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HEADER HYDROLASE/HYDROLASE INHIBITOR 05-MAR-12 4E15
TITLE CRYSTAL STRUCTURE OF KYNURENINE FORMAMIDASE CONJUGATED WITH AN
TITLE 2 INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KYNURENINE FORMAMIDASE;
COMPND 3 CHAIN: A, B;
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 4E15 1 JRNL
REVDAT 1 27-JUN-12 4E15 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. 1.50 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) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.5
REMARK 3 NUMBER OF REFLECTIONS : 85145
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) : 0.172
REMARK 3 R VALUE (WORKING SET) : 0.171
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 : 4501
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) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.54
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5374
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 84.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2090
REMARK 3 BIN FREE R VALUE SET COUNT : 307
REMARK 3 BIN FREE R VALUE : 0.2480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4967
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 515
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.87
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.05000
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): 0.078
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.077
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5108 ; 0.024 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6920 ; 2.070 ; 1.941
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 603 ; 6.169 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 259 ;30.593 ;23.514
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 856 ;13.632 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;14.202 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 753 ; 0.140 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3902 ; 0.012 ; 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): 3013 ; 1.289 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4896 ; 2.086 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2095 ; 3.408 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2024 ; 5.128 ; 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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4E15 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 RCSB071037.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
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 : 90494
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
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 : 14.300
REMARK 200 R MERGE (I) : 0.15000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 25.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.55
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 12.50
REMARK 200 R MERGE FOR SHELL (I) : 0.34000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.000
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 (%): 39.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 7.5, 18% PEG4000, 8%
REMARK 280 2-PROPANOL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 105.18850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 105.18850
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 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.80100
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 38.01050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 35.80100
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 38.01050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 105.18850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.80100
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 38.01050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 105.18850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 35.80100
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 38.01050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 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 GLU A 300
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 TYR A 255 CE2 TYR A 255 CD2 0.104
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 11 NE - CZ - NH2 ANGL. DEV. = -5.2 DEGREES
REMARK 500 ARG A 21 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 21 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ARG A 194 NE - CZ - NH1 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ASP A 244 CB - CG - OD2 ANGL. DEV. = -9.9 DEGREES
REMARK 500 ASP A 257 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 ASP A 278 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ARG A 292 NE - CZ - NH1 ANGL. DEV. = -4.9 DEGREES
REMARK 500 ARG B 11 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG B 21 NE - CZ - NH1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 ARG B 177 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP B 275 CB - CG - OD1 ANGL. DEV. = 5.9 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 3 98.54 -162.59
REMARK 500 ASP A 8 97.35 -163.92
REMARK 500 MET A 93 152.91 75.42
REMARK 500 SEB A 157 -119.96 56.77
REMARK 500 MET A 168 38.54 -140.49
REMARK 500 HIS A 243 50.40 -97.84
REMARK 500 ASP B 8 99.99 -160.20
REMARK 500 MET B 93 152.45 81.03
REMARK 500 SEB B 157 -127.82 64.88
REMARK 500
REMARK 500 REMARK: NULL
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 EDO B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E11 RELATED DB: PDB
REMARK 900 RELATED ID: 4E14 RELATED DB: PDB
DBREF 4E15 A 1 300 UNP Q9VMC9 Q9VMC9_DROME 1 300
DBREF 4E15 B 1 300 UNP Q9VMC9 Q9VMC9_DROME 1 300
SEQADV 4E15 ALA A -2 UNP Q9VMC9 EXPRESSION TAG
SEQADV 4E15 GLY A -1 UNP Q9VMC9 EXPRESSION TAG
SEQADV 4E15 HIS A 0 UNP Q9VMC9 EXPRESSION TAG
SEQADV 4E15 ALA B -2 UNP Q9VMC9 EXPRESSION TAG
SEQADV 4E15 GLY B -1 UNP Q9VMC9 EXPRESSION TAG
SEQADV 4E15 HIS B 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
SEQRES 1 B 303 ALA GLY HIS MET TYR ASN PRO ARG CYS LYS ASP LEU ASP
SEQRES 2 B 303 ARG ASP TYR PHE PRO SER TYR HIS THR THR ARG PHE GLN
SEQRES 3 B 303 ASP GLN PRO GLU PRO ASN LEU ALA VAL LEU GLU HIS PHE
SEQRES 4 B 303 VAL ARG VAL THR LYS GLN HIS GLY ARG GLU LEU THR GLU
SEQRES 5 B 303 LYS GLN GLY ILE THR VAL ASP HIS LEU ARG TYR GLY GLU
SEQRES 6 B 303 GLY ARG GLN LEU VAL ASP VAL PHE TYR SER GLU LYS THR
SEQRES 7 B 303 THR ASN GLN ALA PRO LEU PHE VAL PHE VAL HIS GLY GLY
SEQRES 8 B 303 TYR TRP GLN GLU MET ASP MET SER MET SER CYS SER ILE
SEQRES 9 B 303 VAL GLY PRO LEU VAL ARG ARG GLY TYR ARG VAL ALA VAL
SEQRES 10 B 303 MET ASP TYR ASN LEU CYS PRO GLN VAL THR LEU GLU GLN
SEQRES 11 B 303 LEU MET THR GLN PHE THR HIS PHE LEU ASN TRP ILE PHE
SEQRES 12 B 303 ASP TYR THR GLU MET THR LYS VAL SER SER LEU THR PHE
SEQRES 13 B 303 ALA GLY HIS SEB ALA GLY ALA HIS LEU LEU ALA GLN ILE
SEQRES 14 B 303 LEU MET ARG PRO ASN VAL ILE THR ALA GLN ARG SER LYS
SEQRES 15 B 303 MET VAL TRP ALA LEU ILE PHE LEU CYS GLY VAL TYR ASP
SEQRES 16 B 303 LEU ARG GLU LEU SER ASN LEU GLU SER VAL ASN PRO LYS
SEQRES 17 B 303 ASN ILE LEU GLY LEU ASN GLU ARG ASN ILE GLU SER VAL
SEQRES 18 B 303 SER PRO MET LEU TRP GLU TYR THR ASP VAL THR VAL TRP
SEQRES 19 B 303 ASN SER THR LYS ILE TYR VAL VAL ALA ALA GLU HIS ASP
SEQRES 20 B 303 SER THR THR PHE ILE GLU GLN SER ARG HIS TYR ALA ASP
SEQRES 21 B 303 VAL LEU ARG LYS LYS GLY TYR LYS ALA SER PHE THR LEU
SEQRES 22 B 303 PHE LYS GLY TYR ASP HIS PHE ASP ILE ILE GLU GLU THR
SEQRES 23 B 303 ALA ILE ASP ASP SER ASP VAL SER ARG PHE LEU ARG ASN
SEQRES 24 B 303 ILE GLU ILE GLU
MODRES 4E15 SEB A 157 SER O-BENZYLSULFONYL-SERINE
MODRES 4E15 SEB B 157 SER O-BENZYLSULFONYL-SERINE
HET SEB A 157 16
HET SEB B 157 16
HET EDO A 401 4
HET EDO A 402 4
HET EDO A 403 4
HET EDO A 404 4
HET EDO B 401 4
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 SEB 2(C10 H13 N O5 S)
FORMUL 3 EDO 5(C2 H6 O2)
FORMUL 8 HOH *515(H2 O)
HELIX 1 1 ASP A 8 TYR A 13 1 6
HELIX 2 2 PHE A 14 THR A 19 5 6
HELIX 3 3 GLU A 27 LYS A 50 1 24
HELIX 4 4 ASP A 94 SER A 98 5 5
HELIX 5 5 ILE A 101 ARG A 108 1 8
HELIX 6 6 THR A 124 THR A 146 1 23
HELIX 7 7 SEB A 157 ALA A 164 1 8
HELIX 8 8 GLN A 165 ARG A 169 5 5
HELIX 9 9 THR A 174 MET A 180 1 7
HELIX 10 10 LEU A 193 ASN A 198 1 6
HELIX 11 11 ASN A 203 ILE A 207 5 5
HELIX 12 12 SER A 219 TRP A 223 5 5
HELIX 13 13 ASP A 227 ASN A 232 5 6
HELIX 14 14 SER A 245 GLY A 263 1 19
HELIX 15 15 PHE A 277 GLU A 282 1 6
HELIX 16 16 THR A 283 ILE A 285 5 3
HELIX 17 17 SER A 288 ILE A 299 1 12
HELIX 18 18 ASP B 8 TYR B 13 1 6
HELIX 19 19 PHE B 14 HIS B 18 5 5
HELIX 20 20 GLU B 27 LYS B 50 1 24
HELIX 21 21 ASP B 94 SER B 98 5 5
HELIX 22 22 ILE B 101 ARG B 108 1 8
HELIX 23 23 THR B 124 LYS B 147 1 24
HELIX 24 24 SEB B 157 ALA B 164 1 8
HELIX 25 25 GLN B 165 ARG B 169 5 5
HELIX 26 26 THR B 174 MET B 180 1 7
HELIX 27 27 GLU B 195 LEU B 199 5 5
HELIX 28 28 ASN B 203 ILE B 207 5 5
HELIX 29 29 SER B 219 TRP B 223 5 5
HELIX 30 30 ASP B 227 ASN B 232 5 6
HELIX 31 31 SER B 245 GLY B 263 1 19
HELIX 32 32 PHE B 277 GLU B 282 1 6
HELIX 33 33 THR B 283 ILE B 285 5 3
HELIX 34 34 SER B 288 GLU B 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 112 N PHE A 70
SHEET 4 A 8 LEU A 81 VAL A 85 1 N PHE A 84 O ALA A 113
SHEET 5 A 8 LEU A 151 HIS A 156 1 O ALA A 154 N VAL A 83
SHEET 6 A 8 VAL A 181 LEU A 187 1 O LEU A 187 N GLY A 155
SHEET 7 A 8 LYS A 235 HIS A 243 1 O TYR A 237 N LEU A 184
SHEET 8 A 8 ALA A 266 ASP A 275 1 O PHE A 271 N ALA A 240
SHEET 1 B 8 THR B 54 ARG B 59 0
SHEET 2 B 8 LEU B 66 TYR B 71 -1 O TYR B 71 N THR B 54
SHEET 3 B 8 ARG B 111 MET B 115 -1 O VAL B 114 N ASP B 68
SHEET 4 B 8 LEU B 81 VAL B 85 1 N PHE B 84 O ALA B 113
SHEET 5 B 8 LEU B 151 HIS B 156 1 O THR B 152 N VAL B 83
SHEET 6 B 8 VAL B 181 LEU B 187 1 O LEU B 187 N GLY B 155
SHEET 7 B 8 LYS B 235 ALA B 241 1 O VAL B 239 N PHE B 186
SHEET 8 B 8 ALA B 266 PHE B 271 1 O PHE B 271 N ALA B 240
LINK C HIS A 156 N SEB A 157 1555 1555 1.30
LINK C SEB A 157 N ALA A 158 1555 1555 1.43
LINK C HIS B 156 N SEB B 157 1555 1555 1.38
LINK C SEB B 157 N ALA B 158 1555 1555 1.33
CISPEP 1 CYS A 120 PRO A 121 0 12.55
CISPEP 2 CYS B 120 PRO B 121 0 15.58
SITE 1 AC1 6 LEU A 119 CYS A 120 PRO A 121 GLN A 122
SITE 2 AC1 6 HOH A 576 HOH A 594
SITE 1 AC2 5 LYS A 235 ILE A 236 TYR A 237 LYS A 265
SITE 2 AC2 5 SER A 267
SITE 1 AC3 6 THR A 76 ASN A 77 SER A 197 LEU A 199
SITE 2 AC3 6 GLU A 200 ASN A 203
SITE 1 AC4 7 PHE A 36 HIS A 86 GLY A 87 MET A 93
SITE 2 AC4 7 MET A 97 SER A 98 HIS A 156
SITE 1 AC5 7 PHE B 36 HIS B 86 GLY B 87 MET B 93
SITE 2 AC5 7 MET B 97 SER B 98 HIS B 156
CRYST1 71.602 76.021 210.377 90.00 90.00 90.00 C 2 2 21 16
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 0.013966 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013154 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004753 0.00000
TER 2480 ILE A 299
TER 4969 GLU B 300
MASTER 362 0 7 34 16 0 10 6 5502 2 56 48
END |