HEADER HYDROLASE 16-NOV-09 2WYI
TITLE STRUCTURE OF THE STREPTOCOCCUS PYOGENES FAMILY GH38 ALPHA-MANNOSIDASE
TITLE 2 COMPLEXED WITH SWAINSONINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-MANNOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: ALPHA-MANNOSIDASE II;
COMPND 5 EC: 3.2.1.24;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PYOGENES;
SOURCE 3 ORGANISM_TAXID: 160490;
SOURCE 4 STRAIN: M1 GAS;
SOURCE 5 ATCC: 700294;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS HYDROLASE, GLYCOSIDASE, GLYCOSIDE HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.D.L.SUITS,Y.ZHU,E.J.TAYLOR,D.L.ZECHEL,H.J.GILBERT,G.J.DAVIES
REVDAT 3 20-DEC-23 2WYI 1 REMARK LINK
REVDAT 2 13-JUL-11 2WYI 1 VERSN
REVDAT 1 16-FEB-10 2WYI 0
JRNL AUTH M.D.L.SUITS,Y.ZHU,E.J.TAYLOR,D.L.ZECHEL,H.J.GILBERT,
JRNL AUTH 2 G.J.DAVIES
JRNL TITL STRUCTURE AND KINETIC INVESTIGATION OF STREPTOCOCCUS
JRNL TITL 2 PYOGENES FAMILY GH38 ALPHA-MANNOSIDASE
JRNL REF PLOS ONE V. 5 E9006 2010
JRNL REFN ESSN 1932-6203
JRNL PMID 20140249
JRNL DOI 10.1371/JOURNAL.PONE.0009006
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 132.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 93181
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) : 0.189
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4888
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6786
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.33
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 358
REMARK 3 BIN FREE R VALUE : 0.2960
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 14274
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 114
REMARK 3 SOLVENT ATOMS : 345
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.89000
REMARK 3 B22 (A**2) : 0.89000
REMARK 3 B33 (A**2) : -1.77000
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): 0.327
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.235
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.421
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.949
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14778 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 20061 ; 1.111 ; 1.949
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1808 ; 5.724 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 742 ;33.958 ;24.501
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2434 ;14.680 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 88 ;19.023 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2201 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11361 ; 0.004 ; 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): 8979 ; 0.396 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14493 ; 0.782 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5799 ; 1.193 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5558 ; 2.041 ; 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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 901 5
REMARK 3 1 B 3 B 901 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3572 ; 0.12 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 3572 ; 0.12 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 3490 ; 0.20 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 3490 ; 0.20 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3572 ; 0.35 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 3572 ; 0.35 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 3490 ; 0.48 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 3490 ; 0.48 ; 10.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1000 A 1001 4
REMARK 3 1 B 1000 B 1001 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 13 ; 0.16 ; 0.50
REMARK 3 MEDIUM POSITIONAL 2 B (A): 13 ; 0.16 ; 0.50
REMARK 3 MEDIUM THERMAL 2 A (A**2): 13 ; 0.30 ; 2.00
REMARK 3 MEDIUM THERMAL 2 B (A**2): 13 ; 0.30 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 901
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5857 -61.3333 13.3467
REMARK 3 T TENSOR
REMARK 3 T11: 0.0431 T22: 0.1583
REMARK 3 T33: 0.0477 T12: 0.0489
REMARK 3 T13: -0.0093 T23: 0.0531
REMARK 3 L TENSOR
REMARK 3 L11: 0.7310 L22: 0.4806
REMARK 3 L33: 0.6155 L12: 0.2130
REMARK 3 L13: 0.1368 L23: -0.0138
REMARK 3 S TENSOR
REMARK 3 S11: 0.1001 S12: 0.0618 S13: -0.0083
REMARK 3 S21: 0.0105 S22: -0.1346 S23: -0.0976
REMARK 3 S31: 0.0949 S32: 0.1789 S33: 0.0345
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 3 B 901
REMARK 3 ORIGIN FOR THE GROUP (A): 18.5605 -23.1757 6.7078
REMARK 3 T TENSOR
REMARK 3 T11: 0.1580 T22: 0.1393
REMARK 3 T33: 0.2586 T12: -0.0061
REMARK 3 T13: -0.0435 T23: 0.1098
REMARK 3 L TENSOR
REMARK 3 L11: 0.6737 L22: 0.5354
REMARK 3 L33: 0.9816 L12: 0.1355
REMARK 3 L13: 0.3071 L23: 0.1770
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: 0.0926 S13: 0.3779
REMARK 3 S21: -0.0551 S22: -0.1015 S23: 0.0820
REMARK 3 S31: -0.2933 S32: 0.0388 S33: 0.1470
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. U VALUES RESIDUAL ONLY DISORDERED REGION OF MOLECULES
REMARK 3 WERE MODELED STEREOCHEMICALLY AGAINST THE APO STRUCTURE
REMARK 3 (RESIDUES 156- 163). ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY
REMARK 4
REMARK 4 2WYI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-NOV-09.
REMARK 100 THE DEPOSITION ID IS D_1290041714.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-08
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 : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9334
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93181
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 27.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP, SHELX, RESOLVE, PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2WYH
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.84
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 MG/ML 3C CLEAVED SPGH38 MIXED WITH
REMARK 280 3% V/V GLYCEROL, 54% V/V TACSIMATE (PH 7.0) AND 2% V/V
REMARK 280 POLYETHYLENE GLYCOL 6000
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
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 99.11850
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 89.34000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 89.34000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 148.67775
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 89.34000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 89.34000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 49.55925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 89.34000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.34000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 148.67775
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 89.34000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.34000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 49.55925
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 99.11850
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9790 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 62150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.1 KCAL/MOL
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 -21
REMARK 465 GLY A -20
REMARK 465 SER A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 LEU A -8
REMARK 465 GLU A -7
REMARK 465 VAL A -6
REMARK 465 LEU A -5
REMARK 465 PHE A -4
REMARK 465 GLN A -3
REMARK 465 GLY A -2
REMARK 465 PRO A -1
REMARK 465 ALA A 0
REMARK 465 THR A 516
REMARK 465 THR A 517
REMARK 465 PRO A 518
REMARK 465 SER A 519
REMARK 465 GLU A 520
REMARK 465 MET B -21
REMARK 465 GLY B -20
REMARK 465 SER B -19
REMARK 465 SER B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 GLY B -9
REMARK 465 LEU B -8
REMARK 465 GLU B -7
REMARK 465 VAL B -6
REMARK 465 LEU B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 ALA B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 516
REMARK 465 THR B 517
REMARK 465 PRO B 518
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PHE A 156 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN A 157 CG OD1 ND2
REMARK 470 ASN A 158 CG OD1 ND2
REMARK 470 GLN A 159 CG CD OE1 NE2
REMARK 470 VAL A 160 CG1 CG2
REMARK 470 LYS A 165 CE NZ
REMARK 470 LYS A 386 CG CD CE NZ
REMARK 470 HIS A 581 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 620 CG CD CE NZ
REMARK 470 LYS A 710 CE NZ
REMARK 470 GLU A 728 CG CD OE1 OE2
REMARK 470 LYS A 789 CG CD CE NZ
REMARK 470 LYS A 881 CG CD CE NZ
REMARK 470 ASN B 158 CG OD1 ND2
REMARK 470 GLN B 159 CG CD OE1 NE2
REMARK 470 VAL B 160 CG1 CG2
REMARK 470 SER B 163 OG
REMARK 470 GLN B 249 CG CD OE1 NE2
REMARK 470 GLU B 274 CG CD OE1 OE2
REMARK 470 GLN B 280 CG CD OE1 NE2
REMARK 470 MET B 399 CG SD CE
REMARK 470 GLN B 431 CG CD OE1 NE2
REMARK 470 ASN B 514 CG OD1 ND2
REMARK 470 GLU B 515 CG CD OE1 OE2
REMARK 470 SER B 519 OG
REMARK 470 GLU B 520 CG CD OE1 OE2
REMARK 470 THR B 521 OG1 CG2
REMARK 470 ASP B 527 CG OD1 OD2
REMARK 470 SER B 528 OG
REMARK 470 LYS B 538 CG CD CE NZ
REMARK 470 MET B 540 CG SD CE
REMARK 470 LYS B 620 CG CD CE NZ
REMARK 470 LYS B 685 CG CD CE NZ
REMARK 470 LYS B 699 CG CD CE NZ
REMARK 470 LYS B 710 CG CD CE NZ
REMARK 470 GLU B 728 CG CD OE1 OE2
REMARK 470 GLN B 790 CG CD OE1 NE2
REMARK 470 GLU B 815 CG CD OE1 OE2
REMARK 470 LYS B 881 CG CD CE NZ
REMARK 470 GLN B 887 CG CD OE1 NE2
REMARK 470 LYS B 900 CG CD CE NZ
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 TRP A 18 -99.73 -161.32
REMARK 500 LEU A 51 42.77 -91.03
REMARK 500 ASN A 180 8.96 82.46
REMARK 500 TRP A 191 162.48 66.90
REMARK 500 GLU A 287 52.91 -104.06
REMARK 500 ASN A 534 -156.46 -126.11
REMARK 500 ASN A 599 102.82 -161.05
REMARK 500 SER A 693 -166.19 -114.35
REMARK 500 GLU A 719 -93.34 -90.58
REMARK 500 ASP A 763 -136.24 51.71
REMARK 500 SER A 862 26.58 -146.43
REMARK 500 ASN A 867 0.45 82.50
REMARK 500 TRP B 18 -100.53 -153.53
REMARK 500 ASN B 180 3.67 84.49
REMARK 500 TRP B 191 159.56 72.27
REMARK 500 GLU B 287 51.40 -105.08
REMARK 500 ILE B 318 -63.00 -123.99
REMARK 500 MET B 503 60.40 33.50
REMARK 500 ASN B 534 -159.26 -125.93
REMARK 500 SER B 693 -166.36 -124.82
REMARK 500 GLU B 719 -95.33 -90.10
REMARK 500 GLU B 728 -27.16 -141.27
REMARK 500 ASP B 763 -139.41 58.54
REMARK 500 PHE B 837 88.38 -150.80
REMARK 500 ASP B 843 14.45 -148.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 90 ASP A 91 148.87
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 A1906 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 13 NE2
REMARK 620 2 ASP A 15 OD1 106.1
REMARK 620 3 ASP A 125 OD2 104.0 149.8
REMARK 620 4 SWA A1907 O11 159.2 76.2 75.4
REMARK 620 5 SWA A1907 O13 94.5 90.0 86.6 64.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1908 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 15 OD1
REMARK 620 2 HIS B 351 NE2 77.5
REMARK 620 3 SWA B1909 O13 92.8 153.1
REMARK 620 4 SWA B1909 O11 84.2 85.4 68.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A 1902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A 1903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A 1904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 A 1905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1906
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SWA A 1907
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B 1902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B 1903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B 1904
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B 1905
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B 1906
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG0 B 1907
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1908
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SWA B 1909
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WYH RELATED DB: PDB
REMARK 900 STRUCTURE OF THE STREPTOCOCCUS PYOGENES FAMILY GH38 ALPHA-
REMARK 900 MANNOSIDASE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE FIRST 22 RESIDUES ARE A C3 PROTEASE CLEAVABLE AFFINITY
REMARK 999 TAG (MGSSHHHHHHSSGLEVLFQGPA)
DBREF 2WYI A -21 0 PDB 2WYI 2WYI -21 0
DBREF 2WYI A 1 901 UNP Q99YP5 Q99YP5_STRP1 1 901
DBREF 2WYI B -21 0 PDB 2WYI 2WYI -21 0
DBREF 2WYI B 1 901 UNP Q99YP5 Q99YP5_STRP1 1 901
SEQRES 1 A 923 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 923 LEU GLU VAL LEU PHE GLN GLY PRO ALA MET ALA THR LYS
SEQRES 3 A 923 LYS VAL HIS ILE ILE SER HIS SER HIS TRP ASP ARG GLU
SEQRES 4 A 923 TRP TYR MET ALA TYR GLU GLN HIS HIS MET ARG LEU ILE
SEQRES 5 A 923 ASN LEU ILE ASP ASP LEU LEU GLU VAL PHE GLN THR ASP
SEQRES 6 A 923 PRO ASP PHE HIS SER PHE HIS LEU ASP GLY GLN THR ILE
SEQRES 7 A 923 ILE LEU ASP ASP TYR LEU LYS VAL ARG PRO GLU ARG GLU
SEQRES 8 A 923 PRO GLU ILE ARG GLN ALA ILE ALA SER GLY LYS LEU ARG
SEQRES 9 A 923 ILE GLY PRO PHE TYR ILE LEU GLN ASP ASP PHE LEU THR
SEQRES 10 A 923 SER SER GLU SER ASN VAL ARG ASN MET LEU ILE GLY LYS
SEQRES 11 A 923 GLU ASP CYS ASP ARG TRP GLY ALA SER VAL PRO LEU GLY
SEQRES 12 A 923 TYR PHE PRO ASP THR PHE GLY ASN MET GLY GLN THR PRO
SEQRES 13 A 923 GLN LEU MET LEU LYS ALA GLY LEU GLN ALA ALA ALA PHE
SEQRES 14 A 923 GLY ARG GLY ILE ARG PRO THR GLY PHE ASN ASN GLN VAL
SEQRES 15 A 923 ASP THR SER GLU LYS TYR SER SER GLN PHE SER GLU ILE
SEQRES 16 A 923 SER TRP GLN GLY PRO ASP ASN SER ARG ILE LEU GLY LEU
SEQRES 17 A 923 LEU PHE ALA ASN TRP TYR SER ASN GLY ASN GLU ILE PRO
SEQRES 18 A 923 THR THR GLU ALA GLU ALA ARG LEU PHE TRP ASP LYS LYS
SEQRES 19 A 923 LEU ALA ASP ALA GLU ARG PHE ALA SER THR LYS HIS LEU
SEQRES 20 A 923 LEU MET MET ASN GLY CYS ASP HIS GLN PRO VAL GLN LEU
SEQRES 21 A 923 ASP VAL THR LYS ALA ILE ALA LEU ALA ASN GLN LEU TYR
SEQRES 22 A 923 PRO ASP TYR GLU PHE VAL HIS SER CYS PHE GLU ASP TYR
SEQRES 23 A 923 LEU ALA ASP LEU ALA ASP ASP LEU PRO GLU ASN LEU SER
SEQRES 24 A 923 THR VAL GLN GLY GLU ILE THR SER GLN GLU THR ASP GLY
SEQRES 25 A 923 TRP TYR THR LEU ALA ASN THR ALA SER ALA ARG ILE TYR
SEQRES 26 A 923 LEU LYS GLN ALA ASN THR ARG VAL SER ARG GLN LEU GLU
SEQRES 27 A 923 ASN ILE THR GLU PRO LEU ALA ALA MET ALA TYR GLU VAL
SEQRES 28 A 923 THR SER THR TYR PRO HIS ASP GLN LEU ARG TYR ALA TRP
SEQRES 29 A 923 LYS THR LEU MET GLN ASN HIS PRO HIS ASP SER ILE CYS
SEQRES 30 A 923 GLY CYS SER VAL ASP SER VAL HIS ARG GLU MET MET THR
SEQRES 31 A 923 ARG PHE GLU LYS ALA TYR GLU VAL GLY HIS TYR LEU ALA
SEQRES 32 A 923 LYS GLU ALA ALA LYS GLN ILE ALA ASP ALA ILE ASP THR
SEQRES 33 A 923 ARG ASP PHE PRO MET ASP SER GLN PRO PHE VAL LEU PHE
SEQRES 34 A 923 ASN THR SER GLY HIS SER LYS THR SER VAL ALA GLU LEU
SEQRES 35 A 923 SER LEU THR TRP LYS LYS TYR HIS PHE GLY GLN ARG PHE
SEQRES 36 A 923 PRO LYS GLU VAL TYR GLN GLU ALA GLN GLU TYR LEU ALA
SEQRES 37 A 923 ARG LEU SER GLN SER PHE GLN ILE ILE ASP THR SER GLY
SEQRES 38 A 923 GLN VAL ARG PRO GLU ALA GLU ILE LEU GLY THR SER ILE
SEQRES 39 A 923 ALA PHE ASP TYR ASP LEU PRO LYS ARG SER PHE ARG GLU
SEQRES 40 A 923 PRO TYR PHE ALA ILE LYS VAL ARG LEU ARG LEU PRO ILE
SEQRES 41 A 923 THR LEU PRO ALA MET SER TRP LYS THR LEU ALA LEU LYS
SEQRES 42 A 923 LEU GLY ASN GLU THR THR PRO SER GLU THR VAL SER LEU
SEQRES 43 A 923 TYR ASP ASP SER ASN GLN CYS LEU GLU ASN GLY PHE LEU
SEQRES 44 A 923 LYS VAL MET ILE GLN THR ASP GLY ARG LEU THR ILE THR
SEQRES 45 A 923 ASP LYS GLN SER GLY LEU ILE TYR GLN ASP LEU LEU ARG
SEQRES 46 A 923 PHE GLU ASP CYS GLY ASP ILE GLY ASN GLU TYR ILE SER
SEQRES 47 A 923 ARG GLN PRO ASN HIS ASP GLN PRO PHE TYR ALA ASP GLN
SEQRES 48 A 923 GLY THR ILE LYS LEU ASN ILE ILE SER ASN THR ALA GLN
SEQRES 49 A 923 VAL ALA GLU LEU GLU ILE GLN GLN THR PHE ALA ILE PRO
SEQRES 50 A 923 ILE SER ALA ASP LYS LEU LEU GLN ALA GLU MET GLU ALA
SEQRES 51 A 923 VAL ILE ASP ILE THR GLU ARG GLN ALA ARG ARG SER GLN
SEQRES 52 A 923 GLU LYS ALA GLU LEU THR LEU THR THR LEU ILE ARG MET
SEQRES 53 A 923 GLU LYS ASN ASN PRO ARG LEU GLN PHE THR THR ARG PHE
SEQRES 54 A 923 ASP ASN GLN MET THR ASN HIS ARG LEU ARG VAL LEU PHE
SEQRES 55 A 923 PRO THR HIS LEU LYS THR ASP HIS HIS LEU ALA ASP SER
SEQRES 56 A 923 ILE PHE GLU THR VAL LYS ARG PRO ASN HIS PRO ASP ALA
SEQRES 57 A 923 THR PHE TRP LYS ASN PRO SER ASN PRO GLN HIS GLN GLU
SEQRES 58 A 923 CYS PHE VAL SER LEU PHE ASP GLY GLU ASN GLY VAL THR
SEQRES 59 A 923 ILE GLY ASN TYR GLY LEU ASN GLU TYR GLU ILE LEU PRO
SEQRES 60 A 923 ASP THR ASN THR ILE ALA ILE THR LEU LEU ARG SER VAL
SEQRES 61 A 923 GLY GLU MET GLY ASP TRP GLY TYR PHE PRO THR PRO GLU
SEQRES 62 A 923 ALA GLN CYS LEU GLY LYS HIS SER LEU SER TYR SER PHE
SEQRES 63 A 923 GLU SER ILE THR LYS GLN THR GLN PHE ALA SER TYR TRP
SEQRES 64 A 923 ARG ALA GLN GLU GLY GLN VAL PRO VAL ILE THR THR GLN
SEQRES 65 A 923 THR ASN GLN HIS GLU GLY THR LEU ALA ALA GLU TYR SER
SEQRES 66 A 923 TYR LEU THR GLY THR ASN ASP GLN VAL ALA LEU THR ALA
SEQRES 67 A 923 PHE LYS ARG ARG LEU ALA ASP ASN ALA LEU ILE THR ARG
SEQRES 68 A 923 SER TYR ASN LEU SER ASN ASP LYS THR CYS ASP PHE SER
SEQRES 69 A 923 LEU SER LEU PRO ASN TYR ASN ALA LYS VAL THR ASN LEU
SEQRES 70 A 923 LEU GLU LYS ASP SER LYS GLN SER THR PRO SER GLN LEU
SEQRES 71 A 923 GLY LYS ALA GLU ILE LEU THR LEU ALA TRP LYS LYS GLN
SEQRES 1 B 923 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 923 LEU GLU VAL LEU PHE GLN GLY PRO ALA MET ALA THR LYS
SEQRES 3 B 923 LYS VAL HIS ILE ILE SER HIS SER HIS TRP ASP ARG GLU
SEQRES 4 B 923 TRP TYR MET ALA TYR GLU GLN HIS HIS MET ARG LEU ILE
SEQRES 5 B 923 ASN LEU ILE ASP ASP LEU LEU GLU VAL PHE GLN THR ASP
SEQRES 6 B 923 PRO ASP PHE HIS SER PHE HIS LEU ASP GLY GLN THR ILE
SEQRES 7 B 923 ILE LEU ASP ASP TYR LEU LYS VAL ARG PRO GLU ARG GLU
SEQRES 8 B 923 PRO GLU ILE ARG GLN ALA ILE ALA SER GLY LYS LEU ARG
SEQRES 9 B 923 ILE GLY PRO PHE TYR ILE LEU GLN ASP ASP PHE LEU THR
SEQRES 10 B 923 SER SER GLU SER ASN VAL ARG ASN MET LEU ILE GLY LYS
SEQRES 11 B 923 GLU ASP CYS ASP ARG TRP GLY ALA SER VAL PRO LEU GLY
SEQRES 12 B 923 TYR PHE PRO ASP THR PHE GLY ASN MET GLY GLN THR PRO
SEQRES 13 B 923 GLN LEU MET LEU LYS ALA GLY LEU GLN ALA ALA ALA PHE
SEQRES 14 B 923 GLY ARG GLY ILE ARG PRO THR GLY PHE ASN ASN GLN VAL
SEQRES 15 B 923 ASP THR SER GLU LYS TYR SER SER GLN PHE SER GLU ILE
SEQRES 16 B 923 SER TRP GLN GLY PRO ASP ASN SER ARG ILE LEU GLY LEU
SEQRES 17 B 923 LEU PHE ALA ASN TRP TYR SER ASN GLY ASN GLU ILE PRO
SEQRES 18 B 923 THR THR GLU ALA GLU ALA ARG LEU PHE TRP ASP LYS LYS
SEQRES 19 B 923 LEU ALA ASP ALA GLU ARG PHE ALA SER THR LYS HIS LEU
SEQRES 20 B 923 LEU MET MET ASN GLY CYS ASP HIS GLN PRO VAL GLN LEU
SEQRES 21 B 923 ASP VAL THR LYS ALA ILE ALA LEU ALA ASN GLN LEU TYR
SEQRES 22 B 923 PRO ASP TYR GLU PHE VAL HIS SER CYS PHE GLU ASP TYR
SEQRES 23 B 923 LEU ALA ASP LEU ALA ASP ASP LEU PRO GLU ASN LEU SER
SEQRES 24 B 923 THR VAL GLN GLY GLU ILE THR SER GLN GLU THR ASP GLY
SEQRES 25 B 923 TRP TYR THR LEU ALA ASN THR ALA SER ALA ARG ILE TYR
SEQRES 26 B 923 LEU LYS GLN ALA ASN THR ARG VAL SER ARG GLN LEU GLU
SEQRES 27 B 923 ASN ILE THR GLU PRO LEU ALA ALA MET ALA TYR GLU VAL
SEQRES 28 B 923 THR SER THR TYR PRO HIS ASP GLN LEU ARG TYR ALA TRP
SEQRES 29 B 923 LYS THR LEU MET GLN ASN HIS PRO HIS ASP SER ILE CYS
SEQRES 30 B 923 GLY CYS SER VAL ASP SER VAL HIS ARG GLU MET MET THR
SEQRES 31 B 923 ARG PHE GLU LYS ALA TYR GLU VAL GLY HIS TYR LEU ALA
SEQRES 32 B 923 LYS GLU ALA ALA LYS GLN ILE ALA ASP ALA ILE ASP THR
SEQRES 33 B 923 ARG ASP PHE PRO MET ASP SER GLN PRO PHE VAL LEU PHE
SEQRES 34 B 923 ASN THR SER GLY HIS SER LYS THR SER VAL ALA GLU LEU
SEQRES 35 B 923 SER LEU THR TRP LYS LYS TYR HIS PHE GLY GLN ARG PHE
SEQRES 36 B 923 PRO LYS GLU VAL TYR GLN GLU ALA GLN GLU TYR LEU ALA
SEQRES 37 B 923 ARG LEU SER GLN SER PHE GLN ILE ILE ASP THR SER GLY
SEQRES 38 B 923 GLN VAL ARG PRO GLU ALA GLU ILE LEU GLY THR SER ILE
SEQRES 39 B 923 ALA PHE ASP TYR ASP LEU PRO LYS ARG SER PHE ARG GLU
SEQRES 40 B 923 PRO TYR PHE ALA ILE LYS VAL ARG LEU ARG LEU PRO ILE
SEQRES 41 B 923 THR LEU PRO ALA MET SER TRP LYS THR LEU ALA LEU LYS
SEQRES 42 B 923 LEU GLY ASN GLU THR THR PRO SER GLU THR VAL SER LEU
SEQRES 43 B 923 TYR ASP ASP SER ASN GLN CYS LEU GLU ASN GLY PHE LEU
SEQRES 44 B 923 LYS VAL MET ILE GLN THR ASP GLY ARG LEU THR ILE THR
SEQRES 45 B 923 ASP LYS GLN SER GLY LEU ILE TYR GLN ASP LEU LEU ARG
SEQRES 46 B 923 PHE GLU ASP CYS GLY ASP ILE GLY ASN GLU TYR ILE SER
SEQRES 47 B 923 ARG GLN PRO ASN HIS ASP GLN PRO PHE TYR ALA ASP GLN
SEQRES 48 B 923 GLY THR ILE LYS LEU ASN ILE ILE SER ASN THR ALA GLN
SEQRES 49 B 923 VAL ALA GLU LEU GLU ILE GLN GLN THR PHE ALA ILE PRO
SEQRES 50 B 923 ILE SER ALA ASP LYS LEU LEU GLN ALA GLU MET GLU ALA
SEQRES 51 B 923 VAL ILE ASP ILE THR GLU ARG GLN ALA ARG ARG SER GLN
SEQRES 52 B 923 GLU LYS ALA GLU LEU THR LEU THR THR LEU ILE ARG MET
SEQRES 53 B 923 GLU LYS ASN ASN PRO ARG LEU GLN PHE THR THR ARG PHE
SEQRES 54 B 923 ASP ASN GLN MET THR ASN HIS ARG LEU ARG VAL LEU PHE
SEQRES 55 B 923 PRO THR HIS LEU LYS THR ASP HIS HIS LEU ALA ASP SER
SEQRES 56 B 923 ILE PHE GLU THR VAL LYS ARG PRO ASN HIS PRO ASP ALA
SEQRES 57 B 923 THR PHE TRP LYS ASN PRO SER ASN PRO GLN HIS GLN GLU
SEQRES 58 B 923 CYS PHE VAL SER LEU PHE ASP GLY GLU ASN GLY VAL THR
SEQRES 59 B 923 ILE GLY ASN TYR GLY LEU ASN GLU TYR GLU ILE LEU PRO
SEQRES 60 B 923 ASP THR ASN THR ILE ALA ILE THR LEU LEU ARG SER VAL
SEQRES 61 B 923 GLY GLU MET GLY ASP TRP GLY TYR PHE PRO THR PRO GLU
SEQRES 62 B 923 ALA GLN CYS LEU GLY LYS HIS SER LEU SER TYR SER PHE
SEQRES 63 B 923 GLU SER ILE THR LYS GLN THR GLN PHE ALA SER TYR TRP
SEQRES 64 B 923 ARG ALA GLN GLU GLY GLN VAL PRO VAL ILE THR THR GLN
SEQRES 65 B 923 THR ASN GLN HIS GLU GLY THR LEU ALA ALA GLU TYR SER
SEQRES 66 B 923 TYR LEU THR GLY THR ASN ASP GLN VAL ALA LEU THR ALA
SEQRES 67 B 923 PHE LYS ARG ARG LEU ALA ASP ASN ALA LEU ILE THR ARG
SEQRES 68 B 923 SER TYR ASN LEU SER ASN ASP LYS THR CYS ASP PHE SER
SEQRES 69 B 923 LEU SER LEU PRO ASN TYR ASN ALA LYS VAL THR ASN LEU
SEQRES 70 B 923 LEU GLU LYS ASP SER LYS GLN SER THR PRO SER GLN LEU
SEQRES 71 B 923 GLY LYS ALA GLU ILE LEU THR LEU ALA TRP LYS LYS GLN
HET PG0 A1902 8
HET PG0 A1903 8
HET PG0 A1904 8
HET PG0 A1905 8
HET ZN A1906 1
HET SWA A1907 12
HET PG0 B1901 8
HET PG0 B1902 8
HET PG0 B1903 8
HET PG0 B1904 8
HET PG0 B1905 8
HET PG0 B1906 8
HET PG0 B1907 8
HET ZN B1908 1
HET SWA B1909 12
HETNAM PG0 2-(2-METHOXYETHOXY)ETHANOL
HETNAM ZN ZINC ION
HETNAM SWA 1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL
HETSYN PG0 PEG 6000
HETSYN SWA SWAINSONINE
FORMUL 3 PG0 11(C5 H12 O3)
FORMUL 7 ZN 2(ZN 2+)
FORMUL 8 SWA 2(C8 H15 N O3)
FORMUL 18 HOH *345(H2 O)
HELIX 1 1 ALA A 21 ASP A 43 1 23
HELIX 2 2 THR A 55 LYS A 63 1 9
HELIX 3 3 ARG A 65 GLU A 67 5 3
HELIX 4 4 ARG A 68 SER A 78 1 11
HELIX 5 5 SER A 96 GLY A 115 1 20
HELIX 6 6 GLN A 132 LYS A 139 1 8
HELIX 7 7 THR A 201 ARG A 218 1 18
HELIX 8 8 ASP A 239 TYR A 251 1 13
HELIX 9 9 CYS A 260 LEU A 272 1 13
HELIX 10 10 LEU A 294 ALA A 300 5 7
HELIX 11 11 ARG A 301 ILE A 318 1 18
HELIX 12 12 ILE A 318 SER A 331 1 14
HELIX 13 13 PRO A 334 GLN A 347 1 14
HELIX 14 14 PRO A 350 CYS A 355 1 6
HELIX 15 15 VAL A 359 ILE A 392 1 34
HELIX 16 16 PHE A 433 LEU A 448 1 16
HELIX 17 17 ASP A 588 GLY A 590 5 3
HELIX 18 18 LYS A 620 ALA A 628 1 9
HELIX 19 19 ASP A 631 ARG A 635 5 5
HELIX 20 20 THR A 769 CYS A 774 5 6
HELIX 21 21 THR A 791 GLY A 802 1 12
HELIX 22 22 ALA B 21 ASP B 43 1 23
HELIX 23 23 THR B 55 ARG B 65 1 11
HELIX 24 24 ARG B 68 SER B 78 1 11
HELIX 25 25 SER B 96 GLY B 115 1 20
HELIX 26 26 GLN B 132 LYS B 139 1 8
HELIX 27 27 THR B 201 ARG B 218 1 18
HELIX 28 28 ASP B 239 TYR B 251 1 13
HELIX 29 29 CYS B 260 LEU B 272 1 13
HELIX 30 30 LEU B 294 ALA B 300 5 7
HELIX 31 31 ARG B 301 ILE B 318 1 18
HELIX 32 32 ILE B 318 SER B 331 1 14
HELIX 33 33 PRO B 334 GLN B 347 1 14
HELIX 34 34 PRO B 350 CYS B 355 1 6
HELIX 35 35 VAL B 359 ASP B 390 1 32
HELIX 36 36 PHE B 433 LEU B 448 1 16
HELIX 37 37 ASP B 588 GLY B 590 5 3
HELIX 38 38 LYS B 620 ALA B 628 1 9
HELIX 39 39 ASP B 631 ARG B 635 5 5
HELIX 40 40 THR B 769 CYS B 774 5 6
HELIX 41 41 THR B 791 GLY B 802 1 12
SHEET 1 AA 3 HIS A 224 ASN A 229 0
SHEET 2 AA 3 LYS A 4 SER A 10 1 O LYS A 5 N LEU A 225
SHEET 3 AA 3 TYR A 254 HIS A 258 1 O GLU A 255 N VAL A 6
SHEET 1 AB 2 PHE A 49 HIS A 50 0
SHEET 2 AB 2 LEU A 81 ARG A 82 1 N ARG A 82 O PHE A 49
SHEET 1 AC 5 GLY A 121 PHE A 123 0
SHEET 2 AC 5 ALA A 144 PHE A 147 1 O ALA A 144 N GLY A 121
SHEET 3 AC 5 ARG A 182 LEU A 187 1 O LEU A 184 N ALA A 145
SHEET 4 AC 5 GLU A 172 GLN A 176 -1 O ILE A 173 N GLY A 185
SHEET 5 AC 5 THR A 278 GLN A 280 1 O VAL A 279 N GLN A 176
SHEET 1 AD 2 ARG A 152 PRO A 153 0
SHEET 2 AD 2 SER A 167 SER A 168 1 N SER A 168 O ARG A 152
SHEET 1 AE 2 SER A 451 ILE A 455 0
SHEET 2 AE 2 SER A 504 GLY A 513 -1 O ALA A 509 N ILE A 455
SHEET 1 AF 4 ILE A 807 GLN A 810 0
SHEET 2 AF 4 GLN A 402 ASN A 408 -1 O VAL A 405 N THR A 809
SHEET 3 AF 4 SER A 504 GLY A 513 -1 O SER A 504 N ASN A 408
SHEET 4 AF 4 GLU A 821 SER A 823 1 O TYR A 822 N TRP A 505
SHEET 1 AG 4 ILE A 807 GLN A 810 0
SHEET 2 AG 4 GLN A 402 ASN A 408 -1 O VAL A 405 N THR A 809
SHEET 3 AG 4 SER A 504 GLY A 513 -1 O SER A 504 N ASN A 408
SHEET 4 AG 4 SER A 451 ILE A 455 -1 O SER A 451 N GLY A 513
SHEET 1 AH 2 GLU A 821 SER A 823 0
SHEET 2 AH 2 SER A 504 GLY A 513 1 O TRP A 505 N TYR A 822
SHEET 1 AI 3 LYS A 414 HIS A 428 0
SHEET 2 AI 3 GLU A 485 LEU A 500 -1 O PHE A 488 N TYR A 427
SHEET 3 AI 3 GLU A 466 ASP A 477 -1 O GLU A 466 N ARG A 495
SHEET 1 AJ 5 TYR A 525 ASP A 526 0
SHEET 2 AJ 5 CYS A 531 GLU A 533 -1 O CYS A 531 N ASP A 526
SHEET 3 AJ 5 LEU A 537 ILE A 541 -1 O VAL A 539 N LEU A 532
SHEET 4 AJ 5 LEU A 547 ASP A 551 -1 O THR A 548 N MET A 540
SHEET 5 AJ 5 ILE A 557 LEU A 561 -1 O TYR A 558 N ILE A 549
SHEET 1 AK 6 PHE A 585 TYR A 586 0
SHEET 2 AK 6 ARG A 563 GLY A 568 -1 O ASP A 566 N PHE A 585
SHEET 3 AK 6 HIS A 674 PRO A 681 -1 O ARG A 675 N CYS A 567
SHEET 4 AK 6 THR A 749 SER A 757 -1 O ILE A 750 N PHE A 680
SHEET 5 AK 6 GLU A 740 LEU A 744 -1 O GLU A 740 N THR A 753
SHEET 6 AK 6 GLN A 716 HIS A 717 -1 O GLN A 716 N TYR A 741
SHEET 1 AL 9 THR A 591 ASN A 599 0
SHEET 2 AL 9 VAL A 603 PRO A 615 -1 O GLU A 605 N ILE A 597
SHEET 3 AL 9 LYS A 643 GLU A 655 -1 O ALA A 644 N ILE A 614
SHEET 4 AL 9 LEU A 661 ASN A 669 -1 O GLN A 662 N ARG A 653
SHEET 5 AL 9 GLY A 776 THR A 788 -1 O GLY A 776 N ASN A 669
SHEET 6 AL 9 ASN A 729 TYR A 736 -1 O GLY A 730 N ILE A 787
SHEET 7 AL 9 PHE A 721 PHE A 725 -1 O VAL A 722 N ILE A 733
SHEET 8 AL 9 HIS A 688 SER A 693 -1 O LEU A 690 N SER A 723
SHEET 9 AL 9 GLU A 696 PRO A 701 -1 O GLU A 696 N SER A 693
SHEET 1 AM 4 VAL A 832 ARG A 839 0
SHEET 2 AM 4 LEU A 846 ASN A 852 -1 O ILE A 847 N LYS A 838
SHEET 3 AM 4 ILE A 893 LYS A 900 -1 O LEU A 894 N SER A 850
SHEET 4 AM 4 TYR A 868 THR A 873 -1 O ASN A 869 N LYS A 899
SHEET 1 AN 2 CYS A 859 ASP A 860 0
SHEET 2 AN 2 GLN A 887 LEU A 888 -1 O LEU A 888 N CYS A 859
SHEET 1 BA 3 HIS B 224 ASN B 229 0
SHEET 2 BA 3 LYS B 4 SER B 10 1 O LYS B 5 N LEU B 225
SHEET 3 BA 3 TYR B 254 HIS B 258 1 O GLU B 255 N VAL B 6
SHEET 1 BB 2 PHE B 49 HIS B 50 0
SHEET 2 BB 2 LEU B 81 ARG B 82 1 N ARG B 82 O PHE B 49
SHEET 1 BC 5 GLY B 121 PHE B 123 0
SHEET 2 BC 5 ALA B 144 PHE B 147 1 O ALA B 144 N GLY B 121
SHEET 3 BC 5 ARG B 182 LEU B 187 1 O LEU B 184 N ALA B 145
SHEET 4 BC 5 GLU B 172 GLN B 176 -1 O ILE B 173 N GLY B 185
SHEET 5 BC 5 THR B 278 GLN B 280 1 O VAL B 279 N GLN B 176
SHEET 1 BD 2 ARG B 152 PRO B 153 0
SHEET 2 BD 2 SER B 167 SER B 168 1 N SER B 168 O ARG B 152
SHEET 1 BE 2 SER B 451 ILE B 455 0
SHEET 2 BE 2 SER B 504 GLY B 513 -1 O ALA B 509 N ILE B 455
SHEET 1 BF 4 ILE B 807 GLN B 810 0
SHEET 2 BF 4 GLN B 402 ASN B 408 -1 O VAL B 405 N THR B 809
SHEET 3 BF 4 SER B 504 GLY B 513 -1 O SER B 504 N ASN B 408
SHEET 4 BF 4 GLU B 821 SER B 823 1 O TYR B 822 N TRP B 505
SHEET 1 BG 4 ILE B 807 GLN B 810 0
SHEET 2 BG 4 GLN B 402 ASN B 408 -1 O VAL B 405 N THR B 809
SHEET 3 BG 4 SER B 504 GLY B 513 -1 O SER B 504 N ASN B 408
SHEET 4 BG 4 SER B 451 ILE B 455 -1 O SER B 451 N GLY B 513
SHEET 1 BH 2 GLU B 821 SER B 823 0
SHEET 2 BH 2 SER B 504 GLY B 513 1 O TRP B 505 N TYR B 822
SHEET 1 BI 3 LYS B 414 HIS B 428 0
SHEET 2 BI 3 GLU B 485 LEU B 500 -1 O PHE B 488 N TYR B 427
SHEET 3 BI 3 GLU B 466 ASP B 477 -1 O GLU B 466 N ARG B 495
SHEET 1 BJ 5 TYR B 525 ASP B 526 0
SHEET 2 BJ 5 CYS B 531 GLU B 533 -1 O CYS B 531 N ASP B 526
SHEET 3 BJ 5 LEU B 537 ILE B 541 -1 O VAL B 539 N LEU B 532
SHEET 4 BJ 5 LEU B 547 ASP B 551 -1 O THR B 548 N MET B 540
SHEET 5 BJ 5 ILE B 557 LEU B 561 -1 O TYR B 558 N ILE B 549
SHEET 1 BK 6 PHE B 585 TYR B 586 0
SHEET 2 BK 6 ARG B 563 GLY B 568 -1 O ASP B 566 N PHE B 585
SHEET 3 BK 6 HIS B 674 PRO B 681 -1 O ARG B 675 N CYS B 567
SHEET 4 BK 6 THR B 749 ARG B 756 -1 O ILE B 750 N PHE B 680
SHEET 5 BK 6 GLU B 740 LEU B 744 -1 O GLU B 740 N THR B 753
SHEET 6 BK 6 GLN B 716 HIS B 717 -1 O GLN B 716 N TYR B 741
SHEET 1 BL 9 THR B 591 ASN B 599 0
SHEET 2 BL 9 VAL B 603 PRO B 615 -1 O GLU B 605 N ILE B 597
SHEET 3 BL 9 LYS B 643 GLU B 655 -1 O ALA B 644 N ILE B 614
SHEET 4 BL 9 LEU B 661 ASN B 669 -1 O GLN B 662 N ARG B 653
SHEET 5 BL 9 GLY B 776 THR B 788 -1 O GLY B 776 N ASN B 669
SHEET 6 BL 9 ASN B 729 ASN B 735 -1 O GLY B 730 N ILE B 787
SHEET 7 BL 9 PHE B 721 PHE B 725 -1 O VAL B 722 N ILE B 733
SHEET 8 BL 9 HIS B 688 SER B 693 -1 O LEU B 690 N SER B 723
SHEET 9 BL 9 GLU B 696 PRO B 701 -1 O GLU B 696 N SER B 693
SHEET 1 BM 4 VAL B 832 ARG B 839 0
SHEET 2 BM 4 LEU B 846 ASN B 852 -1 O ILE B 847 N LYS B 838
SHEET 3 BM 4 ILE B 893 LYS B 900 -1 O LEU B 894 N SER B 850
SHEET 4 BM 4 TYR B 868 THR B 873 -1 O ASN B 869 N LYS B 899
SHEET 1 BN 2 CYS B 859 ASP B 860 0
SHEET 2 BN 2 GLN B 887 LEU B 888 -1 O LEU B 888 N CYS B 859
LINK NE2 HIS A 13 ZN ZN A1906 1555 1555 2.39
LINK OD1 ASP A 15 ZN ZN A1906 1555 1555 2.39
LINK OD2 ASP A 125 ZN ZN A1906 1555 1555 2.43
LINK ZN ZN A1906 O11 SWA A1907 1555 1555 2.38
LINK ZN ZN A1906 O13 SWA A1907 1555 1555 2.36
LINK OD1 ASP B 15 ZN ZN B1908 1555 1555 2.49
LINK NE2 HIS B 351 ZN ZN B1908 1555 1555 2.51
LINK ZN ZN B1908 O13 SWA B1909 1555 1555 2.41
LINK ZN ZN B1908 O11 SWA B1909 1555 1555 2.36
CISPEP 1 GLY A 84 PRO A 85 0 2.61
CISPEP 2 GLY B 84 PRO B 85 0 8.30
SITE 1 AC1 5 TYR A 303 GLU A 771 LEU A 775 LYS A 777
SITE 2 AC1 5 PG0 A1903
SITE 1 AC2 4 GLU A 771 PG0 A1902 HOH A2218 PG0 B1902
SITE 1 AC3 1 GLY A 802
SITE 1 AC4 4 ARG A 310 TYR A 374 HOH A2221 HOH A2222
SITE 1 AC5 5 HIS A 13 ASP A 15 ASP A 125 HIS A 351
SITE 2 AC5 5 SWA A1907
SITE 1 AC6 13 HIS A 13 ASP A 15 TRP A 18 ASP A 125
SITE 2 AC6 13 PHE A 127 ARG A 149 TYR A 192 ASP A 232
SITE 3 AC6 13 HIS A 351 ASP A 352 TYR A 574 ASP A 763
SITE 4 AC6 13 ZN A1906
SITE 1 AC7 4 PG0 A1903 LEU B 775 HOH B2114 HOH B2116
SITE 1 AC8 3 ARG B 310 TYR B 374 PG0 B1905
SITE 1 AC9 2 GLY B 802 PG0 B1905
SITE 1 BC1 5 ARG B 310 SER B 781 PG0 B1903 PG0 B1904
SITE 2 BC1 5 HOH B2123
SITE 1 BC2 1 ALA B 624
SITE 1 BC3 1 ARG B 149
SITE 1 BC4 5 HIS B 13 ASP B 15 ASP B 125 HIS B 351
SITE 2 BC4 5 SWA B1909
SITE 1 BC5 13 HIS B 13 ASP B 15 TRP B 18 ASP B 125
SITE 2 BC5 13 PHE B 127 ARG B 149 TYR B 192 ASP B 232
SITE 3 BC5 13 HIS B 351 ASP B 352 TYR B 574 ASP B 763
SITE 4 BC5 13 ZN B1908
CRYST1 178.680 178.680 198.237 90.00 90.00 90.00 P 43 21 2 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 0.005597 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005597 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005044 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
