HEADER TRANSFERASE/TRANSFERASE INHIBITOR 02-APR-13 4JZB
TITLE CRYSTAL STRUCTURE OF LESHMANIASIS MAJOR FARNESYL DIPHOSPHATE SYNTHASE
TITLE 2 IN COMPLEX WITH 1-(2-HYDROXY-2,2-DIPHOSPHONOETHYL)-3-
TITLE 3 PHENYLPYRIDINIUM, IPP AND CA2+
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FARNESYL PYROPHOSPHATE SYNTHASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 2.5.1.1, 2.5.1.10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;
SOURCE 3 ORGANISM_TAXID: 5664;
SOURCE 4 GENE: FPPS, LMJF_22_1360;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS GERANYL TRANSFERASE, FPPS, FARNESYL PYROPHOSPHATE SYNTHASE, FARNESYL
KEYWDS 2 DIPHOSPHATE SYNTHASE, CYTOSOLIC, TRANSFERASE-TRANSFERASE INHIBITOR
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.ARIPIRALA,L.M.AMZEL,S.GABELLI
REVDAT 4 15-NOV-17 4JZB 1 REMARK
REVDAT 3 24-SEP-14 4JZB 1 JRNL
REVDAT 2 05-MAR-14 4JZB 1 JRNL
REVDAT 1 12-FEB-14 4JZB 0
JRNL AUTH S.ARIPIRALA,D.GONZALEZ-PACANOWSKA,E.OLDFIELD,M.KAISER,
JRNL AUTH 2 L.M.AMZEL,S.B.GABELLI
JRNL TITL STRUCTURAL AND THERMODYNAMIC BASIS OF THE INHIBITION OF
JRNL TITL 2 LEISHMANIA MAJOR FARNESYL DIPHOSPHATE SYNTHASE BY
JRNL TITL 3 NITROGEN-CONTAINING BISPHOSPHONATES.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 802 2014
JRNL REFN ISSN 0907-4449
JRNL PMID 24598749
JRNL DOI 10.1107/S1399004713033221
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 66.96
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 58732
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2971
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3837
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 192
REMARK 3 BIN FREE R VALUE : 0.3250
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5752
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 696
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.72000
REMARK 3 B22 (A**2) : -0.67000
REMARK 3 B33 (A**2) : -0.05000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.159
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.140
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.884
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.950
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6027 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8195 ; 1.076 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 742 ; 4.298 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 272 ;36.973 ;24.485
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1035 ;12.503 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ; 9.251 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 911 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4512 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 3320 ; 0.192 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4225 ; 0.298 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 675 ; 0.116 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 35 ; 0.162 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 52 ; 0.165 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 35 ; 0.115 ; 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): 3647 ; 0.600 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5884 ; 1.181 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2475 ; 1.710 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2304 ; 2.667 ; 5.000
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 : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4JZB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078693.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : VARIMAX MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 58810
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 66.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 6.800
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.47300
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: MOLECULAR REPLACEMENT
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 (%): 45.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 40.18050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.53700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.98350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.53700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.18050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.98350
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -136.0 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: 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 119 -76.64 -112.01
REMARK 500 THR A 120 156.23 75.62
REMARK 500 THR A 208 -50.33 -128.32
REMARK 500 VAL B 119 -78.35 -112.48
REMARK 500 THR B 120 157.66 78.84
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 NA A 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 561 O
REMARK 620 2 HOH A 554 O 68.9
REMARK 620 3 GLU A 270 OE1 153.6 86.6
REMARK 620 4 HOH A 671 O 89.4 158.2 114.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA B 406 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 562 O
REMARK 620 2 HOH B 615 O 64.5
REMARK 620 3 HOH B 766 O 89.0 153.4
REMARK 620 4 GLU B 270 OE1 147.8 87.4 117.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 511 O
REMARK 620 2 ASP B 98 OD1 85.0
REMARK 620 3 ASP B 102 OD2 93.7 87.3
REMARK 620 4 HOH B 503 O 90.1 174.6 90.9
REMARK 620 5 P2H B 402 O16 97.2 87.9 167.7 94.8
REMARK 620 6 P2H B 402 O10 170.6 88.2 79.5 96.5 89.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 102 OD2
REMARK 620 2 ASP A 98 OD2 92.7
REMARK 620 3 HOH A 502 O 94.4 86.3
REMARK 620 4 HOH A 503 O 89.9 176.0 90.5
REMARK 620 5 P2H A 405 O16 169.0 86.5 96.5 91.5
REMARK 620 6 P2H A 405 O10 81.2 88.1 172.7 95.3 87.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 405 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH B 504 O
REMARK 620 2 ASP B 98 OD2 82.1
REMARK 620 3 HOH B 512 O 80.4 96.2
REMARK 620 4 ASP B 102 OD2 157.9 84.2 118.4
REMARK 620 5 HOH B 502 O 90.3 172.0 85.0 102.3
REMARK 620 6 ASP B 102 OD1 150.0 92.5 70.8 47.7 95.4
REMARK 620 7 P2H B 402 O10 88.7 95.6 162.7 75.4 81.7 121.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 504 O
REMARK 620 2 ASP A 98 OD1 86.1
REMARK 620 3 HOH A 501 O 86.8 172.5
REMARK 620 4 ASP A 102 OD2 160.7 82.7 104.7
REMARK 620 5 HOH A 511 O 82.3 95.0 81.8 114.3
REMARK 620 6 ASP A 102 OD1 148.6 88.4 96.5 46.9 67.4
REMARK 620 7 P2H A 405 O10 89.7 98.9 83.3 76.6 163.5 121.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 250 OD2
REMARK 620 2 HOH B 505 O 91.5
REMARK 620 3 HOH B 506 O 165.0 80.2
REMARK 620 4 HOH B 514 O 84.6 94.3 83.5
REMARK 620 5 P2H B 402 O11 95.4 89.3 97.0 176.5
REMARK 620 6 P2H B 402 O15 92.5 171.5 97.3 93.6 82.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 250 OD2
REMARK 620 2 HOH A 505 O 91.5
REMARK 620 3 HOH A 506 O 162.7 80.9
REMARK 620 4 HOH A 512 O 79.2 95.2 86.0
REMARK 620 5 P2H A 405 O11 98.3 90.1 97.2 174.2
REMARK 620 6 P2H A 405 O15 91.5 172.8 97.9 91.8 82.9
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPE A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P2H A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P2H B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 406
DBREF 4JZB A 2 362 UNP Q4QBL1 Q4QBL1_LEIMA 2 362
DBREF 4JZB B 2 362 UNP Q4QBL1 Q4QBL1_LEIMA 2 362
SEQADV 4JZB FME A 1 UNP Q4QBL1 EXPRESSION TAG
SEQADV 4JZB FME B 1 UNP Q4QBL1 EXPRESSION TAG
SEQRES 1 A 362 FME ALA HIS MET GLU ARG PHE GLN LYS VAL TYR GLU GLU
SEQRES 2 A 362 VAL GLN GLU PHE LEU LEU GLY ASP ALA GLU LYS ARG PHE
SEQRES 3 A 362 GLU MET ASP VAL HIS ARG LYS GLY TYR LEU LYS SER MET
SEQRES 4 A 362 MET ASP THR THR CYS LEU GLY GLY LYS TYR ASN ARG GLY
SEQRES 5 A 362 LEU CYS VAL VAL ASP VAL ALA GLU ALA MET ALA LYS ASP
SEQRES 6 A 362 THR GLN MET ASP ALA ALA ALA MET GLU ARG VAL LEU HIS
SEQRES 7 A 362 ASP ALA CYS VAL CYS GLY TRP MET ILE GLU MET LEU GLN
SEQRES 8 A 362 ALA HIS PHE LEU VAL GLU ASP ASP ILE MET ASP HIS SER
SEQRES 9 A 362 LYS THR ARG ARG GLY LYS PRO CYS TRP TYR LEU HIS PRO
SEQRES 10 A 362 GLY VAL THR ALA GLN VAL ALA ILE ASN ASP GLY LEU ILE
SEQRES 11 A 362 LEU LEU ALA TRP ALA THR GLN MET ALA LEU HIS TYR PHE
SEQRES 12 A 362 ALA ASP ARG PRO PHE LEU ALA GLU VAL LEU ARG VAL PHE
SEQRES 13 A 362 HIS ASP VAL ASP LEU THR THR THR ILE GLY GLN LEU TYR
SEQRES 14 A 362 ASP VAL THR SER MET VAL ASP SER ALA LYS LEU ASP ALA
SEQRES 15 A 362 LYS VAL ALA HIS ALA ASN THR THR ASP TYR VAL GLU TYR
SEQRES 16 A 362 THR PRO PHE ASN HIS ARG ARG ILE VAL VAL TYR LYS THR
SEQRES 17 A 362 ALA TYR TYR THR TYR TRP LEU PRO LEU VAL MET GLY LEU
SEQRES 18 A 362 LEU VAL SER GLY THR LEU GLU LYS VAL ASP LYS LYS ALA
SEQRES 19 A 362 THR HIS LYS VAL ALA MET VAL MET GLY GLU TYR PHE GLN
SEQRES 20 A 362 VAL GLN ASP ASP VAL MET ASP CYS PHE THR PRO PRO GLU
SEQRES 21 A 362 LYS LEU GLY LYS ILE GLY THR ASP ILE GLU ASP ALA LYS
SEQRES 22 A 362 CYS SER TRP LEU ALA VAL THR PHE LEU THR THR ALA PRO
SEQRES 23 A 362 ALA GLU LYS VAL ALA GLU PHE LYS ALA ASN TYR GLY SER
SEQRES 24 A 362 THR ASP PRO ALA ALA VAL ALA VAL ILE LYS GLN LEU TYR
SEQRES 25 A 362 THR GLU GLN ASN LEU LEU ALA ARG PHE GLU GLU TYR GLU
SEQRES 26 A 362 LYS ALA VAL VAL ALA GLU VAL GLU GLN LEU ILE ALA ALA
SEQRES 27 A 362 LEU GLU ALA GLN ASN ALA ALA PHE ALA ALA SER VAL LYS
SEQRES 28 A 362 VAL LEU TRP SER LYS THR TYR LYS ARG GLN LYS
SEQRES 1 B 362 FME ALA HIS MET GLU ARG PHE GLN LYS VAL TYR GLU GLU
SEQRES 2 B 362 VAL GLN GLU PHE LEU LEU GLY ASP ALA GLU LYS ARG PHE
SEQRES 3 B 362 GLU MET ASP VAL HIS ARG LYS GLY TYR LEU LYS SER MET
SEQRES 4 B 362 MET ASP THR THR CYS LEU GLY GLY LYS TYR ASN ARG GLY
SEQRES 5 B 362 LEU CYS VAL VAL ASP VAL ALA GLU ALA MET ALA LYS ASP
SEQRES 6 B 362 THR GLN MET ASP ALA ALA ALA MET GLU ARG VAL LEU HIS
SEQRES 7 B 362 ASP ALA CYS VAL CYS GLY TRP MET ILE GLU MET LEU GLN
SEQRES 8 B 362 ALA HIS PHE LEU VAL GLU ASP ASP ILE MET ASP HIS SER
SEQRES 9 B 362 LYS THR ARG ARG GLY LYS PRO CYS TRP TYR LEU HIS PRO
SEQRES 10 B 362 GLY VAL THR ALA GLN VAL ALA ILE ASN ASP GLY LEU ILE
SEQRES 11 B 362 LEU LEU ALA TRP ALA THR GLN MET ALA LEU HIS TYR PHE
SEQRES 12 B 362 ALA ASP ARG PRO PHE LEU ALA GLU VAL LEU ARG VAL PHE
SEQRES 13 B 362 HIS ASP VAL ASP LEU THR THR THR ILE GLY GLN LEU TYR
SEQRES 14 B 362 ASP VAL THR SER MET VAL ASP SER ALA LYS LEU ASP ALA
SEQRES 15 B 362 LYS VAL ALA HIS ALA ASN THR THR ASP TYR VAL GLU TYR
SEQRES 16 B 362 THR PRO PHE ASN HIS ARG ARG ILE VAL VAL TYR LYS THR
SEQRES 17 B 362 ALA TYR TYR THR TYR TRP LEU PRO LEU VAL MET GLY LEU
SEQRES 18 B 362 LEU VAL SER GLY THR LEU GLU LYS VAL ASP LYS LYS ALA
SEQRES 19 B 362 THR HIS LYS VAL ALA MET VAL MET GLY GLU TYR PHE GLN
SEQRES 20 B 362 VAL GLN ASP ASP VAL MET ASP CYS PHE THR PRO PRO GLU
SEQRES 21 B 362 LYS LEU GLY LYS ILE GLY THR ASP ILE GLU ASP ALA LYS
SEQRES 22 B 362 CYS SER TRP LEU ALA VAL THR PHE LEU THR THR ALA PRO
SEQRES 23 B 362 ALA GLU LYS VAL ALA GLU PHE LYS ALA ASN TYR GLY SER
SEQRES 24 B 362 THR ASP PRO ALA ALA VAL ALA VAL ILE LYS GLN LEU TYR
SEQRES 25 B 362 THR GLU GLN ASN LEU LEU ALA ARG PHE GLU GLU TYR GLU
SEQRES 26 B 362 LYS ALA VAL VAL ALA GLU VAL GLU GLN LEU ILE ALA ALA
SEQRES 27 B 362 LEU GLU ALA GLN ASN ALA ALA PHE ALA ALA SER VAL LYS
SEQRES 28 B 362 VAL LEU TRP SER LYS THR TYR LYS ARG GLN LYS
MODRES 4JZB FME A 1 MET N-FORMYLMETHIONINE
MODRES 4JZB FME B 1 MET N-FORMYLMETHIONINE
HET FME A 1 10
HET FME B 1 10
HET CA A 401 1
HET CA A 402 1
HET CA A 403 1
HET IPE A 404 14
HET P2H A 405 23
HET NA A 406 1
HET IPE B 401 14
HET P2H B 402 23
HET CA B 403 1
HET CA B 404 1
HET CA B 405 1
HET NA B 406 1
HETNAM FME N-FORMYLMETHIONINE
HETNAM CA CALCIUM ION
HETNAM IPE 3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE
HETNAM P2H 1-(2-HYDROXY-2,2-DIPHOSPHONOETHYL)-3-PHENYLPYRIDINIUM
HETNAM NA SODIUM ION
HETSYN IPE ISOPENTENYL PYROPHOSPHATE
FORMUL 1 FME 2(C6 H11 N O3 S)
FORMUL 3 CA 6(CA 2+)
FORMUL 6 IPE 2(C5 H12 O7 P2)
FORMUL 7 P2H 2(C13 H16 N O7 P2 1+)
FORMUL 8 NA 2(NA 1+)
FORMUL 15 HOH *696(H2 O)
HELIX 1 1 HIS A 3 GLU A 27 1 25
HELIX 2 2 ASP A 29 LEU A 45 1 17
HELIX 3 3 TYR A 49 THR A 66 1 18
HELIX 4 4 ASP A 69 ASP A 102 1 34
HELIX 5 5 TRP A 113 HIS A 116 5 4
HELIX 6 6 THR A 120 PHE A 143 1 24
HELIX 7 7 PHE A 148 THR A 172 1 25
HELIX 8 8 ASP A 176 LEU A 180 5 5
HELIX 9 9 THR A 196 THR A 208 1 13
HELIX 10 10 THR A 208 TYR A 213 1 6
HELIX 11 11 TYR A 213 SER A 224 1 12
HELIX 12 12 THR A 226 VAL A 230 5 5
HELIX 13 13 ASP A 231 THR A 257 1 27
HELIX 14 14 PRO A 258 GLY A 263 1 6
HELIX 15 15 SER A 275 ALA A 285 1 11
HELIX 16 16 PRO A 286 ALA A 295 1 10
HELIX 17 17 ASP A 301 GLN A 315 1 15
HELIX 18 18 ASN A 316 ASN A 343 1 28
HELIX 19 19 ASN A 343 TYR A 358 1 16
HELIX 20 20 HIS B 3 GLU B 27 1 25
HELIX 21 21 ASP B 29 LEU B 45 1 17
HELIX 22 22 TYR B 49 THR B 66 1 18
HELIX 23 23 ASP B 69 ASP B 102 1 34
HELIX 24 24 TRP B 113 HIS B 116 5 4
HELIX 25 25 THR B 120 PHE B 143 1 24
HELIX 26 26 PHE B 148 THR B 172 1 25
HELIX 27 27 ASP B 176 LEU B 180 5 5
HELIX 28 28 THR B 196 THR B 208 1 13
HELIX 29 29 THR B 208 TYR B 213 1 6
HELIX 30 30 TYR B 213 SER B 224 1 12
HELIX 31 31 THR B 226 VAL B 230 5 5
HELIX 32 32 ASP B 231 THR B 257 1 27
HELIX 33 33 PRO B 258 GLY B 263 1 6
HELIX 34 34 SER B 275 ALA B 285 1 11
HELIX 35 35 PRO B 286 TYR B 297 1 12
HELIX 36 36 ASP B 301 GLN B 315 1 15
HELIX 37 37 ASN B 316 ALA B 341 1 26
HELIX 38 38 ASN B 343 TYR B 358 1 16
SHEET 1 A 2 THR A 106 ARG A 107 0
SHEET 2 A 2 LYS A 110 PRO A 111 -1 O LYS A 110 N ARG A 107
SHEET 1 B 2 THR B 106 ARG B 107 0
SHEET 2 B 2 LYS B 110 PRO B 111 -1 O LYS B 110 N ARG B 107
LINK C FME A 1 N ALA A 2 1555 1555 1.34
LINK C FME B 1 N ALA B 2 1555 1555 1.34
LINK NA NA A 406 O HOH A 561 1555 1555 2.01
LINK NA NA B 406 O HOH B 562 1555 1555 2.18
LINK NA NA A 406 O HOH A 554 1555 1555 2.20
LINK CA CA B 403 O HOH B 511 1555 1555 2.21
LINK OD2 ASP A 102 CA CA A 401 1555 1555 2.22
LINK OD1 ASP B 98 CA CA B 403 1555 1555 2.23
LINK OD2 ASP A 98 CA CA A 401 1555 1555 2.24
LINK CA CA A 401 O HOH A 502 1555 1555 2.25
LINK OD2 ASP B 102 CA CA B 403 1555 1555 2.27
LINK NA NA B 406 O HOH B 615 1555 1555 2.28
LINK CA CA B 403 O HOH B 503 1555 1555 2.29
LINK CA CA B 405 O HOH B 504 1555 1555 2.30
LINK CA CA A 402 O HOH A 504 1555 1555 2.32
LINK OD2 ASP B 98 CA CA B 405 1555 1555 2.32
LINK CA CA A 401 O HOH A 503 1555 1555 2.34
LINK OD2 ASP B 250 CA CA B 404 1555 1555 2.34
LINK OD1 ASP A 98 CA CA A 402 1555 1555 2.35
LINK OD2 ASP A 250 CA CA A 403 1555 1555 2.35
LINK CA CA B 405 O HOH B 512 1555 1555 2.37
LINK CA CA A 403 O HOH A 505 1555 1555 2.37
LINK CA CA A 403 O HOH A 506 1555 1555 2.38
LINK CA CA A 402 O HOH A 501 1555 1555 2.38
LINK OD2 ASP B 102 CA CA B 405 1555 1555 2.39
LINK CA CA B 405 O HOH B 502 1555 1555 2.40
LINK CA CA B 404 O HOH B 505 1555 1555 2.42
LINK OD2 ASP A 102 CA CA A 402 1555 1555 2.44
LINK CA CA B 404 O HOH B 506 1555 1555 2.45
LINK CA CA B 404 O HOH B 514 1555 1555 2.46
LINK CA CA A 403 O HOH A 512 1555 1555 2.50
LINK CA CA A 402 O HOH A 511 1555 1555 2.53
LINK NA NA B 406 O HOH B 766 1555 1555 2.72
LINK OE1 GLU B 270 NA NA B 406 1555 1555 2.81
LINK OD1 ASP B 102 CA CA B 405 1555 1555 2.89
LINK OE1 GLU A 270 NA NA A 406 1555 1555 2.91
LINK OD1 ASP A 102 CA CA A 402 1555 1555 2.92
LINK NA NA A 406 O HOH A 671 1555 1555 2.92
LINK O16 P2H B 402 CA CA B 403 1555 1555 2.06
LINK CA CA A 401 O16 P2H A 405 1555 1555 2.11
LINK O11 P2H B 402 CA CA B 404 1555 1555 2.24
LINK CA CA A 403 O11 P2H A 405 1555 1555 2.25
LINK O15 P2H B 402 CA CA B 404 1555 1555 2.27
LINK O10 P2H B 402 CA CA B 403 1555 1555 2.31
LINK CA CA A 403 O15 P2H A 405 1555 1555 2.32
LINK CA CA A 401 O10 P2H A 405 1555 1555 2.33
LINK CA CA A 402 O10 P2H A 405 1555 1555 2.34
LINK O10 P2H B 402 CA CA B 405 1555 1555 2.40
SITE 1 AC1 6 ASP A 98 ASP A 102 CA A 402 P2H A 405
SITE 2 AC1 6 HOH A 502 HOH A 503
SITE 1 AC2 7 ASP A 98 ASP A 102 CA A 401 P2H A 405
SITE 2 AC2 7 HOH A 501 HOH A 504 HOH A 511
SITE 1 AC3 5 ASP A 250 P2H A 405 HOH A 505 HOH A 506
SITE 2 AC3 5 HOH A 512
SITE 1 AC4 18 GLY A 47 LYS A 48 ARG A 51 GLN A 91
SITE 2 AC4 18 ARG A 108 THR A 208 TYR A 211 PHE A 246
SITE 3 AC4 18 GLN A 247 ASP A 250 P2H A 405 HOH A 509
SITE 4 AC4 18 HOH A 531 HOH A 536 HOH A 552 HOH A 587
SITE 5 AC4 18 HOH A 617 HOH A 645
SITE 1 AC5 18 PHE A 94 ASP A 98 MET A 101 ASP A 102
SITE 2 AC5 18 ARG A 107 THR A 163 GLN A 167 LYS A 207
SITE 3 AC5 18 THR A 208 ASP A 250 LYS A 264 CA A 401
SITE 4 AC5 18 CA A 402 CA A 403 IPE A 404 HOH A 504
SITE 5 AC5 18 HOH A 513 HOH A 532
SITE 1 AC6 5 GLY A 266 GLU A 270 HOH A 554 HOH A 561
SITE 2 AC6 5 HOH A 671
SITE 1 AC7 18 GLY B 47 LYS B 48 ARG B 51 GLN B 91
SITE 2 AC7 18 ARG B 108 THR B 208 TYR B 211 PHE B 246
SITE 3 AC7 18 GLN B 247 ASP B 250 P2H B 402 HOH B 509
SITE 4 AC7 18 HOH B 523 HOH B 527 HOH B 542 HOH B 580
SITE 5 AC7 18 HOH B 622 HOH B 651
SITE 1 AC8 18 PHE B 94 ASP B 98 MET B 101 ASP B 102
SITE 2 AC8 18 ARG B 107 THR B 163 GLN B 167 LYS B 207
SITE 3 AC8 18 THR B 208 ASP B 250 LYS B 264 IPE B 401
SITE 4 AC8 18 CA B 403 CA B 404 CA B 405 HOH B 504
SITE 5 AC8 18 HOH B 513 HOH B 545
SITE 1 AC9 6 ASP B 98 ASP B 102 P2H B 402 CA B 405
SITE 2 AC9 6 HOH B 503 HOH B 511
SITE 1 BC1 5 ASP B 250 P2H B 402 HOH B 505 HOH B 506
SITE 2 BC1 5 HOH B 514
SITE 1 BC2 7 ASP B 98 ASP B 102 P2H B 402 CA B 403
SITE 2 BC2 7 HOH B 502 HOH B 504 HOH B 512
SITE 1 BC3 5 GLY B 266 GLU B 270 HOH B 562 HOH B 615
SITE 2 BC3 5 HOH B 766
CRYST1 80.361 85.967 107.074 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012444 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009339 0.00000
HETATM 1 N FME A 1 34.627 48.074 25.308 1.00 41.41 N
HETATM 2 CN FME A 1 33.637 49.016 25.460 1.00 41.99 C
HETATM 3 O1 FME A 1 32.548 48.664 25.891 1.00 43.96 O
HETATM 4 CA FME A 1 35.577 48.487 24.274 1.00 40.56 C
HETATM 5 CB FME A 1 36.996 48.204 24.767 1.00 41.43 C
HETATM 6 CG FME A 1 37.391 49.204 25.853 1.00 43.61 C
HETATM 7 SD FME A 1 38.652 48.540 26.895 1.00 47.58 S
HETATM 8 CE FME A 1 39.156 49.808 28.016 1.00 46.89 C
HETATM 9 C FME A 1 35.259 47.760 22.994 1.00 38.91 C
HETATM 10 O FME A 1 34.603 46.713 23.031 1.00 38.68 O
(ATOM LINES ARE NOT SHOWN.)
END
