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HEADER HYDROLASE 10-SEP-15 5DNU
TITLE CRYSTAL STRUCTURE OF STRIGA KAI2-LIKE PROTEIN IN COMPLEX WITH KARRIKIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SHKAI2IB;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STRIGA HERMONTHICA;
SOURCE 3 ORGANISM_TAXID: 68872;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KAI2 KARRIKIN STRIGA, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA
REVDAT 1 17-AUG-16 5DNU 0
JRNL AUTH Y.XU,T.MIYAKAWA,A.NAKAMURA,M.TANOKURA
JRNL TITL STRUCTURAL BASIS OF UNIQUE LIGAND SPECIFICITY OF KAI2-LIKE
JRNL TITL 2 PROTEIN FROM PARASITIC WEED STRIGA HERMONTHICA
JRNL REF TO BE PUBLISHED
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0124
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 91454
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) : 0.141
REMARK 3 R VALUE (WORKING SET) : 0.140
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4887
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6607
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.1930
REMARK 3 BIN FREE R VALUE SET COUNT : 350
REMARK 3 BIN FREE R VALUE : 0.2290
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2076
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 209
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : -0.03000
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): 0.032
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.031
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.018
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.862
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.978
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2210 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2089 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2987 ; 1.692 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4777 ; 1.057 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 276 ; 6.256 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 100 ;30.709 ;22.800
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 341 ;12.698 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;18.496 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 333 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2523 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 542 ; 0.002 ; 0.020
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): 1077 ; 2.239 ; 2.017
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1078 ; 2.240 ; 2.018
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1347 ; 2.666 ; 3.035
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1348 ; 2.673 ; 3.039
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1133 ; 2.274 ; 2.281
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1134 ; 2.273 ; 2.280
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1636 ; 2.665 ; 3.310
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2712 ; 3.501 ;17.817
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2713 ; 3.500 ;17.815
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 4298 ; 2.143 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 57 ;30.658 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 4413 ;12.863 ; 5.000
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 : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5DNU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 95
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 96642
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 19.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 20.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 97.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.22
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.60
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.300
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: 5DNW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.45
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, TRIS, PH 7.5, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 278K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 60.42200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 120.84400
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.63300
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 151.05500
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 30.21100
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 60.42200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 120.84400
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 151.05500
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 90.63300
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 30.21100
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 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 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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -4
REMARK 465 PRO A -3
REMARK 465 LEU A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 SER A 270
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 DISTANCE
REMARK 500 OG SER A 68 O HOH A 401 2.15
REMARK 500 O HOH A 445 O HOH A 575 2.18
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 THR A 28 -165.38 -110.79
REMARK 500 SER A 88 72.17 -164.53
REMARK 500 SER A 95 -131.86 53.82
REMARK 500 ARG A 123 125.18 -175.57
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 A 609 DISTANCE = 6.92 ANGSTROMS
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 313 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PHE A 64 O
REMARK 620 2 SER A 68 OG 114.2
REMARK 620 3 HOH A 401 O 151.8 45.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 312 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 83 OE2
REMARK 620 2 EDO A 316 O2 126.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 311 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 267 OD1
REMARK 620 2 FMT A 302 O2 112.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KKN A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 315
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 316
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 317
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 318
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue BEZ A 319
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5DNV RELATED DB: PDB
REMARK 900 RELATED ID: 5DNW RELATED DB: PDB
DBREF 5DNU A -4 270 PDB 5DNU 5DNU -4 270
SEQRES 1 A 275 GLY PRO LEU GLY SER MET ASN ARG VAL GLU ALA ALA ARG
SEQRES 2 A 275 ASN VAL HIS ILE VAL GLY SER GLY ASP THR THR VAL VAL
SEQRES 3 A 275 LEU GLY HIS GLY PHE GLY THR ASP GLN SER VAL TRP LYS
SEQRES 4 A 275 HIS LEU VAL PRO TYR LEU VAL ASP SER TYR ARG VAL LEU
SEQRES 5 A 275 LEU TYR ASP ASN MET GLY ALA GLY SER THR ASN PRO GLU
SEQRES 6 A 275 TYR PHE HIS PHE GLU ARG TYR SER THR LEU GLN GLY TYR
SEQRES 7 A 275 ALA HIS ASP LEU LEU VAL ILE LEU HIS GLU PHE ASN ILE
SEQRES 8 A 275 ARG SER CYS ILE PHE VAL GLY HIS SER LEU SER ALA MET
SEQRES 9 A 275 THR GLY ALA ILE ALA SER ILE ILE ARG PRO ASP LEU PHE
SEQRES 10 A 275 GLN LYS ILE VAL MET LEU SER ALA SER PRO ARG PHE LEU
SEQRES 11 A 275 ASN THR ALA ASP TYR LEU GLY GLY PHE GLU PRO ALA ASP
SEQRES 12 A 275 VAL GLU GLN LEU ALA GLY ALA ILE GLU ALA ASN TYR LYS
SEQRES 13 A 275 SER TRP VAL SER GLY PHE ALA PRO MET VAL VAL GLY GLY
SEQRES 14 A 275 ASP MET ASP SER VAL ALA VAL GLN GLU PHE SER ARG THR
SEQRES 15 A 275 LEU PHE ASN MET ARG PRO ASP ILE ALA ARG SER VAL PHE
SEQRES 16 A 275 ARG THR ILE PHE THR SER ASP LEU ARG ASP TYR LEU GLY
SEQRES 17 A 275 ARG VAL THR VAL PRO CYS HIS ILE ILE GLN SER SER ARG
SEQRES 18 A 275 ASP MET ALA VAL PRO VAL SER VAL ALA GLY TYR ILE HIS
SEQRES 19 A 275 ASN ARG VAL GLY GLY ARG SER VAL VAL GLU VAL MET ASN
SEQRES 20 A 275 THR GLU GLY HIS LEU PRO GLN LEU SER ALA PRO GLU VAL
SEQRES 21 A 275 ALA ILE PRO VAL LEU LEU ARG HIS ILE LYS ASN ASP ILE
SEQRES 22 A 275 ASP SER
HET KKN A 301 11
HET FMT A 302 3
HET FMT A 303 3
HET FMT A 304 3
HET FMT A 305 3
HET FMT A 306 3
HET FMT A 307 3
HET FMT A 308 3
HET FMT A 309 3
HET FMT A 310 3
HET NA A 311 1
HET NA A 312 1
HET NA A 313 1
HET EDO A 314 4
HET EDO A 315 4
HET EDO A 316 4
HET EDO A 317 4
HET EDO A 318 4
HET BEZ A 319 9
HETNAM KKN 3-METHYL-2H-FURO[2,3-C]PYRAN-2-ONE
HETNAM FMT FORMIC ACID
HETNAM NA SODIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM BEZ BENZOIC ACID
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 KKN C8 H6 O3
FORMUL 3 FMT 9(C H2 O2)
FORMUL 12 NA 3(NA 1+)
FORMUL 15 EDO 5(C2 H6 O2)
FORMUL 20 BEZ C7 H6 O2
FORMUL 21 HOH *209(H2 O)
HELIX 1 AA1 ARG A 3 ASN A 9 1 7
HELIX 2 AA2 ASP A 29 LYS A 34 5 6
HELIX 3 AA3 LEU A 36 LEU A 40 5 5
HELIX 4 AA4 PHE A 64 SER A 68 5 5
HELIX 5 AA5 THR A 69 PHE A 84 1 16
HELIX 6 AA6 SER A 95 ARG A 108 1 14
HELIX 7 AA7 GLU A 135 GLY A 144 1 10
HELIX 8 AA8 ASN A 149 GLY A 163 1 15
HELIX 9 AA9 SER A 168 PHE A 179 1 12
HELIX 10 AB1 ARG A 182 THR A 195 1 14
HELIX 11 AB2 LEU A 198 VAL A 205 5 8
HELIX 12 AB3 VAL A 222 VAL A 232 1 11
HELIX 13 AB4 LEU A 247 ALA A 252 1 6
HELIX 14 AB5 ALA A 252 ASN A 266 1 15
SHEET 1 AA1 7 HIS A 11 GLY A 14 0
SHEET 2 AA1 7 ARG A 45 LEU A 48 -1 O VAL A 46 N VAL A 13
SHEET 3 AA1 7 THR A 19 GLY A 23 1 N VAL A 20 O ARG A 45
SHEET 4 AA1 7 CYS A 89 HIS A 94 1 O VAL A 92 N VAL A 21
SHEET 5 AA1 7 PHE A 112 LEU A 118 1 O VAL A 116 N PHE A 91
SHEET 6 AA1 7 CYS A 209 ARG A 216 1 O HIS A 210 N MET A 117
SHEET 7 AA1 7 SER A 236 GLU A 244 1 O VAL A 237 N ILE A 211
LINK O PHE A 64 NA NA A 313 1555 1555 2.86
LINK OG SER A 68 NA NA A 313 1555 1555 2.99
LINK OE2 GLU A 83 NA NA A 312 1555 1555 2.56
LINK OD1 ASP A 267 NA NA A 311 1555 1555 2.48
LINK O2 FMT A 302 NA NA A 311 1555 1555 2.76
LINK NA NA A 313 O HOH A 401 1555 1555 2.25
LINK NA NA A 312 O2 EDO A 316 1555 12545 2.74
CISPEP 1 ILE A 268 ASP A 269 0 -13.27
SITE 1 AC1 10 PHE A 26 SER A 95 LEU A 96 PHE A 124
SITE 2 AC1 10 LEU A 142 ILE A 193 PHE A 194 ALA A 219
SITE 3 AC1 10 HIS A 246 HOH A 424
SITE 1 AC2 6 TYR A 44 ILE A 90 GLN A 113 ILE A 264
SITE 2 AC2 6 LYS A 265 NA A 311
SITE 1 AC3 9 SER A 15 ASP A 129 TYR A 130 ARG A 199
SITE 2 AC3 9 TYR A 227 ARG A 231 FMT A 309 HOH A 442
SITE 3 AC3 9 HOH A 547
SITE 1 AC4 6 PHE A 64 GLU A 65 ARG A 66 ARG A 108
SITE 2 AC4 6 ASP A 110 HOH A 497
SITE 1 AC5 7 PRO A 109 PHE A 112 GLN A 113 VAL A 207
SITE 2 AC5 7 EDO A 317 HOH A 405 HOH A 408
SITE 1 AC6 5 GLU A 65 SER A 68 PRO A 109 HOH A 444
SITE 2 AC6 5 HOH A 604
SITE 1 AC7 5 PRO A 258 VAL A 259 ARG A 262 HOH A 455
SITE 2 AC7 5 HOH A 462
SITE 1 AC8 5 GLN A 71 SER A 196 ASP A 197 LEU A 198
SITE 2 AC8 5 ARG A 204
SITE 1 AC9 8 GLY A 14 SER A 15 ARG A 199 ASP A 200
SITE 2 AC9 8 ARG A 231 FMT A 303 HOH A 413 HOH A 421
SITE 1 AD1 5 ARG A 262 HIS A 263 ASN A 266 ASP A 267
SITE 2 AD1 5 HOH A 500
SITE 1 AD2 5 GLN A 113 LYS A 114 ASN A 266 ASP A 267
SITE 2 AD2 5 FMT A 302
SITE 1 AD3 5 VAL A 4 ARG A 8 VAL A 79 GLU A 83
SITE 2 AD3 5 EDO A 316
SITE 1 AD4 5 HIS A 63 PHE A 64 GLU A 65 SER A 68
SITE 2 AD4 5 HOH A 401
SITE 1 AD5 8 PRO A 38 ARG A 123 LEU A 125 THR A 195
SITE 2 AD5 8 SER A 196 ASP A 197 HOH A 425 HOH A 473
SITE 1 AD6 7 ILE A 12 ARG A 45 TYR A 227 ASN A 230
SITE 2 AD6 7 ARG A 231 HOH A 493 HOH A 510
SITE 1 AD7 6 ARG A 8 ARG A 66 VAL A 79 HIS A 82
SITE 2 AD7 6 NA A 312 HOH A 543
SITE 1 AD8 5 THR A 206 VAL A 207 FMT A 305 HOH A 405
SITE 2 AD8 5 HOH A 565
SITE 1 AD9 4 TYR A 130 LEU A 131 SER A 223 HOH A 510
SITE 1 AE1 5 GLN A 71 ILE A 103 ILE A 107 TYR A 201
SITE 2 AE1 5 HOH A 553
CRYST1 75.757 75.757 181.266 90.00 90.00 120.00 P 61 2 2 12
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 0.013200 0.007621 0.000000 0.00000
SCALE2 0.000000 0.015242 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005517 0.00000
TER 2103 ASP A 269
MASTER 432 0 19 14 7 0 39 6 2355 1 75 22
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