HEADER HYDROLASE 07-JAN-08 3BVT
TITLE GOLGI MANNOSIDASE II D204A CATALYTIC NUCLEOPHILE MUTANT COMPLEX WITH
TITLE 2 METHYL (ALPHA-D-MANNOPYRANOSYL)-(1->3)-S-ALPHA-D-MANNOPYRANOSIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-MANNOSIDASE 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN; UNP RESIDUES 76-1108;
COMPND 5 SYNONYM: ALPHA-MANNOSIDASE II, MANNOSYL-OLIGOSACCHARIDE 1,3-1,6-
COMPND 6 ALPHA-MANNOSIDASE, MAN II, GOLGI ALPHA-MANNOSIDASE II, AMAN II;
COMPND 7 EC: 3.2.1.114;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 GENE: ALPHA-MAN-II, GMII;
SOURCE 5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: S2 CELLS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: STABLE TRANSFECTION PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PMTBIP_NHIS
KEYWDS FAMILY 38 GLYCOYSL HYDROLASE, GLYCOSIDASE, GOLGI APPARATUS, MEMBRANE,
KEYWDS 2 SIGNAL-ANCHOR, TRANSMEMBRANE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.KUNTZ,D.R.ROSE
REVDAT 9 30-AUG-23 3BVT 1 REMARK
REVDAT 8 20-OCT-21 3BVT 1 SEQADV HETSYN
REVDAT 7 29-JUL-20 3BVT 1 COMPND REMARK SEQADV HET
REVDAT 7 2 1 HETNAM HETSYN FORMUL LINK
REVDAT 7 3 1 SITE ATOM
REVDAT 6 24-JUL-19 3BVT 1 REMARK LINK
REVDAT 5 25-OCT-17 3BVT 1 REMARK
REVDAT 4 13-JUL-11 3BVT 1 VERSN
REVDAT 3 24-FEB-09 3BVT 1 VERSN
REVDAT 2 22-JUL-08 3BVT 1 JRNL
REVDAT 1 01-JUL-08 3BVT 0
JRNL AUTH W.ZHONG,D.A.KUNTZ,B.EMBER,H.SINGH,K.W.MOREMEN,D.R.ROSE,
JRNL AUTH 2 G.J.BOONS
JRNL TITL PROBING THE SUBSTRATE SPECIFICITY OF GOLGI ALPHA-MANNOSIDASE
JRNL TITL 2 II BY USE OF SYNTHETIC OLIGOSACCHARIDES AND A CATALYTIC
JRNL TITL 3 NUCLEOPHILE MUTANT.
JRNL REF J.AM.CHEM.SOC. V. 130 8975 2008
JRNL REFN ISSN 0002-7863
JRNL PMID 18558690
JRNL DOI 10.1021/JA711248Y
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.84
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 256139
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.500
REMARK 3 FREE R VALUE TEST SET COUNT : 3801
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) : 1.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 17986
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.36
REMARK 3 BIN R VALUE (WORKING SET) : 0.2560
REMARK 3 BIN FREE R VALUE SET COUNT : 274
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8194
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 1453
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.050
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.035
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.807
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8777 ; 0.014 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11979 ; 1.520 ; 1.943
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1089 ; 6.087 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 432 ;37.004 ;23.681
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1488 ;12.160 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 60 ;18.705 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1277 ; 0.101 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6816 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4324 ; 0.203 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6031 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1242 ; 0.142 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.019 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 82 ; 0.212 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 69 ; 0.116 ; 0.200
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): 5361 ; 1.031 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8534 ; 1.636 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3868 ; 2.320 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3421 ; 3.539 ; 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 : 1.20
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 3BVT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JAN-08.
REMARK 100 THE DEPOSITION ID IS D_1000046018.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.977
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 256264
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.33
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.88700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1HTY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRIS, NACL, PEG6000, MPD. CRYSTALS
REMARK 280 WASHED IN PHOSPHATE BUFFERED RESERVOIR SOLUTION BEFORE SOAKING
REMARK 280 WITH SUBSTRATE FOR 24 HRS, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 34.52000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.31350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 54.92350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.31350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.52000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 54.92350
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 ARG A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 HIS A 4
REMARK 465 HIS A 5
REMARK 465 HIS A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 GLY A 10
REMARK 465 GLU A 11
REMARK 465 PHE A 12
REMARK 465 ASP A 13
REMARK 465 ASP A 14
REMARK 465 PRO A 15
REMARK 465 ILE A 16
REMARK 465 ARG A 17
REMARK 465 PRO A 18
REMARK 465 PRO A 19
REMARK 465 LEU A 20
REMARK 465 LYS A 21
REMARK 465 VAL A 22
REMARK 465 ALA A 23
REMARK 465 ARG A 24
REMARK 465 SER A 25
REMARK 465 PRO A 26
REMARK 465 ARG A 27
REMARK 465 PRO A 28
REMARK 465 GLY A 29
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 56 78.32 -105.11
REMARK 500 HIS A 79 84.74 -151.78
REMARK 500 TRP A 95 -83.65 -170.91
REMARK 500 ASP A 106 -61.01 -132.50
REMARK 500 THR A 162 -67.59 69.11
REMARK 500 GLN A 227 -44.21 -139.31
REMARK 500 ASP A 340 -171.73 -172.88
REMARK 500 LYS A 345 -70.24 -87.14
REMARK 500 SER A 411 -126.36 41.96
REMARK 500 SER A 411 -130.46 48.95
REMARK 500 ILE A 549 -48.67 -140.73
REMARK 500 LEU A 550 117.58 -171.16
REMARK 500 PRO A 562 40.41 -84.69
REMARK 500 ARG A 653 147.78 -173.30
REMARK 500 ASN A 732 57.35 -92.20
REMARK 500 GLN A 742 76.69 -119.60
REMARK 500 SER A 762 -4.05 72.44
REMARK 500 ILE A 831 75.83 -118.03
REMARK 500 SER A 833 -15.09 -152.15
REMARK 500 ASP A 839 -160.35 -124.04
REMARK 500 GLU A 991 82.27 22.70
REMARK 500 GLU A 992 -161.77 -116.91
REMARK 500 HIS A 993 93.75 36.17
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 ZN A1048 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 90 NE2
REMARK 620 2 ASP A 92 OD1 96.2
REMARK 620 3 HIS A 471 NE2 106.5 98.5
REMARK 620 4 MAN B 2 O3 152.6 92.8 97.5
REMARK 620 5 MAN B 2 O2 85.2 144.8 114.9 72.8
REMARK 620 N 1 2 3 4
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HTY RELATED DB: PDB
REMARK 900 DGMII + TRIS
REMARK 900 RELATED ID: 1HWW RELATED DB: PDB
REMARK 900 DGMII + SWAINSONINE
REMARK 900 RELATED ID: 1HXK RELATED DB: PDB
REMARK 900 DGMII + DEOXYMANNOJIRIMICIN
REMARK 900 RELATED ID: 1PS2 RELATED DB: PDB
REMARK 900 DGMII + KIFUNENSINE
REMARK 900 RELATED ID: 1QWN RELATED DB: PDB
REMARK 900 DGMII + 5FLUORO-GULOSYLFLUORIDE
REMARK 900 RELATED ID: 1QX1 RELATED DB: PDB
REMARK 900 DGMII + 2F-MANNOSYLF
REMARK 900 RELATED ID: 1R33 RELATED DB: PDB
REMARK 900 DGMII + 5-THIO-D-MANNOPYRANOSYLAMINE
REMARK 900 RELATED ID: 1R34 RELATED DB: PDB
REMARK 900 DGMII + 5-THIO-D-MANNOPYRANOSYLAMIDINIUM SALT
REMARK 900 RELATED ID: 1TQS RELATED DB: PDB
REMARK 900 DGMII + SALACINOL
REMARK 900 RELATED ID: 1TQT RELATED DB: PDB
REMARK 900 DGMII + DIASTEREOMER OF SALACINOL
REMARK 900 RELATED ID: 1TQU RELATED DB: PDB
REMARK 900 DGMII + GHAVAMIOL
REMARK 900 RELATED ID: 1TQV RELATED DB: PDB
REMARK 900 DGMII + BLINTOL
REMARK 900 RELATED ID: 1TQW RELATED DB: PDB
REMARK 900 DGMII + BLINTOL DIASTEREOMER
REMARK 900 RELATED ID: 2ALW RELATED DB: PDB
REMARK 900 DGMII + NOEUROMYCIN
REMARK 900 RELATED ID: 2F18 RELATED DB: PDB
REMARK 900 DGMII + (2R,3R,4S)-2-({[(1R)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)
REMARK 900 PYRROLIDINE-3,4-DIOL
REMARK 900 RELATED ID: 2F1A RELATED DB: PDB
REMARK 900 DGMII + (2R,3R,4S)-2-({[(1S)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)
REMARK 900 PYRROLIDINE-3,4-DIOL
REMARK 900 RELATED ID: 2F1B RELATED DB: PDB
REMARK 900 DGMII + (2R,3R,4S,5R)-2-({[(1R)-2-HYDROXY-1-PHENYLETHYL]AMINO}
REMARK 900 METHYL)-5-METHYLPYRROLIDINE-3,4-DIOL
REMARK 900 RELATED ID: 2F7O RELATED DB: PDB
REMARK 900 DGMII + MANNOSTATIN A
REMARK 900 RELATED ID: 2F7P RELATED DB: PDB
REMARK 900 DGMII + BENZYL-MANNOSTATIN A
REMARK 900 RELATED ID: 2F7Q RELATED DB: PDB
REMARK 900 DGMII + AMINOCYCLOPENTITETROL
REMARK 900 RELATED ID: 2F7R RELATED DB: PDB
REMARK 900 DGMII + BENZYL-AMINOCYCLOPENTITETROL
REMARK 900 RELATED ID: 3BUB RELATED DB: PDB
REMARK 900 DGMII EMPTY ACTIVE SITE
REMARK 900 RELATED ID: 3BUD RELATED DB: PDB
REMARK 900 DGMII NUCLEOPHILE MUTANT D204A EMPTY ACTIVE SITE
REMARK 900 RELATED ID: 3BUI RELATED DB: PDB
REMARK 900 DGMII NUCLEOPHILE MUTANT D204A + TRIS
REMARK 900 RELATED ID: 3BUP RELATED DB: PDB
REMARK 900 DGMII ACID-BASE CATALYST MUTANT D341N + MANNOSE
REMARK 900 RELATED ID: 3BUQ RELATED DB: PDB
REMARK 900 DGMII NUCLEOPHILE MUTANT D204A + MANNOSE
REMARK 900 RELATED ID: 3BVU RELATED DB: PDB
REMARK 900 DGMII_D204A + SUBSTRATE WZ2
REMARK 900 RELATED ID: 3BVV RELATED DB: PDB
REMARK 900 DGMII_D204A + SUBSTRATE WZ3
REMARK 900 RELATED ID: 3BVW RELATED DB: PDB
REMARK 900 DGMII_D204A + SUBSTRATE WZ4
REMARK 900 RELATED ID: 3BVX RELATED DB: PDB
REMARK 900 DGMII_D204A + SUBSTRATE WZ5
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 E970K CONFLICT IN UNP ENTRY Q24451
DBREF 3BVT A 13 1045 UNP Q24451 MAN2_DROME 76 1108
SEQADV 3BVT ARG A 1 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT SER A 2 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT SER A 3 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT HIS A 4 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT HIS A 5 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT HIS A 6 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT HIS A 7 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT HIS A 8 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT HIS A 9 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT GLY A 10 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT GLU A 11 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT PHE A 12 UNP Q24451 EXPRESSION TAG
SEQADV 3BVT ALA A 204 UNP Q24451 ASP 267 ENGINEERED MUTATION
SEQADV 3BVT LYS A 907 UNP Q24451 GLU 970 SEE REMARK 999
SEQRES 1 A 1045 ARG SER SER HIS HIS HIS HIS HIS HIS GLY GLU PHE ASP
SEQRES 2 A 1045 ASP PRO ILE ARG PRO PRO LEU LYS VAL ALA ARG SER PRO
SEQRES 3 A 1045 ARG PRO GLY GLN CYS GLN ASP VAL VAL GLN ASP VAL PRO
SEQRES 4 A 1045 ASN VAL ASP VAL GLN MET LEU GLU LEU TYR ASP ARG MET
SEQRES 5 A 1045 SER PHE LYS ASP ILE ASP GLY GLY VAL TRP LYS GLN GLY
SEQRES 6 A 1045 TRP ASN ILE LYS TYR ASP PRO LEU LYS TYR ASN ALA HIS
SEQRES 7 A 1045 HIS LYS LEU LYS VAL PHE VAL VAL PRO HIS SER HIS ASN
SEQRES 8 A 1045 ASP PRO GLY TRP ILE GLN THR PHE GLU GLU TYR TYR GLN
SEQRES 9 A 1045 HIS ASP THR LYS HIS ILE LEU SER ASN ALA LEU ARG HIS
SEQRES 10 A 1045 LEU HIS ASP ASN PRO GLU MET LYS PHE ILE TRP ALA GLU
SEQRES 11 A 1045 ILE SER TYR PHE ALA ARG PHE TYR HIS ASP LEU GLY GLU
SEQRES 12 A 1045 ASN LYS LYS LEU GLN MET LYS SER ILE VAL LYS ASN GLY
SEQRES 13 A 1045 GLN LEU GLU PHE VAL THR GLY GLY TRP VAL MET PRO ASP
SEQRES 14 A 1045 GLU ALA ASN SER HIS TRP ARG ASN VAL LEU LEU GLN LEU
SEQRES 15 A 1045 THR GLU GLY GLN THR TRP LEU LYS GLN PHE MET ASN VAL
SEQRES 16 A 1045 THR PRO THR ALA SER TRP ALA ILE ALA PRO PHE GLY HIS
SEQRES 17 A 1045 SER PRO THR MET PRO TYR ILE LEU GLN LYS SER GLY PHE
SEQRES 18 A 1045 LYS ASN MET LEU ILE GLN ARG THR HIS TYR SER VAL LYS
SEQRES 19 A 1045 LYS GLU LEU ALA GLN GLN ARG GLN LEU GLU PHE LEU TRP
SEQRES 20 A 1045 ARG GLN ILE TRP ASP ASN LYS GLY ASP THR ALA LEU PHE
SEQRES 21 A 1045 THR HIS MET MET PRO PHE TYR SER TYR ASP ILE PRO HIS
SEQRES 22 A 1045 THR CYS GLY PRO ASP PRO LYS VAL CYS CYS GLN PHE ASP
SEQRES 23 A 1045 PHE LYS ARG MET GLY SER PHE GLY LEU SER CYS PRO TRP
SEQRES 24 A 1045 LYS VAL PRO PRO ARG THR ILE SER ASP GLN ASN VAL ALA
SEQRES 25 A 1045 ALA ARG SER ASP LEU LEU VAL ASP GLN TRP LYS LYS LYS
SEQRES 26 A 1045 ALA GLU LEU TYR ARG THR ASN VAL LEU LEU ILE PRO LEU
SEQRES 27 A 1045 GLY ASP ASP PHE ARG PHE LYS GLN ASN THR GLU TRP ASP
SEQRES 28 A 1045 VAL GLN ARG VAL ASN TYR GLU ARG LEU PHE GLU HIS ILE
SEQRES 29 A 1045 ASN SER GLN ALA HIS PHE ASN VAL GLN ALA GLN PHE GLY
SEQRES 30 A 1045 THR LEU GLN GLU TYR PHE ASP ALA VAL HIS GLN ALA GLU
SEQRES 31 A 1045 ARG ALA GLY GLN ALA GLU PHE PRO THR LEU SER GLY ASP
SEQRES 32 A 1045 PHE PHE THR TYR ALA ASP ARG SER ASP ASN TYR TRP SER
SEQRES 33 A 1045 GLY TYR TYR THR SER ARG PRO TYR HIS LYS ARG MET ASP
SEQRES 34 A 1045 ARG VAL LEU MET HIS TYR VAL ARG ALA ALA GLU MET LEU
SEQRES 35 A 1045 SER ALA TRP HIS SER TRP ASP GLY MET ALA ARG ILE GLU
SEQRES 36 A 1045 GLU ARG LEU GLU GLN ALA ARG ARG GLU LEU SER LEU PHE
SEQRES 37 A 1045 GLN HIS HIS ASP GLY ILE THR GLY THR ALA LYS THR HIS
SEQRES 38 A 1045 VAL VAL VAL ASP TYR GLU GLN ARG MET GLN GLU ALA LEU
SEQRES 39 A 1045 LYS ALA CYS GLN MET VAL MET GLN GLN SER VAL TYR ARG
SEQRES 40 A 1045 LEU LEU THR LYS PRO SER ILE TYR SER PRO ASP PHE SER
SEQRES 41 A 1045 PHE SER TYR PHE THR LEU ASP ASP SER ARG TRP PRO GLY
SEQRES 42 A 1045 SER GLY VAL GLU ASP SER ARG THR THR ILE ILE LEU GLY
SEQRES 43 A 1045 GLU ASP ILE LEU PRO SER LYS HIS VAL VAL MET HIS ASN
SEQRES 44 A 1045 THR LEU PRO HIS TRP ARG GLU GLN LEU VAL ASP PHE TYR
SEQRES 45 A 1045 VAL SER SER PRO PHE VAL SER VAL THR ASP LEU ALA ASN
SEQRES 46 A 1045 ASN PRO VAL GLU ALA GLN VAL SER PRO VAL TRP SER TRP
SEQRES 47 A 1045 HIS HIS ASP THR LEU THR LYS THR ILE HIS PRO GLN GLY
SEQRES 48 A 1045 SER THR THR LYS TYR ARG ILE ILE PHE LYS ALA ARG VAL
SEQRES 49 A 1045 PRO PRO MET GLY LEU ALA THR TYR VAL LEU THR ILE SER
SEQRES 50 A 1045 ASP SER LYS PRO GLU HIS THR SER TYR ALA SER ASN LEU
SEQRES 51 A 1045 LEU LEU ARG LYS ASN PRO THR SER LEU PRO LEU GLY GLN
SEQRES 52 A 1045 TYR PRO GLU ASP VAL LYS PHE GLY ASP PRO ARG GLU ILE
SEQRES 53 A 1045 SER LEU ARG VAL GLY ASN GLY PRO THR LEU ALA PHE SER
SEQRES 54 A 1045 GLU GLN GLY LEU LEU LYS SER ILE GLN LEU THR GLN ASP
SEQRES 55 A 1045 SER PRO HIS VAL PRO VAL HIS PHE LYS PHE LEU LYS TYR
SEQRES 56 A 1045 GLY VAL ARG SER HIS GLY ASP ARG SER GLY ALA TYR LEU
SEQRES 57 A 1045 PHE LEU PRO ASN GLY PRO ALA SER PRO VAL GLU LEU GLY
SEQRES 58 A 1045 GLN PRO VAL VAL LEU VAL THR LYS GLY LYS LEU GLU SER
SEQRES 59 A 1045 SER VAL SER VAL GLY LEU PRO SER VAL VAL HIS GLN THR
SEQRES 60 A 1045 ILE MET ARG GLY GLY ALA PRO GLU ILE ARG ASN LEU VAL
SEQRES 61 A 1045 ASP ILE GLY SER LEU ASP ASN THR GLU ILE VAL MET ARG
SEQRES 62 A 1045 LEU GLU THR HIS ILE ASP SER GLY ASP ILE PHE TYR THR
SEQRES 63 A 1045 ASP LEU ASN GLY LEU GLN PHE ILE LYS ARG ARG ARG LEU
SEQRES 64 A 1045 ASP LYS LEU PRO LEU GLN ALA ASN TYR TYR PRO ILE PRO
SEQRES 65 A 1045 SER GLY MET PHE ILE GLU ASP ALA ASN THR ARG LEU THR
SEQRES 66 A 1045 LEU LEU THR GLY GLN PRO LEU GLY GLY SER SER LEU ALA
SEQRES 67 A 1045 SER GLY GLU LEU GLU ILE MET GLN ASP ARG ARG LEU ALA
SEQRES 68 A 1045 SER ASP ASP GLU ARG GLY LEU GLY GLN GLY VAL LEU ASP
SEQRES 69 A 1045 ASN LYS PRO VAL LEU HIS ILE TYR ARG LEU VAL LEU GLU
SEQRES 70 A 1045 LYS VAL ASN ASN CYS VAL ARG PRO SER LYS LEU HIS PRO
SEQRES 71 A 1045 ALA GLY TYR LEU THR SER ALA ALA HIS LYS ALA SER GLN
SEQRES 72 A 1045 SER LEU LEU ASP PRO LEU ASP LYS PHE ILE PHE ALA GLU
SEQRES 73 A 1045 ASN GLU TRP ILE GLY ALA GLN GLY GLN PHE GLY GLY ASP
SEQRES 74 A 1045 HIS PRO SER ALA ARG GLU ASP LEU ASP VAL SER VAL MET
SEQRES 75 A 1045 ARG ARG LEU THR LYS SER SER ALA LYS THR GLN ARG VAL
SEQRES 76 A 1045 GLY TYR VAL LEU HIS ARG THR ASN LEU MET GLN CYS GLY
SEQRES 77 A 1045 THR PRO GLU GLU HIS THR GLN LYS LEU ASP VAL CYS HIS
SEQRES 78 A 1045 LEU LEU PRO ASN VAL ALA ARG CYS GLU ARG THR THR LEU
SEQRES 79 A 1045 THR PHE LEU GLN ASN LEU GLU HIS LEU ASP GLY MET VAL
SEQRES 80 A 1045 ALA PRO GLU VAL CYS PRO MET GLU THR ALA ALA TYR VAL
SEQRES 81 A 1045 SER SER HIS SER SER
MODRES 3BVT ASN A 194 ASN GLYCOSYLATION SITE
HET Z4R B 1 13
HET MAN B 2 11
HET NAG A1046 14
HET PO4 A1047 5
HET ZN A1048 1
HET MRD A1049 8
HET MPD A1051 8
HET MPD A1052 8
HETNAM Z4R METHYL 3-THIO-ALPHA-D-MANNOPYRANOSIDE
HETNAM MAN ALPHA-D-MANNOPYRANOSE
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM PO4 PHOSPHATE ION
HETNAM ZN ZINC ION
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE
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 2 Z4R C7 H14 O5 S
FORMUL 2 MAN C6 H12 O6
FORMUL 3 NAG C8 H15 N O6
FORMUL 4 PO4 O4 P 3-
FORMUL 5 ZN ZN 2+
FORMUL 6 MRD C6 H14 O2
FORMUL 7 MPD 2(C6 H14 O2)
FORMUL 9 HOH *1453(H2 O)
HELIX 1 1 MET A 45 MET A 52 1 8
HELIX 2 2 ASP A 71 TYR A 75 5 5
HELIX 3 3 THR A 98 ASP A 106 1 9
HELIX 4 4 ASP A 106 ASN A 121 1 16
HELIX 5 5 GLU A 130 HIS A 139 1 10
HELIX 6 6 GLY A 142 ASN A 155 1 14
HELIX 7 7 HIS A 174 ASN A 194 1 21
HELIX 8 8 PRO A 210 LYS A 218 1 9
HELIX 9 9 HIS A 230 GLN A 240 1 11
HELIX 10 10 ASP A 270 THR A 274 5 5
HELIX 11 11 ASP A 278 CYS A 283 1 6
HELIX 12 12 GLN A 284 MET A 290 5 7
HELIX 13 13 ASN A 310 GLU A 327 1 18
HELIX 14 14 GLN A 346 GLN A 367 1 22
HELIX 15 15 ALA A 368 PHE A 370 5 3
HELIX 16 16 THR A 378 ALA A 392 1 15
HELIX 17 17 SER A 416 THR A 420 5 5
HELIX 18 18 ARG A 422 TRP A 445 1 24
HELIX 19 19 ASP A 449 ALA A 452 5 4
HELIX 20 20 ARG A 453 GLN A 469 1 17
HELIX 21 21 LYS A 479 LEU A 509 1 31
HELIX 22 22 PRO A 823 TYR A 828 5 6
HELIX 23 23 THR A 915 ASP A 927 1 13
HELIX 24 24 ASP A 998 LEU A 1002 5 5
HELIX 25 25 ASP A 1024 VAL A 1027 5 4
SHEET 1 A 6 VAL A 43 GLN A 44 0
SHEET 2 A 6 THR A 399 SER A 401 1 O SER A 401 N VAL A 43
SHEET 3 A 6 GLU A 244 TRP A 247 1 N LEU A 246 O LEU A 400
SHEET 4 A 6 LEU A 259 MET A 263 -1 O THR A 261 N PHE A 245
SHEET 5 A 6 ASN A 223 ILE A 226 1 N MET A 224 O HIS A 262
SHEET 6 A 6 ALA A 199 ALA A 202 1 N ALA A 202 O LEU A 225
SHEET 1 B 3 VAL A 333 ASP A 341 0
SHEET 2 B 3 LEU A 81 HIS A 90 1 N LYS A 82 O LEU A 334
SHEET 3 B 3 VAL A 372 PHE A 376 1 O GLN A 375 N VAL A 85
SHEET 1 C 2 PHE A 126 TRP A 128 0
SHEET 2 C 2 LEU A 158 PHE A 160 1 O GLU A 159 N PHE A 126
SHEET 1 D 6 PHE A 524 ASP A 527 0
SHEET 2 D 6 ASP A 930 PHE A 934 -1 O ILE A 933 N THR A 525
SHEET 3 D 6 SER A 552 ASN A 559 -1 N VAL A 556 O PHE A 932
SHEET 4 D 6 GLY A 628 ILE A 636 -1 O TYR A 632 N VAL A 555
SHEET 5 D 6 VAL A 578 ASP A 582 -1 N THR A 581 O VAL A 633
SHEET 6 D 6 PRO A 587 VAL A 588 -1 O VAL A 588 N VAL A 580
SHEET 1 E 5 PHE A 524 ASP A 527 0
SHEET 2 E 5 ASP A 930 PHE A 934 -1 O ILE A 933 N THR A 525
SHEET 3 E 5 SER A 552 ASN A 559 -1 N VAL A 556 O PHE A 932
SHEET 4 E 5 GLY A 628 ILE A 636 -1 O TYR A 632 N VAL A 555
SHEET 5 E 5 GLN A 945 PHE A 946 -1 O PHE A 946 N LEU A 629
SHEET 1 F 5 THR A 542 ILE A 543 0
SHEET 2 F 5 ARG A 565 VAL A 573 1 O TYR A 572 N ILE A 543
SHEET 3 F 5 THR A 606 VAL A 624 -1 O VAL A 624 N ARG A 565
SHEET 4 F 5 ALA A 590 ASP A 601 -1 N SER A 597 O GLN A 610
SHEET 5 F 5 THR A 644 TYR A 646 1 O SER A 645 N VAL A 592
SHEET 1 G12 LYS A 669 GLY A 671 0
SHEET 2 G12 SER A 648 LEU A 652 1 N LEU A 651 O LYS A 669
SHEET 3 G12 VAL A 745 LYS A 749 -1 O VAL A 745 N LEU A 652
SHEET 4 G12 SER A 754 LEU A 760 -1 O SER A 757 N LEU A 746
SHEET 5 G12 VAL A 763 MET A 769 -1 O MET A 769 N SER A 754
SHEET 6 G12 GLU A 775 VAL A 780 -1 O GLU A 775 N ILE A 768
SHEET 7 G12 VAL A 888 LYS A 898 -1 O VAL A 888 N VAL A 780
SHEET 8 G12 THR A 842 THR A 848 -1 N THR A 845 O VAL A 895
SHEET 9 G12 GLY A 834 GLU A 838 -1 N MET A 835 O LEU A 846
SHEET 10 G12 ILE A 803 LEU A 808 -1 N TYR A 805 O PHE A 836
SHEET 11 G12 GLN A 812 ARG A 817 -1 O ARG A 816 N PHE A 804
SHEET 12 G12 ALA A 911 GLY A 912 -1 O GLY A 912 N PHE A 813
SHEET 1 H 5 ILE A 676 ARG A 679 0
SHEET 2 H 5 THR A 685 PHE A 688 -1 O PHE A 688 N ILE A 676
SHEET 3 H 5 LEU A 694 GLN A 698 -1 O LYS A 695 N ALA A 687
SHEET 4 H 5 VAL A 706 TYR A 715 -1 O VAL A 706 N ILE A 697
SHEET 5 H 5 SER A 736 PRO A 737 -1 O SER A 736 N LYS A 714
SHEET 1 I 8 ILE A 676 ARG A 679 0
SHEET 2 I 8 THR A 685 PHE A 688 -1 O PHE A 688 N ILE A 676
SHEET 3 I 8 LEU A 694 GLN A 698 -1 O LYS A 695 N ALA A 687
SHEET 4 I 8 VAL A 706 TYR A 715 -1 O VAL A 706 N ILE A 697
SHEET 5 I 8 THR A 788 THR A 796 -1 O ARG A 793 N LYS A 711
SHEET 6 I 8 GLU A 861 ARG A 869 -1 O GLN A 866 N ILE A 790
SHEET 7 I 8 LEU A 852 SER A 855 -1 N GLY A 853 O MET A 865
SHEET 8 I 8 TYR A 829 ILE A 831 -1 N TYR A 829 O GLY A 854
SHEET 1 J 5 LEU A 957 ARG A 964 0
SHEET 2 J 5 GLN A 973 ARG A 981 -1 O GLY A 976 N ARG A 963
SHEET 3 J 5 THR A1036 HIS A1043 -1 O ALA A1037 N LEU A 979
SHEET 4 J 5 VAL A1006 THR A1012 -1 N ALA A1007 O SER A1042
SHEET 5 J 5 ASN A1019 HIS A1022 -1 O LEU A1020 N ARG A1011
SSBOND 1 CYS A 31 CYS A 1032 1555 1555 2.05
SSBOND 2 CYS A 275 CYS A 282 1555 1555 2.03
SSBOND 3 CYS A 283 CYS A 297 1555 1555 2.10
SSBOND 4 CYS A 902 CYS A 987 1555 1555 2.05
SSBOND 5 CYS A 1000 CYS A 1009 1555 1555 2.00
LINK ND2 ASN A 194 C1 NAG A1046 1555 1555 1.49
LINK S3 Z4R B 1 C1 MAN B 2 1555 1555 1.81
LINK NE2 HIS A 90 ZN ZN A1048 1555 1555 2.08
LINK OD1 ASP A 92 ZN ZN A1048 1555 1555 2.00
LINK NE2 HIS A 471 ZN ZN A1048 1555 1555 2.07
LINK ZN ZN A1048 O3 MAN B 2 1555 1555 2.13
LINK ZN ZN A1048 O2 MAN B 2 1555 1555 2.23
CISPEP 1 PHE A 405 THR A 406 0 -4.77
CISPEP 2 TRP A 531 PRO A 532 0 -6.29
CRYST1 69.040 109.847 138.627 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 0.014484 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009104 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007214 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
