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HEADER HYDROLASE 12-FEB-08 3C8H
TITLE CRYSTAL STRUCTURE OF THE ENTEROBACTIN ESTERASE IROD FROM
TITLE 2 SHIGELLA FLEXNERI IN THE PRESENCE OF 2,3-DI-HYDROXY-N-
TITLE 3 BENZOYL-SERINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENTEROCHELIN ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
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 ALPHA-BETA-ALPHA SANDWICH, IROD, IRON AQUISITION,
KEYWDS 2 STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 3 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,N.MALTSEVA,R.ABERGEL,D.HOLZLE,K.RAYMOND,A.JOACHIMIAK,
AUTHOR 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 26-FEB-08 3C8H 0
JRNL AUTH Y.KIM,N.MALTSEVA,R.ABERGEL,D.HOLZLE,K.RAYMOND,
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. 2.48 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.48
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 NUMBER OF REFLECTIONS : 56986
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 2886
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 2.48
REMARK 3 BIN RESOLUTION RANGE LOW : 2.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1673
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3900
REMARK 3 BIN FREE R VALUE SET COUNT : 110
REMARK 3 BIN FREE R VALUE : 0.3200
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 53.56
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.15
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.61000
REMARK 3 B22 (A**2) : 11.16000
REMARK 3 B33 (A**2) : -6.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.006 NULL
REMARK 3 ANGLE : 0.683 NULL
REMARK 3 CHIRALITY : 0.049 NULL
REMARK 3 PLANARITY : 0.003 NULL
REMARK 3 DIHEDRAL : 14.225 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 397
REMARK 3 ORIGIN FOR THE GROUP (A): 26.8095 3.1795 19.2529
REMARK 3 T TENSOR
REMARK 3 T11: 0.1267 T22: 0.2401
REMARK 3 T33: 0.1373 T12: -0.0476
REMARK 3 T13: -0.0065 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 0.1269 L22: 0.0234
REMARK 3 L33: 0.1390 L12: -0.0290
REMARK 3 L13: 0.0065 L23: 0.0002
REMARK 3 S TENSOR
REMARK 3 S11: -0.0415 S12: 0.1200 S13: 0.0553
REMARK 3 S21: 0.0082 S22: 0.1080 S23: -0.0265
REMARK 3 S31: 0.0570 S32: -0.0587 S33: -0.0663
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 6 B 397
REMARK 3 ORIGIN FOR THE GROUP (A): 27.1462 -1.8309 54.8134
REMARK 3 T TENSOR
REMARK 3 T11: 0.1755 T22: 0.2456
REMARK 3 T33: 0.1696 T12: 0.0948
REMARK 3 T13: -0.0148 T23: -0.0588
REMARK 3 L TENSOR
REMARK 3 L11: 0.0502 L22: 0.0886
REMARK 3 L33: 0.0877 L12: 0.0410
REMARK 3 L13: 0.0231 L23: -0.0249
REMARK 3 S TENSOR
REMARK 3 S11: -0.0424 S12: -0.0734 S13: -0.0155
REMARK 3 S21: 0.0083 S22: 0.1226 S23: -0.0301
REMARK 3 S31: -0.0344 S32: -0.0947 S33: -0.0796
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 : C 6 C 397
REMARK 3 ORIGIN FOR THE GROUP (A): 82.9249 26.2557 23.4061
REMARK 3 T TENSOR
REMARK 3 T11: 0.1528 T22: 0.1579
REMARK 3 T33: 0.1348 T12: -0.0575
REMARK 3 T13: -0.0018 T23: -0.0257
REMARK 3 L TENSOR
REMARK 3 L11: 0.0839 L22: 0.0512
REMARK 3 L33: 0.0763 L12: -0.0459
REMARK 3 L13: -0.0099 L23: -0.0177
REMARK 3 S TENSOR
REMARK 3 S11: -0.0425 S12: 0.0314 S13: 0.0279
REMARK 3 S21: -0.0070 S22: 0.0983 S23: -0.0160
REMARK 3 S31: 0.0506 S32: -0.0424 S33: -0.0551
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 : D 6 D 397
REMARK 3 ORIGIN FOR THE GROUP (A): 82.5244 21.2868 59.0346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1285 T22: 0.1040
REMARK 3 T33: 0.1002 T12: 0.0282
REMARK 3 T13: -0.0009 T23: -0.0135
REMARK 3 L TENSOR
REMARK 3 L11: 0.1110 L22: 0.1117
REMARK 3 L33: 0.0411 L12: -0.0698
REMARK 3 L13: -0.0198 L23: 0.0202
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: -0.0725 S13: 0.0118
REMARK 3 S21: -0.0762 S22: 0.0340 S23: 0.0066
REMARK 3 S31: -0.0137 S32: 0.0118 S33: -0.0244
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. TWINNING: TWIN LAW=-H,-K,L, TWIN
REMARK 3 FRACTION: 0.502. 2. STRUCTURE HAS BEEN REFINED USING
REMARK 3 PHENIX.REFINE, PHENIX.XTRIAGE PROGRAMS. 3. WHEN REFINING TLS,
REMARK 3 THE OUTPUT PDB FILE ALWAYS HAS THE ANISOU RECORDS FOR THE
REMARK 3 ATOMS INVOLVED IN TLS GROUPS. THE ANISOTROPIC B-FACTOR IN
REMARK 3 ANISOU RECORDS IS THE TOTAL B-FACTOR (B_TLS + B_INDIVIDUAL).
REMARK 3 THE ISOTROPIC EQUIVALENT B-FACTOR IN ATOM RECORDS IS THE MEAN
REMARK 3 OF THE TRACE OF THE ANISOU MATRIX DIVIDED BY 10000 AND
REMARK 3 MULTIPLIED BY 8*PI^2 AND REPRESENTS THE ISOTROPIC EQUIVALENT
REMARK 3 OF THE TOTAL B-FACTOR (B_TLS + B_INDIVIDUAL). TO OBTAIN THE
REMARK 3 INDIVIDUAL B-FACTORS, ONE NEEDS TO COMPUTE THE TLS COMPONENT
REMARK 3 (B_TLS) USING THE TLS RECORDS IN THE PDB FILE HEADER AND THEN
REMARK 3 SUBTRACT IT FROM THE TOTAL B-FACTORS (ON THE ANISOU RECORDS).
REMARK 4
REMARK 4 3C8H 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 RCSB046473.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-NOV-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.60
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) : 0.9793
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-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57160
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.480
REMARK 200 RESOLUTION RANGE LOW (A) : 47.230
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 FOR THE DATA SET : 8.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.46200
REMARK 200 FOR SHELL : 2.120
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2B20
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20 % PEG 3000, 0.1 M TRI-SODIUM
REMARK 280 CITRATE PH 5.6, 3 MM DHBS, 1 MM FECL3, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 24.38850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMER
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 3120 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 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMER
REMARK 350 SOFTWARE USED: PISA
REMARK 350 AVERAGE BURIED SURFACE AREA: 3140 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 LEU A 4
REMARK 465 LYS A 5
REMARK 465 ASP A 58
REMARK 465 HIS A 59
REMARK 465 HIS A 60
REMARK 465 GLN A 61
REMARK 465 ASN A 62
REMARK 465 SER A 63
REMARK 465 THR A 190
REMARK 465 ALA A 191
REMARK 465 GLU A 192
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 LEU B 4
REMARK 465 LYS B 5
REMARK 465 HIS B 59
REMARK 465 HIS B 60
REMARK 465 GLN B 61
REMARK 465 ASN B 62
REMARK 465 SER B 63
REMARK 465 GLN B 64
REMARK 465 THR B 190
REMARK 465 ALA B 191
REMARK 465 GLU B 192
REMARK 465 ASP B 398
REMARK 465 ARG B 399
REMARK 465 SER B 400
REMARK 465 SER C -2
REMARK 465 ASN C -1
REMARK 465 ALA C 0
REMARK 465 MSE C 1
REMARK 465 THR C 2
REMARK 465 ALA C 3
REMARK 465 LEU C 4
REMARK 465 LYS C 5
REMARK 465 ASP C 58
REMARK 465 HIS C 59
REMARK 465 HIS C 60
REMARK 465 GLN C 61
REMARK 465 ASN C 62
REMARK 465 SER C 63
REMARK 465 THR C 190
REMARK 465 ALA C 191
REMARK 465 GLU C 192
REMARK 465 ASP C 398
REMARK 465 ARG C 399
REMARK 465 SER C 400
REMARK 465 SER D -2
REMARK 465 ASN D -1
REMARK 465 ALA D 0
REMARK 465 MSE D 1
REMARK 465 THR D 2
REMARK 465 ALA D 3
REMARK 465 LEU D 4
REMARK 465 LYS D 5
REMARK 465 HIS D 59
REMARK 465 HIS D 60
REMARK 465 GLN D 61
REMARK 465 ASN D 62
REMARK 465 SER D 63
REMARK 465 GLN D 64
REMARK 465 THR D 190
REMARK 465 ALA D 191
REMARK 465 GLU D 192
REMARK 465 ASP D 398
REMARK 465 ARG D 399
REMARK 465 SER D 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 NH2 ARG B 179 OE1 GLU B 243 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 THR A 57 C THR A 57 O 0.134
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 LEU A 137 42.93 -100.00
REMARK 500 PRO A 210 120.30 -39.94
REMARK 500 ILE A 235 -77.27 80.61
REMARK 500 CYS A 246 51.73 39.97
REMARK 500 SER A 281 -107.86 58.31
REMARK 500 LEU A 359 43.83 -94.01
REMARK 500 SER A 365 35.61 -98.76
REMARK 500 PRO A 394 -3.73 -59.75
REMARK 500 ASP B 25 -18.82 -47.20
REMARK 500 PRO B 107 -169.16 -75.49
REMARK 500 ILE B 235 -75.36 76.74
REMARK 500 SER B 281 -102.19 63.78
REMARK 500 GLU B 318 152.11 -48.09
REMARK 500 ALA B 332 44.15 -106.87
REMARK 500 LEU C 137 34.14 -90.40
REMARK 500 ILE C 235 -82.41 81.43
REMARK 500 SER C 281 -107.24 53.83
REMARK 500 SER C 305 32.19 74.11
REMARK 500 ALA C 332 43.73 -97.71
REMARK 500 LEU C 359 31.38 -94.22
REMARK 500 ASP D 126 108.53 -55.62
REMARK 500 LEU D 137 42.89 -101.73
REMARK 500 ILE D 235 -74.89 79.17
REMARK 500 SER D 281 -107.27 58.45
REMARK 500 ALA D 332 44.45 -99.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY B 314 GLY B 315 -145.27
REMARK 500 GLU C 345 PRO C 346 -145.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M=MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C 425 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH D 435 DISTANCE = 6.65 ANGSTROMS
REMARK 525 HOH C 446 DISTANCE = 5.79 ANGSTROMS
REMARK 525 HOH A 451 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH B 470 DISTANCE = 6.41 ANGSTROMS
REMARK 525 HOH A 460 DISTANCE = 5.09 ANGSTROMS
REMARK 525 HOH D 461 DISTANCE = 5.69 ANGSTROMS
REMARK 525 HOH B 475 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 469 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH D 469 DISTANCE = 7.09 ANGSTROMS
REMARK 525 HOH D 470 DISTANCE = 5.16 ANGSTROMS
REMARK 525 HOH D 474 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH D 476 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH C 478 DISTANCE = 5.66 ANGSTROMS
REMARK 525 HOH C 489 DISTANCE = 5.37 ANGSTROMS
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: 3C87 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ENTEROBACTIN ESTERASE IROD FROM
REMARK 900 SHIGELLA FLEXNERI IN THE PRESENCE OF ENTEROBACTIN
REMARK 900 RELATED ID: 3C8D RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE ENTEROBACTIN ESTERASE IROD FROM
REMARK 900 SHIGELLA FLEXNERI IN THE PRESENCE OF 2,3-DI-HYDROXY-N-
REMARK 900 BENZOYL-GLYCINE
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
DBREF 3C8H A 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
DBREF 3C8H B 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
DBREF 3C8H C 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
DBREF 3C8H D 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
SEQADV 3C8H SER A -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ASN A -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ALA A 0 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H SER B -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ASN B -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ALA B 0 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H SER C -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ASN C -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ALA C 0 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H SER D -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ASN D -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8H ALA D 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
SEQRES 1 C 403 SER ASN ALA MSE THR ALA LEU LYS VAL GLY SER GLU SER
SEQRES 2 C 403 TRP TRP GLN SER LYS HIS GLY PRO GLU TRP GLN ARG LEU
SEQRES 3 C 403 ASN ASP GLU MSE PHE GLU VAL THR PHE TRP TRP ARG ASP
SEQRES 4 C 403 PRO GLN GLY SER GLU GLU TYR SER THR ILE LYS ARG VAL
SEQRES 5 C 403 TRP VAL TYR ILE THR GLY VAL THR ASP HIS HIS GLN ASN
SEQRES 6 C 403 SER GLN PRO GLN SER MSE GLN ARG ILE ALA GLY THR ASP
SEQRES 7 C 403 VAL TRP GLN TRP THR THR GLN LEU ASN ALA ASN TRP ARG
SEQRES 8 C 403 GLY SER TYR CYS PHE ILE PRO THR GLU ARG ASP ASP ILE
SEQRES 9 C 403 PHE SER ALA PRO SER PRO ASP ARG LEU GLU LEU ARG GLU
SEQRES 10 C 403 GLY TRP ARG LYS LEU LEU PRO GLN ALA ILE ALA ASP PRO
SEQRES 11 C 403 LEU ASN PRO GLN SER TRP LYS GLY GLY LEU GLY HIS ALA
SEQRES 12 C 403 VAL SER ALA LEU GLU MSE PRO GLN ALA PRO LEU GLN PRO
SEQRES 13 C 403 GLY TRP ASP CYS PRO GLN ALA PRO GLU ILE PRO ALA LYS
SEQRES 14 C 403 GLU ILE ILE TRP LYS SER GLU ARG LEU LYS ASN SER ARG
SEQRES 15 C 403 ARG VAL TRP ILE PHE THR THR GLY ASP VAL THR ALA GLU
SEQRES 16 C 403 GLU ARG PRO LEU ALA VAL LEU LEU ASP GLY GLU PHE TRP
SEQRES 17 C 403 ALA GLN SER MSE PRO VAL TRP PRO VAL LEU THR SER LEU
SEQRES 18 C 403 THR HIS ARG GLN GLN LEU PRO PRO ALA VAL TYR VAL LEU
SEQRES 19 C 403 ILE ASP ALA ILE ASP THR THR HIS ARG ALA HIS GLU LEU
SEQRES 20 C 403 PRO CYS ASN ALA ASP PHE TRP LEU ALA VAL GLN GLN GLU
SEQRES 21 C 403 LEU LEU PRO LEU VAL LYS VAL ILE ALA PRO PHE SER ASP
SEQRES 22 C 403 ARG ALA ASP ARG THR VAL VAL ALA GLY GLN SER PHE GLY
SEQRES 23 C 403 GLY LEU SER ALA LEU TYR ALA GLY LEU HIS TRP PRO GLU
SEQRES 24 C 403 ARG PHE GLY CYS VAL LEU SER GLN SER GLY SER TYR TRP
SEQRES 25 C 403 TRP PRO HIS ARG GLY GLY GLN GLN GLU GLY VAL LEU LEU
SEQRES 26 C 403 GLU LYS LEU LYS ALA GLY GLU VAL SER ALA GLU GLY LEU
SEQRES 27 C 403 ARG ILE VAL LEU GLU ALA GLY ILE ARG GLU PRO MSE ILE
SEQRES 28 C 403 MSE ARG ALA ASN GLN ALA LEU TYR ALA GLN LEU HIS PRO
SEQRES 29 C 403 ILE LYS GLU SER ILE PHE TRP ARG GLN VAL ASP GLY GLY
SEQRES 30 C 403 HIS ASP ALA LEU CYS TRP ARG GLY GLY LEU MSE GLN GLY
SEQRES 31 C 403 LEU ILE ASP LEU TRP GLN PRO LEU PHE HIS ASP ARG SER
SEQRES 1 D 403 SER ASN ALA MSE THR ALA LEU LYS VAL GLY SER GLU SER
SEQRES 2 D 403 TRP TRP GLN SER LYS HIS GLY PRO GLU TRP GLN ARG LEU
SEQRES 3 D 403 ASN ASP GLU MSE PHE GLU VAL THR PHE TRP TRP ARG ASP
SEQRES 4 D 403 PRO GLN GLY SER GLU GLU TYR SER THR ILE LYS ARG VAL
SEQRES 5 D 403 TRP VAL TYR ILE THR GLY VAL THR ASP HIS HIS GLN ASN
SEQRES 6 D 403 SER GLN PRO GLN SER MSE GLN ARG ILE ALA GLY THR ASP
SEQRES 7 D 403 VAL TRP GLN TRP THR THR GLN LEU ASN ALA ASN TRP ARG
SEQRES 8 D 403 GLY SER TYR CYS PHE ILE PRO THR GLU ARG ASP ASP ILE
SEQRES 9 D 403 PHE SER ALA PRO SER PRO ASP ARG LEU GLU LEU ARG GLU
SEQRES 10 D 403 GLY TRP ARG LYS LEU LEU PRO GLN ALA ILE ALA ASP PRO
SEQRES 11 D 403 LEU ASN PRO GLN SER TRP LYS GLY GLY LEU GLY HIS ALA
SEQRES 12 D 403 VAL SER ALA LEU GLU MSE PRO GLN ALA PRO LEU GLN PRO
SEQRES 13 D 403 GLY TRP ASP CYS PRO GLN ALA PRO GLU ILE PRO ALA LYS
SEQRES 14 D 403 GLU ILE ILE TRP LYS SER GLU ARG LEU LYS ASN SER ARG
SEQRES 15 D 403 ARG VAL TRP ILE PHE THR THR GLY ASP VAL THR ALA GLU
SEQRES 16 D 403 GLU ARG PRO LEU ALA VAL LEU LEU ASP GLY GLU PHE TRP
SEQRES 17 D 403 ALA GLN SER MSE PRO VAL TRP PRO VAL LEU THR SER LEU
SEQRES 18 D 403 THR HIS ARG GLN GLN LEU PRO PRO ALA VAL TYR VAL LEU
SEQRES 19 D 403 ILE ASP ALA ILE ASP THR THR HIS ARG ALA HIS GLU LEU
SEQRES 20 D 403 PRO CYS ASN ALA ASP PHE TRP LEU ALA VAL GLN GLN GLU
SEQRES 21 D 403 LEU LEU PRO LEU VAL LYS VAL ILE ALA PRO PHE SER ASP
SEQRES 22 D 403 ARG ALA ASP ARG THR VAL VAL ALA GLY GLN SER PHE GLY
SEQRES 23 D 403 GLY LEU SER ALA LEU TYR ALA GLY LEU HIS TRP PRO GLU
SEQRES 24 D 403 ARG PHE GLY CYS VAL LEU SER GLN SER GLY SER TYR TRP
SEQRES 25 D 403 TRP PRO HIS ARG GLY GLY GLN GLN GLU GLY VAL LEU LEU
SEQRES 26 D 403 GLU LYS LEU LYS ALA GLY GLU VAL SER ALA GLU GLY LEU
SEQRES 27 D 403 ARG ILE VAL LEU GLU ALA GLY ILE ARG GLU PRO MSE ILE
SEQRES 28 D 403 MSE ARG ALA ASN GLN ALA LEU TYR ALA GLN LEU HIS PRO
SEQRES 29 D 403 ILE LYS GLU SER ILE PHE TRP ARG GLN VAL ASP GLY GLY
SEQRES 30 D 403 HIS ASP ALA LEU CYS TRP ARG GLY GLY LEU MSE GLN GLY
SEQRES 31 D 403 LEU ILE ASP LEU TRP GLN PRO LEU PHE HIS ASP ARG SER
MODRES 3C8H MSE A 27 MET SELENOMETHIONINE
MODRES 3C8H MSE A 68 MET SELENOMETHIONINE
MODRES 3C8H MSE A 146 MET SELENOMETHIONINE
MODRES 3C8H MSE A 209 MET SELENOMETHIONINE
MODRES 3C8H MSE A 347 MET SELENOMETHIONINE
MODRES 3C8H MSE A 349 MET SELENOMETHIONINE
MODRES 3C8H MSE A 385 MET SELENOMETHIONINE
MODRES 3C8H MSE B 27 MET SELENOMETHIONINE
MODRES 3C8H MSE B 68 MET SELENOMETHIONINE
MODRES 3C8H MSE B 146 MET SELENOMETHIONINE
MODRES 3C8H MSE B 209 MET SELENOMETHIONINE
MODRES 3C8H MSE B 347 MET SELENOMETHIONINE
MODRES 3C8H MSE B 349 MET SELENOMETHIONINE
MODRES 3C8H MSE B 385 MET SELENOMETHIONINE
MODRES 3C8H MSE C 27 MET SELENOMETHIONINE
MODRES 3C8H MSE C 68 MET SELENOMETHIONINE
MODRES 3C8H MSE C 146 MET SELENOMETHIONINE
MODRES 3C8H MSE C 209 MET SELENOMETHIONINE
MODRES 3C8H MSE C 347 MET SELENOMETHIONINE
MODRES 3C8H MSE C 349 MET SELENOMETHIONINE
MODRES 3C8H MSE C 385 MET SELENOMETHIONINE
MODRES 3C8H MSE D 27 MET SELENOMETHIONINE
MODRES 3C8H MSE D 68 MET SELENOMETHIONINE
MODRES 3C8H MSE D 146 MET SELENOMETHIONINE
MODRES 3C8H MSE D 209 MET SELENOMETHIONINE
MODRES 3C8H MSE D 347 MET SELENOMETHIONINE
MODRES 3C8H MSE D 349 MET SELENOMETHIONINE
MODRES 3C8H MSE D 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 MSE C 27 8
HET MSE C 68 8
HET MSE C 146 8
HET MSE C 209 8
HET MSE C 347 8
HET MSE C 349 8
HET MSE C 385 8
HET MSE D 27 8
HET MSE D 68 8
HET MSE D 146 8
HET MSE D 209 8
HET MSE D 347 8
HET MSE D 349 8
HET MSE D 385 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 28(C5 H11 N O2 SE)
FORMUL 5 HOH *333(H2 O)
HELIX 1 1 SER A 8 SER A 14 1 7
HELIX 2 2 ASP A 108 LEU A 120 1 13
HELIX 3 3 PRO A 121 ALA A 123 5 3
HELIX 4 4 ASP A 201 SER A 208 1 8
HELIX 5 5 VAL A 211 ARG A 221 1 11
HELIX 6 6 ASP A 236 LEU A 244 1 9
HELIX 7 7 ASN A 247 ALA A 266 1 20
HELIX 8 8 ARG A 271 ARG A 274 5 4
HELIX 9 9 SER A 281 TRP A 294 1 14
HELIX 10 10 GLY A 319 ALA A 327 1 9
HELIX 11 11 GLU A 345 LEU A 359 1 15
HELIX 12 12 ILE A 362 GLU A 364 5 3
HELIX 13 13 ASP A 376 GLN A 393 1 18
HELIX 14 14 PRO A 394 HIS A 397 5 4
HELIX 15 15 SER B 8 SER B 14 1 7
HELIX 16 16 ASP B 108 LEU B 120 1 13
HELIX 17 17 PRO B 121 ALA B 123 5 3
HELIX 18 18 ASP B 201 SER B 208 1 8
HELIX 19 19 VAL B 211 ARG B 221 1 11
HELIX 20 20 ASP B 236 LEU B 244 1 9
HELIX 21 21 ASN B 247 GLU B 257 1 11
HELIX 22 22 GLU B 257 ALA B 266 1 10
HELIX 23 23 ARG B 271 ARG B 274 5 4
HELIX 24 24 SER B 281 TRP B 294 1 14
HELIX 25 25 GLY B 319 ALA B 327 1 9
HELIX 26 26 GLU B 345 LEU B 359 1 15
HELIX 27 27 HIS B 360 GLU B 364 5 5
HELIX 28 28 ASP B 376 TRP B 392 1 17
HELIX 29 29 GLN B 393 PHE B 396 5 4
HELIX 30 30 SER C 8 SER C 14 1 7
HELIX 31 31 ASP C 108 LEU C 120 1 13
HELIX 32 32 PRO C 121 ALA C 123 5 3
HELIX 33 33 ASP C 201 GLN C 207 1 7
HELIX 34 34 VAL C 211 ARG C 221 1 11
HELIX 35 35 ASP C 236 LEU C 244 1 9
HELIX 36 36 ASN C 247 GLU C 257 1 11
HELIX 37 37 GLU C 257 ALA C 266 1 10
HELIX 38 38 ARG C 271 ASP C 273 5 3
HELIX 39 39 SER C 281 TRP C 294 1 14
HELIX 40 40 GLY C 319 ALA C 327 1 9
HELIX 41 41 GLU C 345 LEU C 359 1 15
HELIX 42 42 HIS C 360 GLU C 364 5 5
HELIX 43 43 ASP C 376 TRP C 392 1 17
HELIX 44 44 GLN C 393 HIS C 397 5 5
HELIX 45 45 SER D 10 LYS D 15 5 6
HELIX 46 46 ASP D 108 LEU D 120 1 13
HELIX 47 47 PRO D 121 ALA D 123 5 3
HELIX 48 48 ASP D 201 GLN D 207 1 7
HELIX 49 49 VAL D 211 ARG D 221 1 11
HELIX 50 50 ASP D 236 LEU D 244 1 9
HELIX 51 51 ASN D 247 GLU D 257 1 11
HELIX 52 52 GLU D 257 ALA D 266 1 10
HELIX 53 53 ARG D 271 ARG D 274 5 4
HELIX 54 54 SER D 281 TRP D 294 1 14
HELIX 55 55 GLY D 319 ALA D 327 1 9
HELIX 56 56 GLU D 345 LEU D 359 1 15
HELIX 57 57 HIS D 360 LYS D 363 5 4
HELIX 58 58 ASP D 376 TRP D 392 1 17
HELIX 59 59 GLN D 393 PHE D 396 5 4
SHEET 1 A 4 GLU A 19 ARG A 22 0
SHEET 2 A 4 PHE A 28 ARG A 35 -1 O THR A 31 N GLU A 19
SHEET 3 A 4 VAL A 76 LEU A 83 -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 CYS A 92 N TYR A 52
SHEET 3 B 4 ALA A 140 GLU A 145 -1 O SER A 142 N TYR A 91
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 LEU A 231 N TRP A 182
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 ILE A 337
SHEET 1 D 4 GLU B 19 ARG B 22 0
SHEET 2 D 4 MSE B 27 ARG B 35 -1 O GLU B 29 N GLN B 21
SHEET 3 D 4 VAL B 76 ASN B 84 -1 O TRP B 79 N PHE B 32
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 CYS B 92 N TYR B 52
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 ILE B 183 N LYS B 166
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 200 1 N LEU B 199 O VAL B 230
SHEET 5 F 8 VAL B 276 GLN B 280 1 O ALA B 278 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 ILE B 366 VAL B 371 1 O PHE B 367 N LEU B 339
SHEET 1 G 4 GLU C 19 ASN C 24 0
SHEET 2 G 4 MSE C 27 ARG C 35 -1 O THR C 31 N GLU C 19
SHEET 3 G 4 VAL C 76 LEU C 83 -1 O THR C 81 N VAL C 30
SHEET 4 G 4 GLN C 69 ARG C 70 -1 N GLN C 69 O GLN C 78
SHEET 1 H 2 ARG C 48 VAL C 51 0
SHEET 2 H 2 PHE C 93 THR C 96 -1 O THR C 96 N ARG C 48
SHEET 1 I 3 ARG C 88 TYR C 91 0
SHEET 2 I 3 ALA C 140 GLU C 145 -1 O LEU C 144 N GLY C 89
SHEET 3 I 3 SER C 132 LYS C 134 -1 N TRP C 133 O VAL C 141
SHEET 1 J 8 LYS C 166 LYS C 171 0
SHEET 2 J 8 SER C 178 THR C 186 -1 O ARG C 179 N TRP C 170
SHEET 3 J 8 ALA C 227 ILE C 232 -1 O LEU C 231 N TRP C 182
SHEET 4 J 8 LEU C 196 LEU C 199 1 N ALA C 197 O VAL C 230
SHEET 5 J 8 THR C 275 GLN C 280 1 O VAL C 276 N LEU C 196
SHEET 6 J 8 CYS C 300 GLN C 304 1 O LEU C 302 N VAL C 277
SHEET 7 J 8 ARG C 336 ARG C 344 1 O VAL C 338 N VAL C 301
SHEET 8 J 8 ILE C 366 GLY C 374 1 O PHE C 367 N ILE C 337
SHEET 1 K 4 GLU D 19 ARG D 22 0
SHEET 2 K 4 MSE D 27 ARG D 35 -1 O GLU D 29 N GLN D 21
SHEET 3 K 4 VAL D 76 ASN D 84 -1 O TRP D 77 N TRP D 34
SHEET 4 K 4 GLN D 69 ARG D 70 -1 N GLN D 69 O GLN D 78
SHEET 1 L 4 ARG D 48 ILE D 53 0
SHEET 2 L 4 ARG D 88 THR D 96 -1 O THR D 96 N ARG D 48
SHEET 3 L 4 ALA D 140 GLU D 145 -1 O SER D 142 N TYR D 91
SHEET 4 L 4 SER D 132 LYS D 134 -1 N TRP D 133 O VAL D 141
SHEET 1 M 8 LYS D 166 SER D 172 0
SHEET 2 M 8 ASN D 177 THR D 185 -1 O VAL D 181 N ILE D 168
SHEET 3 M 8 VAL D 228 ILE D 232 -1 O TYR D 229 N PHE D 184
SHEET 4 M 8 LEU D 196 LEU D 199 1 N ALA D 197 O VAL D 230
SHEET 5 M 8 VAL D 276 GLN D 280 1 O ALA D 278 N VAL D 198
SHEET 6 M 8 CYS D 300 GLN D 304 1 O LEU D 302 N VAL D 277
SHEET 7 M 8 ARG D 336 GLY D 342 1 O VAL D 338 N VAL D 301
SHEET 8 M 8 ILE D 366 VAL D 371 1 O PHE D 367 N LEU D 339
CISPEP 1 TRP A 310 PRO A 311 0 1.36
CISPEP 2 TRP B 310 PRO B 311 0 11.67
CISPEP 3 TRP C 310 PRO C 311 0 1.17
CISPEP 4 TRP D 310 PRO D 311 0 5.11
CRYST1 111.508 48.777 156.399 90.00 90.00 90.00 P 1 21 1 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 0.008968 -0.000000 -0.000001 0.00000
SCALE2 0.000000 0.020501 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006394 0.00000
END |