HEADER HYDROLASE 18-JAN-06 2DCY
TITLE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS FAMILY-11 XYLANASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDO-1,4-BETA-XYLANASE A;
COMPND 3 CHAIN: A, B, C, D, E;
COMPND 4 SYNONYM: XYLANASE A, 1,4-BETA-D-XYLAN XYLANOHYDROLASE A;
COMPND 5 EC: 3.2.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: XYNA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTD-TAC
KEYWDS ALL BETA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.KONDO,K.MIYAZAKI,M.TAKENOUCHI,N.NORO,M.SUZUKI,S.TSUDA
REVDAT 5 25-OCT-23 2DCY 1 REMARK
REVDAT 4 10-JUL-19 2DCY 1 COMPND REMARK HET HETNAM
REVDAT 4 2 1 FORMUL LINK SITE ATOM
REVDAT 3 24-FEB-09 2DCY 1 VERSN
REVDAT 2 25-APR-06 2DCY 1 JRNL
REVDAT 1 07-FEB-06 2DCY 0
JRNL AUTH K.MIYAZAKI,M.TAKENOUCHI,H.KONDO,N.NORO,M.SUZUKI,S.TSUDA
JRNL TITL THERMAL STABILIZATION OF BACILLUS SUBTILIS FAMILY-11
JRNL TITL 2 XYLANASE BY DIRECTED EVOLUTION
JRNL REF J.BIOL.CHEM. V. 281 10236 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16467302
JRNL DOI 10.1074/JBC.M511948200
REMARK 2
REMARK 2 RESOLUTION. 1.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 1.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 169733
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8929
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) : 1.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.44
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10466
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2460
REMARK 3 BIN FREE R VALUE SET COUNT : 532
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7235
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 88
REMARK 3 SOLVENT ATOMS : 248
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.16
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.08000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -0.05000
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): 0.066
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.066
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.040
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.993
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.943
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7596 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10406 ; 1.701 ; 1.883
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 920 ; 8.009 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1071 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6069 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2955 ; 0.201 ; 0.200
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): 315 ; 0.101 ; 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): 88 ; 0.220 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.090 ; 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): 4543 ; 0.937 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7323 ; 1.536 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3053 ; 2.291 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3083 ; 3.036 ; 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 : BABINET MODEL WITH 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 2DCY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000025267.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-DEC-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 178663
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.400
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : 0.04400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.30100
REMARK 200 R SYM FOR SHELL (I) : 0.30100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1XNB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M IMIDAZOLE, 1.0-1.1K/NA TARTRATE,
REMARK 280 PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 65.22250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 93.10450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 65.22250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 93.10450
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, 3, 4, 5
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E
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 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 O GLN A 175 O1 TLA B 503 2.03
REMARK 500 NH1 ARG B 112 O11 TLA B 503 2.14
REMARK 500 O1 TLA B 503 O HOH B 633 2.15
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 ASP A 101 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 119 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 121 CB - CG - OD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ARG B 132 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP C 4 CB - CG - OD2 ANGL. DEV. = 6.2 DEGREES
REMARK 500 LYS C 99 CD - CE - NZ ANGL. DEV. = 14.2 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 ALA A 165 -155.28 -88.92
REMARK 500 ALA B 165 -152.60 -101.28
REMARK 500 ASN C 8 87.51 -151.16
REMARK 500 ALA C 165 -153.61 -96.46
REMARK 500 SER D 74 -4.51 124.80
REMARK 500 ALA D 165 -155.59 -82.48
REMARK 500 ALA E 165 -155.19 -95.98
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 SER D 74 PRO D 75 38.68
REMARK 500 GLY D 161 SER D 162 -137.51
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 DIO C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DIO B 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR B 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR C 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TAR A 507
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DCZ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN(Q7H/N8F/S179C)
DBREF 2DCY A 1 185 UNP P18429 XYNA_BACSU 29 213
DBREF 2DCY B 1 185 UNP P18429 XYNA_BACSU 29 213
DBREF 2DCY C 1 185 UNP P18429 XYNA_BACSU 29 213
DBREF 2DCY D 1 185 UNP P18429 XYNA_BACSU 29 213
DBREF 2DCY E 1 185 UNP P18429 XYNA_BACSU 29 213
SEQRES 1 A 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 A 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 A 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 A 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 A 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 A 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 A 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 A 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 A 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 A 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 A 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 A 185 ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 A 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 A 185 ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 A 185 THR VAL TRP
SEQRES 1 B 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 B 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 B 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 B 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 B 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 B 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 B 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 B 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 B 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 B 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 B 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 B 185 ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 B 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 B 185 ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 B 185 THR VAL TRP
SEQRES 1 C 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 C 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 C 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 C 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 C 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 C 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 C 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 C 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 C 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 C 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 C 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 C 185 ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 C 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 C 185 ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 C 185 THR VAL TRP
SEQRES 1 D 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 D 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 D 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 D 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 D 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 D 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 D 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 D 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 D 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 D 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 D 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 D 185 ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 D 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 D 185 ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 D 185 THR VAL TRP
SEQRES 1 E 185 ALA SER THR ASP TYR TRP GLN ASN TRP THR ASP GLY GLY
SEQRES 2 E 185 GLY ILE VAL ASN ALA VAL ASN GLY SER GLY GLY ASN TYR
SEQRES 3 E 185 SER VAL ASN TRP SER ASN THR GLY ASN PHE VAL VAL GLY
SEQRES 4 E 185 LYS GLY TRP THR THR GLY SER PRO PHE ARG THR ILE ASN
SEQRES 5 E 185 TYR ASN ALA GLY VAL TRP ALA PRO ASN GLY ASN GLY TYR
SEQRES 6 E 185 LEU THR LEU TYR GLY TRP THR ARG SER PRO LEU ILE GLU
SEQRES 7 E 185 TYR TYR VAL VAL ASP SER TRP GLY THR TYR ARG PRO THR
SEQRES 8 E 185 GLY THR TYR LYS GLY THR VAL LYS SER ASP GLY GLY THR
SEQRES 9 E 185 TYR ASP ILE TYR THR THR THR ARG TYR ASN ALA PRO SER
SEQRES 10 E 185 ILE ASP GLY ASP ARG THR THR PHE THR GLN TYR TRP SER
SEQRES 11 E 185 VAL ARG GLN SER LYS ARG PRO THR GLY SER ASN ALA THR
SEQRES 12 E 185 ILE THR PHE SER ASN HIS VAL ASN ALA TRP LYS SER HIS
SEQRES 13 E 185 GLY MET ASN LEU GLY SER ASN TRP ALA TYR GLN VAL MET
SEQRES 14 E 185 ALA THR GLU GLY TYR GLN SER SER GLY SER SER ASN VAL
SEQRES 15 E 185 THR VAL TRP
HET DIO A 602 6
HET TLA A 504 10
HET TAR A 507 10
HET DIO B 603 6
HET TLA B 502 10
HET TLA B 503 10
HET TLA B 505 10
HET DIO C 601 6
HET TLA C 506 10
HET TLA E 501 10
HETNAM DIO 1,4-DIETHYLENE DIOXIDE
HETNAM TLA L(+)-TARTARIC ACID
HETNAM TAR D(-)-TARTARIC ACID
FORMUL 6 DIO 3(C4 H8 O2)
FORMUL 7 TLA 6(C4 H6 O6)
FORMUL 8 TAR C4 H6 O6
FORMUL 16 HOH *248(H2 O)
HELIX 1 1 PHE A 146 HIS A 156 1 11
HELIX 2 2 PHE B 146 HIS B 156 1 11
HELIX 3 3 PHE C 146 HIS C 156 1 11
HELIX 4 4 PHE D 146 SER D 155 1 10
HELIX 5 5 PHE E 146 HIS E 156 1 11
SHEET 1 A 8 TYR A 5 THR A 10 0
SHEET 2 A 8 ASN A 35 TRP A 42 -1 O GLY A 39 N GLN A 7
SHEET 3 A 8 ASN A 163 TYR A 174 -1 O THR A 171 N VAL A 38
SHEET 4 A 8 GLY A 64 ARG A 73 -1 N THR A 67 O ALA A 170
SHEET 5 A 8 ILE A 77 TRP A 85 -1 O TYR A 79 N GLY A 70
SHEET 6 A 8 GLY A 120 ARG A 132 1 O SER A 130 N VAL A 82
SHEET 7 A 8 GLY A 103 SER A 117 -1 N THR A 110 O GLN A 127
SHEET 8 A 8 THR A 93 SER A 100 -1 N GLY A 96 O ILE A 107
SHEET 1 B 5 ILE A 15 ASN A 20 0
SHEET 2 B 5 ASN A 25 SER A 31 -1 O ASN A 29 N ASN A 17
SHEET 3 B 5 SER A 177 TRP A 185 -1 O GLY A 178 N TRP A 30
SHEET 4 B 5 THR A 50 ASN A 61 -1 N ASN A 61 O SER A 177
SHEET 5 B 5 ALA A 142 THR A 145 -1 O ALA A 142 N TYR A 53
SHEET 1 C 8 TYR B 5 THR B 10 0
SHEET 2 C 8 ASN B 35 TRP B 42 -1 O GLY B 39 N GLN B 7
SHEET 3 C 8 ASN B 163 TRP B 185 -1 O GLN B 167 N TRP B 42
SHEET 4 C 8 THR B 50 ARG B 73 -1 N ASN B 61 O SER B 177
SHEET 5 C 8 ILE B 77 TRP B 85 -1 O TYR B 79 N GLY B 70
SHEET 6 C 8 GLY B 120 ARG B 132 1 O SER B 130 N VAL B 82
SHEET 7 C 8 GLY B 103 SER B 117 -1 N THR B 110 O GLN B 127
SHEET 8 C 8 THR B 93 SER B 100 -1 N GLY B 96 O ILE B 107
SHEET 1 D 5 ILE B 15 ASN B 20 0
SHEET 2 D 5 ASN B 25 SER B 31 -1 O ASN B 29 N ASN B 17
SHEET 3 D 5 ASN B 163 TRP B 185 -1 O GLY B 178 N TRP B 30
SHEET 4 D 5 THR B 50 ARG B 73 -1 N ASN B 61 O SER B 177
SHEET 5 D 5 ALA B 142 THR B 145 -1 O ILE B 144 N ILE B 51
SHEET 1 E 8 TYR C 5 THR C 10 0
SHEET 2 E 8 ASN C 35 TRP C 42 -1 O GLY C 39 N GLN C 7
SHEET 3 E 8 ASN C 163 TYR C 174 -1 O THR C 171 N VAL C 38
SHEET 4 E 8 GLY C 64 ARG C 73 -1 N THR C 67 O ALA C 170
SHEET 5 E 8 ILE C 77 TRP C 85 -1 O VAL C 81 N LEU C 68
SHEET 6 E 8 GLY C 120 ARG C 132 1 O SER C 130 N VAL C 82
SHEET 7 E 8 GLY C 103 SER C 117 -1 N THR C 110 O GLN C 127
SHEET 8 E 8 THR C 93 SER C 100 -1 N LYS C 95 O ILE C 107
SHEET 1 F 5 ILE C 15 ASN C 20 0
SHEET 2 F 5 ASN C 25 SER C 31 -1 O ASN C 29 N ASN C 17
SHEET 3 F 5 SER C 177 TRP C 185 -1 O GLY C 178 N TRP C 30
SHEET 4 F 5 THR C 50 ASN C 61 -1 N ASN C 61 O SER C 177
SHEET 5 F 5 ALA C 142 THR C 145 -1 O ILE C 144 N ILE C 51
SHEET 1 G 8 TYR D 5 THR D 10 0
SHEET 2 G 8 ASN D 35 TRP D 42 -1 O GLY D 39 N GLN D 7
SHEET 3 G 8 ASN D 163 TRP D 185 -1 O THR D 171 N VAL D 38
SHEET 4 G 8 THR D 50 ARG D 73 -1 N ASN D 61 O SER D 177
SHEET 5 G 8 ILE D 77 TRP D 85 -1 O ILE D 77 N THR D 72
SHEET 6 G 8 GLY D 120 ARG D 132 1 O SER D 130 N VAL D 82
SHEET 7 G 8 GLY D 103 SER D 117 -1 N ARG D 112 O PHE D 125
SHEET 8 G 8 THR D 93 SER D 100 -1 N VAL D 98 O TYR D 105
SHEET 1 H 5 ILE D 15 ASN D 20 0
SHEET 2 H 5 ASN D 25 SER D 31 -1 O ASN D 29 N ASN D 17
SHEET 3 H 5 ASN D 163 TRP D 185 -1 O SER D 180 N VAL D 28
SHEET 4 H 5 THR D 50 ARG D 73 -1 N ASN D 61 O SER D 177
SHEET 5 H 5 ALA D 142 THR D 145 -1 O ILE D 144 N ILE D 51
SHEET 1 I 8 TYR E 5 THR E 10 0
SHEET 2 I 8 ASN E 35 TRP E 42 -1 O GLY E 39 N GLN E 7
SHEET 3 I 8 ASN E 163 TRP E 185 -1 O GLN E 167 N TRP E 42
SHEET 4 I 8 THR E 50 ARG E 73 -1 N THR E 67 O ALA E 170
SHEET 5 I 8 ILE E 77 TRP E 85 -1 O TYR E 79 N GLY E 70
SHEET 6 I 8 GLY E 120 ARG E 132 1 O SER E 130 N VAL E 82
SHEET 7 I 8 GLY E 103 SER E 117 -1 N THR E 110 O GLN E 127
SHEET 8 I 8 THR E 93 SER E 100 -1 N GLY E 96 O ILE E 107
SHEET 1 J 5 ILE E 15 ASN E 20 0
SHEET 2 J 5 ASN E 25 SER E 31 -1 O ASN E 29 N ASN E 17
SHEET 3 J 5 ASN E 163 TRP E 185 -1 O GLY E 178 N TRP E 30
SHEET 4 J 5 THR E 50 ARG E 73 -1 N THR E 67 O ALA E 170
SHEET 5 J 5 ALA E 142 THR E 145 -1 O ILE E 144 N ILE E 51
CISPEP 1 SER A 74 PRO A 75 0 -1.20
CISPEP 2 SER B 74 PRO B 75 0 1.55
CISPEP 3 SER C 74 PRO C 75 0 -0.90
CISPEP 4 SER E 74 PRO E 75 0 0.58
SITE 1 AC1 6 TRP C 9 TYR C 69 PRO C 116 SER C 117
SITE 2 AC1 6 TYR C 166 HOH C 638
SITE 1 AC2 4 ASN A 29 TRP A 30 ASN B 29 TRP B 30
SITE 1 AC3 10 ILE A 15 ASN A 17 ASN A 29 TRP A 30
SITE 2 AC3 10 SER A 31 ILE B 15 ASN B 17 ASN B 29
SITE 3 AC3 10 TRP B 30 SER B 31
SITE 1 AC4 9 SER A 134 LYS A 135 SER E 74 LYS E 99
SITE 2 AC4 9 SER E 100 ASP E 101 GLY E 102 GLY E 103
SITE 3 AC4 9 HOH E 528
SITE 1 AC5 6 ASN B 8 VAL B 16 ASN B 17 ALA B 18
SITE 2 AC5 6 TYR B 113 TLA B 505
SITE 1 AC6 14 GLN A 175 SER A 176 HOH A 610 TYR B 65
SITE 2 AC6 14 TYR B 88 PRO B 90 THR B 91 THR B 110
SITE 3 AC6 14 ARG B 112 GLN B 127 TRP B 129 HOH B 630
SITE 4 AC6 14 HOH B 633 HOH B 639
SITE 1 AC7 4 SER A 100 ASP A 101 GLY A 102 ASN A 148
SITE 1 AC8 8 TRP B 6 ASN B 8 ALA B 18 TYR B 113
SITE 2 AC8 8 TLA B 502 SER C 134 LYS C 135 HOH C 644
SITE 1 AC9 10 ALA A 1 THR C 3 ASP C 4 TYR C 5
SITE 2 AC9 10 ASN C 20 SER C 22 GLY C 23 GLY C 24
SITE 3 AC9 10 LYS C 40 HOH C 634
SITE 1 BC1 11 TRP A 58 SER A 84 TRP A 85 LYS A 135
SITE 2 BC1 11 HOH A 607 HOH A 619 HOH A 626 VAL E 98
SITE 3 BC1 11 ASN E 148 ASN E 151 ALA E 152
CRYST1 130.445 186.209 37.979 90.00 90.00 90.00 P 21 21 2 20
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 0.007666 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005370 0.000000 0.00000
SCALE3 0.000000 0.000000 0.026330 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
