HEADER HYDROLASE 05-OCT-00 1G01
TITLE ALKALINE CELLULASE K CATALYTIC DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENDOGLUCANASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALKALINE CELLULASE K CATALYTIC DOMAIN;
COMPND 5 EC: 3.2.1.4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP.;
SOURCE 3 ORGANISM_TAXID: 1415;
SOURCE 4 STRAIN: KSM-635;
SOURCE 5 EXPRESSION_SYSTEM: BACILLUS SUBTILIS;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 1423;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PHSP-BC115B
KEYWDS ALPHA/BETA BARREL, TIM BARREL, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.SHIRAI,H.ISHIDA,J.NODA,T.YAMANE,K.OZAKI,Y.HAKAMADA,S.ITO
REVDAT 6 13-MAR-24 1G01 1 REMARK SEQADV LINK
REVDAT 5 16-NOV-11 1G01 1 HETATM
REVDAT 4 13-JUL-11 1G01 1 VERSN
REVDAT 3 24-FEB-09 1G01 1 VERSN
REVDAT 2 31-DEC-02 1G01 1 REMARK
REVDAT 1 01-AUG-01 1G01 0
JRNL AUTH T.SHIRAI,H.ISHIDA,J.NODA,T.YAMANE,K.OZAKI,Y.HAKAMADA,S.ITO
JRNL TITL CRYSTAL STRUCTURE OF ALKALINE CELLULASE K: INSIGHT INTO THE
JRNL TITL 2 ALKALINE ADAPTATION OF AN INDUSTRIAL ENZYME.
JRNL REF J.MOL.BIOL. V. 310 1079 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11501997
JRNL DOI 10.1006/JMBI.2001.4835
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 8.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 48446
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2422
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 2791
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 465
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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) : NULL
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) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 2.400
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G01 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012063.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 RU300
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49176
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 8.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 11.70
REMARK 200 R MERGE (I) : 0.07700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.20200
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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CADMIUM SULFATE HYDRATE, SODIUM
REMARK 280 ACETATE, HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 81.33333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.66667
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.66667
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 81.33333
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CD CD A 593 LIES ON A SPECIAL POSITION.
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 GLY A 221
REMARK 465 ARG A 222
REMARK 465 LYS A 580
REMARK 465 PHE A 581
REMARK 465 THR A 582
REMARK 465 LYS A 583
REMARK 465 LEU A 584
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 HOH A 763 O HOH A 857 2.15
REMARK 500 O HOH A 865 O HOH A 867 2.18
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 HIS A 265 NE2 HIS A 265 CD2 -0.068
REMARK 500 HIS A 322 NE2 HIS A 322 CD2 -0.073
REMARK 500 HIS A 331 NE2 HIS A 331 CD2 -0.070
REMARK 500 HIS A 333 NE2 HIS A 333 CD2 -0.071
REMARK 500 HIS A 356 NE2 HIS A 356 CD2 -0.086
REMARK 500 HIS A 360 NE2 HIS A 360 CD2 -0.075
REMARK 500 HIS A 364 NE2 HIS A 364 CD2 -0.073
REMARK 500 HIS A 442 NE2 HIS A 442 CD2 -0.076
REMARK 500 HIS A 448 NE2 HIS A 448 CD2 -0.067
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 269 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 269 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP A 286 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 286 CE2 - CD2 - CG ANGL. DEV. = -5.6 DEGREES
REMARK 500 TRP A 330 CD1 - CG - CD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 TRP A 330 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 HIS A 356 CB - CG - CD2 ANGL. DEV. = -10.6 DEGREES
REMARK 500 TRP A 368 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 368 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 391 CD1 - CG - CD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 TRP A 391 CE2 - CD2 - CG ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 420 CD1 - CG - CD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 TRP A 420 CE2 - CD2 - CG ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 423 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 464 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 464 NE - CZ - NH2 ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 486 CD1 - CG - CD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 TRP A 486 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 505 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 505 CE2 - CD2 - CG ANGL. DEV. = -5.4 DEGREES
REMARK 500 TRP A 516 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 516 CE2 - CD2 - CG ANGL. DEV. = -5.7 DEGREES
REMARK 500 TRP A 519 CD1 - CG - CD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 519 CE2 - CD2 - CG ANGL. DEV. = -5.3 DEGREES
REMARK 500 TRP A 552 CD1 - CG - CD2 ANGL. DEV. = 6.4 DEGREES
REMARK 500 TRP A 552 CE2 - CD2 - CG ANGL. DEV. = -5.7 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 ASN A 284 -62.91 -91.89
REMARK 500 HIS A 333 -68.11 -159.65
REMARK 500 ALA A 371 96.21 -160.97
REMARK 500 ASP A 387 -171.71 -170.75
REMARK 500 ARG A 423 52.86 -117.81
REMARK 500 SER A 489 -165.63 -106.83
REMARK 500 LEU A 536 -56.17 -26.15
REMARK 500 ARG A 538 91.81 -172.63
REMARK 500 THR A 539 128.48 168.31
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 CD A 585 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 276 OE1
REMARK 620 2 GLU A 276 OE2 48.5
REMARK 620 3 GLU A 321 OE1 119.3 86.6
REMARK 620 4 GLU A 321 OE2 137.3 90.0 56.3
REMARK 620 5 GLU A 463 OE1 92.6 125.6 146.3 108.2
REMARK 620 6 GLU A 463 OE2 134.3 176.4 92.9 86.7 54.3
REMARK 620 7 HOH A 696 O 72.6 98.8 78.5 133.4 103.2 84.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 594 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 314 OE2
REMARK 620 2 HOH A 811 O 173.8
REMARK 620 3 HOH A 920 O 83.0 98.8
REMARK 620 4 HOH A1006 O 81.0 100.8 141.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 586 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 322 ND1
REMARK 620 2 ACY A 596 O 90.6
REMARK 620 3 ACY A 596 OXT 108.0 49.4
REMARK 620 4 ACY A 597 O 95.0 136.5 88.1
REMARK 620 5 ACY A 597 OXT 99.6 165.3 134.7 53.6
REMARK 620 6 HOH A 803 O 164.5 84.9 80.1 98.5 82.6
REMARK 620 7 HOH A 850 O 80.5 88.3 135.9 135.2 83.0 84.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 592 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 333 NE2
REMARK 620 2 ACY A 599 OXT 79.1
REMARK 620 3 ACY A 599 O 75.7 47.5
REMARK 620 4 HOH A1026 O 96.6 78.3 125.8
REMARK 620 5 HOH A1063 O 114.3 142.2 99.5 130.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 593 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 351 OE2
REMARK 620 2 GLU A 351 OE1 53.2
REMARK 620 3 GLU A 351 OE1 87.4 122.1
REMARK 620 4 GLU A 351 OE2 91.5 83.8 53.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 589 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 356 ND1
REMARK 620 2 HIS A 452 NE2 100.4
REMARK 620 3 HOH A 716 O 108.1 82.6
REMARK 620 4 HOH A 806 O 84.4 97.2 167.4
REMARK 620 5 HOH A1036 O 77.6 166.5 85.3 96.0
REMARK 620 6 HOH A1064 O 149.0 110.4 80.2 88.2 73.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 587 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 359 OD2
REMARK 620 2 ASP A 359 OD1 49.8
REMARK 620 3 GLU A 403 OE1 164.4 139.6
REMARK 620 4 GLU A 403 OE2 147.8 98.4 45.6
REMARK 620 5 HOH A 985 O 85.6 130.8 88.9 120.6
REMARK 620 6 HOH A1037 O 90.0 110.5 75.1 109.2 85.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 591 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 373 OE2
REMARK 620 2 GLU A 373 OE1 50.4
REMARK 620 3 GLU A 485 OE2 137.3 97.7
REMARK 620 4 HOH A 699 O 78.2 95.0 77.4
REMARK 620 5 HOH A 717 O 92.6 97.3 122.7 154.4
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 588 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 396 OE2
REMARK 620 2 ASP A 500 OD1 90.7
REMARK 620 3 ASP A 500 OD2 108.2 52.7
REMARK 620 4 GLU A 501 OE2 152.9 74.7 81.3
REMARK 620 5 GLU A 501 OE1 104.7 84.6 125.0 52.1
REMARK 620 6 ACY A 595 OXT 92.7 174.8 122.4 103.7 98.3
REMARK 620 7 ACY A 595 O 118.3 131.8 80.7 88.0 119.2 43.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CD A 590 CD
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 512 NE2
REMARK 620 2 ACY A 598 O 77.7
REMARK 620 3 ACY A 598 OXT 84.4 49.5
REMARK 620 4 HOH A 919 O 91.9 113.4 162.9
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 585
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 586
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 587
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 588
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 589
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 590
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 591
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 592
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 593
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 594
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 595
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 596
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 597
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 598
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 599
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G0C RELATED DB: PDB
REMARK 900 1G0C CONTAINS ALKALINE CELLULASE K CATALYTIC DOMAIN COMPLEXED WITH
REMARK 900 CELLOBIOSE.
DBREF 1G01 A 228 584 UNP P19424 GUN_BACS6 228 584
SEQADV 1G01 GLY A 221 UNP P19424 CLONING ARTIFACT
SEQADV 1G01 ARG A 222 UNP P19424 CLONING ARTIFACT
SEQADV 1G01 PRO A 223 UNP P19424 CLONING ARTIFACT
SEQADV 1G01 ALA A 224 UNP P19424 CLONING ARTIFACT
SEQADV 1G01 GLY A 225 UNP P19424 CLONING ARTIFACT
SEQADV 1G01 MET A 226 UNP P19424 CLONING ARTIFACT
SEQADV 1G01 GLN A 227 UNP P19424 CLONING ARTIFACT
SEQRES 1 A 364 GLY ARG PRO ALA GLY MET GLN ALA VAL LYS SER PRO SER
SEQRES 2 A 364 GLU ALA GLY ALA LEU GLN LEU VAL GLU LEU ASN GLY GLN
SEQRES 3 A 364 LEU THR LEU ALA GLY GLU ASP GLY THR PRO VAL GLN LEU
SEQRES 4 A 364 ARG GLY MET SER THR HIS GLY LEU GLN TRP PHE GLY GLU
SEQRES 5 A 364 ILE VAL ASN GLU ASN ALA PHE VAL ALA LEU SER ASN ASP
SEQRES 6 A 364 TRP GLY SER ASN MET ILE ARG LEU ALA MET TYR ILE GLY
SEQRES 7 A 364 GLU ASN GLY TYR ALA THR ASN PRO GLU VAL LYS ASP LEU
SEQRES 8 A 364 VAL TYR GLU GLY ILE GLU LEU ALA PHE GLU HIS ASP MET
SEQRES 9 A 364 TYR VAL ILE VAL ASP TRP HIS VAL HIS ALA PRO GLY ASP
SEQRES 10 A 364 PRO ARG ALA ASP VAL TYR SER GLY ALA TYR ASP PHE PHE
SEQRES 11 A 364 GLU GLU ILE ALA ASP HIS TYR LYS ASP HIS PRO LYS ASN
SEQRES 12 A 364 HIS TYR ILE ILE TRP GLU LEU ALA ASN GLU PRO SER PRO
SEQRES 13 A 364 ASN ASN ASN GLY GLY PRO GLY LEU THR ASN ASP GLU LYS
SEQRES 14 A 364 GLY TRP GLU ALA VAL LYS GLU TYR ALA GLU PRO ILE VAL
SEQRES 15 A 364 GLU MET LEU ARG GLU LYS GLY ASP ASN MET ILE LEU VAL
SEQRES 16 A 364 GLY ASN PRO ASN TRP SER GLN ARG PRO ASP LEU SER ALA
SEQRES 17 A 364 ASP ASN PRO ILE ASP ALA GLU ASN ILE MET TYR SER VAL
SEQRES 18 A 364 HIS PHE TYR THR GLY SER HIS GLY ALA SER HIS ILE GLY
SEQRES 19 A 364 TYR PRO GLU GLY THR PRO SER SER GLU ARG SER ASN VAL
SEQRES 20 A 364 MET ALA ASN VAL ARG TYR ALA LEU ASP ASN GLY VAL ALA
SEQRES 21 A 364 VAL PHE ALA THR GLU TRP GLY THR SER GLN ALA ASN GLY
SEQRES 22 A 364 ASP GLY GLY PRO TYR PHE ASP GLU ALA ASP VAL TRP LEU
SEQRES 23 A 364 ASN PHE LEU ASN LYS HIS ASN ILE SER TRP ALA ASN TRP
SEQRES 24 A 364 SER LEU THR ASN LYS ASN GLU ILE SER GLY ALA PHE THR
SEQRES 25 A 364 PRO PHE GLU LEU GLY ARG THR ASP ALA THR ASP LEU ASP
SEQRES 26 A 364 PRO GLY ALA ASN GLN VAL TRP ALA PRO GLU GLU LEU SER
SEQRES 27 A 364 LEU SER GLY GLU TYR VAL ARG ALA ARG ILE LYS GLY ILE
SEQRES 28 A 364 GLU TYR THR PRO ILE ASP ARG THR LYS PHE THR LYS LEU
HET CD A 585 1
HET CD A 586 1
HET CD A 587 1
HET CD A 588 1
HET CD A 589 1
HET CD A 590 1
HET CD A 591 1
HET CD A 592 1
HET CD A 593 1
HET CD A 594 1
HET ACY A 595 4
HET ACY A 596 4
HET ACY A 597 4
HET ACY A 598 4
HET ACY A 599 4
HETNAM CD CADMIUM ION
HETNAM ACY ACETIC ACID
FORMUL 2 CD 10(CD 2+)
FORMUL 12 ACY 5(C2 H4 O2)
FORMUL 17 HOH *465(H2 O)
HELIX 1 1 SER A 231 GLY A 236 1 6
HELIX 2 2 GLY A 266 GLY A 271 1 6
HELIX 3 3 GLU A 272 VAL A 274 5 3
HELIX 4 4 ASN A 275 ASN A 284 1 10
HELIX 5 5 GLU A 307 HIS A 322 1 16
HELIX 6 6 ALA A 340 SER A 344 5 5
HELIX 7 7 GLY A 345 LYS A 358 1 14
HELIX 8 8 LYS A 362 HIS A 364 5 3
HELIX 9 9 ASP A 387 GLY A 409 1 23
HELIX 10 10 ASN A 417 GLN A 422 1 6
HELIX 11 11 ARG A 423 ASN A 430 1 8
HELIX 12 12 PRO A 460 ARG A 464 5 5
HELIX 13 13 ASN A 466 ASN A 477 1 12
HELIX 14 14 TYR A 498 HIS A 512 1 15
HELIX 15 15 ALA A 553 GLU A 556 5 4
HELIX 16 16 SER A 558 GLY A 570 1 13
SHEET 1 A 2 GLN A 239 LEU A 243 0
SHEET 2 A 2 GLN A 246 ALA A 250 -1 O GLN A 246 N LEU A 243
SHEET 1 B 9 ARG A 260 THR A 264 0
SHEET 2 B 9 MET A 290 TYR A 296 1 N MET A 290 O ARG A 260
SHEET 3 B 9 TYR A 325 HIS A 331 1 O TYR A 325 N ILE A 291
SHEET 4 B 9 ILE A 366 GLU A 369 1 O ILE A 367 N VAL A 328
SHEET 5 B 9 ILE A 413 VAL A 415 1 N LEU A 414 O TRP A 368
SHEET 6 B 9 ILE A 437 TYR A 444 1 O MET A 438 N VAL A 415
SHEET 7 B 9 VAL A 481 GLY A 487 1 N PHE A 482 O TYR A 439
SHEET 8 B 9 TRP A 516 LEU A 521 1 N ALA A 517 O ALA A 483
SHEET 9 B 9 ARG A 260 THR A 264 1 O GLY A 261 N ASN A 518
LINK OE1 GLU A 276 CD CD A 585 5665 1555 2.78
LINK OE2 GLU A 276 CD CD A 585 5665 1555 2.41
LINK OE2 GLU A 314 CD CD A 594 1555 1555 2.45
LINK OE1 GLU A 321 CD CD A 585 5665 1555 2.43
LINK OE2 GLU A 321 CD CD A 585 5665 1555 2.25
LINK ND1 HIS A 322 CD CD A 586 1555 1555 2.94
LINK NE2 HIS A 333 CD CD A 592 1555 1555 2.98
LINK OE2 GLU A 351 CD CD A 593 1555 1555 2.27
LINK OE1 GLU A 351 CD CD A 593 1555 1555 2.50
LINK OE1 GLU A 351 CD CD A 593 4555 1555 2.43
LINK OE2 GLU A 351 CD CD A 593 4555 1555 2.36
LINK ND1 HIS A 356 CD CD A 589 1555 1555 2.67
LINK OD2 ASP A 359 CD CD A 587 4555 1555 2.44
LINK OD1 ASP A 359 CD CD A 587 4555 1555 2.67
LINK OE2 GLU A 373 CD CD A 591 1555 1555 2.76
LINK OE1 GLU A 373 CD CD A 591 1555 1555 2.24
LINK OE2 GLU A 396 CD CD A 588 1555 1555 2.25
LINK OE1 GLU A 403 CD CD A 587 1555 1555 2.69
LINK OE2 GLU A 403 CD CD A 587 1555 1555 2.86
LINK NE2 HIS A 452 CD CD A 589 5565 1555 2.96
LINK OE1 GLU A 463 CD CD A 585 1555 1555 2.31
LINK OE2 GLU A 463 CD CD A 585 1555 1555 2.42
LINK OE2 GLU A 485 CD CD A 591 1555 1555 2.22
LINK OD1 ASP A 500 CD CD A 588 2654 1555 2.56
LINK OD2 ASP A 500 CD CD A 588 2654 1555 2.31
LINK OE2 GLU A 501 CD CD A 588 2654 1555 2.64
LINK OE1 GLU A 501 CD CD A 588 2654 1555 2.28
LINK NE2 HIS A 512 CD CD A 590 1555 1555 3.10
LINK CD CD A 585 O HOH A 696 1555 5665 3.08
LINK CD CD A 586 O ACY A 596 1555 1555 2.66
LINK CD CD A 586 OXT ACY A 596 1555 1555 2.49
LINK CD CD A 586 O ACY A 597 1555 1555 2.43
LINK CD CD A 586 OXT ACY A 597 1555 1555 2.44
LINK CD CD A 586 O HOH A 803 1555 1555 2.53
LINK CD CD A 586 O HOH A 850 1555 1555 2.62
LINK CD CD A 587 O HOH A 985 1555 1555 2.84
LINK CD CD A 587 O HOH A1037 1555 1555 2.64
LINK CD CD A 588 OXT ACY A 595 1555 1555 2.43
LINK CD CD A 588 O ACY A 595 1555 1555 2.97
LINK CD CD A 589 O HOH A 716 1555 1555 2.67
LINK CD CD A 589 O HOH A 806 1555 5565 2.80
LINK CD CD A 589 O HOH A1036 1555 1555 2.94
LINK CD CD A 589 O HOH A1064 1555 1555 2.91
LINK CD CD A 590 O ACY A 598 1555 1555 2.67
LINK CD CD A 590 OXT ACY A 598 1555 1555 2.72
LINK CD CD A 590 O HOH A 919 1555 1555 2.32
LINK CD CD A 591 O HOH A 699 1555 1555 2.56
LINK CD CD A 591 O HOH A 717 1555 1555 2.45
LINK CD CD A 592 OXT ACY A 599 1555 1555 2.78
LINK CD CD A 592 O ACY A 599 1555 1555 2.66
LINK CD CD A 592 O HOH A1026 1555 1555 2.33
LINK CD CD A 592 O HOH A1063 1555 1555 2.60
LINK CD CD A 594 O HOH A 811 1555 1555 2.39
LINK CD CD A 594 O HOH A 920 1555 1555 2.02
LINK CD CD A 594 O HOH A1006 1555 5565 2.09
CISPEP 1 ALA A 334 PRO A 335 0 -0.48
CISPEP 2 GLY A 496 PRO A 497 0 2.20
CISPEP 3 TRP A 519 SER A 520 0 -0.09
SITE 1 AC1 4 GLU A 276 GLU A 321 GLU A 463 HOH A 696
SITE 1 AC2 5 HIS A 322 ACY A 596 ACY A 597 HOH A 803
SITE 2 AC2 5 HOH A 850
SITE 1 AC3 4 ASP A 359 GLU A 403 HOH A 985 HOH A1037
SITE 1 AC4 4 GLU A 396 ASP A 500 GLU A 501 ACY A 595
SITE 1 AC5 6 HIS A 356 HIS A 452 HOH A 716 HOH A 806
SITE 2 AC5 6 HOH A1036 HOH A1064
SITE 1 AC6 3 HIS A 512 ACY A 598 HOH A 919
SITE 1 AC7 5 GLU A 373 TYR A 444 GLU A 485 HOH A 699
SITE 2 AC7 5 HOH A 717
SITE 1 AC8 4 HIS A 333 ACY A 599 HOH A1026 HOH A1063
SITE 1 AC9 1 GLU A 351
SITE 1 BC1 4 GLU A 314 HOH A 811 HOH A 920 HOH A1006
SITE 1 BC2 9 ARG A 339 GLU A 396 PRO A 497 TYR A 498
SITE 2 BC2 9 ASP A 500 GLU A 501 CD A 588 HOH A 712
SITE 3 BC2 9 HOH A 867
SITE 1 BC3 6 VAL A 280 ASN A 284 CD A 586 ACY A 597
SITE 2 BC3 6 HOH A 917 HOH A 922
SITE 1 BC4 5 ASN A 284 GLU A 321 HIS A 322 CD A 586
SITE 2 BC4 5 ACY A 596
SITE 1 BC5 5 GLN A 246 ARG A 472 ASP A 476 HIS A 512
SITE 2 BC5 5 CD A 590
SITE 1 BC6 3 HIS A 333 CD A 592 HOH A 619
CRYST1 98.200 98.200 122.000 90.00 90.00 120.00 P 32 2 1 6
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 0.010183 0.005879 0.000000 0.00000
SCALE2 0.000000 0.011759 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008197 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
