longtext: 3C87-pdb

content
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
END