HEADER HYDROLASE 14-DEC-10 3PZT
TITLE STRUCTURE OF THE ENDO-1,4-BETA-GLUCANASE FROM BACILLUS SUBTILIS 168
TITLE 2 WITH MANGANESE(II) ION
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 3 21-FEB-24 3PZT 1 REMARK SEQADV LINK
REVDAT 2 28-DEC-11 3PZT 1 JRNL
REVDAT 1 14-SEP-11 3PZT 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. 1.97 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) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 44663
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2378
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.97
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.02
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2857
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 85.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 159
REMARK 3 BIN FREE R VALUE : 0.2900
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4635
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 452
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.08000
REMARK 3 B22 (A**2) : -0.77000
REMARK 3 B33 (A**2) : -1.30000
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): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.277
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4780 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6478 ; 1.938 ; 1.932
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 593 ; 6.658 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 231 ;37.817 ;25.411
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 807 ;15.559 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;21.625 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 682 ; 0.162 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3658 ; 0.011 ; 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): 2915 ; 1.212 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4669 ; 1.973 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1865 ; 3.210 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1806 ; 4.864 ; 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 3PZT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000063015.
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 : 47366
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 42.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
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) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.04
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.8
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 (%): 46.89
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
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 24.76300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 61.13100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.30850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 61.13100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.76300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.30850
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 PRO A 35
REMARK 465 VAL A 36
REMARK 465 ALA A 37
REMARK 465 LYS A 38
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 PRO B 35
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 OG SER A 261 O ASN A 266 1.98
REMARK 500 O HOH B 335 O HOH B 475 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 PHE B 230 CE1 PHE B 230 CZ 0.114
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 LYS A 80 CD - CE - NZ ANGL. DEV. = -18.0 DEGREES
REMARK 500 ASP A 99 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU B 239 CB - CG - CD2 ANGL. DEV. = 12.1 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 LEU A 133 -76.98 -157.68
REMARK 500 ALA A 167 89.80 -169.59
REMARK 500 ASP A 217 62.75 -152.63
REMARK 500 ASN A 266 -159.43 -126.54
REMARK 500 ASN B 105 79.67 -160.74
REMARK 500 LEU B 133 -77.31 -161.24
REMARK 500 ALA B 167 88.77 -163.14
REMARK 500 ASN B 168 -73.54 -36.04
REMARK 500 ASP B 217 56.96 -155.09
REMARK 500 SER B 261 -165.15 -103.26
REMARK 500 ASN B 266 -147.58 -132.50
REMARK 500 PHE B 270 79.29 -119.66
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 MN A 1 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 195 OD1
REMARK 620 2 ASP A 197 OD2 91.6
REMARK 620 3 HOH A 339 O 119.2 83.2
REMARK 620 4 HOH A 532 O 152.6 104.5 85.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B 2 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 157 O
REMARK 620 2 ASP B 195 OD1 85.8
REMARK 620 3 ASP B 197 OD2 149.9 82.9
REMARK 620 4 HOH B 489 O 102.5 151.1 100.8
REMARK 620 5 HOH B 557 O 60.2 106.2 96.6 101.8
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 334
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3PZU RELATED DB: PDB
REMARK 900 P212121 CRYSTAL FORM
REMARK 900 RELATED ID: 3PZV RELATED DB: PDB
REMARK 900 C2 CRYSTAL FORM
DBREF 3PZT A 27 332 UNP P10475 GUN2_BACSU 27 332
DBREF 3PZT B 27 332 UNP P10475 GUN2_BACSU 27 332
SEQADV 3PZT MET A 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZT GLY A 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER A 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER A 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS A 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS A 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS A 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS A 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS A 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS A 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER A 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER A 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZT GLY A 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZT LEU A 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZT VAL A 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZT PRO A 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZT ARG A 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZT GLY A 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER A 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS A 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZT MET A 26 UNP P10475 EXPRESSION TAG
SEQADV 3PZT MET B 6 UNP P10475 EXPRESSION TAG
SEQADV 3PZT GLY B 7 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER B 8 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER B 9 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS B 10 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS B 11 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS B 12 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS B 13 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS B 14 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS B 15 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER B 16 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER B 17 UNP P10475 EXPRESSION TAG
SEQADV 3PZT GLY B 18 UNP P10475 EXPRESSION TAG
SEQADV 3PZT LEU B 19 UNP P10475 EXPRESSION TAG
SEQADV 3PZT VAL B 20 UNP P10475 EXPRESSION TAG
SEQADV 3PZT PRO B 21 UNP P10475 EXPRESSION TAG
SEQADV 3PZT ARG B 22 UNP P10475 EXPRESSION TAG
SEQADV 3PZT GLY B 23 UNP P10475 EXPRESSION TAG
SEQADV 3PZT SER B 24 UNP P10475 EXPRESSION TAG
SEQADV 3PZT HIS B 25 UNP P10475 EXPRESSION TAG
SEQADV 3PZT 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 MN A 1 1
HET GOL A 333 6
HET MN B 2 1
HET GOL B 1 6
HET GOL B 333 6
HET PO4 B 334 5
HETNAM MN MANGANESE (II) ION
HETNAM GOL GLYCEROL
HETNAM PO4 PHOSPHATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 MN 2(MN 2+)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 8 PO4 O4 P 3-
FORMUL 9 HOH *452(H2 O)
HELIX 1 1 GLY A 66 GLY A 71 1 6
HELIX 2 2 GLU A 72 VAL A 74 5 3
HELIX 3 3 ASN A 75 TRP A 86 1 12
HELIX 4 4 ASN A 105 SER A 107 5 3
HELIX 5 5 VAL A 108 GLY A 123 1 16
HELIX 6 6 ASN A 141 GLY A 157 1 17
HELIX 7 7 ASP A 179 ASP A 195 1 17
HELIX 8 8 THR A 204 GLN A 209 1 6
HELIX 9 9 ASP A 210 ASP A 216 1 7
HELIX 10 10 GLY A 236 LYS A 249 1 14
HELIX 11 11 PHE A 270 LYS A 284 1 15
HELIX 12 12 ARG A 314 LEU A 318 5 5
HELIX 13 13 SER A 319 GLY A 331 1 13
HELIX 14 14 GLY B 66 GLY B 71 1 6
HELIX 15 15 GLU B 72 VAL B 74 5 3
HELIX 16 16 ASN B 75 TRP B 86 1 12
HELIX 17 17 ASN B 105 SER B 107 5 3
HELIX 18 18 VAL B 108 GLY B 123 1 16
HELIX 19 19 ASN B 141 GLY B 157 1 17
HELIX 20 20 ASP B 179 ASP B 195 1 17
HELIX 21 21 THR B 204 GLN B 209 1 6
HELIX 22 22 ASP B 210 ASP B 216 1 7
HELIX 23 23 GLY B 236 LYS B 249 1 14
HELIX 24 24 PHE B 270 LYS B 284 1 15
HELIX 25 25 ARG B 314 LEU B 318 5 5
HELIX 26 26 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 ALA A 93
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 ALA B 93
SHEET 4 D 9 VAL B 162 GLU B 165 1 O GLU B 165 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 MET B 225 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
LINK MN MN A 1 OD1 ASP A 195 1555 1555 2.42
LINK MN MN A 1 OD2 ASP A 197 1555 1555 2.15
LINK MN MN A 1 O HOH A 339 1555 1555 2.49
LINK MN MN A 1 O HOH A 532 1555 1555 2.37
LINK MN MN B 2 O GLY B 157 1555 1555 2.50
LINK MN MN B 2 OD1 ASP B 195 1555 1555 2.36
LINK MN MN B 2 OD2 ASP B 197 1555 1555 2.41
LINK MN MN B 2 O HOH B 489 1555 1555 2.02
LINK MN MN B 2 O HOH B 557 1555 1555 2.60
CISPEP 1 TRP A 291 ASN A 292 0 6.65
CISPEP 2 TRP B 291 ASN B 292 0 3.01
SITE 1 AC1 6 GLY A 157 ASP A 195 ASP A 197 ASN A 198
SITE 2 AC1 6 HOH A 339 HOH A 532
SITE 1 AC2 7 GLY A 172 VAL A 174 GLY A 205 ASP A 210
SITE 2 AC2 7 HOH A 373 HOH A 477 HOH B 351
SITE 1 AC3 6 GLY B 157 ASP B 195 ASP B 197 ASN B 198
SITE 2 AC3 6 HOH B 489 HOH B 557
SITE 1 AC4 12 GLN A 48 ALA A 56 THR A 285 THR B 206
SITE 2 AC4 12 TRP B 207 GLN B 209 HIS B 235 ALA B 263
SITE 3 AC4 12 HOH B 375 HOH B 439 HOH B 468 HOH B 503
SITE 1 AC5 9 ASN A 134 GLY A 136 ASN A 171 GLY A 172
SITE 2 AC5 9 HOH A 365 THR B 47 GLN B 48 LYS B 284
SITE 3 AC5 9 HOH B 398
SITE 1 AC6 3 ASP B 85 TRP B 313 ARG B 326
CRYST1 49.526 110.617 122.262 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 0.020191 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009040 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008179 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
