HEADER HYDROLASE 16-JUL-13 3WF3
TITLE CRYSTAL STRUCTURE OF HUMAN BETA-GALACTOSIDASE MUTANT I51T IN COMPLEX
TITLE 2 WITH GALACTOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ACID BETA-GALACTOSIDASE, LACTASE, ELASTIN RECEPTOR 1;
COMPND 5 EC: 3.2.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ELNR1, GLB1;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922
KEYWDS GLYCOSYL HYDROLASE, TIM-BARREL DOMAIN, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SUZUKI,U.OHTO,T.SHIMIZU
REVDAT 3 08-NOV-23 3WF3 1 HETSYN
REVDAT 2 29-JUL-20 3WF3 1 COMPND REMARK SEQADV HETNAM
REVDAT 2 2 1 LINK SITE
REVDAT 1 23-APR-14 3WF3 0
JRNL AUTH H.SUZUKI,U.OHTO,K.HIGAKI,T.MENA-BARRAGAN,M.AGUILAR-MONCAYO,
JRNL AUTH 2 C.ORTIZ MELLET,E.NANBA,J.M.GARCIA FERNANDEZ,Y.SUZUKI,
JRNL AUTH 3 T.SHIMIZU
JRNL TITL STRUCTURAL BASIS OF PHARMACOLOGICAL CHAPERONING FOR HUMAN
JRNL TITL 2 BETA-GALACTOSIDASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 158881
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.242
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 7765
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) : 2.15
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.21
REMARK 3 REFLECTION IN BIN (WORKING SET) : 11376
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 562
REMARK 3 BIN FREE R VALUE : 0.3020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 19202
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 348
REMARK 3 SOLVENT ATOMS : 1428
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.41
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.243
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.200
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.538
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.913
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 20234 ; 0.014 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 18635 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 27606 ; 1.700 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 42857 ; 1.345 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 2410 ; 7.154 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 912 ;36.642 ;23.805
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 3077 ;15.301 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 96 ;20.092 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2985 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 22684 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 4760 ; 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): 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 : MASK
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 3WF3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-13.
REMARK 100 THE DEPOSITION ID IS D_1000096255.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-JAN-13
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NE3A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 160267
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.47800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
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: 3THC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM SULFATE, HEPES, PH
REMARK 280 7.5, VAPOR DIFFUSION, SITTINGDROP, TEMPERATURE 277K, VAPOR
REMARK 280 DIFFUSION, SITTING DROP
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 57.94400
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
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: 6030 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 6160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44600 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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 0
REMARK 465 ALA A 1
REMARK 465 GLU A 2
REMARK 465 ALA A 3
REMARK 465 TYR A 4
REMARK 465 VAL A 5
REMARK 465 GLU A 6
REMARK 465 PHE A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 ASP A 14
REMARK 465 TYR A 15
REMARK 465 LYS A 16
REMARK 465 ASP A 17
REMARK 465 ASP A 18
REMARK 465 ASP A 19
REMARK 465 ASP A 20
REMARK 465 LYS A 21
REMARK 465 THR A 22
REMARK 465 SER A 23
REMARK 465 LEU A 24
REMARK 465 ARG A 25
REMARK 465 ASN A 26
REMARK 465 ALA A 27
REMARK 465 THR A 28
REMARK 465 ASP A 531
REMARK 465 SER A 532
REMARK 465 GLY A 533
REMARK 465 HIS A 534
REMARK 465 HIS A 535
REMARK 465 ASP A 536
REMARK 465 GLU A 537
REMARK 465 ALA A 538
REMARK 465 TRP A 539
REMARK 465 ALA A 540
REMARK 465 HIS A 541
REMARK 465 ASN A 542
REMARK 465 SER A 543
REMARK 465 SER A 544
REMARK 465 VAL A 648
REMARK 465 THR A 649
REMARK 465 TYR A 650
REMARK 465 ASP A 651
REMARK 465 HIS A 652
REMARK 465 PRO A 653
REMARK 465 SER A 654
REMARK 465 LYS A 655
REMARK 465 PRO A 656
REMARK 465 VAL A 657
REMARK 465 GLU A 658
REMARK 465 LYS A 659
REMARK 465 ARG A 660
REMARK 465 LEU A 661
REMARK 465 MET A 662
REMARK 465 PRO A 663
REMARK 465 PRO A 664
REMARK 465 PRO A 665
REMARK 465 PRO A 666
REMARK 465 GLN A 667
REMARK 465 LYS A 668
REMARK 465 ASN A 669
REMARK 465 LYS A 670
REMARK 465 ASP A 671
REMARK 465 SER A 672
REMARK 465 TRP A 673
REMARK 465 LEU A 674
REMARK 465 ASP A 675
REMARK 465 HIS A 676
REMARK 465 VAL A 677
REMARK 465 GLU B 0
REMARK 465 ALA B 1
REMARK 465 GLU B 2
REMARK 465 ALA B 3
REMARK 465 TYR B 4
REMARK 465 VAL B 5
REMARK 465 GLU B 6
REMARK 465 PHE B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 ASP B 14
REMARK 465 TYR B 15
REMARK 465 LYS B 16
REMARK 465 ASP B 17
REMARK 465 ASP B 18
REMARK 465 ASP B 19
REMARK 465 ASP B 20
REMARK 465 LYS B 21
REMARK 465 THR B 22
REMARK 465 SER B 23
REMARK 465 LEU B 24
REMARK 465 ARG B 25
REMARK 465 ASN B 26
REMARK 465 ALA B 27
REMARK 465 THR B 28
REMARK 465 ASP B 531
REMARK 465 SER B 532
REMARK 465 GLY B 533
REMARK 465 HIS B 534
REMARK 465 HIS B 535
REMARK 465 ASP B 536
REMARK 465 GLU B 537
REMARK 465 ALA B 538
REMARK 465 TRP B 539
REMARK 465 ALA B 540
REMARK 465 HIS B 541
REMARK 465 ASN B 542
REMARK 465 SER B 543
REMARK 465 SER B 544
REMARK 465 VAL B 648
REMARK 465 THR B 649
REMARK 465 TYR B 650
REMARK 465 ASP B 651
REMARK 465 HIS B 652
REMARK 465 PRO B 653
REMARK 465 SER B 654
REMARK 465 LYS B 655
REMARK 465 PRO B 656
REMARK 465 VAL B 657
REMARK 465 GLU B 658
REMARK 465 LYS B 659
REMARK 465 ARG B 660
REMARK 465 LEU B 661
REMARK 465 MET B 662
REMARK 465 PRO B 663
REMARK 465 PRO B 664
REMARK 465 PRO B 665
REMARK 465 PRO B 666
REMARK 465 GLN B 667
REMARK 465 LYS B 668
REMARK 465 ASN B 669
REMARK 465 LYS B 670
REMARK 465 ASP B 671
REMARK 465 SER B 672
REMARK 465 TRP B 673
REMARK 465 LEU B 674
REMARK 465 ASP B 675
REMARK 465 HIS B 676
REMARK 465 VAL B 677
REMARK 465 GLU C 0
REMARK 465 ALA C 1
REMARK 465 GLU C 2
REMARK 465 ALA C 3
REMARK 465 TYR C 4
REMARK 465 VAL C 5
REMARK 465 GLU C 6
REMARK 465 PHE C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 HIS C 13
REMARK 465 ASP C 14
REMARK 465 TYR C 15
REMARK 465 LYS C 16
REMARK 465 ASP C 17
REMARK 465 ASP C 18
REMARK 465 ASP C 19
REMARK 465 ASP C 20
REMARK 465 LYS C 21
REMARK 465 THR C 22
REMARK 465 SER C 23
REMARK 465 LEU C 24
REMARK 465 ARG C 25
REMARK 465 ASN C 26
REMARK 465 ALA C 27
REMARK 465 THR C 28
REMARK 465 HIS C 529
REMARK 465 ARG C 530
REMARK 465 ASP C 531
REMARK 465 SER C 532
REMARK 465 GLY C 533
REMARK 465 HIS C 534
REMARK 465 HIS C 535
REMARK 465 ASP C 536
REMARK 465 GLU C 537
REMARK 465 ALA C 538
REMARK 465 TRP C 539
REMARK 465 ALA C 540
REMARK 465 HIS C 541
REMARK 465 ASN C 542
REMARK 465 SER C 543
REMARK 465 SER C 544
REMARK 465 VAL C 648
REMARK 465 THR C 649
REMARK 465 TYR C 650
REMARK 465 ASP C 651
REMARK 465 HIS C 652
REMARK 465 PRO C 653
REMARK 465 SER C 654
REMARK 465 LYS C 655
REMARK 465 PRO C 656
REMARK 465 VAL C 657
REMARK 465 GLU C 658
REMARK 465 LYS C 659
REMARK 465 ARG C 660
REMARK 465 LEU C 661
REMARK 465 MET C 662
REMARK 465 PRO C 663
REMARK 465 PRO C 664
REMARK 465 PRO C 665
REMARK 465 PRO C 666
REMARK 465 GLN C 667
REMARK 465 LYS C 668
REMARK 465 ASN C 669
REMARK 465 LYS C 670
REMARK 465 ASP C 671
REMARK 465 SER C 672
REMARK 465 TRP C 673
REMARK 465 LEU C 674
REMARK 465 ASP C 675
REMARK 465 HIS C 676
REMARK 465 VAL C 677
REMARK 465 GLU D 0
REMARK 465 ALA D 1
REMARK 465 GLU D 2
REMARK 465 ALA D 3
REMARK 465 TYR D 4
REMARK 465 VAL D 5
REMARK 465 GLU D 6
REMARK 465 PHE D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 HIS D 11
REMARK 465 HIS D 12
REMARK 465 HIS D 13
REMARK 465 ASP D 14
REMARK 465 TYR D 15
REMARK 465 LYS D 16
REMARK 465 ASP D 17
REMARK 465 ASP D 18
REMARK 465 ASP D 19
REMARK 465 ASP D 20
REMARK 465 LYS D 21
REMARK 465 THR D 22
REMARK 465 SER D 23
REMARK 465 LEU D 24
REMARK 465 ARG D 25
REMARK 465 ASN D 26
REMARK 465 ALA D 27
REMARK 465 THR D 28
REMARK 465 HIS D 529
REMARK 465 ARG D 530
REMARK 465 ASP D 531
REMARK 465 SER D 532
REMARK 465 GLY D 533
REMARK 465 HIS D 534
REMARK 465 HIS D 535
REMARK 465 ASP D 536
REMARK 465 GLU D 537
REMARK 465 ALA D 538
REMARK 465 TRP D 539
REMARK 465 ALA D 540
REMARK 465 HIS D 541
REMARK 465 ASN D 542
REMARK 465 SER D 543
REMARK 465 SER D 544
REMARK 465 VAL D 648
REMARK 465 THR D 649
REMARK 465 TYR D 650
REMARK 465 ASP D 651
REMARK 465 HIS D 652
REMARK 465 PRO D 653
REMARK 465 SER D 654
REMARK 465 LYS D 655
REMARK 465 PRO D 656
REMARK 465 VAL D 657
REMARK 465 GLU D 658
REMARK 465 LYS D 659
REMARK 465 ARG D 660
REMARK 465 LEU D 661
REMARK 465 MET D 662
REMARK 465 PRO D 663
REMARK 465 PRO D 664
REMARK 465 PRO D 665
REMARK 465 PRO D 666
REMARK 465 GLN D 667
REMARK 465 LYS D 668
REMARK 465 ASN D 669
REMARK 465 LYS D 670
REMARK 465 ASP D 671
REMARK 465 SER D 672
REMARK 465 TRP D 673
REMARK 465 LEU D 674
REMARK 465 ASP D 675
REMARK 465 HIS D 676
REMARK 465 VAL D 677
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 CB ASN D 555 O5 NAG D 703 2.09
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 ASP A 101 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 206 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 MET A 609 CA - CB - CG ANGL. DEV. = 12.6 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 GLU A 100 -120.68 70.29
REMARK 500 CYS A 127 -106.25 64.61
REMARK 500 ASP A 151 121.86 -33.44
REMARK 500 GLU A 186 -160.60 60.66
REMARK 500 ALA A 315 -115.35 59.93
REMARK 500 ASN A 458 -16.93 73.75
REMARK 500 TYR A 488 41.04 -101.30
REMARK 500 LYS A 493 155.24 93.57
REMARK 500 SER A 503 -7.48 78.90
REMARK 500 ASP A 508 78.32 79.04
REMARK 500 THR A 577 -70.62 -134.10
REMARK 500 TRP A 592 65.88 -162.53
REMARK 500 SER A 611 -61.48 54.19
REMARK 500 GLU A 622 -50.70 -124.65
REMARK 500 CYS A 626 12.46 -143.00
REMARK 500 SER A 628 168.65 -34.86
REMARK 500 ASP A 629 42.67 -91.56
REMARK 500 ASP B 44 49.69 39.57
REMARK 500 GLU B 100 -123.50 57.80
REMARK 500 CYS B 127 -100.60 65.38
REMARK 500 GLU B 131 119.43 -35.91
REMARK 500 MET B 132 28.24 47.90
REMARK 500 GLU B 186 -163.82 60.45
REMARK 500 HIS B 224 137.42 -170.75
REMARK 500 GLU B 268 85.86 -152.58
REMARK 500 ALA B 315 -118.91 59.91
REMARK 500 TYR B 333 -0.30 76.08
REMARK 500 LEU B 382 -60.00 -100.02
REMARK 500 ASN B 458 -49.26 78.89
REMARK 500 TYR B 488 43.14 -97.13
REMARK 500 LYS B 493 155.99 78.51
REMARK 500 ASP B 508 84.35 68.58
REMARK 500 THR B 577 -67.37 -127.77
REMARK 500 TRP B 592 65.89 -155.52
REMARK 500 GLU C 100 -124.01 55.97
REMARK 500 CYS C 127 -103.81 66.23
REMARK 500 GLU C 131 117.55 -31.35
REMARK 500 GLU C 186 -170.43 59.58
REMARK 500 ALA C 315 -127.58 50.21
REMARK 500 TYR C 333 -6.12 76.22
REMARK 500 LEU C 382 -62.49 -101.47
REMARK 500 ASP C 448 56.89 37.43
REMARK 500 ASN C 459 -45.10 -151.48
REMARK 500 VAL C 483 129.14 -34.75
REMARK 500 TYR C 488 38.76 -98.34
REMARK 500 LYS C 493 150.55 78.20
REMARK 500 SER C 503 -8.32 62.77
REMARK 500 ASP C 508 87.62 66.88
REMARK 500 THR C 577 -64.49 -129.49
REMARK 500 TRP C 592 69.05 -152.85
REMARK 500
REMARK 500 THIS ENTRY HAS 67 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3WEZ RELATED DB: PDB
REMARK 900 RELATED ID: 3WF0 RELATED DB: PDB
REMARK 900 RELATED ID: 3WF1 RELATED DB: PDB
REMARK 900 RELATED ID: 3WF2 RELATED DB: PDB
REMARK 900 RELATED ID: 3WF4 RELATED DB: PDB
DBREF 3WF3 A 24 677 UNP P16278 BGAL_HUMAN 24 677
DBREF 3WF3 B 24 677 UNP P16278 BGAL_HUMAN 24 677
DBREF 3WF3 C 24 677 UNP P16278 BGAL_HUMAN 24 677
DBREF 3WF3 D 24 677 UNP P16278 BGAL_HUMAN 24 677
SEQADV 3WF3 GLU A 0 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA A 1 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU A 2 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA A 3 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR A 4 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 VAL A 5 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU A 6 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 PHE A 7 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS A 8 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS A 9 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS A 10 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS A 11 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS A 12 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS A 13 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP A 14 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR A 15 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS A 16 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP A 17 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP A 18 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP A 19 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP A 20 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS A 21 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR A 22 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 SER A 23 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR A 51 UNP P16278 ILE 51 ENGINEERED MUTATION
SEQADV 3WF3 GLU B 0 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA B 1 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU B 2 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA B 3 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR B 4 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 VAL B 5 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU B 6 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 PHE B 7 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS B 8 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS B 9 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS B 10 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS B 11 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS B 12 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS B 13 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP B 14 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR B 15 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS B 16 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP B 17 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP B 18 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP B 19 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP B 20 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS B 21 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR B 22 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 SER B 23 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR B 51 UNP P16278 ILE 51 ENGINEERED MUTATION
SEQADV 3WF3 GLU C 0 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA C 1 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU C 2 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA C 3 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR C 4 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 VAL C 5 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU C 6 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 PHE C 7 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS C 8 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS C 9 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS C 10 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS C 11 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS C 12 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS C 13 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP C 14 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR C 15 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS C 16 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP C 17 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP C 18 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP C 19 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP C 20 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS C 21 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR C 22 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 SER C 23 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR C 51 UNP P16278 ILE 51 ENGINEERED MUTATION
SEQADV 3WF3 GLU D 0 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA D 1 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU D 2 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ALA D 3 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR D 4 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 VAL D 5 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 GLU D 6 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 PHE D 7 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS D 8 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS D 9 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS D 10 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS D 11 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS D 12 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 HIS D 13 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP D 14 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 TYR D 15 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS D 16 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP D 17 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP D 18 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP D 19 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 ASP D 20 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 LYS D 21 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR D 22 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 SER D 23 UNP P16278 EXPRESSION TAG
SEQADV 3WF3 THR D 51 UNP P16278 ILE 51 ENGINEERED MUTATION
SEQRES 1 A 678 GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS
SEQRES 2 A 678 HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG
SEQRES 3 A 678 ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG
SEQRES 4 A 678 ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR
SEQRES 5 A 678 SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR
SEQRES 6 A 678 TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU
SEQRES 7 A 678 ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU
SEQRES 8 A 678 PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP
SEQRES 9 A 678 VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU
SEQRES 10 A 678 LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU
SEQRES 11 A 678 TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS
SEQRES 12 A 678 GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU
SEQRES 13 A 678 ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS
SEQRES 14 A 678 MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE
SEQRES 15 A 678 THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA
SEQRES 16 A 678 CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE
SEQRES 17 A 678 ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR
SEQRES 18 A 678 ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU
SEQRES 19 A 678 GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER
SEQRES 20 A 678 ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU
SEQRES 21 A 678 PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY
SEQRES 22 A 678 TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS
SEQRES 23 A 678 THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA
SEQRES 24 A 678 ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY
SEQRES 25 A 678 THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR
SEQRES 26 A 678 ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU
SEQRES 27 A 678 SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU
SEQRES 28 A 678 ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY
SEQRES 29 A 678 PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS
SEQRES 30 A 678 VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU
SEQRES 31 A 678 ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR
SEQRES 32 A 678 PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE
SEQRES 33 A 678 VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN
SEQRES 34 A 678 PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP
SEQRES 35 A 678 ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL
SEQRES 36 A 678 LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY
SEQRES 37 A 678 LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET
SEQRES 38 A 678 GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS
SEQRES 39 A 678 GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU
SEQRES 40 A 678 THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA
SEQRES 41 A 678 VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER
SEQRES 42 A 678 GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN
SEQRES 43 A 678 TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE
SEQRES 44 A 678 PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE
SEQRES 45 A 678 GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN
SEQRES 46 A 678 GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO
SEQRES 47 A 678 GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR
SEQRES 48 A 678 SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP
SEQRES 49 A 678 ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL
SEQRES 50 A 678 THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR
SEQRES 51 A 678 TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET
SEQRES 52 A 678 PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP
SEQRES 53 A 678 HIS VAL
SEQRES 1 B 678 GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS
SEQRES 2 B 678 HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG
SEQRES 3 B 678 ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG
SEQRES 4 B 678 ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR
SEQRES 5 B 678 SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR
SEQRES 6 B 678 TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU
SEQRES 7 B 678 ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU
SEQRES 8 B 678 PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP
SEQRES 9 B 678 VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU
SEQRES 10 B 678 LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU
SEQRES 11 B 678 TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS
SEQRES 12 B 678 GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU
SEQRES 13 B 678 ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS
SEQRES 14 B 678 MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE
SEQRES 15 B 678 THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA
SEQRES 16 B 678 CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE
SEQRES 17 B 678 ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR
SEQRES 18 B 678 ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU
SEQRES 19 B 678 GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER
SEQRES 20 B 678 ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU
SEQRES 21 B 678 PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY
SEQRES 22 B 678 TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS
SEQRES 23 B 678 THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA
SEQRES 24 B 678 ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY
SEQRES 25 B 678 THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR
SEQRES 26 B 678 ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU
SEQRES 27 B 678 SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU
SEQRES 28 B 678 ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY
SEQRES 29 B 678 PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS
SEQRES 30 B 678 VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU
SEQRES 31 B 678 ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR
SEQRES 32 B 678 PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE
SEQRES 33 B 678 VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN
SEQRES 34 B 678 PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP
SEQRES 35 B 678 ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL
SEQRES 36 B 678 LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY
SEQRES 37 B 678 LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET
SEQRES 38 B 678 GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS
SEQRES 39 B 678 GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU
SEQRES 40 B 678 THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA
SEQRES 41 B 678 VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER
SEQRES 42 B 678 GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN
SEQRES 43 B 678 TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE
SEQRES 44 B 678 PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE
SEQRES 45 B 678 GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN
SEQRES 46 B 678 GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO
SEQRES 47 B 678 GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR
SEQRES 48 B 678 SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP
SEQRES 49 B 678 ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL
SEQRES 50 B 678 THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR
SEQRES 51 B 678 TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET
SEQRES 52 B 678 PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP
SEQRES 53 B 678 HIS VAL
SEQRES 1 C 678 GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS
SEQRES 2 C 678 HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG
SEQRES 3 C 678 ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG
SEQRES 4 C 678 ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR
SEQRES 5 C 678 SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR
SEQRES 6 C 678 TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU
SEQRES 7 C 678 ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU
SEQRES 8 C 678 PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP
SEQRES 9 C 678 VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU
SEQRES 10 C 678 LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU
SEQRES 11 C 678 TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS
SEQRES 12 C 678 GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU
SEQRES 13 C 678 ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS
SEQRES 14 C 678 MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE
SEQRES 15 C 678 THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA
SEQRES 16 C 678 CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE
SEQRES 17 C 678 ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR
SEQRES 18 C 678 ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU
SEQRES 19 C 678 GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER
SEQRES 20 C 678 ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU
SEQRES 21 C 678 PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY
SEQRES 22 C 678 TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS
SEQRES 23 C 678 THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA
SEQRES 24 C 678 ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY
SEQRES 25 C 678 THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR
SEQRES 26 C 678 ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU
SEQRES 27 C 678 SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU
SEQRES 28 C 678 ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY
SEQRES 29 C 678 PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS
SEQRES 30 C 678 VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU
SEQRES 31 C 678 ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR
SEQRES 32 C 678 PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE
SEQRES 33 C 678 VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN
SEQRES 34 C 678 PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP
SEQRES 35 C 678 ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL
SEQRES 36 C 678 LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY
SEQRES 37 C 678 LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET
SEQRES 38 C 678 GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS
SEQRES 39 C 678 GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU
SEQRES 40 C 678 THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA
SEQRES 41 C 678 VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER
SEQRES 42 C 678 GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN
SEQRES 43 C 678 TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE
SEQRES 44 C 678 PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE
SEQRES 45 C 678 GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN
SEQRES 46 C 678 GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO
SEQRES 47 C 678 GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR
SEQRES 48 C 678 SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP
SEQRES 49 C 678 ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL
SEQRES 50 C 678 THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR
SEQRES 51 C 678 TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET
SEQRES 52 C 678 PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP
SEQRES 53 C 678 HIS VAL
SEQRES 1 D 678 GLU ALA GLU ALA TYR VAL GLU PHE HIS HIS HIS HIS HIS
SEQRES 2 D 678 HIS ASP TYR LYS ASP ASP ASP ASP LYS THR SER LEU ARG
SEQRES 3 D 678 ASN ALA THR GLN ARG MET PHE GLU ILE ASP TYR SER ARG
SEQRES 4 D 678 ASP SER PHE LEU LYS ASP GLY GLN PRO PHE ARG TYR THR
SEQRES 5 D 678 SER GLY SER ILE HIS TYR SER ARG VAL PRO ARG PHE TYR
SEQRES 6 D 678 TRP LYS ASP ARG LEU LEU LYS MET LYS MET ALA GLY LEU
SEQRES 7 D 678 ASN ALA ILE GLN THR TYR VAL PRO TRP ASN PHE HIS GLU
SEQRES 8 D 678 PRO TRP PRO GLY GLN TYR GLN PHE SER GLU ASP HIS ASP
SEQRES 9 D 678 VAL GLU TYR PHE LEU ARG LEU ALA HIS GLU LEU GLY LEU
SEQRES 10 D 678 LEU VAL ILE LEU ARG PRO GLY PRO TYR ILE CYS ALA GLU
SEQRES 11 D 678 TRP GLU MET GLY GLY LEU PRO ALA TRP LEU LEU GLU LYS
SEQRES 12 D 678 GLU SER ILE LEU LEU ARG SER SER ASP PRO ASP TYR LEU
SEQRES 13 D 678 ALA ALA VAL ASP LYS TRP LEU GLY VAL LEU LEU PRO LYS
SEQRES 14 D 678 MET LYS PRO LEU LEU TYR GLN ASN GLY GLY PRO VAL ILE
SEQRES 15 D 678 THR VAL GLN VAL GLU ASN GLU TYR GLY SER TYR PHE ALA
SEQRES 16 D 678 CYS ASP PHE ASP TYR LEU ARG PHE LEU GLN LYS ARG PHE
SEQRES 17 D 678 ARG HIS HIS LEU GLY ASP ASP VAL VAL LEU PHE THR THR
SEQRES 18 D 678 ASP GLY ALA HIS LYS THR PHE LEU LYS CYS GLY ALA LEU
SEQRES 19 D 678 GLN GLY LEU TYR THR THR VAL ASP PHE GLY THR GLY SER
SEQRES 20 D 678 ASN ILE THR ASP ALA PHE LEU SER GLN ARG LYS CYS GLU
SEQRES 21 D 678 PRO LYS GLY PRO LEU ILE ASN SER GLU PHE TYR THR GLY
SEQRES 22 D 678 TRP LEU ASP HIS TRP GLY GLN PRO HIS SER THR ILE LYS
SEQRES 23 D 678 THR GLU ALA VAL ALA SER SER LEU TYR ASP ILE LEU ALA
SEQRES 24 D 678 ARG GLY ALA SER VAL ASN LEU TYR MET PHE ILE GLY GLY
SEQRES 25 D 678 THR ASN PHE ALA TYR TRP ASN GLY ALA ASN SER PRO TYR
SEQRES 26 D 678 ALA ALA GLN PRO THR SER TYR ASP TYR ASP ALA PRO LEU
SEQRES 27 D 678 SER GLU ALA GLY ASP LEU THR GLU LYS TYR PHE ALA LEU
SEQRES 28 D 678 ARG ASN ILE ILE GLN LYS PHE GLU LYS VAL PRO GLU GLY
SEQRES 29 D 678 PRO ILE PRO PRO SER THR PRO LYS PHE ALA TYR GLY LYS
SEQRES 30 D 678 VAL THR LEU GLU LYS LEU LYS THR VAL GLY ALA ALA LEU
SEQRES 31 D 678 ASP ILE LEU CYS PRO SER GLY PRO ILE LYS SER LEU TYR
SEQRES 32 D 678 PRO LEU THR PHE ILE GLN VAL LYS GLN HIS TYR GLY PHE
SEQRES 33 D 678 VAL LEU TYR ARG THR THR LEU PRO GLN ASP CYS SER ASN
SEQRES 34 D 678 PRO ALA PRO LEU SER SER PRO LEU ASN GLY VAL HIS ASP
SEQRES 35 D 678 ARG ALA TYR VAL ALA VAL ASP GLY ILE PRO GLN GLY VAL
SEQRES 36 D 678 LEU GLU ARG ASN ASN VAL ILE THR LEU ASN ILE THR GLY
SEQRES 37 D 678 LYS ALA GLY ALA THR LEU ASP LEU LEU VAL GLU ASN MET
SEQRES 38 D 678 GLY ARG VAL ASN TYR GLY ALA TYR ILE ASN ASP PHE LYS
SEQRES 39 D 678 GLY LEU VAL SER ASN LEU THR LEU SER SER ASN ILE LEU
SEQRES 40 D 678 THR ASP TRP THR ILE PHE PRO LEU ASP THR GLU ASP ALA
SEQRES 41 D 678 VAL ARG SER HIS LEU GLY GLY TRP GLY HIS ARG ASP SER
SEQRES 42 D 678 GLY HIS HIS ASP GLU ALA TRP ALA HIS ASN SER SER ASN
SEQRES 43 D 678 TYR THR LEU PRO ALA PHE TYR MET GLY ASN PHE SER ILE
SEQRES 44 D 678 PRO SER GLY ILE PRO ASP LEU PRO GLN ASP THR PHE ILE
SEQRES 45 D 678 GLN PHE PRO GLY TRP THR LYS GLY GLN VAL TRP ILE ASN
SEQRES 46 D 678 GLY PHE ASN LEU GLY ARG TYR TRP PRO ALA ARG GLY PRO
SEQRES 47 D 678 GLN LEU THR LEU PHE VAL PRO GLN HIS ILE LEU MET THR
SEQRES 48 D 678 SER ALA PRO ASN THR ILE THR VAL LEU GLU LEU GLU TRP
SEQRES 49 D 678 ALA PRO CYS SER SER ASP ASP PRO GLU LEU CYS ALA VAL
SEQRES 50 D 678 THR PHE VAL ASP ARG PRO VAL ILE GLY SER SER VAL THR
SEQRES 51 D 678 TYR ASP HIS PRO SER LYS PRO VAL GLU LYS ARG LEU MET
SEQRES 52 D 678 PRO PRO PRO PRO GLN LYS ASN LYS ASP SER TRP LEU ASP
SEQRES 53 D 678 HIS VAL
MODRES 3WF3 ASN A 464 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN B 498 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN A 247 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN A 498 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN B 247 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN D 247 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN C 498 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN C 464 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN C 247 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN B 464 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN C 555 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN D 498 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN A 555 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN D 464 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN B 555 ASN GLYCOSYLATION SITE
MODRES 3WF3 ASN D 555 ASN GLYCOSYLATION SITE
HET NAG A 701 14
HET NAG A 702 14
HET NAG A 703 14
HET NAG A 704 14
HET GAL A 705 12
HET CL A 706 1
HET SO4 A 707 5
HET SO4 A 708 5
HET EDO A 709 4
HET EDO A 710 4
HET NAG B 701 14
HET NAG B 702 14
HET NAG B 703 14
HET NAG B 704 14
HET CL B 705 1
HET SO4 B 706 5
HET SO4 B 707 5
HET EDO B 708 4
HET EDO B 709 4
HET GAL B 710 12
HET NAG C 701 14
HET NAG C 702 14
HET NAG C 703 14
HET NAG C 704 14
HET CL C 705 1
HET GAL C 706 12
HET SO4 C 707 5
HET SO4 C 708 5
HET EDO C 709 4
HET EDO C 710 4
HET NAG D 701 14
HET NAG D 702 14
HET NAG D 703 14
HET NAG D 704 14
HET CL D 705 1
HET GAL D 706 12
HET SO4 D 707 5
HET SO4 D 708 5
HET EDO D 709 4
HET EDO D 710 4
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM GAL BETA-D-GALACTOPYRANOSE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
HETSYN GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 5 NAG 16(C8 H15 N O6)
FORMUL 9 GAL 4(C6 H12 O6)
FORMUL 10 CL 4(CL 1-)
FORMUL 11 SO4 8(O4 S 2-)
FORMUL 13 EDO 8(C2 H6 O2)
FORMUL 45 HOH *1428(H2 O)
HELIX 1 1 TYR A 57 VAL A 60 5 4
HELIX 2 2 PRO A 61 PHE A 63 5 3
HELIX 3 3 TYR A 64 ALA A 75 1 12
HELIX 4 4 PRO A 85 GLU A 90 1 6
HELIX 5 5 SER A 99 HIS A 102 5 4
HELIX 6 6 ASP A 103 LEU A 114 1 12
HELIX 7 7 TRP A 130 LEU A 135 5 6
HELIX 8 8 PRO A 136 LYS A 142 5 7
HELIX 9 9 ASP A 151 LYS A 170 1 20
HELIX 10 10 PRO A 171 GLY A 177 5 7
HELIX 11 11 GLU A 188 TYR A 192 5 5
HELIX 12 12 ASP A 196 GLY A 212 1 17
HELIX 13 13 HIS A 224 ALA A 232 1 9
HELIX 14 14 ASN A 247 GLU A 259 1 13
HELIX 15 15 LYS A 285 ARG A 299 1 15
HELIX 16 16 THR A 344 LYS A 356 1 13
HELIX 17 17 ALA A 388 CYS A 393 1 6
HELIX 18 18 PHE A 406 LYS A 410 5 5
HELIX 19 19 ASP A 515 SER A 522 1 8
HELIX 20 20 PRO A 604 LEU A 608 5 5
HELIX 21 21 ASP A 630 LEU A 633 5 4
HELIX 22 22 HIS B 56 VAL B 60 5 5
HELIX 23 23 PRO B 61 PHE B 63 5 3
HELIX 24 24 TYR B 64 ALA B 75 1 12
HELIX 25 25 PRO B 85 GLU B 90 1 6
HELIX 26 26 SER B 99 HIS B 102 5 4
HELIX 27 27 ASP B 103 LEU B 114 1 12
HELIX 28 28 TRP B 130 LEU B 135 5 6
HELIX 29 29 PRO B 136 LYS B 142 5 7
HELIX 30 30 ASP B 151 LYS B 170 1 20
HELIX 31 31 PRO B 171 GLY B 177 5 7
HELIX 32 32 GLU B 188 TYR B 192 5 5
HELIX 33 33 ASP B 196 GLY B 212 1 17
HELIX 34 34 HIS B 224 ALA B 232 1 9
HELIX 35 35 ASN B 247 GLU B 259 1 13
HELIX 36 36 LYS B 285 ARG B 299 1 15
HELIX 37 37 THR B 344 LYS B 356 1 13
HELIX 38 38 ALA B 388 CYS B 393 1 6
HELIX 39 39 PHE B 406 LYS B 410 5 5
HELIX 40 40 ASP B 515 SER B 522 1 8
HELIX 41 41 HIS B 523 GLY B 526 5 4
HELIX 42 42 PRO B 604 LEU B 608 5 5
HELIX 43 43 ASP B 630 LEU B 633 5 4
HELIX 44 44 TYR C 36 ASP C 39 5 4
HELIX 45 45 HIS C 56 VAL C 60 5 5
HELIX 46 46 PRO C 61 PHE C 63 5 3
HELIX 47 47 TYR C 64 ALA C 75 1 12
HELIX 48 48 PRO C 85 GLU C 90 1 6
HELIX 49 49 SER C 99 HIS C 102 5 4
HELIX 50 50 ASP C 103 LEU C 114 1 12
HELIX 51 51 TRP C 130 LEU C 135 5 6
HELIX 52 52 PRO C 136 LYS C 142 5 7
HELIX 53 53 ASP C 151 LYS C 170 1 20
HELIX 54 54 PRO C 171 GLY C 177 5 7
HELIX 55 55 GLU C 188 TYR C 192 5 5
HELIX 56 56 ASP C 196 GLY C 212 1 17
HELIX 57 57 HIS C 224 ALA C 232 1 9
HELIX 58 58 ASN C 247 GLU C 259 1 13
HELIX 59 59 LYS C 285 ARG C 299 1 15
HELIX 60 60 THR C 344 GLU C 358 1 15
HELIX 61 61 ALA C 388 CYS C 393 1 6
HELIX 62 62 ASP C 515 SER C 522 1 8
HELIX 63 63 PRO C 604 LEU C 608 5 5
HELIX 64 64 ASP C 630 LEU C 633 5 4
HELIX 65 65 TYR D 36 ASP D 39 5 4
HELIX 66 66 HIS D 56 VAL D 60 5 5
HELIX 67 67 PRO D 61 PHE D 63 5 3
HELIX 68 68 TYR D 64 ALA D 75 1 12
HELIX 69 69 PRO D 85 GLU D 90 1 6
HELIX 70 70 SER D 99 HIS D 102 5 4
HELIX 71 71 ASP D 103 LEU D 114 1 12
HELIX 72 72 TRP D 130 LEU D 135 5 6
HELIX 73 73 PRO D 136 LYS D 142 5 7
HELIX 74 74 ASP D 151 LYS D 170 1 20
HELIX 75 75 PRO D 171 GLY D 177 5 7
HELIX 76 76 GLU D 188 TYR D 192 5 5
HELIX 77 77 ASP D 196 GLY D 212 1 17
HELIX 78 78 HIS D 224 ALA D 232 1 9
HELIX 79 79 ASN D 247 GLU D 259 1 13
HELIX 80 80 LYS D 285 ARG D 299 1 15
HELIX 81 81 THR D 344 GLN D 355 1 12
HELIX 82 82 ALA D 388 CYS D 393 1 6
HELIX 83 83 ASP D 515 SER D 522 1 8
HELIX 84 84 PRO D 604 LEU D 608 5 5
HELIX 85 85 ASP D 630 LEU D 633 5 4
SHEET 1 A 3 PHE A 32 ASP A 35 0
SHEET 2 A 3 SER A 40 LYS A 43 -1 O SER A 40 N ASP A 35
SHEET 3 A 3 GLN A 46 PHE A 48 -1 O GLN A 46 N LYS A 43
SHEET 1 B 9 THR A 51 ILE A 55 0
SHEET 2 B 9 ALA A 79 TYR A 83 1 O GLN A 81 N ILE A 55
SHEET 3 B 9 LEU A 117 ARG A 121 1 O ILE A 119 N ILE A 80
SHEET 4 B 9 VAL A 180 GLN A 184 1 O GLN A 184 N LEU A 120
SHEET 5 B 9 VAL A 216 GLY A 222 1 O VAL A 216 N VAL A 183
SHEET 6 B 9 TYR A 237 ASP A 241 1 O TYR A 237 N THR A 219
SHEET 7 B 9 ILE A 265 TYR A 270 1 O SER A 267 N VAL A 240
SHEET 8 B 9 SER A 302 ILE A 309 1 O ASN A 304 N PHE A 269
SHEET 9 B 9 THR A 51 ILE A 55 1 N SER A 52 O VAL A 303
SHEET 1 C 2 ALA A 320 ASN A 321 0
SHEET 2 C 2 ALA A 325 ALA A 326 -1 O ALA A 325 N ASN A 321
SHEET 1 D 4 GLY A 375 THR A 378 0
SHEET 2 D 4 ALA A 635 VAL A 639 -1 O PHE A 638 N GLY A 375
SHEET 3 D 4 THR A 569 GLN A 572 -1 N PHE A 570 O VAL A 639
SHEET 4 D 4 LEU A 601 VAL A 603 -1 O VAL A 603 N THR A 569
SHEET 1 E 5 GLU A 380 THR A 384 0
SHEET 2 E 5 ALA A 550 PHE A 556 -1 O MET A 553 N GLU A 380
SHEET 3 E 5 ASN A 614 GLU A 620 -1 O ILE A 616 N GLY A 554
SHEET 4 E 5 GLY A 579 ILE A 583 -1 N GLN A 580 O LEU A 619
SHEET 5 E 5 PHE A 586 TYR A 591 -1 O PHE A 586 N ILE A 583
SHEET 1 F 6 ILE A 398 SER A 400 0
SHEET 2 F 6 TRP A 509 PRO A 513 -1 O TRP A 509 N SER A 400
SHEET 3 F 6 PHE A 415 THR A 421 -1 N ARG A 419 O THR A 510
SHEET 4 F 6 THR A 472 GLU A 478 -1 O LEU A 475 N TYR A 418
SHEET 5 F 6 ARG A 442 VAL A 447 -1 N ALA A 446 O ASP A 474
SHEET 6 F 6 ILE A 450 GLU A 456 -1 O GLN A 452 N VAL A 445
SHEET 1 G 4 THR A 462 GLY A 467 0
SHEET 2 G 4 CYS A 426 SER A 433 -1 N ALA A 430 O ILE A 465
SHEET 3 G 4 THR A 500 LEU A 501 -1 O THR A 500 N SER A 433
SHEET 4 G 4 ASN A 504 ILE A 505 -1 O ASN A 504 N LEU A 501
SHEET 1 H 2 VAL A 439 HIS A 440 0
SHEET 2 H 2 GLY A 494 LEU A 495 -1 O GLY A 494 N HIS A 440
SHEET 1 I 3 PHE B 32 ASP B 35 0
SHEET 2 I 3 SER B 40 LYS B 43 -1 O LEU B 42 N GLU B 33
SHEET 3 I 3 GLN B 46 PHE B 48 -1 O GLN B 46 N LYS B 43
SHEET 1 J 9 THR B 51 SER B 54 0
SHEET 2 J 9 ALA B 79 TYR B 83 1 O GLN B 81 N GLY B 53
SHEET 3 J 9 LEU B 117 ARG B 121 1 O ILE B 119 N ILE B 80
SHEET 4 J 9 VAL B 180 GLN B 184 1 O THR B 182 N LEU B 120
SHEET 5 J 9 VAL B 216 GLY B 222 1 O VAL B 216 N VAL B 183
SHEET 6 J 9 TYR B 237 ASP B 241 1 O TYR B 237 N LEU B 217
SHEET 7 J 9 ILE B 265 TYR B 270 1 O SER B 267 N VAL B 240
SHEET 8 J 9 SER B 302 TYR B 306 1 O ASN B 304 N PHE B 269
SHEET 9 J 9 THR B 51 SER B 54 1 N SER B 52 O VAL B 303
SHEET 1 K 2 ALA B 320 ASN B 321 0
SHEET 2 K 2 ALA B 325 ALA B 326 -1 O ALA B 325 N ASN B 321
SHEET 1 L 4 GLY B 375 THR B 378 0
SHEET 2 L 4 ALA B 635 VAL B 639 -1 O VAL B 636 N VAL B 377
SHEET 3 L 4 THR B 569 GLN B 572 -1 N GLN B 572 O THR B 637
SHEET 4 L 4 LEU B 601 VAL B 603 -1 O LEU B 601 N ILE B 571
SHEET 1 M 5 GLU B 380 THR B 384 0
SHEET 2 M 5 ALA B 550 PHE B 556 -1 O MET B 553 N GLU B 380
SHEET 3 M 5 ASN B 614 GLU B 620 -1 O ILE B 616 N GLY B 554
SHEET 4 M 5 GLY B 579 ILE B 583 -1 N TRP B 582 O THR B 617
SHEET 5 M 5 PHE B 586 TYR B 591 -1 O PHE B 586 N ILE B 583
SHEET 1 N 6 ILE B 398 SER B 400 0
SHEET 2 N 6 TRP B 509 PRO B 513 -1 O TRP B 509 N SER B 400
SHEET 3 N 6 PHE B 415 THR B 421 -1 N ARG B 419 O THR B 510
SHEET 4 N 6 THR B 472 GLU B 478 -1 O LEU B 475 N TYR B 418
SHEET 5 N 6 ARG B 442 VAL B 447 -1 N ALA B 446 O ASP B 474
SHEET 6 N 6 ILE B 450 GLU B 456 -1 O GLN B 452 N VAL B 445
SHEET 1 O 4 THR B 462 GLY B 467 0
SHEET 2 O 4 CYS B 426 SER B 433 -1 N LEU B 432 O LEU B 463
SHEET 3 O 4 THR B 500 LEU B 501 -1 O THR B 500 N SER B 433
SHEET 4 O 4 ASN B 504 ILE B 505 -1 O ASN B 504 N LEU B 501
SHEET 1 P 2 VAL B 439 HIS B 440 0
SHEET 2 P 2 GLY B 494 LEU B 495 -1 O GLY B 494 N HIS B 440
SHEET 1 Q 3 PHE C 32 ASP C 35 0
SHEET 2 Q 3 SER C 40 LYS C 43 -1 O SER C 40 N ASP C 35
SHEET 3 Q 3 GLN C 46 PHE C 48 -1 O GLN C 46 N LYS C 43
SHEET 1 R 9 THR C 51 SER C 54 0
SHEET 2 R 9 ALA C 79 TYR C 83 1 O GLN C 81 N GLY C 53
SHEET 3 R 9 LEU C 117 ARG C 121 1 O LEU C 117 N ILE C 80
SHEET 4 R 9 VAL C 180 GLN C 184 1 O ILE C 181 N VAL C 118
SHEET 5 R 9 VAL C 216 GLY C 222 1 O VAL C 216 N VAL C 183
SHEET 6 R 9 TYR C 237 ASP C 241 1 O TYR C 237 N THR C 219
SHEET 7 R 9 ILE C 265 TYR C 270 1 O SER C 267 N VAL C 240
SHEET 8 R 9 SER C 302 TYR C 306 1 O ASN C 304 N PHE C 269
SHEET 9 R 9 THR C 51 SER C 54 1 N SER C 54 O LEU C 305
SHEET 1 S 2 ALA C 320 ASN C 321 0
SHEET 2 S 2 ALA C 325 ALA C 326 -1 O ALA C 325 N ASN C 321
SHEET 1 T 4 GLY C 375 THR C 378 0
SHEET 2 T 4 ALA C 635 VAL C 639 -1 O VAL C 636 N VAL C 377
SHEET 3 T 4 THR C 569 GLN C 572 -1 N PHE C 570 O VAL C 639
SHEET 4 T 4 LEU C 601 VAL C 603 -1 O VAL C 603 N THR C 569
SHEET 1 U 5 GLU C 380 THR C 384 0
SHEET 2 U 5 ALA C 550 PHE C 556 -1 O PHE C 551 N LEU C 382
SHEET 3 U 5 ASN C 614 GLU C 620 -1 O ASN C 614 N PHE C 556
SHEET 4 U 5 GLY C 579 ILE C 583 -1 N TRP C 582 O THR C 617
SHEET 5 U 5 PHE C 586 TYR C 591 -1 O TYR C 591 N GLY C 579
SHEET 1 V 6 ILE C 398 SER C 400 0
SHEET 2 V 6 TRP C 509 PRO C 513 -1 O TRP C 509 N SER C 400
SHEET 3 V 6 GLY C 414 THR C 421 -1 N ARG C 419 O THR C 510
SHEET 4 V 6 THR C 472 ASN C 479 -1 O ASN C 479 N GLY C 414
SHEET 5 V 6 ARG C 442 VAL C 447 -1 N ALA C 446 O ASP C 474
SHEET 6 V 6 ILE C 450 GLU C 456 -1 O ILE C 450 N VAL C 447
SHEET 1 W 4 THR C 462 GLY C 467 0
SHEET 2 W 4 CYS C 426 SER C 433 -1 N LEU C 432 O LEU C 463
SHEET 3 W 4 THR C 500 LEU C 501 -1 O THR C 500 N SER C 433
SHEET 4 W 4 ASN C 504 ILE C 505 -1 O ASN C 504 N LEU C 501
SHEET 1 X 2 VAL C 439 HIS C 440 0
SHEET 2 X 2 GLY C 494 LEU C 495 -1 O GLY C 494 N HIS C 440
SHEET 1 Y 3 PHE D 32 ASP D 35 0
SHEET 2 Y 3 SER D 40 LYS D 43 -1 O SER D 40 N ASP D 35
SHEET 3 Y 3 GLN D 46 PHE D 48 -1 O GLN D 46 N LYS D 43
SHEET 1 Z 9 THR D 51 SER D 54 0
SHEET 2 Z 9 ALA D 79 TYR D 83 1 O GLN D 81 N GLY D 53
SHEET 3 Z 9 LEU D 117 ARG D 121 1 O ILE D 119 N ILE D 80
SHEET 4 Z 9 VAL D 180 GLN D 184 1 O ILE D 181 N VAL D 118
SHEET 5 Z 9 VAL D 216 GLY D 222 1 O PHE D 218 N VAL D 183
SHEET 6 Z 9 TYR D 237 ASP D 241 1 O TYR D 237 N THR D 219
SHEET 7 Z 9 ILE D 265 TYR D 270 1 O SER D 267 N VAL D 240
SHEET 8 Z 9 SER D 302 TYR D 306 1 O ASN D 304 N PHE D 269
SHEET 9 Z 9 THR D 51 SER D 54 1 N SER D 52 O VAL D 303
SHEET 1 AA 2 ALA D 320 ASN D 321 0
SHEET 2 AA 2 ALA D 325 ALA D 326 -1 O ALA D 325 N ASN D 321
SHEET 1 AB 4 GLY D 375 THR D 378 0
SHEET 2 AB 4 ALA D 635 VAL D 639 -1 O PHE D 638 N GLY D 375
SHEET 3 AB 4 THR D 569 GLN D 572 -1 N GLN D 572 O THR D 637
SHEET 4 AB 4 LEU D 601 VAL D 603 -1 O LEU D 601 N ILE D 571
SHEET 1 AC 5 GLU D 380 THR D 384 0
SHEET 2 AC 5 ALA D 550 PHE D 556 -1 O PHE D 551 N LEU D 382
SHEET 3 AC 5 ASN D 614 GLU D 620 -1 O VAL D 618 N TYR D 552
SHEET 4 AC 5 GLY D 579 ILE D 583 -1 N TRP D 582 O THR D 617
SHEET 5 AC 5 PHE D 586 TYR D 591 -1 O TYR D 591 N GLY D 579
SHEET 1 AD 6 ILE D 398 SER D 400 0
SHEET 2 AD 6 TRP D 509 PRO D 513 -1 O TRP D 509 N SER D 400
SHEET 3 AD 6 GLY D 414 THR D 421 -1 N LEU D 417 O PHE D 512
SHEET 4 AD 6 THR D 472 ASN D 479 -1 O LEU D 473 N THR D 420
SHEET 5 AD 6 ARG D 442 VAL D 447 -1 N ALA D 446 O ASP D 474
SHEET 6 AD 6 ILE D 450 GLU D 456 -1 O GLN D 452 N VAL D 445
SHEET 1 AE 4 THR D 462 GLY D 467 0
SHEET 2 AE 4 CYS D 426 SER D 433 -1 N ALA D 430 O ILE D 465
SHEET 3 AE 4 THR D 500 LEU D 501 -1 O THR D 500 N SER D 433
SHEET 4 AE 4 ASN D 504 ILE D 505 -1 O ASN D 504 N LEU D 501
SHEET 1 AF 2 VAL D 439 HIS D 440 0
SHEET 2 AF 2 GLY D 494 LEU D 495 -1 O GLY D 494 N HIS D 440
SSBOND 1 CYS A 195 CYS A 230 1555 1555 2.09
SSBOND 2 CYS A 626 CYS A 634 1555 1555 2.08
SSBOND 3 CYS B 195 CYS B 230 1555 1555 2.05
SSBOND 4 CYS B 626 CYS B 634 1555 1555 2.03
SSBOND 5 CYS C 195 CYS C 230 1555 1555 2.08
SSBOND 6 CYS C 626 CYS C 634 1555 1555 2.08
SSBOND 7 CYS D 195 CYS D 230 1555 1555 2.06
SSBOND 8 CYS D 626 CYS D 634 1555 1555 2.06
LINK ND2 ASN A 247 C1 NAG A 704 1555 1555 1.43
LINK ND2 ASN A 464 C1 NAG A 701 1555 1555 1.43
LINK ND2 ASN A 498 C1 NAG A 702 1555 1555 1.45
LINK ND2 ASN A 555 C1 NAG A 703 1555 1555 1.47
LINK ND2 ASN B 247 C1 NAG B 704 1555 1555 1.45
LINK ND2 ASN B 464 C1 NAG B 701 1555 1555 1.46
LINK ND2 ASN B 498 C1 NAG B 702 1555 1555 1.43
LINK ND2 ASN B 555 C1 NAG B 703 1555 1555 1.47
LINK ND2 ASN C 247 C1 NAG C 704 1555 1555 1.46
LINK ND2 ASN C 464 C1 NAG C 701 1555 1555 1.46
LINK ND2 ASN C 498 C1 NAG C 702 1555 1555 1.45
LINK ND2 ASN C 555 C1 NAG C 703 1555 1555 1.46
LINK ND2 ASN D 247 C1 NAG D 704 1555 1555 1.45
LINK ND2 ASN D 464 C1 NAG D 701 1555 1555 1.47
LINK ND2 ASN D 498 C1 NAG D 702 1555 1555 1.46
LINK ND2 ASN D 555 C1 NAG D 703 1555 1555 1.55
CISPEP 1 GLY A 123 PRO A 124 0 20.16
CISPEP 2 TYR A 306 MET A 307 0 -11.35
CISPEP 3 SER A 322 PRO A 323 0 3.25
CISPEP 4 HIS A 440 ASP A 441 0 18.55
CISPEP 5 LEU A 565 PRO A 566 0 3.50
CISPEP 6 GLY A 596 PRO A 597 0 6.95
CISPEP 7 GLY B 123 PRO B 124 0 10.88
CISPEP 8 TYR B 306 MET B 307 0 -8.21
CISPEP 9 SER B 322 PRO B 323 0 4.85
CISPEP 10 HIS B 440 ASP B 441 0 16.72
CISPEP 11 LEU B 565 PRO B 566 0 4.10
CISPEP 12 GLY B 596 PRO B 597 0 2.11
CISPEP 13 GLY C 123 PRO C 124 0 10.58
CISPEP 14 TYR C 306 MET C 307 0 -11.38
CISPEP 15 SER C 322 PRO C 323 0 -2.42
CISPEP 16 HIS C 440 ASP C 441 0 12.40
CISPEP 17 LEU C 565 PRO C 566 0 3.44
CISPEP 18 GLY C 596 PRO C 597 0 7.26
CISPEP 19 GLY D 123 PRO D 124 0 14.50
CISPEP 20 TYR D 306 MET D 307 0 -15.47
CISPEP 21 SER D 322 PRO D 323 0 3.29
CISPEP 22 HIS D 440 ASP D 441 0 20.42
CISPEP 23 LEU D 565 PRO D 566 0 0.86
CISPEP 24 GLY D 596 PRO D 597 0 -1.10
CRYST1 94.960 115.888 140.284 90.00 92.23 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 0.010531 0.000000 0.000410 0.00000
SCALE2 0.000000 0.008629 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007134 0.00000
(ATOM LINES ARE NOT SHOWN.)
END