HEADER HYDROLASE 29-JUL-96 1FSU
TITLE CRYSTAL STRUCTURE OF 4-SULFATASE (HUMAN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: N-ACETYLGALACTOSAMINE-4-SULFATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ARYLSULFATASE B, ASB, 4-SULFATASE;
COMPND 5 EC: 3.1.6.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LIVER;
SOURCE 6 CELLULAR_LOCATION: LYSOSOME;
SOURCE 7 GENE: G4S;
SOURCE 8 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;
SOURCE 9 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 10029;
SOURCE 11 EXPRESSION_SYSTEM_VARIANT: K1;
SOURCE 12 EXPRESSION_SYSTEM_CELL_LINE: CHO452;
SOURCE 13 EXPRESSION_SYSTEM_ORGANELLE: LYSOSOME;
SOURCE 14 EXPRESSION_SYSTEM_CELLULAR_LOCATION: SECRETED;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR: PEF NEO
KEYWDS SULFATASE, GLYCOSAMINOGLYCAN DEGRADATION, HYDROLASE, GLYCOPROTEIN,
KEYWDS 2 LYSOSOME
EXPDTA X-RAY DIFFRACTION
AUTHOR C.BOND,M.GUSS
REVDAT 6 26-MAR-25 1FSU 1 HETSYN
REVDAT 5 29-JUL-20 1FSU 1 COMPND REMARK SEQADV HETNAM
REVDAT 5 2 1 LINK SITE ATOM
REVDAT 4 02-DEC-15 1FSU 1 FORMUL HET HETATM HETNAM
REVDAT 4 2 1 REMARK
REVDAT 3 13-JUL-11 1FSU 1 VERSN
REVDAT 2 24-FEB-09 1FSU 1 VERSN
REVDAT 1 04-FEB-98 1FSU 0
JRNL AUTH C.S.BOND,P.R.CLEMENTS,S.J.ASHBY,C.A.COLLYER,S.J.HARROP,
JRNL AUTH 2 J.J.HOPWOOD,J.M.GUSS
JRNL TITL STRUCTURE OF A HUMAN LYSOSOMAL SULFATASE.
JRNL REF STRUCTURE V. 5 277 1997
JRNL REFN ISSN 0969-2126
JRNL PMID 9032078
JRNL DOI 10.1016/S0969-2126(97)00185-8
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : NULL
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) (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 27332
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) : 0.188
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.700
REMARK 3 FREE R VALUE TEST SET COUNT : 1032
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 73.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2047
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE : 0.2580
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.90
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 83
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 : 3811
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 58
REMARK 3 SOLVENT ATOMS : 270
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 7.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 6.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.33
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.600
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.080
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.500 ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.000 ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.500 ; 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 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FSU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173407.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : SEP-95
REMARK 200 TEMPERATURE (KELVIN) : 123
REMARK 200 PH : 5.1
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 RUH2R
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NI FILTER
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27332
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : NULL
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08900
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.25000
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS
REMARK 200 REPLACEMENT
REMARK 200 SOFTWARE USED: X-PLOR 3.1
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROPS, 0.2 M MALATE/ 0.1 M
REMARK 280 ACETATE BUFFERED AT PH 5.1. 12-15 % PEG8000, 20% GLYCEROL.,
REMARK 280 VAPOR DIFFUSION - HANGING DROP, VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 72.41500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.50000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.50000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 36.20750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.50000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.50000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 108.62250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.50000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.50000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 36.20750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.50000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.50000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 108.62250
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 72.41500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 PRO A 406
REMARK 465 ARG A 407
REMARK 465 ASN A 408
REMARK 465 SER A 409
REMARK 465 MET A 410
REMARK 465 ALA A 411
REMARK 465 PRO A 412
REMARK 465 ALA A 413
REMARK 465 LYS A 414
REMARK 465 ASP A 415
REMARK 465 ASP A 416
REMARK 465 SER A 417
REMARK 465 SER A 418
REMARK 465 LEU A 419
REMARK 465 PRO A 420
REMARK 465 GLU A 421
REMARK 465 TYR A 422
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 ALS A 91 -77.69 -52.56
REMARK 500 GLN A 112 -126.96 46.43
REMARK 500 TRP A 146 -76.22 -96.04
REMARK 500 MET A 150 6.18 -159.68
REMARK 500 GLU A 173 -176.78 -172.34
REMARK 500 GLU A 229 -8.59 89.37
REMARK 500 VAL A 241 54.11 -114.79
REMARK 500 GLU A 249 -30.89 -36.51
REMARK 500 ARG A 317 -166.78 -166.31
REMARK 500 TRP A 319 -21.54 87.47
REMARK 500 SER A 334 136.77 -170.85
REMARK 500 ASN A 394 158.89 175.24
REMARK 500 THR A 427 1.59 -67.79
REMARK 500 ASN A 458 50.56 -96.06
REMARK 500 TRP A 532 -5.99 -141.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 604 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 53 OD1
REMARK 620 2 ASP A 54 OD1 80.6
REMARK 620 3 ALS A 91 OS4 95.1 83.7
REMARK 620 4 ALS A 91 OS1 101.6 139.0 55.3
REMARK 620 5 ASP A 300 OD2 80.7 137.9 135.3 81.7
REMARK 620 6 ASP A 300 OD1 76.8 92.1 171.4 128.5 46.9
REMARK 620 7 ASN A 301 OD1 148.6 86.7 112.0 106.8 90.1 75.0
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: MEB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THIS IS THE METAL BINDING SITE. THE METAL WAS
REMARK 800 IDENTIFIED AS CALCIUM BY ITS PEAK HEIGHT IN DIFFERENCE ELECTRON
REMARK 800 DENSITY MAPS, BY SUCCESSIVE TEMPERATURE FACTOR REFINEMENT AND BY
REMARK 800 THE NATURE AND GEOMETRY OF THE COORDINATING LIGANDS.
REMARK 800
REMARK 800 SITE_IDENTIFIER: SAL
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: THESE RESIDUES AND THE METAL ION STABILIZE THE
REMARK 800 SULFATE ESTER RESIDUE 91. TOGETHER WITH THE METAL BINDING SITE
REMARK 800 THIS FORMS THE CENTER OF THE CATALYTIC ACTIVE SITE.
DBREF 1FSU A 42 533 UNP P15848 ARSB_HUMAN 42 533
SEQADV 1FSU ALS A 91 UNP P15848 CYS 91 CONFLICT
SEQRES 1 A 492 SER ARG PRO PRO HIS LEU VAL PHE LEU LEU ALA ASP ASP
SEQRES 2 A 492 LEU GLY TRP ASN ASP VAL GLY PHE HIS GLY SER ARG ILE
SEQRES 3 A 492 ARG THR PRO HIS LEU ASP ALA LEU ALA ALA GLY GLY VAL
SEQRES 4 A 492 LEU LEU ASP ASN TYR TYR THR GLN PRO LEU ALS THR PRO
SEQRES 5 A 492 SER ARG SER GLN LEU LEU THR GLY ARG TYR GLN ILE ARG
SEQRES 6 A 492 THR GLY LEU GLN HIS GLN ILE ILE TRP PRO CYS GLN PRO
SEQRES 7 A 492 SER CYS VAL PRO LEU ASP GLU LYS LEU LEU PRO GLN LEU
SEQRES 8 A 492 LEU LYS GLU ALA GLY TYR THR THR HIS MET VAL GLY LYS
SEQRES 9 A 492 TRP HIS LEU GLY MET TYR ARG LYS GLU CYS LEU PRO THR
SEQRES 10 A 492 ARG ARG GLY PHE ASP THR TYR PHE GLY TYR LEU LEU GLY
SEQRES 11 A 492 SER GLU ASP TYR TYR SER HIS GLU ARG CYS THR LEU ILE
SEQRES 12 A 492 ASP ALA LEU ASN VAL THR ARG CYS ALA LEU ASP PHE ARG
SEQRES 13 A 492 ASP GLY GLU GLU VAL ALA THR GLY TYR LYS ASN MET TYR
SEQRES 14 A 492 SER THR ASN ILE PHE THR LYS ARG ALA ILE ALA LEU ILE
SEQRES 15 A 492 THR ASN HIS PRO PRO GLU LYS PRO LEU PHE LEU TYR LEU
SEQRES 16 A 492 ALA LEU GLN SER VAL HIS GLU PRO LEU GLN VAL PRO GLU
SEQRES 17 A 492 GLU TYR LEU LYS PRO TYR ASP PHE ILE GLN ASP LYS ASN
SEQRES 18 A 492 ARG HIS HIS TYR ALA GLY MET VAL SER LEU MET ASP GLU
SEQRES 19 A 492 ALA VAL GLY ASN VAL THR ALA ALA LEU LYS SER SER GLY
SEQRES 20 A 492 LEU TRP ASN ASN THR VAL PHE ILE PHE SER THR ASP ASN
SEQRES 21 A 492 GLY GLY GLN THR LEU ALA GLY GLY ASN ASN TRP PRO LEU
SEQRES 22 A 492 ARG GLY ARG LYS TRP SER LEU TRP GLU GLY GLY VAL ARG
SEQRES 23 A 492 GLY VAL GLY PHE VAL ALA SER PRO LEU LEU LYS GLN LYS
SEQRES 24 A 492 GLY VAL LYS ASN ARG GLU LEU ILE HIS ILE SER ASP TRP
SEQRES 25 A 492 LEU PRO THR LEU VAL LYS LEU ALA ARG GLY HIS THR ASN
SEQRES 26 A 492 GLY THR LYS PRO LEU ASP GLY PHE ASP VAL TRP LYS THR
SEQRES 27 A 492 ILE SER GLU GLY SER PRO SER PRO ARG ILE GLU LEU LEU
SEQRES 28 A 492 HIS ASN ILE ASP PRO ASN PHE VAL ASP SER SER PRO CYS
SEQRES 29 A 492 PRO ARG ASN SER MET ALA PRO ALA LYS ASP ASP SER SER
SEQRES 30 A 492 LEU PRO GLU TYR SER ALA PHE ASN THR SER VAL HIS ALA
SEQRES 31 A 492 ALA ILE ARG HIS GLY ASN TRP LYS LEU LEU THR GLY TYR
SEQRES 32 A 492 PRO GLY CYS GLY TYR TRP PHE PRO PRO PRO SER GLN TYR
SEQRES 33 A 492 ASN VAL SER GLU ILE PRO SER SER ASP PRO PRO THR LYS
SEQRES 34 A 492 THR LEU TRP LEU PHE ASP ILE ASP ARG ASP PRO GLU GLU
SEQRES 35 A 492 ARG HIS ASP LEU SER ARG GLU TYR PRO HIS ILE VAL THR
SEQRES 36 A 492 LYS LEU LEU SER ARG LEU GLN PHE TYR HIS LYS HIS SER
SEQRES 37 A 492 VAL PRO VAL TYR PHE PRO ALA GLN ASP PRO ARG CYS ASP
SEQRES 38 A 492 PRO LYS ALA THR GLY VAL TRP GLY PRO TRP MET
MODRES 1FSU ASN A 279 ASN GLYCOSYLATION SITE
MODRES 1FSU ASN A 426 ASN GLYCOSYLATION SITE
MODRES 1FSU ALS A 91 ALA (3S)-3-(SULFOOXY)-L-SERINE
HET ALS A 91 11
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET CA A 604 1
HET CL A 605 1
HETNAM ALS (3S)-3-(SULFOOXY)-L-SERINE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE 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 1 ALS C3 H7 N O7 S
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 4 CA CA 2+
FORMUL 5 CL CL 1-
FORMUL 6 HOH *270(H2 O)
HELIX 1 1 GLY A 61 HIS A 63 5 3
HELIX 2 2 PRO A 70 ALA A 77 1 8
HELIX 3 3 PRO A 93 THR A 100 1 8
HELIX 4 4 GLN A 104 THR A 107 1 4
HELIX 5 5 LEU A 129 GLU A 135 1 7
HELIX 6 6 LYS A 153 CYS A 155 5 3
HELIX 7 7 PRO A 157 ARG A 159 5 3
HELIX 8 8 ASP A 185 LEU A 187 5 3
HELIX 9 9 SER A 211 THR A 224 1 14
HELIX 10 10 GLU A 249 TYR A 255 5 7
HELIX 11 11 LYS A 261 SER A 286 1 26
HELIX 12 12 TRP A 290 ASN A 292 5 3
HELIX 13 13 THR A 305 ALA A 307 5 3
HELIX 14 14 GLU A 323 VAL A 326 1 4
HELIX 15 15 ILE A 350 LEU A 360 5 11
HELIX 16 16 TRP A 377 GLU A 382 1 6
HELIX 17 17 PRO A 492 HIS A 508 1 17
HELIX 18 18 PRO A 519 CYS A 521 5 3
SHEET 1 A 6 THR A 164 PHE A 166 0
SHEET 2 A 6 TYR A 138 GLY A 144 1 N MET A 142 O THR A 164
SHEET 3 A 6 PRO A 231 ALA A 237 1 N PRO A 231 O THR A 139
SHEET 4 A 6 HIS A 46 ALA A 52 1 N LEU A 47 O LEU A 234
SHEET 5 A 6 THR A 293 THR A 299 1 N VAL A 294 O HIS A 46
SHEET 6 A 6 GLY A 330 ALA A 333 -1 N ALA A 333 O PHE A 295
SHEET 1 B 2 VAL A 80 LEU A 82 0
SHEET 2 B 2 VAL A 342 ASN A 344 1 N VAL A 342 O LEU A 81
SHEET 1 C 2 GLU A 179 ILE A 184 0
SHEET 2 C 2 VAL A 189 LEU A 194 -1 N ALA A 193 O ARG A 180
SHEET 1 D 4 LEU A 472 ASP A 476 0
SHEET 2 D 4 TRP A 438 THR A 442 -1 N LEU A 441 O TRP A 473
SHEET 3 D 4 HIS A 430 HIS A 435 -1 N HIS A 435 O TRP A 438
SHEET 4 D 4 GLU A 390 ASP A 396 -1 N ASP A 396 O HIS A 430
SSBOND 1 CYS A 117 CYS A 521 1555 1555 2.03
SSBOND 2 CYS A 121 CYS A 155 1555 1555 2.03
SSBOND 3 CYS A 181 CYS A 192 1555 1555 2.03
SSBOND 4 CYS A 405 CYS A 447 1555 1555 2.03
LINK C LEU A 90 N ALS A 91 1555 1555 1.33
LINK C ALS A 91 N THR A 92 1555 1555 1.34
LINK ND2 ASN A 279 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 426 C1 NAG C 1 1555 1555 1.48
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.46
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK OD1 ASP A 53 CA CA A 604 1555 1555 2.54
LINK OD1 ASP A 54 CA CA A 604 1555 1555 2.52
LINK OS4 ALS A 91 CA CA A 604 1555 1555 2.53
LINK OS1 ALS A 91 CA CA A 604 1555 1555 2.61
LINK OD2 ASP A 300 CA CA A 604 1555 1555 2.64
LINK OD1 ASP A 300 CA CA A 604 1555 1555 2.87
LINK OD1 ASN A 301 CA CA A 604 1555 1555 2.50
CISPEP 1 SER A 240 VAL A 241 0 -4.57
CISPEP 2 GLU A 243 PRO A 244 0 0.38
CISPEP 3 TRP A 312 PRO A 313 0 0.15
SITE 1 MEB 5 ASP A 53 ASP A 54 ALS A 91 ASP A 300
SITE 2 MEB 5 ASN A 301
SITE 1 SAL 6 ALS A 91 HIS A 242 LYS A 318 LYS A 145
SITE 2 SAL 6 ARG A 95 HIS A 147
CRYST1 107.000 107.000 144.830 90.00 90.00 90.00 P 41 21 2 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 0.009346 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009346 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006905 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
