HEADER HYDROLASE 10-FEB-06 2CEQ
TITLE BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH
TITLE 2 GLUCOIMIDAZOLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-GALACTOSIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: BETA-GLYCOSIDASE, LACTASE;
COMPND 5 EC: 3.2.1.23;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS ARCHAEON, FAMILY 1, GLYCOSIDE HYDROLASE, GLUCOIMIDAZOLE, GLYCOSIDASE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.M.GLOSTER,M.MORACCI,A.VASELLA,G.J.DAVIES
REVDAT 4 13-DEC-23 2CEQ 1 REMARK
REVDAT 3 24-FEB-09 2CEQ 1 VERSN
REVDAT 2 04-OCT-06 2CEQ 1 JRNL
REVDAT 1 27-SEP-06 2CEQ 0
JRNL AUTH T.M.GLOSTER,S.ROBERTS,G.PERUGINO,M.ROSSI,M.MORACCI,N.PANDAY,
JRNL AUTH 2 M.TERINEK,A.VASELLA,G.J.DAVIES
JRNL TITL STRUCTURAL, KINETIC, AND THERMODYNAMIC ANALYSIS OF
JRNL TITL 2 GLUCOIMIDAZOLE-DERIVED GLYCOSIDASE INHIBITORS.
JRNL REF BIOCHEMISTRY V. 45 11879 2006
JRNL REFN ISSN 0006-2960
JRNL PMID 17002288
JRNL DOI 10.1021/BI060973X
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 145.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 79106
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4163
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) : 2.14
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.19
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5667
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 304
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7992
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 876
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.05000
REMARK 3 B22 (A**2) : -1.05000
REMARK 3 B33 (A**2) : 1.57000
REMARK 3 B12 (A**2) : -0.52000
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): 0.177
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.159
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.243
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8541 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11661 ; 1.353 ; 1.937
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1057 ; 6.439 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 445 ;37.452 ;23.101
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1355 ;15.286 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 66 ;18.378 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1163 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6830 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4085 ; 0.205 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5743 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 672 ; 0.140 ; 0.200
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): 124 ; 0.160 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 46 ; 0.159 ; 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): 5128 ; 0.739 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8066 ; 1.206 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4058 ; 1.783 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3554 ; 2.580 ; 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 : 1
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 489 5
REMARK 3 1 B 1 B 489 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1945 ; 0.19 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 1989 ; 0.39 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1945 ; 1.28 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 1989 ; 1.98 ; 10.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2CEQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1290024722.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-APR-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.60
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) : 0.934
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : SAGITALLY FOCUSING GE(220) AND A
REMARK 200 MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83599
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1UWQ
REMARK 200
REMARK 200 REMARK: STRUCTURE ISOMORPHOUS WITH STARTING MODEL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11-14 PEG 4K, 0.1 M SODIUM ACETATE, PH
REMARK 280 4.6 0.2 AMMONIUM ACETATE, 10-13 MG/ML PROTEIN 25% ETHYLENE
REMARK 280 GLYCOL AS CRYO, PH 4.60
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 31.14000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 62.28000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 62.28000
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 31.14000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400
REMARK 400 COMPOUND
REMARK 400 HYDROLYSIS OF TERMINAL NON-REDUCING BETA-D-
REMARK 400 GALACTOSE RESIDUES IN BETA-D-GALACTOSIDES
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 ARG A 94 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 100 CB CG CD OE1 OE2
REMARK 470 LYS A 273 CD CE NZ
REMARK 470 GLU A 331 CB CG CD OE1 OE2
REMARK 470 LYS A 332 CB CG CD CE NZ
REMARK 470 ARG B 94 CB CG CD NE CZ NH1 NH2
REMARK 470 GLU B 120 CB CG CD OE1 OE2
REMARK 470 LYS B 273 CD CE NZ
REMARK 470 GLU B 303 CB CG CD OE1 OE2
REMARK 470 GLU B 331 CG CD OE1 OE2
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 OE2 GLU A 27 OH TYR A 34 1.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 79 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 LEU A 80 CA - CB - CG ANGL. DEV. = 15.2 DEGREES
REMARK 500 LEU B 80 CA - CB - CG ANGL. DEV. = 15.9 DEGREES
REMARK 500 GLY B 301 N - CA - C ANGL. DEV. = -20.1 DEGREES
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 PRO A 5 151.41 -47.45
REMARK 500 HIS A 150 50.62 -141.73
REMARK 500 TRP A 151 -59.44 102.93
REMARK 500 VAL A 216 -63.77 -128.65
REMARK 500 SER A 228 109.58 -165.85
REMARK 500 ASP A 272 0.36 -67.86
REMARK 500 ARG A 286 -60.25 -135.56
REMARK 500 LYS A 332 -70.37 -48.20
REMARK 500 SER A 348 -150.95 -155.48
REMARK 500 PHE A 364 70.09 -157.18
REMARK 500 ASP A 392 83.72 -161.90
REMARK 500 TRP A 433 -130.98 53.47
REMARK 500 TRP B 151 -59.64 104.18
REMARK 500 VAL B 216 -56.36 -129.30
REMARK 500 SER B 228 113.61 -167.13
REMARK 500 ARG B 286 -63.75 -135.01
REMARK 500 ARG B 300 -86.60 -105.86
REMARK 500 ASN B 302 -15.79 94.43
REMARK 500 SER B 348 -153.02 -148.36
REMARK 500 PHE B 364 74.55 -158.04
REMARK 500 ASP B 392 80.67 -160.83
REMARK 500 TRP B 433 -131.01 53.86
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 ARG B 300 GLY B 301 138.96
REMARK 500 GLY B 301 ASN B 302 56.12
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 A2110 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH B2002 DISTANCE = 6.76 ANGSTROMS
REMARK 525 HOH B2019 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH B2086 DISTANCE = 7.72 ANGSTROMS
REMARK 525 HOH B2135 DISTANCE = 6.02 ANGSTROMS
REMARK 525 HOH B2189 DISTANCE = 7.06 ANGSTROMS
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 9-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 10-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A1491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1490
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1491
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B1492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GIM A1492
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GIM B1493
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GOW RELATED DB: PDB
REMARK 900 BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS
REMARK 900 RELATED ID: 1UWI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MUTATED BETA-GLYCOSIDASE FROM SULFOLOBUS
REMARK 900 SOLFATARICUS, WORKING AT MODERATE TEMPERATURE
REMARK 900 RELATED ID: 1UWQ RELATED DB: PDB
REMARK 900 STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS
REMARK 900 RELATED ID: 1UWR RELATED DB: PDB
REMARK 900 STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN
REMARK 900 COMPLEX WITH 2-DEOXY-2- FLUORO-GALACTOSE
REMARK 900 RELATED ID: 1UWS RELATED DB: PDB
REMARK 900 STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN
REMARK 900 COMPLEX WITH 2-DEOXY-2- FLUORO-GLUCOSE
REMARK 900 RELATED ID: 1UWT RELATED DB: PDB
REMARK 900 STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN
REMARK 900 COMPLEX WITH D- GALACTOHYDROXIMO-1,5-LACTAM
REMARK 900 RELATED ID: 1UWU RELATED DB: PDB
REMARK 900 STRUCTURE OF BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN
REMARK 900 COMPLEX WITH D- GLUCOHYDROXYIMO-1,5-LACTAM
REMARK 900 RELATED ID: 2CER RELATED DB: PDB
REMARK 900 BETA-GLYCOSIDASE FROM SULFOLOBUS SOLFATARICUS IN COMPLEX WITH
REMARK 900 PHENETHYL-SUBSTITUTED GLUCOIMIDAZOLE
DBREF 2CEQ A 1 489 UNP P22498 BGAL_SULSO 1 489
DBREF 2CEQ B 1 489 UNP P22498 BGAL_SULSO 1 489
SEQRES 1 A 489 MET TYR SER PHE PRO ASN SER PHE ARG PHE GLY TRP SER
SEQRES 2 A 489 GLN ALA GLY PHE GLN SER GLU MET GLY THR PRO GLY SER
SEQRES 3 A 489 GLU ASP PRO ASN THR ASP TRP TYR LYS TRP VAL HIS ASP
SEQRES 4 A 489 PRO GLU ASN MET ALA ALA GLY LEU VAL SER GLY ASP LEU
SEQRES 5 A 489 PRO GLU ASN GLY PRO GLY TYR TRP GLY ASN TYR LYS THR
SEQRES 6 A 489 PHE HIS ASP ASN ALA GLN LYS MET GLY LEU LYS ILE ALA
SEQRES 7 A 489 ARG LEU ASN VAL GLU TRP SER ARG ILE PHE PRO ASN PRO
SEQRES 8 A 489 LEU PRO ARG PRO GLN ASN PHE ASP GLU SER LYS GLN ASP
SEQRES 9 A 489 VAL THR GLU VAL GLU ILE ASN GLU ASN GLU LEU LYS ARG
SEQRES 10 A 489 LEU ASP GLU TYR ALA ASN LYS ASP ALA LEU ASN HIS TYR
SEQRES 11 A 489 ARG GLU ILE PHE LYS ASP LEU LYS SER ARG GLY LEU TYR
SEQRES 12 A 489 PHE ILE LEU ASN MET TYR HIS TRP PRO LEU PRO LEU TRP
SEQRES 13 A 489 LEU HIS ASP PRO ILE ARG VAL ARG ARG GLY ASP PHE THR
SEQRES 14 A 489 GLY PRO SER GLY TRP LEU SER THR ARG THR VAL TYR GLU
SEQRES 15 A 489 PHE ALA ARG PHE SER ALA TYR ILE ALA TRP LYS PHE ASP
SEQRES 16 A 489 ASP LEU VAL ASP GLU TYR SER THR MET ASN GLU PRO ASN
SEQRES 17 A 489 VAL VAL GLY GLY LEU GLY TYR VAL GLY VAL LYS SER GLY
SEQRES 18 A 489 PHE PRO PRO GLY TYR LEU SER PHE GLU LEU SER ARG ARG
SEQRES 19 A 489 ALA MET TYR ASN ILE ILE GLN ALA HIS ALA ARG ALA TYR
SEQRES 20 A 489 ASP GLY ILE LYS SER VAL SER LYS LYS PRO VAL GLY ILE
SEQRES 21 A 489 ILE TYR ALA ASN SER SER PHE GLN PRO LEU THR ASP LYS
SEQRES 22 A 489 ASP MET GLU ALA VAL GLU MET ALA GLU ASN ASP ASN ARG
SEQRES 23 A 489 TRP TRP PHE PHE ASP ALA ILE ILE ARG GLY GLU ILE THR
SEQRES 24 A 489 ARG GLY ASN GLU LYS ILE VAL ARG ASP ASP LEU LYS GLY
SEQRES 25 A 489 ARG LEU ASP TRP ILE GLY VAL ASN TYR TYR THR ARG THR
SEQRES 26 A 489 VAL VAL LYS ARG THR GLU LYS GLY TYR VAL SER LEU GLY
SEQRES 27 A 489 GLY TYR GLY HIS GLY CYS GLU ARG ASN SER VAL SER LEU
SEQRES 28 A 489 ALA GLY LEU PRO THR SER ASP PHE GLY TRP GLU PHE PHE
SEQRES 29 A 489 PRO GLU GLY LEU TYR ASP VAL LEU THR LYS TYR TRP ASN
SEQRES 30 A 489 ARG TYR HIS LEU TYR MET TYR VAL THR GLU ASN GLY ILE
SEQRES 31 A 489 ALA ASP ASP ALA ASP TYR GLN ARG PRO TYR TYR LEU VAL
SEQRES 32 A 489 SER HIS VAL TYR GLN VAL HIS ARG ALA ILE ASN SER GLY
SEQRES 33 A 489 ALA ASP VAL ARG GLY TYR LEU HIS TRP SER LEU ALA ASP
SEQRES 34 A 489 ASN TYR GLU TRP ALA SER GLY PHE SER MET ARG PHE GLY
SEQRES 35 A 489 LEU LEU LYS VAL ASP TYR ASN THR LYS ARG LEU TYR TRP
SEQRES 36 A 489 ARG PRO SER ALA LEU VAL TYR ARG GLU ILE ALA THR ASN
SEQRES 37 A 489 GLY ALA ILE THR ASP GLU ILE GLU HIS LEU ASN SER VAL
SEQRES 38 A 489 PRO PRO VAL LYS PRO LEU ARG HIS
SEQRES 1 B 489 MET TYR SER PHE PRO ASN SER PHE ARG PHE GLY TRP SER
SEQRES 2 B 489 GLN ALA GLY PHE GLN SER GLU MET GLY THR PRO GLY SER
SEQRES 3 B 489 GLU ASP PRO ASN THR ASP TRP TYR LYS TRP VAL HIS ASP
SEQRES 4 B 489 PRO GLU ASN MET ALA ALA GLY LEU VAL SER GLY ASP LEU
SEQRES 5 B 489 PRO GLU ASN GLY PRO GLY TYR TRP GLY ASN TYR LYS THR
SEQRES 6 B 489 PHE HIS ASP ASN ALA GLN LYS MET GLY LEU LYS ILE ALA
SEQRES 7 B 489 ARG LEU ASN VAL GLU TRP SER ARG ILE PHE PRO ASN PRO
SEQRES 8 B 489 LEU PRO ARG PRO GLN ASN PHE ASP GLU SER LYS GLN ASP
SEQRES 9 B 489 VAL THR GLU VAL GLU ILE ASN GLU ASN GLU LEU LYS ARG
SEQRES 10 B 489 LEU ASP GLU TYR ALA ASN LYS ASP ALA LEU ASN HIS TYR
SEQRES 11 B 489 ARG GLU ILE PHE LYS ASP LEU LYS SER ARG GLY LEU TYR
SEQRES 12 B 489 PHE ILE LEU ASN MET TYR HIS TRP PRO LEU PRO LEU TRP
SEQRES 13 B 489 LEU HIS ASP PRO ILE ARG VAL ARG ARG GLY ASP PHE THR
SEQRES 14 B 489 GLY PRO SER GLY TRP LEU SER THR ARG THR VAL TYR GLU
SEQRES 15 B 489 PHE ALA ARG PHE SER ALA TYR ILE ALA TRP LYS PHE ASP
SEQRES 16 B 489 ASP LEU VAL ASP GLU TYR SER THR MET ASN GLU PRO ASN
SEQRES 17 B 489 VAL VAL GLY GLY LEU GLY TYR VAL GLY VAL LYS SER GLY
SEQRES 18 B 489 PHE PRO PRO GLY TYR LEU SER PHE GLU LEU SER ARG ARG
SEQRES 19 B 489 ALA MET TYR ASN ILE ILE GLN ALA HIS ALA ARG ALA TYR
SEQRES 20 B 489 ASP GLY ILE LYS SER VAL SER LYS LYS PRO VAL GLY ILE
SEQRES 21 B 489 ILE TYR ALA ASN SER SER PHE GLN PRO LEU THR ASP LYS
SEQRES 22 B 489 ASP MET GLU ALA VAL GLU MET ALA GLU ASN ASP ASN ARG
SEQRES 23 B 489 TRP TRP PHE PHE ASP ALA ILE ILE ARG GLY GLU ILE THR
SEQRES 24 B 489 ARG GLY ASN GLU LYS ILE VAL ARG ASP ASP LEU LYS GLY
SEQRES 25 B 489 ARG LEU ASP TRP ILE GLY VAL ASN TYR TYR THR ARG THR
SEQRES 26 B 489 VAL VAL LYS ARG THR GLU LYS GLY TYR VAL SER LEU GLY
SEQRES 27 B 489 GLY TYR GLY HIS GLY CYS GLU ARG ASN SER VAL SER LEU
SEQRES 28 B 489 ALA GLY LEU PRO THR SER ASP PHE GLY TRP GLU PHE PHE
SEQRES 29 B 489 PRO GLU GLY LEU TYR ASP VAL LEU THR LYS TYR TRP ASN
SEQRES 30 B 489 ARG TYR HIS LEU TYR MET TYR VAL THR GLU ASN GLY ILE
SEQRES 31 B 489 ALA ASP ASP ALA ASP TYR GLN ARG PRO TYR TYR LEU VAL
SEQRES 32 B 489 SER HIS VAL TYR GLN VAL HIS ARG ALA ILE ASN SER GLY
SEQRES 33 B 489 ALA ASP VAL ARG GLY TYR LEU HIS TRP SER LEU ALA ASP
SEQRES 34 B 489 ASN TYR GLU TRP ALA SER GLY PHE SER MET ARG PHE GLY
SEQRES 35 B 489 LEU LEU LYS VAL ASP TYR ASN THR LYS ARG LEU TYR TRP
SEQRES 36 B 489 ARG PRO SER ALA LEU VAL TYR ARG GLU ILE ALA THR ASN
SEQRES 37 B 489 GLY ALA ILE THR ASP GLU ILE GLU HIS LEU ASN SER VAL
SEQRES 38 B 489 PRO PRO VAL LYS PRO LEU ARG HIS
HET ACT A1490 4
HET ACT A1491 4
HET GIM A1492 14
HET ACT B1490 4
HET ACT B1491 4
HET ACT B1492 4
HET GIM B1493 14
HETNAM ACT ACETATE ION
HETNAM GIM GLUCOIMIDAZOLE
HETSYN GIM (5S,6S,7R,8R)-5-(HYDROXYMETHYL)-1,5,6,7,8,8A-
HETSYN 2 GIM HEXAHYDROIMIDAZO[1,2-A]PYRIDINE-6,7,8-TRIOL
FORMUL 3 ACT 5(C2 H3 O2 1-)
FORMUL 5 GIM 2(C8 H13 N2 O4 1+)
FORMUL 10 HOH *876(H2 O)
HELIX 1 1 ALA A 15 GLU A 20 1 6
HELIX 2 2 THR A 31 ASP A 39 1 9
HELIX 3 3 ASP A 39 ALA A 45 1 7
HELIX 4 4 LEU A 52 GLY A 56 5 5
HELIX 5 5 GLY A 58 MET A 73 1 16
HELIX 6 6 GLU A 83 PHE A 88 1 6
HELIX 7 7 ASN A 111 ALA A 122 1 12
HELIX 8 8 ASN A 123 SER A 139 1 17
HELIX 9 9 LEU A 155 LEU A 157 5 3
HELIX 10 10 ASP A 159 ARG A 165 1 7
HELIX 11 11 GLY A 173 LEU A 175 5 3
HELIX 12 12 SER A 176 ASP A 195 1 20
HELIX 13 13 GLU A 206 VAL A 216 1 11
HELIX 14 14 GLY A 217 GLY A 221 5 5
HELIX 15 15 SER A 228 SER A 252 1 25
HELIX 16 16 ASP A 274 ARG A 286 1 13
HELIX 17 17 ARG A 286 GLY A 296 1 11
HELIX 18 18 PRO A 365 HIS A 380 1 16
HELIX 19 19 GLN A 397 SER A 415 1 19
HELIX 20 20 TRP A 433 SER A 435 5 3
HELIX 21 21 PHE A 437 MET A 439 5 3
HELIX 22 22 ARG A 456 GLY A 469 1 14
HELIX 23 23 THR A 472 ASN A 479 5 8
HELIX 24 24 ALA B 15 GLU B 20 1 6
HELIX 25 25 THR B 31 ASP B 39 1 9
HELIX 26 26 ASP B 39 ALA B 45 1 7
HELIX 27 27 LEU B 52 GLY B 56 5 5
HELIX 28 28 GLY B 58 MET B 73 1 16
HELIX 29 29 GLU B 83 PHE B 88 1 6
HELIX 30 30 ASN B 111 GLU B 120 1 10
HELIX 31 31 ASN B 123 ARG B 140 1 18
HELIX 32 32 ASP B 159 ARG B 165 1 7
HELIX 33 33 GLY B 173 LEU B 175 5 3
HELIX 34 34 SER B 176 ASP B 195 1 20
HELIX 35 35 GLU B 206 VAL B 216 1 11
HELIX 36 36 GLY B 217 GLY B 221 5 5
HELIX 37 37 SER B 228 SER B 252 1 25
HELIX 38 38 ASP B 274 ARG B 286 1 13
HELIX 39 39 ARG B 286 GLY B 296 1 11
HELIX 40 40 PRO B 365 HIS B 380 1 16
HELIX 41 41 GLN B 397 SER B 415 1 19
HELIX 42 42 GLU B 432 MET B 439 5 8
HELIX 43 43 ARG B 456 GLY B 469 1 14
HELIX 44 44 THR B 472 ASN B 479 5 8
SHEET 1 AA 2 TYR A 2 SER A 3 0
SHEET 2 AA 2 ALA A 470 ILE A 471 -1 O ILE A 471 N TYR A 2
SHEET 1 AB10 ARG A 9 SER A 13 0
SHEET 2 AB10 VAL A 419 HIS A 424 1 O ARG A 420 N ARG A 9
SHEET 3 AB10 MET A 383 GLU A 387 1 O MET A 383 N ARG A 420
SHEET 4 AB10 ILE A 317 ARG A 329 1 O ILE A 317 N TYR A 384
SHEET 5 AB10 VAL A 258 PRO A 269 1 O ILE A 260 N GLY A 318
SHEET 6 AB10 GLU A 200 ASN A 205 1 O TYR A 201 N GLY A 259
SHEET 7 AB10 TYR A 143 ASN A 147 1 O LEU A 146 N SER A 202
SHEET 8 AB10 ILE A 77 ASN A 81 1 O ALA A 78 N ILE A 145
SHEET 9 AB10 ARG A 9 SER A 13 1 O TRP A 12 N ARG A 79
SHEET 10 AB10 ARG A 9 SER A 13 0
SHEET 1 AC 2 GLU A 297 ARG A 300 0
SHEET 2 AC 2 GLU A 303 VAL A 306 -1 O GLU A 303 N ARG A 300
SHEET 1 AD 2 LEU A 444 VAL A 446 0
SHEET 2 AD 2 LEU A 453 TRP A 455 -1 O TYR A 454 N LYS A 445
SHEET 1 BA 2 TYR B 2 SER B 3 0
SHEET 2 BA 2 ALA B 470 ILE B 471 -1 O ILE B 471 N TYR B 2
SHEET 1 BB10 ARG B 9 SER B 13 0
SHEET 2 BB10 VAL B 419 HIS B 424 1 O ARG B 420 N ARG B 9
SHEET 3 BB10 MET B 383 GLU B 387 1 O MET B 383 N ARG B 420
SHEET 4 BB10 ILE B 317 ARG B 329 1 O ILE B 317 N TYR B 384
SHEET 5 BB10 VAL B 258 PRO B 269 1 O ILE B 260 N GLY B 318
SHEET 6 BB10 GLU B 200 ASN B 205 1 O TYR B 201 N GLY B 259
SHEET 7 BB10 TYR B 143 ASN B 147 1 O LEU B 146 N SER B 202
SHEET 8 BB10 ILE B 77 ASN B 81 1 O ALA B 78 N ILE B 145
SHEET 9 BB10 ARG B 9 SER B 13 1 O TRP B 12 N ARG B 79
SHEET 10 BB10 ARG B 9 SER B 13 0
SHEET 1 BC 2 GLU B 297 THR B 299 0
SHEET 2 BC 2 LYS B 304 VAL B 306 -1 O ILE B 305 N ILE B 298
SHEET 1 BD 2 LEU B 444 ASP B 447 0
SHEET 2 BD 2 ARG B 452 TRP B 455 -1 O ARG B 452 N ASP B 447
CISPEP 1 PRO A 223 PRO A 224 0 -1.90
CISPEP 2 TRP A 425 SER A 426 0 5.12
CISPEP 3 PRO B 223 PRO B 224 0 0.12
CISPEP 4 TRP B 425 SER B 426 0 4.71
SITE 1 AC1 4 GLY A 46 SER A 49 ALA A 434 HOH A2442
SITE 1 AC2 1 ARG A 234
SITE 1 AC3 4 ASN A 113 TYR B 2 HIS B 410 ASN B 414
SITE 1 AC4 3 THR B 323 HIS B 342 GIM B1493
SITE 1 AC5 4 TRP B 455 ARG B 463 GLU B 464 GLU B 474
SITE 1 AC6 12 GLN A 18 HIS A 150 TRP A 151 ASN A 205
SITE 2 AC6 12 GLU A 206 TYR A 322 TRP A 361 GLU A 387
SITE 3 AC6 12 TRP A 425 GLU A 432 TRP A 433 PHE A 441
SITE 1 AC7 12 GLN B 18 HIS B 150 ASN B 205 GLU B 206
SITE 2 AC7 12 TYR B 322 TRP B 361 GLU B 387 TRP B 425
SITE 3 AC7 12 GLU B 432 TRP B 433 PHE B 441 ACT B1491
CRYST1 167.927 167.927 93.420 90.00 90.00 120.00 P 31 2 1 12
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 0.005955 0.003438 0.000000 0.00000
SCALE2 0.000000 0.006876 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010704 0.00000
MTRIX1 1 -0.942000 0.034000 -0.335000 271.26645 1
MTRIX2 1 0.032000 -0.981000 -0.189000 137.54636 1
MTRIX3 1 -0.335000 -0.189000 0.923000 60.68984 1
(ATOM LINES ARE NOT SHOWN.)
END
