HEADER HYDROLASE 31-OCT-07 3B7T
TITLE [E296Q]LTA4H IN COMPLEX WITH ARG-ALA-ARG SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LTA-4 HYDROLASE,LEUKOTRIENE A(4) HYDROLASE,TRIPEPTIDE
COMPND 5 AMINOPEPTIDASE LTA4H;
COMPND 6 EC: 3.3.2.6,3.4.11.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: RAR PEPTIDE;
COMPND 11 CHAIN: B;
COMPND 12 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: JM101;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PT7T3;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS TRANSITION STATE, ANALOGUE PEPTIDE, HYDROLYSIS, ALTERNATIVE SPLICING,
KEYWDS 2 CYTOPLASM, HYDROLASE, LEUKOTRIENE BIOSYNTHESIS, METAL-BINDING,
KEYWDS 3 METALLOPROTEASE, MULTIFUNCTIONAL ENZYME, PROTEASE, ZINC, TRIPEPTIDE
KEYWDS 4 SUBSTRATE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.THOLANDER,J.HAEGGSTROM,M.THUNNISSEN,A.MUROYA,B.-P.ROQUES,M.-
AUTHOR 2 C.FOURNIE-ZALUSKI
REVDAT 7 30-AUG-23 3B7T 1 REMARK
REVDAT 6 20-OCT-21 3B7T 1 COMPND SOURCE REMARK DBREF
REVDAT 6 2 1 SEQADV LINK
REVDAT 5 20-NOV-19 3B7T 1 SEQADV LINK
REVDAT 4 07-MAR-18 3B7T 1 REMARK
REVDAT 3 24-FEB-09 3B7T 1 VERSN
REVDAT 2 07-OCT-08 3B7T 1 JRNL
REVDAT 1 16-SEP-08 3B7T 0
JRNL AUTH F.THOLANDER,A.MUROYA,B.P.ROQUES,M.C.FOURNIE-ZALUSKI,
JRNL AUTH 2 M.M.THUNNISSEN,J.Z.HAEGGSTROM
JRNL TITL STRUCTURE-BASED DISSECTION OF THE ACTIVE SITE CHEMISTRY OF
JRNL TITL 2 LEUKOTRIENE A4 HYDROLASE: IMPLICATIONS FOR M1
JRNL TITL 3 AMINOPEPTIDASES AND INHIBITOR DESIGN.
JRNL REF CHEM.BIOL. V. 15 920 2008
JRNL REFN ISSN 1074-5521
JRNL PMID 18804029
JRNL DOI 10.1016/J.CHEMBIOL.2008.07.018
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.THOLANDER,J.Z.HAEGGSTROM
REMARK 1 TITL ASSAY FOR RAPID ANALYSIS OF THE TRI-PEPTIDASE ACTIVITY OF
REMARK 1 TITL 2 LTA4 HYDROLASE.
REMARK 1 REF PROTEINS V. 67 1113 2007
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 17357161
REMARK 1 DOI 10.1002/PROT.21329
REMARK 1 REFERENCE 2
REMARK 1 AUTH P.C.RUDBERG,F.THOLANDER,M.ANDBERG,M.M.THUNNISSEN,
REMARK 1 AUTH 2 J.Z.HAEGGSTROM
REMARK 1 TITL LEUKOTRIENE A4 HYDROLASE: IDENTIFICATION OF A COMMON
REMARK 1 TITL 2 CARBOXYLATE RECOGNITION SITE FOR THE EPOXIDE HYDROLASE AND
REMARK 1 TITL 3 AMINOPEPTIDASE SUBSTRATES.
REMARK 1 REF J.BIOL.CHEM. V. 279 27376 2004
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 15078870
REMARK 1 DOI 10.1074/JBC.M401031200
REMARK 1 REFERENCE 3
REMARK 1 AUTH P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,J.Z.HAEGGSTROM
REMARK 1 TITL LEUKOTRIENE A4 HYDROLASE/AMINOPEPTIDASE. GLUTAMATE 271 IS A
REMARK 1 TITL 2 CATALYTIC RESIDUE WITH SPECIFIC ROLES IN TWO DISTINCT ENZYME
REMARK 1 TITL 3 MECHANISMS.
REMARK 1 REF J.BIOL.CHEM. V. 277 1398 2002
REMARK 1 REFN ISSN 0021-9258
REMARK 1 PMID 11675384
REMARK 1 DOI 10.1074/JBC.M106577200
REMARK 1 REFERENCE 4
REMARK 1 AUTH P.C.RUDBERG,F.THOLANDER,M.M.THUNNISSEN,B.SAMUELSSON,
REMARK 1 AUTH 2 J.Z.HAEGGSTROM
REMARK 1 TITL LEUKOTRIENE A4 HYDROLASE: SELECTIVE ABROGATION OF
REMARK 1 TITL 2 LEUKOTRIENE B4 FORMATION BY MUTATION OF ASPARTIC ACID 375.
REMARK 1 REF PROC.NATL.ACAD.SCI.USA V. 99 4215 2002
REMARK 1 REFN ISSN 0027-8424
REMARK 1 PMID 11917124
REMARK 1 DOI 10.1073/PNAS.072090099
REMARK 1 REFERENCE 5
REMARK 1 AUTH M.M.THUNNISSEN,P.NORDLUND,J.Z.HAEGGSTROM
REMARK 1 TITL CRYSTAL STRUCTURE OF HUMAN LEUKOTRIENE A(4) HYDROLASE, A
REMARK 1 TITL 2 BIFUNCTIONAL ENZYME IN INFLAMMATION.
REMARK 1 REF NAT.STRUCT.BIOL. V. 8 131 2001
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 11175901
REMARK 1 DOI 10.1038/84117
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.5
REMARK 3 NUMBER OF REFLECTIONS : 57183
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 SET) : 0.206
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.300
REMARK 3 FREE R VALUE TEST SET COUNT : 1902
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.006
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.40
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6960
REMARK 3 BIN R VALUE (WORKING SET) : 0.2940
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 254
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4903
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 8
REMARK 3 SOLVENT ATOMS : 31
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 4.92000
REMARK 3 B22 (A**2) : -5.86000
REMARK 3 B33 (A**2) : 0.94000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.29
REMARK 3 ESD FROM SIGMAA (A) : 0.37
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.38
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.43
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : CNS BULK SOLVENT MODEL USED
REMARK 3 KSOL : 0.38
REMARK 3 BSOL : 42.08
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3B7T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-NOV-07.
REMARK 100 THE DEPOSITION ID IS D_1000045186.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-OCT-05
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 : MAX II
REMARK 200 BEAMLINE : I711
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS, XFIT
REMARK 200 DATA SCALING SOFTWARE : XSCALE, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57220
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 43.420
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.12500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.54
REMARK 200 R MERGE FOR SHELL (I) : 0.80100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: XFIT
REMARK 200 STARTING MODEL: PDB ENTRY 1H19
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRI-PEPTIDE WAS CO-CRYSTALLIZED WITH
REMARK 280 [E296Q]LTA4H BY LIQUID-LIQUID DIFFUSION IN MELTING-POINT
REMARK 280 CAPILLARIES. A TRIS-BUFFERED (10 MM, PH 7.5) SOLUTION OF PROTEIN
REMARK 280 AND TRIPEPTIDE, MOLAR RATIO 1:10 (~70 MICROM PROTEIN), WAS
REMARK 280 LAYERED ON THE PRECIPITATE SOLUTION CONTAINING 28% (WEIGHT/
REMARK 280 VOLUME) POLYETHYLENE GLYCOL (MW 8000), 50 MM NA ACETATE, 100 MM
REMARK 280 IMIDAZOLE, PH 6.8, AND 5 MM YBCL3. CRYSTALS WERE ADDITIONALLY
REMARK 280 SOAKED IN SOLUTIONS WITH INCREASED TRI-PEPTIDE CONCENTRATION
REMARK 280 PRIOR TO DATA COLLECTION, LIQUID-LIQUID DIFFUSION, TEMPERATURE
REMARK 280 298K
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 39.24500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 49.95800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.89250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 49.95800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 39.24500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 43.89250
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1580 ANGSTROM**2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
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 SER A 80 -134.75 45.36
REMARK 500 LYS A 126 -1.92 71.43
REMARK 500 ASP A 183 105.29 176.00
REMARK 500 SER A 222 177.18 175.61
REMARK 500 GLU A 271 46.66 -75.30
REMARK 500 CYS A 274 -19.97 72.64
REMARK 500 TRP A 301 -74.28 -119.97
REMARK 500 LEU A 369 24.29 -73.78
REMARK 500 SER A 379 -166.14 -169.99
REMARK 500 PRO A 458 -177.95 -60.82
REMARK 500 THR A 463 -70.49 -27.68
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 702 YB
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 47 OD1
REMARK 620 2 ASP A 47 OD2 51.3
REMARK 620 3 ASP A 481 OD1 35.9 29.3
REMARK 620 4 ASP A 481 OD2 36.3 29.2 0.4
REMARK 620 5 HOH A 709 O 33.6 29.9 2.4 2.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 295 NE2
REMARK 620 2 HIS A 299 NE2 98.6
REMARK 620 3 GLU A 318 OE1 96.8 104.4
REMARK 620 4 GLU A 318 OE2 150.8 92.3 54.2
REMARK 620 5 ARG B 702 N 135.4 98.6 118.1 68.4
REMARK 620 6 ARG B 702 O 85.8 165.9 88.3 90.2 69.4
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 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 IMD A 704
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R59 RELATED DB: PDB
REMARK 900 SAME ENZYME COMPLEXED WITH INHIBITOR RB3041
REMARK 900 RELATED ID: 3B7R RELATED DB: PDB
REMARK 900 RELATED ID: 3B7S RELATED DB: PDB
REMARK 900 RELATED ID: 3B7U RELATED DB: PDB
DBREF 3B7T A 1 610 UNP P09960 LKHA4_HUMAN 2 611
DBREF 3B7T B 702 704 PDB 3B7T 3B7T 702 704
SEQADV 3B7T HIS A -5 UNP P09960 EXPRESSION TAG
SEQADV 3B7T HIS A -4 UNP P09960 EXPRESSION TAG
SEQADV 3B7T HIS A -3 UNP P09960 EXPRESSION TAG
SEQADV 3B7T HIS A -2 UNP P09960 EXPRESSION TAG
SEQADV 3B7T HIS A -1 UNP P09960 EXPRESSION TAG
SEQADV 3B7T HIS A 0 UNP P09960 EXPRESSION TAG
SEQADV 3B7T GLN A 296 UNP P09960 GLU 297 ENGINEERED MUTATION
SEQRES 1 A 616 HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR CYS
SEQRES 2 A 616 SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS HIS
SEQRES 3 A 616 LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG THR
SEQRES 4 A 616 LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN GLU
SEQRES 5 A 616 ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP LEU
SEQRES 6 A 616 THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL LYS
SEQRES 7 A 616 TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER PRO
SEQRES 8 A 616 MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN GLN
SEQRES 9 A 616 GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO LYS
SEQRES 10 A 616 SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR SER
SEQRES 11 A 616 GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN ALA
SEQRES 12 A 616 ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR PRO
SEQRES 13 A 616 SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL PRO
SEQRES 14 A 616 LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP GLY
SEQRES 15 A 616 GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE TYR
SEQRES 16 A 616 LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU ILE
SEQRES 17 A 616 ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE GLY
SEQRES 18 A 616 PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL GLU
SEQRES 19 A 616 LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET LEU
SEQRES 20 A 616 LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP GLY
SEQRES 21 A 616 GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO TYR
SEQRES 22 A 616 GLY GLY MET GLU ASN PRO CYS LEU THR PHE VAL THR PRO
SEQRES 23 A 616 THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL ILE
SEQRES 24 A 616 ALA HIS GLN ILE SER HIS SER TRP THR GLY ASN LEU VAL
SEQRES 25 A 616 THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU GLY
SEQRES 26 A 616 HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG LEU
SEQRES 27 A 616 PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY GLY
SEQRES 28 A 616 TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY GLU
SEQRES 29 A 616 THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR ASP
SEQRES 30 A 616 ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR GLU
SEQRES 31 A 616 LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU LEU
SEQRES 32 A 616 GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA TYR
SEQRES 33 A 616 VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP ASP
SEQRES 34 A 616 TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS VAL
SEQRES 35 A 616 ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU TYR
SEQRES 36 A 616 SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP MET
SEQRES 37 A 616 THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG TRP
SEQRES 38 A 616 ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN ALA
SEQRES 39 A 616 THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN GLU
SEQRES 40 A 616 PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO LEU
SEQRES 41 A 616 GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE ASN
SEQRES 42 A 616 ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU ARG
SEQRES 43 A 616 LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO LEU
SEQRES 44 A 616 ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS PHE
SEQRES 45 A 616 THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP LYS
SEQRES 46 A 616 SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS LYS
SEQRES 47 A 616 ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY LYS
SEQRES 48 A 616 ASP LEU LYS VAL ASP
SEQRES 1 B 3 ARG ALA ARG
HET ZN A 701 1
HET YB A 702 1
HET YB A 703 1
HET IMD A 704 5
HETNAM ZN ZINC ION
HETNAM YB YTTERBIUM (III) ION
HETNAM IMD IMIDAZOLE
FORMUL 3 ZN ZN 2+
FORMUL 4 YB 2(YB 3+)
FORMUL 6 IMD C3 H5 N2 1+
FORMUL 7 HOH *31(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 ASP A 312 5 3
HELIX 11 11 HIS A 313 GLY A 334 1 22
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 MET A 462 THR A 477 1 16
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 LYS A 608 1 13
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 SER A 105 N GLU A 62
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 SER A 26 O THR A 35
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 LEU A 258 N TRP A 221
SHEET 4 D 5 LEU A 275 VAL A 278 1 O THR A 276 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 702 1555 1545 2.56
LINK OD2 ASP A 47 YB YB A 702 1555 1545 2.53
LINK OD2 ASP A 175 YB YB A 703 1555 1555 2.68
LINK NE2 HIS A 295 ZN ZN A 701 1555 1555 2.11
LINK NE2 HIS A 299 ZN ZN A 701 1555 1555 2.16
LINK OE1 GLU A 318 ZN ZN A 701 1555 1555 2.15
LINK OE2 GLU A 318 ZN ZN A 701 1555 1555 2.57
LINK OD1 ASP A 481 YB YB A 702 1555 1555 2.55
LINK OD2 ASP A 481 YB YB A 702 1555 1555 2.54
LINK ZN ZN A 701 N ARG B 702 1555 1555 2.29
LINK ZN ZN A 701 O ARG B 702 1555 1555 2.54
LINK YB YB A 702 O HOH A 709 1555 1555 2.83
CISPEP 1 GLN A 136 ALA A 137 0 1.10
CISPEP 2 ALA A 510 PRO A 511 0 0.49
SITE 1 AC1 4 HIS A 295 HIS A 299 GLU A 318 ARG B 702
SITE 1 AC2 3 ASP A 47 ASP A 481 HOH A 709
SITE 1 AC3 4 GLY A 344 ASN A 351 GLU A 501 GLN A 508
CRYST1 78.490 87.785 99.916 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 0.012740 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011391 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010008 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
