HEADER HYDROLASE 13-FEB-02 1ITX
TITLE CATALYTIC DOMAIN OF CHITINASE A1 FROM BACILLUS CIRCULANS WL-12
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLYCOSYL HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: CHITINASE A1;
COMPND 6 EC: 3.2.1.14;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CIRCULANS;
SOURCE 3 ORGANISM_TAXID: 1397;
SOURCE 4 GENE: CHIA1;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HB101;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PKK223-3
KEYWDS ALPHA-BETA (TIM) BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.IWAHORI,T.MATSUMOTO,T.WATANABE,T.NONAKA
REVDAT 5 25-OCT-23 1ITX 1 REMARK
REVDAT 4 13-JUL-11 1ITX 1 VERSN
REVDAT 3 24-FEB-09 1ITX 1 VERSN
REVDAT 2 07-JAN-03 1ITX 1 REMARK
REVDAT 1 13-MAR-02 1ITX 0
JRNL AUTH T.MATSUMOTO,T.NONAKA,M.HASHIMOTO,T.WATANABE,Y.MITSUI
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE CATALYTIC DOMAIN OF
JRNL TITL 2 CHITINASE A1 FROM BACILLUS CIRCULANS WL-12 AT A VERY HIGH
JRNL TITL 3 RESOLUTION
JRNL REF PROC.JPN.ACAD.,SER.B V. 75 269 1999
JRNL REFN ISSN 0386-2208
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.WATANABE,A.ISHIBASHI,Y.ARIGA,M.HASHIMOTO,N.NIKAIDOU,
REMARK 1 AUTH 2 J.SUGIYAMA,T.MATSUMOTO,T.NONAKA
REMARK 1 TITL TRP122 AND TRP134 ON THE SURFACE OF THE CATALYTIC DOMAIN ARE
REMARK 1 TITL 2 ESSENTIAL FOR CRYSTALLINE CHITIN HYDROLYSIS BY BACILLUS
REMARK 1 TITL 3 CIRCULANS CHITINASE A1
REMARK 1 REF FEBS LETT. V. 494 74 2001
REMARK 1 REFN ISSN 0014-5793
REMARK 1 DOI 10.1016/S0014-5793(01)02317-1
REMARK 1 REFERENCE 2
REMARK 1 AUTH T.MATSUMOTO,T.NONAKA,H.KATOUDA,M.HASHIMOTO,T.WATANABE,
REMARK 1 AUTH 2 Y.MITSUI
REMARK 1 TITL CRYSTALLIZATION AND A PRELIMINARY CRYSTALLOGRAPHIC ANALYSIS
REMARK 1 TITL 2 OF THE CATALYTIC DOMAIN OF CHITINASE AL FROM BACILLUS
REMARK 1 TITL 3 CIRCULANS WL-12
REMARK 1 REF PROTEIN PEPT.LETT. V. 6 399 1999
REMARK 1 REFN ISSN 0929-8665
REMARK 1 REFERENCE 3
REMARK 1 AUTH T.WATANABE,K.KOBORI,K.MIYASHITA,T.FUJII,H.SAKAI,M.UCHIDA,
REMARK 1 AUTH 2 H.TANAKA
REMARK 1 TITL IDENTIFICATION OF GLUTAMIC ACID 204 AND ASPARTIC ACID 200 IN
REMARK 1 TITL 2 CHITINASE A1 OF BACILLUS CIRCULANS WL-12 AS ESSENTIAL
REMARK 1 TITL 3 RESIDUES FOR CHITINASE ACTIVITY
REMARK 1 REF J.BIOL.CHEM. V. 268 18567 1993
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 4
REMARK 1 AUTH T.WATANABE,K.SUZUKI,W.OYANAGI,K.OHNISHI,H.TANAKA
REMARK 1 TITL GENE CLONING OF CHITINASE A1 FROM BACILLUS CIRCULANS WL-12
REMARK 1 TITL 2 REVEALED ITS EVOLUTIONARY RELATIONSHIP TO SERRATIA CHITINASE
REMARK 1 TITL 3 AND TO THE TYPE III HOMOLOGY UNITS OF FIBRONECTIN
REMARK 1 REF J.BIOL.CHEM. V. 265 15659 1990
REMARK 1 REFN ISSN 0021-9258
REMARK 1 REFERENCE 5
REMARK 1 AUTH T.UCHIYAMA,F.KATOUNO,N.NIKAIDOU,T.NONAKA,J.SUGIYAMA,
REMARK 1 AUTH 2 T.WATANABE
REMARK 1 TITL ROLES OF THE EXPOSED AROMATIC RESIDUES IN CRYSTALLINE CHITIN
REMARK 1 TITL 2 HYDROLYSIS BY CHITINASE A FROM SERRATIA MARCESCENS 2170
REMARK 1 REF J.BIOL.CHEM. V. 276 41343 2001
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.M103610200
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.0
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.79
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 139823
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) : 0.117
REMARK 3 R VALUE (WORKING SET) : 0.116
REMARK 3 FREE R VALUE : 0.137
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 7125
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) : 1.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9684
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.80
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE SET COUNT : 545
REMARK 3 BIN FREE R VALUE : 0.2120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3221
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 770
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 5.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.979
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3685 ; 0.012 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 3115 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5088 ; 1.675 ; 1.930
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7345 ; 0.864 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 497 ; 5.181 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 581 ;16.200 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 545 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4175 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 739 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1141 ; 0.831 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3568 ; 0.466 ; 0.300
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 30 ; 1.137 ; 0.500
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 560 ; 0.170 ; 0.500
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): 27 ; 0.293 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): 132 ; 0.304 ; 0.300
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 68 ; 0.166 ; 0.500
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): 2260 ; 1.077 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3683 ; 1.573 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1425 ; 1.966 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1399 ; 2.764 ; 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): 3685 ; 1.170 ; 2.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 770 ; 2.912 ; 2.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3584 ; 2.237 ; 2.000
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:
REMARK 3 SOME WATERS ARE LISTED AS DISORDERS COUPLED
REMARK 3 WITH SOME PARTS OF THE PROTEIN MOLECULES.
REMARK 4
REMARK 4 1ITX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-FEB-02.
REMARK 100 THE DEPOSITION ID IS D_1000005270.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-01
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.50000
REMARK 200 MONOCHROMATOR : UNDULATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 139823
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 36.793
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 1.900
REMARK 200 R MERGE (I) : 0.04200
REMARK 200 R SYM (I) : 0.04200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 1.90
REMARK 200 R MERGE FOR SHELL (I) : 0.24800
REMARK 200 R SYM FOR SHELL (I) : 0.24800
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: ARP/WARP
REMARK 200 STARTING MODEL: PDB ENTRY 1CTN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, POTASSIUM DIHYDROPHOSPHATE,
REMARK 280 PH 5.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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 232 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 232 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 308 CB - CG - OD2 ANGL. DEV. = 6.4 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 ASP A 42 -17.10 -47.18
REMARK 500 TYR A 56 -129.73 -89.93
REMARK 500 ASP A 120 79.62 -150.53
REMARK 500 PHE A 129 -166.35 -123.27
REMARK 500 ASP A 135 55.60 -93.53
REMARK 500 ALA A 139 -135.80 -123.32
REMARK 500 LYS A 149 7.65 -68.50
REMARK 500 ASP A 202 68.89 -109.50
REMARK 500 VAL A 207 -56.82 75.54
REMARK 500 GLU A 263 73.12 -102.80
REMARK 500 ALA A 290 -168.66 -167.44
REMARK 500 PHE A 337 39.05 -99.99
REMARK 500 TYR A 379 -38.14 -131.47
REMARK 500 ASP A 438 62.08 -117.22
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1011
DBREF 1ITX A 33 451 UNP P20533 CHIA1_BACCI 33 451
SEQRES 1 A 419 LEU GLN PRO ALA THR ALA GLU ALA ALA ASP SER TYR LYS
SEQRES 2 A 419 ILE VAL GLY TYR TYR PRO SER TRP ALA ALA TYR GLY ARG
SEQRES 3 A 419 ASN TYR ASN VAL ALA ASP ILE ASP PRO THR LYS VAL THR
SEQRES 4 A 419 HIS ILE ASN TYR ALA PHE ALA ASP ILE CYS TRP ASN GLY
SEQRES 5 A 419 ILE HIS GLY ASN PRO ASP PRO SER GLY PRO ASN PRO VAL
SEQRES 6 A 419 THR TRP THR CYS GLN ASN GLU LYS SER GLN THR ILE ASN
SEQRES 7 A 419 VAL PRO ASN GLY THR ILE VAL LEU GLY ASP PRO TRP ILE
SEQRES 8 A 419 ASP THR GLY LYS THR PHE ALA GLY ASP THR TRP ASP GLN
SEQRES 9 A 419 PRO ILE ALA GLY ASN ILE ASN GLN LEU ASN LYS LEU LYS
SEQRES 10 A 419 GLN THR ASN PRO ASN LEU LYS THR ILE ILE SER VAL GLY
SEQRES 11 A 419 GLY TRP THR TRP SER ASN ARG PHE SER ASP VAL ALA ALA
SEQRES 12 A 419 THR ALA ALA THR ARG GLU VAL PHE ALA ASN SER ALA VAL
SEQRES 13 A 419 ASP PHE LEU ARG LYS TYR ASN PHE ASP GLY VAL ASP LEU
SEQRES 14 A 419 ASP TRP GLU TYR PRO VAL SER GLY GLY LEU ASP GLY ASN
SEQRES 15 A 419 SER LYS ARG PRO GLU ASP LYS GLN ASN TYR THR LEU LEU
SEQRES 16 A 419 LEU SER LYS ILE ARG GLU LYS LEU ASP ALA ALA GLY ALA
SEQRES 17 A 419 VAL ASP GLY LYS LYS TYR LEU LEU THR ILE ALA SER GLY
SEQRES 18 A 419 ALA SER ALA THR TYR ALA ALA ASN THR GLU LEU ALA LYS
SEQRES 19 A 419 ILE ALA ALA ILE VAL ASP TRP ILE ASN ILE MET THR TYR
SEQRES 20 A 419 ASP PHE ASN GLY ALA TRP GLN LYS ILE SER ALA HIS ASN
SEQRES 21 A 419 ALA PRO LEU ASN TYR ASP PRO ALA ALA SER ALA ALA GLY
SEQRES 22 A 419 VAL PRO ASP ALA ASN THR PHE ASN VAL ALA ALA GLY ALA
SEQRES 23 A 419 GLN GLY HIS LEU ASP ALA GLY VAL PRO ALA ALA LYS LEU
SEQRES 24 A 419 VAL LEU GLY VAL PRO PHE TYR GLY ARG GLY TRP ASP GLY
SEQRES 25 A 419 CYS ALA GLN ALA GLY ASN GLY GLN TYR GLN THR CYS THR
SEQRES 26 A 419 GLY GLY SER SER VAL GLY THR TRP GLU ALA GLY SER PHE
SEQRES 27 A 419 ASP PHE TYR ASP LEU GLU ALA ASN TYR ILE ASN LYS ASN
SEQRES 28 A 419 GLY TYR THR ARG TYR TRP ASN ASP THR ALA LYS VAL PRO
SEQRES 29 A 419 TYR LEU TYR ASN ALA SER ASN LYS ARG PHE ILE SER TYR
SEQRES 30 A 419 ASP ASP ALA GLU SER VAL GLY TYR LYS THR ALA TYR ILE
SEQRES 31 A 419 LYS SER LYS GLY LEU GLY GLY ALA MET PHE TRP GLU LEU
SEQRES 32 A 419 SER GLY ASP ARG ASN LYS THR LEU GLN ASN LYS LEU LYS
SEQRES 33 A 419 ALA ASP LEU
HET GOL A1001 6
HET GOL A1002 6
HET GOL A1003 8
HET GOL A1004 6
HET GOL A1005 6
HET GOL A1006 6
HET GOL A1007 6
HET GOL A1008 6
HET GOL A1009 6
HET GOL A1010 6
HET GOL A1011 6
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 11(C3 H8 O3)
FORMUL 13 HOH *770(H2 O)
HELIX 1 1 GLU A 39 TYR A 44 5 6
HELIX 2 2 TRP A 53 TYR A 56 5 4
HELIX 3 3 ASN A 61 ILE A 65 5 5
HELIX 4 4 ASP A 66 VAL A 70 5 5
HELIX 5 5 ASP A 120 GLY A 126 1 7
HELIX 6 6 ALA A 139 ASN A 152 1 14
HELIX 7 7 ARG A 169 ALA A 175 1 7
HELIX 8 8 THR A 176 ASN A 195 1 20
HELIX 9 9 GLU A 219 GLY A 243 1 25
HELIX 10 10 SER A 255 ASN A 261 1 7
HELIX 11 11 GLU A 263 VAL A 271 1 9
HELIX 12 12 ASP A 298 ALA A 304 1 7
HELIX 13 13 ASN A 313 GLY A 325 1 13
HELIX 14 14 PRO A 327 ALA A 329 5 3
HELIX 15 15 GLN A 347 GLN A 352 5 6
HELIX 16 16 PHE A 372 TYR A 379 1 8
HELIX 17 17 ASP A 411 GLY A 426 1 16
HELIX 18 18 GLU A 434 ASP A 438 5 5
HELIX 19 19 LYS A 441 LEU A 451 1 11
SHEET 1 A10 ILE A 116 LEU A 118 0
SHEET 2 A10 HIS A 72 ILE A 80 -1 N ASP A 79 O VAL A 117
SHEET 3 A10 LYS A 156 GLY A 162 1 O LYS A 156 N ILE A 73
SHEET 4 A10 GLY A 198 ASP A 202 1 O GLY A 198 N ILE A 159
SHEET 5 A10 LEU A 247 SER A 252 1 O LEU A 247 N VAL A 199
SHEET 6 A10 TRP A 273 ILE A 276 1 O TRP A 273 N ILE A 250
SHEET 7 A10 LEU A 331 PRO A 336 1 N VAL A 332 O ILE A 274
SHEET 8 A10 GLY A 429 TRP A 433 1 O GLY A 429 N LEU A 333
SHEET 9 A10 LYS A 45 PRO A 51 1 O LYS A 45 N ALA A 430
SHEET 10 A10 HIS A 72 ILE A 80 1 O HIS A 72 N GLY A 48
SHEET 1 B 2 ILE A 85 ASN A 88 0
SHEET 2 B 2 VAL A 97 THR A 100 -1 O VAL A 97 N ASN A 88
SHEET 1 C 7 GLY A 358 GLY A 359 0
SHEET 2 C 7 TYR A 338 ASP A 343 -1 N ASP A 343 O GLY A 358
SHEET 3 C 7 SER A 369 ASP A 371 -1 O PHE A 370 N GLY A 339
SHEET 4 C 7 TYR A 338 ASP A 343 -1 N GLY A 339 O PHE A 370
SHEET 5 C 7 PHE A 406 SER A 408 -1 O PHE A 406 N TRP A 342
SHEET 6 C 7 VAL A 395 ASN A 400 -1 N LEU A 398 O ILE A 407
SHEET 7 C 7 TYR A 385 ASN A 390 -1 N THR A 386 O TYR A 399
SSBOND 1 CYS A 81 CYS A 101 1555 1555 2.06
SSBOND 2 CYS A 345 CYS A 356 1555 1555 2.05
CISPEP 1 ALA A 76 PHE A 77 0 4.29
CISPEP 2 GLU A 204 TYR A 205 0 6.15
CISPEP 3 TRP A 433 GLU A 434 0 -2.14
SITE 1 AC1 8 GLY A 87 PRO A 89 ARG A 169 HOH A1034
SITE 2 AC1 8 HOH A1094 HOH A1270 HOH A1380 HOH A1561
SITE 1 AC2 9 TRP A 82 ASN A 113 THR A 179 ARG A 387
SITE 2 AC2 9 TRP A 389 GLU A 413 GOL A1011 HOH A1059
SITE 3 AC2 9 HOH A1748
SITE 1 AC3 10 THR A 128 ASP A 132 THR A 133 TRP A 134
SITE 2 AC3 10 THR A 176 ALA A 177 ASP A 391 LYS A 394
SITE 3 AC3 10 HOH A1052 HOH A1588
SITE 1 AC4 10 ASP A 343 GLY A 344 ASN A 403 LYS A 404
SITE 2 AC4 10 ARG A 405 SER A 424 LYS A 425 HOH A1133
SITE 3 AC4 10 HOH A1359 HOH A1761
SITE 1 AC5 9 ASN A 59 ASN A 61 ASP A 64 VAL A 207
SITE 2 AC5 9 PRO A 218 LYS A 221 HOH A1169 HOH A1191
SITE 3 AC5 9 HOH A1755
SITE 1 AC6 8 ASN A 83 ASN A 110 PRO A 112 ASN A 113
SITE 2 AC6 8 ASN A 381 HOH A1103 HOH A1195 HOH A1468
SITE 1 AC7 10 TYR A 49 PHE A 77 ASP A 202 GLU A 204
SITE 2 AC7 10 ALA A 251 MET A 277 TYR A 279 TRP A 433
SITE 3 AC7 10 HOH A1104 HOH A1230
SITE 1 AC8 10 LEU A 33 GLN A 34 PRO A 35 GLY A 253
SITE 2 AC8 10 ALA A 254 MET A 277 TYR A 279 ASP A 280
SITE 3 AC8 10 HOH A1759 HOH A1766
SITE 1 AC9 11 ILE A 138 ASN A 143 ASN A 146 LYS A 193
SITE 2 AC9 11 GLN A 347 HOH A1097 HOH A1198 HOH A1248
SITE 3 AC9 11 HOH A1309 HOH A1387 HOH A1465
SITE 1 BC1 8 ASN A 195 ASP A 242 GLN A 347 ALA A 348
SITE 2 BC1 8 GLY A 349 HOH A1069 HOH A1152 HOH A1537
SITE 1 BC2 12 TRP A 82 ASN A 83 ARG A 387 TYR A 388
SITE 2 BC2 12 TRP A 389 GOL A1002 HOH A1043 HOH A1411
SITE 3 BC2 12 HOH A1426 HOH A1742 HOH A1762 HOH A1767
CRYST1 43.007 46.839 55.700 109.29 95.45 116.68 P 1 1
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 0.023252 0.011684 0.007844 0.00000
SCALE2 0.000000 0.023894 0.011040 0.00000
SCALE3 0.000000 0.000000 0.019867 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
