HEADER HYDROLASE 14-DEC-10 3PZU
TITLE P212121 CRYSTAL FORM OF THE ENDO-1,4-BETA-GLUCANASE FROM BACILLUS
TITLE 2 SUBTILIS 168
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 27-332;
COMPND 5 SYNONYM: CARBOXYMETHYL-CELLULASE, CMCASE, CELLULASE, ENDO-1,4-BETA-
COMPND 6 GLUCANASE;
COMPND 7 EC: 3.2.1.4;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: EGLS, BGLC, GLD, BSU18130;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA BARREL, GLYCOSYL HYDROLASE, CELLULOSE BINDING, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.SANTOS,J.H.PAIVA,P.K.AKAO,A.N.MEZA,J.C.SILVA,F.M.SQUINA,R.J.WARD,
AUTHOR 2 R.RULLER,M.T.MURAKAMI
REVDAT 4 21-FEB-24 3PZU 1 REMARK SEQADV
REVDAT 3 15-NOV-17 3PZU 1 REMARK
REVDAT 2 28-DEC-11 3PZU 1 JRNL
REVDAT 1 14-SEP-11 3PZU 0
JRNL AUTH C.R.SANTOS,J.H.PAIVA,M.L.SFORCA,J.L.NEVES,R.Z.NAVARRO,
JRNL AUTH 2 J.COTA,P.K.AKAO,Z.B.HOFFMAM,A.N.MEZA,J.H.SMETANA,
JRNL AUTH 3 M.L.NOGUEIRA,I.POLIKARPOV,J.XAVIER-NETO,F.M.SQUINA,R.J.WARD,
JRNL AUTH 4 R.RULLER,A.C.ZERI,M.T.MURAKAMI
JRNL TITL DISSECTING STRUCTURE-FUNCTION-STABILITY RELATIONSHIPS OF A
JRNL TITL 2 THERMOSTABLE GH5-CBM3 CELLULASE FROM BACILLUS SUBTILIS 168.
JRNL REF BIOCHEM.J. V. 441 95 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 21880019
JRNL DOI 10.1042/BJ20110869
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 36885
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1952
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2322
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2020
REMARK 3 BIN FREE R VALUE SET COUNT : 129
REMARK 3 BIN FREE R VALUE : 0.2690
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4670
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 18
REMARK 3 SOLVENT ATOMS : 330
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.92000
REMARK 3 B22 (A**2) : -3.44000
REMARK 3 B33 (A**2) : -0.48000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.176
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.298
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4798 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6497 ; 1.903 ; 1.931
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 592 ; 6.765 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 230 ;37.620 ;25.391
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 808 ;15.933 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;20.100 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 685 ; 0.152 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3662 ; 0.010 ; 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): 2933 ; 1.053 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4695 ; 1.771 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1865 ; 3.117 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1802 ; 4.724 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3PZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000063016.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : LNLS
REMARK 200 BEAMLINE : W01B-MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.4586
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 39069
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 38.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG1500, PH 6.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
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 25.12100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.68950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.38100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 60.68950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.12100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.38100
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: PISA
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: PISA
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 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 6
REMARK 465 GLY A 7
REMARK 465 SER A 8
REMARK 465 SER A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 HIS A 13
REMARK 465 HIS A 14
REMARK 465 HIS A 15
REMARK 465 SER A 16
REMARK 465 SER A 17
REMARK 465 GLY A 18
REMARK 465 LEU A 19
REMARK 465 VAL A 20
REMARK 465 PRO A 21
REMARK 465 ARG A 22
REMARK 465 GLY A 23
REMARK 465 SER A 24
REMARK 465 HIS A 25
REMARK 465 MET A 26
REMARK 465 ALA A 27
REMARK 465 SER A 28
REMARK 465 ALA A 29
REMARK 465 ALA A 30
REMARK 465 GLY A 31
REMARK 465 THR A 32
REMARK 465 LYS A 33
REMARK 465 THR A 34
REMARK 465 THR A 332
REMARK 465 MET B 6
REMARK 465 GLY B 7
REMARK 465 SER B 8
REMARK 465 SER B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 HIS B 13
REMARK 465 HIS B 14
REMARK 465 HIS B 15
REMARK 465 SER B 16
REMARK 465 SER B 17
REMARK 465 GLY B 18
REMARK 465 LEU B 19
REMARK 465 VAL B 20
REMARK 465 PRO B 21
REMARK 465 ARG B 22
REMARK 465 GLY B 23
REMARK 465 SER B 24
REMARK 465 HIS B 25
REMARK 465 MET B 26
REMARK 465 ALA B 27
REMARK 465 SER B 28
REMARK 465 ALA B 29
REMARK 465 ALA B 30
REMARK 465 GLY B 31
REMARK 465 THR B 32
REMARK 465 LYS B 33
REMARK 465 THR B 34
REMARK 465 THR B 332
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 OD2 ASP A 197 O HOH A 341 2.10
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 VAL A 57 CG1 - CB - CG2 ANGL. DEV. = 10.9 DEGREES
REMARK 500 PRO A 182 C - N - CA ANGL. DEV. = -10.7 DEGREES
REMARK 500 PRO B 106 C - N - CA ANGL. DEV. = 11.0 DEGREES
REMARK 500 ARG B 192 NE - CZ - NH1 ANGL. DEV. = 3.4 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 LEU A 133 -79.92 -162.18
REMARK 500 ALA A 167 87.53 -168.87
REMARK 500 ASP A 217 62.51 -152.26
REMARK 500 THR A 234 -48.98 -132.67
REMARK 500 ASN A 266 -156.48 -128.92
REMARK 500 TYR B 70 17.64 -149.24
REMARK 500 LEU B 133 -78.73 -155.21
REMARK 500 ALA B 167 89.51 -163.29
REMARK 500 ASP B 217 63.41 -155.73
REMARK 500 SER B 261 -169.94 -101.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 333
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PZT RELATED DB: PDB
REMARK 900 WITH MANGANASE(II) ION
REMARK 900 RELATED ID: 3PZV RELATED DB: PDB
REMARK 900 C2 CRYSTAL FORM
DBREF 3PZU A 27 332 UNP P10475 GUN2_BACSU 27 332
DBREF 3PZU B 27 332 UNP P10475 GUN2_BACSU 27 332
SEQADV 3PZU MET A 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZU GLY A 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER A 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER A 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS A 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS A 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS A 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS A 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS A 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS A 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER A 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER A 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZU GLY A 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZU LEU A 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZU VAL A 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZU PRO A 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZU ARG A 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZU GLY A 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER A 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS A 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZU MET A 26 UNP P10475 EXPRESSION TAG
SEQADV 3PZU MET B 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZU GLY B 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER B 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER B 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS B 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS B 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS B 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS B 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS B 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS B 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER B 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER B 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZU GLY B 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZU LEU B 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZU VAL B 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZU PRO B 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZU ARG B 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZU GLY B 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZU SER B 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZU HIS B 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZU MET B 26 UNP P10475 EXPRESSION TAG
SEQRES 1 A 327 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 327 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY
SEQRES 3 A 327 THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE
SEQRES 4 A 327 LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL
SEQRES 5 A 327 GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR
SEQRES 6 A 327 GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG
SEQRES 7 A 327 ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR
SEQRES 8 A 327 THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS
SEQRES 9 A 327 ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU
SEQRES 10 A 327 GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP
SEQRES 11 A 327 GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE
SEQRES 12 A 327 PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN
SEQRES 13 A 327 VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL
SEQRES 14 A 327 ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL
SEQRES 15 A 327 ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE
SEQRES 16 A 327 ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP
SEQRES 17 A 327 ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR
SEQRES 18 A 327 ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU
SEQRES 19 A 327 ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO
SEQRES 20 A 327 ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY
SEQRES 21 A 327 ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU
SEQRES 22 A 327 LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP
SEQRES 23 A 327 ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS
SEQRES 24 A 327 PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP
SEQRES 25 A 327 LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU
SEQRES 26 A 327 GLY THR
SEQRES 1 B 327 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 327 LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA GLY
SEQRES 3 B 327 THR LYS THR PRO VAL ALA LYS ASN GLY GLN LEU SER ILE
SEQRES 4 B 327 LYS GLY THR GLN LEU VAL ASN ARG ASP GLY LYS ALA VAL
SEQRES 5 B 327 GLN LEU LYS GLY ILE SER SER HIS GLY LEU GLN TRP TYR
SEQRES 6 B 327 GLY GLU TYR VAL ASN LYS ASP SER LEU LYS TRP LEU ARG
SEQRES 7 B 327 ASP ASP TRP GLY ILE THR VAL PHE ARG ALA ALA MET TYR
SEQRES 8 B 327 THR ALA ASP GLY GLY TYR ILE ASP ASN PRO SER VAL LYS
SEQRES 9 B 327 ASN LYS VAL LYS GLU ALA VAL GLU ALA ALA LYS GLU LEU
SEQRES 10 B 327 GLY ILE TYR VAL ILE ILE ASP TRP HIS ILE LEU ASN ASP
SEQRES 11 B 327 GLY ASN PRO ASN GLN ASN LYS GLU LYS ALA LYS GLU PHE
SEQRES 12 B 327 PHE LYS GLU MET SER SER LEU TYR GLY ASN THR PRO ASN
SEQRES 13 B 327 VAL ILE TYR GLU ILE ALA ASN GLU PRO ASN GLY ASP VAL
SEQRES 14 B 327 ASN TRP LYS ARG ASP ILE LYS PRO TYR ALA GLU GLU VAL
SEQRES 15 B 327 ILE SER VAL ILE ARG LYS ASN ASP PRO ASP ASN ILE ILE
SEQRES 16 B 327 ILE VAL GLY THR GLY THR TRP SER GLN ASP VAL ASN ASP
SEQRES 17 B 327 ALA ALA ASP ASP GLN LEU LYS ASP ALA ASN VAL MET TYR
SEQRES 18 B 327 ALA LEU HIS PHE TYR ALA GLY THR HIS GLY GLN PHE LEU
SEQRES 19 B 327 ARG ASP LYS ALA ASN TYR ALA LEU SER LYS GLY ALA PRO
SEQRES 20 B 327 ILE PHE VAL THR GLU TRP GLY THR SER ASP ALA SER GLY
SEQRES 21 B 327 ASN GLY GLY VAL PHE LEU ASP GLN SER ARG GLU TRP LEU
SEQRES 22 B 327 LYS TYR LEU ASP SER LYS THR ILE SER TRP VAL ASN TRP
SEQRES 23 B 327 ASN LEU SER ASP LYS GLN GLU SER SER SER ALA LEU LYS
SEQRES 24 B 327 PRO GLY ALA SER LYS THR GLY GLY TRP ARG LEU SER ASP
SEQRES 25 B 327 LEU SER ALA SER GLY THR PHE VAL ARG GLU ASN ILE LEU
SEQRES 26 B 327 GLY THR
HET GOL A 1 6
HET GOL B 1 6
HET GOL B 333 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 3(C3 H8 O3)
FORMUL 6 HOH *330(H2 O)
HELIX 1 1 PRO A 35 GLY A 40 1 6
HELIX 2 2 GLY A 66 GLY A 71 1 6
HELIX 3 3 GLU A 72 VAL A 74 5 3
HELIX 4 4 ASN A 75 TRP A 86 1 12
HELIX 5 5 ASN A 105 SER A 107 5 3
HELIX 6 6 VAL A 108 GLY A 123 1 16
HELIX 7 7 ASN A 137 GLN A 140 5 4
HELIX 8 8 ASN A 141 GLY A 157 1 17
HELIX 9 9 ASP A 179 ASP A 195 1 17
HELIX 10 10 THR A 204 GLN A 209 1 6
HELIX 11 11 ASP A 210 ASP A 217 1 8
HELIX 12 12 GLY A 236 LYS A 249 1 14
HELIX 13 13 PHE A 270 LYS A 284 1 15
HELIX 14 14 ARG A 314 LEU A 318 5 5
HELIX 15 15 SER A 319 GLY A 331 1 13
HELIX 16 16 PRO B 35 GLY B 40 1 6
HELIX 17 17 GLY B 66 GLY B 71 1 6
HELIX 18 18 GLU B 72 VAL B 74 5 3
HELIX 19 19 ASN B 75 GLY B 87 1 13
HELIX 20 20 SER B 107 GLY B 123 1 17
HELIX 21 21 ASN B 141 GLY B 157 1 17
HELIX 22 22 ASP B 179 ASP B 195 1 17
HELIX 23 23 THR B 204 GLN B 209 1 6
HELIX 24 24 ASP B 210 ASP B 216 1 7
HELIX 25 25 GLY B 236 LYS B 249 1 14
HELIX 26 26 PHE B 270 LYS B 284 1 15
HELIX 27 27 ARG B 314 LEU B 318 5 5
HELIX 28 28 SER B 319 GLY B 331 1 13
SHEET 1 A 2 SER A 43 LYS A 45 0
SHEET 2 A 2 GLN A 48 VAL A 50 -1 O GLN A 48 N LYS A 45
SHEET 1 B 9 LYS A 60 SER A 64 0
SHEET 2 B 9 VAL A 90 TYR A 96 1 O ARG A 92 N SER A 64
SHEET 3 B 9 TYR A 125 HIS A 131 1 O ILE A 127 N PHE A 91
SHEET 4 B 9 VAL A 162 GLU A 165 1 O GLU A 165 N ILE A 128
SHEET 5 B 9 ILE A 200 VAL A 202 1 O ILE A 201 N TYR A 164
SHEET 6 B 9 VAL A 224 TYR A 231 1 O MET A 225 N VAL A 202
SHEET 7 B 9 ILE A 253 GLY A 259 1 O PHE A 254 N TYR A 226
SHEET 8 B 9 TRP A 288 LEU A 293 1 O TRP A 291 N TRP A 258
SHEET 9 B 9 LYS A 60 SER A 64 1 N SER A 63 O LEU A 293
SHEET 1 C 2 SER B 43 LYS B 45 0
SHEET 2 C 2 GLN B 48 VAL B 50 -1 O VAL B 50 N SER B 43
SHEET 1 D 9 LYS B 60 SER B 64 0
SHEET 2 D 9 VAL B 90 TYR B 96 1 O ARG B 92 N SER B 64
SHEET 3 D 9 TYR B 125 HIS B 131 1 O ILE B 127 N PHE B 91
SHEET 4 D 9 VAL B 162 GLU B 165 1 O ILE B 163 N ILE B 128
SHEET 5 D 9 ILE B 200 VAL B 202 1 O ILE B 201 N TYR B 164
SHEET 6 D 9 VAL B 224 TYR B 231 1 O ALA B 227 N VAL B 202
SHEET 7 D 9 ILE B 253 GLY B 259 1 O PHE B 254 N TYR B 226
SHEET 8 D 9 TRP B 288 LEU B 293 1 O TRP B 291 N TRP B 258
SHEET 9 D 9 LYS B 60 SER B 64 1 N SER B 63 O LEU B 293
CISPEP 1 TRP A 291 ASN A 292 0 5.72
CISPEP 2 TRP B 291 ASN B 292 0 -0.59
SITE 1 AC1 10 ALA A 37 LYS A 38 GLY A 306 ALA A 307
SITE 2 AC1 10 SER A 308 TRP A 313 HOH A 438 HOH A 501
SITE 3 AC1 10 LYS B 296 GLN B 297
SITE 1 AC2 8 GLN A 48 ALA A 56 THR A 285 TRP B 207
SITE 2 AC2 8 GLN B 209 HIS B 235 HOH B 343 HOH B 360
SITE 1 AC3 7 PRO A 35 ASN A 39 THR A 89 HOH A 401
SITE 2 AC3 7 ASP B 262 SER B 264 HOH B 490
CRYST1 50.242 110.762 121.379 90.00 90.00 90.00 P 21 21 21 8
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 0.019904 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008239 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
