HEADER ISOMERASE/ISOMERASE INHIBITOR 15-JUN-11 3SGW
TITLE CRYSTAL STRUCTURE OF RIBOSE-5-PHOSPHATE ISOMERASE B RPIB FROM
TITLE 2 COCCIDIOIDES IMMITIS SEMI-COVALENTLY BOUND TO MALONIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSE 5-PHOSPHATE ISOMERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.3.1.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COCCIDIOIDES IMMITIS;
SOURCE 3 ORGANISM_COMMON: VALLEY FEVER FUNGUS;
SOURCE 4 ORGANISM_TAXID: 246410;
SOURCE 5 STRAIN: RS;
SOURCE 6 GENE: CIMG_07932;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAVA0421
KEYWDS STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR
KEYWDS 2 INFECTIOUS DISEASE, SSGCID, VALLEY FEVER, COCCIDIOIDOMYCOSIS
KEYWDS 3 IMMITIS, PATHOGENIC FUNGUS, RPIB, DUST-BORNE PATHOGEN, IODOACETIC
KEYWDS 4 ACID, COVALENT INHIBITOR, RIBULOSE-5-PHOSPHATE, RIBOSE-5-PHOSPHATE,
KEYWDS 5 ISOMERASE, ISOMERASE-ISOMERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 4 13-SEP-23 3SGW 1 REMARK SEQADV LINK
REVDAT 3 29-APR-15 3SGW 1 HETSYN
REVDAT 2 26-OCT-11 3SGW 1 JRNL VERSN
REVDAT 1 29-JUN-11 3SGW 0
JRNL AUTH T.E.EDWARDS,A.B.ABRAMOV,E.R.SMITH,R.O.BAYDO,J.T.LEONARD,
JRNL AUTH 2 D.J.LEIBLY,K.B.THOMPKINS,M.C.CLIFTON,A.S.GARDBERG,
JRNL AUTH 3 B.L.STAKER,W.C.VAN VOORHIS,P.J.MYLER,L.J.STEWART
JRNL TITL STRUCTURAL CHARACTERIZATION OF A RIBOSE-5-PHOSPHATE
JRNL TITL 2 ISOMERASE B FROM THE PATHOGENIC FUNGUS COCCIDIOIDES IMMITIS.
JRNL REF BMC STRUCT.BIOL. V. 11 39 2011
JRNL REFN ESSN 1472-6807
JRNL PMID 21995815
JRNL DOI 10.1186/1472-6807-11-39
REMARK 2
REMARK 2 RESOLUTION. 1.70 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 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.08
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 16509
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) : 0.144
REMARK 3 R VALUE (WORKING SET) : 0.142
REMARK 3 FREE R VALUE : 0.175
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 832
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 968
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 79.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.1560
REMARK 3 BIN FREE R VALUE SET COUNT : 55
REMARK 3 BIN FREE R VALUE : 0.1890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1183
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 168
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.01
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.75
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.26000
REMARK 3 B22 (A**2) : 0.68000
REMARK 3 B33 (A**2) : -0.41000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.092
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.235
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.957
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1240 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1683 ; 1.323 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 165 ; 5.100 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 48 ;36.788 ;24.375
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 209 ;10.199 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ; 6.074 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 202 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 917 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 797 ; 0.641 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1285 ; 1.119 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 443 ; 2.024 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 394 ; 3.535 ; 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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 6 A 43
REMARK 3 ORIGIN FOR THE GROUP (A): 34.2517 9.3855 12.0686
REMARK 3 T TENSOR
REMARK 3 T11: -0.0009 T22: 0.0293
REMARK 3 T33: 0.0501 T12: 0.0336
REMARK 3 T13: -0.0046 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 1.0962 L22: 2.8630
REMARK 3 L33: 1.0874 L12: 1.1510
REMARK 3 L13: -0.0283 L23: 0.4532
REMARK 3 S TENSOR
REMARK 3 S11: -0.0137 S12: -0.0391 S13: -0.1466
REMARK 3 S21: 0.0141 S22: 0.0675 S23: -0.2126
REMARK 3 S31: 0.0748 S32: 0.2051 S33: -0.0538
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 44 A 98
REMARK 3 ORIGIN FOR THE GROUP (A): 29.3015 17.5790 4.3904
REMARK 3 T TENSOR
REMARK 3 T11: 0.0266 T22: 0.0197
REMARK 3 T33: 0.0152 T12: 0.0037
REMARK 3 T13: 0.0102 T23: -0.0136
REMARK 3 L TENSOR
REMARK 3 L11: 0.6714 L22: 0.6671
REMARK 3 L33: 0.6017 L12: 0.1969
REMARK 3 L13: 0.0526 L23: 0.0000
REMARK 3 S TENSOR
REMARK 3 S11: 0.0082 S12: 0.0427 S13: -0.0174
REMARK 3 S21: -0.0392 S22: 0.0281 S23: -0.0273
REMARK 3 S31: -0.0162 S32: 0.0166 S33: -0.0363
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 99 A 140
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7120 10.6651 15.2827
REMARK 3 T TENSOR
REMARK 3 T11: 0.0361 T22: 0.0047
REMARK 3 T33: 0.0203 T12: 0.0034
REMARK 3 T13: -0.0004 T23: -0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.4015 L22: 0.6029
REMARK 3 L33: 0.9976 L12: 0.0736
REMARK 3 L13: 0.3333 L23: 0.5660
REMARK 3 S TENSOR
REMARK 3 S11: 0.0156 S12: 0.0038 S13: -0.0305
REMARK 3 S21: 0.0445 S22: 0.0157 S23: 0.0087
REMARK 3 S31: 0.0816 S32: -0.0068 S33: -0.0313
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 141 A 163
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8644 12.6784 -4.3764
REMARK 3 T TENSOR
REMARK 3 T11: 0.0479 T22: 0.0485
REMARK 3 T33: 0.0475 T12: 0.0077
REMARK 3 T13: -0.0523 T23: -0.0418
REMARK 3 L TENSOR
REMARK 3 L11: 0.2639 L22: 1.3298
REMARK 3 L33: 2.8260 L12: 0.8747
REMARK 3 L13: -0.7872 L23: -1.6200
REMARK 3 S TENSOR
REMARK 3 S11: 0.0440 S12: 0.1303 S13: -0.0855
REMARK 3 S21: -0.0744 S22: 0.0812 S23: 0.0716
REMARK 3 S31: 0.2082 S32: 0.0119 S33: -0.1252
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3SGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000066186.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
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 FR-E+ SUPERBRIGHT
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : VARIMAX
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU SATURN 944+
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16561
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.5
REMARK 200 DATA REDUNDANCY : 9.600
REMARK 200 R MERGE (I) : 0.04400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 34.7400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.2
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.25600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.620
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3SDW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.32
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN AT 66 MG/ML WITH 20 MM RIBOSE
REMARK 280 -5-PHOSPHATE AND 12 MM MNCL2. RESERVOIR: 25% PEG 1500 AND 0.1 M
REMARK 280 MIB (MALONIC ACID, IMIDAZOLE, BORIC ACID), WITH 25% ETHYLENE
REMARK 280 GLYCOL AS CRYO-PROTECTION REAGENT, PH 5.0, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.21000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 48.08500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.21000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.08500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.21000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.08500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.21000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 48.08500
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 48.08500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 48.08500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 48.08500
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 48.08500
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 42.21000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 42.21000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 42.21000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 38.73000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 42.21000
REMARK 290 SMTRY3 16 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 38.73000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 42.21000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 14220 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -143.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 42.21000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 48.08500
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 38.73000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 48.08500
REMARK 350 BIOMT1 4 -1.000000 0.000000 0.000000 38.73000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 42.21000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 CL CL A 167 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 186 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 302 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 317 LIES ON A SPECIAL POSITION.
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 -20
REMARK 465 ALA A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 MET A -12
REMARK 465 GLY A -11
REMARK 465 THR A -10
REMARK 465 LEU A -9
REMARK 465 GLU A -8
REMARK 465 ALA A -7
REMARK 465 GLN A -6
REMARK 465 THR A -5
REMARK 465 GLN A -4
REMARK 465 GLY A -3
REMARK 465 PRO A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 THR A 4
REMARK 465 PRO A 5
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 32 CG OD1 OD2
REMARK 470 LYS A 68 CG CD CE NZ
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MLA A 164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 167
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 168
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QD5 RELATED DB: PDB
REMARK 900 C. IMMITIS RPIB IODIDE PHASED
REMARK 900 RELATED ID: 3SDW RELATED DB: PDB
REMARK 900 C. IMMITIS RPIB PHOSPHATE BOUND
REMARK 900 RELATED ID: 3S5P RELATED DB: PDB
REMARK 900 GIARDIA LAMBLIA RPIB
REMARK 900 RELATED ID: COIMA.00584.A RELATED DB: TARGETDB
DBREF 3SGW A 1 163 UNP P0CL19 RPIB_COCIM 1 163
SEQADV 3SGW MET A -20 UNP P0CL19 INITIATING METHIONINE
SEQADV 3SGW ALA A -19 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW HIS A -18 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW HIS A -17 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW HIS A -16 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW HIS A -15 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW HIS A -14 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW HIS A -13 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW MET A -12 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW GLY A -11 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW THR A -10 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW LEU A -9 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW GLU A -8 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW ALA A -7 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW GLN A -6 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW THR A -5 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW GLN A -4 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW GLY A -3 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW PRO A -2 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW GLY A -1 UNP P0CL19 EXPRESSION TAG
SEQADV 3SGW SER A 0 UNP P0CL19 EXPRESSION TAG
SEQRES 1 A 184 MET ALA HIS HIS HIS HIS HIS HIS MET GLY THR LEU GLU
SEQRES 2 A 184 ALA GLN THR GLN GLY PRO GLY SER MET ALA ALA THR PRO
SEQRES 3 A 184 LEU PRO PRO LEU ARG LEU ALA ILE ALA CYS ASP ASP ALA
SEQRES 4 A 184 GLY VAL SER TYR LYS GLU ALA LEU LYS ALA HIS LEU SER
SEQRES 5 A 184 ASP ASN PRO LEU VAL SER SER ILE THR ASP VAL GLY VAL
SEQRES 6 A 184 THR SER THR THR ASP LYS THR ALA TYR PRO HIS VAL ALA
SEQRES 7 A 184 ILE GLN ALA ALA GLN LEU ILE LYS ASP GLY LYS VAL ASP
SEQRES 8 A 184 ARG ALA LEU MET ILE CYS GLY THR GLY LEU GLY VAL ALA
SEQRES 9 A 184 ILE SER ALA ASN LYS VAL PRO GLY ILE ARG ALA VAL THR
SEQRES 10 A 184 ALA HIS ASP THR PHE SER VAL GLU ARG ALA ILE LEU SER
SEQRES 11 A 184 ASN ASP ALA GLN VAL LEU CYS PHE GLY GLN ARG VAL ILE
SEQRES 12 A 184 GLY ILE GLU LEU ALA LYS ARG LEU ALA GLY GLU TRP LEU
SEQRES 13 A 184 THR TYR ARG PHE ASP GLN LYS SER ALA SER ALA GLN LYS
SEQRES 14 A 184 VAL GLN ALA ILE SER ASP TYR GLU LYS LYS PHE VAL GLU
SEQRES 15 A 184 VAL ASN
HET MLA A 164 7
HET EDO A 165 4
HET EDO A 166 8
HET CL A 167 1
HET CL A 168 1
HETNAM MLA MALONIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM CL CHLORIDE ION
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METHANEDICARBOXYLIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 MLA C3 H4 O4
FORMUL 3 EDO 2(C2 H6 O2)
FORMUL 5 CL 2(CL 1-)
FORMUL 7 HOH *168(H2 O)
HELIX 1 1 GLY A 19 SER A 31 1 13
HELIX 2 2 ALA A 52 ASP A 66 1 15
HELIX 3 3 GLY A 79 LYS A 88 1 10
HELIX 4 4 ASP A 99 SER A 109 1 11
HELIX 5 5 GLY A 123 LEU A 135 1 13
HELIX 6 6 SER A 143 LYS A 157 1 15
SHEET 1 A 5 VAL A 36 ASP A 41 0
SHEET 2 A 5 LEU A 9 CYS A 15 1 N LEU A 11 O SER A 38
SHEET 3 A 5 ARG A 71 CYS A 76 1 O ILE A 75 N ALA A 14
SHEET 4 A 5 VAL A 114 GLY A 118 1 O LEU A 115 N MET A 74
SHEET 5 A 5 ALA A 94 THR A 96 1 N VAL A 95 O CYS A 116
LINK SG CYS A 76 C2 MLA A 164 1555 1555 2.18
CISPEP 1 GLY A 43 VAL A 44 0 -3.79
SITE 1 AC1 14 ASP A 16 TYR A 53 CYS A 76 GLY A 77
SITE 2 AC1 14 THR A 78 GLY A 79 LEU A 80 GLY A 81
SITE 3 AC1 14 VAL A 82 ASN A 110 CL A 168 HOH A 308
SITE 4 AC1 14 HOH A 312 HOH A 313
SITE 1 AC2 5 ARG A 71 ASP A 111 ALA A 112 HOH A 183
SITE 2 AC2 5 HOH A 238
SITE 1 AC3 3 LYS A 88 PHE A 159 HOH A 199
SITE 1 AC4 2 ASP A 99 THR A 100
SITE 1 AC5 4 ARG A 120 MLA A 164 HOH A 311 HOH A 313
CRYST1 77.460 84.420 96.170 90.00 90.00 90.00 F 2 2 2 16
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 0.012910 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011846 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010398 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
