HEADER OXIDOREDUCTASE 14-AUG-00 1FLG
TITLE CRYSTAL STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE FROM
TITLE 2 PSEUDOMONAS AERUGINOSA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (QUINOPROTEIN ETHANOL DEHYDROGENASE);
COMPND 3 CHAIN: A, B
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287
KEYWDS QUINOPROTEIN, SUPERBARREL, DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KEITEL,A.DIEHL,T.KNAUTE,J.J.STEZOWSKI,W.HOHNE,H.GORISCH
REVDAT 3 04-OCT-17 1FLG 1 REMARK
REVDAT 2 24-FEB-09 1FLG 1 VERSN
REVDAT 1 30-AUG-00 1FLG 0
SPRSDE 30-AUG-00 1FLG 1EEE
JRNL AUTH T.KEITEL,A.DIEHL,T.KNAUTE,J.J.STEZOWSKI,W.HOHNE,H.GORISCH
JRNL TITL X-RAY STRUCTURE OF THE QUINOPROTEIN ETHANOL DEHYDROGENASE
JRNL TITL 2 FROM PSEUDOMONAS AERUGINOSA: BASIS OF SUBSTRATE SPECIFICITY.
JRNL REF J.MOL.BIOL. V. 297 961 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10736230
JRNL DOI 10.1006/JMBI.2000.3603
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 28304
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 + TEST SET) : 0.142
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1476
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9074
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 52
REMARK 3 SOLVENT ATOMS : 106
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 28.20
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 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 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : 0.013 ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD
REMARK 4
REMARK 4 1FLG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011688.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-89
REMARK 200 TEMPERATURE (KELVIN) : 293.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X31
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM, ROTAVATA
REMARK 200 DATA SCALING SOFTWARE : CCP4 (AGROVATA, ROTAVATA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.520
REMARK 200 RESOLUTION RANGE LOW (A) : 25.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
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) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.33000
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 (%): 50.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG1500, 50 MM CALCIUM CHLORIDE,
REMARK 280 4.5 MM GLYCINE/NAOH PH 8, PH 8.00, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 79.70000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 46.01482
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 43.65000
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 79.70000
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 46.01482
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 43.65000
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 79.70000
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 46.01482
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 43.65000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 92.02963
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 87.30000
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 92.02963
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 87.30000
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 92.02963
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 87.30000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 38710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 ASN A 133 O THR A 136 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CD2 HIS A 373 NH2 ARG A 456 2665 1.57
REMARK 500 OG SER A 372 NH2 ARG A 456 2665 1.92
REMARK 500 OG SER A 372 NH1 ARG A 456 2665 2.04
REMARK 500 CG HIS A 373 NH2 ARG A 456 2665 2.08
REMARK 500 CD2 HIS A 373 CZ ARG A 456 2665 2.13
REMARK 500 OG SER A 372 CZ ARG A 456 2665 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 SER A 299 CB SER A 299 OG -0.084
REMARK 500 ASN A 312 N ASN A 312 CA 0.122
REMARK 500 ASN A 367 N ASN A 367 CA 0.234
REMARK 500 GLY A 386 N GLY A 386 CA 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 ASP A 2 O - C - N ANGL. DEV. = -10.8 DEGREES
REMARK 500 GLU A 6 OE1 - CD - OE2 ANGL. DEV. = -8.9 DEGREES
REMARK 500 ASP A 12 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 THR A 14 CA - C - N ANGL. DEV. = 14.4 DEGREES
REMARK 500 THR A 14 O - C - N ANGL. DEV. = -17.4 DEGREES
REMARK 500 ASP A 17 CB - CG - OD1 ANGL. DEV. = 9.4 DEGREES
REMARK 500 TYR A 21 CG - CD2 - CE2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 TYR A 21 OH - CZ - CE2 ANGL. DEV. = 16.3 DEGREES
REMARK 500 HIS A 26 CB - CG - CD2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 ALA A 27 N - CA - CB ANGL. DEV. = -9.2 DEGREES
REMARK 500 ARG A 29 CD - NE - CZ ANGL. DEV. = 38.0 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 ARG A 29 NE - CZ - NH2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 LYS A 34 CA - CB - CG ANGL. DEV. = 18.3 DEGREES
REMARK 500 LEU A 44 CB - CA - C ANGL. DEV. = 11.7 DEGREES
REMARK 500 SER A 49 N - CA - CB ANGL. DEV. = -11.1 DEGREES
REMARK 500 PHE A 52 CB - CG - CD2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 ASP A 54 CB - CG - OD2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 LYS A 56 CA - CB - CG ANGL. DEV. = 19.3 DEGREES
REMARK 500 GLU A 61 OE1 - CD - OE2 ANGL. DEV. = -15.8 DEGREES
REMARK 500 SER A 67 N - CA - CB ANGL. DEV. = -9.8 DEGREES
REMARK 500 GLY A 69 C - N - CA ANGL. DEV. = -23.6 DEGREES
REMARK 500 TYR A 72 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 TYR A 72 CG - CD1 - CE1 ANGL. DEV. = 7.2 DEGREES
REMARK 500 TYR A 72 CD1 - CE1 - CZ ANGL. DEV. = -5.5 DEGREES
REMARK 500 VAL A 73 CB - CA - C ANGL. DEV. = -13.6 DEGREES
REMARK 500 VAL A 73 O - C - N ANGL. DEV. = -9.7 DEGREES
REMARK 500 TYR A 77 CB - CG - CD2 ANGL. DEV. = -8.6 DEGREES
REMARK 500 TYR A 77 CB - CG - CD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ARG A 79 CD - NE - CZ ANGL. DEV. = 12.9 DEGREES
REMARK 500 ARG A 79 NH1 - CZ - NH2 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 79 NE - CZ - NH2 ANGL. DEV. = 8.2 DEGREES
REMARK 500 PHE A 81 CB - CG - CD2 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ALA A 82 CA - C - O ANGL. DEV. = 13.8 DEGREES
REMARK 500 ALA A 82 O - C - N ANGL. DEV. = -9.6 DEGREES
REMARK 500 THR A 87 N - CA - CB ANGL. DEV. = -17.1 DEGREES
REMARK 500 THR A 87 CA - C - O ANGL. DEV. = -13.7 DEGREES
REMARK 500 THR A 87 CA - C - N ANGL. DEV. = 25.9 DEGREES
REMARK 500 THR A 87 O - C - N ANGL. DEV. = -11.8 DEGREES
REMARK 500 GLY A 88 C - N - CA ANGL. DEV. = -13.6 DEGREES
REMARK 500 GLY A 88 O - C - N ANGL. DEV. = -11.3 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP A 100 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 101 OD1 - CG - OD2 ANGL. DEV. = 14.7 DEGREES
REMARK 500 ASP A 101 CB - CG - OD1 ANGL. DEV. = -8.2 DEGREES
REMARK 500 ASP A 101 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ARG A 103 CD - NE - CZ ANGL. DEV. = 20.2 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 103 NE - CZ - NH2 ANGL. DEV. = -8.3 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 308 ANGLE DEVIATIONS.
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 VAL A 3 93.08 71.80
REMARK 500 TRP A 48 157.38 176.28
REMARK 500 GLN A 57 -107.95 -116.21
REMARK 500 ARG A 58 -172.86 59.92
REMARK 500 ASP A 68 -135.53 42.58
REMARK 500 SER A 78 75.48 52.66
REMARK 500 ASP A 107 158.01 97.79
REMARK 500 ALA A 127 73.71 43.29
REMARK 500 THR A 136 -168.55 -122.31
REMARK 500 THR A 155 -33.94 -133.55
REMARK 500 SER A 215 -100.52 -114.95
REMARK 500 ASN A 231 -9.89 92.86
REMARK 500 GLN A 249 -135.68 -106.72
REMARK 500 ALA A 330 -116.09 -17.40
REMARK 500 LYS A 331 -56.89 -125.96
REMARK 500 GLU A 385 -88.19 -46.10
REMARK 500 PRO A 394 119.78 -35.58
REMARK 500 HIS A 398 143.67 -171.59
REMARK 500 ASN A 413 -136.75 -89.07
REMARK 500 ASN A 415 102.16 -49.21
REMARK 500 TRP A 433 -174.34 -170.73
REMARK 500 LYS A 434 -176.14 -170.68
REMARK 500 LEU A 451 -60.22 -93.23
REMARK 500 PRO A 487 154.71 -49.92
REMARK 500 TRP A 489 23.56 -153.86
REMARK 500 VAL B 3 92.70 54.75
REMARK 500 LYS B 34 13.62 -142.09
REMARK 500 TRP B 48 160.77 176.77
REMARK 500 GLN B 57 -119.37 -117.81
REMARK 500 ARG B 58 175.26 71.33
REMARK 500 PRO B 99 170.64 -51.43
REMARK 500 ASP B 107 157.22 105.99
REMARK 500 LYS B 165 -61.62 -94.35
REMARK 500 ASN B 211 46.24 30.51
REMARK 500 ASP B 214 157.76 -44.27
REMARK 500 SER B 215 -93.57 -130.10
REMARK 500 VAL B 217 129.78 111.91
REMARK 500 GLN B 249 -144.40 -113.44
REMARK 500 PRO B 269 169.48 -45.31
REMARK 500 HIS B 283 115.00 -164.80
REMARK 500 TYR B 289 25.99 4.40
REMARK 500 ASP B 313 97.99 -55.73
REMARK 500 PHE B 317 49.93 -95.86
REMARK 500 SER B 318 112.09 -32.40
REMARK 500 ALA B 330 -85.26 -2.68
REMARK 500 LYS B 331 -3.36 -173.07
REMARK 500 ASP B 332 93.27 172.88
REMARK 500 ASN B 345 27.76 -79.96
REMARK 500 ASN B 355 9.17 -155.85
REMARK 500 ASP B 366 -118.50 -44.54
REMARK 500
REMARK 500 THIS ENTRY HAS 62 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 268 PRO A 269 -35.12
REMARK 500 ASP A 284 TYR A 285 143.89
REMARK 500 LEU A 288 TYR A 289 35.07
REMARK 500 GLY B 268 PRO B 269 -63.81
REMARK 500 ASP B 284 TYR B 285 136.30
REMARK 500 LEU B 288 TYR B 289 -106.97
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 GLU A 6 -10.77
REMARK 500 ASP A 11 -10.76
REMARK 500 LYS A 13 19.15
REMARK 500 THR A 14 -12.40
REMARK 500 ARG A 58 10.20
REMARK 500 GLY A 69 16.02
REMARK 500 ASN A 95 -17.28
REMARK 500 VAL A 120 -17.46
REMARK 500 LYS A 142 11.29
REMARK 500 ALA A 157 -16.51
REMARK 500 PRO A 158 -12.99
REMARK 500 GLY A 177 -11.55
REMARK 500 LEU A 210 11.70
REMARK 500 ASP A 220 -10.26
REMARK 500 THR A 234 13.43
REMARK 500 TRP A 248 11.12
REMARK 500 ALA A 251 -11.47
REMARK 500 GLY A 268 -19.49
REMARK 500 ASP A 284 -18.41
REMARK 500 ASP A 316 -12.94
REMARK 500 TYR A 328 12.24
REMARK 500 LYS A 331 -12.82
REMARK 500 ALA A 338 -12.16
REMARK 500 PHE A 347 13.66
REMARK 500 ARG A 353 -12.16
REMARK 500 PRO A 363 20.64
REMARK 500 GLU A 385 10.08
REMARK 500 ASN A 413 -13.92
REMARK 500 THR A 423 10.04
REMARK 500 VAL A 478 17.25
REMARK 500 GLY A 528 10.21
REMARK 500 GLY A 559 -11.12
REMARK 500 ASP A 563 -11.01
REMARK 500 ASN B 40 -11.43
REMARK 500 SER B 49 13.11
REMARK 500 ILE B 65 13.58
REMARK 500 ARG B 103 -14.95
REMARK 500 LYS B 142 -16.09
REMARK 500 THR B 218 10.08
REMARK 500 THR B 234 13.59
REMARK 500 VAL B 262 -10.32
REMARK 500 GLY B 268 -32.21
REMARK 500 TYR B 285 10.11
REMARK 500 SER B 287 10.76
REMARK 500 TYR B 289 -10.49
REMARK 500 VAL B 351 10.35
REMARK 500 GLY B 356 11.59
REMARK 500 ASP B 366 14.42
REMARK 500 PRO B 390 10.54
REMARK 500 ARG B 459 -11.30
REMARK 500
REMARK 500 THIS ENTRY HAS 51 MAIN CHAIN PLANARITY DEVIATIONS.
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 751 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 179 OE1
REMARK 620 2 GLU A 179 OE2 44.2
REMARK 620 3 PQQ A 701 N6 82.0 123.1
REMARK 620 4 ASP A 316 OD1 109.4 78.6 151.0
REMARK 620 5 PQQ A 701 O5 97.4 130.7 58.9 92.7
REMARK 620 6 PQQ A 701 O7A 87.9 97.5 56.1 147.2 113.1
REMARK 620 7 ASN A 266 OD1 130.8 90.0 125.7 67.4 131.3 80.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 761 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 17 O
REMARK 620 2 ASP A 17 OD1 76.3
REMARK 620 3 THR A 14 O 87.1 92.4
REMARK 620 4 THR A 14 OG1 131.5 67.2 64.5
REMARK 620 5 ASP A 11 O 156.0 126.1 99.1 71.1
REMARK 620 6 ASP A 11 OD1 101.0 82.1 168.7 104.1 76.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 752 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 179 OE2
REMARK 620 2 ASN B 266 OD1 90.9
REMARK 620 3 ASP B 316 OD1 80.5 62.2
REMARK 620 4 PQQ B 702 O5 126.7 132.9 94.0
REMARK 620 5 PQQ B 702 N6 124.0 121.9 153.2 63.3
REMARK 620 6 PQQ B 702 O7A 99.5 72.2 134.4 119.5 58.6
REMARK 620 7 GLU B 179 OE1 44.6 126.9 119.3 100.0 80.8 86.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 762 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 11 OD1
REMARK 620 2 THR B 14 OG1 112.4
REMARK 620 3 ASP B 17 OD1 88.2 72.2
REMARK 620 4 THR B 14 O 172.9 61.1 92.2
REMARK 620 5 ASP B 17 O 99.4 135.3 78.6 87.6
REMARK 620 6 ASP B 11 O 72.7 82.8 139.8 102.7 138.2
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 CA A 751
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 752
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 762
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQQ A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQQ B 702
DBREF 1FLG A 1 582 UNP Q9Z4J7 EXAA_PSEAE 35 616
DBREF 1FLG B 1 582 UNP Q9Z4J7 EXAA_PSEAE 35 616
SEQRES 1 A 582 LYS ASP VAL THR TRP GLU ASP ILE ALA ASN ASP ASP LYS
SEQRES 2 A 582 THR THR GLY ASP VAL LEU GLN TYR GLY MET GLY THR HIS
SEQRES 3 A 582 ALA GLN ARG TRP SER PRO LEU LYS GLN VAL ASN ALA ASP
SEQRES 4 A 582 ASN VAL PHE LYS LEU THR PRO ALA TRP SER TYR SER PHE
SEQRES 5 A 582 GLY ASP GLU LYS GLN ARG GLY GLN GLU SER GLN ALA ILE
SEQRES 6 A 582 VAL SER ASP GLY VAL ILE TYR VAL THR ALA SER TYR SER
SEQRES 7 A 582 ARG LEU PHE ALA LEU ASP ALA LYS THR GLY LYS ARG LEU
SEQRES 8 A 582 TRP THR TYR ASN HIS ARG LEU PRO ASP ASP ILE ARG PRO
SEQRES 9 A 582 CYS CYS ASP VAL VAL ASN ARG GLY ALA ALA ILE TYR GLY
SEQRES 10 A 582 ASP LYS VAL PHE PHE GLY THR LEU ASP ALA SER VAL VAL
SEQRES 11 A 582 ALA LEU ASN LYS ASN THR GLY LYS VAL VAL TRP LYS LYS
SEQRES 12 A 582 LYS PHE ALA ASP HIS GLY ALA GLY TYR THR MET THR GLY
SEQRES 13 A 582 ALA PRO THR ILE VAL LYS ASP GLY LYS THR GLY LYS VAL
SEQRES 14 A 582 LEU LEU ILE HIS GLY SER SER GLY ASP GLU PHE GLY VAL
SEQRES 15 A 582 VAL GLY ARG LEU PHE ALA ARG ASP PRO ASP THR GLY GLU
SEQRES 16 A 582 GLU ILE TRP MET ARG PRO PHE VAL GLU GLY HIS MET GLY
SEQRES 17 A 582 ARG LEU ASN GLY LYS ASP SER THR VAL THR GLY ASP VAL
SEQRES 18 A 582 LYS ALA PRO SER TRP PRO ASP ASP ARG ASN SER PRO THR
SEQRES 19 A 582 GLY LYS VAL GLU SER TRP SER HIS GLY GLY GLY ALA PRO
SEQRES 20 A 582 TRP GLN SER ALA SER PHE ASP ALA GLU THR ASN THR ILE
SEQRES 21 A 582 ILE VAL GLY ALA GLY ASN PRO GLY PRO TRP ASN THR TRP
SEQRES 22 A 582 ALA ARG THR ALA LYS GLY GLY ASN PRO HIS ASP TYR ASP
SEQRES 23 A 582 SER LEU TYR THR SER GLY GLN VAL GLY VAL ASP PRO SER
SEQRES 24 A 582 SER GLY GLU VAL LYS TRP PHE TYR GLN HIS THR PRO ASN
SEQRES 25 A 582 ASP ALA TRP ASP PHE SER GLY ASN ASN GLU LEU VAL LEU
SEQRES 26 A 582 PHE ASP TYR LYS ALA LYS ASP GLY LYS ILE VAL LYS ALA
SEQRES 27 A 582 THR ALA HIS ALA ASP ARG ASN GLY PHE PHE TYR VAL VAL
SEQRES 28 A 582 ASP ARG SER ASN GLY LYS LEU GLN ASN ALA PHE PRO PHE
SEQRES 29 A 582 VAL ASP ASN ILE THR TRP ALA SER HIS ILE ASP LEU LYS
SEQRES 30 A 582 THR GLY ARG PRO VAL GLU ARG GLU GLY GLN ARG PRO PRO
SEQRES 31 A 582 LEU PRO GLU PRO GLY GLN LYS HIS GLY LYS ALA VAL GLU
SEQRES 32 A 582 VAL SER PRO PRO PHE LEU GLY GLY LYS ASN TRP ASN PRO
SEQRES 33 A 582 MET ALA TYR SER GLN ASP THR GLY LEU PHE TYR VAL PRO
SEQRES 34 A 582 ALA ASN HIS TRP LYS GLU ASP TYR TRP THR GLU GLU VAL
SEQRES 35 A 582 SER TYR THR LYS GLY SER ALA TYR LEU GLY MET GLY PHE
SEQRES 36 A 582 ARG ILE LYS ARG MET TYR ASP ASP HIS VAL GLY SER LEU
SEQRES 37 A 582 ARG ALA MET ASP PRO VAL SER GLY LYS VAL VAL TRP GLU
SEQRES 38 A 582 HIS LYS GLU HIS LEU PRO LEU TRP ALA GLY VAL LEU ALA
SEQRES 39 A 582 THR ALA GLY ASN LEU VAL PHE THR GLY THR GLY ASP GLY
SEQRES 40 A 582 TYR PHE LYS ALA PHE ASP ALA LYS SER GLY LYS GLU LEU
SEQRES 41 A 582 TRP LYS PHE GLN THR GLY SER GLY ILE VAL SER PRO PRO
SEQRES 42 A 582 ILE THR TRP GLU GLN ASP GLY GLU GLN TYR LEU GLY VAL
SEQRES 43 A 582 THR VAL GLY TYR GLY GLY ALA VAL PRO LEU TRP GLY GLY
SEQRES 44 A 582 ASP MET ALA ASP LEU THR ARG PRO VAL ALA GLN GLY GLY
SEQRES 45 A 582 SER PHE TRP VAL PHE LYS LEU PRO SER TRP
SEQRES 1 B 582 LYS ASP VAL THR TRP GLU ASP ILE ALA ASN ASP ASP LYS
SEQRES 2 B 582 THR THR GLY ASP VAL LEU GLN TYR GLY MET GLY THR HIS
SEQRES 3 B 582 ALA GLN ARG TRP SER PRO LEU LYS GLN VAL ASN ALA ASP
SEQRES 4 B 582 ASN VAL PHE LYS LEU THR PRO ALA TRP SER TYR SER PHE
SEQRES 5 B 582 GLY ASP GLU LYS GLN ARG GLY GLN GLU SER GLN ALA ILE
SEQRES 6 B 582 VAL SER ASP GLY VAL ILE TYR VAL THR ALA SER TYR SER
SEQRES 7 B 582 ARG LEU PHE ALA LEU ASP ALA LYS THR GLY LYS ARG LEU
SEQRES 8 B 582 TRP THR TYR ASN HIS ARG LEU PRO ASP ASP ILE ARG PRO
SEQRES 9 B 582 CYS CYS ASP VAL VAL ASN ARG GLY ALA ALA ILE TYR GLY
SEQRES 10 B 582 ASP LYS VAL PHE PHE GLY THR LEU ASP ALA SER VAL VAL
SEQRES 11 B 582 ALA LEU ASN LYS ASN THR GLY LYS VAL VAL TRP LYS LYS
SEQRES 12 B 582 LYS PHE ALA ASP HIS GLY ALA GLY TYR THR MET THR GLY
SEQRES 13 B 582 ALA PRO THR ILE VAL LYS ASP GLY LYS THR GLY LYS VAL
SEQRES 14 B 582 LEU LEU ILE HIS GLY SER SER GLY ASP GLU PHE GLY VAL
SEQRES 15 B 582 VAL GLY ARG LEU PHE ALA ARG ASP PRO ASP THR GLY GLU
SEQRES 16 B 582 GLU ILE TRP MET ARG PRO PHE VAL GLU GLY HIS MET GLY
SEQRES 17 B 582 ARG LEU ASN GLY LYS ASP SER THR VAL THR GLY ASP VAL
SEQRES 18 B 582 LYS ALA PRO SER TRP PRO ASP ASP ARG ASN SER PRO THR
SEQRES 19 B 582 GLY LYS VAL GLU SER TRP SER HIS GLY GLY GLY ALA PRO
SEQRES 20 B 582 TRP GLN SER ALA SER PHE ASP ALA GLU THR ASN THR ILE
SEQRES 21 B 582 ILE VAL GLY ALA GLY ASN PRO GLY PRO TRP ASN THR TRP
SEQRES 22 B 582 ALA ARG THR ALA LYS GLY GLY ASN PRO HIS ASP TYR ASP
SEQRES 23 B 582 SER LEU TYR THR SER GLY GLN VAL GLY VAL ASP PRO SER
SEQRES 24 B 582 SER GLY GLU VAL LYS TRP PHE TYR GLN HIS THR PRO ASN
SEQRES 25 B 582 ASP ALA TRP ASP PHE SER GLY ASN ASN GLU LEU VAL LEU
SEQRES 26 B 582 PHE ASP TYR LYS ALA LYS ASP GLY LYS ILE VAL LYS ALA
SEQRES 27 B 582 THR ALA HIS ALA ASP ARG ASN GLY PHE PHE TYR VAL VAL
SEQRES 28 B 582 ASP ARG SER ASN GLY LYS LEU GLN ASN ALA PHE PRO PHE
SEQRES 29 B 582 VAL ASP ASN ILE THR TRP ALA SER HIS ILE ASP LEU LYS
SEQRES 30 B 582 THR GLY ARG PRO VAL GLU ARG GLU GLY GLN ARG PRO PRO
SEQRES 31 B 582 LEU PRO GLU PRO GLY GLN LYS HIS GLY LYS ALA VAL GLU
SEQRES 32 B 582 VAL SER PRO PRO PHE LEU GLY GLY LYS ASN TRP ASN PRO
SEQRES 33 B 582 MET ALA TYR SER GLN ASP THR GLY LEU PHE TYR VAL PRO
SEQRES 34 B 582 ALA ASN HIS TRP LYS GLU ASP TYR TRP THR GLU GLU VAL
SEQRES 35 B 582 SER TYR THR LYS GLY SER ALA TYR LEU GLY MET GLY PHE
SEQRES 36 B 582 ARG ILE LYS ARG MET TYR ASP ASP HIS VAL GLY SER LEU
SEQRES 37 B 582 ARG ALA MET ASP PRO VAL SER GLY LYS VAL VAL TRP GLU
SEQRES 38 B 582 HIS LYS GLU HIS LEU PRO LEU TRP ALA GLY VAL LEU ALA
SEQRES 39 B 582 THR ALA GLY ASN LEU VAL PHE THR GLY THR GLY ASP GLY
SEQRES 40 B 582 TYR PHE LYS ALA PHE ASP ALA LYS SER GLY LYS GLU LEU
SEQRES 41 B 582 TRP LYS PHE GLN THR GLY SER GLY ILE VAL SER PRO PRO
SEQRES 42 B 582 ILE THR TRP GLU GLN ASP GLY GLU GLN TYR LEU GLY VAL
SEQRES 43 B 582 THR VAL GLY TYR GLY GLY ALA VAL PRO LEU TRP GLY GLY
SEQRES 44 B 582 ASP MET ALA ASP LEU THR ARG PRO VAL ALA GLN GLY GLY
SEQRES 45 B 582 SER PHE TRP VAL PHE LYS LEU PRO SER TRP
HET CA A 751 1
HET CA A 761 1
HET PQQ A 701 24
HET CA B 752 1
HET CA B 762 1
HET PQQ B 702 24
HETNAM CA CALCIUM ION
HETNAM PQQ PYRROLOQUINOLINE QUINONE
FORMUL 3 CA 4(CA 2+)
FORMUL 5 PQQ 2(C14 H6 N2 O8)
FORMUL 9 HOH *106(H2 O)
HELIX 1 1 THR A 4 ASN A 10 1 7
HELIX 2 2 ASP A 11 THR A 14 5 4
HELIX 3 3 ASN A 40 LEU A 44 5 5
HELIX 4 4 ASP A 147 GLY A 151 5 5
HELIX 5 5 GLY A 177 GLY A 181 5 5
HELIX 6 6 VAL A 237 GLY A 243 5 7
HELIX 7 7 ASN A 271 THR A 276 5 6
HELIX 8 8 GLY A 552 GLY A 558 1 7
HELIX 9 9 GLY A 559 ARG A 566 1 8
HELIX 10 10 THR B 4 ASP B 11 1 8
HELIX 11 11 ASN B 40 LEU B 44 5 5
HELIX 12 12 ASP B 147 GLY B 151 5 5
HELIX 13 13 GLY B 177 GLY B 181 5 5
HELIX 14 14 VAL B 237 HIS B 242 1 6
HELIX 15 15 ASN B 271 THR B 276 5 6
HELIX 16 16 GLU B 385 ARG B 388 5 4
HELIX 17 17 ALA B 553 GLY B 558 1 6
HELIX 18 18 GLY B 559 ARG B 566 1 8
SHEET 1 A 5 TRP A 30 SER A 31 0
SHEET 2 A 5 LEU A 493 THR A 495 1 O ALA A 494 N SER A 31
SHEET 3 A 5 LEU A 499 GLY A 503 -1 O LEU A 499 N THR A 495
SHEET 4 A 5 TYR A 508 ASP A 513 -1 N LYS A 510 O THR A 502
SHEET 5 A 5 GLU A 519 GLN A 524 -1 N LEU A 520 O ALA A 511
SHEET 1 B 4 THR A 45 SER A 51 0
SHEET 2 B 4 SER A 573 LYS A 578 -1 N PHE A 574 O TYR A 50
SHEET 3 B 4 GLU A 541 VAL A 548 -1 O LEU A 544 N PHE A 577
SHEET 4 B 4 ILE A 534 GLN A 538 -1 O ILE A 534 N GLY A 545
SHEET 1 C 4 ILE A 65 SER A 67 0
SHEET 2 C 4 VAL A 70 ALA A 75 -1 O VAL A 70 N SER A 67
SHEET 3 C 4 ARG A 79 ASP A 84 -1 O ARG A 79 N ALA A 75
SHEET 4 C 4 ARG A 90 ASN A 95 -1 N LEU A 91 O ALA A 82
SHEET 1 D 4 ALA A 114 TYR A 116 0
SHEET 2 D 4 LYS A 119 THR A 124 -1 N LYS A 119 O TYR A 116
SHEET 3 D 4 SER A 128 ASN A 133 -1 O SER A 128 N THR A 124
SHEET 4 D 4 VAL A 139 LYS A 144 -1 N VAL A 140 O ALA A 131
SHEET 1 E 6 THR A 159 LYS A 162 0
SHEET 2 E 6 VAL A 169 HIS A 173 -1 N LEU A 170 O VAL A 161
SHEET 3 E 6 ARG A 185 ARG A 189 -1 O PHE A 187 N HIS A 173
SHEET 4 E 6 GLU A 196 PRO A 201 -1 N ILE A 197 O ALA A 188
SHEET 5 E 6 MET A 207 LEU A 210 -1 N ARG A 209 O MET A 199
SHEET 6 E 6 LYS A 213 VAL A 217 -1 O LYS A 213 N LEU A 210
SHEET 1 F 4 SER A 252 ASP A 254 0
SHEET 2 F 4 THR A 259 ALA A 264 -1 O THR A 259 N ASP A 254
SHEET 3 F 4 GLY A 292 VAL A 296 -1 O GLY A 292 N ALA A 264
SHEET 4 F 4 VAL A 303 GLN A 308 -1 N LYS A 304 O GLY A 295
SHEET 1 G 4 VAL A 324 LYS A 329 0
SHEET 2 G 4 ILE A 335 ALA A 342 -1 N VAL A 336 O TYR A 328
SHEET 3 G 4 PHE A 347 ASP A 352 -1 N TYR A 349 O HIS A 341
SHEET 4 G 4 LEU A 358 PRO A 363 -1 N GLN A 359 O VAL A 350
SHEET 1 H 2 ALA A 371 ILE A 374 0
SHEET 2 H 2 PRO A 381 GLU A 383 -1 O VAL A 382 N SER A 372
SHEET 1 I 3 VAL A 402 VAL A 404 0
SHEET 2 I 3 TRP A 433 THR A 439 -1 N GLU A 435 O VAL A 404
SHEET 3 I 3 MET A 453 ARG A 459 -1 N GLY A 454 O TRP A 438
SHEET 1 J 4 ALA A 418 TYR A 419 0
SHEET 2 J 4 PHE A 426 ASN A 431 -1 N TYR A 427 O ALA A 418
SHEET 3 J 4 GLY A 466 MET A 471 -1 N SER A 467 O ALA A 430
SHEET 4 J 4 VAL A 478 GLU A 484 -1 N VAL A 479 O ALA A 470
SHEET 1 K 5 TRP B 30 SER B 31 0
SHEET 2 K 5 LEU B 493 THR B 495 1 O ALA B 494 N SER B 31
SHEET 3 K 5 LEU B 499 GLY B 503 -1 O LEU B 499 N THR B 495
SHEET 4 K 5 TYR B 508 ASP B 513 -1 N LYS B 510 O THR B 502
SHEET 5 K 5 GLU B 519 GLN B 524 -1 N LEU B 520 O ALA B 511
SHEET 1 L 4 THR B 45 SER B 51 0
SHEET 2 L 4 SER B 573 LYS B 578 -1 N PHE B 574 O TYR B 50
SHEET 3 L 4 GLU B 541 VAL B 548 -1 O LEU B 544 N PHE B 577
SHEET 4 L 4 ILE B 534 GLN B 538 -1 O ILE B 534 N GLY B 545
SHEET 1 M 4 ILE B 65 SER B 67 0
SHEET 2 M 4 VAL B 70 ALA B 75 -1 O VAL B 70 N SER B 67
SHEET 3 M 4 ARG B 79 ASP B 84 -1 O ARG B 79 N ALA B 75
SHEET 4 M 4 ARG B 90 ASN B 95 -1 N LEU B 91 O ALA B 82
SHEET 1 N 4 ALA B 114 TYR B 116 0
SHEET 2 N 4 LYS B 119 THR B 124 -1 O LYS B 119 N TYR B 116
SHEET 3 N 4 SER B 128 ASN B 133 -1 O SER B 128 N THR B 124
SHEET 4 N 4 VAL B 139 LYS B 144 -1 N VAL B 140 O ALA B 131
SHEET 1 O 6 THR B 159 LYS B 162 0
SHEET 2 O 6 VAL B 169 HIS B 173 -1 N LEU B 170 O VAL B 161
SHEET 3 O 6 ARG B 185 ARG B 189 -1 N PHE B 187 O HIS B 173
SHEET 4 O 6 GLU B 196 PRO B 201 -1 N ILE B 197 O ALA B 188
SHEET 5 O 6 ARG B 209 LEU B 210 -1 N ARG B 209 O MET B 199
SHEET 6 O 6 LYS B 213 ASP B 214 -1 N LYS B 213 O LEU B 210
SHEET 1 P 4 SER B 252 ASP B 254 0
SHEET 2 P 4 THR B 259 ALA B 264 -1 O THR B 259 N ASP B 254
SHEET 3 P 4 GLY B 292 VAL B 296 -1 O GLY B 292 N ALA B 264
SHEET 4 P 4 VAL B 303 GLN B 308 -1 N LYS B 304 O GLY B 295
SHEET 1 Q 4 VAL B 324 LYS B 329 0
SHEET 2 Q 4 ILE B 335 ALA B 342 -1 N VAL B 336 O TYR B 328
SHEET 3 Q 4 PHE B 347 ASP B 352 -1 N TYR B 349 O HIS B 341
SHEET 4 Q 4 LEU B 358 PRO B 363 -1 N GLN B 359 O VAL B 350
SHEET 1 R 2 ALA B 371 ASP B 375 0
SHEET 2 R 2 ARG B 380 GLU B 383 -1 O ARG B 380 N ASP B 375
SHEET 1 S 3 VAL B 402 VAL B 404 0
SHEET 2 S 3 TRP B 433 THR B 439 -1 O GLU B 435 N VAL B 404
SHEET 3 S 3 MET B 453 ARG B 459 -1 N GLY B 454 O TRP B 438
SHEET 1 T 4 ALA B 418 TYR B 419 0
SHEET 2 T 4 PHE B 426 ASN B 431 -1 N TYR B 427 O ALA B 418
SHEET 3 T 4 GLY B 466 MET B 471 -1 N SER B 467 O ALA B 430
SHEET 4 T 4 VAL B 478 GLU B 484 -1 N VAL B 479 O ALA B 470
SSBOND 1 CYS A 105 CYS A 106 1555 1555 2.01
SSBOND 2 CYS B 105 CYS B 106 1555 1555 2.07
LINK CA CA A 751 OE1 GLU A 179 1555 1555 2.84
LINK CA CA A 751 OE2 GLU A 179 1555 1555 2.93
LINK CA CA A 751 N6 PQQ A 701 1555 1555 2.93
LINK CA CA A 751 OD1 ASP A 316 1555 1555 2.84
LINK CA CA A 751 O5 PQQ A 701 1555 1555 2.73
LINK CA CA A 751 O7A PQQ A 701 1555 1555 2.79
LINK CA CA A 751 OD1 ASN A 266 1555 1555 2.92
LINK CA CA A 761 O ASP A 17 1555 1555 2.70
LINK CA CA A 761 OD1 ASP A 17 1555 1555 2.72
LINK CA CA A 761 O THR A 14 1555 1555 2.88
LINK CA CA A 761 OG1 THR A 14 1555 1555 2.91
LINK CA CA A 761 O ASP A 11 1555 1555 2.85
LINK CA CA A 761 OD1 ASP A 11 1555 1555 2.88
LINK CA CA B 752 OE2 GLU B 179 1555 1555 2.93
LINK CA CA B 752 OD1 ASN B 266 1555 1555 2.75
LINK CA CA B 752 OD1 ASP B 316 1555 1555 3.17
LINK CA CA B 752 O5 PQQ B 702 1555 1555 2.82
LINK CA CA B 752 N6 PQQ B 702 1555 1555 2.93
LINK CA CA B 752 O7A PQQ B 702 1555 1555 2.79
LINK CA CA B 752 OE1 GLU B 179 1555 1555 2.79
LINK CA CA B 762 OD1 ASP B 11 1555 1555 2.66
LINK CA CA B 762 OG1 THR B 14 1555 1555 3.04
LINK CA CA B 762 OD1 ASP B 17 1555 1555 2.65
LINK CA CA B 762 O THR B 14 1555 1555 2.72
LINK CA CA B 762 O ASP B 17 1555 1555 2.93
LINK CA CA B 762 O ASP B 11 1555 1555 2.81
CISPEP 1 SER A 405 PRO A 406 0 -5.45
CISPEP 2 SER B 405 PRO B 406 0 8.00
SITE 1 AC1 4 GLU A 179 ASN A 266 ASP A 316 PQQ A 701
SITE 1 AC2 3 ASP A 11 THR A 14 ASP A 17
SITE 1 AC3 4 GLU B 179 ASN B 266 ASP B 316 PQQ B 702
SITE 1 AC4 3 ASP B 11 THR B 14 ASP B 17
SITE 1 AC5 17 GLU A 61 CYS A 105 CYS A 106 ARG A 111
SITE 2 AC5 17 THR A 155 SER A 176 GLY A 177 ASP A 178
SITE 3 AC5 17 TRP A 248 ASN A 266 ARG A 344 ASN A 413
SITE 4 AC5 17 TRP A 414 TRP A 489 GLY A 552 ALA A 553
SITE 5 AC5 17 CA A 751
SITE 1 AC6 19 GLU B 61 CYS B 105 CYS B 106 ARG B 111
SITE 2 AC6 19 THR B 155 SER B 176 GLY B 177 ASP B 178
SITE 3 AC6 19 GLU B 179 TRP B 248 ASN B 266 ARG B 344
SITE 4 AC6 19 LEU B 409 ASN B 413 TRP B 414 TRP B 489
SITE 5 AC6 19 GLY B 552 ALA B 553 CA B 752
CRYST1 159.400 159.400 130.950 90.00 90.00 120.00 H 3 18
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 0.006270 0.003620 0.000000 0.00000
SCALE2 0.000000 0.007240 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007640 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
