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HEADER HYDROLASE 11-FEB-08 3C8D
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-GLYCINE
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 3C8D 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.0
REMARK 3 NUMBER OF REFLECTIONS : 149377
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) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.150
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.970
REMARK 3 FREE R VALUE TEST SET COUNT : 14889
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW : 1.83
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5615
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 644
REMARK 3 BIN FREE R VALUE : 0.3400
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 : 0.35
REMARK 3 B_SOL : 42.52
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) : 26.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.03000
REMARK 3 B22 (A**2) : -7.16000
REMARK 3 B33 (A**2) : 9.19000
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 0.58000
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: 0.3540
REMARK 3 OPERATOR: H,-K,-L
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 NULL
REMARK 3 ANGLE : 0.637 NULL
REMARK 3 CHIRALITY : 0.049 NULL
REMARK 3 PLANARITY : 0.003 NULL
REMARK 3 DIHEDRAL : 12.042 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): 1.3076 -0.2853 1.3719
REMARK 3 T TENSOR
REMARK 3 T11: 0.0811 T22: 0.0920
REMARK 3 T33: 0.1068 T12: -0.0028
REMARK 3 T13: 0.0225 T23: -0.0195
REMARK 3 L TENSOR
REMARK 3 L11: 0.0937 L22: 0.0265
REMARK 3 L33: 0.0625 L12: 0.0222
REMARK 3 L13: -0.0145 L23: -0.0190
REMARK 3 S TENSOR
REMARK 3 S11: -0.0436 S12: -0.0069 S13: -0.0522
REMARK 3 S21: -0.0155 S22: -0.0008 S23: -0.0145
REMARK 3 S31: 0.0103 S32: -0.0146 S33: 0.0392
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 7 B 398
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7465 35.1929 -3.3536
REMARK 3 T TENSOR
REMARK 3 T11: 0.0869 T22: 0.1171
REMARK 3 T33: 0.0812 T12: 0.0015
REMARK 3 T13: -0.0145 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 0.0565 L22: 0.0389
REMARK 3 L33: 0.0458 L12: -0.0152
REMARK 3 L13: -0.0117 L23: 0.0166
REMARK 3 S TENSOR
REMARK 3 S11: -0.0135 S12: 0.0233 S13: 0.0172
REMARK 3 S21: 0.0337 S22: -0.0100 S23: -0.0135
REMARK 3 S31: 0.0096 S32: -0.0296 S33: 0.0176
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 396
REMARK 3 ORIGIN FOR THE GROUP (A): 56.2897 4.1571 25.4354
REMARK 3 T TENSOR
REMARK 3 T11: 0.1445 T22: 0.1572
REMARK 3 T33: 0.1482 T12: 0.0110
REMARK 3 T13: 0.0079 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 0.0529 L22: 0.0671
REMARK 3 L33: 0.0715 L12: 0.0195
REMARK 3 L13: 0.0163 L23: 0.0014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0215 S12: -0.0197 S13: -0.0270
REMARK 3 S21: -0.0386 S22: -0.0208 S23: -0.0360
REMARK 3 S31: -0.0251 S32: -0.0357 S33: 0.0393
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 396
REMARK 3 ORIGIN FOR THE GROUP (A): 56.7798 39.2926 20.2906
REMARK 3 T TENSOR
REMARK 3 T11: 0.0925 T22: 0.1112
REMARK 3 T33: 0.1420 T12: 0.0098
REMARK 3 T13: -0.0305 T23: -0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.0538 L22: 0.0657
REMARK 3 L33: 0.0803 L12: -0.0354
REMARK 3 L13: 0.0160 L23: -0.0198
REMARK 3 S TENSOR
REMARK 3 S11: -0.0324 S12: 0.0138 S13: 0.0752
REMARK 3 S21: 0.0136 S22: 0.0050 S23: -0.0646
REMARK 3 S31: 0.0300 S32: -0.0206 S33: 0.0249
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1. TWINNING: TWIN LAW: H,-K,-L, TWIN
REMARK 3 FRACTION: 0.354. 2. WHEN REFINING TLS, THE OUTPUT PDB FILE
REMARK 3 ALWAYS HAS THE ANISOU RECORDS FOR THE ATOMS INVOLVED IN TLS
REMARK 3 GROUPS. THE ANISOTROPIC B-FACTOR IN ANISOU RECORDS IS THE
REMARK 3 TOTAL B-FACTOR (B_TLS + B_INDIVIDUAL). THE ISOTROPIC
REMARK 3 EQUIVALENT B-FACTOR IN ATOM RECORDS IS THE MEAN OF THE TRACE
REMARK 3 OF THE ANISOU MATRIX DIVIDED BY 10000 AND MULTIPLIED BY 8*PI^2
REMARK 3 AND REPRESENTS THE ISOTROPIC EQUIVALENT OF THE TOTAL B-FACTOR
REMARK 3 (B_TLS + B_INDIVIDUAL). TO OBTAIN THE INDIVIDUAL B-FACTORS,
REMARK 3 ONE NEEDS TO COMPUTE THE TLS COMPONENT (B_TLS) USING THE TLS
REMARK 3 RECORDS IN THE PDB FILE HEADER AND THEN SUBTRACT IT FROM THE
REMARK 3 TOTAL B-FACTORS (ON THE ANISOU RECORDS).
REMARK 4
REMARK 4 3C8D 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 RCSB046469.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-OCT-2006
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
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) : 0.97900
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 : 149451
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 48.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06200
REMARK 200 FOR THE DATA SET : 10.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37900
REMARK 200 FOR SHELL : 2.390
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 (%): 46.30
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3000, 0.1 M CITRATE PH 5.5,
REMARK 280 3 MM DHBG, 1 MM FECL3, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 77.98600
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: 3250 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: 3470 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 MET 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 GLN A 64
REMARK 465 SER A 106
REMARK 465 PRO A 107
REMARK 465 GLY A 187
REMARK 465 ASP A 188
REMARK 465 VAL A 189
REMARK 465 THR A 190
REMARK 465 ALA A 191
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 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 465 LEU B 4
REMARK 465 LYS B 5
REMARK 465 VAL B 6
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 GLY B 135
REMARK 465 GLY B 136
REMARK 465 ASP B 188
REMARK 465 VAL B 189
REMARK 465 THR B 190
REMARK 465 ALA B 191
REMARK 465 GLU B 192
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 MET 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 GLN C 64
REMARK 465 ASP C 188
REMARK 465 VAL C 189
REMARK 465 THR C 190
REMARK 465 ALA C 191
REMARK 465 GLU C 192
REMARK 465 HIS C 397
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 MET 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 PRO D 105
REMARK 465 SER D 106
REMARK 465 GLY D 136
REMARK 465 GLY D 187
REMARK 465 ASP D 188
REMARK 465 VAL D 189
REMARK 465 THR D 190
REMARK 465 ALA D 191
REMARK 465 GLU D 192
REMARK 465 HIS D 397
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 O PRO A 394 ND1 HIS A 397 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 GLU B 193 N - CA - C ANGL. DEV. = -21.0 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 PRO A 37 0.15 -61.48
REMARK 500 CYS A 157 72.67 -156.81
REMARK 500 ILE A 235 -72.58 74.42
REMARK 500 SER A 281 -113.79 46.86
REMARK 500 VAL B 56 -51.97 -122.42
REMARK 500 THR B 57 -68.79 -97.93
REMARK 500 LEU B 120 -32.15 -39.41
REMARK 500 ILE B 235 -72.90 79.85
REMARK 500 SER B 281 -117.87 51.86
REMARK 500 PHE B 367 93.22 -69.18
REMARK 500 ASP B 372 10.66 -68.72
REMARK 500 HIS C 16 36.05 -143.09
REMARK 500 VAL C 56 -30.61 -132.63
REMARK 500 ASP C 99 -6.86 -140.14
REMARK 500 LEU C 137 45.12 -104.67
REMARK 500 ILE C 235 -69.34 72.47
REMARK 500 SER C 281 -117.24 47.57
REMARK 500 GLN D 38 1.38 -63.73
REMARK 500 ILE D 235 -78.79 73.65
REMARK 500 SER D 281 -112.39 45.96
REMARK 500 ALA D 332 49.03 -108.00
REMARK 500 ILE D 362 44.12 -140.90
REMARK 500 LEU D 395 11.92 -68.24
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 D 729 DISTANCE = 7.16 ANGSTROMS
REMARK 525 HOH B 612 DISTANCE = 6.09 ANGSTROMS
REMARK 525 HOH C 828 DISTANCE = 6.62 ANGSTROMS
REMARK 525 HOH A 672 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH A 720 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH A 721 DISTANCE = 7.34 ANGSTROMS
REMARK 525 HOH D 845 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 746 DISTANCE = 7.75 ANGSTROMS
REMARK 525 HOH B 748 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH B 764 DISTANCE = 5.86 ANGSTROMS
REMARK 525 HOH B 769 DISTANCE = 7.35 ANGSTROMS
REMARK 525 HOH B 773 DISTANCE = 5.24 ANGSTROMS
REMARK 525 HOH B 815 DISTANCE = 5.58 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: CIT BINDING SITE FOR RESIDUE A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: CIT BINDING SITE FOR RESIDUE B 501
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: CIT BINDING SITE FOR RESIDUE C 501
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: CIT BINDING SITE FOR RESIDUE C 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: 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: 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 3C8D A 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
DBREF 3C8D B 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
DBREF 3C8D C 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
DBREF 3C8D D 1 400 UNP Q83SB9 Q83SB9_SHIFL 1 400
SEQADV 3C8D SER A -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ASN A -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ALA A 0 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D SER B -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ASN B -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ALA B 0 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D SER C -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ASN C -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ALA C 0 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D SER D -2 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ASN D -1 UNP Q83SB9 EXPRESSION TAG
SEQADV 3C8D ALA D 0 UNP Q83SB9 EXPRESSION TAG
SEQRES 1 A 403 SER ASN ALA MET 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 MET 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 MET 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 MET 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 MET 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 MET ILE
SEQRES 28 A 403 MET 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 MET 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 MET 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 MET 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 MET 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 MET 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 MET 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 MET ILE
SEQRES 28 B 403 MET 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 MET 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 MET 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 MET 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 MET 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 MET 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 MET 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 MET ILE
SEQRES 28 C 403 MET 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 MET 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 MET 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 MET 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 MET 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 MET 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 MET 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 MET ILE
SEQRES 28 D 403 MET 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 MET GLN GLY
SEQRES 31 D 403 LEU ILE ASP LEU TRP GLN PRO LEU PHE HIS ASP ARG SER
HET CIT A 501 13
HET CIT B 501 13
HET CIT C 501 13
HET CIT C 502 13
HETNAM CIT CITRIC ACID
FORMUL 5 CIT 4(C6 H8 O7)
FORMUL 9 HOH *1120(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 GLU A 257 1 11
HELIX 8 8 GLU A 257 ALA A 266 1 10
HELIX 9 9 ARG A 271 ARG A 274 5 4
HELIX 10 10 SER A 281 TRP A 294 1 14
HELIX 11 11 GLY A 319 ALA A 327 1 9
HELIX 12 12 GLU A 345 LEU A 359 1 15
HELIX 13 13 HIS A 360 LYS A 363 5 4
HELIX 14 14 ASP A 376 GLN A 393 1 18
HELIX 15 15 PRO A 394 PHE A 396 5 3
HELIX 16 16 SER B 8 SER B 14 1 7
HELIX 17 17 ASP B 108 LEU B 120 1 13
HELIX 18 18 PRO B 121 ALA B 123 5 3
HELIX 19 19 ASP B 201 SER B 208 1 8
HELIX 20 20 VAL B 211 ARG B 221 1 11
HELIX 21 21 ASP B 236 LEU B 244 1 9
HELIX 22 22 ASN B 247 GLU B 257 1 11
HELIX 23 23 GLU B 257 VAL B 264 1 8
HELIX 24 24 ARG B 271 ARG B 274 5 4
HELIX 25 25 SER B 281 TRP B 294 1 14
HELIX 26 26 GLY B 319 GLY B 328 1 10
HELIX 27 27 GLU B 345 LEU B 359 1 15
HELIX 28 28 HIS B 360 GLU B 364 5 5
HELIX 29 29 ASP B 376 GLN B 393 1 18
HELIX 30 30 PRO B 394 HIS B 397 5 4
HELIX 31 31 SER C 8 SER C 14 1 7
HELIX 32 32 ASP C 108 LEU C 120 1 13
HELIX 33 33 PRO C 121 ALA C 123 5 3
HELIX 34 34 ASP C 201 SER C 208 1 8
HELIX 35 35 VAL C 211 ARG C 221 1 11
HELIX 36 36 ASP C 236 LEU C 244 1 9
HELIX 37 37 ASN C 247 GLU C 257 1 11
HELIX 38 38 GLU C 257 VAL C 264 1 8
HELIX 39 39 ARG C 271 ARG C 274 5 4
HELIX 40 40 SER C 281 TRP C 294 1 14
HELIX 41 41 GLY C 319 ALA C 327 1 9
HELIX 42 42 GLU C 345 LEU C 359 1 15
HELIX 43 43 HIS C 360 GLU C 364 5 5
HELIX 44 44 ASP C 376 GLN C 393 1 18
HELIX 45 45 PRO C 394 PHE C 396 5 3
HELIX 46 46 SER D 8 SER D 14 1 7
HELIX 47 47 ASP D 108 LEU D 120 1 13
HELIX 48 48 PRO D 121 ALA D 123 5 3
HELIX 49 49 ASP D 201 SER D 208 1 8
HELIX 50 50 VAL D 211 ARG D 221 1 11
HELIX 51 51 ASP D 236 LEU D 244 1 9
HELIX 52 52 ASN D 247 GLU D 257 1 11
HELIX 53 53 GLU D 257 ALA D 266 1 10
HELIX 54 54 ARG D 271 ARG D 274 5 4
HELIX 55 55 SER D 281 TRP D 294 1 14
HELIX 56 56 GLY D 319 ALA D 327 1 9
HELIX 57 57 GLU D 345 LEU D 359 1 15
HELIX 58 58 HIS D 360 LYS D 363 5 4
HELIX 59 59 ASP D 376 TRP D 392 1 17
HELIX 60 60 GLN D 393 PHE D 396 5 4
SHEET 1 A 4 GLU A 19 ARG A 22 0
SHEET 2 A 4 MET A 27 ARG A 35 -1 O THR A 31 N GLU A 19
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 VAL A 141 GLU A 145 -1 O SER A 142 N TYR A 91
SHEET 4 B 4 SER A 132 TRP A 133 -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 ALA A 197 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 8 GLU B 19 ARG B 22 0
SHEET 2 D 8 MET B 27 ARG B 35 -1 O GLU B 29 N GLN B 21
SHEET 3 D 8 VAL B 76 ASN B 84 -1 O TRP B 79 N PHE B 32
SHEET 4 D 8 SER B 67 ARG B 70 -1 N GLN B 69 O GLN B 78
SHEET 5 D 8 ARG B 48 ILE B 53 -1 N VAL B 49 O MET B 68
SHEET 6 D 8 ARG B 88 THR B 96 -1 O THR B 96 N ARG B 48
SHEET 7 D 8 VAL B 141 GLU B 145 -1 O SER B 142 N TYR B 91
SHEET 8 D 8 SER B 132 TRP B 133 -1 N TRP B 133 O VAL B 141
SHEET 1 E 8 LYS B 166 SER B 172 0
SHEET 2 E 8 ASN B 177 THR B 185 -1 O ILE B 183 N LYS B 166
SHEET 3 E 8 VAL B 228 ILE B 232 -1 O TYR B 229 N PHE B 184
SHEET 4 E 8 LEU B 196 LEU B 199 1 N ALA B 197 O VAL B 230
SHEET 5 E 8 VAL B 276 GLN B 280 1 O VAL B 276 N VAL B 198
SHEET 6 E 8 CYS B 300 GLN B 304 1 O LEU B 302 N VAL B 277
SHEET 7 E 8 ARG B 336 GLY B 342 1 O VAL B 338 N VAL B 301
SHEET 8 E 8 ILE B 366 VAL B 371 1 O VAL B 371 N ALA B 341
SHEET 1 F 4 GLU C 19 ARG C 22 0
SHEET 2 F 4 MET C 27 ARG C 35 -1 O THR C 31 N GLU C 19
SHEET 3 F 4 VAL C 76 ASN C 84 -1 O TRP C 79 N PHE C 32
SHEET 4 F 4 GLN C 69 ARG C 70 -1 N GLN C 69 O GLN C 78
SHEET 1 G 4 ARG C 48 ILE C 53 0
SHEET 2 G 4 ARG C 88 THR C 96 -1 O CYS C 92 N TYR C 52
SHEET 3 G 4 ALA C 140 GLU C 145 -1 O SER C 142 N TYR C 91
SHEET 4 G 4 SER C 132 LYS C 134 -1 N TRP C 133 O VAL C 141
SHEET 1 H 8 LYS C 166 LYS C 171 0
SHEET 2 H 8 SER C 178 THR C 185 -1 O ILE C 183 N LYS C 166
SHEET 3 H 8 VAL C 228 ILE C 232 -1 O TYR C 229 N PHE C 184
SHEET 4 H 8 LEU C 196 LEU C 199 1 N ALA C 197 O VAL C 230
SHEET 5 H 8 VAL C 276 GLN C 280 1 O ALA C 278 N VAL C 198
SHEET 6 H 8 CYS C 300 GLN C 304 1 O LEU C 302 N VAL C 277
SHEET 7 H 8 ARG C 336 GLY C 342 1 O VAL C 338 N VAL C 301
SHEET 8 H 8 ILE C 366 VAL C 371 1 O VAL C 371 N ALA C 341
SHEET 1 I 4 GLU D 19 ARG D 22 0
SHEET 2 I 4 MET D 27 ARG D 35 -1 O GLU D 29 N GLN D 21
SHEET 3 I 4 VAL D 76 ASN D 84 -1 O THR D 81 N VAL D 30
SHEET 4 I 4 GLN D 69 ARG D 70 -1 N GLN D 69 O GLN D 78
SHEET 1 J 4 ARG D 48 ILE D 53 0
SHEET 2 J 4 ARG D 88 THR D 96 -1 O THR D 96 N ARG D 48
SHEET 3 J 4 ALA D 140 GLU D 145 -1 O SER D 142 N TYR D 91
SHEET 4 J 4 SER D 132 LYS D 134 -1 N TRP D 133 O VAL D 141
SHEET 1 K 8 LYS D 166 SER D 172 0
SHEET 2 K 8 ASN D 177 THR D 185 -1 O ARG D 179 N TRP D 170
SHEET 3 K 8 VAL D 228 ILE D 232 -1 O TYR D 229 N PHE D 184
SHEET 4 K 8 LEU D 196 LEU D 199 1 N LEU D 199 O VAL D 230
SHEET 5 K 8 VAL D 276 GLN D 280 1 O VAL D 276 N VAL D 198
SHEET 6 K 8 CYS D 300 GLN D 304 1 O LEU D 302 N VAL D 277
SHEET 7 K 8 ARG D 336 GLY D 342 1 O VAL D 338 N VAL D 301
SHEET 8 K 8 ILE D 366 VAL D 371 1 O PHE D 367 N ILE D 337
CISPEP 1 TRP A 310 PRO A 311 0 -2.01
CISPEP 2 TRP B 310 PRO B 311 0 1.60
CISPEP 3 TRP C 310 PRO C 311 0 4.23
CISPEP 4 TRP D 310 PRO D 311 0 4.29
SITE 1 AC1 6 ARG A 240 SER A 281 PHE A 282 SER A 307
SITE 2 AC1 6 TRP A 309 HIS B 312
SITE 1 AC2 7 PRO A 311 HIS A 312 ARG B 240 SER B 281
SITE 2 AC2 7 PHE B 282 SER B 307 HIS B 375
SITE 1 AC3 8 PRO C 311 HIS C 312 ARG C 313 ARG D 240
SITE 2 AC3 8 SER D 281 PHE D 282 SER D 307 TRP D 309
SITE 1 AC4 7 ARG C 240 SER C 281 PHE C 282 SER C 307
SITE 2 AC4 7 HIS C 375 PRO D 311 HIS D 312
CRYST1 111.297 155.972 48.480 90.00 90.01 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 0.008985 -0.000000 0.000002 0.00000
SCALE2 0.000000 0.006411 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020627 0.00000
END |