HEADER HYDROLASE 10-DEC-04 1Y7V
TITLE X-RAY STRUCTURE OF HUMAN ACID-BETA-GLUCOSIDASE COVALENTLY BOUND TO
TITLE 2 CONDURITOL B EPOXIDE
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 ENGINEERED: YES;
COMPND 8 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: GBA, GC;
SOURCE 6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS
KEYWDS GAUCHER DISEASE, GLUCOSIDASE, GLUCOCEREBROSIDASE, CEREZYME,
KEYWDS 2 HYDROLASE, GLYCOSIDASE, SPHINGOLIPID METABOLISM, GLYCOPROTEIN,
KEYWDS 3 LYSOSOME, MEMBRANE, DISEASE MUTATION, ALTERNATIVE INITIATION, ISRAEL
KEYWDS 4 STRUCTURAL PROTEOMICS CENTER, ISPC, STRUCTURAL GENOMICS
EXPDTA X-RAY DIFFRACTION
AUTHOR L.PREMKUMAR,A.R.SAWKAR,S.BOLDIN-ADAMSKY,L.TOKER,I.SILMAN,J.W.KELLY,
AUTHOR 2 A.H.FUTERMAN,J.L.SUSSMAN,ISRAEL STRUCTURAL PROTEOMICS CENTER (ISPC)
REVDAT 8 23-AUG-23 1Y7V 1 REMARK
REVDAT 7 20-OCT-21 1Y7V 1 SEQADV HETSYN
REVDAT 6 29-JUL-20 1Y7V 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 13-JUL-11 1Y7V 1 VERSN
REVDAT 4 24-FEB-09 1Y7V 1 VERSN
REVDAT 3 26-JUL-05 1Y7V 1 JRNL
REVDAT 2 26-APR-05 1Y7V 1 SOURCE
REVDAT 1 12-APR-05 1Y7V 0
JRNL AUTH L.PREMKUMAR,A.R.SAWKAR,S.BOLDIN-ADAMSKY,L.TOKER,I.SILMAN,
JRNL AUTH 2 J.W.KELLY,A.H.FUTERMAN,J.L.SUSSMAN
JRNL TITL X-RAY STRUCTURE OF HUMAN ACID-BETA-GLUCOSIDASE COVALENTLY
JRNL TITL 2 BOUND TO CONDURITOL-B-EPOXIDE. IMPLICATIONS FOR GAUCHER
JRNL TITL 3 DISEASE.
JRNL REF J.BIOL.CHEM. V. 280 23815 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15817452
JRNL DOI 10.1074/JBC.M502799200
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 53193
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 SET) : 0.242
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2686
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7860
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 143
REMARK 3 SOLVENT ATOMS : 286
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 36.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 28.23000
REMARK 3 B22 (A**2) : -9.87000
REMARK 3 B33 (A**2) : -18.37000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.36
REMARK 3 ESD FROM SIGMAA (A) : 0.65
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.43
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.69
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.012
REMARK 3 BOND ANGLES (DEGREES) : 1.700
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.100
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1Y7V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031226.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55401
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
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 : 12.7500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.7
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 : 4.880
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIFFERENCE FOURIER
REMARK 200 TECHNIQUE
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1OGS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, GUANIDINE HCL, KCL,
REMARK 280 ACETATE , PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
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 45.75500
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 45.75500
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 52.24500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 142.80500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 52.24500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 142.80500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.75500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 52.24500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 142.80500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.75500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 52.24500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 142.80500
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, 3, 4, 5, 6
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 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: PISA
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -354.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 45.75500
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 52.24500
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 142.80500
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 45.75500
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 -52.24500
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 142.80500
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15580 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 66110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -350.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -45.75500
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 52.24500
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 142.80500
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 -45.75500
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 -52.24500
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 142.80500
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -166.0 KCAL/MOL
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 APPLY THE FOLLOWING TO CHAINS: B, D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 -52.24500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 142.80500
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 45.75500
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 OE2 GLU B 235 OH TYR B 313 2.12
REMARK 500 OD2 ASP B 127 O4 INS B 506 2.16
REMARK 500 OE2 GLU A 235 OH TYR A 313 2.16
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 CYS A 342 CB CYS A 342 SG -0.128
REMARK 500 CYS B 342 CB CYS B 342 SG -0.112
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 PRO A 245 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 ARG A 353 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 353 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 353 NE - CZ - NH2 ANGL. DEV. = -6.6 DEGREES
REMARK 500 PRO B 245 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 ARG B 353 NE - CZ - NH1 ANGL. DEV. = -6.2 DEGREES
REMARK 500 ARG B 353 NE - CZ - NH2 ANGL. DEV. = 5.0 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 THR A 63 32.97 -142.30
REMARK 500 PHE A 75 -142.77 -128.28
REMARK 500 ALA A 124 -148.42 84.43
REMARK 500 PHE A 128 55.24 -100.27
REMARK 500 TYR A 133 159.36 177.09
REMARK 500 ALA A 136 72.31 -154.12
REMARK 500 LEU A 156 -64.38 -100.96
REMARK 500 ASN A 192 -153.85 -116.99
REMARK 500 SER A 196 -162.65 -126.64
REMARK 500 ASP A 203 -166.81 -76.64
REMARK 500 GLU A 233 139.92 173.28
REMARK 500 GLU A 235 63.23 34.41
REMARK 500 GLN A 247 118.53 -39.90
REMARK 500 LEU A 249 96.38 -168.28
REMARK 500 LEU A 281 -82.61 66.14
REMARK 500 ALA A 318 69.90 -172.85
REMARK 500 PRO A 319 125.50 -32.80
REMARK 500 THR A 323 -76.55 -110.48
REMARK 500 LEU A 354 107.59 -48.79
REMARK 500 HIS A 374 -3.70 78.04
REMARK 500 TRP A 381 -128.36 -79.55
REMARK 500 ASN A 396 55.00 -98.00
REMARK 500 ASP A 409 46.75 38.21
REMARK 500 LEU A 436 96.04 -165.92
REMARK 500 THR B 63 -35.75 130.16
REMARK 500 PRO B 71 -30.79 -37.91
REMARK 500 PHE B 75 -142.92 -129.06
REMARK 500 ALA B 124 -148.78 84.72
REMARK 500 PHE B 128 58.96 -102.11
REMARK 500 TYR B 133 158.96 175.12
REMARK 500 ALA B 136 71.95 -156.12
REMARK 500 ASN B 146 31.37 -98.21
REMARK 500 ASP B 153 -60.29 -90.68
REMARK 500 LEU B 156 -65.82 -101.56
REMARK 500 ASN B 192 -155.08 -116.03
REMARK 500 SER B 196 -163.24 -126.14
REMARK 500 ASP B 203 -166.50 -77.95
REMARK 500 GLU B 233 138.27 174.75
REMARK 500 GLU B 235 62.92 34.73
REMARK 500 LEU B 249 95.57 -167.10
REMARK 500 LEU B 281 -79.84 64.40
REMARK 500 ALA B 318 67.71 -173.39
REMARK 500 PRO B 319 127.11 -31.51
REMARK 500 THR B 323 -77.50 -110.34
REMARK 500 PRO B 332 -19.54 -49.68
REMARK 500 LEU B 354 108.24 -51.41
REMARK 500 HIS B 374 -6.20 77.08
REMARK 500 TRP B 381 -129.65 -76.68
REMARK 500 TRP B 393 -8.16 -58.20
REMARK 500 ASN B 396 55.02 -96.02
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OGS RELATED DB: PDB
REMARK 900 NATIVE HUMAN ACID-BETA-GLUCOSIDASE
REMARK 900 RELATED ID: W00572 RELATED DB: TARGETDB
DBREF 1Y7V A 1 497 UNP P04062 GLCM_HUMAN 40 536
DBREF 1Y7V B 1 497 UNP P04062 GLCM_HUMAN 40 536
SEQADV 1Y7V HIS A 495 UNP P04062 ARG 534 ENGINEERED MUTATION
SEQADV 1Y7V HIS B 495 UNP P04062 ARG 534 ENGINEERED MUTATION
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
MODRES 1Y7V ASN A 19 ASN GLYCOSYLATION SITE
MODRES 1Y7V 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 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 INS A 507 11
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 INS B 506 11
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM SO4 SULFATE ION
HETNAM INS 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE
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 INS MYO-INOSITOL
FORMUL 3 NAG 4(C8 H15 N O6)
FORMUL 5 SO4 13(O4 S 2-)
FORMUL 12 INS 2(C6 H12 O6)
FORMUL 20 HOH *286(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 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 LYS A 408 5 3
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 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 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 TYR B 373 1 18
HELIX 31 31 ILE B 406 LYS B 408 5 3
HELIX 32 32 GLN B 414 LYS B 425 1 12
SHEET 1 A 4 PRO A 6 LYS A 7 0
SHEET 2 A 4 VAL A 15 ASN A 19 -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 ILE A 403 O TYR A 412
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 LEU A 444 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 66 LYS A 77 -1 N THR A 68 O VAL A 437
SHEET 8 B 9 VAL A 468 ASP A 474 1 O LYS A 473 N LEU A 67
SHEET 9 B 9 GLY A 478 SER A 484 -1 O SER A 484 N VAL A 468
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 SER A 177 N MET A 123
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 ARG A 277 N VAL A 230
SHEET 6 C 9 GLY A 307 TYR A 313 1 O GLY A 307 N MET A 280
SHEET 7 C 9 MET A 335 CYS A 342 1 O PHE A 337 N VAL A 310
SHEET 8 C 9 VAL A 375 ASN A 382 1 O VAL A 376 N LEU A 336
SHEET 9 C 9 GLY A 80 ALA A 84 1 N ALA A 84 O TRP A 381
SHEET 1 D 4 PRO B 6 LYS B 7 0
SHEET 2 D 4 VAL B 15 ASN B 19 -1 O VAL B 15 N LYS B 7
SHEET 3 D 4 THR B 410 LYS B 413 -1 O PHE B 411 N CYS B 18
SHEET 4 D 4 ILE B 402 ASP B 405 -1 N ILE B 403 O TYR B 412
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 458 O TYR B 492
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 67
SHEET 9 E 9 GLY B 478 SER B 484 -1 O GLY B 478 N ASP B 474
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 SER B 177 N MET B 123
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 ARG B 277 N VAL B 230
SHEET 6 F 9 GLY B 307 TYR B 313 1 O GLY B 307 N MET B 280
SHEET 7 F 9 MET B 335 CYS B 342 1 O PHE B 337 N VAL B 310
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
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.06
SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.04
SSBOND 3 CYS B 4 CYS B 16 1555 1555 2.06
SSBOND 4 CYS B 18 CYS B 23 1555 1555 2.05
LINK ND2 ASN A 19 C1 NAG C 1 1555 1555 1.46
LINK OE2 GLU A 340 C1 INS A 507 1555 1555 1.43
LINK ND2 ASN B 19 C1 NAG D 1 1555 1555 1.45
LINK OE2 GLU B 340 C1 INS B 506 1555 1555 1.43
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.39
LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.39
CISPEP 1 LEU A 288 PRO A 289 0 0.32
CISPEP 2 GLY A 390 PRO A 391 0 0.17
CISPEP 3 LEU B 288 PRO B 289 0 0.09
CISPEP 4 GLY B 390 PRO B 391 0 0.23
CRYST1 104.490 285.610 91.510 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 0.009570 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010928 0.00000
(ATOM LINES ARE NOT SHOWN.)
END