35 35 ARG B 360 GLY B 378 1 19
HELIX 36 36 LYS B 379 VAL B 381 5 3
HELIX 37 37 ASP C 50 ARG C 60 1 11
HELIX 38 38 GLY C 68 ILE C 72 5 5
HELIX 39 39 ALA C 85 GLU C 87 5 3
HELIX 40 40 TRP C 88 ALA C 93 1 6
HELIX 41 41 PRO C 96 LYS C 102 1 7
HELIX 42 42 LEU C 103 TRP C 107 5 5
HELIX 43 43 ASP C 113 GLY C 125 1 13
HELIX 44 44 VAL C 151 THR C 154 5 4
HELIX 45 45 ASP C 159 GLU C 171 1 13
HELIX 46 46 SER C 195 TYR C 220 1 26
HELIX 47 47 ASP C 233 LYS C 238 1 6
HELIX 48 48 ASN C 239 VAL C 254 1 16
HELIX 49 49 SER C 261 ARG C 264 5 4
HELIX 50 50 ASP C 297 TRP C 303 5 7
HELIX 51 51 ASP C 321 SER C 325 5 5
HELIX 52 52 THR C 329 SER C 342 1 14
HELIX 53 53 ARG C 360 GLY C 378 1 19
HELIX 54 54 LYS C 379 VAL C 381 5 3
HELIX 55 55 ASP D 50 ARG D 60 1 11
HELIX 56 56 GLY D 68 ILE D 72 5 5
HELIX 57 57 ALA D 85 GLU D 87 5 3
HELIX 58 58 TRP D 88 ALA D 93 1 6
HELIX 59 59 PRO D 96 LEU D 101 1 6
HELIX 60 60 LYS D 102 TRP D 107 5 6
HELIX 61 61 ASP D 113 GLY D 125 1 13
HELIX 62 62 VAL D 151 THR D 154 5 4
HELIX 63 63 ASP D 159 GLU D 171 1 13
HELIX 64 64 SER D 195 TYR D 220 1 26
HELIX 65 65 ASP D 233 LYS D 238 1 6
HELIX 66 66 ASN D 239 VAL D 254 1 16
HELIX 67 67 SER D 261 ARG D 264 5 4
HELIX 68 68 ASP D 297 TRP D 303 5 7
HELIX 69 69 ASP D 321 SER D 325 5 5
HELIX 70 70 THR D 329 MET D 343 1 15
HELIX 71 71 ARG D 360 GLY D 378 1 19
HELIX 72 72 LYS D 379 VAL D 381 5 3
SHEET 1 AA 7 ALA A 258 ILE A 259 0
SHEET 2 AA 7 ASP A 225 ASP A 229 1 N PHE A 226 O ALA A 258
SHEET 3 AA 7 ASP A 174 SER A 180 1 O PHE A 177 N TRP A 227
SHEET 4 AA 7 TYR A 128 THR A 132 1 O VAL A 129 N HIS A 176
SHEET 5 AA 7 LEU A 61 ILE A 65 1 O ALA A 63 N LYS A 130
SHEET 6 AA 7 ASN A 346 PHE A 351 1 O MET A 347 N GLY A 62
SHEET 7 AA 7 GLU A 306 MET A 309 1 O ALA A 307 N VAL A 348
SHEET 1 AB 2 GLU A 76 TRP A 77 0
SHEET 2 AB 2 LYS A 80 VAL A 81 -1 O LYS A 80 N TRP A 77
SHEET 1 AC 5 GLY A 395 ARG A 399 0
SHEET 2 AC 5 VAL A 405 VAL A 409 -1 O TYR A 406 N THR A 398
SHEET 3 AC 5 TYR A 463 ALA A 471 -1 O TYR A 463 N VAL A 409
SHEET 4 AC 5 ILE A 426 LEU A 433 -1 O THR A 427 N ARG A 470
SHEET 5 AC 5 ASP A 439 ILE A 440 -1 O ILE A 440 N ALA A 431
SHEET 1 AD 3 ARG A 417 LYS A 421 0
SHEET 2 AD 3 GLU A 449 SER A 453 -1 O TYR A 450 N VAL A 420
SHEET 3 AD 3 VAL A 442 THR A 446 -1 O VAL A 443 N ASN A 451
SHEET 1 BA 7 ALA B 258 ILE B 259 0
SHEET 2 BA 7 ASP B 225 ASP B 229 1 N PHE B 226 O ALA B 258
SHEET 3 BA 7 ASP B 174 SER B 180 1 O PHE B 177 N TRP B 227
SHEET 4 BA 7 TYR B 128 THR B 132 1 O VAL B 129 N HIS B 176
SHEET 5 BA 7 LEU B 61 ILE B 65 1 O ALA B 63 N LYS B 130
SHEET 6 BA 7 GLY B 345 PHE B 351 1 O MET B 347 N GLY B 62
SHEET 7 BA 7 TRP B 305 MET B 309 1 O TRP B 305 N ASN B 346
SHEET 1 BB 2 GLU B 76 TRP B 77 0
SHEET 2 BB 2 LYS B 80 VAL B 81 -1 O LYS B 80 N TRP B 77
SHEET 1 BC 4 GLY B 395 ARG B 399 0
SHEET 2 BC 4 VAL B 405 VAL B 409 -1 O TYR B 406 N THR B 398
SHEET 3 BC 4 TYR B 463 ARG B 470 -1 O TYR B 463 N VAL B 409
SHEET 4 BC 4 THR B 427 LEU B 433 -1 O THR B 427 N ARG B 470
SHEET 1 BD 3 ARG B 417 LYS B 421 0
SHEET 2 BD 3 GLU B 449 SER B 453 -1 O TYR B 450 N VAL B 420
SHEET 3 BD 3 VAL B 442 THR B 446 -1 O VAL B 443 N ASN B 451
SHEET 1 CA 7 ALA C 258 ILE C 259 0
SHEET 2 CA 7 ASP C 225 ASP C 229 1 N PHE C 226 O ALA C 258
SHEET 3 CA 7 ASP C 174 SER C 180 1 O PHE C 177 N TRP C 227
SHEET 4 CA 7 TYR C 128 LYS C 134 1 O VAL C 129 N HIS C 176
SHEET 5 CA 7 LEU C 61 ILE C 65 1 O ALA C 63 N LYS C 130
SHEET 6 CA 7 GLY C 345 PHE C 351 1 O MET C 347 N GLY C 62
SHEET 7 CA 7 TRP C 305 MET C 309 1 O TRP C 305 N ASN C 346
SHEET 1 CB 2 GLU C 76 TRP C 77 0
SHEET 2 CB 2 LYS C 80 VAL C 81 -1 O LYS C 80 N TRP C 77
SHEET 1 CC 5 GLY C 395 ARG C 399 0
SHEET 2 CC 5 GLU C 404 VAL C 409 -1 O TYR C 406 N THR C 398
SHEET 3 CC 5 TYR C 463 ARG C 470 -1 O TYR C 463 N VAL C 409
SHEET 4 CC 5 THR C 427 LEU C 433 -1 O THR C 427 N ARG C 470
SHEET 5 CC 5 ASP C 439 ILE C 440 -1 O ILE C 440 N ALA C 431
SHEET 1 CD 3 ARG C 417 LYS C 421 0
SHEET 2 CD 3 GLU C 449 SER C 453 -1 O TYR C 450 N VAL C 420
SHEET 3 CD 3 VAL C 442 THR C 446 -1 O VAL C 443 N ASN C 451
SHEET 1 DA 7 ALA D 258 ILE D 259 0
SHEET 2 DA 7 ASP D 225 ASP D 229 1 N PHE D 226 O ALA D 258
SHEET 3 DA 7 ASP D 174 SER D 180 1 O PHE D 177 N TRP D 227
SHEET 4 DA 7 TYR D 128 LYS D 134 1 O VAL D 129 N HIS D 176
SHEET 5 DA 7 LEU D 61 ILE D 65 1 O ALA D 63 N LYS D 130
SHEET 6 DA 7 ASN D 346 PHE D 351 1 O MET D 347 N GLY D 62
SHEET 7 DA 7 GLU D 306 MET D 309 1 O ALA D 307 N VAL D 348
SHEET 1 DB 2 GLU D 76 TRP D 77 0
SHEET 2 DB 2 LYS D 80 VAL D 81 -1 O LYS D 80 N TRP D 77
SHEET 1 DC 4 GLY D 395 ARG D 399 0
SHEET 2 DC 4 VAL D 405 VAL D 409 -1 O TYR D 406 N THR D 398
SHEET 3 DC 4 TYR D 463 ALA D 471 -1 O TYR D 463 N VAL D 409
SHEET 4 DC 4 ILE D 426 LEU D 433 -1 O THR D 427 N ARG D 470
SHEET 1 DD 3 ARG D 417 LYS D 421 0
SHEET 2 DD 3 GLU D 449 SER D 453 -1 O TYR D 450 N VAL D 420
SHEET 3 DD 3 VAL D 442 THR D 446 -1 O VAL D 443 N ASN D 451
LINK OD2 ASP A 229 C1 FUF A1449 1555 1555 1.42
LINK OD2 ASP B 229 C1 FUF B1449 1555 1555 1.43
LINK OD2 ASP C 229 C1 FUF C1449 1555 1555 1.43
LINK OD2 ASP D 229 C1 FUF D1449 1555 1555 1.42
CRYST1 54.840 185.160 97.870 90.00 94.57 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 0.018235 0.000000 0.001458 0.00000
SCALE2 0.000000 0.005401 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010250 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
