HEADER HYDROLASE 30-SEP-08 3EQA
TITLE CATALYTIC DOMAIN OF GLUCOAMYLASE FROM ASPERGILLUS NIGER COMPLEXED WITH
TITLE 2 TRIS AND GLYCEROL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCOAMYLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN (RESIDUES 25-494);
COMPND 5 SYNONYM: GLUCAN 1,4-ALPHA-GLUCOSIDASE; 1,4-ALPHA-D-GLUCAN
COMPND 6 GLUCOHYDROLASE;
COMPND 7 EC: 3.2.1.3;
COMPND 8 OTHER_DETAILS: PREPARED BY SUBTILISIN C-TERMINAL CLEAVAGE, COMPLEXED
COMPND 9 WITH TRIS AND GLYCEROL
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIGER;
SOURCE 3 ORGANISM_TAXID: 5061;
SOURCE 4 OTHER_DETAILS: GENE GLAA
KEYWDS HYDROLASE, GLYCOPROTEIN, GLYCOSIDASE, POLYSACCHARIDE DEGRADATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LEE,M.PAETZEL
REVDAT 7 06-SEP-23 3EQA 1 HETSYN
REVDAT 6 29-JUL-20 3EQA 1 COMPND REMARK HETNAM LINK
REVDAT 6 2 1 SITE ATOM
REVDAT 5 25-OCT-17 3EQA 1 REMARK
REVDAT 4 13-JUL-11 3EQA 1 VERSN
REVDAT 3 16-FEB-11 3EQA 1 JRNL
REVDAT 2 09-FEB-11 3EQA 1 JRNL
REVDAT 1 13-OCT-09 3EQA 0
JRNL AUTH J.LEE,M.PAETZEL
JRNL TITL STRUCTURE OF THE CATALYTIC DOMAIN OF GLUCOAMYLASE FROM
JRNL TITL 2 ASPERGILLUS NIGER.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 67 188 2011
JRNL REFN ESSN 1744-3091
JRNL PMID 21301084
JRNL DOI 10.1107/S1744309110049390
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELYHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 33439
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1762
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 67.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3474
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 235
REMARK 3 SOLVENT ATOMS : 390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : -1.73000
REMARK 3 B33 (A**2) : 1.32000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; 0.009 ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; 1.150 ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; 0.076 ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; 0.004 ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; 0.186 ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; 0.304 ; 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 ; 0.119 ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; 0.131 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3EQA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049641.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-AUG-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35298
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.07600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 71.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.29200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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 3GLY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRIS-ACETATE (PH 8.5), 22.5 %
REMARK 280 PEG 6000, 0.4 M SODIUM ACETATE, 10 % GLYCEROL, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 28.91300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.39650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.61100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.39650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.91300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.61100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 ALA A 25
REMARK 465 THR A 26
REMARK 465 LEU A 27
REMARK 465 ASP A 28
REMARK 465 SER A 29
REMARK 465 THR A 488
REMARK 465 SER A 489
REMARK 465 TRP A 490
REMARK 465 PRO A 491
REMARK 465 SER A 492
REMARK 465 ILE A 493
REMARK 465 VAL A 494
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 171 58.13 -93.94
REMARK 500 SER A 232 -153.40 -117.99
REMARK 500 ASN A 271 -51.24 -29.94
REMARK 500 ASN A 337 -11.14 85.76
REMARK 500 SER A 423 -169.40 -78.61
REMARK 500 SER A 423 -169.12 -79.07
REMARK 500 SER A 435 -154.34 61.50
REMARK 500 ALA A 466 41.60 -148.49
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3EQA A 25 494 UNP P69328 AMYG_ASPNG 25 494
SEQRES 1 A 470 ALA THR LEU ASP SER TRP LEU SER ASN GLU ALA THR VAL
SEQRES 2 A 470 ALA ARG THR ALA ILE LEU ASN ASN ILE GLY ALA ASP GLY
SEQRES 3 A 470 ALA TRP VAL SER GLY ALA ASP SER GLY ILE VAL VAL ALA
SEQRES 4 A 470 SER PRO SER THR ASP ASN PRO ASP TYR PHE TYR THR TRP
SEQRES 5 A 470 THR ARG ASP SER GLY LEU VAL LEU LYS THR LEU VAL ASP
SEQRES 6 A 470 LEU PHE ARG ASN GLY ASP THR SER LEU LEU SER THR ILE
SEQRES 7 A 470 GLU ASN TYR ILE SER ALA GLN ALA ILE VAL GLN GLY ILE
SEQRES 8 A 470 SER ASN PRO SER GLY ASP LEU SER SER GLY ALA GLY LEU
SEQRES 9 A 470 GLY GLU PRO LYS PHE ASN VAL ASP GLU THR ALA TYR THR
SEQRES 10 A 470 GLY SER TRP GLY ARG PRO GLN ARG ASP GLY PRO ALA LEU
SEQRES 11 A 470 ARG ALA THR ALA MET ILE GLY PHE GLY GLN TRP LEU LEU
SEQRES 12 A 470 ASP ASN GLY TYR THR SER THR ALA THR ASP ILE VAL TRP
SEQRES 13 A 470 PRO LEU VAL ARG ASN ASP LEU SER TYR VAL ALA GLN TYR
SEQRES 14 A 470 TRP ASN GLN THR GLY TYR ASP LEU TRP GLU GLU VAL ASN
SEQRES 15 A 470 GLY SER SER PHE PHE THR ILE ALA VAL GLN HIS ARG ALA
SEQRES 16 A 470 LEU VAL GLU GLY SER ALA PHE ALA THR ALA VAL GLY SER
SEQRES 17 A 470 SER CYS SER TRP CYS ASP SER GLN ALA PRO GLU ILE LEU
SEQRES 18 A 470 CYS TYR LEU GLN SER PHE TRP THR GLY SER PHE ILE LEU
SEQRES 19 A 470 ALA ASN PHE ASP SER SER ARG SER GLY LYS ASP ALA ASN
SEQRES 20 A 470 THR LEU LEU GLY SER ILE HIS THR PHE ASP PRO GLU ALA
SEQRES 21 A 470 ALA CYS ASP ASP SER THR PHE GLN PRO CYS SER PRO ARG
SEQRES 22 A 470 ALA LEU ALA ASN HIS LYS GLU VAL VAL ASP SER PHE ARG
SEQRES 23 A 470 SER ILE TYR THR LEU ASN ASP GLY LEU SER ASP SER GLU
SEQRES 24 A 470 ALA VAL ALA VAL GLY ARG TYR PRO GLU ASP THR TYR TYR
SEQRES 25 A 470 ASN GLY ASN PRO TRP PHE LEU CYS THR LEU ALA ALA ALA
SEQRES 26 A 470 GLU GLN LEU TYR ASP ALA LEU TYR GLN TRP ASP LYS GLN
SEQRES 27 A 470 GLY SER LEU GLU VAL THR ASP VAL SER LEU ASP PHE PHE
SEQRES 28 A 470 LYS ALA LEU TYR SER ASP ALA ALA THR GLY THR TYR SER
SEQRES 29 A 470 SER SER SER SER THR TYR SER SER ILE VAL ASP ALA VAL
SEQRES 30 A 470 LYS THR PHE ALA ASP GLY PHE VAL SER ILE VAL GLU THR
SEQRES 31 A 470 HIS ALA ALA SER ASN GLY SER MET SER GLU GLN TYR ASP
SEQRES 32 A 470 LYS SER ASP GLY GLU GLN LEU SER ALA ARG ASP LEU THR
SEQRES 33 A 470 TRP SER TYR ALA ALA LEU LEU THR ALA ASN ASN ARG ARG
SEQRES 34 A 470 ASN SER VAL VAL PRO ALA SER TRP GLY GLU THR SER ALA
SEQRES 35 A 470 SER SER VAL PRO GLY THR CYS ALA ALA THR SER ALA ILE
SEQRES 36 A 470 GLY THR TYR SER SER VAL THR VAL THR SER TRP PRO SER
SEQRES 37 A 470 ILE VAL
MODRES 3EQA ASN A 195 ASN GLYCOSYLATION SITE
MODRES 3EQA ASN A 419 ASN GLYCOSYLATION SITE
MODRES 3EQA SER A 467 SER GLYCOSYLATION SITE
MODRES 3EQA SER A 468 SER GLYCOSYLATION SITE
MODRES 3EQA THR A 476 THR GLYCOSYLATION SITE
MODRES 3EQA SER A 477 SER GLYCOSYLATION SITE
MODRES 3EQA SER A 483 SER GLYCOSYLATION SITE
MODRES 3EQA SER A 484 SER GLYCOSYLATION SITE
MODRES 3EQA THR A 486 THR GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET BMA B 3 11
HET MAN B 4 11
HET NAG C 1 14
HET NAG C 2 14
HET BMA C 3 11
HET MAN C 4 11
HET MAN C 5 11
HET MAN C 6 11
HET MAN C 7 11
HET MAN C 8 11
HET MAN A 600 11
HET MAN A 601 11
HET MAN A 602 11
HET MAN A 603 11
HET MAN A 604 11
HET MAN A 605 11
HET MAN A 606 11
HET TRS A 701 8
HET GOL A 801 6
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM BMA BETA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
HETNAM GOL GLYCEROL
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 BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN TRS TRIS BUFFER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 NAG 4(C8 H15 N O6)
FORMUL 2 BMA 2(C6 H12 O6)
FORMUL 2 MAN 13(C6 H12 O6)
FORMUL 11 TRS C4 H12 N O3 1+
FORMUL 12 GOL C3 H8 O3
FORMUL 13 HOH *390(H2 O)
HELIX 1 1 TRP A 30 ASN A 45 1 16
HELIX 2 2 THR A 77 ASN A 93 1 17
HELIX 3 3 ASP A 95 SER A 97 5 3
HELIX 4 4 LEU A 98 GLN A 113 1 16
HELIX 5 5 GLY A 125 GLU A 130 5 6
HELIX 6 6 ARG A 149 ASN A 169 1 21
HELIX 7 7 TYR A 171 ILE A 178 1 8
HELIX 8 8 ILE A 178 TRP A 194 1 17
HELIX 9 9 PHE A 210 VAL A 230 1 21
HELIX 10 10 CYS A 234 GLN A 249 1 16
HELIX 11 11 SER A 250 TRP A 252 5 3
HELIX 12 12 ASP A 269 THR A 279 1 11
HELIX 13 13 ASP A 287 PHE A 291 5 5
HELIX 14 14 SER A 295 SER A 308 1 14
HELIX 15 15 TYR A 313 ASP A 317 5 5
HELIX 16 16 THR A 334 GLY A 338 5 5
HELIX 17 17 TRP A 341 GLY A 363 1 23
HELIX 18 18 SER A 371 TYR A 379 1 9
HELIX 19 19 SER A 391 ALA A 416 1 26
HELIX 20 20 LEU A 439 ASN A 454 1 16
HELIX 21 21 GLY A 462 ALA A 466 5 5
SHEET 1 A 3 THR A 75 TRP A 76 0
SHEET 2 A 3 LYS A 132 ASN A 134 -1 O PHE A 133 N THR A 75
SHEET 3 A 3 THR A 138 ALA A 139 -1 O THR A 138 N ASN A 134
SHEET 1 B 3 GLY A 198 TYR A 199 0
SHEET 2 B 3 ASN A 206 SER A 209 -1 O GLY A 207 N GLY A 198
SHEET 3 B 3 ASN A 260 PHE A 261 -1 O PHE A 261 N SER A 208
SHEET 1 C 2 SER A 364 VAL A 367 0
SHEET 2 C 2 GLY A 385 SER A 388 -1 O TYR A 387 N LEU A 365
SHEET 1 D 2 GLN A 425 TYR A 426 0
SHEET 2 D 2 GLN A 433 LEU A 434 -1 O LEU A 434 N GLN A 425
SSBOND 1 CYS A 234 CYS A 237 1555 1555 2.05
SSBOND 2 CYS A 246 CYS A 473 1555 1555 2.03
SSBOND 3 CYS A 286 CYS A 294 1555 1555 2.05
LINK ND2 ASN A 195 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 419 C1 NAG C 1 1555 1555 1.44
LINK OG SER A 467 C1 MAN A 600 1555 1555 1.44
LINK OG SER A 468 C1 MAN A 601 1555 1555 1.45
LINK OG1 THR A 476 C1 MAN A 602 1555 1555 1.45
LINK OG SER A 477 C1 MAN A 603 1555 1555 1.44
LINK OG SER A 483 C1 MAN A 604 1555 1555 1.44
LINK OG SER A 484 C1 MAN A 605 1555 1555 1.45
LINK OG1 THR A 486 C1 MAN A 606 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43
LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.44
LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.44
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44
LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.44
LINK O6 BMA C 3 C1 MAN C 7 1555 1555 1.44
LINK O2 MAN C 4 C1 MAN C 5 1555 1555 1.45
LINK O2 MAN C 5 C1 MAN C 6 1555 1555 1.44
LINK O3 MAN C 7 C1 MAN C 8 1555 1555 1.45
CISPEP 1 GLY A 47 ALA A 48 0 3.68
CISPEP 2 ASN A 69 PRO A 70 0 3.21
CISPEP 3 ARG A 146 PRO A 147 0 -4.10
CISPEP 4 PHE A 261 ASP A 262 0 -6.32
CRYST1 57.826 73.222 106.793 90.00 90.00 90.00 P 21 21 21 4
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 0.017293 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013657 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009364 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
