HEADER HYDROLASE 18-MAR-99 1EGZ
TITLE CELLULASE CEL5 FROM ERWINIA CHRYSANTHEMI, A FAMILY GH 5-2 ENZYME
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE Z;
COMPND 3 CHAIN: A, B, C;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN;
COMPND 5 SYNONYM: EGZ, CEL5;
COMPND 6 EC: 3.2.1.4;
COMPND 7 OTHER_DETAILS: THREE COPIES IN THE ASYMMETRIC UNIT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ERWINIA CHRYSANTHEMI;
SOURCE 3 ORGANISM_TAXID: 556;
SOURCE 4 SECRETION: TYPE II;
SOURCE 5 CELLULAR_LOCATION: EXTERIOR;
SOURCE 6 OTHER_DETAILS: GENE: CELZ
KEYWDS GLYCOSYL HYDROLASE; CLAN GH-A; FAMILY 5-2; CELLULASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.CZJZEK,M.EL HASSOUNI,B.PY,F.BARRAS
REVDAT 4 09-AUG-23 1EGZ 1 REMARK LINK
REVDAT 3 24-FEB-09 1EGZ 1 VERSN
REVDAT 2 04-JAN-05 1EGZ 1 HEADER COMPND SOURCE JRNL
REVDAT 2 2 1 KEYWDS HELIX SHEET CRYST1
REVDAT 2 3 1 REMARK
REVDAT 1 26-MAR-99 1EGZ 0
JRNL AUTH M.CHAPON,M.CZJZEK,M.EL HASSOUNI,B.PY,M.JUY,F.BARRAS
JRNL TITL TYPE II PROTEIN SECRETION IN GRAM-NEGATIVE PATHOGENIC
JRNL TITL 2 BACTERIA: THE STUDY OF THE STRUCTURE/SECRETION RELATIONSHIPS
JRNL TITL 3 OF THE CELLULASE CEL5 (FORMERLY EGZ) FROM ERWINIA
JRNL TITL 4 CHRYSANTHEMI
JRNL REF J.MOL.BIOL. V. 310 1055 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11501995
JRNL DOI 10.1006/JMBI.2001.4787
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.500
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 100000.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0010
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 81.5
REMARK 3 NUMBER OF REFLECTIONS : 33555
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 SET) : 0.179
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1616
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 69.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3141
REMARK 3 BIN R VALUE (WORKING SET) : 0.2610
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 171
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6806
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 3
REMARK 3 SOLVENT ATOMS : 333
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.40
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : 29.0
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.650
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.00
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.130
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PARHCSDX.PRO
REMARK 3 PARAMETER FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 1 : TOPHCSDX.PRO
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EGZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000686.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-95
REMARK 200 TEMPERATURE (KELVIN) : 287
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE SINGLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38365
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.13400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.45000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1A3H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION HANGING DROP; PEG 4000
REMARK 280 28%, TRIS PH 8.0 20 MM, MGSO4 20 MM, VAPOR DIFFUSION, HANGING
REMARK 280 DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 84.40000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.60000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 84.40000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.60000
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
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP B 269 CB CG OD1 OD2
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 TRP A 254 C ALA A 255 N 0.279
REMARK 500 ALA A 255 N ALA A 255 CA -0.162
REMARK 500 ALA A 255 C LEU A 256 N 0.250
REMARK 500 ALA B 255 N ALA B 255 CA -0.206
REMARK 500 ALA B 255 CA ALA B 255 C 0.292
REMARK 500 ASN C 253 C TRP C 254 N 0.194
REMARK 500 TRP C 254 CA TRP C 254 CB -0.154
REMARK 500 TRP C 254 C ALA C 255 N 0.223
REMARK 500 ALA C 255 N ALA C 255 CA -0.121
REMARK 500 ALA C 255 C LEU C 256 N 0.312
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 TRP A 254 O - C - N ANGL. DEV. = -16.8 DEGREES
REMARK 500 ALA A 255 N - CA - CB ANGL. DEV. = -8.6 DEGREES
REMARK 500 LEU A 256 N - CA - CB ANGL. DEV. = -24.7 DEGREES
REMARK 500 ALA B 255 N - CA - C ANGL. DEV. = -23.2 DEGREES
REMARK 500 ALA B 255 CA - C - N ANGL. DEV. = -19.1 DEGREES
REMARK 500 TRP C 254 CA - C - N ANGL. DEV. = 18.0 DEGREES
REMARK 500 TRP C 254 O - C - N ANGL. DEV. = -14.3 DEGREES
REMARK 500 ALA C 255 CB - CA - C ANGL. DEV. = -12.6 DEGREES
REMARK 500 ALA C 255 N - CA - CB ANGL. DEV. = -12.0 DEGREES
REMARK 500 ALA C 255 CA - C - O ANGL. DEV. = 13.5 DEGREES
REMARK 500 ALA C 255 CA - C - N ANGL. DEV. = -22.1 DEGREES
REMARK 500 LEU C 256 N - CA - CB ANGL. DEV. = -14.9 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 HIS A 98 68.89 -68.74
REMARK 500 SER A 101 46.60 -153.92
REMARK 500 ASN A 132 -74.88 -44.72
REMARK 500 LEU A 135 -143.88 -98.94
REMARK 500 THR A 142 -58.08 -121.25
REMARK 500 SER A 169 77.40 49.85
REMARK 500 ASP A 180 63.29 -160.23
REMARK 500 ASN B 30 132.56 -33.39
REMARK 500 SER B 101 49.93 -155.58
REMARK 500 TYR B 131 85.40 -163.38
REMARK 500 ASN B 132 -72.15 -37.79
REMARK 500 LEU B 135 -146.83 -88.45
REMARK 500 THR B 142 -50.72 -138.74
REMARK 500 SER B 169 65.08 62.08
REMARK 500 SER B 171 60.32 61.12
REMARK 500 LYS B 185 -116.13 -50.28
REMARK 500 PRO B 268 134.24 -38.71
REMARK 500 VAL C 2 102.56 73.26
REMARK 500 ASN C 30 137.56 -22.39
REMARK 500 ASP C 90 65.23 60.72
REMARK 500 SER C 101 38.23 -156.52
REMARK 500 TYR C 131 95.28 -164.56
REMARK 500 ASN C 132 -75.51 -44.58
REMARK 500 LEU C 135 -158.53 -89.21
REMARK 500 ILE C 157 -53.46 -122.38
REMARK 500 ASP C 180 62.55 -158.79
REMARK 500 LYS C 185 -77.03 -60.68
REMARK 500 ASN C 186 77.75 -110.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LEU A 256 14.32
REMARK 500 LEU B 256 14.61
REMARK 500 LEU C 256 12.93
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 CA A 300 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 121 O
REMARK 620 2 ASP A 158 OD1 92.2
REMARK 620 3 ASP A 160 OD1 169.7 88.0
REMARK 620 4 ASN A 161 OD1 86.8 81.3 103.4
REMARK 620 5 HOH A1348 O 90.1 88.6 79.7 169.4
REMARK 620 6 HOH A1401 O 86.2 171.8 94.9 90.6 99.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 300 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 121 O
REMARK 620 2 ASP B 158 OD1 80.0
REMARK 620 3 ASP B 160 OD1 153.1 73.8
REMARK 620 4 ASN B 161 OD1 82.1 72.4 84.5
REMARK 620 5 HOH B2336 O 92.2 73.0 85.6 145.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 300 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY C 121 O
REMARK 620 2 ASP C 158 OD1 84.2
REMARK 620 3 ASP C 160 OD2 172.3 99.9
REMARK 620 4 ASP C 160 OD1 144.9 68.5 42.4
REMARK 620 5 ASN C 161 OD1 91.1 72.3 84.0 100.4
REMARK 620 6 HOH C3345 O 94.6 177.9 81.5 112.0 109.5
REMARK 620 7 HOH C3383 O 89.2 64.6 98.4 59.8 136.6 113.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CTA
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: GLU133 IS THE NUCLEOPHILE AND GLU220 THE
REMARK 800 ACID/BASE AT THE CATALYTIC SITE OF THIS GLYCOSYL HYDROLASE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTB
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: GLU133 IS THE NUCLEOPHILE AND GLU220 THE
REMARK 800 ACID/BASE AT THE CATALYTIC SITE OF THIS GLYCOSYL HYDROLASE
REMARK 800
REMARK 800 SITE_IDENTIFIER: CTC
REMARK 800 EVIDENCE_CODE: AUTHOR
REMARK 800 SITE_DESCRIPTION: GLU133 IS THE NUCLEOPHILE AND GLU220 THE
REMARK 800 ACID/BASE AT THE CATALYTIC SITE OF THIS GLYCOSYL HYDROLASE
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 300
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SECRETED (MATURE) PROTEIN,
REMARK 999 CONSISTING ONLY OF THE CATALYTIC DOMAIN
DBREF 1EGZ A 1 291 UNP P07103 GUNZ_ERWCH 44 335
DBREF 1EGZ B 1 291 UNP P07103 GUNZ_ERWCH 44 335
DBREF 1EGZ C 1 291 UNP P07103 GUNZ_ERWCH 44 335
SEQRES 1 A 291 SER VAL GLU PRO LEU SER VAL ASN GLY ASN LYS ILE TYR
SEQRES 2 A 291 ALA GLY GLU LYS ALA LYS SER PHE ALA GLY ASN SER LEU
SEQRES 3 A 291 PHE TRP SER ASN ASN GLY TRP GLY GLY GLU LYS PHE TYR
SEQRES 4 A 291 THR ALA ASP THR VAL ALA SER LEU LYS LYS ASP TRP LYS
SEQRES 5 A 291 SER SER ILE VAL ARG ALA ALA MET GLY VAL GLN GLU SER
SEQRES 6 A 291 GLY GLY TYR LEU GLN ASP PRO ALA GLY ASN LYS ALA LYS
SEQRES 7 A 291 VAL GLU ARG VAL VAL ASP ALA ALA ILE ALA ASN ASP MET
SEQRES 8 A 291 TYR ALA ILE ILE GLY TRP HIS SER HIS SER ALA GLU ASN
SEQRES 9 A 291 ASN ARG SER GLU ALA ILE ARG PHE PHE GLN GLU MET ALA
SEQRES 10 A 291 ARG LYS TYR GLY ASN LYS PRO ASN VAL ILE TYR GLU ILE
SEQRES 11 A 291 TYR ASN GLU PRO LEU GLN VAL SER TRP SER ASN THR ILE
SEQRES 12 A 291 LYS PRO TYR ALA GLU ALA VAL ILE SER ALA ILE ARG ALA
SEQRES 13 A 291 ILE ASP PRO ASP ASN LEU ILE ILE VAL GLY THR PRO SER
SEQRES 14 A 291 TRP SER GLN ASN VAL ASP GLU ALA SER ARG ASP PRO ILE
SEQRES 15 A 291 ASN ALA LYS ASN ILE ALA TYR THR LEU HIS PHE TYR ALA
SEQRES 16 A 291 GLY THR HIS GLY GLU SER LEU ARG ASN LYS ALA ARG GLN
SEQRES 17 A 291 ALA LEU ASN ASN GLY ILE ALA LEU PHE VAL THR GLU TRP
SEQRES 18 A 291 GLY THR VAL ASN ALA ASP GLY ASN GLY GLY VAL ASN GLN
SEQRES 19 A 291 THR GLU THR ASP ALA TRP VAL THR PHE MET ARG ASP ASN
SEQRES 20 A 291 ASN ILE SER ASN ALA ASN TRP ALA LEU ASN ASP LYS ASN
SEQRES 21 A 291 GLU GLY ALA SER THR TYR TYR PRO ASP SER LYS ASN LEU
SEQRES 22 A 291 THR GLU SER GLY LYS LYS VAL LYS SER ILE ILE GLN SER
SEQRES 23 A 291 TRP PRO TYR LYS ALA
SEQRES 1 B 291 SER VAL GLU PRO LEU SER VAL ASN GLY ASN LYS ILE TYR
SEQRES 2 B 291 ALA GLY GLU LYS ALA LYS SER PHE ALA GLY ASN SER LEU
SEQRES 3 B 291 PHE TRP SER ASN ASN GLY TRP GLY GLY GLU LYS PHE TYR
SEQRES 4 B 291 THR ALA ASP THR VAL ALA SER LEU LYS LYS ASP TRP LYS
SEQRES 5 B 291 SER SER ILE VAL ARG ALA ALA MET GLY VAL GLN GLU SER
SEQRES 6 B 291 GLY GLY TYR LEU GLN ASP PRO ALA GLY ASN LYS ALA LYS
SEQRES 7 B 291 VAL GLU ARG VAL VAL ASP ALA ALA ILE ALA ASN ASP MET
SEQRES 8 B 291 TYR ALA ILE ILE GLY TRP HIS SER HIS SER ALA GLU ASN
SEQRES 9 B 291 ASN ARG SER GLU ALA ILE ARG PHE PHE GLN GLU MET ALA
SEQRES 10 B 291 ARG LYS TYR GLY ASN LYS PRO ASN VAL ILE TYR GLU ILE
SEQRES 11 B 291 TYR ASN GLU PRO LEU GLN VAL SER TRP SER ASN THR ILE
SEQRES 12 B 291 LYS PRO TYR ALA GLU ALA VAL ILE SER ALA ILE ARG ALA
SEQRES 13 B 291 ILE ASP PRO ASP ASN LEU ILE ILE VAL GLY THR PRO SER
SEQRES 14 B 291 TRP SER GLN ASN VAL ASP GLU ALA SER ARG ASP PRO ILE
SEQRES 15 B 291 ASN ALA LYS ASN ILE ALA TYR THR LEU HIS PHE TYR ALA
SEQRES 16 B 291 GLY THR HIS GLY GLU SER LEU ARG ASN LYS ALA ARG GLN
SEQRES 17 B 291 ALA LEU ASN ASN GLY ILE ALA LEU PHE VAL THR GLU TRP
SEQRES 18 B 291 GLY THR VAL ASN ALA ASP GLY ASN GLY GLY VAL ASN GLN
SEQRES 19 B 291 THR GLU THR ASP ALA TRP VAL THR PHE MET ARG ASP ASN
SEQRES 20 B 291 ASN ILE SER ASN ALA ASN TRP ALA LEU ASN ASP LYS ASN
SEQRES 21 B 291 GLU GLY ALA SER THR TYR TYR PRO ASP SER LYS ASN LEU
SEQRES 22 B 291 THR GLU SER GLY LYS LYS VAL LYS SER ILE ILE GLN SER
SEQRES 23 B 291 TRP PRO TYR LYS ALA
SEQRES 1 C 291 SER VAL GLU PRO LEU SER VAL ASN GLY ASN LYS ILE TYR
SEQRES 2 C 291 ALA GLY GLU LYS ALA LYS SER PHE ALA GLY ASN SER LEU
SEQRES 3 C 291 PHE TRP SER ASN ASN GLY TRP GLY GLY GLU LYS PHE TYR
SEQRES 4 C 291 THR ALA ASP THR VAL ALA SER LEU LYS LYS ASP TRP LYS
SEQRES 5 C 291 SER SER ILE VAL ARG ALA ALA MET GLY VAL GLN GLU SER
SEQRES 6 C 291 GLY GLY TYR LEU GLN ASP PRO ALA GLY ASN LYS ALA LYS
SEQRES 7 C 291 VAL GLU ARG VAL VAL ASP ALA ALA ILE ALA ASN ASP MET
SEQRES 8 C 291 TYR ALA ILE ILE GLY TRP HIS SER HIS SER ALA GLU ASN
SEQRES 9 C 291 ASN ARG SER GLU ALA ILE ARG PHE PHE GLN GLU MET ALA
SEQRES 10 C 291 ARG LYS TYR GLY ASN LYS PRO ASN VAL ILE TYR GLU ILE
SEQRES 11 C 291 TYR ASN GLU PRO LEU GLN VAL SER TRP SER ASN THR ILE
SEQRES 12 C 291 LYS PRO TYR ALA GLU ALA VAL ILE SER ALA ILE ARG ALA
SEQRES 13 C 291 ILE ASP PRO ASP ASN LEU ILE ILE VAL GLY THR PRO SER
SEQRES 14 C 291 TRP SER GLN ASN VAL ASP GLU ALA SER ARG ASP PRO ILE
SEQRES 15 C 291 ASN ALA LYS ASN ILE ALA TYR THR LEU HIS PHE TYR ALA
SEQRES 16 C 291 GLY THR HIS GLY GLU SER LEU ARG ASN LYS ALA ARG GLN
SEQRES 17 C 291 ALA LEU ASN ASN GLY ILE ALA LEU PHE VAL THR GLU TRP
SEQRES 18 C 291 GLY THR VAL ASN ALA ASP GLY ASN GLY GLY VAL ASN GLN
SEQRES 19 C 291 THR GLU THR ASP ALA TRP VAL THR PHE MET ARG ASP ASN
SEQRES 20 C 291 ASN ILE SER ASN ALA ASN TRP ALA LEU ASN ASP LYS ASN
SEQRES 21 C 291 GLU GLY ALA SER THR TYR TYR PRO ASP SER LYS ASN LEU
SEQRES 22 C 291 THR GLU SER GLY LYS LYS VAL LYS SER ILE ILE GLN SER
SEQRES 23 C 291 TRP PRO TYR LYS ALA
HET CA A 300 1
HET CA B 300 1
HET CA C 300 1
HETNAM CA CALCIUM ION
FORMUL 4 CA 3(CA 2+)
FORMUL 7 HOH *333(H2 O)
HELIX 1 1 GLY A 35 PHE A 38 5 4
HELIX 2 2 ALA A 41 LYS A 49 1 9
HELIX 3 3 PRO A 72 ALA A 88 1 17
HELIX 4 4 ALA A 102 TYR A 120 5 19
HELIX 5 5 ILE A 143 ILE A 157 1 15
HELIX 6 6 PRO A 168 SER A 171 1 4
HELIX 7 7 VAL A 174 ASP A 180 1 7
HELIX 8 8 GLU A 200 ASN A 211 1 12
HELIX 9 9 GLN A 234 ASP A 246 1 13
HELIX 10 10 GLU A 275 SER A 286 1 12
HELIX 11 11 GLY B 35 PHE B 38 5 4
HELIX 12 12 ALA B 41 LYS B 49 1 9
HELIX 13 13 PRO B 72 ALA B 88 1 17
HELIX 14 14 ALA B 102 ASN B 104 5 3
HELIX 15 15 ARG B 106 TYR B 120 1 15
HELIX 16 16 ILE B 143 ILE B 157 1 15
HELIX 17 17 PRO B 168 SER B 171 1 4
HELIX 18 18 VAL B 174 ARG B 179 1 6
HELIX 19 19 GLU B 200 ASN B 212 1 13
HELIX 20 20 GLN B 234 ASP B 246 1 13
HELIX 21 21 GLU B 275 GLN B 285 1 11
HELIX 22 22 GLY C 35 PHE C 38 5 4
HELIX 23 23 ALA C 41 LYS C 49 1 9
HELIX 24 24 PRO C 72 ALA C 88 1 17
HELIX 25 25 ALA C 102 TYR C 120 5 19
HELIX 26 26 ILE C 143 ARG C 155 1 13
HELIX 27 27 PRO C 168 SER C 171 1 4
HELIX 28 28 VAL C 174 ASP C 180 1 7
HELIX 29 29 GLU C 200 ASN C 211 1 12
HELIX 30 30 GLN C 234 ASP C 246 1 13
HELIX 31 31 GLU C 275 GLN C 285 1 11
SHEET 1 A 2 LEU A 5 ASN A 8 0
SHEET 2 A 2 LYS A 11 ALA A 14 -1 N TYR A 13 O SER A 6
SHEET 1 B 5 ASN A 251 ASN A 253 0
SHEET 2 B 5 ALA A 22 SER A 25 1 N GLY A 23 O ASN A 251
SHEET 3 B 5 ILE A 55 GLY A 61 1 N ILE A 55 O ASN A 24
SHEET 4 B 5 TYR A 92 HIS A 98 1 N TYR A 92 O VAL A 56
SHEET 5 B 5 VAL A 126 GLU A 129 1 N ILE A 127 O ALA A 93
SHEET 1 C 2 ILE A 163 VAL A 165 0
SHEET 2 C 2 ILE A 187 TYR A 189 1 N ALA A 188 O ILE A 163
SHEET 1 D 2 HIS A 192 TYR A 194 0
SHEET 2 D 2 GLU A 220 GLY A 222 1 N GLU A 220 O PHE A 193
SHEET 1 E 2 LEU B 5 ASN B 8 0
SHEET 2 E 2 LYS B 11 ALA B 14 -1 N TYR B 13 O SER B 6
SHEET 1 F 5 ASN B 251 ASN B 253 0
SHEET 2 F 5 ALA B 22 SER B 25 1 N GLY B 23 O ASN B 251
SHEET 3 F 5 ILE B 55 GLY B 61 1 N ILE B 55 O ASN B 24
SHEET 4 F 5 TYR B 92 HIS B 98 1 N TYR B 92 O VAL B 56
SHEET 5 F 5 VAL B 126 GLU B 129 1 N ILE B 127 O ALA B 93
SHEET 1 G 2 ILE B 163 VAL B 165 0
SHEET 2 G 2 ILE B 187 TYR B 189 1 N ALA B 188 O ILE B 163
SHEET 1 H 2 HIS B 192 TYR B 194 0
SHEET 2 H 2 GLU B 220 GLY B 222 1 N GLU B 220 O PHE B 193
SHEET 1 I 2 LEU C 5 ASN C 8 0
SHEET 2 I 2 LYS C 11 ALA C 14 -1 N TYR C 13 O SER C 6
SHEET 1 J 5 ASN C 251 ASN C 253 0
SHEET 2 J 5 ALA C 22 SER C 25 1 N GLY C 23 O ASN C 251
SHEET 3 J 5 ILE C 55 GLY C 61 1 N ILE C 55 O ASN C 24
SHEET 4 J 5 TYR C 92 HIS C 98 1 N TYR C 92 O VAL C 56
SHEET 5 J 5 VAL C 126 GLU C 129 1 N ILE C 127 O ALA C 93
SHEET 1 K 2 ILE C 163 VAL C 165 0
SHEET 2 K 2 ILE C 187 TYR C 189 1 N ALA C 188 O ILE C 163
SHEET 1 L 2 HIS C 192 TYR C 194 0
SHEET 2 L 2 GLU C 220 GLY C 222 1 N GLU C 220 O PHE C 193
LINK O GLY A 121 CA CA A 300 1555 1555 2.14
LINK OD1 ASP A 158 CA CA A 300 1555 1555 2.11
LINK OD1 ASP A 160 CA CA A 300 1555 1555 2.71
LINK OD1 ASN A 161 CA CA A 300 1555 1555 2.21
LINK CA CA A 300 O HOH A1348 1555 1555 2.14
LINK CA CA A 300 O HOH A1401 1555 1555 2.78
LINK O GLY B 121 CA CA B 300 1555 1555 2.19
LINK OD1 ASP B 158 CA CA B 300 1555 1555 2.65
LINK OD1 ASP B 160 CA CA B 300 1555 1555 2.41
LINK OD1 ASN B 161 CA CA B 300 1555 1555 2.41
LINK CA CA B 300 O HOH B2336 1555 1555 2.27
LINK O GLY C 121 CA CA C 300 1555 1555 2.26
LINK OD1 ASP C 158 CA CA C 300 1555 1555 2.75
LINK OD2 ASP C 160 CA CA C 300 1555 1555 3.00
LINK OD1 ASP C 160 CA CA C 300 1555 1555 3.09
LINK OD1 ASN C 161 CA CA C 300 1555 1555 2.29
LINK CA CA C 300 O HOH C3345 1555 1555 2.35
LINK CA CA C 300 O HOH C3383 1555 1555 2.29
CISPEP 1 TRP A 254 ALA A 255 0 3.78
CISPEP 2 TRP C 254 ALA C 255 0 -26.03
SITE 1 CTA 2 GLU A 133 GLU A 220
SITE 1 CTB 2 GLU B 133 GLU B 220
SITE 1 CTC 2 GLU C 133 GLU C 220
SITE 1 AC1 6 GLY A 121 ASP A 158 ASP A 160 ASN A 161
SITE 2 AC1 6 HOH A1348 HOH A1401
SITE 1 AC2 5 GLY B 121 ASP B 158 ASP B 160 ASN B 161
SITE 2 AC2 5 HOH B2336
SITE 1 AC3 6 GLY C 121 ASP C 158 ASP C 160 ASN C 161
SITE 2 AC3 6 HOH C3345 HOH C3383
CRYST1 168.800 47.200 120.100 90.00 105.00 90.00 C 1 2 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005924 0.000000 0.001587 0.00000
SCALE2 0.000000 0.021186 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008620 0.00000
MTRIX1 1 -0.131870 -0.032280 0.990740 -111.24346 1
MTRIX2 1 0.436860 0.895280 0.087320 -29.71191 1
MTRIX3 1 -0.889810 0.444330 -0.103960 25.89464 1
MTRIX1 2 -0.857940 -0.512970 -0.028150 37.33757 1
MTRIX2 2 0.513640 -0.855390 -0.066950 33.30179 1
MTRIX3 2 0.010270 -0.071900 0.997360 -40.37063 1
(ATOM LINES ARE NOT SHOWN.)
END
