HEADER HYDROLASE 22-FEB-11 3QT9
TITLE ANALYSIS OF A NEW FAMILY OF WIDELY DISTRIBUTED METAL-INDEPENDENT ALPHA
TITLE 2 MANNOSIDASES PROVIDES UNIQUE INSIGHT INTO THE PROCESSING OF N-LINKED
TITLE 3 GLYCANS, CLOSTRIDIUM PERFRINGENS CPE0426 COMPLEXED WITH ALPHA-1,6-
TITLE 4 LINKED 1-THIO-ALPHA-MANNOBIOSE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE UNCHARACTERIZED PROTEIN CPE0426;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PERFRINGENS;
SOURCE 3 ORGANISM_TAXID: 1502;
SOURCE 4 GENE: CPE0426;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA-ALPHA SIX FOLD, GLYCOSIDE HYDROLASE, MANNOSIDASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.J.GREGG,W.F.ZANDBERG,J.-H.HEHEMANN,G.E.WHITWORTH,L.E.DENG,
AUTHOR 2 D.J.VOCADLO,A.B.BORASTON
REVDAT 7 21-FEB-24 3QT9 1 REMARK
REVDAT 6 05-AUG-20 3QT9 1 REMARK HET HETNAM HETSYN
REVDAT 6 2 1 FORMUL LINK ATOM
REVDAT 5 29-JUL-20 3QT9 1 COMPND REMARK SEQADV HET
REVDAT 5 2 1 HETNAM FORMUL LINK SITE
REVDAT 5 3 1 ATOM
REVDAT 4 11-MAY-11 3QT9 1 JRNL
REVDAT 3 23-MAR-11 3QT9 1 JRNL
REVDAT 2 16-MAR-11 3QT9 1 REMARK
REVDAT 1 09-MAR-11 3QT9 0
JRNL AUTH K.J.GREGG,W.F.ZANDBERG,J.H.HEHEMANN,G.E.WHITWORTH,L.DENG,
JRNL AUTH 2 D.J.VOCADLO,A.B.BORASTON
JRNL TITL ANALYSIS OF A NEW FAMILY OF WIDELY DISTRIBUTED
JRNL TITL 2 METAL-INDEPENDENT {ALPHA}-MANNOSIDASES PROVIDES UNIQUE
JRNL TITL 3 INSIGHT INTO THE PROCESSING OF N-LINKED GLYCANS.
JRNL REF J.BIOL.CHEM. V. 286 15586 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21388958
JRNL DOI 10.1074/JBC.M111.223172
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.6
REMARK 3 NUMBER OF REFLECTIONS : 28513
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.158
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1532
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1351
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 57.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE SET COUNT : 76
REMARK 3 BIN FREE R VALUE : 0.2360
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3492
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 403
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 1.37000
REMARK 3 B33 (A**2) : -1.41000
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): 0.165
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.096
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.503
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3627 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4898 ; 1.391 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 423 ; 6.178 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;36.682 ;24.785
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 624 ;14.142 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;17.162 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 514 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2762 ; 0.007 ; 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): 2109 ; 0.767 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3415 ; 1.419 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1518 ; 2.377 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1483 ; 3.868 ; 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 : 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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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
REMARK 4
REMARK 4 3QT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000064074.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 117
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9794
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 (DCM)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28513
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 109.150
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
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 : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
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 : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.36
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES, 12% POLYETHYLENE GLYCOL
REMARK 280 (PEG) 20,000, PH 6.5, VAPOR DIFFUSION, HANGING DROP
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 24.93500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.57500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 48.29500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.57500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.93500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 48.29500
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
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 MET A 1
REMARK 465 SER A 2
REMARK 465 LYS A 427
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 N LEU A 3 O HOH A 601 2.17
REMARK 500 O HOH A 859 O HOH A 955 2.17
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 ASP A 101 106.51 -166.24
REMARK 500 PHE A 281 -40.53 -135.49
REMARK 500 MET A 298 -176.06 178.67
REMARK 500 GLU A 313 20.40 81.01
REMARK 500 LEU A 330 33.65 -94.22
REMARK 500 GLN A 354 1.04 82.62
REMARK 500 HIS A 392 -169.06 -122.13
REMARK 500 GLU A 393 -78.87 -78.06
REMARK 500 ARG A 405 93.15 67.14
REMARK 500 VAL A 423 -66.81 -109.65
REMARK 500 ASN A 425 36.40 -96.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1003 DISTANCE = 6.39 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QT3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN IN NATIVE APO FORM
DBREF 3QT9 A 1 427 UNP Q8XNB2 Q8XNB2_CLOPE 1 427
SEQADV 3QT9 TYR A 159 UNP Q8XNB2 ASP 159 ENGINEERED MUTATION
SEQRES 1 A 427 MET SER LEU SER THR ASN GLU LEU LYS GLU ILE VAL ARG
SEQRES 2 A 427 LYS ILE GLY LYS ASP LEU SER GLY LYS ILE GLU ASP LYS
SEQRES 3 A 427 LYS LEU GLN GLU LEU PHE TYR ASN CYS PHE ILE ASN THR
SEQRES 4 A 427 MET ASP THR THR VAL GLU VAL SER GLU GLY ASP ALA PHE
SEQRES 5 A 427 VAL ILE THR GLY ASP ILE PRO ALA MET TRP LEU ARG ASP
SEQRES 6 A 427 SER THR SER GLN VAL GLU HIS TYR LEU PRO PHE VAL LYS
SEQRES 7 A 427 GLU TYR PRO GLU LEU LYS ALA ILE PHE THR GLY LEU ILE
SEQRES 8 A 427 ASN ARG GLN VAL LYS CYS ILE PHE ILE ASP PRO TYR ALA
SEQRES 9 A 427 ASN ALA PHE ASN LYS GLU PRO ASN GLY GLN LYS TRP ASP
SEQRES 10 A 427 ASN ASP ILE THR LYS ASP SER PRO TRP VAL TRP GLU ARG
SEQRES 11 A 427 LYS TYR GLU ILE ASP SER LEU CYS TYR PRO VAL ARG LEU
SEQRES 12 A 427 ILE HIS LYS TYR TRP LYS GLU SER GLY ASP GLU THR PHE
SEQRES 13 A 427 PHE ASN TYR ASP ILE LYS LYS ALA PHE ASN MET ILE ILE
SEQRES 14 A 427 ASP LEU TRP ARG VAL GLU GLN TYR HIS ARG GLU LYS SER
SEQRES 15 A 427 ASP TYR SER PHE GLN ARG LEU ASN CYS SER VAL THR ASP
SEQRES 16 A 427 THR LEU SER HIS GLU GLY LEU GLY THR PRO VAL THR TYR
SEQRES 17 A 427 THR GLY MET THR TRP SER GLY PHE ARG PRO SER ASP ASP
SEQRES 18 A 427 ALA CYS GLU TYR GLY TYR LEU ILE PRO ALA ASN MET PHE
SEQRES 19 A 427 ALA VAL VAL ALA LEU ARG TYR ILE SER GLU ILE ALA GLU
SEQRES 20 A 427 LYS VAL TYR LYS ASP GLU GLU LEU LYS GLU LYS ALA ASP
SEQRES 21 A 427 SER LEU ARG GLU GLU ILE ASP ASN ALA ILE GLU LYS HIS
SEQRES 22 A 427 GLY LYS VAL TYR LYS GLU GLY PHE GLY GLU VAL TYR ALA
SEQRES 23 A 427 TYR GLU THR ASP GLY MET GLY ASN TYR ASN PHE MET ASP
SEQRES 24 A 427 ASP ALA ASN VAL PRO SER LEU LEU SER ILE PRO TYR LEU
SEQRES 25 A 427 GLU TYR LYS GLY ILE GLU ASP GLU VAL TYR GLN ASN THR
SEQRES 26 A 427 ARG LYS PHE ILE LEU SER LYS ASN ASN ARG PHE PHE PHE
SEQRES 27 A 427 GLU GLY LYS ALA ALA LYS GLY ILE GLY SER PRO HIS THR
SEQRES 28 A 427 PRO ASP GLN TYR ILE TRP HIS ILE ALA LEU SER MET GLN
SEQRES 29 A 427 GLY LEU THR THR ASN ASN GLN GLU GLU ILE ASP GLN LEU
SEQRES 30 A 427 ILE LYS LEU LEU LYS GLU THR ASP ALA GLY THR GLY TYR
SEQRES 31 A 427 MET HIS GLU GLY PHE HIS VAL ASP ASP PRO THR LYS PHE
SEQRES 32 A 427 THR ARG ASP TRP PHE ALA TRP SER ASN SER LEU PHE SER
SEQRES 33 A 427 HIS PHE ILE TYR GLU LYS VAL ILE ASN LYS LYS
HET Z4Y B 1 12
HET MAN B 2 11
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET EDO A 506 4
HETNAM Z4Y 6-THIO-ALPHA-D-MANNOPYRANOSE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN Z4Y 6-THIO-ALPHA-D-MANNOSE; 6-THIO-D-MANNOSE; 6-THIO-
HETSYN 2 Z4Y MANNOSE
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 Z4Y C6 H12 O5 S
FORMUL 2 MAN C6 H12 O6
FORMUL 3 EDO 6(C2 H6 O2)
FORMUL 9 HOH *403(H2 O)
HELIX 1 1 SER A 4 GLY A 21 1 18
HELIX 2 2 ASP A 25 THR A 43 1 19
HELIX 3 3 LEU A 63 VAL A 70 1 8
HELIX 4 4 GLU A 71 VAL A 77 5 7
HELIX 5 5 TYR A 80 GLU A 82 5 3
HELIX 6 6 LEU A 83 ASP A 101 1 19
HELIX 7 7 ILE A 134 GLY A 152 1 19
HELIX 8 8 ASN A 158 GLU A 175 1 18
HELIX 9 9 TYR A 177 SER A 182 1 6
HELIX 10 10 SER A 192 THR A 196 5 5
HELIX 11 11 LEU A 197 LEU A 202 1 6
HELIX 12 12 ILE A 229 VAL A 249 1 21
HELIX 13 13 ASP A 252 GLY A 274 1 23
HELIX 14 14 SER A 308 GLU A 313 1 6
HELIX 15 15 ASP A 319 LEU A 330 1 12
HELIX 16 16 HIS A 358 THR A 367 1 10
HELIX 17 17 ASN A 370 THR A 384 1 15
HELIX 18 18 PHE A 408 VAL A 423 1 16
SHEET 1 A 2 VAL A 44 SER A 47 0
SHEET 2 A 2 ASP A 50 VAL A 53 -1 O PHE A 52 N GLU A 45
SHEET 1 B 3 MET A 61 TRP A 62 0
SHEET 2 B 3 ALA A 106 PHE A 107 -1 O PHE A 107 N MET A 61
SHEET 3 B 3 VAL A 127 GLU A 129 -1 O GLU A 129 N ALA A 106
SHEET 1 C 3 TYR A 227 LEU A 228 0
SHEET 2 C 3 GLU A 288 THR A 289 -1 O THR A 289 N TYR A 227
SHEET 3 C 3 TYR A 295 ASN A 296 -1 O ASN A 296 N GLU A 288
SHEET 1 D 2 LYS A 275 LYS A 278 0
SHEET 2 D 2 GLY A 282 TYR A 285 -1 O GLY A 282 N LYS A 278
SHEET 1 E 2 PHE A 337 GLU A 339 0
SHEET 2 E 2 LYS A 344 ILE A 346 -1 O GLY A 345 N PHE A 338
SHEET 1 F 3 TYR A 355 TRP A 357 0
SHEET 2 F 3 GLY A 394 HIS A 396 -1 O PHE A 395 N ILE A 356
SHEET 3 F 3 ASP A 399 PHE A 403 -1 O LYS A 402 N HIS A 396
LINK S6 Z4Y B 1 C1 MAN B 2 1555 1555 1.87
CISPEP 1 VAL A 303 PRO A 304 0 6.94
CRYST1 49.870 96.590 109.150 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 0.020052 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010353 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009162 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
