HEADER HYDROLASE 02-APR-09 3GXM
TITLE CRYSTAL STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 4.5, PHOSPHATE
TITLE 2 CRYSTALLIZATION CONDITION
CAVEAT 3GXM NAG D 498 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: BETA-GLUCOCEREBROSIDASE, ACID BETA-GLUCOSIDASE, D-GLUCOSYL-
COMPND 5 N-ACYLSPHINGOSINE GLUCOHYDROLASE, ALGLUCERASE, IMIGLUCERASE;
COMPND 6 EC: 3.2.1.45;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: GBA, GC, GLUC;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029
KEYWDS HYDROLASE, ALTERNATIVE INITIATION, DISEASE MUTATION, DISULFIDE BOND,
KEYWDS 2 GAUCHER DISEASE, GLYCOPROTEIN, GLYCOSIDASE, ICHTHYOSIS, LIPID
KEYWDS 3 METABOLISM, LYSOSOME, MEMBRANE, SPHINGOLIPID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.L.LIEBERMAN
REVDAT 4 29-JUL-20 3GXM 1 CAVEAT COMPND REMARK HETNAM
REVDAT 4 2 1 LINK SITE
REVDAT 3 13-JUL-11 3GXM 1 VERSN
REVDAT 2 16-JUN-09 3GXM 1 JRNL
REVDAT 1 05-MAY-09 3GXM 0
JRNL AUTH R.L.LIEBERMAN,J.A.D'AQUINO,D.RINGE,G.A.PETSKO
JRNL TITL EFFECTS OF PH AND IMINOSUGAR PHARMACOLOGICAL CHAPERONES ON
JRNL TITL 2 LYSOSOMAL GLYCOSIDASE STRUCTURE AND STABILITY.
JRNL REF BIOCHEMISTRY V. 48 4816 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19374450
JRNL DOI 10.1021/BI9002265
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.34
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 138784
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) : 0.223
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6970
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8760
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.59
REMARK 3 BIN R VALUE (WORKING SET) : 0.4080
REMARK 3 BIN FREE R VALUE SET COUNT : 504
REMARK 3 BIN FREE R VALUE : 0.4710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15720
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 196
REMARK 3 SOLVENT ATOMS : 1144
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.01000
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): 0.259
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.226
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.196
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.245
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16384 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22368 ; 1.682 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1984 ; 7.689 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 720 ;37.157 ;23.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2516 ;17.716 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 84 ;21.807 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2440 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12532 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 8004 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 10770 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1245 ; 0.312 ; 0.200
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): 76 ; 0.192 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 20 ; 0.217 ; 0.200
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): 10168 ; 0.823 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16072 ; 1.394 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7140 ; 2.053 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6296 ; 3.084 ; 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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3GXM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-APR-09.
REMARK 100 THE DEPOSITION ID IS D_1000052433.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 138784
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 34.340
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION
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 45.88950
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13060 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -386.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 70180 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -378.0 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 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 91.77900
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -194.0 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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -174.0 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 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 LEU D 149 O HOH D 665 2.08
REMARK 500 O HOH B 580 O HOH B 1179 2.08
REMARK 500 O HOH D 535 O HOH D 1169 2.09
REMARK 500 O HOH B 522 O HOH B 1115 2.11
REMARK 500 O HOH D 524 O HOH D 1142 2.14
REMARK 500 O HOH C 521 O HOH C 1128 2.17
REMARK 500 OE2 GLU A 254 O HOH A 579 2.17
REMARK 500 OD2 ASP A 405 O HOH A 953 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TRP A 378 CB TRP A 378 CG -0.114
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 LEU A 165 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 PRO A 319 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU B 286 CA - CB - CG ANGL. DEV. = 19.8 DEGREES
REMARK 500 LEU B 480 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 ASN C 92 N - CA - C ANGL. DEV. = -22.6 DEGREES
REMARK 500 LEU D 480 CA - CB - CG ANGL. DEV. = 17.2 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 TYR A 11 -166.39 -101.00
REMARK 500 SER A 13 -157.30 -133.92
REMARK 500 ASN A 19 -155.62 -155.59
REMARK 500 ALA A 33 158.85 -49.03
REMARK 500 MET A 49 44.29 38.70
REMARK 500 PHE A 75 -137.70 -115.82
REMARK 500 ALA A 124 -153.69 74.07
REMARK 500 TYR A 133 150.64 163.70
REMARK 500 PRO A 150 -165.53 -72.93
REMARK 500 LEU A 156 -77.89 -99.39
REMARK 500 ASN A 188 1.67 -67.91
REMARK 500 ASN A 192 -163.93 -120.05
REMARK 500 SER A 196 -167.56 -122.66
REMARK 500 ASP A 203 -173.09 -67.90
REMARK 500 GLU A 233 144.85 -178.11
REMARK 500 ASP A 263 -64.14 -122.63
REMARK 500 HIS A 273 45.67 -102.78
REMARK 500 LEU A 281 -88.02 63.84
REMARK 500 TYR A 313 -64.49 -25.05
REMARK 500 LEU A 314 45.74 -98.47
REMARK 500 THR A 323 -71.32 -113.69
REMARK 500 VAL A 343 -93.11 -79.97
REMARK 500 SER A 345 -90.19 -76.85
REMARK 500 TRP A 381 -144.01 -75.20
REMARK 500 ARG A 395 130.77 179.60
REMARK 500 THR B 63 -56.36 90.37
REMARK 500 PHE B 75 -134.74 -113.01
REMARK 500 ALA B 124 -151.32 77.26
REMARK 500 PHE B 128 57.47 -93.02
REMARK 500 LEU B 156 -68.95 -106.64
REMARK 500 PRO B 182 141.68 -36.82
REMARK 500 GLU B 233 133.62 158.89
REMARK 500 LEU B 281 -82.76 78.56
REMARK 500 PHE B 316 67.67 -116.15
REMARK 500 LEU B 317 100.21 -52.78
REMARK 500 ALA B 320 -80.31 151.05
REMARK 500 THR B 323 -70.25 -119.54
REMARK 500 LYS B 346 85.51 -2.84
REMARK 500 GLN B 350 175.77 -59.28
REMARK 500 TRP B 381 -139.69 -73.92
REMARK 500 ASN C 19 -153.69 -140.81
REMARK 500 PHE C 75 -135.03 -121.26
REMARK 500 ASN C 92 -52.22 -129.15
REMARK 500 ALA C 124 -157.74 67.18
REMARK 500 TYR C 133 149.94 177.31
REMARK 500 ASP C 141 71.73 -100.89
REMARK 500 PRO C 150 -169.57 -76.67
REMARK 500 LEU C 156 -62.56 -104.78
REMARK 500 PRO C 182 139.81 -39.20
REMARK 500 LEU C 281 -87.34 71.12
REMARK 500
REMARK 500 THIS ENTRY HAS 72 RAMACHANDRAN OUTLIERS.
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 CYS A 342 VAL A 343 -147.70
REMARK 500 GLY B 344 SER B 345 145.48
REMARK 500 LEU C 91 ASN C 92 -118.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3GXF RELATED DB: PDB
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH ISOFAGOMINE AT NEUTRAL PH
REMARK 900 RELATED ID: 3GXI RELATED DB: PDB
REMARK 900 STRUCTURE OF ACID-BETA-GLUCOSIDASE AT PH 5.5
DBREF 3GXM A 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 3GXM B 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 3GXM C 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 3GXM D 1 497 UNP P04062 GLCM_HUMAN 40 536
SEQADV 3GXM HIS A 495 UNP P04062 ARG 534 VARIANT
SEQADV 3GXM HIS B 495 UNP P04062 ARG 534 VARIANT
SEQADV 3GXM HIS C 495 UNP P04062 ARG 534 VARIANT
SEQADV 3GXM HIS D 495 UNP P04062 ARG 534 VARIANT
SEQRES 1 A 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 A 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 A 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 A 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 A 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 A 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 A 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 A 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 A 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 A 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 A 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 A 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 A 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 A 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 A 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 A 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 A 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 A 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 A 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 A 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 A 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 A 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 A 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 A 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 A 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 A 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 A 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 A 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 A 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 A 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 A 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 A 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 A 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 A 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 A 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 A 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 A 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 A 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 A 497 HIS ARG GLN
SEQRES 1 B 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 B 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 B 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 B 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 B 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 B 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 B 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 B 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 B 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 B 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 B 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 B 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 B 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 B 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 B 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 B 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 B 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 B 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 B 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 B 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 B 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 B 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 B 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 B 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 B 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 B 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 B 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 B 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 B 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 B 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 B 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 B 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 B 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 B 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 B 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 B 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 B 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 B 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 B 497 HIS ARG GLN
SEQRES 1 C 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 C 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 C 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 C 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 C 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 C 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 C 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 C 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 C 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 C 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 C 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 C 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 C 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 C 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 C 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 C 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 C 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 C 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 C 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 C 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 C 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 C 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 C 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 C 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 C 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 C 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 C 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 C 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 C 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 C 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 C 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 C 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 C 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 C 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 C 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 C 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 C 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 C 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 C 497 HIS ARG GLN
SEQRES 1 D 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER
SEQRES 2 D 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE
SEQRES 3 D 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG
SEQRES 4 D 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER
SEQRES 5 D 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU
SEQRES 6 D 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL
SEQRES 7 D 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU
SEQRES 8 D 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU
SEQRES 9 D 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN
SEQRES 10 D 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE
SEQRES 11 D 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN
SEQRES 12 D 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU
SEQRES 13 D 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN
SEQRES 14 D 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO
SEQRES 15 D 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY
SEQRES 16 D 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR
SEQRES 17 D 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA
SEQRES 18 D 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN
SEQRES 19 D 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN
SEQRES 20 D 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE
SEQRES 21 D 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS
SEQRES 22 D 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU
SEQRES 23 D 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO
SEQRES 24 D 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP
SEQRES 25 D 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY
SEQRES 26 D 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA
SEQRES 27 D 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER
SEQRES 28 D 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER
SEQRES 29 D 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY
SEQRES 30 D 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY
SEQRES 31 D 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE
SEQRES 32 D 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET
SEQRES 33 D 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU
SEQRES 34 D 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN
SEQRES 35 D 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER
SEQRES 36 D 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL
SEQRES 37 D 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU
SEQRES 38 D 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP
SEQRES 39 D 497 HIS ARG GLN
MODRES 3GXM ASN A 19 ASN GLYCOSYLATION SITE
MODRES 3GXM ASN B 19 ASN GLYCOSYLATION SITE
MODRES 3GXM ASN C 19 ASN GLYCOSYLATION SITE
MODRES 3GXM ASN D 19 ASN GLYCOSYLATION SITE
HET NAG A 498 14
HET SO4 A 499 5
HET SO4 A 500 5
HET SO4 A 501 5
HET SO4 A 502 5
HET SO4 A 503 5
HET SO4 A 504 5
HET SO4 A 505 5
HET SO4 A 506 5
HET NAG B 498 14
HET SO4 B 499 5
HET SO4 B 500 5
HET SO4 B 501 5
HET SO4 B 502 5
HET SO4 B 503 5
HET SO4 B 504 5
HET SO4 B 505 5
HET NAG C 498 14
HET SO4 C 499 5
HET SO4 C 500 5
HET SO4 C 501 5
HET SO4 C 502 5
HET SO4 C 503 5
HET SO4 C 504 5
HET SO4 C 505 5
HET NAG D 498 14
HET SO4 D 499 5
HET SO4 D 500 5
HET SO4 D 501 5
HET SO4 D 502 5
HET SO4 D 503 5
HET SO4 D 504 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
FORMUL 5 NAG 4(C8 H15 N O6)
FORMUL 6 SO4 28(O4 S 2-)
FORMUL 37 HOH *1144(H2 O)
HELIX 1 1 THR A 86 LEU A 94 1 9
HELIX 2 2 SER A 97 SER A 110 1 14
HELIX 3 3 PRO A 150 LYS A 155 1 6
HELIX 4 4 LEU A 156 ALA A 168 1 13
HELIX 5 5 PRO A 182 LYS A 186 5 5
HELIX 6 6 ASP A 203 HIS A 223 1 21
HELIX 7 7 GLU A 235 LEU A 241 5 7
HELIX 8 8 THR A 252 ASP A 263 1 12
HELIX 9 9 ASP A 263 ASN A 270 1 8
HELIX 10 10 LEU A 286 LEU A 288 5 3
HELIX 11 11 PRO A 289 THR A 297 1 9
HELIX 12 12 ASP A 298 LYS A 303 1 6
HELIX 13 13 PRO A 319 PHE A 331 1 13
HELIX 14 14 SER A 356 TYR A 373 1 18
HELIX 15 15 ILE A 406 ASP A 409 5 4
HELIX 16 16 GLN A 414 LYS A 425 1 12
HELIX 17 17 THR B 86 LEU B 94 1 9
HELIX 18 18 SER B 97 SER B 110 1 14
HELIX 19 19 PRO B 150 LYS B 155 1 6
HELIX 20 20 LEU B 156 ALA B 168 1 13
HELIX 21 21 PRO B 182 LYS B 186 5 5
HELIX 22 22 ASP B 203 HIS B 223 1 21
HELIX 23 23 GLU B 235 LEU B 241 5 7
HELIX 24 24 THR B 252 ASP B 263 1 12
HELIX 25 25 ASP B 263 SER B 271 1 9
HELIX 26 26 LEU B 286 LEU B 288 5 3
HELIX 27 27 PRO B 289 THR B 297 1 9
HELIX 28 28 ASP B 298 LYS B 303 1 6
HELIX 29 29 THR B 323 PHE B 331 1 9
HELIX 30 30 SER B 356 LEU B 372 1 17
HELIX 31 31 GLN B 414 LYS B 425 1 12
HELIX 32 32 THR C 86 LEU C 94 1 9
HELIX 33 33 SER C 97 SER C 110 1 14
HELIX 34 34 PRO C 150 LYS C 155 1 6
HELIX 35 35 LEU C 156 ALA C 168 1 13
HELIX 36 36 PRO C 182 LYS C 186 5 5
HELIX 37 37 ASP C 203 HIS C 223 1 21
HELIX 38 38 GLU C 235 LEU C 241 5 7
HELIX 39 39 THR C 252 ASP C 263 1 12
HELIX 40 40 ASP C 263 ASN C 270 1 8
HELIX 41 41 LEU C 286 LEU C 288 5 3
HELIX 42 42 PRO C 289 THR C 297 1 9
HELIX 43 43 ASP C 298 LYS C 303 1 6
HELIX 44 44 PRO C 319 PHE C 331 1 13
HELIX 45 45 SER C 356 TYR C 373 1 18
HELIX 46 46 ILE C 406 ASP C 409 5 4
HELIX 47 47 GLN C 414 LYS C 425 1 12
HELIX 48 48 THR D 86 LEU D 94 1 9
HELIX 49 49 SER D 97 SER D 110 1 14
HELIX 50 50 PRO D 150 LYS D 155 1 6
HELIX 51 51 LEU D 156 ALA D 168 1 13
HELIX 52 52 PRO D 182 LYS D 186 5 5
HELIX 53 53 ASP D 203 GLU D 222 1 20
HELIX 54 54 GLU D 235 LEU D 241 5 7
HELIX 55 55 THR D 252 ASP D 263 1 12
HELIX 56 56 ASP D 263 ASN D 270 1 8
HELIX 57 57 LEU D 286 LEU D 288 5 3
HELIX 58 58 PRO D 289 THR D 297 1 9
HELIX 59 59 ASP D 298 LYS D 303 1 6
HELIX 60 60 THR D 323 PHE D 331 1 9
HELIX 61 61 SER D 356 TYR D 373 1 18
HELIX 62 62 ILE D 406 ASP D 409 5 4
HELIX 63 63 GLN D 414 LYS D 425 1 12
SHEET 1 A 4 PRO A 6 LYS A 7 0
SHEET 2 A 4 VAL A 15 CYS A 18 -1 O VAL A 15 N LYS A 7
SHEET 3 A 4 THR A 410 LYS A 413 -1 O PHE A 411 N CYS A 18
SHEET 4 A 4 ILE A 402 ASP A 405 -1 N ASP A 405 O THR A 410
SHEET 1 B 9 GLU A 50 PRO A 55 0
SHEET 2 B 9 THR A 36 THR A 43 -1 N ARG A 39 O SER A 52
SHEET 3 B 9 SER A 488 TRP A 494 -1 O LEU A 493 N SER A 38
SHEET 4 B 9 ALA A 456 ASN A 462 -1 N VAL A 458 O TYR A 492
SHEET 5 B 9 ASP A 445 MET A 450 -1 N ASP A 445 O LEU A 461
SHEET 6 B 9 GLN A 432 ALA A 438 -1 N GLN A 432 O MET A 450
SHEET 7 B 9 LEU A 65 LYS A 77 -1 N PHE A 75 O ARG A 433
SHEET 8 B 9 VAL A 468 ASP A 474 1 O LYS A 473 N LEU A 69
SHEET 9 B 9 GLY A 478 SER A 484 -1 O THR A 482 N LEU A 470
SHEET 1 C 9 GLY A 80 ALA A 84 0
SHEET 2 C 9 ILE A 118 MET A 123 1 O ARG A 120 N GLY A 83
SHEET 3 C 9 SER A 173 PRO A 178 1 O LEU A 175 N VAL A 121
SHEET 4 C 9 ALA A 229 THR A 231 1 O THR A 231 N ALA A 176
SHEET 5 C 9 ARG A 277 GLN A 284 1 O LEU A 279 N VAL A 230
SHEET 6 C 9 GLY A 307 HIS A 311 1 O ALA A 309 N MET A 280
SHEET 7 C 9 MET A 335 ALA A 341 1 O MET A 335 N ILE A 308
SHEET 8 C 9 VAL A 375 ASN A 382 1 O THR A 379 N ALA A 341
SHEET 9 C 9 GLY A 80 ALA A 84 1 N GLY A 82 O ASP A 380
SHEET 1 D 5 PRO B 6 LYS B 7 0
SHEET 2 D 5 VAL B 15 CYS B 18 -1 O VAL B 15 N LYS B 7
SHEET 3 D 5 THR B 410 LYS B 413 -1 O PHE B 411 N CYS B 18
SHEET 4 D 5 ILE B 402 ASP B 405 -1 N ASP B 405 O THR B 410
SHEET 5 D 5 ALA B 384 LEU B 385 1 N LEU B 385 O VAL B 404
SHEET 1 E 9 GLU B 50 PRO B 55 0
SHEET 2 E 9 THR B 36 THR B 43 -1 N ARG B 39 O SER B 52
SHEET 3 E 9 SER B 488 TRP B 494 -1 O LEU B 493 N SER B 38
SHEET 4 E 9 ALA B 456 ASN B 462 -1 N VAL B 460 O HIS B 490
SHEET 5 E 9 LEU B 444 MET B 450 -1 N ASP B 445 O LEU B 461
SHEET 6 E 9 GLN B 432 ALA B 438 -1 N GLN B 432 O MET B 450
SHEET 7 E 9 LEU B 65 LYS B 77 -1 N THR B 68 O VAL B 437
SHEET 8 E 9 VAL B 468 ASP B 474 1 O LYS B 473 N LEU B 69
SHEET 9 E 9 GLY B 478 SER B 484 -1 O SER B 484 N VAL B 468
SHEET 1 F 9 GLY B 80 ALA B 84 0
SHEET 2 F 9 ILE B 118 MET B 123 1 O ARG B 120 N GLY B 83
SHEET 3 F 9 SER B 173 PRO B 178 1 O LEU B 175 N VAL B 121
SHEET 4 F 9 ALA B 229 THR B 231 1 O THR B 231 N ALA B 176
SHEET 5 F 9 ARG B 277 GLN B 284 1 O LEU B 279 N VAL B 230
SHEET 6 F 9 GLY B 307 TYR B 313 1 O ALA B 309 N MET B 280
SHEET 7 F 9 MET B 335 CYS B 342 1 O MET B 335 N ILE B 308
SHEET 8 F 9 VAL B 375 ASN B 382 1 O VAL B 376 N LEU B 336
SHEET 9 F 9 GLY B 80 ALA B 84 1 N ALA B 84 O TRP B 381
SHEET 1 G 5 PRO C 6 LYS C 7 0
SHEET 2 G 5 VAL C 15 CYS C 18 -1 O VAL C 15 N LYS C 7
SHEET 3 G 5 THR C 410 LYS C 413 -1 O PHE C 411 N CYS C 18
SHEET 4 G 5 ILE C 402 ASP C 405 -1 N ILE C 403 O TYR C 412
SHEET 5 G 5 ALA C 384 LEU C 385 1 N LEU C 385 O VAL C 404
SHEET 1 H 9 GLU C 50 PRO C 55 0
SHEET 2 H 9 THR C 36 THR C 43 -1 N GLU C 41 O GLU C 50
SHEET 3 H 9 SER C 488 TRP C 494 -1 O LEU C 493 N SER C 38
SHEET 4 H 9 ALA C 456 ASN C 462 -1 N VAL C 458 O TYR C 492
SHEET 5 H 9 ASP C 445 MET C 450 -1 N ASP C 445 O LEU C 461
SHEET 6 H 9 GLN C 432 ALA C 438 -1 N GLN C 432 O MET C 450
SHEET 7 H 9 LEU C 65 LYS C 77 -1 N PHE C 75 O ARG C 433
SHEET 8 H 9 VAL C 468 ASP C 474 1 O THR C 471 N LEU C 67
SHEET 9 H 9 GLY C 478 SER C 484 -1 O SER C 484 N VAL C 468
SHEET 1 I 9 GLY C 80 ALA C 84 0
SHEET 2 I 9 ILE C 118 MET C 123 1 O ARG C 120 N GLY C 83
SHEET 3 I 9 SER C 173 PRO C 178 1 O LEU C 175 N VAL C 121
SHEET 4 I 9 ALA C 229 THR C 231 1 O THR C 231 N ALA C 176
SHEET 5 I 9 ARG C 277 GLN C 284 1 O LEU C 279 N VAL C 230
SHEET 6 I 9 GLY C 307 HIS C 311 1 O ALA C 309 N MET C 280
SHEET 7 I 9 MET C 335 GLU C 340 1 O MET C 335 N ILE C 308
SHEET 8 I 9 VAL C 375 ASN C 382 1 O VAL C 376 N LEU C 336
SHEET 9 I 9 GLY C 80 ALA C 84 1 N GLY C 82 O ASP C 380
SHEET 1 J 4 PRO D 6 LYS D 7 0
SHEET 2 J 4 VAL D 15 CYS D 18 -1 O VAL D 15 N LYS D 7
SHEET 3 J 4 THR D 410 LYS D 413 -1 O PHE D 411 N CYS D 18
SHEET 4 J 4 ILE D 402 ASP D 405 -1 N ASP D 405 O THR D 410
SHEET 1 K 9 GLU D 50 PRO D 55 0
SHEET 2 K 9 THR D 36 THR D 43 -1 N GLU D 41 O GLU D 50
SHEET 3 K 9 SER D 488 TRP D 494 -1 O LEU D 493 N SER D 38
SHEET 4 K 9 ALA D 456 ASN D 462 -1 N VAL D 460 O HIS D 490
SHEET 5 K 9 LEU D 444 MET D 450 -1 N ASP D 445 O LEU D 461
SHEET 6 K 9 GLN D 432 ALA D 438 -1 N GLN D 432 O MET D 450
SHEET 7 K 9 LEU D 65 LYS D 77 -1 N PHE D 75 O ARG D 433
SHEET 8 K 9 VAL D 468 ASP D 474 1 O LYS D 473 N LEU D 69
SHEET 9 K 9 GLY D 478 SER D 484 -1 O SER D 484 N VAL D 468
SHEET 1 L 9 GLY D 80 ALA D 84 0
SHEET 2 L 9 ILE D 118 MET D 123 1 O ARG D 120 N GLY D 83
SHEET 3 L 9 SER D 173 PRO D 178 1 O LEU D 175 N VAL D 121
SHEET 4 L 9 ALA D 229 THR D 231 1 O THR D 231 N ALA D 176
SHEET 5 L 9 ARG D 277 GLN D 284 1 O LEU D 279 N VAL D 230
SHEET 6 L 9 GLY D 307 TYR D 313 1 O ALA D 309 N MET D 280
SHEET 7 L 9 MET D 335 CYS D 342 1 O MET D 335 N ILE D 308
SHEET 8 L 9 VAL D 375 ASN D 382 1 O VAL D 376 N LEU D 336
SHEET 9 L 9 GLY D 80 ALA D 84 1 N GLY D 82 O ASP D 380
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.06
SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.10
SSBOND 3 CYS B 4 CYS B 16 1555 1555 2.12
SSBOND 4 CYS B 18 CYS B 23 1555 1555 2.13
SSBOND 5 CYS C 4 CYS C 16 1555 1555 2.06
SSBOND 6 CYS C 18 CYS C 23 1555 1555 2.13
SSBOND 7 CYS D 4 CYS D 16 1555 1555 2.12
SSBOND 8 CYS D 18 CYS D 23 1555 1555 2.14
LINK ND2 ASN A 19 C1 NAG A 498 1555 1555 1.45
LINK ND2 ASN B 19 C1 NAG B 498 1555 1555 1.47
LINK ND2 ASN C 19 C1 NAG C 498 1555 1555 1.45
LINK ND2 ASN D 19 C1 NAG D 498 1555 1555 1.46
CISPEP 1 LEU A 288 PRO A 289 0 2.69
CISPEP 2 GLY A 344 SER A 345 0 -19.60
CISPEP 3 GLY A 390 PRO A 391 0 -0.93
CISPEP 4 GLY B 62 THR B 63 0 13.87
CISPEP 5 LEU B 288 PRO B 289 0 -0.39
CISPEP 6 PRO B 319 ALA B 320 0 -3.85
CISPEP 7 GLY B 390 PRO B 391 0 4.82
CISPEP 8 LEU C 288 PRO C 289 0 2.58
CISPEP 9 TYR C 313 LEU C 314 0 24.98
CISPEP 10 VAL C 343 GLY C 344 0 0.87
CISPEP 11 GLY C 390 PRO C 391 0 -1.81
CISPEP 12 LEU D 288 PRO D 289 0 1.43
CISPEP 13 GLY D 390 PRO D 391 0 6.20
CRYST1 110.505 91.779 152.751 90.00 111.24 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 0.009049 0.000000 0.003517 0.00000
SCALE2 0.000000 0.010896 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007024 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
