HEADER TRANSFERASE 08-AUG-16 5GR3
TITLE CRYSTAL STRUCTURE OF BRANCHING ENZYME L541A/W655A MUTANT FROM
TITLE 2 CYANOTHECE SP. ATCC 51142
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 1,4-ALPHA-GLUCAN BRANCHING ENZYME GLGB;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 1,4-ALPHA-D-GLUCAN:1,4-ALPHA-D-GLUCAN 6-GLUCOSYL-
COMPND 5 TRANSFERASE,ALPHA-(1->4)-GLUCAN BRANCHING ENZYME,GLYCOGEN BRANCHING
COMPND 6 ENZYME;
COMPND 7 EC: 2.4.1.18;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CYANOTHECE SP. (STRAIN ATCC 51142);
SOURCE 3 ORGANISM_TAXID: 43989;
SOURCE 4 STRAIN: ATCC 51142;
SOURCE 5 ATCC: 51142;
SOURCE 6 GENE: GLGB, GLGB1, CCE_2248;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS BRANCHING ENZYME, GLYCOSIDE HYDROLASE FAMILY 13, CYANOBACTERIA,
KEYWDS 2 STARCH, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.SUZUKI,E.SUZUKI
REVDAT 2 08-NOV-23 5GR3 1 LINK
REVDAT 1 16-AUG-17 5GR3 0
JRNL AUTH M.HAYASHI,R.SUZUKI,C.COLLEONI,S.G.BALL,N.FUJITA,E.SUZUKI
JRNL TITL STRUCTURAL BASIS FOR SUBSTRATE BINDING AND CATALYSIS OF
JRNL TITL 2 BRANCHING ENZYME FROM CYANOTHECE SP. ATCC 51142
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.HAYASHI,R.SUZUKI,C.COLLEONI,S.G.BALL,N.FUJITA,E.SUZUKI
REMARK 1 TITL CRYSTALLIZATION AND CRYSTALLOGRAPHIC ANALYSIS OF BRANCHING
REMARK 1 TITL 2 ENZYMES FROM CYANOTHECE SP. ATCC 51142.
REMARK 1 REF ACTA CRYSTALLOGR F STRUCT V. 71 1109 2015
REMARK 1 REF 2 BIOL COMMUN
REMARK 1 REFN ESSN 2053-230X
REMARK 1 PMID 26249708
REMARK 1 DOI 10.1107/S2053230X1501198X
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 49627
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) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2669
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3591
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.1910
REMARK 3 BIN FREE R VALUE SET COUNT : 204
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6261
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 477
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.223
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.116
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.364
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6484 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 5774 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8821 ; 1.930 ; 1.922
REMARK 3 BOND ANGLES OTHERS (DEGREES): 13297 ; 0.895 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 754 ; 6.845 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 354 ;36.479 ;24.068
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1006 ;14.924 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;17.762 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 872 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7435 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1655 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3019 ; 2.544 ; 2.750
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3018 ; 2.542 ; 2.747
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3772 ; 3.904 ; 4.116
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 3773 ; 3.904 ; 4.119
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3465 ; 3.521 ; 3.063
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3465 ; 3.521 ; 3.063
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5050 ; 5.387 ; 4.466
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 7828 ; 6.882 ;22.574
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 7674 ; 6.844 ;22.474
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5GR3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1300000167.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2 - 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52373
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 14.80
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 15.00
REMARK 200 R MERGE FOR SHELL (I) : 0.37100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.000
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: 5GR2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.68
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MAGNESIUM CHLORIDE, ETHANOL, HEPES
REMARK 280 -NAOH, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 92.75950
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 66.80800
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 66.80800
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 46.37975
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 66.80800
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 66.80800
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 139.13925
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 66.80800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 66.80800
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 46.37975
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 66.80800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 66.80800
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 139.13925
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 92.75950
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 80 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 THR A 2
REMARK 465 THR A 3
REMARK 465 THR A 4
REMARK 465 GLU A 760
REMARK 465 GLY A 761
REMARK 465 THR A 762
REMARK 465 THR A 763
REMARK 465 ILE A 764
REMARK 465 LYS A 765
REMARK 465 GLU A 766
REMARK 465 ILE A 767
REMARK 465 ALA A 768
REMARK 465 ALA A 769
REMARK 465 ASP A 770
REMARK 465 GLU A 771
REMARK 465 GLU A 772
REMARK 465 GLU A 773
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 GLU A 58 CG GLU A 58 CD 0.095
REMARK 500 GLU A 58 CD GLU A 58 OE2 0.077
REMARK 500 GLU A 74 CD GLU A 74 OE2 0.110
REMARK 500 TRP A 285 CB TRP A 285 CG -0.117
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 ARG A 42 NE - CZ - NH1 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 111 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 242 NE - CZ - NH1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ARG A 442 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 501 CB - CG - OD1 ANGL. DEV. = 5.9 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 68 -17.64 58.11
REMARK 500 ALA A 148 60.72 -159.71
REMARK 500 THR A 176 -42.75 -145.31
REMARK 500 GLU A 184 -37.72 88.59
REMARK 500 HIS A 233 23.39 -142.02
REMARK 500 SER A 266 7.44 -69.87
REMARK 500 ASN A 274 56.85 35.37
REMARK 500 TRP A 327 -2.89 70.25
REMARK 500 LEU A 385 -66.24 -95.57
REMARK 500 SER A 496 46.78 -101.86
REMARK 500 SER A 562 158.98 70.48
REMARK 500 SER A 598 -25.10 97.80
REMARK 500 TYR A 644 -18.65 -145.80
REMARK 500 ILE A 656 -69.81 -101.15
REMARK 500 LEU A 722 57.71 31.17
REMARK 500 TRP A 730 94.16 -162.93
REMARK 500 THR A 756 64.01 -113.19
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 MG A 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 612 OD1
REMARK 620 2 HOH A 919 O 81.6
REMARK 620 3 HOH A1018 O 88.7 85.8
REMARK 620 4 HOH A1075 O 93.2 174.3 92.1
REMARK 620 5 HOH A1082 O 96.2 85.2 169.0 97.5
REMARK 620 6 HOH A1187 O 170.8 90.4 86.3 94.7 87.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 925 O
REMARK 620 2 HOH A1070 O 156.7
REMARK 620 3 HOH A1163 O 79.6 86.3
REMARK 620 4 HOH A1210 O 77.6 82.3 82.4
REMARK 620 5 HOH A1272 O 88.4 113.6 106.9 161.6
REMARK 620 6 HOH A1348 O 96.6 88.6 155.6 73.3 97.0
REMARK 620 N 1 2 3 4 5
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 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 803
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5GQU RELATED DB: PDB
REMARK 900 RELATED ID: 5GQV RELATED DB: PDB
REMARK 900 RELATED ID: 5GQW RELATED DB: PDB
REMARK 900 RELATED ID: 5GQX RELATED DB: PDB
REMARK 900 RELATED ID: 5GQY RELATED DB: PDB
REMARK 900 RELATED ID: 5GQZ RELATED DB: PDB
REMARK 900 RELATED ID: 5GR0 RELATED DB: PDB
REMARK 900 RELATED ID: 5GR1 RELATED DB: PDB
REMARK 900 RELATED ID: 5GR2 RELATED DB: PDB
REMARK 900 RELATED ID: 5GR4 RELATED DB: PDB
REMARK 900 RELATED ID: 5GR5 RELATED DB: PDB
REMARK 900 RELATED ID: 5GR6 RELATED DB: PDB
DBREF 5GR3 A 1 773 UNP B1WPM8 B1WPM8_CYAA5 1 773
SEQADV 5GR3 MET A -19 UNP B1WPM8 INITIATING METHIONINE
SEQADV 5GR3 GLY A -18 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 SER A -17 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 SER A -16 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 HIS A -15 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 HIS A -14 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 HIS A -13 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 HIS A -12 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 HIS A -11 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 HIS A -10 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 SER A -9 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 SER A -8 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 GLY A -7 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 LEU A -6 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 VAL A -5 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 PRO A -4 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 ARG A -3 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 GLY A -2 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 SER A -1 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 HIS A 0 UNP B1WPM8 EXPRESSION TAG
SEQADV 5GR3 ALA A 541 UNP B1WPM8 LEU 541 ENGINEERED MUTATION
SEQADV 5GR3 ALA A 655 UNP B1WPM8 TRP 655 ENGINEERED MUTATION
SEQRES 1 A 793 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 793 LEU VAL PRO ARG GLY SER HIS MET THR THR THR ILE SER
SEQRES 3 A 793 ALA ASP GLN VAL ASN GLN ILE ILE TYR ASN LEU HIS HIS
SEQRES 4 A 793 ASP PRO PHE GLU ILE LEU GLY CYS HIS LEU LEU GLU GLU
SEQRES 5 A 793 GLY LYS ASN THR LYS LYS TRP VAL VAL ARG ALA TYR LEU
SEQRES 6 A 793 PRO LYS ALA GLU ALA ALA TRP VAL ILE ARG PRO THR GLU
SEQRES 7 A 793 ARG LYS GLU ASP PRO MET ASN SER VAL HIS HIS PRO ASN
SEQRES 8 A 793 PHE PHE GLU CYS ILE ILE GLU THR PRO GLU LEU ASN HIS
SEQRES 9 A 793 TYR GLN LEU LYS VAL LYS GLU GLY GLU HIS GLU LYS VAL
SEQRES 10 A 793 ILE TYR ASP PRO TYR ALA PHE SER SER PRO TYR LEU THR
SEQRES 11 A 793 ASP GLU ASP ILE TYR LEU PHE SER GLU GLY ASN HIS HIS
SEQRES 12 A 793 ARG ILE TYR GLU LYS LEU GLY ALA HIS VAL GLY GLU ILE
SEQRES 13 A 793 ASN GLY VAL LYS GLY VAL TYR PHE ALA VAL TRP ALA PRO
SEQRES 14 A 793 ASN ALA ARG ASN VAL SER VAL ILE GLY ASP PHE ASN ASN
SEQRES 15 A 793 TRP ASP GLY ARG GLU HIS GLN MET ARG LYS ARG ASN TYR
SEQRES 16 A 793 THR ILE TRP GLU LEU PHE VAL PRO GLU ILE GLY SER GLY
SEQRES 17 A 793 THR VAL TYR LYS TYR GLU ILE LYS ASN SER GLU GLY HIS
SEQRES 18 A 793 ILE TYR GLU LYS SER ASP PRO TYR GLY PHE TYR ARG GLU
SEQRES 19 A 793 VAL ARG PRO ASN THR ALA SER ILE VAL VAL ASP ILE ASP
SEQRES 20 A 793 ASN ILE TYR GLN TRP HIS ASP GLU GLU TRP LEU GLU LYS
SEQRES 21 A 793 ARG ARG ASN SER ASP PRO LEU LYS GLN PRO VAL SER VAL
SEQRES 22 A 793 TYR GLU VAL HIS LEU GLY SER TRP LEU HIS GLY SER SER
SEQRES 23 A 793 ALA GLU LYS MET PRO LEU LEU ASN GLY GLU ALA ASP PRO
SEQRES 24 A 793 VAL ILE VAL SER GLU TRP ASN PRO GLY ALA ARG PHE LEU
SEQRES 25 A 793 SER TYR TYR GLU LEU ALA GLU LYS LEU ILE PRO TYR VAL
SEQRES 26 A 793 LYS ASP MET GLY TYR THR HIS ILE GLU LEU LEU PRO ILE
SEQRES 27 A 793 ALA GLU HIS PRO PHE ASP GLY SER TRP GLY TYR GLN VAL
SEQRES 28 A 793 THR GLY PHE TYR SER PRO THR SER ARG PHE GLY ARG PRO
SEQRES 29 A 793 GLU ASP PHE MET TYR PHE VAL ASP LYS CYS HIS GLU ASN
SEQRES 30 A 793 GLY ILE GLY VAL ILE LEU ASP TRP VAL PRO GLY HIS PHE
SEQRES 31 A 793 PRO LYS ASP SER HIS GLY LEU ALA TYR PHE ASP GLY THR
SEQRES 32 A 793 HIS LEU TYR GLU HIS ALA ASP PRO ARG ILE GLY GLU HIS
SEQRES 33 A 793 LYS GLU TRP GLY THR LEU VAL PHE ASN TYR GLY ARG HIS
SEQRES 34 A 793 GLU VAL ARG ASN PHE LEU VAL ALA ASN VAL LEU PHE TRP
SEQRES 35 A 793 PHE ASP LYS TYR HIS VAL ASP GLY ILE ARG VAL ASP ALA
SEQRES 36 A 793 VAL ALA SER MET LEU TYR ARG ASN TYR LEU ARG LYS GLU
SEQRES 37 A 793 GLY GLU TRP ILE ALA ASN GLU TYR GLY GLY ASP GLU HIS
SEQRES 38 A 793 ILE GLU ALA VAL SER PHE ILE ARG GLU VAL ASN THR LEU
SEQRES 39 A 793 LEU PHE GLU TYR PHE PRO GLY ILE LEU SER ILE ALA GLU
SEQRES 40 A 793 GLU SER THR GLU TRP GLU LYS VAL SER ARG PRO VAL TYR
SEQRES 41 A 793 ASP GLY GLY LEU GLY PHE ASN LEU LYS TRP ASP MET GLY
SEQRES 42 A 793 TRP MET HIS ASP MET LEU ASP TYR PHE ASN ILE ASP PRO
SEQRES 43 A 793 TYR PHE ARG GLN TYR HIS GLN ASN ASN VAL THR PHE SER
SEQRES 44 A 793 MET ALA TYR TYR TYR ASN GLU ASN PHE MET LEU ALA LEU
SEQRES 45 A 793 SER HIS ASP GLU ILE VAL HIS GLY LYS SER ASN MET LEU
SEQRES 46 A 793 GLY LYS MET PRO GLY ASP GLU TRP GLN LYS TYR ALA ASN
SEQRES 47 A 793 VAL ARG ALA LEU PHE THR TYR MET TYR THR HIS PRO GLY
SEQRES 48 A 793 LYS LYS THR MET PHE MET SER MET GLU PHE GLY GLN TRP
SEQRES 49 A 793 SER GLU TRP ASN VAL TRP GLY ASP LEU GLU TRP HIS LEU
SEQRES 50 A 793 LEU GLN TYR GLU PRO HIS GLN GLN LEU LYS GLN PHE PHE
SEQRES 51 A 793 THR ASP LEU ASN ALA LEU TYR GLN GLN GLU PRO ALA LEU
SEQRES 52 A 793 TYR THR HIS ASP PHE GLU TYR HIS GLY PHE GLU ALA ILE
SEQRES 53 A 793 ASP CYS ASN ASP ASN THR HIS SER VAL VAL SER PHE LEU
SEQRES 54 A 793 ARG ARG SER ASP ASP PRO ASN ASP SER LEU VAL VAL VAL
SEQRES 55 A 793 CYS ASN PHE THR PRO GLN PRO HIS SER HIS TYR ARG ILE
SEQRES 56 A 793 GLY VAL PRO GLU ALA GLY TYR TYR VAL GLU LEU PHE ASN
SEQRES 57 A 793 SER ASP ALA LYS GLN TYR GLY GLY SER ASN MET GLY ASN
SEQRES 58 A 793 LEU GLY GLY LYS TRP ALA ASP GLU TRP SER PHE HIS ASN
SEQRES 59 A 793 LYS PRO TYR SER LEU ASP LEU CYS LEU PRO PRO LEU ALA
SEQRES 60 A 793 VAL LEU ILE LEU LYS LEU ASP PRO THR LYS VAL PRO GLU
SEQRES 61 A 793 GLY THR THR ILE LYS GLU ILE ALA ALA ASP GLU GLU GLU
HET GOL A 801 6
HET MG A 802 1
HET MG A 803 1
HETNAM GOL GLYCEROL
HETNAM MG MAGNESIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL C3 H8 O3
FORMUL 3 MG 2(MG 2+)
FORMUL 5 HOH *477(H2 O)
HELIX 1 AA1 SER A 6 TYR A 15 1 10
HELIX 2 AA2 ASP A 20 ILE A 24 5 5
HELIX 3 AA3 THR A 110 GLU A 119 1 10
HELIX 4 AA4 ARG A 124 LYS A 128 5 5
HELIX 5 AA5 PHE A 160 ASN A 162 5 3
HELIX 6 AA6 ASP A 234 ASN A 243 1 10
HELIX 7 AA7 ASP A 245 GLN A 249 5 5
HELIX 8 AA8 SER A 293 GLY A 309 1 17
HELIX 9 AA9 PHE A 323 TRP A 327 5 5
HELIX 10 AB1 SER A 339 GLY A 342 5 4
HELIX 11 AB2 ARG A 343 ASN A 357 1 15
HELIX 12 AB3 ASP A 390 GLY A 394 1 5
HELIX 13 AB4 LYS A 397 TRP A 399 5 3
HELIX 14 AB5 ARG A 408 HIS A 427 1 20
HELIX 15 AB6 VAL A 436 TYR A 441 1 6
HELIX 16 AB7 HIS A 461 PHE A 479 1 19
HELIX 17 AB8 PRO A 498 GLY A 502 5 5
HELIX 18 AB9 ASP A 511 ILE A 524 1 14
HELIX 19 AC1 ASP A 525 THR A 537 5 13
HELIX 20 AC2 SER A 539 TYR A 544 1 6
HELIX 21 AC3 SER A 553 ILE A 557 5 5
HELIX 22 AC4 MET A 564 MET A 568 5 5
HELIX 23 AC5 ASP A 571 HIS A 589 1 19
HELIX 24 AC6 GLU A 614 GLN A 619 5 6
HELIX 25 AC7 TYR A 620 GLU A 640 1 21
HELIX 26 AC8 PRO A 641 TYR A 644 5 4
HELIX 27 AC9 GLU A 649 HIS A 651 5 3
HELIX 28 AD1 ASP A 674 SER A 678 5 5
HELIX 29 AD2 ALA A 711 GLY A 715 5 5
SHEET 1 AA1 4 GLY A 26 GLU A 32 0
SHEET 2 AA1 4 LYS A 37 TYR A 44 -1 O LYS A 38 N LEU A 30
SHEET 3 AA1 4 PHE A 72 GLU A 78 -1 O ILE A 77 N TRP A 39
SHEET 4 AA1 4 ASN A 65 SER A 66 -1 N ASN A 65 O GLU A 74
SHEET 1 AA2 4 LYS A 60 PRO A 63 0
SHEET 2 AA2 4 ALA A 50 ARG A 55 -1 N VAL A 53 O ASP A 62
SHEET 3 AA2 4 GLN A 86 GLU A 91 -1 O LYS A 90 N ALA A 50
SHEET 4 AA2 4 HIS A 94 ILE A 98 -1 O LYS A 96 N VAL A 89
SHEET 1 AA3 4 GLY A 130 ILE A 136 0
SHEET 2 AA3 4 VAL A 139 TRP A 147 -1 O ALA A 145 N GLY A 130
SHEET 3 AA3 4 ILE A 177 PRO A 183 -1 O LEU A 180 N PHE A 144
SHEET 4 AA3 4 ARG A 171 ARG A 173 -1 N ARG A 173 O ILE A 177
SHEET 1 AA4 3 ASN A 153 GLY A 158 0
SHEET 2 AA4 3 VAL A 190 LYS A 196 -1 O LYS A 192 N ILE A 157
SHEET 3 AA4 3 ILE A 202 LYS A 205 -1 O TYR A 203 N ILE A 195
SHEET 1 AA5 3 ASN A 153 GLY A 158 0
SHEET 2 AA5 3 VAL A 190 LYS A 196 -1 O LYS A 192 N ILE A 157
SHEET 3 AA5 3 SER A 221 ILE A 222 -1 O SER A 221 N TYR A 191
SHEET 1 AA6 9 SER A 252 VAL A 256 0
SHEET 2 AA6 9 HIS A 312 LEU A 315 1 O GLU A 314 N VAL A 256
SHEET 3 AA6 9 GLY A 360 ASP A 364 1 O ILE A 362 N LEU A 315
SHEET 4 AA6 9 GLY A 430 VAL A 433 1 O GLY A 430 N LEU A 363
SHEET 5 AA6 9 LEU A 483 ALA A 486 1 O ILE A 485 N ILE A 431
SHEET 6 AA6 9 LEU A 508 TRP A 510 1 O TRP A 510 N ALA A 486
SHEET 7 AA6 9 PHE A 548 LEU A 552 1 O MET A 549 N LYS A 509
SHEET 8 AA6 9 LYS A 592 PHE A 596 1 O LYS A 592 N LEU A 550
SHEET 9 AA6 9 SER A 252 VAL A 256 1 N GLU A 255 O MET A 595
SHEET 1 AA7 2 HIS A 263 SER A 265 0
SHEET 2 AA7 2 ALA A 289 PHE A 291 -1 O ARG A 290 N GLY A 264
SHEET 1 AA8 2 MET A 270 LEU A 272 0
SHEET 2 AA8 2 GLY A 275 ALA A 277 -1 O ALA A 277 N MET A 270
SHEET 1 AA9 2 ALA A 319 GLU A 320 0
SHEET 2 AA9 2 GLY A 333 PRO A 337 -1 O GLY A 333 N GLU A 320
SHEET 1 AB1 3 PHE A 370 PRO A 371 0
SHEET 2 AB1 3 THR A 401 LEU A 402 -1 O LEU A 402 N PHE A 370
SHEET 3 AB1 3 GLU A 395 HIS A 396 -1 N HIS A 396 O THR A 401
SHEET 1 AB2 6 PHE A 653 ASP A 657 0
SHEET 2 AB2 6 VAL A 665 ARG A 670 -1 O LEU A 669 N GLU A 654
SHEET 3 AB2 6 LEU A 679 ASN A 684 -1 O VAL A 681 N PHE A 668
SHEET 4 AB2 6 ALA A 747 ASP A 754 -1 O LEU A 751 N VAL A 680
SHEET 5 AB2 6 TYR A 702 ASN A 708 -1 N VAL A 704 O LYS A 752
SHEET 6 AB2 6 GLY A 724 TRP A 726 -1 O LYS A 725 N TYR A 703
SHEET 1 AB3 2 HIS A 690 VAL A 697 0
SHEET 2 AB3 2 TYR A 737 LEU A 743 -1 O LEU A 741 N TYR A 693
LINK OD1 ASP A 612 MG MG A 802 1555 1555 1.83
LINK MG MG A 802 O HOH A 919 1555 1555 2.01
LINK MG MG A 802 O HOH A1018 1555 1555 2.10
LINK MG MG A 802 O HOH A1075 1555 1555 2.02
LINK MG MG A 802 O HOH A1082 1555 1555 1.93
LINK MG MG A 802 O HOH A1187 1555 3545 1.93
LINK MG MG A 803 O HOH A 925 1555 1555 2.35
LINK MG MG A 803 O HOH A1070 1555 7556 2.31
LINK MG MG A 803 O HOH A1163 1555 1555 2.18
LINK MG MG A 803 O HOH A1210 1555 1555 2.18
LINK MG MG A 803 O HOH A1272 1555 1555 2.08
LINK MG MG A 803 O HOH A1348 1555 7556 2.27
CISPEP 1 ARG A 216 PRO A 217 0 5.90
SITE 1 AC1 8 GLU A 572 TRP A 573 TYR A 576 ARG A 580
SITE 2 AC1 8 PRO A 622 GLN A 625 TYR A 714 GLY A 715
SITE 1 AC2 6 ASP A 612 HOH A 919 HOH A1018 HOH A1075
SITE 2 AC2 6 HOH A1082 HOH A1187
SITE 1 AC3 6 HOH A 925 HOH A1070 HOH A1163 HOH A1210
SITE 2 AC3 6 HOH A1272 HOH A1348
CRYST1 133.616 133.616 185.519 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.007484 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007484 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005390 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
