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HEADER HYDROLASE/HYDROLASE INHIBITOR 05-MAR-12 4E14
TITLE CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE CONJUGATED WITH
TITLE 2 PHENYLMETHYLSULFONYL FLUORIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KYNURENINE FORMAMIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ARYLFORMAMIDASE, ARYL-FORMYLAMINE AMIDOHYDROLASE,
COMPND 5 FORMYLKYNURENINASE, CG9542, RH42281P;
COMPND 6 EC: 3.5.1.9;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 3 ORGANISM_COMMON: FRUIT FLY;
SOURCE 4 ORGANISM_TAXID: 7227;
SOURCE 5 GENE: CG9542, DMEL_CG9542;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PTYB
KEYWDS ALPHA/BETA HYDROLASE FOLD, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.HAN,H.ROBINSON,J.LI
REVDAT 2 29-AUG-12 4E14 1 JRNL
REVDAT 1 27-JUN-12 4E14 0
JRNL AUTH Q.HAN,H.ROBINSON,J.LI
JRNL TITL BIOCHEMICAL IDENTIFICATION AND CRYSTAL STRUCTURE OF
JRNL TITL 2 KYNURENINE FORMAMIDASE FROM DROSOPHILA MELANOGASTER.
JRNL REF BIOCHEM.J. V. 446 253 2012
JRNL REFN ISSN 0264-6021
JRNL PMID 22690733
JRNL DOI 10.1042/BJ20120416
REMARK 2
REMARK 2 RESOLUTION. 1.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 1.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.64
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 34267
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1793
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) : 1.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.69
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2364
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.53
REMARK 3 BIN R VALUE (WORKING SET) : 0.3310
REMARK 3 BIN FREE R VALUE SET COUNT : 122
REMARK 3 BIN FREE R VALUE : 0.3550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2470
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 155
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.00000
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): 0.123
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.116
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.013
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2575 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3494 ; 1.525 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 310 ; 6.005 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 131 ;36.040 ;23.588
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 433 ;17.246 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;22.500 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 381 ; 0.107 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1971 ; 0.007 ; 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): 1513 ; 0.680 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2468 ; 1.009 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1062 ; 1.896 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1020 ; 2.608 ; 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 : 3
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 0 A 50
REMARK 3 ORIGIN FOR THE GROUP (A): 19.9566 11.3113 27.4146
REMARK 3 T TENSOR
REMARK 3 T11: 0.5392 T22: 0.4644
REMARK 3 T33: 0.2062 T12: -0.2108
REMARK 3 T13: 0.1035 T23: -0.1250
REMARK 3 L TENSOR
REMARK 3 L11: 0.9483 L22: 3.0244
REMARK 3 L33: 7.9418 L12: -0.0561
REMARK 3 L13: 0.0091 L23: -3.9240
REMARK 3 S TENSOR
REMARK 3 S11: 0.1158 S12: -0.5468 S13: 0.1932
REMARK 3 S21: 1.0295 S22: -0.0685 S23: 0.1647
REMARK 3 S31: -0.7068 S32: -0.4501 S33: -0.0473
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 : A 51 A 186
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8625 -1.5304 8.6088
REMARK 3 T TENSOR
REMARK 3 T11: 0.0518 T22: 0.0886
REMARK 3 T33: 0.1014 T12: -0.0658
REMARK 3 T13: -0.0057 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 1.7798 L22: 3.4990
REMARK 3 L33: 1.6942 L12: 0.4367
REMARK 3 L13: 0.5424 L23: -0.1115
REMARK 3 S TENSOR
REMARK 3 S11: 0.1587 S12: -0.1770 S13: -0.0616
REMARK 3 S21: 0.1910 S22: -0.2002 S23: 0.1087
REMARK 3 S31: 0.1721 S32: -0.1745 S33: 0.0416
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 : A 187 A 299
REMARK 3 ORIGIN FOR THE GROUP (A): 28.3121 -2.9831 24.4241
REMARK 3 T TENSOR
REMARK 3 T11: 0.3107 T22: 0.3038
REMARK 3 T33: 0.1240 T12: -0.1797
REMARK 3 T13: -0.0373 T23: 0.0717
REMARK 3 L TENSOR
REMARK 3 L11: 1.2053 L22: 2.3066
REMARK 3 L33: 2.0031 L12: -0.1125
REMARK 3 L13: 0.1485 L23: 0.3405
REMARK 3 S TENSOR
REMARK 3 S11: 0.1270 S12: -0.4275 S13: -0.0743
REMARK 3 S21: 0.5515 S22: -0.2286 S23: -0.0449
REMARK 3 S31: 0.1682 S32: -0.0194 S33: 0.1016
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4E14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-12.
REMARK 100 THE RCSB ID CODE IS RCSB071036.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0750
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL SI(111)
REMARK 200 OPTICS : NULL
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36090
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.640
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 27.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: PDB ENTRY 4E11
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% ETHYLENE GLYCOL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 37.73550
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 23.51450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 37.73550
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.51450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NA NA A 405 LIES ON A SPECIAL POSITION.
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 ALA A -2
REMARK 465 GLY A -1
REMARK 465 GLU A 300
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 TYR A 2 -16.55 71.53
REMARK 500 GLN A 91 -5.90 -148.96
REMARK 500 MET A 93 150.46 78.78
REMARK 500 SEB A 157 -125.22 61.14
REMARK 500 ASN A 211 -175.89 -173.43
REMARK 500 HIS A 243 43.97 -96.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A 405 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 503 O
REMARK 620 2 HOH A 502 O 84.7
REMARK 620 3 SER A 150 OG 103.9 140.7
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 405
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E11 RELATED DB: PDB
REMARK 900 RELATED ID: 4E15 RELATED DB: PDB
DBREF 4E14 A 1 300 UNP Q9VMC9 Q9VMC9_DROME 1 300
SEQADV 4E14 ALA A -2 UNP Q9VMC9 EXPRESSION TAG
SEQADV 4E14 GLY A -1 UNP Q9VMC9 EXPRESSION TAG
SEQADV 4E14 HIS A 0 UNP Q9VMC9 EXPRESSION TAG
SEQRES 1 A 303 ALA GLY HIS MET TYR ASN PRO ARG CYS LYS ASP LEU ASP
SEQRES 2 A 303 ARG ASP TYR PHE PRO SER TYR HIS THR THR ARG PHE GLN
SEQRES 3 A 303 ASP GLN PRO GLU PRO ASN LEU ALA VAL LEU GLU HIS PHE
SEQRES 4 A 303 VAL ARG VAL THR LYS GLN HIS GLY ARG GLU LEU THR GLU
SEQRES 5 A 303 LYS GLN GLY ILE THR VAL ASP HIS LEU ARG TYR GLY GLU
SEQRES 6 A 303 GLY ARG GLN LEU VAL ASP VAL PHE TYR SER GLU LYS THR
SEQRES 7 A 303 THR ASN GLN ALA PRO LEU PHE VAL PHE VAL HIS GLY GLY
SEQRES 8 A 303 TYR TRP GLN GLU MET ASP MET SER MET SER CYS SER ILE
SEQRES 9 A 303 VAL GLY PRO LEU VAL ARG ARG GLY TYR ARG VAL ALA VAL
SEQRES 10 A 303 MET ASP TYR ASN LEU CYS PRO GLN VAL THR LEU GLU GLN
SEQRES 11 A 303 LEU MET THR GLN PHE THR HIS PHE LEU ASN TRP ILE PHE
SEQRES 12 A 303 ASP TYR THR GLU MET THR LYS VAL SER SER LEU THR PHE
SEQRES 13 A 303 ALA GLY HIS SEB ALA GLY ALA HIS LEU LEU ALA GLN ILE
SEQRES 14 A 303 LEU MET ARG PRO ASN VAL ILE THR ALA GLN ARG SER LYS
SEQRES 15 A 303 MET VAL TRP ALA LEU ILE PHE LEU CYS GLY VAL TYR ASP
SEQRES 16 A 303 LEU ARG GLU LEU SER ASN LEU GLU SER VAL ASN PRO LYS
SEQRES 17 A 303 ASN ILE LEU GLY LEU ASN GLU ARG ASN ILE GLU SER VAL
SEQRES 18 A 303 SER PRO MET LEU TRP GLU TYR THR ASP VAL THR VAL TRP
SEQRES 19 A 303 ASN SER THR LYS ILE TYR VAL VAL ALA ALA GLU HIS ASP
SEQRES 20 A 303 SER THR THR PHE ILE GLU GLN SER ARG HIS TYR ALA ASP
SEQRES 21 A 303 VAL LEU ARG LYS LYS GLY TYR LYS ALA SER PHE THR LEU
SEQRES 22 A 303 PHE LYS GLY TYR ASP HIS PHE ASP ILE ILE GLU GLU THR
SEQRES 23 A 303 ALA ILE ASP ASP SER ASP VAL SER ARG PHE LEU ARG ASN
SEQRES 24 A 303 ILE GLU ILE GLU
MODRES 4E14 SEB A 157 SER O-BENZYLSULFONYL-SERINE
HET SEB A 157 16
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET NA A 405 1
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 SEB C10 H13 N O5 S
FORMUL 2 EDO 4(C2 H6 O2)
FORMUL 6 NA NA 1+
FORMUL 7 HOH *155(H2 O)
HELIX 1 1 ASP A 10 THR A 19 5 10
HELIX 2 2 GLU A 27 LYS A 50 1 24
HELIX 3 3 ASP A 94 SER A 98 5 5
HELIX 4 4 ILE A 101 ARG A 108 1 8
HELIX 5 5 THR A 124 THR A 146 1 23
HELIX 6 6 SEB A 157 ALA A 164 1 8
HELIX 7 7 GLN A 165 ARG A 169 5 5
HELIX 8 8 THR A 174 MET A 180 1 7
HELIX 9 9 GLU A 195 LEU A 199 5 5
HELIX 10 10 ASN A 203 ILE A 207 5 5
HELIX 11 11 SER A 219 TRP A 223 5 5
HELIX 12 12 ASP A 227 ASN A 232 5 6
HELIX 13 13 SER A 245 GLY A 263 1 19
HELIX 14 14 PHE A 277 GLU A 282 1 6
HELIX 15 15 THR A 283 ILE A 285 5 3
HELIX 16 16 SER A 288 GLU A 298 1 11
SHEET 1 A 8 THR A 54 ARG A 59 0
SHEET 2 A 8 LEU A 66 TYR A 71 -1 O TYR A 71 N THR A 54
SHEET 3 A 8 ARG A 111 MET A 115 -1 O VAL A 114 N ASP A 68
SHEET 4 A 8 LEU A 81 VAL A 85 1 N PHE A 82 O ALA A 113
SHEET 5 A 8 LEU A 151 HIS A 156 1 O THR A 152 N VAL A 83
SHEET 6 A 8 VAL A 181 LEU A 187 1 O TRP A 182 N LEU A 151
SHEET 7 A 8 LYS A 235 HIS A 243 1 O TYR A 237 N PHE A 186
SHEET 8 A 8 ALA A 266 ASP A 275 1 O SER A 267 N VAL A 238
LINK C HIS A 156 N SEB A 157 1555 1555 1.34
LINK C SEB A 157 N ALA A 158 1555 1555 1.35
LINK NA NA A 405 O HOH A 503 1555 1555 2.19
LINK NA NA A 405 O HOH A 502 1555 1555 2.24
LINK OG ASER A 150 NA NA A 405 1555 1555 2.29
CISPEP 1 CYS A 120 PRO A 121 0 13.30
SITE 1 AC1 6 THR A 48 GLU A 49 TRP A 138 TYR A 142
SITE 2 AC1 6 HOH A 504 HOH A 510
SITE 1 AC2 10 ILE A 166 LEU A 167 MET A 168 ARG A 169
SITE 2 AC2 10 PRO A 170 ILE A 173 SER A 178 ASP A 227
SITE 3 AC2 10 VAL A 230 TRP A 231
SITE 1 AC3 6 LYS A 50 HIS A 57 LEU A 58 ARG A 59
SITE 2 AC3 6 HOH A 512 HOH A 599
SITE 1 AC4 6 HIS A 86 GLY A 87 MET A 93 MET A 97
SITE 2 AC4 6 SER A 98 HIS A 156
SITE 1 AC5 4 SER A 149 SER A 150 HOH A 502 HOH A 503
CRYST1 75.471 47.029 85.282 90.00 90.56 90.00 C 1 2 1 4
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 0.013250 0.000000 0.000130 0.00000
SCALE2 0.000000 0.021263 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011726 0.00000
TER 2493 ILE A 299
MASTER 359 0 6 16 8 0 10 6 2642 1 38 24
END |