HEADER HYDROLASE 15-JUN-09 2WKL
TITLE VELAGLUCERASE ALFA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOSYLCERAMIDASE;
COMPND 3 CHAIN: A, B;
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 OTHER_DETAILS: GLYCOSYLATION ON ASN19 CHAIN A, ASN146 CHAIN A AND ON
COMPND 8 ASN19 CHAIN B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS ALTERNATIVE INITIATION, SPHINGOLIPID METABOLISM, MEMBRANE, LYSOSOME,
KEYWDS 2 HYDROLASE, ICHTHYOSIS, N-NONYL-DEOXYNOJIRIMYCIN, N-NONYL-
KEYWDS 3 DEOXYNOJIRIMYCIN ALTERNATIVE INITIATION, DISULFIDE BOND,
KEYWDS 4 PHARMACEUTICAL, GAUCHER DISEASE, GLYCOSIDASE, POLYMORPHISM,
KEYWDS 5 GLYCOPROTEIN, ALTERNATIVE SPLICING, ACID-BETA-GLUCOSIDASE, LIPID
KEYWDS 6 METABOLISM, DISEASE MUTATION, VELAGLUCERASE ALFA
EXPDTA X-RAY DIFFRACTION
AUTHOR B.BRUMSHTEIN,P.SALINAS,B.PETERSON,V.CHAN,I.SILMAN,J.L.SUSSMAN,
AUTHOR 2 P.J.SAVICKAS,G.S.ROBINSON,A.H.FUTERMAN
REVDAT 4 13-DEC-23 2WKL 1 HETSYN
REVDAT 3 29-JUL-20 2WKL 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 08-DEC-09 2WKL 1 COMPND JRNL
REVDAT 1 22-SEP-09 2WKL 0
JRNL AUTH B.BRUMSHTEIN,P.SALINAS,B.PETERSON,V.CHAN,I.SILMAN,
JRNL AUTH 2 J.L.SUSSMAN,P.J.SAVICKAS,G.S.ROBINSON,A.H.FUTERMAN
JRNL TITL CHARACTERIZATION OF GENE-ACTIVATED HUMAN
JRNL TITL 2 ACID-BETA-GLUCOSIDASE: CRYSTAL STRUCTURE, GLYCAN COMPOSITION
JRNL TITL 3 AND INTERNALIZATION INTO MACROPHAGES.
JRNL REF GLYCOBIOLOGY V. 20 24 2010
JRNL REFN ISSN 0959-6658
JRNL PMID 19741058
JRNL DOI 10.1093/GLYCOB/CWP138
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.91
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 37776
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2682
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.96
REMARK 3 BIN R VALUE (WORKING SET) : 0.2290
REMARK 3 BIN FREE R VALUE SET COUNT : 146
REMARK 3 BIN FREE R VALUE : 0.3170
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7781
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 326
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.84
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) : 0.00000
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): 0.629
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.301
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.199
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.819
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8170 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11159 ; 1.494 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 988 ; 6.468 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 349 ;36.460 ;23.324
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1225 ;17.676 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 43 ;25.213 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1218 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6190 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 4956 ; 0.551 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8004 ; 1.060 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3211 ; 1.524 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3155 ; 2.560 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 7
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 26 5
REMARK 3 1 B 1 B 26 5
REMARK 3 2 A 32 A 58 5
REMARK 3 2 B 32 B 58 5
REMARK 3 3 A 65 A 311 5
REMARK 3 3 B 65 B 311 5
REMARK 3 4 A 320 A 340 5
REMARK 3 4 B 320 B 340 5
REMARK 3 5 A 349 A 392 5
REMARK 3 5 B 349 B 392 5
REMARK 3 6 A 377 A 379 5
REMARK 3 6 B 377 B 379 5
REMARK 3 7 A 400 A 497 5
REMARK 3 7 B 400 B 497 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1864 ; 0.18 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1864 ; 0.18 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1775 ; 0.47 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 1775 ; 0.47 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1864 ; 0.75 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1864 ; 0.75 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1775 ; 0.91 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 1775 ; 0.91 ; 10.00
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. DISORDERED REGIONS WERE NOT MODELED
REMARK 4
REMARK 4 2WKL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUN-09.
REMARK 100 THE DEPOSITION ID IS D_1290040101.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.933
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39866
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.75
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2V3F
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M (NH4)2SO4/0.1 M HEPES, PH 7.0,
REMARK 280 0.5% (W/V) PEG8000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 45.84650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 45.84650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 54.68550
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 142.77600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.68550
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 142.77600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.84650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 54.68550
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 142.77600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.84650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 54.68550
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 142.77600
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2008 LIES ON A SPECIAL POSITION.
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 PHE A 31
REMARK 465 ALA A 318
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASN A 59 OD1 ND2
REMARK 470 LYS A 155 CD CE NZ
REMARK 470 GLN A 166 CG CD OE1 NE2
REMARK 470 LYS A 224 CE NZ
REMARK 470 GLU A 300 CD OE1 OE2
REMARK 470 PHE A 347 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 350 OE1 NE2
REMARK 470 LYS A 441 CG CD CE NZ
REMARK 470 LYS A 466 CD CE NZ
REMARK 470 ASN B 59 CG OD1 ND2
REMARK 470 GLU B 72 CD OE1 OE2
REMARK 470 LYS B 155 CD CE NZ
REMARK 470 ARG B 211 CD NE CZ NH1 NH2
REMARK 470 LYS B 224 CE NZ
REMARK 470 GLN B 226 CD OE1 NE2
REMARK 470 LYS B 346 CE NZ
REMARK 470 PHE B 397 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 408 CE NZ
REMARK 470 LYS B 441 CE NZ
REMARK 470 LYS B 466 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG A 285 O PRO A 319 1.62
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 19 -159.61 -145.80
REMARK 500 MET A 49 47.41 38.39
REMARK 500 GLN A 70 70.68 -115.53
REMARK 500 PHE A 75 -145.21 -116.22
REMARK 500 ASN A 117 16.62 -145.79
REMARK 500 ALA A 124 -161.02 76.25
REMARK 500 CYS A 126 -156.75 -127.21
REMARK 500 TYR A 133 147.23 -175.57
REMARK 500 ASN A 146 36.33 -98.66
REMARK 500 LEU A 156 -66.59 -123.16
REMARK 500 ASN A 192 -167.28 -124.81
REMARK 500 GLU A 233 128.48 160.03
REMARK 500 GLU A 235 66.42 33.91
REMARK 500 LEU A 281 -84.77 73.93
REMARK 500 THR A 323 -79.23 -121.67
REMARK 500 CYS A 342 164.88 175.74
REMARK 500 HIS A 374 -6.79 81.28
REMARK 500 TRP A 381 -134.00 -77.99
REMARK 500 ASN A 396 44.36 -88.06
REMARK 500 GLN A 440 147.08 175.13
REMARK 500 TYR A 487 62.22 60.30
REMARK 500 ASN B 19 -150.84 -141.63
REMARK 500 PHE B 75 -141.34 -127.47
REMARK 500 ASN B 117 18.70 -148.27
REMARK 500 ALA B 124 -154.70 77.31
REMARK 500 TYR B 133 151.73 174.22
REMARK 500 ALA B 136 71.08 -154.96
REMARK 500 LEU B 156 -70.36 -109.57
REMARK 500 TRP B 179 -62.21 -91.28
REMARK 500 ASN B 192 -159.82 -127.02
REMARK 500 GLU B 233 133.22 176.80
REMARK 500 TYR B 244 125.59 -39.70
REMARK 500 LEU B 249 109.62 -160.50
REMARK 500 ASN B 270 29.16 -78.69
REMARK 500 LEU B 281 -83.10 70.29
REMARK 500 TYR B 313 -57.05 -19.37
REMARK 500 LEU B 314 40.95 -106.50
REMARK 500 THR B 323 -77.40 -112.81
REMARK 500 SER B 345 -176.60 -58.34
REMARK 500 SER B 351 -108.36 67.73
REMARK 500 HIS B 374 5.93 82.67
REMARK 500 TRP B 381 -139.94 -78.40
REMARK 500 ASP B 405 79.18 -112.95
REMARK 500 ASP B 409 49.31 33.49
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 B 342 VAL B 343 -147.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AC", "BC" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V3F RELATED DB: PDB
REMARK 900 ACID-BETA-GLUCOSIDASE PRODUCED IN CARROT
REMARK 900 RELATED ID: 1Y7V RELATED DB: PDB
REMARK 900 X-RAY STRUCTURE OF HUMAN ACID-BETA- GLUCOSIDASE COVALENTLYBOUND TO
REMARK 900 CONDURITOL B EPOXIDE
REMARK 900 RELATED ID: 2J25 RELATED DB: PDB
REMARK 900 PARTIALLY DEGLYCOSYLATED GLUCOCERAMIDASE
REMARK 900 RELATED ID: 2V3E RELATED DB: PDB
REMARK 900 ACID-BETA-GLUCOSIDASE WITH N-NONYL- DEOXYNOJIRIMYCIN
REMARK 900 RELATED ID: 2F61 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED ACID BETA-GLUCOSIDASE
REMARK 900 RELATED ID: 2V3D RELATED DB: PDB
REMARK 900 ACID-BETA-GLUCOSIDASE WITH N-BUTYL- DEOXYNOJIRIMYCIN
REMARK 900 RELATED ID: 1OGS RELATED DB: PDB
REMARK 900 HUMAN ACID-BETA-GLUCOSIDASE
DBREF 2WKL A 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 2WKL B 1 497 UNP P04062 GLCM_HUMAN 40 536
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 ARG 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 ARG ARG GLN
MODRES 2WKL ASN A 19 ASN GLYCOSYLATION SITE
MODRES 2WKL ASN A 146 ASN GLYCOSYLATION SITE
MODRES 2WKL ASN B 19 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG D 1 14
HET NAG D 2 14
HET NAG A1498 14
HET SO4 A1501 5
HET SO4 A1502 5
HET SO4 A1503 5
HET SO4 A1504 5
HET SO4 A1505 5
HET SO4 A1506 5
HET SO4 A1507 5
HET SO4 A1508 5
HET SO4 A1509 5
HET SO4 B1500 5
HET SO4 B1501 5
HET SO4 B1502 5
HET SO4 B1503 5
HET SO4 B1504 5
HET SO4 B1505 5
HET SO4 B1506 5
HET SO4 B1507 5
HET SO4 B1508 5
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
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
FORMUL 3 NAG 5(C8 H15 N O6)
FORMUL 6 SO4 18(O4 S 2-)
FORMUL 24 HOH *326(H2 O)
HELIX 1 1 THR A 86 ALA A 95 1 10
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 LEU A 185 5 4
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 THR A 323 PHE A 331 1 9
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 ALA B 95 1 10
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 LEU B 185 5 4
HELIX 22 22 ASP B 203 HIS B 223 1 21
HELIX 23 23 SER B 237 LEU B 241 5 5
HELIX 24 24 THR B 252 ASP B 263 1 12
HELIX 25 25 ASP B 263 ASN B 270 1 8
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 ILE B 406 ASP B 409 5 4
HELIX 32 32 GLN B 414 LYS B 425 1 12
SHEET 1 AA 4 PRO A 6 LYS A 7 0
SHEET 2 AA 4 VAL A 15 CYS A 18 -1 O VAL A 15 N LYS A 7
SHEET 3 AA 4 THR A 410 LYS A 413 -1 O PHE A 411 N CYS A 18
SHEET 4 AA 4 ILE A 402 ASP A 405 -1 O ILE A 403 N TYR A 412
SHEET 1 AB 9 GLU A 50 PRO A 55 0
SHEET 2 AB 9 THR A 36 THR A 43 -1 O PHE A 37 N GLY A 54
SHEET 3 AB 9 SER A 488 TRP A 494 -1 O ILE A 489 N SER A 42
SHEET 4 AB 9 ALA A 456 ASN A 462 -1 O ALA A 456 N TRP A 494
SHEET 5 AB 9 LEU A 444 MET A 450 -1 O ASP A 445 N LEU A 461
SHEET 6 AB 9 GLN A 432 ALA A 438 -1 O GLN A 432 N MET A 450
SHEET 7 AB 9 LEU A 66 LYS A 77 -1 O THR A 68 N VAL A 437
SHEET 8 AB 9 VAL A 468 ASP A 474 1 O THR A 471 N LEU A 67
SHEET 9 AB 9 GLY A 478 SER A 484 -1 O GLY A 478 N ASP A 474
SHEET 1 AC 9 GLY A 80 ALA A 84 0
SHEET 2 AC 9 GLY A 377 ASN A 382 1 O TRP A 378 N GLY A 82
SHEET 3 AC 9 MET A 335 CYS A 342 1 O ALA A 338 N THR A 379
SHEET 4 AC 9 GLY A 307 TYR A 313 1 O ILE A 308 N PHE A 337
SHEET 5 AC 9 ARG A 277 GLN A 284 1 O MET A 280 N ALA A 309
SHEET 6 AC 9 ALA A 229 THR A 231 1 O VAL A 230 N LEU A 279
SHEET 7 AC 9 SER A 173 PRO A 178 1 O ALA A 176 N THR A 231
SHEET 8 AC 9 ILE A 118 MET A 123 1 O ILE A 119 N LEU A 175
SHEET 9 AC 9 GLY A 80 ALA A 84 1 O GLY A 83 N ARG A 120
SHEET 1 BA 4 PRO B 6 LYS B 7 0
SHEET 2 BA 4 VAL B 15 CYS B 18 -1 O VAL B 15 N LYS B 7
SHEET 3 BA 4 THR B 410 LYS B 413 -1 O PHE B 411 N CYS B 18
SHEET 4 BA 4 ILE B 402 ASP B 405 -1 O ILE B 403 N TYR B 412
SHEET 1 BB 9 GLU B 50 PRO B 55 0
SHEET 2 BB 9 THR B 36 THR B 43 -1 O PHE B 37 N GLY B 54
SHEET 3 BB 9 SER B 488 TRP B 494 -1 O ILE B 489 N SER B 42
SHEET 4 BB 9 ALA B 456 ASN B 462 -1 O ALA B 456 N TRP B 494
SHEET 5 BB 9 LEU B 444 MET B 450 -1 O ASP B 445 N LEU B 461
SHEET 6 BB 9 GLN B 432 ALA B 438 -1 O GLN B 432 N MET B 450
SHEET 7 BB 9 LEU B 65 LYS B 77 -1 O THR B 68 N VAL B 437
SHEET 8 BB 9 VAL B 468 ASP B 474 1 O PRO B 469 N LEU B 65
SHEET 9 BB 9 GLY B 478 SER B 484 -1 O GLY B 478 N ASP B 474
SHEET 1 BC 9 GLY B 80 ALA B 84 0
SHEET 2 BC 9 VAL B 375 ASN B 382 1 O TRP B 378 N GLY B 82
SHEET 3 BC 9 MET B 335 GLU B 340 1 O LEU B 336 N VAL B 376
SHEET 4 BC 9 GLY B 307 HIS B 311 1 O ILE B 308 N PHE B 337
SHEET 5 BC 9 ARG B 277 GLN B 284 1 O MET B 280 N ALA B 309
SHEET 6 BC 9 ALA B 229 THR B 231 1 O VAL B 230 N LEU B 279
SHEET 7 BC 9 SER B 173 PRO B 178 1 O ALA B 176 N THR B 231
SHEET 8 BC 9 ILE B 118 MET B 123 1 O ILE B 119 N LEU B 175
SHEET 9 BC 9 GLY B 80 ALA B 84 1 O GLY B 83 N ARG B 120
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.08
SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.09
SSBOND 3 CYS B 4 CYS B 16 1555 1555 2.06
SSBOND 4 CYS B 18 CYS B 23 1555 1555 2.07
LINK ND2 ASN A 19 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 146 C1 NAG A1498 1555 1555 1.45
LINK ND2 ASN B 19 C1 NAG D 1 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.45
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.42
CISPEP 1 LEU A 288 PRO A 289 0 5.60
CISPEP 2 GLY A 390 PRO A 391 0 9.37
CISPEP 3 LEU B 288 PRO B 289 0 4.04
CISPEP 4 GLY B 390 PRO B 391 0 2.62
CRYST1 109.371 285.552 91.693 90.00 90.00 90.00 C 2 2 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009143 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003502 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010906 0.00000
(ATOM LINES ARE NOT SHOWN.)
END