| 3F67-pdb | HEADER HYDROLASE 05-NOV-08 3F67
TITLE CRYSTAL STRUCTURE OF PUTATIVE DIENELACTONE HYDROLASE FROM
TITLE 2 KLEBSIELLA PNEUMONIAE SUBSP. PNEUMONIAE MGH 78578
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE DIENELACTONE HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 28-265;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE SUBSP.
SOURCE 3 PNEUMONIAE MGH 78578;
SOURCE 4 STRAIN: ATCC 700721; MGH 78578;
SOURCE 5 GENE: KPN78578_42700, KPN_04326, YSGA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 MAGIC;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG19
KEYWDS ALPHA-BETA-ALPHA SANDWICH, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,H.LI,J.BEARDEN,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 25-NOV-08 3F67 0
JRNL AUTH Y.KIM,H.LI,J.BEARDEN,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF PUTATIVE DIENELACTONE
JRNL TITL 2 HYDROLASE FROM KLEBSIELLA PNEUMONIAE SUBSP.
JRNL TITL 3 PNEUMONIAE MGH 78578
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.74 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0053
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) : 1.74
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 29596
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1565
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.74
REMARK 3 BIN RESOLUTION RANGE LOW : 1.79
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2070
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 105
REMARK 3 BIN FREE R VALUE : 0.3150
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 2367
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.19
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.91
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.23000
REMARK 3 B22 (A**2) : -0.23000
REMARK 3 B33 (A**2) : 0.45000
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): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.059
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.054
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.967
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2142 ; 0.018 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2944 ; 1.547 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 280 ; 6.190 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 106 ;40.012 ;24.245
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 325 ;14.858 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;12.501 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 306 ; 0.136 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1748 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1335 ; 0.877 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2154 ; 1.503 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 807 ; 2.367 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 790 ; 3.719 ; 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
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 NULL A
REMARK 3 ORIGIN FOR THE GROUP (A): 53.1541 26.6225 7.8597
REMARK 3 T TENSOR
REMARK 3 T11: 0.0264 T22: 0.0055
REMARK 3 T33: 0.0098 T12: -0.0033
REMARK 3 T13: -0.0067 T23: 0.0055
REMARK 3 L TENSOR
REMARK 3 L11: 1.0828 L22: 0.8433
REMARK 3 L33: 0.9773 L12: 0.1974
REMARK 3 L13: -0.2987 L23: -0.2952
REMARK 3 S TENSOR
REMARK 3 S11: -0.0197 S12: 0.0419 S13: 0.0601
REMARK 3 S21: 0.0439 S22: 0.0203 S23: 0.0275
REMARK 3 S31: -0.1122 S32: 0.0229 S33: -0.0006
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 3F67 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 RCSB050196.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-2008
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31820
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 47.850
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 14.000
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.78
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.30
REMARK 200 R MERGE FOR SHELL (I) : 0.86600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, DM, SHELXD, RESOLVE, COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LI2SO4 0.1 M TRIS PH 7.0 1.0
REMARK 280 M K/NA TARTRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.79050
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 53.19250
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 53.19250
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 13.39525
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 53.19250
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 53.19250
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 40.18575
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 53.19250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 53.19250
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 13.39525
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 53.19250
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 53.19250
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.18575
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 26.79050
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 300
REMARK 300 REMARK: MONOMER
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 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 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 HOH A 368 O HOH A 478 2.07
REMARK 500 OE1 GLU A 13 O HOH A 502 2.09
REMARK 500 O HOH A 290 O HOH A 291 2.10
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 CYS A 120 CB CYS A 120 SG -0.106
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 216 NE - CZ - NH2 ANGL. DEV. = 3.1 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 43.46 -107.45
REMARK 500 GLU A 37 -168.87 -77.65
REMARK 500 LEU A 84 -63.87 -126.20
REMARK 500 CYS A 120 -118.91 65.34
REMARK 500 TYR A 143 59.38 36.21
REMARK 500 ASN A 196 58.28 33.38
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 239
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 240
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 241
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 242
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC60631.1 RELATED DB: TARGETDB
DBREF 3F67 A 1 238 UNP A6TGL0 A6TGL0_KLEP7 28 265
SEQADV 3F67 SER A -2 UNP A6TGL0 EXPRESSION TAG
SEQADV 3F67 ASN A -1 UNP A6TGL0 EXPRESSION TAG
SEQADV 3F67 ALA A 0 UNP A6TGL0 EXPRESSION TAG
SEQRES 1 A 241 SER ASN ALA ILE ILE ALA GLY GLU THR SER ILE PRO SER
SEQRES 2 A 241 GLN GLY GLU ASN MSE PRO ALA TYR HIS ALA ARG PRO LYS
SEQRES 3 A 241 ASN ALA ASP GLY PRO LEU PRO ILE VAL ILE VAL VAL GLN
SEQRES 4 A 241 GLU ILE PHE GLY VAL HIS GLU HIS ILE ARG ASP LEU CYS
SEQRES 5 A 241 ARG ARG LEU ALA GLN GLU GLY TYR LEU ALA ILE ALA PRO
SEQRES 6 A 241 GLU LEU TYR PHE ARG GLN GLY ASP PRO ASN GLU TYR HIS
SEQRES 7 A 241 ASP ILE PRO THR LEU PHE LYS GLU LEU VAL SER LYS VAL
SEQRES 8 A 241 PRO ASP ALA GLN VAL LEU ALA ASP LEU ASP HIS VAL ALA
SEQRES 9 A 241 SER TRP ALA ALA ARG HIS GLY GLY ASP ALA HIS ARG LEU
SEQRES 10 A 241 LEU ILE THR GLY PHE CYS TRP GLY GLY ARG ILE THR TRP
SEQRES 11 A 241 LEU TYR ALA ALA HIS ASN PRO GLN LEU LYS ALA ALA VAL
SEQRES 12 A 241 ALA TRP TYR GLY LYS LEU VAL GLY GLU LYS SER LEU ASN
SEQRES 13 A 241 SER PRO LYS HIS PRO VAL ASP ILE ALA VAL ASP LEU ASN
SEQRES 14 A 241 ALA PRO VAL LEU GLY LEU TYR GLY ALA LYS ASP ALA SER
SEQRES 15 A 241 ILE PRO GLN ASP THR VAL GLU THR MSE ARG GLN ALA LEU
SEQRES 16 A 241 ARG ALA ALA ASN ALA THR ALA GLU ILE VAL VAL TYR PRO
SEQRES 17 A 241 GLU ALA ASP HIS ALA PHE ASN ALA ASP TYR ARG ALA SER
SEQRES 18 A 241 TYR HIS GLU GLU SER ALA LYS ASP GLY TRP GLN ARG MSE
SEQRES 19 A 241 LEU ALA TRP PHE ALA GLN TYR
MODRES 3F67 MSE A 15 MET SELENOMETHIONINE
MODRES 3F67 MSE A 188 MET SELENOMETHIONINE
MODRES 3F67 MSE A 231 MET SELENOMETHIONINE
HET MSE A 15 8
HET MSE A 188 8
HET MSE A 231 8
HET EDO A 239 4
HET FMT A 240 3
HET FMT A 241 3
HET ACY A 242 4
HETNAM MSE SELENOMETHIONINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM FMT FORMIC ACID
HETNAM ACY ACETIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 MSE 3(C5 H11 N O2 SE)
FORMUL 2 EDO C2 H6 O2
FORMUL 3 FMT 2(C H2 O2)
FORMUL 5 ACY C2 H4 O2
FORMUL 6 HOH *295(H2 O)
HELIX 1 1 HIS A 42 GLU A 55 1 14
HELIX 2 2 ASP A 70 TYR A 74 5 5
HELIX 3 3 ASP A 76 LEU A 84 1 9
HELIX 4 4 VAL A 85 VAL A 88 5 4
HELIX 5 5 PRO A 89 ARG A 106 1 18
HELIX 6 6 CYS A 120 ALA A 131 1 12
HELIX 7 7 HIS A 157 ALA A 162 1 6
HELIX 8 8 VAL A 163 LEU A 165 5 3
HELIX 9 9 PRO A 181 ALA A 195 1 15
HELIX 10 10 HIS A 220 ALA A 236 1 17
SHEET 1 A 8 ILE A 1 SER A 10 0
SHEET 2 A 8 GLU A 13 PRO A 22 -1 O HIS A 19 N GLY A 4
SHEET 3 A 8 LEU A 58 PRO A 62 -1 O ALA A 61 N TYR A 18
SHEET 4 A 8 LEU A 29 VAL A 35 1 N VAL A 34 O ILE A 60
SHEET 5 A 8 GLY A 109 PHE A 119 1 O THR A 117 N VAL A 35
SHEET 6 A 8 ALA A 138 TRP A 142 1 O TRP A 142 N GLY A 118
SHEET 7 A 8 VAL A 169 GLY A 174 1 O LEU A 172 N ALA A 141
SHEET 8 A 8 ALA A 199 TYR A 204 1 O TYR A 204 N TYR A 173
LINK C ASN A 14 N MSE A 15 1555 1555 1.32
LINK C MSE A 15 N PRO A 16 1555 1555 1.34
LINK C THR A 187 N MSE A 188 1555 1555 1.33
LINK C MSE A 188 N ARG A 189 1555 1555 1.33
LINK C ARG A 230 N MSE A 231 1555 1555 1.33
LINK C MSE A 231 N LEU A 232 1555 1555 1.34
SITE 1 AC1 6 GLU A 5 ALA A 17 TYR A 18 VAL A 41
SITE 2 AC1 6 ARG A 46 GLU A 63
SITE 1 AC2 3 GLU A 55 ARG A 113 HOH A 365
SITE 1 AC3 4 VAL A 203 TYR A 204 PRO A 205 HOH A 402
SITE 1 AC4 7 SER A 102 ARG A 106 HOH A 249 HOH A 258
SITE 2 AC4 7 HOH A 259 HOH A 286 HOH A 287
CRYST1 106.385 106.385 53.581 90.00 90.00 90.00 P 41 21 2 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 0.009400 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009400 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018663 0.00000
TER 2059 TYR A 238
MASTER 358 0 7 10 8 0 6 6 2367 1 44 19
END
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