HEADER ALCOHOL FERMENTATION 17-APR-98 1ZPD
TITLE PYRUVATE DECARBOXYLASE FROM ZYMOMONAS MOBILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PYRUVATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B, E, F;
COMPND 4 EC: 4.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZYMOMONAS MOBILIS;
SOURCE 3 ORGANISM_TAXID: 542;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: SG13009/PREP4;
SOURCE 7 EXPRESSION_SYSTEM_COLLECTION: ATCC 29191
KEYWDS ALCOHOL FERMENTATION, THIAMIN DIPHOSPHATE, DECARBOXYLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LU,D.DOBRITZSCH,G.SCHNEIDER
REVDAT 4 09-AUG-23 1ZPD 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1ZPD 1 VERSN
REVDAT 2 23-MAR-99 1ZPD 1 COMPND REMARK SOURCE
REVDAT 1 02-FEB-99 1ZPD 0
JRNL AUTH D.DOBRITZSCH,S.KONIG,G.SCHNEIDER,G.LU
JRNL TITL HIGH RESOLUTION CRYSTAL STRUCTURE OF PYRUVATE DECARBOXYLASE
JRNL TITL 2 FROM ZYMOMONAS MOBILIS. IMPLICATIONS FOR SUBSTRATE
JRNL TITL 3 ACTIVATION IN PYRUVATE DECARBOXYLASES.
JRNL REF J.BIOL.CHEM. V. 273 20196 1998
JRNL REFN ISSN 0021-9258
JRNL PMID 9685367
JRNL DOI 10.1074/JBC.273.32.20196
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 1.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 3 NUMBER OF REFLECTIONS : 150215
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.300
REMARK 3 FREE R VALUE TEST SET COUNT : 6858
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 17060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 2569
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 10.41
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.87
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) : 0.007 ; 0.020
REMARK 3 ANGLE DISTANCE (A) : 0.020 ; 0.040
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: NCS RESTRAINTS WERE APPLIED TO PROTEIN
REMARK 3 ATOMS AND MOST WATER MOLECULES WITH CHAIN ID W, U, V, AND X,
REMARK 3 WHICH SATISFY ALL THE NCS OPERATIONS. WATER MOLECULES WITH CHAIN
REMARK 3 ID Y SATISFY 3 OF 4 NCS OPERATIONS WHILE WATERS WITH CHAIN ID Z
REMARK 3 SATISFY 2 OF 4 NCS'S. WATERS WITH CHAIN ID S DOES NOT FOLLOW ANY
REMARK 3 NCS OPERATIONS. ESD FROM SIGMAA (A) : 0.15
REMARK 4
REMARK 4 1ZPD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000177501.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : OCT-97
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE(002)
REMARK 200 OPTICS : COLLIMATOR
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 157263
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 22.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.0
REMARK 200 DATA REDUNDANCY : 1.910
REMARK 200 R MERGE (I) : 0.06300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 62.5
REMARK 200 DATA REDUNDANCY IN SHELL : 1.84
REMARK 200 R MERGE FOR SHELL (I) : 0.21000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1YPD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 30290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -178.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F
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 1
REMARK 465 VAL A 567
REMARK 465 VAL A 568
REMARK 465 MET B 1
REMARK 465 VAL B 567
REMARK 465 VAL B 568
REMARK 465 MET E 1
REMARK 465 VAL E 567
REMARK 465 VAL E 568
REMARK 465 MET F 1
REMARK 465 VAL F 567
REMARK 465 VAL F 568
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 B 440 CB - CG - OD1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG B 554 NE - CZ - NH1 ANGL. DEV. = -3.8 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 SER A 74 -72.50 70.27
REMARK 500 HIS A 114 -6.86 75.83
REMARK 500 SER A 248 3.19 86.73
REMARK 500 TRP A 262 55.04 -153.07
REMARK 500 GLU A 409 58.96 -119.05
REMARK 500 ILE A 476 -61.76 -98.28
REMARK 500 ASP A 503 -147.88 -142.66
REMARK 500 SER B 74 -70.27 65.56
REMARK 500 HIS B 114 -5.42 74.46
REMARK 500 SER B 248 3.78 85.85
REMARK 500 TRP B 262 55.44 -154.88
REMARK 500 GLU B 409 61.33 -118.20
REMARK 500 ILE B 476 -60.27 -99.71
REMARK 500 ASP B 503 -146.51 -141.34
REMARK 500 SER E 74 -68.80 63.07
REMARK 500 HIS E 114 -5.94 78.08
REMARK 500 SER E 248 1.92 87.86
REMARK 500 TRP E 262 59.92 -154.02
REMARK 500 GLU E 409 61.91 -119.91
REMARK 500 THR E 446 14.68 -140.07
REMARK 500 ILE E 476 -61.53 -97.92
REMARK 500 ASP E 503 -146.73 -140.86
REMARK 500 SER F 74 -69.78 70.95
REMARK 500 HIS F 114 -5.55 75.74
REMARK 500 SER F 248 3.06 84.11
REMARK 500 TRP F 262 56.02 -155.30
REMARK 500 ASP F 503 -144.72 -138.09
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 DPX A 600
REMARK 615 DPX B 600
REMARK 615 DPX E 600
REMARK 615 DPX F 600
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 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 440 OD1
REMARK 620 2 ASN A 467 OD1 91.5
REMARK 620 3 GLY A 469 O 100.4 92.9
REMARK 620 4 DPX A 600 O21 88.8 177.8 89.2
REMARK 620 5 DPX A 600 O24 167.4 93.3 91.1 86.0
REMARK 620 6 HOH A 611 O 89.6 81.7 168.8 96.1 79.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 440 OD1
REMARK 620 2 ASN B 467 OD1 91.3
REMARK 620 3 GLY B 469 O 98.7 93.4
REMARK 620 4 DPX B 600 O21 87.4 178.5 87.5
REMARK 620 5 DPX B 600 O24 169.3 92.5 91.0 88.6
REMARK 620 6 HOH B 611 O 86.8 83.2 173.6 95.9 83.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 440 OD1
REMARK 620 2 ASN E 467 OD1 89.0
REMARK 620 3 GLY E 469 O 100.0 91.5
REMARK 620 4 DPX E 600 O21 89.6 178.6 89.1
REMARK 620 5 DPX E 600 O24 168.9 93.5 90.7 87.8
REMARK 620 6 HOH E 611 O 87.4 82.9 170.7 96.7 82.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F 601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 440 OD1
REMARK 620 2 ASN F 467 OD1 90.8
REMARK 620 3 GLY F 469 O 101.6 93.5
REMARK 620 4 DPX F 600 O21 87.2 176.3 89.9
REMARK 620 5 DPX F 600 O24 165.7 93.6 91.7 87.7
REMARK 620 6 HOH F 611 O 85.2 81.5 171.7 95.3 82.1
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 MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPX A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPX B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPX E 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT E 610
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DPX F 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT F 610
DBREF 1ZPD A 1 566 UNP P06672 PDC_ZYMMO 1 566
DBREF 1ZPD B 1 566 UNP P06672 PDC_ZYMMO 1 566
DBREF 1ZPD E 1 566 UNP P06672 PDC_ZYMMO 1 566
DBREF 1ZPD F 1 566 UNP P06672 PDC_ZYMMO 1 566
SEQADV 1ZPD ASP A 200 UNP P06672 GLU 200 CONFLICT
SEQADV 1ZPD THR A 233 UNP P06672 ALA 233 CONFLICT
SEQADV 1ZPD ALA A 255 UNP P06672 PRO 255 CONFLICT
SEQADV 1ZPD LEU A 256 UNP P06672 HIS 256 CONFLICT
SEQADV 1ZPD SER A 341 UNP P06672 ALA 341 CONFLICT
SEQADV 1ZPD ALA A 507 UNP P06672 GLY 507 CONFLICT
SEQADV 1ZPD ASP B 200 UNP P06672 GLU 200 CONFLICT
SEQADV 1ZPD THR B 233 UNP P06672 ALA 233 CONFLICT
SEQADV 1ZPD ALA B 255 UNP P06672 PRO 255 CONFLICT
SEQADV 1ZPD LEU B 256 UNP P06672 HIS 256 CONFLICT
SEQADV 1ZPD SER B 341 UNP P06672 ALA 341 CONFLICT
SEQADV 1ZPD ALA B 507 UNP P06672 GLY 507 CONFLICT
SEQADV 1ZPD ASP E 200 UNP P06672 GLU 200 CONFLICT
SEQADV 1ZPD THR E 233 UNP P06672 ALA 233 CONFLICT
SEQADV 1ZPD ALA E 255 UNP P06672 PRO 255 CONFLICT
SEQADV 1ZPD LEU E 256 UNP P06672 HIS 256 CONFLICT
SEQADV 1ZPD SER E 341 UNP P06672 ALA 341 CONFLICT
SEQADV 1ZPD ALA E 507 UNP P06672 GLY 507 CONFLICT
SEQADV 1ZPD ASP F 200 UNP P06672 GLU 200 CONFLICT
SEQADV 1ZPD THR F 233 UNP P06672 ALA 233 CONFLICT
SEQADV 1ZPD ALA F 255 UNP P06672 PRO 255 CONFLICT
SEQADV 1ZPD LEU F 256 UNP P06672 HIS 256 CONFLICT
SEQADV 1ZPD SER F 341 UNP P06672 ALA 341 CONFLICT
SEQADV 1ZPD ALA F 507 UNP P06672 GLY 507 CONFLICT
SEQRES 1 A 568 MET SER TYR THR VAL GLY THR TYR LEU ALA GLU ARG LEU
SEQRES 2 A 568 VAL GLN ILE GLY LEU LYS HIS HIS PHE ALA VAL ALA GLY
SEQRES 3 A 568 ASP TYR ASN LEU VAL LEU LEU ASP ASN LEU LEU LEU ASN
SEQRES 4 A 568 LYS ASN MET GLU GLN VAL TYR CYS CYS ASN GLU LEU ASN
SEQRES 5 A 568 CYS GLY PHE SER ALA GLU GLY TYR ALA ARG ALA LYS GLY
SEQRES 6 A 568 ALA ALA ALA ALA VAL VAL THR TYR SER VAL GLY ALA LEU
SEQRES 7 A 568 SER ALA PHE ASP ALA ILE GLY GLY ALA TYR ALA GLU ASN
SEQRES 8 A 568 LEU PRO VAL ILE LEU ILE SER GLY ALA PRO ASN ASN ASN
SEQRES 9 A 568 ASP HIS ALA ALA GLY HIS VAL LEU HIS HIS ALA LEU GLY
SEQRES 10 A 568 LYS THR ASP TYR HIS TYR GLN LEU GLU MET ALA LYS ASN
SEQRES 11 A 568 ILE THR ALA ALA ALA GLU ALA ILE TYR THR PRO GLU GLU
SEQRES 12 A 568 ALA PRO ALA LYS ILE ASP HIS VAL ILE LYS THR ALA LEU
SEQRES 13 A 568 ARG GLU LYS LYS PRO VAL TYR LEU GLU ILE ALA CYS ASN
SEQRES 14 A 568 ILE ALA SER MET PRO CYS ALA ALA PRO GLY PRO ALA SER
SEQRES 15 A 568 ALA LEU PHE ASN ASP GLU ALA SER ASP GLU ALA SER LEU
SEQRES 16 A 568 ASN ALA ALA VAL ASP GLU THR LEU LYS PHE ILE ALA ASN
SEQRES 17 A 568 ARG ASP LYS VAL ALA VAL LEU VAL GLY SER LYS LEU ARG
SEQRES 18 A 568 ALA ALA GLY ALA GLU GLU ALA ALA VAL LYS PHE THR ASP
SEQRES 19 A 568 ALA LEU GLY GLY ALA VAL ALA THR MET ALA ALA ALA LYS
SEQRES 20 A 568 SER PHE PHE PRO GLU GLU ASN ALA LEU TYR ILE GLY THR
SEQRES 21 A 568 SER TRP GLY GLU VAL SER TYR PRO GLY VAL GLU LYS THR
SEQRES 22 A 568 MET LYS GLU ALA ASP ALA VAL ILE ALA LEU ALA PRO VAL
SEQRES 23 A 568 PHE ASN ASP TYR SER THR THR GLY TRP THR ASP ILE PRO
SEQRES 24 A 568 ASP PRO LYS LYS LEU VAL LEU ALA GLU PRO ARG SER VAL
SEQRES 25 A 568 VAL VAL ASN GLY ILE ARG PHE PRO SER VAL HIS LEU LYS
SEQRES 26 A 568 ASP TYR LEU THR ARG LEU ALA GLN LYS VAL SER LYS LYS
SEQRES 27 A 568 THR GLY SER LEU ASP PHE PHE LYS SER LEU ASN ALA GLY
SEQRES 28 A 568 GLU LEU LYS LYS ALA ALA PRO ALA ASP PRO SER ALA PRO
SEQRES 29 A 568 LEU VAL ASN ALA GLU ILE ALA ARG GLN VAL GLU ALA LEU
SEQRES 30 A 568 LEU THR PRO ASN THR THR VAL ILE ALA GLU THR GLY ASP
SEQRES 31 A 568 SER TRP PHE ASN ALA GLN ARG MET LYS LEU PRO ASN GLY
SEQRES 32 A 568 ALA ARG VAL GLU TYR GLU MET GLN TRP GLY HIS ILE GLY
SEQRES 33 A 568 TRP SER VAL PRO ALA ALA PHE GLY TYR ALA VAL GLY ALA
SEQRES 34 A 568 PRO GLU ARG ARG ASN ILE LEU MET VAL GLY ASP GLY SER
SEQRES 35 A 568 PHE GLN LEU THR ALA GLN GLU VAL ALA GLN MET VAL ARG
SEQRES 36 A 568 LEU LYS LEU PRO VAL ILE ILE PHE LEU ILE ASN ASN TYR
SEQRES 37 A 568 GLY TYR THR ILE GLU VAL MET ILE HIS ASP GLY PRO TYR
SEQRES 38 A 568 ASN ASN ILE LYS ASN TRP ASP TYR ALA GLY LEU MET GLU
SEQRES 39 A 568 VAL PHE ASN GLY ASN GLY GLY TYR ASP SER GLY ALA ALA
SEQRES 40 A 568 LYS GLY LEU LYS ALA LYS THR GLY GLY GLU LEU ALA GLU
SEQRES 41 A 568 ALA ILE LYS VAL ALA LEU ALA ASN THR ASP GLY PRO THR
SEQRES 42 A 568 LEU ILE GLU CYS PHE ILE GLY ARG GLU ASP CYS THR GLU
SEQRES 43 A 568 GLU LEU VAL LYS TRP GLY LYS ARG VAL ALA ALA ALA ASN
SEQRES 44 A 568 SER ARG LYS PRO VAL ASN LYS VAL VAL
SEQRES 1 B 568 MET SER TYR THR VAL GLY THR TYR LEU ALA GLU ARG LEU
SEQRES 2 B 568 VAL GLN ILE GLY LEU LYS HIS HIS PHE ALA VAL ALA GLY
SEQRES 3 B 568 ASP TYR ASN LEU VAL LEU LEU ASP ASN LEU LEU LEU ASN
SEQRES 4 B 568 LYS ASN MET GLU GLN VAL TYR CYS CYS ASN GLU LEU ASN
SEQRES 5 B 568 CYS GLY PHE SER ALA GLU GLY TYR ALA ARG ALA LYS GLY
SEQRES 6 B 568 ALA ALA ALA ALA VAL VAL THR TYR SER VAL GLY ALA LEU
SEQRES 7 B 568 SER ALA PHE ASP ALA ILE GLY GLY ALA TYR ALA GLU ASN
SEQRES 8 B 568 LEU PRO VAL ILE LEU ILE SER GLY ALA PRO ASN ASN ASN
SEQRES 9 B 568 ASP HIS ALA ALA GLY HIS VAL LEU HIS HIS ALA LEU GLY
SEQRES 10 B 568 LYS THR ASP TYR HIS TYR GLN LEU GLU MET ALA LYS ASN
SEQRES 11 B 568 ILE THR ALA ALA ALA GLU ALA ILE TYR THR PRO GLU GLU
SEQRES 12 B 568 ALA PRO ALA LYS ILE ASP HIS VAL ILE LYS THR ALA LEU
SEQRES 13 B 568 ARG GLU LYS LYS PRO VAL TYR LEU GLU ILE ALA CYS ASN
SEQRES 14 B 568 ILE ALA SER MET PRO CYS ALA ALA PRO GLY PRO ALA SER
SEQRES 15 B 568 ALA LEU PHE ASN ASP GLU ALA SER ASP GLU ALA SER LEU
SEQRES 16 B 568 ASN ALA ALA VAL ASP GLU THR LEU LYS PHE ILE ALA ASN
SEQRES 17 B 568 ARG ASP LYS VAL ALA VAL LEU VAL GLY SER LYS LEU ARG
SEQRES 18 B 568 ALA ALA GLY ALA GLU GLU ALA ALA VAL LYS PHE THR ASP
SEQRES 19 B 568 ALA LEU GLY GLY ALA VAL ALA THR MET ALA ALA ALA LYS
SEQRES 20 B 568 SER PHE PHE PRO GLU GLU ASN ALA LEU TYR ILE GLY THR
SEQRES 21 B 568 SER TRP GLY GLU VAL SER TYR PRO GLY VAL GLU LYS THR
SEQRES 22 B 568 MET LYS GLU ALA ASP ALA VAL ILE ALA LEU ALA PRO VAL
SEQRES 23 B 568 PHE ASN ASP TYR SER THR THR GLY TRP THR ASP ILE PRO
SEQRES 24 B 568 ASP PRO LYS LYS LEU VAL LEU ALA GLU PRO ARG SER VAL
SEQRES 25 B 568 VAL VAL ASN GLY ILE ARG PHE PRO SER VAL HIS LEU LYS
SEQRES 26 B 568 ASP TYR LEU THR ARG LEU ALA GLN LYS VAL SER LYS LYS
SEQRES 27 B 568 THR GLY SER LEU ASP PHE PHE LYS SER LEU ASN ALA GLY
SEQRES 28 B 568 GLU LEU LYS LYS ALA ALA PRO ALA ASP PRO SER ALA PRO
SEQRES 29 B 568 LEU VAL ASN ALA GLU ILE ALA ARG GLN VAL GLU ALA LEU
SEQRES 30 B 568 LEU THR PRO ASN THR THR VAL ILE ALA GLU THR GLY ASP
SEQRES 31 B 568 SER TRP PHE ASN ALA GLN ARG MET LYS LEU PRO ASN GLY
SEQRES 32 B 568 ALA ARG VAL GLU TYR GLU MET GLN TRP GLY HIS ILE GLY
SEQRES 33 B 568 TRP SER VAL PRO ALA ALA PHE GLY TYR ALA VAL GLY ALA
SEQRES 34 B 568 PRO GLU ARG ARG ASN ILE LEU MET VAL GLY ASP GLY SER
SEQRES 35 B 568 PHE GLN LEU THR ALA GLN GLU VAL ALA GLN MET VAL ARG
SEQRES 36 B 568 LEU LYS LEU PRO VAL ILE ILE PHE LEU ILE ASN ASN TYR
SEQRES 37 B 568 GLY TYR THR ILE GLU VAL MET ILE HIS ASP GLY PRO TYR
SEQRES 38 B 568 ASN ASN ILE LYS ASN TRP ASP TYR ALA GLY LEU MET GLU
SEQRES 39 B 568 VAL PHE ASN GLY ASN GLY GLY TYR ASP SER GLY ALA ALA
SEQRES 40 B 568 LYS GLY LEU LYS ALA LYS THR GLY GLY GLU LEU ALA GLU
SEQRES 41 B 568 ALA ILE LYS VAL ALA LEU ALA ASN THR ASP GLY PRO THR
SEQRES 42 B 568 LEU ILE GLU CYS PHE ILE GLY ARG GLU ASP CYS THR GLU
SEQRES 43 B 568 GLU LEU VAL LYS TRP GLY LYS ARG VAL ALA ALA ALA ASN
SEQRES 44 B 568 SER ARG LYS PRO VAL ASN LYS VAL VAL
SEQRES 1 E 568 MET SER TYR THR VAL GLY THR TYR LEU ALA GLU ARG LEU
SEQRES 2 E 568 VAL GLN ILE GLY LEU LYS HIS HIS PHE ALA VAL ALA GLY
SEQRES 3 E 568 ASP TYR ASN LEU VAL LEU LEU ASP ASN LEU LEU LEU ASN
SEQRES 4 E 568 LYS ASN MET GLU GLN VAL TYR CYS CYS ASN GLU LEU ASN
SEQRES 5 E 568 CYS GLY PHE SER ALA GLU GLY TYR ALA ARG ALA LYS GLY
SEQRES 6 E 568 ALA ALA ALA ALA VAL VAL THR TYR SER VAL GLY ALA LEU
SEQRES 7 E 568 SER ALA PHE ASP ALA ILE GLY GLY ALA TYR ALA GLU ASN
SEQRES 8 E 568 LEU PRO VAL ILE LEU ILE SER GLY ALA PRO ASN ASN ASN
SEQRES 9 E 568 ASP HIS ALA ALA GLY HIS VAL LEU HIS HIS ALA LEU GLY
SEQRES 10 E 568 LYS THR ASP TYR HIS TYR GLN LEU GLU MET ALA LYS ASN
SEQRES 11 E 568 ILE THR ALA ALA ALA GLU ALA ILE TYR THR PRO GLU GLU
SEQRES 12 E 568 ALA PRO ALA LYS ILE ASP HIS VAL ILE LYS THR ALA LEU
SEQRES 13 E 568 ARG GLU LYS LYS PRO VAL TYR LEU GLU ILE ALA CYS ASN
SEQRES 14 E 568 ILE ALA SER MET PRO CYS ALA ALA PRO GLY PRO ALA SER
SEQRES 15 E 568 ALA LEU PHE ASN ASP GLU ALA SER ASP GLU ALA SER LEU
SEQRES 16 E 568 ASN ALA ALA VAL ASP GLU THR LEU LYS PHE ILE ALA ASN
SEQRES 17 E 568 ARG ASP LYS VAL ALA VAL LEU VAL GLY SER LYS LEU ARG
SEQRES 18 E 568 ALA ALA GLY ALA GLU GLU ALA ALA VAL LYS PHE THR ASP
SEQRES 19 E 568 ALA LEU GLY GLY ALA VAL ALA THR MET ALA ALA ALA LYS
SEQRES 20 E 568 SER PHE PHE PRO GLU GLU ASN ALA LEU TYR ILE GLY THR
SEQRES 21 E 568 SER TRP GLY GLU VAL SER TYR PRO GLY VAL GLU LYS THR
SEQRES 22 E 568 MET LYS GLU ALA ASP ALA VAL ILE ALA LEU ALA PRO VAL
SEQRES 23 E 568 PHE ASN ASP TYR SER THR THR GLY TRP THR ASP ILE PRO
SEQRES 24 E 568 ASP PRO LYS LYS LEU VAL LEU ALA GLU PRO ARG SER VAL
SEQRES 25 E 568 VAL VAL ASN GLY ILE ARG PHE PRO SER VAL HIS LEU LYS
SEQRES 26 E 568 ASP TYR LEU THR ARG LEU ALA GLN LYS VAL SER LYS LYS
SEQRES 27 E 568 THR GLY SER LEU ASP PHE PHE LYS SER LEU ASN ALA GLY
SEQRES 28 E 568 GLU LEU LYS LYS ALA ALA PRO ALA ASP PRO SER ALA PRO
SEQRES 29 E 568 LEU VAL ASN ALA GLU ILE ALA ARG GLN VAL GLU ALA LEU
SEQRES 30 E 568 LEU THR PRO ASN THR THR VAL ILE ALA GLU THR GLY ASP
SEQRES 31 E 568 SER TRP PHE ASN ALA GLN ARG MET LYS LEU PRO ASN GLY
SEQRES 32 E 568 ALA ARG VAL GLU TYR GLU MET GLN TRP GLY HIS ILE GLY
SEQRES 33 E 568 TRP SER VAL PRO ALA ALA PHE GLY TYR ALA VAL GLY ALA
SEQRES 34 E 568 PRO GLU ARG ARG ASN ILE LEU MET VAL GLY ASP GLY SER
SEQRES 35 E 568 PHE GLN LEU THR ALA GLN GLU VAL ALA GLN MET VAL ARG
SEQRES 36 E 568 LEU LYS LEU PRO VAL ILE ILE PHE LEU ILE ASN ASN TYR
SEQRES 37 E 568 GLY TYR THR ILE GLU VAL MET ILE HIS ASP GLY PRO TYR
SEQRES 38 E 568 ASN ASN ILE LYS ASN TRP ASP TYR ALA GLY LEU MET GLU
SEQRES 39 E 568 VAL PHE ASN GLY ASN GLY GLY TYR ASP SER GLY ALA ALA
SEQRES 40 E 568 LYS GLY LEU LYS ALA LYS THR GLY GLY GLU LEU ALA GLU
SEQRES 41 E 568 ALA ILE LYS VAL ALA LEU ALA ASN THR ASP GLY PRO THR
SEQRES 42 E 568 LEU ILE GLU CYS PHE ILE GLY ARG GLU ASP CYS THR GLU
SEQRES 43 E 568 GLU LEU VAL LYS TRP GLY LYS ARG VAL ALA ALA ALA ASN
SEQRES 44 E 568 SER ARG LYS PRO VAL ASN LYS VAL VAL
SEQRES 1 F 568 MET SER TYR THR VAL GLY THR TYR LEU ALA GLU ARG LEU
SEQRES 2 F 568 VAL GLN ILE GLY LEU LYS HIS HIS PHE ALA VAL ALA GLY
SEQRES 3 F 568 ASP TYR ASN LEU VAL LEU LEU ASP ASN LEU LEU LEU ASN
SEQRES 4 F 568 LYS ASN MET GLU GLN VAL TYR CYS CYS ASN GLU LEU ASN
SEQRES 5 F 568 CYS GLY PHE SER ALA GLU GLY TYR ALA ARG ALA LYS GLY
SEQRES 6 F 568 ALA ALA ALA ALA VAL VAL THR TYR SER VAL GLY ALA LEU
SEQRES 7 F 568 SER ALA PHE ASP ALA ILE GLY GLY ALA TYR ALA GLU ASN
SEQRES 8 F 568 LEU PRO VAL ILE LEU ILE SER GLY ALA PRO ASN ASN ASN
SEQRES 9 F 568 ASP HIS ALA ALA GLY HIS VAL LEU HIS HIS ALA LEU GLY
SEQRES 10 F 568 LYS THR ASP TYR HIS TYR GLN LEU GLU MET ALA LYS ASN
SEQRES 11 F 568 ILE THR ALA ALA ALA GLU ALA ILE TYR THR PRO GLU GLU
SEQRES 12 F 568 ALA PRO ALA LYS ILE ASP HIS VAL ILE LYS THR ALA LEU
SEQRES 13 F 568 ARG GLU LYS LYS PRO VAL TYR LEU GLU ILE ALA CYS ASN
SEQRES 14 F 568 ILE ALA SER MET PRO CYS ALA ALA PRO GLY PRO ALA SER
SEQRES 15 F 568 ALA LEU PHE ASN ASP GLU ALA SER ASP GLU ALA SER LEU
SEQRES 16 F 568 ASN ALA ALA VAL ASP GLU THR LEU LYS PHE ILE ALA ASN
SEQRES 17 F 568 ARG ASP LYS VAL ALA VAL LEU VAL GLY SER LYS LEU ARG
SEQRES 18 F 568 ALA ALA GLY ALA GLU GLU ALA ALA VAL LYS PHE THR ASP
SEQRES 19 F 568 ALA LEU GLY GLY ALA VAL ALA THR MET ALA ALA ALA LYS
SEQRES 20 F 568 SER PHE PHE PRO GLU GLU ASN ALA LEU TYR ILE GLY THR
SEQRES 21 F 568 SER TRP GLY GLU VAL SER TYR PRO GLY VAL GLU LYS THR
SEQRES 22 F 568 MET LYS GLU ALA ASP ALA VAL ILE ALA LEU ALA PRO VAL
SEQRES 23 F 568 PHE ASN ASP TYR SER THR THR GLY TRP THR ASP ILE PRO
SEQRES 24 F 568 ASP PRO LYS LYS LEU VAL LEU ALA GLU PRO ARG SER VAL
SEQRES 25 F 568 VAL VAL ASN GLY ILE ARG PHE PRO SER VAL HIS LEU LYS
SEQRES 26 F 568 ASP TYR LEU THR ARG LEU ALA GLN LYS VAL SER LYS LYS
SEQRES 27 F 568 THR GLY SER LEU ASP PHE PHE LYS SER LEU ASN ALA GLY
SEQRES 28 F 568 GLU LEU LYS LYS ALA ALA PRO ALA ASP PRO SER ALA PRO
SEQRES 29 F 568 LEU VAL ASN ALA GLU ILE ALA ARG GLN VAL GLU ALA LEU
SEQRES 30 F 568 LEU THR PRO ASN THR THR VAL ILE ALA GLU THR GLY ASP
SEQRES 31 F 568 SER TRP PHE ASN ALA GLN ARG MET LYS LEU PRO ASN GLY
SEQRES 32 F 568 ALA ARG VAL GLU TYR GLU MET GLN TRP GLY HIS ILE GLY
SEQRES 33 F 568 TRP SER VAL PRO ALA ALA PHE GLY TYR ALA VAL GLY ALA
SEQRES 34 F 568 PRO GLU ARG ARG ASN ILE LEU MET VAL GLY ASP GLY SER
SEQRES 35 F 568 PHE GLN LEU THR ALA GLN GLU VAL ALA GLN MET VAL ARG
SEQRES 36 F 568 LEU LYS LEU PRO VAL ILE ILE PHE LEU ILE ASN ASN TYR
SEQRES 37 F 568 GLY TYR THR ILE GLU VAL MET ILE HIS ASP GLY PRO TYR
SEQRES 38 F 568 ASN ASN ILE LYS ASN TRP ASP TYR ALA GLY LEU MET GLU
SEQRES 39 F 568 VAL PHE ASN GLY ASN GLY GLY TYR ASP SER GLY ALA ALA
SEQRES 40 F 568 LYS GLY LEU LYS ALA LYS THR GLY GLY GLU LEU ALA GLU
SEQRES 41 F 568 ALA ILE LYS VAL ALA LEU ALA ASN THR ASP GLY PRO THR
SEQRES 42 F 568 LEU ILE GLU CYS PHE ILE GLY ARG GLU ASP CYS THR GLU
SEQRES 43 F 568 GLU LEU VAL LYS TRP GLY LYS ARG VAL ALA ALA ALA ASN
SEQRES 44 F 568 SER ARG LYS PRO VAL ASN LYS VAL VAL
HET MG A 601 1
HET DPX A 600 26
HET CIT A 610 13
HET MG B 601 1
HET DPX B 600 26
HET CIT B 610 13
HET MG E 601 1
HET DPX E 600 26
HET CIT E 610 13
HET MG F 601 1
HET DPX F 600 26
HET CIT F 610 13
HETNAM MG MAGNESIUM ION
HETNAM DPX MONO-{4-[(4-AMINO-2-METHYL-PYRIMIDIN-5-YLMETHYL)-
HETNAM 2 DPX AMINO]-2-HYDROXY-3-MERCAPTO-PENT-3-ENYL-PHOSPHONO}
HETNAM 3 DPX ESTER
HETNAM CIT CITRIC ACID
FORMUL 5 MG 4(MG 2+)
FORMUL 6 DPX 4(C11 H20 N4 O8 P2 S)
FORMUL 7 CIT 4(C6 H8 O7)
FORMUL 17 HOH *2569(H2 O)
HELIX 1 1 VAL A 5 ILE A 16 1 12
HELIX 2 2 ASP A 27 LEU A 38 5 12
HELIX 3 3 GLU A 50 LYS A 64 1 15
HELIX 4 4 ALA A 77 ALA A 89 1 13
HELIX 5 5 ASN A 103 ASP A 105 5 3
HELIX 6 6 TYR A 123 ILE A 131 1 9
HELIX 7 7 PRO A 141 GLU A 158 5 18
HELIX 8 8 CYS A 168 ILE A 170 5 3
HELIX 9 9 ALA A 181 PHE A 185 5 5
HELIX 10 10 GLU A 192 ILE A 206 1 15
HELIX 11 11 GLU A 226 LEU A 236 1 11
HELIX 12 12 ALA A 244 ALA A 246 5 3
HELIX 13 13 GLY A 263 VAL A 265 5 3
HELIX 14 14 VAL A 270 GLU A 276 1 7
HELIX 15 15 PRO A 301 LYS A 303 5 3
HELIX 16 16 LEU A 324 LYS A 334 1 11
HELIX 17 17 GLY A 340 LEU A 348 1 9
HELIX 18 18 ASN A 367 LEU A 377 1 11
HELIX 19 19 ASP A 390 ARG A 397 1 8
HELIX 20 20 TRP A 417 GLY A 428 1 12
HELIX 21 21 ASP A 440 ARG A 455 1 16
HELIX 22 22 THR A 471 ILE A 476 1 6
HELIX 23 23 PRO A 480 ASN A 482 5 3
HELIX 24 24 TYR A 489 ASN A 497 1 9
HELIX 25 25 GLY A 515 ALA A 527 1 13
HELIX 26 26 GLU A 546 SER A 560 1 15
HELIX 27 27 VAL B 5 GLN B 15 1 11
HELIX 28 28 LEU B 30 LEU B 38 1 9
HELIX 29 29 GLU B 50 LYS B 64 1 15
HELIX 30 30 ALA B 77 ALA B 89 1 13
HELIX 31 31 ASN B 103 ASP B 105 5 3
HELIX 32 32 TYR B 123 ASN B 130 1 8
HELIX 33 33 PRO B 141 GLU B 158 5 18
HELIX 34 34 CYS B 168 ILE B 170 5 3
HELIX 35 35 ALA B 181 PHE B 185 5 5
HELIX 36 36 GLU B 192 ILE B 206 1 15
HELIX 37 37 GLU B 226 LEU B 236 1 11
HELIX 38 38 ALA B 244 ALA B 246 5 3
HELIX 39 39 GLY B 263 VAL B 265 5 3
HELIX 40 40 VAL B 270 GLU B 276 1 7
HELIX 41 41 LEU B 324 LYS B 334 1 11
HELIX 42 42 GLY B 340 LEU B 348 1 9
HELIX 43 43 ASN B 367 LEU B 377 1 11
HELIX 44 44 ASP B 390 ARG B 397 1 8
HELIX 45 45 TRP B 417 GLY B 428 1 12
HELIX 46 46 ASP B 440 ARG B 455 1 16
HELIX 47 47 THR B 471 VAL B 474 1 4
HELIX 48 48 PRO B 480 ASN B 482 5 3
HELIX 49 49 TYR B 489 ASN B 497 1 9
HELIX 50 50 GLY B 515 ALA B 527 1 13
HELIX 51 51 GLU B 546 SER B 560 1 15
HELIX 52 52 VAL E 5 ILE E 16 1 12
HELIX 53 53 ASP E 27 LEU E 38 5 12
HELIX 54 54 GLU E 50 LYS E 64 1 15
HELIX 55 55 ALA E 77 ALA E 89 1 13
HELIX 56 56 ASN E 103 ASP E 105 5 3
HELIX 57 57 TYR E 123 ASN E 130 1 8
HELIX 58 58 PRO E 141 GLU E 158 5 18
HELIX 59 59 CYS E 168 ILE E 170 5 3
HELIX 60 60 ALA E 181 PHE E 185 5 5
HELIX 61 61 GLU E 192 ILE E 206 1 15
HELIX 62 62 GLU E 226 LEU E 236 1 11
HELIX 63 63 ALA E 244 ALA E 246 5 3
HELIX 64 64 GLY E 263 VAL E 265 5 3
HELIX 65 65 VAL E 270 GLU E 276 1 7
HELIX 66 66 PRO E 301 LYS E 303 5 3
HELIX 67 67 LEU E 324 LYS E 334 1 11
HELIX 68 68 GLY E 340 LEU E 348 1 9
HELIX 69 69 ASN E 367 LEU E 377 1 11
HELIX 70 70 ASP E 390 ARG E 397 1 8
HELIX 71 71 TRP E 417 GLY E 428 1 12
HELIX 72 72 ASP E 440 ARG E 455 1 16
HELIX 73 73 THR E 471 ILE E 476 1 6
HELIX 74 74 PRO E 480 ASN E 482 5 3
HELIX 75 75 TYR E 489 ASN E 497 1 9
HELIX 76 76 GLY E 515 ALA E 527 1 13
HELIX 77 77 GLU E 546 SER E 560 1 15
HELIX 78 78 VAL F 5 GLN F 15 1 11
HELIX 79 79 ASP F 27 LEU F 38 5 12
HELIX 80 80 GLU F 50 LYS F 64 1 15
HELIX 81 81 ALA F 77 ALA F 89 1 13
HELIX 82 82 ASN F 103 ASP F 105 5 3
HELIX 83 83 TYR F 123 ASN F 130 1 8
HELIX 84 84 PRO F 141 GLU F 158 5 18
HELIX 85 85 CYS F 168 ILE F 170 5 3
HELIX 86 86 ALA F 181 PHE F 185 5 5
HELIX 87 87 GLU F 192 ILE F 206 1 15
HELIX 88 88 GLU F 226 LEU F 236 1 11
HELIX 89 89 ALA F 244 ALA F 246 5 3
HELIX 90 90 GLY F 263 VAL F 265 5 3
HELIX 91 91 VAL F 270 GLU F 276 1 7
HELIX 92 92 PRO F 301 LYS F 303 5 3
HELIX 93 93 LEU F 324 LYS F 334 1 11
HELIX 94 94 GLY F 340 LEU F 348 1 9
HELIX 95 95 ASN F 367 LEU F 377 1 11
HELIX 96 96 ASP F 390 ARG F 397 1 8
HELIX 97 97 TRP F 417 GLY F 428 1 12
HELIX 98 98 ASP F 440 ARG F 455 1 16
HELIX 99 99 THR F 471 ILE F 476 1 6
HELIX 100 100 PRO F 480 ASN F 482 5 3
HELIX 101 101 TYR F 489 ASN F 497 1 9
HELIX 102 102 GLY F 515 ALA F 527 1 13
HELIX 103 103 GLU F 546 SER F 560 1 15
SHEET 1 A 2 HIS A 20 ALA A 23 0
SHEET 2 A 2 GLU A 43 TYR A 46 1 N GLU A 43 O HIS A 21
SHEET 1 B 4 ALA A 66 VAL A 71 0
SHEET 2 B 4 PRO A 93 ALA A 100 1 N PRO A 93 O ALA A 67
SHEET 3 B 4 VAL A 162 ALA A 167 1 N VAL A 162 O LEU A 96
SHEET 4 B 4 ALA A 135 ILE A 138 1 N GLU A 136 O TYR A 163
SHEET 1 C 5 TYR A 257 SER A 261 0
SHEET 2 C 5 VAL A 240 MET A 243 1 N VAL A 240 O ILE A 258
SHEET 3 C 5 VAL A 212 VAL A 216 1 N VAL A 214 O ALA A 241
SHEET 4 C 5 ALA A 279 LEU A 283 1 N ALA A 279 O ALA A 213
SHEET 5 C 5 LEU A 304 ALA A 307 1 N VAL A 305 O VAL A 280
SHEET 1 D 2 SER A 311 VAL A 314 0
SHEET 2 D 2 ILE A 317 PRO A 320 -1 N PHE A 319 O VAL A 312
SHEET 1 E 6 ARG A 405 TYR A 408 0
SHEET 2 E 6 THR A 382 ALA A 386 1 N VAL A 384 O ARG A 405
SHEET 3 E 6 ARG A 433 GLY A 439 1 N ARG A 433 O THR A 383
SHEET 4 E 6 ILE A 461 ASN A 466 1 N ILE A 461 O LEU A 436
SHEET 5 E 6 THR A 533 PHE A 538 1 N THR A 533 O ILE A 462
SHEET 6 E 6 LYS A 508 ALA A 512 1 N LYS A 508 O LEU A 534
SHEET 1 F 2 HIS B 20 ALA B 23 0
SHEET 2 F 2 GLU B 43 TYR B 46 1 N GLU B 43 O HIS B 21
SHEET 1 G 4 ALA B 66 VAL B 71 0
SHEET 2 G 4 PRO B 93 ALA B 100 1 N PRO B 93 O ALA B 67
SHEET 3 G 4 VAL B 162 ALA B 167 1 N VAL B 162 O LEU B 96
SHEET 4 G 4 ALA B 134 ILE B 138 1 N ALA B 134 O TYR B 163
SHEET 1 H 5 TYR B 257 SER B 261 0
SHEET 2 H 5 VAL B 240 MET B 243 1 N VAL B 240 O ILE B 258
SHEET 3 H 5 VAL B 212 VAL B 216 1 N VAL B 214 O ALA B 241
SHEET 4 H 5 ALA B 279 LEU B 283 1 N ALA B 279 O ALA B 213
SHEET 5 H 5 LEU B 304 ALA B 307 1 N VAL B 305 O VAL B 280
SHEET 1 I 2 SER B 311 VAL B 314 0
SHEET 2 I 2 ILE B 317 PRO B 320 -1 N PHE B 319 O VAL B 312
SHEET 1 J 6 ARG B 405 TYR B 408 0
SHEET 2 J 6 THR B 382 ALA B 386 1 N VAL B 384 O ARG B 405
SHEET 3 J 6 ARG B 433 GLY B 439 1 N ARG B 433 O THR B 383
SHEET 4 J 6 ILE B 461 ASN B 466 1 N ILE B 461 O LEU B 436
SHEET 5 J 6 THR B 533 PHE B 538 1 N THR B 533 O ILE B 462
SHEET 6 J 6 LYS B 508 ALA B 512 1 N LYS B 508 O LEU B 534
SHEET 1 K 2 HIS E 20 ALA E 23 0
SHEET 2 K 2 GLU E 43 TYR E 46 1 N GLU E 43 O HIS E 21
SHEET 1 L 4 ALA E 66 VAL E 71 0
SHEET 2 L 4 PRO E 93 ALA E 100 1 N PRO E 93 O ALA E 67
SHEET 3 L 4 VAL E 162 ALA E 167 1 N VAL E 162 O LEU E 96
SHEET 4 L 4 ALA E 134 ILE E 138 1 N ALA E 134 O TYR E 163
SHEET 1 M 5 TYR E 257 SER E 261 0
SHEET 2 M 5 VAL E 240 MET E 243 1 N VAL E 240 O ILE E 258
SHEET 3 M 5 VAL E 212 VAL E 216 1 N VAL E 214 O ALA E 241
SHEET 4 M 5 ALA E 279 LEU E 283 1 N ALA E 279 O ALA E 213
SHEET 5 M 5 LEU E 304 ALA E 307 1 N VAL E 305 O VAL E 280
SHEET 1 N 2 SER E 311 VAL E 314 0
SHEET 2 N 2 ILE E 317 PRO E 320 -1 N PHE E 319 O VAL E 312
SHEET 1 O 6 ARG E 405 TYR E 408 0
SHEET 2 O 6 THR E 382 ALA E 386 1 N VAL E 384 O ARG E 405
SHEET 3 O 6 ARG E 433 GLY E 439 1 N ARG E 433 O THR E 383
SHEET 4 O 6 ILE E 461 ASN E 466 1 N ILE E 461 O LEU E 436
SHEET 5 O 6 THR E 533 PHE E 538 1 N THR E 533 O ILE E 462
SHEET 6 O 6 LYS E 508 ALA E 512 1 N LYS E 508 O LEU E 534
SHEET 1 P 2 HIS F 20 ALA F 23 0
SHEET 2 P 2 GLU F 43 TYR F 46 1 N GLU F 43 O HIS F 21
SHEET 1 Q 4 ALA F 66 VAL F 71 0
SHEET 2 Q 4 PRO F 93 ALA F 100 1 N PRO F 93 O ALA F 67
SHEET 3 Q 4 VAL F 162 ALA F 167 1 N VAL F 162 O LEU F 96
SHEET 4 Q 4 ALA F 134 ILE F 138 1 N ALA F 134 O TYR F 163
SHEET 1 R 5 TYR F 257 SER F 261 0
SHEET 2 R 5 VAL F 240 MET F 243 1 N VAL F 240 O ILE F 258
SHEET 3 R 5 VAL F 212 VAL F 216 1 N VAL F 214 O ALA F 241
SHEET 4 R 5 ALA F 279 LEU F 283 1 N ALA F 279 O ALA F 213
SHEET 5 R 5 LEU F 304 ALA F 307 1 N VAL F 305 O VAL F 280
SHEET 1 S 2 SER F 311 VAL F 314 0
SHEET 2 S 2 ILE F 317 PRO F 320 -1 N PHE F 319 O VAL F 312
SHEET 1 T 6 ARG F 405 TYR F 408 0
SHEET 2 T 6 THR F 382 ALA F 386 1 N VAL F 384 O ARG F 405
SHEET 3 T 6 ARG F 433 GLY F 439 1 N ARG F 433 O THR F 383
SHEET 4 T 6 ILE F 461 ASN F 466 1 N ILE F 461 O LEU F 436
SHEET 5 T 6 THR F 533 PHE F 538 1 N THR F 533 O ILE F 462
SHEET 6 T 6 LYS F 508 ALA F 512 1 N LYS F 508 O LEU F 534
LINK OD1 ASP A 440 MG MG A 601 1555 1555 1.94
LINK OD1 ASN A 467 MG MG A 601 1555 1555 2.11
LINK O GLY A 469 MG MG A 601 1555 1555 2.19
LINK O21 DPX A 600 MG MG A 601 1555 1555 2.19
LINK O24 DPX A 600 MG MG A 601 1555 1555 2.31
LINK MG MG A 601 O HOH A 611 1555 1555 2.20
LINK OD1 ASP B 440 MG MG B 601 1555 1555 1.94
LINK OD1 ASN B 467 MG MG B 601 1555 1555 2.13
LINK O GLY B 469 MG MG B 601 1555 1555 2.17
LINK O21 DPX B 600 MG MG B 601 1555 1555 2.18
LINK O24 DPX B 600 MG MG B 601 1555 1555 2.32
LINK MG MG B 601 O HOH B 611 1555 1555 2.22
LINK OD1 ASP E 440 MG MG E 601 1555 1555 1.97
LINK OD1 ASN E 467 MG MG E 601 1555 1555 2.13
LINK O GLY E 469 MG MG E 601 1555 1555 2.20
LINK O21 DPX E 600 MG MG E 601 1555 1555 2.18
LINK O24 DPX E 600 MG MG E 601 1555 1555 2.28
LINK MG MG E 601 O HOH E 611 1555 1555 2.21
LINK OD1 ASP F 440 MG MG F 601 1555 1555 1.97
LINK OD1 ASN F 467 MG MG F 601 1555 1555 2.13
LINK O GLY F 469 MG MG F 601 1555 1555 2.13
LINK O21 DPX F 600 MG MG F 601 1555 1555 2.18
LINK O24 DPX F 600 MG MG F 601 1555 1555 2.29
LINK MG MG F 601 O HOH F 611 1555 1555 2.18
SITE 1 AC1 5 ASP A 440 ASN A 467 GLY A 469 DPX A 600
SITE 2 AC1 5 HOH A 611
SITE 1 AC2 5 ASP B 440 ASN B 467 GLY B 469 DPX B 600
SITE 2 AC2 5 HOH B 611
SITE 1 AC3 5 ASP E 440 ASN E 467 GLY E 469 DPX E 600
SITE 2 AC3 5 HOH E 611
SITE 1 AC4 5 ASP F 440 ASN F 467 GLY F 469 DPX F 600
SITE 2 AC4 5 HOH F 611
SITE 1 AC5 24 ASP A 390 GLY A 413 HIS A 414 ILE A 415
SITE 2 AC5 24 GLY A 439 ASP A 440 GLY A 441 SER A 442
SITE 3 AC5 24 ASN A 467 GLY A 469 TYR A 470 THR A 471
SITE 4 AC5 24 ILE A 472 GLU A 473 MG A 601 HOH A 611
SITE 5 AC5 24 HOH A 612 HOH A 769 HOH A1256 ALA B 25
SITE 6 AC5 24 GLY B 26 GLU B 50 VAL B 75 HIS B 114
SITE 1 AC6 12 ARG A 310 ARG A 318 PRO A 320 SER A 321
SITE 2 AC6 12 HOH A 709 HOH A 746 HOH A 789 HOH A1006
SITE 3 AC6 12 HOH A1049 HIS F 150 LYS F 153 ARG F 157
SITE 1 AC7 23 ALA A 25 GLY A 26 GLU A 50 VAL A 75
SITE 2 AC7 23 HIS A 114 ASP B 390 GLY B 413 HIS B 414
SITE 3 AC7 23 ILE B 415 GLY B 439 ASP B 440 GLY B 441
SITE 4 AC7 23 SER B 442 ASN B 467 GLY B 469 TYR B 470
SITE 5 AC7 23 THR B 471 ILE B 472 GLU B 473 MG B 601
SITE 6 AC7 23 HOH B 611 HOH B 612 HOH B 842
SITE 1 AC8 12 ARG B 310 ARG B 318 PRO B 320 SER B 321
SITE 2 AC8 12 HOH B 688 HOH B 782 HOH B 819 HOH B 861
SITE 3 AC8 12 HOH B1111 HIS E 150 LYS E 153 ARG E 157
SITE 1 AC9 23 ASP E 390 GLY E 413 HIS E 414 ILE E 415
SITE 2 AC9 23 GLY E 439 ASP E 440 GLY E 441 SER E 442
SITE 3 AC9 23 ASN E 467 GLY E 469 TYR E 470 THR E 471
SITE 4 AC9 23 ILE E 472 GLU E 473 MG E 601 HOH E 611
SITE 5 AC9 23 HOH E 612 HOH E 874 ALA F 25 GLY F 26
SITE 6 AC9 23 GLU F 50 VAL F 75 HIS F 114
SITE 1 BC1 12 HIS B 150 LYS B 153 ARG B 157 ARG E 310
SITE 2 BC1 12 ARG E 318 PRO E 320 SER E 321 HOH E 656
SITE 3 BC1 12 HOH E 814 HOH E 851 HOH E 894 HOH E1113
SITE 1 BC2 24 ALA E 25 GLY E 26 GLU E 50 VAL E 75
SITE 2 BC2 24 HIS E 114 ASP F 390 GLY F 413 HIS F 414
SITE 3 BC2 24 ILE F 415 GLY F 439 ASP F 440 GLY F 441
SITE 4 BC2 24 SER F 442 ASN F 467 GLY F 469 TYR F 470
SITE 5 BC2 24 THR F 471 ILE F 472 GLU F 473 MG F 601
SITE 6 BC2 24 HOH F 611 HOH F 612 HOH F 943 HOH F1240
SITE 1 BC3 12 HIS A 150 LYS A 153 ARG A 157 ARG F 310
SITE 2 BC3 12 ARG F 318 PRO F 320 SER F 321 HOH F 712
SITE 3 BC3 12 HOH F 793 HOH F 885 HOH F 920 HOH F 962
CRYST1 69.868 92.168 98.256 102.86 94.59 112.69 P 1 4
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 0.014313 0.005984 0.002911 0.00000
SCALE2 0.000000 0.011760 0.003371 0.00000
SCALE3 0.000000 0.000000 0.010622 0.00000
MTRIX1 1 -0.999996 -0.001489 -0.002410 0.53468 1
MTRIX2 1 -0.000644 -0.709027 0.705181 0.13641 1
MTRIX3 1 -0.002759 0.705180 0.709023 -0.13950 1
MTRIX1 2 0.999999 0.000977 0.000977 0.34429 1
MTRIX2 2 0.000977 -1.000000 0.000055 -0.00492 1
MTRIX3 2 0.000977 -0.000054 -1.000000 -0.63301 1
MTRIX1 3 -0.999999 0.000000 0.001465 0.55823 1
MTRIX2 3 -0.001031 0.710659 -0.703536 -0.27361 1
MTRIX3 3 -0.001041 -0.703537 -0.710658 -0.55083 1
(ATOM LINES ARE NOT SHOWN.)
END
