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HEADER HYDROLASE 11-FEB-08 3C87
TITLE CRYSTAL STRUCTURE OF THE ENTEROBACTIN ESTERASE IROD FROM
TITLE 2 SHIGELLA FLEXNERI IN THE PRESENCE OF ENTEROBACTIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTEROCHELIN ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SHIGELLA FLEXNERI 2A STR. 2457T;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: 2457T / SEROTYPE 2A;
SOURCE 5 ATCC: 700930;
SOURCE 6 GENE: FES, S0503, SF0497;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS SIDEROPHORE, IROD, ALPHA-BETA-ALPHA SANDWICH, STRUCTURAL
KEYWDS 2 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST
KEYWDS 3 CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,N.MALTSEVA,R.ABERGEL,K.RAYMOND,D.HOLZLE,A.JOACHIMIAK,
AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 26-FEB-08 3C87 0
JRNL AUTH Y.KIM,N.MALTSEVA,R.ABERGEL,K.RAYMOND,D.HOLZLE,
JRNL AUTH 2 A.JOACHIMIAK
JRNL TITL SIDEROPHORE MEDIATED IRON ACQUISITION: STRUCTURE
JRNL TITL 2 AND SPECIFICITY OF ENTEROBACTIN ESTERASE FROM
JRNL TITL 3 SHIGELLA FLEXNERI.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.17 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.17
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 41249
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2189
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.17
REMARK 3 BIN RESOLUTION RANGE LOW : 2.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2729
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE SET COUNT : 148
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 6697
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.98
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : 0.19000
REMARK 3 B33 (A**2) : -0.15000
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): 0.286
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.209
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.152
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.702
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6607 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9034 ; 1.624 ; 1.927
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 795 ; 6.561 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 323 ;36.741 ;23.622
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1050 ;17.006 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 50 ;16.709 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 931 ; 0.113 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5190 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2850 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4364 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 314 ; 0.159 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 1 ; 0.000 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 48 ; 0.192 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.162 ; 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): 3945 ; 1.004 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6377 ; 1.883 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2909 ; 2.793 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2657 ; 4.277 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 4 A 396
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0198 53.0228 17.6294
REMARK 3 T TENSOR
REMARK 3 T11: -0.0998 T22: -0.0813
REMARK 3 T33: -0.1278 T12: -0.0580
REMARK 3 T13: -0.0014 T23: 0.0057
REMARK 3 L TENSOR
REMARK 3 L11: 0.6195 L22: 1.9945
REMARK 3 L33: 0.8697 L12: -0.4676
REMARK 3 L13: 0.2891 L23: -0.3277
REMARK 3 S TENSOR
REMARK 3 S11: 0.1048 S12: -0.0145 S13: -0.0193
REMARK 3 S21: 0.0534 S22: -0.1213 S23: -0.0267
REMARK 3 S31: -0.0744 S32: 0.0768 S33: 0.0165
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 : B 4 B 396
REMARK 3 ORIGIN FOR THE GROUP (A): 14.1008 53.8797 53.6496
REMARK 3 T TENSOR
REMARK 3 T11: -0.1245 T22: -0.0678
REMARK 3 T33: -0.0881 T12: -0.0131
REMARK 3 T13: 0.0059 T23: -0.0074
REMARK 3 L TENSOR
REMARK 3 L11: 0.7572 L22: 1.9091
REMARK 3 L33: 0.8418 L12: 0.7186
REMARK 3 L13: 0.2274 L23: -0.1199
REMARK 3 S TENSOR
REMARK 3 S11: -0.0243 S12: 0.0321 S13: 0.0482
REMARK 3 S21: -0.1300 S22: 0.0854 S23: 0.0604
REMARK 3 S31: 0.1102 S32: -0.0808 S33: -0.0611
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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 3C87 COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB046463.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 31-OCT-2007
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.20
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43586
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.170
REMARK 200 RESOLUTION RANGE LOW (A) : 46.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 11.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12400
REMARK 200 FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.17
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.7
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.69700
REMARK 200 FOR SHELL : 3.250
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, SHELXL-97, RESOLVE, MLPHARE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 8000, 0.1 M PHOSPHATE-
REMARK 280 CITRATE PH 4.2, 0.2 M NACL, 5 MM ENTEROBACTIN, VAPOR
REMARK 280 DIFFUSION, SITTING 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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-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 SMTRY1 2 -1.000000 0.000000 0.000000 23.65250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.56150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.62250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 75.56150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.65250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.62250
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: MONOMER
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 2800 ANGSTROM**2
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 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 THR A 2
REMARK 465 ALA A 3
REMARK 465 HIS A 60
REMARK 465 GLN A 61
REMARK 465 SER A 106
REMARK 465 GLY A 314
REMARK 465 GLY A 315
REMARK 465 HIS A 397
REMARK 465 ASP A 398
REMARK 465 ARG A 399
REMARK 465 SER A 400
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 HIS B 60
REMARK 465 GLN B 61
REMARK 465 ASN B 62
REMARK 465 PRO B 105
REMARK 465 SER B 106
REMARK 465 PRO B 107
REMARK 465 GLY B 314
REMARK 465 GLY B 315
REMARK 465 HIS B 397
REMARK 465 ASP B 398
REMARK 465 ARG B 399
REMARK 465 SER B 400
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 OD2 ASP A 233 O HOH A 562 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 233 CB - CG - OD1 ANGL. DEV. = 6.4 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 ASN A 24 -169.40 -160.79
REMARK 500 VAL A 56 -56.28 -127.24
REMARK 500 ILE A 235 -64.62 76.79
REMARK 500 SER A 281 -111.02 41.87
REMARK 500 HIS B 16 36.26 -140.64
REMARK 500 ASN B 24 -167.65 -163.40
REMARK 500 VAL B 56 -56.15 -120.02
REMARK 500 THR B 81 -166.35 -129.72
REMARK 500 ILE B 235 -71.90 78.70
REMARK 500 SER B 281 -118.97 54.42
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 501 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 156 O
REMARK 620 2 HOH A 550 O 85.8
REMARK 620 3 HOH A 551 O 88.1 92.4
REMARK 620 4 HOH A 645 O 89.1 87.7 177.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: NA BINDING SITE FOR RESIDUE A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: PO4 BINDING SITE FOR RESIDUE B 502
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC27316 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 2B20 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ENTEROCHELIN ESTERASE IROD FROM
REMARK 900 SHIGELLA FLEXNERI
REMARK 900 RELATED ID: 2QM0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF IROE PROTEIN FROM BACILLUS CEREUS
REMARK 900 RELATED ID: 2GZR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ENTEROBACTIN AND SALMOCHELIN HYDROLASE
REMARK 900 IROE
REMARK 900 RELATED ID: 2GZS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ENTEROBACTIN HYDROLASE IROE COMPLEX
REMARK 900 WITH DFP
REMARK 900 RELATED ID: 3C8D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ENTEROBACTIN ESTERASE IROD FROM
REMARK 900 SHIGELLA FLEXNERI IN THE PRESENCE OF 2,3-DI-HYDROXY-N-
REMARK 900 BENZOYL-GLYCINE
DBREF 3C87 A 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
DBREF 3C87 B 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
SEQADV 3C87 SER A -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C87 ASN A -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C87 ALA A 0 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C87 SER B -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C87 ASN B -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C87 ALA B 0 UNP Q83SB9 EXPRESSION TAG
SEQRES 1 A 403 SER ASN ALA MSE THR ALA LEU LYS VAL GLY SER GLU SER
SEQRES 2 A 403 TRP TRP GLN SER LYS HIS GLY PRO GLU TRP GLN ARG LEU
SEQRES 3 A 403 ASN ASP GLU MSE PHE GLU VAL THR PHE TRP TRP ARG ASP
SEQRES 4 A 403 PRO GLN GLY SER GLU GLU TYR SER THR ILE LYS ARG VAL
SEQRES 5 A 403 TRP VAL TYR ILE THR GLY VAL THR ASP HIS HIS GLN ASN
SEQRES 6 A 403 SER GLN PRO GLN SER MSE GLN ARG ILE ALA GLY THR ASP
SEQRES 7 A 403 VAL TRP GLN TRP THR THR GLN LEU ASN ALA ASN TRP ARG
SEQRES 8 A 403 GLY SER TYR CYS PHE ILE PRO THR GLU ARG ASP ASP ILE
SEQRES 9 A 403 PHE SER ALA PRO SER PRO ASP ARG LEU GLU LEU ARG GLU
SEQRES 10 A 403 GLY TRP ARG LYS LEU LEU PRO GLN ALA ILE ALA ASP PRO
SEQRES 11 A 403 LEU ASN PRO GLN SER TRP LYS GLY GLY LEU GLY HIS ALA
SEQRES 12 A 403 VAL SER ALA LEU GLU MSE PRO GLN ALA PRO LEU GLN PRO
SEQRES 13 A 403 GLY TRP ASP CYS PRO GLN ALA PRO GLU ILE PRO ALA LYS
SEQRES 14 A 403 GLU ILE ILE TRP LYS SER GLU ARG LEU LYS ASN SER ARG
SEQRES 15 A 403 ARG VAL TRP ILE PHE THR THR GLY ASP VAL THR ALA GLU
SEQRES 16 A 403 GLU ARG PRO LEU ALA VAL LEU LEU ASP GLY GLU PHE TRP
SEQRES 17 A 403 ALA GLN SER MSE PRO VAL TRP PRO VAL LEU THR SER LEU
SEQRES 18 A 403 THR HIS ARG GLN GLN LEU PRO PRO ALA VAL TYR VAL LEU
SEQRES 19 A 403 ILE ASP ALA ILE ASP THR THR HIS ARG ALA HIS GLU LEU
SEQRES 20 A 403 PRO CYS ASN ALA ASP PHE TRP LEU ALA VAL GLN GLN GLU
SEQRES 21 A 403 LEU LEU PRO LEU VAL LYS VAL ILE ALA PRO PHE SER ASP
SEQRES 22 A 403 ARG ALA ASP ARG THR VAL VAL ALA GLY GLN SER PHE GLY
SEQRES 23 A 403 GLY LEU SER ALA LEU TYR ALA GLY LEU HIS TRP PRO GLU
SEQRES 24 A 403 ARG PHE GLY CYS VAL LEU SER GLN SER GLY SER TYR TRP
SEQRES 25 A 403 TRP PRO HIS ARG GLY GLY GLN GLN GLU GLY VAL LEU LEU
SEQRES 26 A 403 GLU LYS LEU LYS ALA GLY GLU VAL SER ALA GLU GLY LEU
SEQRES 27 A 403 ARG ILE VAL LEU GLU ALA GLY ILE ARG GLU PRO MSE ILE
SEQRES 28 A 403 MSE ARG ALA ASN GLN ALA LEU TYR ALA GLN LEU HIS PRO
SEQRES 29 A 403 ILE LYS GLU SER ILE PHE TRP ARG GLN VAL ASP GLY GLY
SEQRES 30 A 403 HIS ASP ALA LEU CYS TRP ARG GLY GLY LEU MSE GLN GLY
SEQRES 31 A 403 LEU ILE ASP LEU TRP GLN PRO LEU PHE HIS ASP ARG SER
SEQRES 1 B 403 SER ASN ALA MSE THR ALA LEU LYS VAL GLY SER GLU SER
SEQRES 2 B 403 TRP TRP GLN SER LYS HIS GLY PRO GLU TRP GLN ARG LEU
SEQRES 3 B 403 ASN ASP GLU MSE PHE GLU VAL THR PHE TRP TRP ARG ASP
SEQRES 4 B 403 PRO GLN GLY SER GLU GLU TYR SER THR ILE LYS ARG VAL
SEQRES 5 B 403 TRP VAL TYR ILE THR GLY VAL THR ASP HIS HIS GLN ASN
SEQRES 6 B 403 SER GLN PRO GLN SER MSE GLN ARG ILE ALA GLY THR ASP
SEQRES 7 B 403 VAL TRP GLN TRP THR THR GLN LEU ASN ALA ASN TRP ARG
SEQRES 8 B 403 GLY SER TYR CYS PHE ILE PRO THR GLU ARG ASP ASP ILE
SEQRES 9 B 403 PHE SER ALA PRO SER PRO ASP ARG LEU GLU LEU ARG GLU
SEQRES 10 B 403 GLY TRP ARG LYS LEU LEU PRO GLN ALA ILE ALA ASP PRO
SEQRES 11 B 403 LEU ASN PRO GLN SER TRP LYS GLY GLY LEU GLY HIS ALA
SEQRES 12 B 403 VAL SER ALA LEU GLU MSE PRO GLN ALA PRO LEU GLN PRO
SEQRES 13 B 403 GLY TRP ASP CYS PRO GLN ALA PRO GLU ILE PRO ALA LYS
SEQRES 14 B 403 GLU ILE ILE TRP LYS SER GLU ARG LEU LYS ASN SER ARG
SEQRES 15 B 403 ARG VAL TRP ILE PHE THR THR GLY ASP VAL THR ALA GLU
SEQRES 16 B 403 GLU ARG PRO LEU ALA VAL LEU LEU ASP GLY GLU PHE TRP
SEQRES 17 B 403 ALA GLN SER MSE PRO VAL TRP PRO VAL LEU THR SER LEU
SEQRES 18 B 403 THR HIS ARG GLN GLN LEU PRO PRO ALA VAL TYR VAL LEU
SEQRES 19 B 403 ILE ASP ALA ILE ASP THR THR HIS ARG ALA HIS GLU LEU
SEQRES 20 B 403 PRO CYS ASN ALA ASP PHE TRP LEU ALA VAL GLN GLN GLU
SEQRES 21 B 403 LEU LEU PRO LEU VAL LYS VAL ILE ALA PRO PHE SER ASP
SEQRES 22 B 403 ARG ALA ASP ARG THR VAL VAL ALA GLY GLN SER PHE GLY
SEQRES 23 B 403 GLY LEU SER ALA LEU TYR ALA GLY LEU HIS TRP PRO GLU
SEQRES 24 B 403 ARG PHE GLY CYS VAL LEU SER GLN SER GLY SER TYR TRP
SEQRES 25 B 403 TRP PRO HIS ARG GLY GLY GLN GLN GLU GLY VAL LEU LEU
SEQRES 26 B 403 GLU LYS LEU LYS ALA GLY GLU VAL SER ALA GLU GLY LEU
SEQRES 27 B 403 ARG ILE VAL LEU GLU ALA GLY ILE ARG GLU PRO MSE ILE
SEQRES 28 B 403 MSE ARG ALA ASN GLN ALA LEU TYR ALA GLN LEU HIS PRO
SEQRES 29 B 403 ILE LYS GLU SER ILE PHE TRP ARG GLN VAL ASP GLY GLY
SEQRES 30 B 403 HIS ASP ALA LEU CYS TRP ARG GLY GLY LEU MSE GLN GLY
SEQRES 31 B 403 LEU ILE ASP LEU TRP GLN PRO LEU PHE HIS ASP ARG SER
MODRES 3C87 MSE A 27 MET SELENOMETHIONINE
MODRES 3C87 MSE A 68 MET SELENOMETHIONINE
MODRES 3C87 MSE A 146 MET SELENOMETHIONINE
MODRES 3C87 MSE A 209 MET SELENOMETHIONINE
MODRES 3C87 MSE A 347 MET SELENOMETHIONINE
MODRES 3C87 MSE A 349 MET SELENOMETHIONINE
MODRES 3C87 MSE A 385 MET SELENOMETHIONINE
MODRES 3C87 MSE B 27 MET SELENOMETHIONINE
MODRES 3C87 MSE B 68 MET SELENOMETHIONINE
MODRES 3C87 MSE B 146 MET SELENOMETHIONINE
MODRES 3C87 MSE B 209 MET SELENOMETHIONINE
MODRES 3C87 MSE B 347 MET SELENOMETHIONINE
MODRES 3C87 MSE B 349 MET SELENOMETHIONINE
MODRES 3C87 MSE B 385 MET SELENOMETHIONINE
HET MSE A 27 8
HET MSE A 68 8
HET MSE A 146 8
HET MSE A 209 8
HET MSE A 347 8
HET MSE A 349 8
HET MSE A 385 8
HET MSE B 27 8
HET MSE B 68 8
HET MSE B 146 8
HET MSE B 209 8
HET MSE B 347 8
HET MSE B 349 8
HET MSE B 385 8
HET NA A 501 1
HET PO4 B 502 5
HETNAM MSE SELENOMETHIONINE
HETNAM NA SODIUM ION
HETNAM PO4 PHOSPHATE ION
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 3 NA NA 1+
FORMUL 4 PO4 O4 P 3-
FORMUL 5 HOH *302(H2 O)
HELIX 1 1 SER A 8 SER A 14 1 7
HELIX 2 2 SER A 40 SER A 44 5 5
HELIX 3 3 ASP A 108 LEU A 120 1 13
HELIX 4 4 PRO A 121 ALA A 123 5 3
HELIX 5 5 ASP A 201 SER A 208 1 8
HELIX 6 6 VAL A 211 ARG A 221 1 11
HELIX 7 7 ASP A 236 LEU A 244 1 9
HELIX 8 8 ASN A 247 GLU A 257 1 11
HELIX 9 9 GLU A 257 ALA A 266 1 10
HELIX 10 10 ARG A 271 ARG A 274 5 4
HELIX 11 11 SER A 281 TRP A 294 1 14
HELIX 12 12 GLY A 319 ALA A 327 1 9
HELIX 13 13 GLU A 345 LEU A 359 1 15
HELIX 14 14 HIS A 360 GLU A 364 5 5
HELIX 15 15 ASP A 376 GLN A 393 1 18
HELIX 16 16 PRO A 394 PHE A 396 5 3
HELIX 17 17 SER B 10 LYS B 15 5 6
HELIX 18 18 ASP B 108 LEU B 120 1 13
HELIX 19 19 PRO B 121 ALA B 123 5 3
HELIX 20 20 ASP B 201 SER B 208 1 8
HELIX 21 21 VAL B 211 ARG B 221 1 11
HELIX 22 22 ASP B 236 LEU B 244 1 9
HELIX 23 23 ASN B 247 GLU B 257 1 11
HELIX 24 24 GLU B 257 ALA B 266 1 10
HELIX 25 25 ARG B 271 ARG B 274 5 4
HELIX 26 26 SER B 281 TRP B 294 1 14
HELIX 27 27 GLY B 319 GLY B 328 1 10
HELIX 28 28 GLU B 345 GLN B 358 1 14
HELIX 29 29 ASP B 376 TRP B 392 1 17
HELIX 30 30 GLN B 393 PHE B 396 5 4
SHEET 1 A 4 GLU A 19 ARG A 22 0
SHEET 2 A 4 MSE A 27 ARG A 35 -1 O GLU A 29 N GLN A 21
SHEET 3 A 4 VAL A 76 ASN A 84 -1 O TRP A 79 N PHE A 32
SHEET 4 A 4 GLN A 69 ARG A 70 -1 N GLN A 69 O GLN A 78
SHEET 1 B 4 ARG A 48 ILE A 53 0
SHEET 2 B 4 ARG A 88 THR A 96 -1 O THR A 96 N ARG A 48
SHEET 3 B 4 ALA A 140 GLU A 145 -1 O LEU A 144 N GLY A 89
SHEET 4 B 4 SER A 132 LYS A 134 -1 N TRP A 133 O VAL A 141
SHEET 1 C 8 LYS A 166 SER A 172 0
SHEET 2 C 8 ASN A 177 THR A 185 -1 O ILE A 183 N LYS A 166
SHEET 3 C 8 VAL A 228 ILE A 232 -1 O TYR A 229 N PHE A 184
SHEET 4 C 8 LEU A 196 LEU A 199 1 N LEU A 199 O VAL A 230
SHEET 5 C 8 VAL A 276 GLN A 280 1 O VAL A 276 N VAL A 198
SHEET 6 C 8 CYS A 300 GLN A 304 1 O LEU A 302 N VAL A 277
SHEET 7 C 8 ARG A 336 GLY A 342 1 O VAL A 338 N VAL A 301
SHEET 8 C 8 ILE A 366 VAL A 371 1 O PHE A 367 N LEU A 339
SHEET 1 D 4 GLU B 19 ARG B 22 0
SHEET 2 D 4 MSE B 27 ARG B 35 -1 O THR B 31 N GLU B 19
SHEET 3 D 4 VAL B 76 ASN B 84 -1 O LEU B 83 N PHE B 28
SHEET 4 D 4 GLN B 69 ARG B 70 -1 N GLN B 69 O GLN B 78
SHEET 1 E 4 ARG B 48 ILE B 53 0
SHEET 2 E 4 ARG B 88 THR B 96 -1 O THR B 96 N ARG B 48
SHEET 3 E 4 ALA B 140 GLU B 145 -1 O SER B 142 N TYR B 91
SHEET 4 E 4 SER B 132 LYS B 134 -1 N TRP B 133 O VAL B 141
SHEET 1 F 8 LYS B 166 SER B 172 0
SHEET 2 F 8 ASN B 177 THR B 185 -1 O ARG B 179 N TRP B 170
SHEET 3 F 8 VAL B 228 ILE B 232 -1 O TYR B 229 N PHE B 184
SHEET 4 F 8 LEU B 196 LEU B 199 1 N LEU B 199 O VAL B 230
SHEET 5 F 8 VAL B 276 GLN B 280 1 O VAL B 276 N VAL B 198
SHEET 6 F 8 CYS B 300 GLN B 304 1 O LEU B 302 N VAL B 277
SHEET 7 F 8 ARG B 336 GLY B 342 1 O VAL B 338 N VAL B 301
SHEET 8 F 8 SER B 365 VAL B 371 1 O SER B 365 N ILE B 337
LINK O ASP A 156 NA NA A 501 1555 1555 2.41
LINK NA NA A 501 O HOH A 550 1555 1555 2.58
LINK NA NA A 501 O HOH A 551 1555 1555 2.45
LINK NA NA A 501 O HOH A 645 1555 1555 2.58
CISPEP 1 TRP A 310 PRO A 311 0 2.34
CISPEP 2 TRP B 310 PRO B 311 0 -3.05
SITE 1 AC1 2 ASP A 156 ASP B 156
SITE 1 AC2 6 SER B 331 ALA B 332 GLU B 333 HIS B 360
SITE 2 AC2 6 LYS B 363 GLU B 364
CRYST1 47.305 113.245 151.123 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 0.021139 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008830 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006617 0.00000
TER 3179 PHE A 396
TER 6391 PHE B 396
MASTER 411 0 16 30 32 0 3 6 6697 2 122 62
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