HEADER LYASE 10-AUG-05 2AMT
TITLE STRUCTURE OF 2C-METHYL-D-ERYTHRITOL 2,4-CLYCODIPHOSPHATE SYNTHASE
TITLE 2 COMPLEXED WITH A CDP DERIVED FLUORESCENT INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: MECPS, MECDP-SYNTHASE;
COMPND 5 EC: 4.6.1.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: ISPF, MECS;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS ISOPRENOID, LYASE, ISOPRENE BIOSYNTHESIS
EXPDTA X-RAY DIFFRACTION
AUTHOR N.L.RAMSDEN,W.N.HUNTER
REVDAT 3 23-AUG-23 2AMT 1 REMARK LINK
REVDAT 2 24-FEB-09 2AMT 1 VERSN
REVDAT 1 28-FEB-06 2AMT 0
JRNL AUTH C.M.CRANE,J.KAISER,N.L.RAMSDEN,S.LAUW,F.ROHDICH,
JRNL AUTH 2 W.EISENREICH,W.N.HUNTER,A.BACHER,F.DIEDERICH
JRNL TITL FLUORESCENT INHIBITORS FOR ISPF, AN ENZYME IN THE
JRNL TITL 2 NON-MEVALONATE PATHWAY FOR ISOPRENOID BIOSYNTHESIS AND A
JRNL TITL 3 POTENTIAL TARGET FOR ANTIMALARIAL THERAPY.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 45 1069 2006
JRNL REFN ESSN 0570-0833
JRNL PMID 16392111
JRNL DOI 10.1002/ANIE.200503003
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.50
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 45024
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) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.243
REMARK 3 FREE R VALUE : 0.280
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2397
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.42
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3352
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.72
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 177
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6996
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 266
REMARK 3 SOLVENT ATOMS : 233
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 29.85
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.19000
REMARK 3 B22 (A**2) : 6.86000
REMARK 3 B33 (A**2) : -3.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.24000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.403
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.268
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.226
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.344
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.914
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.881
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7406 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10038 ; 0.998 ; 2.015
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 931 ; 4.979 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 289 ;35.718 ;23.564
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1189 ;14.840 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 48 ;14.666 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1128 ; 0.060 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5506 ; 0.002 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4103 ; 0.173 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5063 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 476 ; 0.112 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 5 ; 0.054 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 67 ; 0.182 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.153 ; 0.200
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): 4725 ; 0.336 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7308 ; 0.594 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2977 ; 0.518 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2730 ; 0.968 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 2AMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9756
REMARK 200 MONOCHROMATOR : SILICON
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (TRUNCATE)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 47420
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 29.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.09700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.27200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
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: 1GX1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM SULFATE, 10% PEG 200
REMARK 280 MME, 0.1M SODIUM ACETATE, PH 5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 57.63450
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15790 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 10130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16030 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 ALA A 157
REMARK 465 THR A 158
REMARK 465 LYS A 159
REMARK 465 ALA B 157
REMARK 465 THR B 158
REMARK 465 LYS B 159
REMARK 465 ALA C 157
REMARK 465 THR C 158
REMARK 465 LYS C 159
REMARK 465 ALA D 157
REMARK 465 THR D 158
REMARK 465 LYS D 159
REMARK 465 ALA E 157
REMARK 465 THR E 158
REMARK 465 LYS E 159
REMARK 465 ALA F 157
REMARK 465 THR F 158
REMARK 465 LYS F 159
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 PRO D 103 CD PRO D 103 N 0.125
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 GLU A 15 -156.98 -108.61
REMARK 500 LEU A 32 -77.48 -84.91
REMARK 500 HIS A 34 -114.56 50.54
REMARK 500 SER A 35 -166.77 -73.16
REMARK 500 GLU B 15 -142.10 -115.01
REMARK 500 ALA B 33 -168.76 -128.52
REMARK 500 SER B 35 -29.80 -150.09
REMARK 500 ASP B 36 -18.33 80.28
REMARK 500 THR B 64 40.18 -90.84
REMARK 500 ALA C 33 161.65 -45.04
REMARK 500 HIS C 34 42.25 -78.26
REMARK 500 SER C 35 -163.62 -114.61
REMARK 500 SER D 35 -162.75 -109.81
REMARK 500 ALA D 102 -153.95 -100.53
REMARK 500 PRO D 103 130.71 -21.73
REMARK 500 GLU E 15 -144.18 -114.73
REMARK 500 SER E 35 -167.95 -100.54
REMARK 500 ASP E 38 93.44 -67.05
REMARK 500 THR E 64 23.89 -77.41
REMARK 500 SER F 35 -165.45 -126.44
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 LEU A 32 ALA A 33 -146.16
REMARK 500 LEU B 32 ALA B 33 135.69
REMARK 500 ALA B 33 HIS B 34 136.16
REMARK 500 SER B 35 ASP B 36 -133.85
REMARK 500 LEU C 31 LEU C 32 -144.80
REMARK 500 HIS C 34 SER C 35 135.80
REMARK 500 GLN D 101 ALA D 102 -135.28
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 1AA A 1901
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 ZN A1900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 8 OD2
REMARK 620 2 HIS A 10 NE2 99.1
REMARK 620 3 HIS A 42 ND1 82.6 90.9
REMARK 620 4 1AA A1901 O7 111.5 96.8 162.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 8 OD2
REMARK 620 2 HIS B 10 NE2 94.8
REMARK 620 3 HIS B 42 ND1 94.2 92.0
REMARK 620 4 1AA C2901 O8 129.6 115.2 122.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C3900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 8 OD2
REMARK 620 2 HIS C 10 NE2 94.5
REMARK 620 3 HIS C 42 ND1 101.1 97.3
REMARK 620 4 1AA C3901 O8 136.0 95.9 119.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D4900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 8 OD2
REMARK 620 2 HIS D 10 NE2 103.5
REMARK 620 3 HIS D 42 ND1 99.1 98.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN F6900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 1AA D6901 O8
REMARK 620 2 ASP F 8 OD2 121.2
REMARK 620 3 HIS F 10 NE2 109.9 89.8
REMARK 620 4 HIS F 42 ND1 138.1 93.2 91.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E5900 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP E 8 OD2
REMARK 620 2 HIS E 10 NE2 92.8
REMARK 620 3 HIS E 42 ND1 108.1 106.3
REMARK 620 4 1AA E5901 O8 134.4 104.8 106.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 3900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 4900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 5900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 6900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AA A 1901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AA C 2901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AA C 3901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPP A 7903
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AA E 4901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AA E 5901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1AA D 6901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GPP D 8903
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1GX1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CDP
REMARK 900 RELATED ID: 1KNJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH C5P AND CDI
REMARK 900 RELATED ID: 1U3P RELATED DB: PDB
REMARK 900 THE SAME PROTEIN BUT NATIVE
REMARK 900 RELATED ID: 2AO4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH A CDP DERIVED FLUORESCENT DERIVATIVE
DBREF 2AMT A 1 159 UNP P62617 ISPF_ECOLI 1 159
DBREF 2AMT B 1 159 UNP P62617 ISPF_ECOLI 1 159
DBREF 2AMT C 1 159 UNP P62617 ISPF_ECOLI 1 159
DBREF 2AMT D 1 159 UNP P62617 ISPF_ECOLI 1 159
DBREF 2AMT E 1 159 UNP P62617 ISPF_ECOLI 1 159
DBREF 2AMT F 1 159 UNP P62617 ISPF_ECOLI 1 159
SEQRES 1 A 159 MET ARG ILE GLY HIS GLY PHE ASP VAL HIS ALA PHE GLY
SEQRES 2 A 159 GLY GLU GLY PRO ILE ILE ILE GLY GLY VAL ARG ILE PRO
SEQRES 3 A 159 TYR GLU LYS GLY LEU LEU ALA HIS SER ASP GLY ASP VAL
SEQRES 4 A 159 ALA LEU HIS ALA LEU THR ASP ALA LEU LEU GLY ALA ALA
SEQRES 5 A 159 ALA LEU GLY ASP ILE GLY LYS LEU PHE PRO ASP THR ASP
SEQRES 6 A 159 PRO ALA PHE LYS GLY ALA ASP SER ARG GLU LEU LEU ARG
SEQRES 7 A 159 GLU ALA TRP ARG ARG ILE GLN ALA LYS GLY TYR THR LEU
SEQRES 8 A 159 GLY ASN VAL ASP VAL THR ILE ILE ALA GLN ALA PRO LYS
SEQRES 9 A 159 MET LEU PRO HIS ILE PRO GLN MET ARG VAL PHE ILE ALA
SEQRES 10 A 159 GLU ASP LEU GLY CYS HIS MET ASP ASP VAL ASN VAL LYS
SEQRES 11 A 159 ALA THR THR THR GLU LYS LEU GLY PHE THR GLY ARG GLY
SEQRES 12 A 159 GLU GLY ILE ALA CYS GLU ALA VAL ALA LEU LEU ILE LYS
SEQRES 13 A 159 ALA THR LYS
SEQRES 1 B 159 MET ARG ILE GLY HIS GLY PHE ASP VAL HIS ALA PHE GLY
SEQRES 2 B 159 GLY GLU GLY PRO ILE ILE ILE GLY GLY VAL ARG ILE PRO
SEQRES 3 B 159 TYR GLU LYS GLY LEU LEU ALA HIS SER ASP GLY ASP VAL
SEQRES 4 B 159 ALA LEU HIS ALA LEU THR ASP ALA LEU LEU GLY ALA ALA
SEQRES 5 B 159 ALA LEU GLY ASP ILE GLY LYS LEU PHE PRO ASP THR ASP
SEQRES 6 B 159 PRO ALA PHE LYS GLY ALA ASP SER ARG GLU LEU LEU ARG
SEQRES 7 B 159 GLU ALA TRP ARG ARG ILE GLN ALA LYS GLY TYR THR LEU
SEQRES 8 B 159 GLY ASN VAL ASP VAL THR ILE ILE ALA GLN ALA PRO LYS
SEQRES 9 B 159 MET LEU PRO HIS ILE PRO GLN MET ARG VAL PHE ILE ALA
SEQRES 10 B 159 GLU ASP LEU GLY CYS HIS MET ASP ASP VAL ASN VAL LYS
SEQRES 11 B 159 ALA THR THR THR GLU LYS LEU GLY PHE THR GLY ARG GLY
SEQRES 12 B 159 GLU GLY ILE ALA CYS GLU ALA VAL ALA LEU LEU ILE LYS
SEQRES 13 B 159 ALA THR LYS
SEQRES 1 C 159 MET ARG ILE GLY HIS GLY PHE ASP VAL HIS ALA PHE GLY
SEQRES 2 C 159 GLY GLU GLY PRO ILE ILE ILE GLY GLY VAL ARG ILE PRO
SEQRES 3 C 159 TYR GLU LYS GLY LEU LEU ALA HIS SER ASP GLY ASP VAL
SEQRES 4 C 159 ALA LEU HIS ALA LEU THR ASP ALA LEU LEU GLY ALA ALA
SEQRES 5 C 159 ALA LEU GLY ASP ILE GLY LYS LEU PHE PRO ASP THR ASP
SEQRES 6 C 159 PRO ALA PHE LYS GLY ALA ASP SER ARG GLU LEU LEU ARG
SEQRES 7 C 159 GLU ALA TRP ARG ARG ILE GLN ALA LYS GLY TYR THR LEU
SEQRES 8 C 159 GLY ASN VAL ASP VAL THR ILE ILE ALA GLN ALA PRO LYS
SEQRES 9 C 159 MET LEU PRO HIS ILE PRO GLN MET ARG VAL PHE ILE ALA
SEQRES 10 C 159 GLU ASP LEU GLY CYS HIS MET ASP ASP VAL ASN VAL LYS
SEQRES 11 C 159 ALA THR THR THR GLU LYS LEU GLY PHE THR GLY ARG GLY
SEQRES 12 C 159 GLU GLY ILE ALA CYS GLU ALA VAL ALA LEU LEU ILE LYS
SEQRES 13 C 159 ALA THR LYS
SEQRES 1 D 159 MET ARG ILE GLY HIS GLY PHE ASP VAL HIS ALA PHE GLY
SEQRES 2 D 159 GLY GLU GLY PRO ILE ILE ILE GLY GLY VAL ARG ILE PRO
SEQRES 3 D 159 TYR GLU LYS GLY LEU LEU ALA HIS SER ASP GLY ASP VAL
SEQRES 4 D 159 ALA LEU HIS ALA LEU THR ASP ALA LEU LEU GLY ALA ALA
SEQRES 5 D 159 ALA LEU GLY ASP ILE GLY LYS LEU PHE PRO ASP THR ASP
SEQRES 6 D 159 PRO ALA PHE LYS GLY ALA ASP SER ARG GLU LEU LEU ARG
SEQRES 7 D 159 GLU ALA TRP ARG ARG ILE GLN ALA LYS GLY TYR THR LEU
SEQRES 8 D 159 GLY ASN VAL ASP VAL THR ILE ILE ALA GLN ALA PRO LYS
SEQRES 9 D 159 MET LEU PRO HIS ILE PRO GLN MET ARG VAL PHE ILE ALA
SEQRES 10 D 159 GLU ASP LEU GLY CYS HIS MET ASP ASP VAL ASN VAL LYS
SEQRES 11 D 159 ALA THR THR THR GLU LYS LEU GLY PHE THR GLY ARG GLY
SEQRES 12 D 159 GLU GLY ILE ALA CYS GLU ALA VAL ALA LEU LEU ILE LYS
SEQRES 13 D 159 ALA THR LYS
SEQRES 1 E 159 MET ARG ILE GLY HIS GLY PHE ASP VAL HIS ALA PHE GLY
SEQRES 2 E 159 GLY GLU GLY PRO ILE ILE ILE GLY GLY VAL ARG ILE PRO
SEQRES 3 E 159 TYR GLU LYS GLY LEU LEU ALA HIS SER ASP GLY ASP VAL
SEQRES 4 E 159 ALA LEU HIS ALA LEU THR ASP ALA LEU LEU GLY ALA ALA
SEQRES 5 E 159 ALA LEU GLY ASP ILE GLY LYS LEU PHE PRO ASP THR ASP
SEQRES 6 E 159 PRO ALA PHE LYS GLY ALA ASP SER ARG GLU LEU LEU ARG
SEQRES 7 E 159 GLU ALA TRP ARG ARG ILE GLN ALA LYS GLY TYR THR LEU
SEQRES 8 E 159 GLY ASN VAL ASP VAL THR ILE ILE ALA GLN ALA PRO LYS
SEQRES 9 E 159 MET LEU PRO HIS ILE PRO GLN MET ARG VAL PHE ILE ALA
SEQRES 10 E 159 GLU ASP LEU GLY CYS HIS MET ASP ASP VAL ASN VAL LYS
SEQRES 11 E 159 ALA THR THR THR GLU LYS LEU GLY PHE THR GLY ARG GLY
SEQRES 12 E 159 GLU GLY ILE ALA CYS GLU ALA VAL ALA LEU LEU ILE LYS
SEQRES 13 E 159 ALA THR LYS
SEQRES 1 F 159 MET ARG ILE GLY HIS GLY PHE ASP VAL HIS ALA PHE GLY
SEQRES 2 F 159 GLY GLU GLY PRO ILE ILE ILE GLY GLY VAL ARG ILE PRO
SEQRES 3 F 159 TYR GLU LYS GLY LEU LEU ALA HIS SER ASP GLY ASP VAL
SEQRES 4 F 159 ALA LEU HIS ALA LEU THR ASP ALA LEU LEU GLY ALA ALA
SEQRES 5 F 159 ALA LEU GLY ASP ILE GLY LYS LEU PHE PRO ASP THR ASP
SEQRES 6 F 159 PRO ALA PHE LYS GLY ALA ASP SER ARG GLU LEU LEU ARG
SEQRES 7 F 159 GLU ALA TRP ARG ARG ILE GLN ALA LYS GLY TYR THR LEU
SEQRES 8 F 159 GLY ASN VAL ASP VAL THR ILE ILE ALA GLN ALA PRO LYS
SEQRES 9 F 159 MET LEU PRO HIS ILE PRO GLN MET ARG VAL PHE ILE ALA
SEQRES 10 F 159 GLU ASP LEU GLY CYS HIS MET ASP ASP VAL ASN VAL LYS
SEQRES 11 F 159 ALA THR THR THR GLU LYS LEU GLY PHE THR GLY ARG GLY
SEQRES 12 F 159 GLU GLY ILE ALA CYS GLU ALA VAL ALA LEU LEU ILE LYS
SEQRES 13 F 159 ALA THR LYS
HET ZN A1900 1
HET 1AA A1901 37
HET GPP A7903 19
HET ZN B2900 1
HET ZN C3900 1
HET 1AA C2901 37
HET 1AA C3901 37
HET ZN D4900 1
HET 1AA D6901 37
HET GPP D8903 19
HET ZN E5900 1
HET 1AA E4901 37
HET 1AA E5901 37
HET ZN F6900 1
HETNAM ZN ZINC ION
HETNAM 1AA 5'-O-[({[(2-{[(2-AMINOPHENYL)CARBONYL]OXY}ETHYL)
HETNAM 2 1AA OXY]PHOSPHINATO}OXY)PHOSPHINATO]CYTIDINE
HETNAM GPP GERANYL DIPHOSPHATE
FORMUL 7 ZN 6(ZN 2+)
FORMUL 8 1AA 6(C18 H24 N4 O13 P2)
FORMUL 9 GPP 2(C10 H20 O7 P2)
FORMUL 21 HOH *233(H2 O)
HELIX 1 1 ASP A 38 ALA A 52 1 15
HELIX 2 2 ASP A 56 PHE A 61 1 6
HELIX 3 3 ASP A 65 LYS A 69 5 5
HELIX 4 4 ASP A 72 ALA A 86 1 15
HELIX 5 5 HIS A 108 LEU A 120 1 13
HELIX 6 6 HIS A 123 ASP A 125 5 3
HELIX 7 7 LEU A 137 ARG A 142 1 6
HELIX 8 8 ASP B 38 ALA B 52 1 15
HELIX 9 9 ASP B 56 PHE B 61 1 6
HELIX 10 10 ASP B 65 LYS B 69 5 5
HELIX 11 11 ASP B 72 LYS B 87 1 16
HELIX 12 12 MET B 105 PRO B 107 5 3
HELIX 13 13 HIS B 108 GLY B 121 1 14
HELIX 14 14 HIS B 123 ASP B 125 5 3
HELIX 15 15 LEU B 137 ARG B 142 1 6
HELIX 16 16 ASP C 38 ALA C 53 1 16
HELIX 17 17 ASP C 65 LYS C 69 5 5
HELIX 18 18 ASP C 72 LYS C 87 1 16
HELIX 19 19 MET C 105 PRO C 107 5 3
HELIX 20 20 HIS C 108 LEU C 120 1 13
HELIX 21 21 HIS C 123 ASP C 125 5 3
HELIX 22 22 LEU C 137 ARG C 142 1 6
HELIX 23 23 ASP D 38 ALA D 52 1 15
HELIX 24 24 ASP D 56 PHE D 61 1 6
HELIX 25 25 ASP D 72 LYS D 87 1 16
HELIX 26 26 HIS D 108 LEU D 120 1 13
HELIX 27 27 HIS D 123 ASP D 125 5 3
HELIX 28 28 LEU D 137 ARG D 142 1 6
HELIX 29 29 ASP E 38 ALA E 52 1 15
HELIX 30 30 ASP E 56 PHE E 61 1 6
HELIX 31 31 ASP E 72 LYS E 87 1 16
HELIX 32 32 HIS E 108 GLY E 121 1 14
HELIX 33 33 HIS E 123 ASP E 125 5 3
HELIX 34 34 LEU E 137 ARG E 142 1 6
HELIX 35 35 ASP F 38 ALA F 52 1 15
HELIX 36 36 ASP F 56 PHE F 61 1 6
HELIX 37 37 ASP F 72 ALA F 86 1 15
HELIX 38 38 HIS F 108 GLY F 121 1 14
HELIX 39 39 HIS F 123 ASP F 125 5 3
HELIX 40 40 LEU F 137 ARG F 142 1 6
SHEET 1 A 4 ARG A 2 ALA A 11 0
SHEET 2 A 4 GLY A 145 ILE A 155 -1 O ALA A 150 N GLY A 6
SHEET 3 A 4 THR A 90 ILE A 99 -1 N THR A 97 O GLU A 149
SHEET 4 A 4 VAL A 127 THR A 132 1 O LYS A 130 N ILE A 98
SHEET 1 B 2 ILE A 18 ILE A 20 0
SHEET 2 B 2 VAL A 23 ILE A 25 -1 O ILE A 25 N ILE A 18
SHEET 1 C 5 LEU B 31 LEU B 32 0
SHEET 2 C 5 ARG B 2 PHE B 12 -1 N ALA B 11 O LEU B 32
SHEET 3 C 5 GLY B 145 ILE B 155 -1 O ALA B 150 N GLY B 6
SHEET 4 C 5 THR B 90 ILE B 99 -1 N THR B 97 O GLU B 149
SHEET 5 C 5 VAL B 127 THR B 132 1 O LYS B 130 N ILE B 98
SHEET 1 D 2 ILE B 18 ILE B 20 0
SHEET 2 D 2 VAL B 23 ILE B 25 -1 O ILE B 25 N ILE B 18
SHEET 1 E 5 GLY C 30 LEU C 31 0
SHEET 2 E 5 ARG C 2 GLY C 13 -1 N GLY C 13 O GLY C 30
SHEET 3 E 5 GLY C 145 ILE C 155 -1 O ALA C 150 N GLY C 6
SHEET 4 E 5 THR C 90 ILE C 99 -1 N THR C 97 O GLU C 149
SHEET 5 E 5 VAL C 127 THR C 132 1 O LYS C 130 N ILE C 98
SHEET 1 F 2 ILE C 18 ILE C 20 0
SHEET 2 F 2 VAL C 23 ILE C 25 -1 O ILE C 25 N ILE C 18
SHEET 1 G 5 LEU D 31 LEU D 32 0
SHEET 2 G 5 ARG D 2 PHE D 12 -1 N ALA D 11 O LEU D 32
SHEET 3 G 5 GLY D 145 ILE D 155 -1 O ALA D 150 N GLY D 6
SHEET 4 G 5 THR D 90 ILE D 99 -1 N THR D 97 O GLU D 149
SHEET 5 G 5 VAL D 127 THR D 132 1 O LYS D 130 N ILE D 98
SHEET 1 H 2 ILE D 18 ILE D 20 0
SHEET 2 H 2 VAL D 23 ILE D 25 -1 O ILE D 25 N ILE D 18
SHEET 1 I 4 ARG E 2 ALA E 11 0
SHEET 2 I 4 GLY E 145 ILE E 155 -1 O LEU E 154 N ARG E 2
SHEET 3 I 4 THR E 90 ILE E 99 -1 N THR E 97 O GLU E 149
SHEET 4 I 4 VAL E 127 THR E 132 1 O LYS E 130 N ILE E 98
SHEET 1 J 2 ILE E 18 ILE E 20 0
SHEET 2 J 2 VAL E 23 ILE E 25 -1 O ILE E 25 N ILE E 18
SHEET 1 K 4 ARG F 2 ALA F 11 0
SHEET 2 K 4 GLY F 145 ILE F 155 -1 O ALA F 150 N GLY F 6
SHEET 3 K 4 THR F 90 ILE F 99 -1 N THR F 97 O GLU F 149
SHEET 4 K 4 VAL F 127 THR F 132 1 O LYS F 130 N ILE F 98
SHEET 1 L 2 ILE F 18 ILE F 20 0
SHEET 2 L 2 VAL F 23 ILE F 25 -1 O ILE F 25 N ILE F 18
LINK OD2 ASP A 8 ZN ZN A1900 1555 1555 2.17
LINK NE2 HIS A 10 ZN ZN A1900 1555 1555 2.14
LINK ND1 HIS A 42 ZN ZN A1900 1555 1555 2.35
LINK ZN ZN A1900 O7 1AA A1901 1555 1555 2.70
LINK OD2 ASP B 8 ZN ZN B2900 1555 1555 2.06
LINK NE2 HIS B 10 ZN ZN B2900 1555 1555 2.13
LINK ND1 HIS B 42 ZN ZN B2900 1555 1555 2.19
LINK ZN ZN B2900 O8 1AA C2901 1555 1555 2.47
LINK OD2 ASP C 8 ZN ZN C3900 1555 1555 2.07
LINK NE2 HIS C 10 ZN ZN C3900 1555 1555 2.11
LINK ND1 HIS C 42 ZN ZN C3900 1555 1555 2.21
LINK ZN ZN C3900 O8 1AA C3901 1555 1555 1.97
LINK OD2 ASP D 8 ZN ZN D4900 1555 1555 2.03
LINK NE2 HIS D 10 ZN ZN D4900 1555 1555 2.14
LINK ND1 HIS D 42 ZN ZN D4900 1555 1555 2.16
LINK O8 1AA D6901 ZN ZN F6900 1555 1555 2.02
LINK OD2 ASP E 8 ZN ZN E5900 1555 1555 2.07
LINK NE2 HIS E 10 ZN ZN E5900 1555 1555 2.01
LINK ND1 HIS E 42 ZN ZN E5900 1555 1555 2.06
LINK ZN ZN E5900 O8 1AA E5901 1555 1555 1.92
LINK OD2 ASP F 8 ZN ZN F6900 1555 1555 2.18
LINK NE2 HIS F 10 ZN ZN F6900 1555 1555 2.26
LINK ND1 HIS F 42 ZN ZN F6900 1555 1555 2.15
CISPEP 1 ALA A 102 PRO A 103 0 9.56
CISPEP 2 ALA B 102 PRO B 103 0 -2.89
CISPEP 3 GLY C 16 PRO C 17 0 2.49
CISPEP 4 ALA C 102 PRO C 103 0 -1.18
CISPEP 5 GLY D 16 PRO D 17 0 -0.09
CISPEP 6 ALA E 102 PRO E 103 0 -3.27
CISPEP 7 GLY F 16 PRO F 17 0 1.60
CISPEP 8 ALA F 102 PRO F 103 0 3.45
SITE 1 AC1 5 ASP A 8 HIS A 10 HIS A 34 HIS A 42
SITE 2 AC1 5 1AA A1901
SITE 1 AC2 4 ASP B 8 HIS B 10 HIS B 42 1AA C2901
SITE 1 AC3 4 ASP C 8 HIS C 10 HIS C 42 1AA C3901
SITE 1 AC4 4 ASP D 8 HIS D 10 HIS D 42 1AA E4901
SITE 1 AC5 4 ASP E 8 HIS E 10 HIS E 42 1AA E5901
SITE 1 AC6 4 1AA D6901 ASP F 8 HIS F 10 HIS F 42
SITE 1 AC7 17 ASP A 8 HIS A 10 HIS A 34 ASP A 56
SITE 2 AC7 17 GLY A 58 PHE A 61 ZN A1900 HOH A7911
SITE 3 AC7 17 ALA B 100 PRO B 103 LYS B 104 MET B 105
SITE 4 AC7 17 LEU B 106 ALA B 131 THR B 132 THR B 133
SITE 5 AC7 17 GLU B 135
SITE 1 AC8 18 ASP B 8 HIS B 34 SER B 35 HIS B 42
SITE 2 AC8 18 ASP B 56 ILE B 57 GLY B 58 LEU B 76
SITE 3 AC8 18 ZN B2900 ALA C 100 PRO C 103 LYS C 104
SITE 4 AC8 18 MET C 105 LEU C 106 ALA C 131 THR C 132
SITE 5 AC8 18 THR C 133 HOH C3942
SITE 1 AC9 21 ALA A 100 PRO A 103 LYS A 104 MET A 105
SITE 2 AC9 21 LEU A 106 ALA A 131 THR A 132 THR A 133
SITE 3 AC9 21 GLU A 135 ASP C 8 HIS C 10 ALA C 33
SITE 4 AC9 21 HIS C 34 SER C 35 HIS C 42 ASP C 56
SITE 5 AC9 21 ILE C 57 GLY C 58 ASP C 63 ZN C3900
SITE 6 AC9 21 HOH C3927
SITE 1 BC1 13 GLY A 138 PHE A 139 THR A 140 ARG A 142
SITE 2 BC1 13 PHE B 7 GLY B 138 PHE B 139 ARG B 142
SITE 3 BC1 13 PHE C 7 GLY C 138 PHE C 139 ARG C 142
SITE 4 BC1 13 GLU C 149
SITE 1 BC2 18 ASP D 8 HIS D 10 HIS D 34 SER D 35
SITE 2 BC2 18 ASP D 56 GLY D 58 ZN D4900 HOH D8912
SITE 3 BC2 18 ALA E 100 PRO E 103 LYS E 104 MET E 105
SITE 4 BC2 18 LEU E 106 ALA E 131 THR E 132 THR E 133
SITE 5 BC2 18 GLU E 135 HOH E5934
SITE 1 BC3 24 ASP E 8 HIS E 10 HIS E 34 SER E 35
SITE 2 BC3 24 HIS E 42 ASP E 56 ILE E 57 GLY E 58
SITE 3 BC3 24 PHE E 61 ASP E 63 LEU E 76 ZN E5900
SITE 4 BC3 24 HOH E5903 HOH E5912 ALA F 100 PRO F 103
SITE 5 BC3 24 LYS F 104 MET F 105 LEU F 106 ALA F 131
SITE 6 BC3 24 THR F 132 THR F 133 GLU F 135 HOH F6926
SITE 1 BC4 19 ALA D 100 PRO D 103 LYS D 104 MET D 105
SITE 2 BC4 19 LEU D 106 ALA D 131 THR D 132 THR D 133
SITE 3 BC4 19 GLU D 135 ASP F 8 HIS F 10 HIS F 34
SITE 4 BC4 19 ASP F 56 ILE F 57 GLY F 58 PHE F 61
SITE 5 BC4 19 LEU F 76 ZN F6900 HOH F6903
SITE 1 BC5 12 GLY D 138 PHE D 139 ARG D 142 GLU D 149
SITE 2 BC5 12 PHE E 7 GLY E 138 PHE E 139 ARG E 142
SITE 3 BC5 12 PHE F 7 GLY F 138 PHE F 139 ARG F 142
CRYST1 54.033 115.269 87.609 90.00 90.18 90.00 P 1 21 1 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.018507 0.000000 0.000058 0.00000
SCALE2 0.000000 0.008675 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011414 0.00000
(ATOM LINES ARE NOT SHOWN.)
END