HEADER HYDROLASE 14-JAN-09 3FUI
TITLE LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH N-BENZYL-4-[(2R)-PYRROLIDIN-
TITLE 2 2-YLMETHOXY]ANILINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LEUKOTRIENE A(4) HYDROLASE, LTA-4 HYDROLASE;
COMPND 5 EC: 3.3.2.6;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LTA4H, LTA4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-AI/PRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS LEUKOTRIENE A4 HYDROLASE, LTA4H, FRAGMENT CRYSTALLOGRAPHY, FRAGMENTS
KEYWDS 2 OF LIFE, FOL, ALTERNATIVE SPLICING, CYTOPLASM, HYDROLASE,
KEYWDS 3 LEUKOTRIENE BIOSYNTHESIS, METAL-BINDING, METALLOPROTEASE,
KEYWDS 4 MULTIFUNCTIONAL ENZYME, POLYMORPHISM, PROTEASE, ZINC
EXPDTA X-RAY DIFFRACTION
AUTHOR D.R.DAVIES
REVDAT 4 06-SEP-23 3FUI 1 REMARK LINK
REVDAT 3 01-NOV-17 3FUI 1 REMARK
REVDAT 2 15-SEP-09 3FUI 1 JRNL
REVDAT 1 28-JUL-09 3FUI 0
JRNL AUTH D.R.DAVIES,B.MAMAT,O.T.MAGNUSSON,J.CHRISTENSEN,
JRNL AUTH 2 M.H.HARALDSSON,R.MISHRA,B.PEASE,E.HANSEN,J.SINGH,D.ZEMBOWER,
JRNL AUTH 3 H.KIM,A.S.KISELYOV,A.B.BURGIN,M.E.GURNEY,L.J.STEWART
JRNL TITL DISCOVERY OF LEUKOTRIENE A4 HYDROLASE INHIBITORS USING
JRNL TITL 2 METABOLOMICS BIASED FRAGMENT CRYSTALLOGRAPHY.
JRNL REF J.MED.CHEM. V. 52 4694 2009
JRNL REFN ISSN 0022-2623
JRNL PMID 19618939
JRNL DOI 10.1021/JM900259H
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0067
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 33387
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) : 0.184
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.244
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1680
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1902
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 101
REMARK 3 BIN FREE R VALUE : 0.3400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4846
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.32
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.02000
REMARK 3 B22 (A**2) : -2.33000
REMARK 3 B33 (A**2) : 2.31000
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): 0.282
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.156
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.213
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.953
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4998 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6790 ; 1.484 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 605 ; 6.263 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 222 ;37.321 ;24.414
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 855 ;15.985 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;21.268 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 753 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3770 ; 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): 3034 ; 0.637 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4928 ; 1.205 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1964 ; 2.235 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1862 ; 3.572 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3FUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-09.
REMARK 100 THE DEPOSITION ID IS D_1000051057.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54178
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33425
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.0
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.18900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28
REMARK 200 COMPLETENESS FOR SHELL (%) : 81.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.89000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 3FH7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 8000, 100 MM IMIDAZOLE PH 6.5,
REMARK 280 100 MM NA ACETATE, 5 MM YBCL3, CRYSTAL SOAKED WITH N-BENZYL-4-
REMARK 280 [(2R)-PYRROLIDIN-2-YLMETHOXY]ANILINE, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 39.11050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.70400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.48600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.70400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.11050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.48600
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 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; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 PRO A 1
REMARK 465 GLU A 2
REMARK 465 ILE A 3
REMARK 465 VAL A 4
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 CD LYS A 242 O HOH A 1615 2.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1008 O HOH A 1611 1565 2.15
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 LEU A 52 CA - CB - CG ANGL. DEV. = 16.6 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 GLN A 79 61.63 -108.10
REMARK 500 SER A 80 -133.75 63.05
REMARK 500 ASN A 97 -1.98 81.93
REMARK 500 ASP A 183 99.27 175.05
REMARK 500 GLU A 271 44.93 -72.18
REMARK 500 CYS A 274 -19.40 76.61
REMARK 500 LEU A 275 88.45 -152.90
REMARK 500 SER A 379 -174.73 -171.79
REMARK 500 PHE A 432 41.42 -108.45
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 YB A 701 YB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 47 OD1
REMARK 620 2 ASP A 47 OD2 49.7
REMARK 620 3 ASP A 481 OD1 28.5 39.1
REMARK 620 4 ASP A 481 OD2 28.5 38.8 0.3
REMARK 620 5 HOH A1008 O 128.7 79.0 109.9 109.7
REMARK 620 6 HOH A1034 O 67.7 79.0 92.7 92.6 106.7
REMARK 620 7 HOH A1135 O 83.3 132.9 100.0 100.2 148.0 82.4
REMARK 620 8 HOH A1611 O 126.6 91.0 98.1 98.1 41.9 148.6 124.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 704 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 295 NE2
REMARK 620 2 HIS A 299 NE2 97.0
REMARK 620 3 GLU A 318 OE1 102.2 99.5
REMARK 620 4 HOH A1153 O 105.7 130.0 117.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 YB A 703 YB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 426 OD2
REMARK 620 2 HOH A1155 O 94.5
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 YB A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YB A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 812 A 710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 801
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FH7 RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH INHIBITOR 4-[(2S)-2-{[4-(4-
REMARK 900 CHLOROPHENOXY)PHENOXY]METHYL}PYRROLIDIN-1-YL]BUTANOATE
REMARK 900 RELATED ID: 3FTS RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH RESVERATROL
REMARK 900 RELATED ID: 3FTU RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH DIHYDRORESVERATROL
REMARK 900 RELATED ID: 3FTV RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT N-(PYRIDIN-3-
REMARK 900 YLMETHYL)ANILINE
REMARK 900 RELATED ID: 3FTW RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENTS N-(PYRIDIN-3-
REMARK 900 YLMETHYL)ANILINE AND ACETATE
REMARK 900 RELATED ID: 3FTX RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH DIHYDRORESVERATROL AND
REMARK 900 BESTATIN
REMARK 900 RELATED ID: 3FTY RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 3-(BENZYLOXY)
REMARK 900 PYRIDIN-2-AMINE
REMARK 900 RELATED ID: 3FTZ RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 2-(PYRIDIN-3-
REMARK 900 YLMETHOXY)ANILINE
REMARK 900 RELATED ID: 3FU0 RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 4-(4-
REMARK 900 FLUOROBENZOYL)PYRIDINE
REMARK 900 RELATED ID: 3FU3 RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 4-(2-AMINO-1,3-
REMARK 900 THIAZOL-4-YL)PHENOL
REMARK 900 RELATED ID: 3FU5 RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (5-THIOPHEN-2-YLTHIOPHEN-2-
REMARK 900 YL)METHYLAMINE
REMARK 900 RELATED ID: 3FU6 RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT (4-THIOPHEN-2-
REMARK 900 YLPHENYL)METHANAMINE
REMARK 900 RELATED ID: 3FUD RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH N-METHYL-1-(2-THIOPHEN-2-
REMARK 900 YLPHENYL)METHANAMINE
REMARK 900 RELATED ID: 3FUE RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 5-CHLOROINDOLE
REMARK 900 AND BESTATIN
REMARK 900 RELATED ID: 3FUF RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 5-FLUOROINDOLE
REMARK 900 AND BESTATIN
REMARK 900 RELATED ID: 3FUH RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH FRAGMENT 5-HYDROXYINDOLE
REMARK 900 AND BESTATIN
REMARK 900 RELATED ID: 3FUJ RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 5-[2-(1H-PYRROL-1-YL)
REMARK 900 ETHOXY]-1H-INDOLE
REMARK 900 RELATED ID: 3FUK RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH 1-[2-(1H-INDOL-5-YLOXY)
REMARK 900 ETHYL]PIPERIDINE-4-CARBOXYLIC ACID
REMARK 900 RELATED ID: 3FUL RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH PYRIDIN-4-YL[4-(2-
REMARK 900 PYRROLIDIN-1-YLETHOXY)PHENYL]METHANONE
REMARK 900 RELATED ID: 3FUM RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH (R)-PYRIDIN-4-YL[4-(2-
REMARK 900 PYRROLIDIN-1-YLETHOXY)PHENYL]METHANOL
REMARK 900 RELATED ID: 3FUN RELATED DB: PDB
REMARK 900 LEUKOTRIENE A4 HYDROLASE IN COMPLEX WITH {4-[(2R)-PYRROLIDIN-2-
REMARK 900 YLMETHOXY]PHENYL}(4-THIOPHEN-3-YLPHENYL)METHANONE
DBREF 3FUI A 0 610 UNP P09960 LKHA4_HUMAN 1 611
SEQRES 1 A 611 MET PRO GLU ILE VAL ASP THR CYS SER LEU ALA SER PRO
SEQRES 2 A 611 ALA SER VAL CYS ARG THR LYS HIS LEU HIS LEU ARG CYS
SEQRES 3 A 611 SER VAL ASP PHE THR ARG ARG THR LEU THR GLY THR ALA
SEQRES 4 A 611 ALA LEU THR VAL GLN SER GLN GLU ASP ASN LEU ARG SER
SEQRES 5 A 611 LEU VAL LEU ASP THR LYS ASP LEU THR ILE GLU LYS VAL
SEQRES 6 A 611 VAL ILE ASN GLY GLN GLU VAL LYS TYR ALA LEU GLY GLU
SEQRES 7 A 611 ARG GLN SER TYR LYS GLY SER PRO MET GLU ILE SER LEU
SEQRES 8 A 611 PRO ILE ALA LEU SER LYS ASN GLN GLU ILE VAL ILE GLU
SEQRES 9 A 611 ILE SER PHE GLU THR SER PRO LYS SER SER ALA LEU GLN
SEQRES 10 A 611 TRP LEU THR PRO GLU GLN THR SER GLY LYS GLU HIS PRO
SEQRES 11 A 611 TYR LEU PHE SER GLN CYS GLN ALA ILE HIS CYS ARG ALA
SEQRES 12 A 611 ILE LEU PRO CYS GLN ASP THR PRO SER VAL LYS LEU THR
SEQRES 13 A 611 TYR THR ALA GLU VAL SER VAL PRO LYS GLU LEU VAL ALA
SEQRES 14 A 611 LEU MET SER ALA ILE ARG ASP GLY GLU THR PRO ASP PRO
SEQRES 15 A 611 GLU ASP PRO SER ARG LYS ILE TYR LYS PHE ILE GLN LYS
SEQRES 16 A 611 VAL PRO ILE PRO CYS TYR LEU ILE ALA LEU VAL VAL GLY
SEQRES 17 A 611 ALA LEU GLU SER ARG GLN ILE GLY PRO ARG THR LEU VAL
SEQRES 18 A 611 TRP SER GLU LYS GLU GLN VAL GLU LYS SER ALA TYR GLU
SEQRES 19 A 611 PHE SER GLU THR GLU SER MET LEU LYS ILE ALA GLU ASP
SEQRES 20 A 611 LEU GLY GLY PRO TYR VAL TRP GLY GLN TYR ASP LEU LEU
SEQRES 21 A 611 VAL LEU PRO PRO SER PHE PRO TYR GLY GLY MET GLU ASN
SEQRES 22 A 611 PRO CYS LEU THR PHE VAL THR PRO THR LEU LEU ALA GLY
SEQRES 23 A 611 ASP LYS SER LEU SER ASN VAL ILE ALA HIS GLU ILE SER
SEQRES 24 A 611 HIS SER TRP THR GLY ASN LEU VAL THR ASN LYS THR TRP
SEQRES 25 A 611 ASP HIS PHE TRP LEU ASN GLU GLY HIS THR VAL TYR LEU
SEQRES 26 A 611 GLU ARG HIS ILE CYS GLY ARG LEU PHE GLY GLU LYS PHE
SEQRES 27 A 611 ARG HIS PHE ASN ALA LEU GLY GLY TRP GLY GLU LEU GLN
SEQRES 28 A 611 ASN SER VAL LYS THR PHE GLY GLU THR HIS PRO PHE THR
SEQRES 29 A 611 LYS LEU VAL VAL ASP LEU THR ASP ILE ASP PRO ASP VAL
SEQRES 30 A 611 ALA TYR SER SER VAL PRO TYR GLU LYS GLY PHE ALA LEU
SEQRES 31 A 611 LEU PHE TYR LEU GLU GLN LEU LEU GLY GLY PRO GLU ILE
SEQRES 32 A 611 PHE LEU GLY PHE LEU LYS ALA TYR VAL GLU LYS PHE SER
SEQRES 33 A 611 TYR LYS SER ILE THR THR ASP ASP TRP LYS ASP PHE LEU
SEQRES 34 A 611 TYR SER TYR PHE LYS ASP LYS VAL ASP VAL LEU ASN GLN
SEQRES 35 A 611 VAL ASP TRP ASN ALA TRP LEU TYR SER PRO GLY LEU PRO
SEQRES 36 A 611 PRO ILE LYS PRO ASN TYR ASP MET THR LEU THR ASN ALA
SEQRES 37 A 611 CYS ILE ALA LEU SER GLN ARG TRP ILE THR ALA LYS GLU
SEQRES 38 A 611 ASP ASP LEU ASN SER PHE ASN ALA THR ASP LEU LYS ASP
SEQRES 39 A 611 LEU SER SER HIS GLN LEU ASN GLU PHE LEU ALA GLN THR
SEQRES 40 A 611 LEU GLN ARG ALA PRO LEU PRO LEU GLY HIS ILE LYS ARG
SEQRES 41 A 611 MET GLN GLU VAL TYR ASN PHE ASN ALA ILE ASN ASN SER
SEQRES 42 A 611 GLU ILE ARG PHE ARG TRP LEU ARG LEU CYS ILE GLN SER
SEQRES 43 A 611 LYS TRP GLU ASP ALA ILE PRO LEU ALA LEU LYS MET ALA
SEQRES 44 A 611 THR GLU GLN GLY ARG MET LYS PHE THR ARG PRO LEU PHE
SEQRES 45 A 611 LYS ASP LEU ALA ALA PHE ASP LYS SER HIS ASP GLN ALA
SEQRES 46 A 611 VAL ARG THR TYR GLN GLU HIS LYS ALA SER MET HIS PRO
SEQRES 47 A 611 VAL THR ALA MET LEU VAL GLY LYS ASP LEU LYS VAL ASP
HET YB A 701 1
HET YB A 702 1
HET YB A 703 1
HET ZN A 704 1
HET 812 A 710 21
HET IMD A 801 5
HETNAM YB YTTERBIUM (III) ION
HETNAM ZN ZINC ION
HETNAM 812 N-BENZYL-4-[(2R)-PYRROLIDIN-2-YLMETHOXY]ANILINE
HETNAM IMD IMIDAZOLE
FORMUL 2 YB 3(YB 3+)
FORMUL 5 ZN ZN 2+
FORMUL 6 812 C18 H22 N2 O
FORMUL 7 IMD C3 H5 N2 1+
FORMUL 8 HOH *294(H2 O)
HELIX 1 1 GLN A 79 GLY A 83 5 5
HELIX 2 2 THR A 119 THR A 123 5 5
HELIX 3 3 HIS A 139 ILE A 143 5 5
HELIX 4 4 TYR A 200 ILE A 202 5 3
HELIX 5 5 GLU A 223 GLU A 225 5 3
HELIX 6 6 GLN A 226 PHE A 234 1 9
HELIX 7 7 GLU A 236 GLY A 249 1 14
HELIX 8 8 PRO A 280 LEU A 283 5 4
HELIX 9 9 SER A 290 HIS A 299 1 10
HELIX 10 10 THR A 310 HIS A 313 5 4
HELIX 11 11 PHE A 314 GLY A 334 1 21
HELIX 12 12 GLY A 334 GLY A 357 1 24
HELIX 13 13 HIS A 360 LYS A 364 5 5
HELIX 14 14 ASP A 373 TYR A 378 1 6
HELIX 15 15 SER A 380 LEU A 397 1 18
HELIX 16 16 GLY A 399 SER A 415 1 17
HELIX 17 17 THR A 420 PHE A 432 1 13
HELIX 18 18 LYS A 435 ASN A 440 1 6
HELIX 19 19 ASP A 443 SER A 450 1 8
HELIX 20 20 THR A 465 ALA A 478 1 14
HELIX 21 21 LYS A 479 PHE A 486 5 8
HELIX 22 22 ASN A 487 LYS A 492 5 6
HELIX 23 23 SER A 495 GLN A 508 1 14
HELIX 24 24 PRO A 513 ASN A 525 1 13
HELIX 25 25 PHE A 526 ILE A 529 5 4
HELIX 26 26 ASN A 531 SER A 545 1 15
HELIX 27 27 ASP A 549 GLN A 561 1 13
HELIX 28 28 ARG A 563 PHE A 577 1 15
HELIX 29 29 SER A 580 LYS A 592 1 13
HELIX 30 30 ALA A 593 MET A 595 5 3
HELIX 31 31 HIS A 596 LEU A 607 1 12
SHEET 1 A 8 GLN A 69 GLU A 70 0
SHEET 2 A 8 LEU A 59 ILE A 66 -1 N ILE A 66 O GLN A 69
SHEET 3 A 8 GLU A 99 THR A 108 -1 O GLU A 107 N THR A 60
SHEET 4 A 8 THR A 33 SER A 44 -1 N LEU A 40 O ILE A 102
SHEET 5 A 8 CYS A 16 ASP A 28 -1 N ASP A 28 O THR A 33
SHEET 6 A 8 LYS A 153 PRO A 163 1 O SER A 161 N CYS A 25
SHEET 7 A 8 ARG A 186 PRO A 198 -1 O GLN A 193 N TYR A 156
SHEET 8 A 8 ILE A 173 PRO A 179 -1 N THR A 178 O ILE A 188
SHEET 1 B 3 LEU A 49 THR A 56 0
SHEET 2 B 3 SER A 84 LEU A 94 -1 O ILE A 88 N LEU A 52
SHEET 3 B 3 TYR A 73 LEU A 75 -1 N ALA A 74 O GLU A 87
SHEET 1 C 4 LEU A 115 LEU A 118 0
SHEET 2 C 4 TYR A 130 SER A 133 -1 O TYR A 130 N LEU A 118
SHEET 3 C 4 LEU A 204 GLY A 207 -1 O VAL A 206 N LEU A 131
SHEET 4 C 4 VAL A 167 MET A 170 -1 N VAL A 167 O GLY A 207
SHEET 1 D 5 GLU A 210 GLY A 215 0
SHEET 2 D 5 THR A 218 SER A 222 -1 O SER A 222 N GLU A 210
SHEET 3 D 5 ASP A 257 VAL A 260 1 O VAL A 260 N TRP A 221
SHEET 4 D 5 LEU A 275 VAL A 278 1 O VAL A 278 N LEU A 259
SHEET 5 D 5 GLY A 269 MET A 270 -1 N MET A 270 O PHE A 277
SHEET 1 E 2 VAL A 306 ASN A 308 0
SHEET 2 E 2 LYS A 417 ILE A 419 1 O ILE A 419 N THR A 307
LINK OD1 ASP A 47 YB YB A 701 1555 1555 2.77
LINK OD2 ASP A 47 YB YB A 701 1555 1555 2.59
LINK OD1 ASP A 175 YB YB A 702 1555 1555 2.64
LINK NE2 HIS A 295 ZN ZN A 704 1555 1555 2.25
LINK NE2 HIS A 299 ZN ZN A 704 1555 1555 2.22
LINK OE1 GLU A 318 ZN ZN A 704 1555 1555 1.99
LINK OD2 ASP A 426 YB YB A 703 1555 1555 3.13
LINK OD1 ASP A 481 YB YB A 701 1555 1545 2.56
LINK OD2 ASP A 481 YB YB A 701 1555 1545 2.61
LINK YB YB A 701 O HOH A1008 1555 1555 3.22
LINK YB YB A 701 O HOH A1034 1555 1555 2.27
LINK YB YB A 701 O HOH A1135 1555 1565 2.45
LINK YB YB A 701 O HOH A1611 1555 1565 2.26
LINK YB YB A 703 O HOH A1155 1555 2555 2.61
LINK ZN ZN A 704 O HOH A1153 1555 1555 2.00
CISPEP 1 GLN A 136 ALA A 137 0 4.68
CISPEP 2 ALA A 510 PRO A 511 0 2.92
SITE 1 AC1 5 ASP A 47 ASP A 481 HOH A1034 HOH A1135
SITE 2 AC1 5 HOH A1611
SITE 1 AC2 1 ASP A 175
SITE 1 AC3 3 ASP A 426 ASP A 610 HOH A1155
SITE 1 AC4 4 HIS A 295 HIS A 299 GLU A 318 HOH A1153
SITE 1 AC5 11 GLN A 134 GLN A 136 TYR A 267 GLY A 269
SITE 2 AC5 11 MET A 270 TRP A 311 PHE A 314 VAL A 367
SITE 3 AC5 11 PRO A 374 ALA A 377 TYR A 378
SITE 1 AC6 7 GLY A 344 GLY A 347 GLU A 348 ASN A 351
SITE 2 AC6 7 GLU A 501 ALA A 504 GLN A 508
CRYST1 78.221 86.972 99.408 90.00 90.00 90.00 P 21 21 21 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 0.012784 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010060 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
