HEADER HYDROLASE 28-NOV-05 2F61
TITLE CRYSTAL STRUCTURE OF PARTIALLY DEGLYCOSYLATED ACID BETA-GLUCOSIDASE
CAVEAT 2F61 NAG A 1001 HAS WRONG CHIRALITY AT ATOM C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACID BETA-GLUCOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-GLUCOCEREBROSIDASE, GLUCOSYLCERAMIDASE, D-GLUCOSYL-N-
COMPND 5 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;
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: CHO;
SOURCE 10 EXPRESSION_SYSTEM_CELL: OVARY
KEYWDS ALPHA/BETA, TIM BARREL, IMMUNOGLOBULIN FOLD, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.S.HEGDE,G.GRABOWSKI
REVDAT 6 23-AUG-23 2F61 1 HETSYN
REVDAT 5 29-JUL-20 2F61 1 CAVEAT COMPND REMARK HET
REVDAT 5 2 1 HETNAM FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 13-JUL-11 2F61 1 VERSN
REVDAT 3 24-FEB-09 2F61 1 VERSN
REVDAT 2 28-FEB-06 2F61 1 JRNL
REVDAT 1 27-DEC-05 2F61 0
JRNL AUTH B.LIOU,A.KAZIMIERCZUK,M.ZHANG,C.R.SCOTT,R.S.HEGDE,
JRNL AUTH 2 G.A.GRABOWSKI
JRNL TITL ANALYSES OF VARIANT ACID BETA-GLUCOSIDASES: EFFECTS OF
JRNL TITL 2 GAUCHER DISEASE MUTATIONS.
JRNL REF J.BIOL.CHEM. V. 281 4242 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16293621
JRNL DOI 10.1074/JBC.M511110200
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 67.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 302034.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 84.6
REMARK 3 NUMBER OF REFLECTIONS : 41894
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) : 0.196
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4212
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.10
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6061
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE : 0.3350
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 673
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.013
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 : 72
REMARK 3 SOLVENT ATOMS : 406
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 13.80000
REMARK 3 B22 (A**2) : -4.35000
REMARK 3 B33 (A**2) : -9.46000
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) : 0.26
REMARK 3 ESD FROM SIGMAA (A) : 0.28
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) : 0.36
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.40
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.890
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) : 1.460 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.360 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.840 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.670 ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 33.85
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 : PROTEIN.TOP
REMARK 3 PARAMETER FILE 2 : CARBOHYDRATE.TOP
REMARK 3 PARAMETER FILE 3 : WATER.TOP
REMARK 3 PARAMETER FILE 4 : ION.TOP
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 2 : CARBOHYDRATE.PARAM
REMARK 3 TOPOLOGY FILE 3 : WATER_REP.PARAM
REMARK 3 TOPOLOGY FILE 4 : ION.PARAM
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2F61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-05.
REMARK 100 THE DEPOSITION ID IS D_1000035494.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 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 RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41998
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 67.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 89.0
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY: 1OGS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2-1.4 M AMMONIUM SULPHATE, 96 MM NA
REMARK 280 -CITRATE, 10 MM MGCL2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K, PH 6
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 45.77000
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 45.77000
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 54.32000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 142.21500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.32000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 142.21500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 45.77000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 54.32000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 142.21500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 45.77000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 54.32000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 142.21500
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER
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
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 APPLY THE FOLLOWING TO CHAINS: B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 32 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASN A 19 -158.00 -127.73
REMARK 500 PHE A 75 -134.13 -132.45
REMARK 500 ALA A 124 -156.51 81.96
REMARK 500 TYR A 133 160.39 176.47
REMARK 500 LEU A 156 -77.31 -98.14
REMARK 500 ASN A 192 -162.85 -129.12
REMARK 500 GLU A 233 142.63 170.07
REMARK 500 GLU A 235 64.91 36.25
REMARK 500 LEU A 249 93.59 -167.34
REMARK 500 LEU A 281 -79.72 61.41
REMARK 500 HIS A 311 -84.25 -109.25
REMARK 500 TRP A 312 122.43 49.94
REMARK 500 TYR A 313 -163.27 -72.08
REMARK 500 THR A 323 -73.73 -105.75
REMARK 500 LYS A 346 121.04 -32.78
REMARK 500 HIS A 374 -1.17 69.88
REMARK 500 TRP A 381 -138.11 -87.35
REMARK 500 ARG A 395 140.39 -177.30
REMARK 500 PHE A 397 -4.26 -149.32
REMARK 500 PHE A 423 -66.61 -105.84
REMARK 500 ILE A 427 79.42 -119.92
REMARK 500 VAL A 477 -53.13 -121.62
REMARK 500 CYS B 23 132.59 -171.08
REMARK 500 THR B 63 16.46 -164.59
REMARK 500 PHE B 75 -147.36 -136.01
REMARK 500 ALA B 124 -158.17 81.67
REMARK 500 ARG B 131 143.35 -176.53
REMARK 500 ALA B 136 76.21 -150.23
REMARK 500 LEU B 144 43.52 73.78
REMARK 500 LEU B 156 -73.39 -111.55
REMARK 500 ASN B 192 -158.84 -119.82
REMARK 500 GLU B 233 142.28 168.73
REMARK 500 GLU B 235 64.86 34.61
REMARK 500 ASP B 263 -72.72 -118.49
REMARK 500 LEU B 281 -80.62 66.56
REMARK 500 LEU B 314 -6.82 -53.12
REMARK 500 ALA B 322 -3.92 -56.32
REMARK 500 THR B 323 -82.30 -124.81
REMARK 500 LYS B 346 152.34 -49.85
REMARK 500 PHE B 347 21.10 -77.96
REMARK 500 TRP B 348 -7.48 -154.50
REMARK 500 GLN B 350 158.93 -46.60
REMARK 500 HIS B 374 -3.94 70.55
REMARK 500 TRP B 381 -138.00 -78.17
REMARK 500 PHE B 423 -60.04 -109.69
REMARK 500 GLN B 440 148.83 -172.29
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2F61 A 1 497 GB 183028 AAA35880 40 536
DBREF 2F61 B 1 497 GB 183028 AAA35880 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 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 2F61 ASN A 19 ASN GLYCOSYLATION SITE
MODRES 2F61 ASN B 19 ASN GLYCOSYLATION SITE
HET NAG C 1 14
HET NAG C 2 14
HET NAG A1001 14
HET SO4 A1500 5
HET SO4 A1502 5
HET SO4 A1501 5
HET SO4 B1503 5
HET SO4 B1504 5
HET SO4 B1505 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 3(C8 H15 N O6)
FORMUL 5 SO4 6(O4 S 2-)
FORMUL 11 HOH *406(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 GLN A 284 LEU A 288 5 5
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 LYS A 408 5 3
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 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 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 65 LYS A 77 -1 N GLN A 70 O GLY A 435
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 LEU A 480 N ILE A 472
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 ASP A 283 1 O LEU A 279 N VAL A 230
SHEET 6 C 9 GLY A 307 VAL A 310 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 VAL A 376 N LEU A 336
SHEET 9 C 9 GLY A 80 ALA A 84 1 N GLY A 82 O ASP A 380
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 ASP B 405 O THR B 410
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 VAL B 437 -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 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 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 GLY B 307 N MET B 280
SHEET 7 F 9 MET B 335 CYS B 342 1 O GLU B 340 N TRP B 312
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 GLY B 82 O ASP B 380
SSBOND 1 CYS A 4 CYS A 16 1555 1555 2.04
SSBOND 2 CYS A 18 CYS A 23 1555 1555 2.04
SSBOND 3 CYS B 4 CYS B 16 1555 1555 2.04
SSBOND 4 CYS B 18 CYS B 23 1555 1555 2.05
LINK ND2 ASN A 19 C1 NAG A1001 1555 1555 1.46
LINK ND2 ASN B 19 C1 NAG C 1 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.38
CISPEP 1 LEU A 288 PRO A 289 0 0.15
CISPEP 2 GLY A 390 PRO A 391 0 0.21
CISPEP 3 LEU B 288 PRO B 289 0 0.23
CISPEP 4 GLY B 390 PRO B 391 0 0.55
CRYST1 108.640 284.430 91.540 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 0.009200 0.000000 0.000000 0.00000
SCALE2 0.000000 0.003520 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010920 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
