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HEADER HYDROLASE/HYDROLASE INHIBITOR 13-DEC-13 4O08
TITLE CRYSTAL STRUCTURE OF BACILLUS MEGATERIUM EPOXIDE HYDROLASE IN COMPLEX
TITLE 2 WITH AN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SOLUBLE EPOXIDE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.2.2.10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS MEGATERIUM;
SOURCE 3 ORGANISM_TAXID: 1404;
SOURCE 4 STRAIN: ECU1001;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET 28A
KEYWDS A/B HYDROLASE FOLD, EPOXIDE HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR X.D.KONG,J.H.ZHOU,J.H.XU
REVDAT 1 29-OCT-14 4O08 0
JRNL AUTH X.D.KONG,S.YUAN,L.LI,J.H.XU,J.H.XU,J.H.ZHOU
JRNL TITL ENGINEERING OF AN EPOXIDE HYDROLASE FOR EFFICIENT
JRNL TITL 2 BIORESOLUTION OF BULKY PHARMACO SUBSTRATES
JRNL REF PROC.NATL.ACAD.SCI.USA 2014
JRNL REFN ESSN 1091-6490
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_637)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.83
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 50352
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.170
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 2564
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 44.8384 - 5.1081 0.99 2905 159 0.1783 0.1868
REMARK 3 2 5.1081 - 4.0553 0.99 2786 129 0.1269 0.1534
REMARK 3 3 4.0553 - 3.5429 0.99 2689 190 0.1428 0.1713
REMARK 3 4 3.5429 - 3.2191 0.99 2722 147 0.1695 0.1974
REMARK 3 5 3.2191 - 2.9884 1.00 2715 143 0.1967 0.2596
REMARK 3 6 2.9884 - 2.8122 0.99 2724 114 0.2005 0.2348
REMARK 3 7 2.8122 - 2.6714 0.99 2686 148 0.1819 0.2264
REMARK 3 8 2.6714 - 2.5551 0.99 2672 131 0.1710 0.2434
REMARK 3 9 2.5551 - 2.4568 0.99 2668 140 0.1674 0.2076
REMARK 3 10 2.4568 - 2.3720 0.99 2637 158 0.1738 0.2345
REMARK 3 11 2.3720 - 2.2979 0.98 2660 130 0.1768 0.2382
REMARK 3 12 2.2979 - 2.2322 0.98 2628 138 0.1794 0.2186
REMARK 3 13 2.2322 - 2.1734 0.97 2567 153 0.1702 0.2248
REMARK 3 14 2.1734 - 2.1204 0.97 2575 137 0.1800 0.2481
REMARK 3 15 2.1204 - 2.0722 0.96 2572 121 0.1821 0.2242
REMARK 3 16 2.0722 - 2.0281 0.95 2561 124 0.1849 0.2430
REMARK 3 17 2.0281 - 1.9875 0.95 2546 142 0.2109 0.2574
REMARK 3 18 1.9875 - 1.9500 0.94 2475 160 0.2271 0.2915
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.36
REMARK 3 B_SOL : 43.39
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.170
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.62380
REMARK 3 B22 (A**2) : -1.62380
REMARK 3 B33 (A**2) : 3.24770
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 4992
REMARK 3 ANGLE : 1.035 6772
REMARK 3 CHIRALITY : 0.073 682
REMARK 3 PLANARITY : 0.005 893
REMARK 3 DIHEDRAL : 13.598 1840
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4O08 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JAN-14.
REMARK 100 THE RCSB ID CODE IS RCSB083877.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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) : 1.5418
REMARK 200 MONOCHROMATOR : VARIMAX-HF
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 : 51301
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 79.523
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.02
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LI2SO4, 0.1M TRIS-HCL, 2.0M (NH4)
REMARK 280 2SO4, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 58.42150
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 54.27050
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 54.27050
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 29.21075
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 54.27050
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 54.27050
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 87.63225
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 54.27050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 54.27050
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 29.21075
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 54.27050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 54.27050
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 87.63225
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 58.42150
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 300 REMARK: 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 300
REMARK 300 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 300 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 300 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 300 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 300 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 300 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 300 SOFTWARE USED: PISA
REMARK 300 APPLY THE FOLLOWING TO CHAINS: A
REMARK 300 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 300 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 300 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 300
REMARK 300 BIOMOLECULE: 2
REMARK 300 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 300 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 300 SOFTWARE USED: PISA
REMARK 300 APPLY THE FOLLOWING TO CHAINS: B
REMARK 300 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 300 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 300 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
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 MET A -33
REMARK 465 GLY A -32
REMARK 465 SER A -31
REMARK 465 SER A -30
REMARK 465 HIS A -29
REMARK 465 HIS A -28
REMARK 465 HIS A -27
REMARK 465 HIS A -26
REMARK 465 HIS A -25
REMARK 465 HIS A -24
REMARK 465 SER A -23
REMARK 465 SER A -22
REMARK 465 GLY A -21
REMARK 465 LEU A -20
REMARK 465 VAL A -19
REMARK 465 PRO A -18
REMARK 465 ARG A -17
REMARK 465 GLY A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 MET A -13
REMARK 465 ALA A -12
REMARK 465 SER A -11
REMARK 465 MET A -10
REMARK 465 THR A -9
REMARK 465 GLY A -8
REMARK 465 GLY A -7
REMARK 465 GLN A -6
REMARK 465 GLN A -5
REMARK 465 MET A -4
REMARK 465 GLY A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 MET B -33
REMARK 465 GLY B -32
REMARK 465 SER B -31
REMARK 465 SER B -30
REMARK 465 HIS B -29
REMARK 465 HIS B -28
REMARK 465 HIS B -27
REMARK 465 HIS B -26
REMARK 465 HIS B -25
REMARK 465 HIS B -24
REMARK 465 SER B -23
REMARK 465 SER B -22
REMARK 465 GLY B -21
REMARK 465 LEU B -20
REMARK 465 VAL B -19
REMARK 465 PRO B -18
REMARK 465 ARG B -17
REMARK 465 GLY B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 MET B -13
REMARK 465 ALA B -12
REMARK 465 SER B -11
REMARK 465 MET B -10
REMARK 465 THR B -9
REMARK 465 GLY B -8
REMARK 465 GLY B -7
REMARK 465 GLN B -6
REMARK 465 GLN B -5
REMARK 465 MET B -4
REMARK 465 GLY B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 LYS B 3
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 PRO A 31 48.47 -104.16
REMARK 500 ASP A 32 -156.67 -94.05
REMARK 500 PHE A 33 -172.90 -172.22
REMARK 500 ASN A 59 -119.34 46.21
REMARK 500 ASP A 97 -128.18 59.06
REMARK 500 LYS A 207 75.91 -103.48
REMARK 500 ASN A 256 52.55 -103.26
REMARK 500 SER A 266 -133.83 -109.57
REMARK 500 PRO B 31 48.13 -102.13
REMARK 500 PHE B 33 -168.57 -164.61
REMARK 500 ASN B 59 -125.11 50.05
REMARK 500 ASP B 97 -130.35 59.70
REMARK 500 LYS B 207 76.03 -115.41
REMARK 500 ILE B 208 14.85 -141.28
REMARK 500 ASN B 256 48.69 -103.47
REMARK 500 SER B 266 -134.65 -113.09
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 PO6 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO6 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO6 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO6 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO6 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4NZZ RELATED DB: PDB
DBREF 4O08 A 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
DBREF 4O08 B 1 287 UNP G9BEX6 G9BEX6_BACME 1 287
SEQADV 4O08 MET A -33 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY A -32 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER A -31 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER A -30 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS A -29 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS A -28 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS A -27 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS A -26 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS A -25 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS A -24 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER A -23 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER A -22 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY A -21 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 LEU A -20 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 VAL A -19 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 PRO A -18 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 ARG A -17 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY A -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER A -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS A -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 MET A -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 ALA A -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER A -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 MET A -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 THR A -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY A -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY A -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLN A -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLN A -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 MET A -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY A -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 ARG A -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY A -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER A 0 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 MET B -33 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY B -32 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER B -31 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER B -30 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS B -29 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS B -28 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS B -27 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS B -26 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS B -25 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS B -24 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER B -23 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER B -22 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY B -21 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 LEU B -20 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 VAL B -19 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 PRO B -18 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 ARG B -17 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY B -16 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER B -15 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 HIS B -14 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 MET B -13 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 ALA B -12 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER B -11 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 MET B -10 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 THR B -9 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY B -8 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY B -7 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLN B -6 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLN B -5 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 MET B -4 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY B -3 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 ARG B -2 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 GLY B -1 UNP G9BEX6 EXPRESSION TAG
SEQADV 4O08 SER B 0 UNP G9BEX6 EXPRESSION TAG
SEQRES 1 A 321 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 321 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 321 GLY GLN GLN MET GLY ARG GLY SER MET SER LYS GLN TYR
SEQRES 4 A 321 ILE ASN VAL ASN GLY VAL ASN LEU HIS TYR ILE SER LYS
SEQRES 5 A 321 GLY GLN GLY GLU LEU MET LEU PHE LEU HIS GLY PHE PRO
SEQRES 6 A 321 ASP PHE SER HIS ILE TRP ARG HIS GLN ILE ASP GLU PHE
SEQRES 7 A 321 SER ASN ASP PHE HIS THR VAL ALA LEU ASP LEU ARG GLY
SEQRES 8 A 321 TYR ASN LEU SER GLU LYS PRO SER GLY LEU GLU SER TYR
SEQRES 9 A 321 GLU ILE ASP VAL LEU VAL GLU ASP ILE ARG GLN VAL ILE
SEQRES 10 A 321 GLU GLY LEU GLY TYR SER SER CYS THR LEU VAL VAL HIS
SEQRES 11 A 321 ASP TRP GLY ALA GLY ILE GLY TRP THR PHE ALA TYR ARG
SEQRES 12 A 321 TYR PRO GLU TYR VAL GLN LYS LEU ILE ALA PHE ASN GLY
SEQRES 13 A 321 PRO HIS PRO TYR THR PHE MET ARG GLU LEU ARG THR ASN
SEQRES 14 A 321 LYS ASN GLN GLN LYS ALA SER GLU TYR MET LYS TRP PHE
SEQRES 15 A 321 GLN LYS GLN GLU VAL GLN ASP TYR MET GLU ARG ASP ASN
SEQRES 16 A 321 PHE SER GLY LEU ARG LYS LEU VAL ILE ASP PRO GLY VAL
SEQRES 17 A 321 LYS LYS GLY TYR LEU THR ALA ASP ASP VAL GLN ALA TYR
SEQRES 18 A 321 MET ASN SER TRP GLU ASN GLY SER VAL LEU SER MET LEU
SEQRES 19 A 321 SER TYR TYR ARG ASN LEU LYS ILE PHE THR GLU GLU ASP
SEQRES 20 A 321 LEU ARG ARG LYS SER LEU PHE PRO LEU GLU GLU GLU VAL
SEQRES 21 A 321 LEU ASN ILE PRO VAL GLN ILE ILE TRP GLY ASN GLN ASP
SEQRES 22 A 321 PRO THR PHE MET PRO GLU ASN LEU ASP GLY ILE GLU GLU
SEQRES 23 A 321 TYR VAL PRO ASN ILE SER VAL HIS ARG LEU ALA GLU ALA
SEQRES 24 A 321 SER HIS ALA PRO GLN HIS GLU LYS PRO GLN GLU VAL ASN
SEQRES 25 A 321 ASN VAL MET TRP ASN PHE LEU ASN LYS
SEQRES 1 B 321 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 321 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 B 321 GLY GLN GLN MET GLY ARG GLY SER MET SER LYS GLN TYR
SEQRES 4 B 321 ILE ASN VAL ASN GLY VAL ASN LEU HIS TYR ILE SER LYS
SEQRES 5 B 321 GLY GLN GLY GLU LEU MET LEU PHE LEU HIS GLY PHE PRO
SEQRES 6 B 321 ASP PHE SER HIS ILE TRP ARG HIS GLN ILE ASP GLU PHE
SEQRES 7 B 321 SER ASN ASP PHE HIS THR VAL ALA LEU ASP LEU ARG GLY
SEQRES 8 B 321 TYR ASN LEU SER GLU LYS PRO SER GLY LEU GLU SER TYR
SEQRES 9 B 321 GLU ILE ASP VAL LEU VAL GLU ASP ILE ARG GLN VAL ILE
SEQRES 10 B 321 GLU GLY LEU GLY TYR SER SER CYS THR LEU VAL VAL HIS
SEQRES 11 B 321 ASP TRP GLY ALA GLY ILE GLY TRP THR PHE ALA TYR ARG
SEQRES 12 B 321 TYR PRO GLU TYR VAL GLN LYS LEU ILE ALA PHE ASN GLY
SEQRES 13 B 321 PRO HIS PRO TYR THR PHE MET ARG GLU LEU ARG THR ASN
SEQRES 14 B 321 LYS ASN GLN GLN LYS ALA SER GLU TYR MET LYS TRP PHE
SEQRES 15 B 321 GLN LYS GLN GLU VAL GLN ASP TYR MET GLU ARG ASP ASN
SEQRES 16 B 321 PHE SER GLY LEU ARG LYS LEU VAL ILE ASP PRO GLY VAL
SEQRES 17 B 321 LYS LYS GLY TYR LEU THR ALA ASP ASP VAL GLN ALA TYR
SEQRES 18 B 321 MET ASN SER TRP GLU ASN GLY SER VAL LEU SER MET LEU
SEQRES 19 B 321 SER TYR TYR ARG ASN LEU LYS ILE PHE THR GLU GLU ASP
SEQRES 20 B 321 LEU ARG ARG LYS SER LEU PHE PRO LEU GLU GLU GLU VAL
SEQRES 21 B 321 LEU ASN ILE PRO VAL GLN ILE ILE TRP GLY ASN GLN ASP
SEQRES 22 B 321 PRO THR PHE MET PRO GLU ASN LEU ASP GLY ILE GLU GLU
SEQRES 23 B 321 TYR VAL PRO ASN ILE SER VAL HIS ARG LEU ALA GLU ALA
SEQRES 24 B 321 SER HIS ALA PRO GLN HIS GLU LYS PRO GLN GLU VAL ASN
SEQRES 25 B 321 ASN VAL MET TRP ASN PHE LEU ASN LYS
HET PO6 A 301 11
HET PO6 A 302 11
HET PO6 A 303 11
HET SO4 A 304 5
HET SO4 A 305 5
HET PO6 B 301 11
HET PO6 B 302 11
HET SO4 B 303 5
HETNAM PO6 2-PHENOXYACETAMIDE
HETNAM SO4 SULFATE ION
FORMUL 3 PO6 5(C8 H9 N O2)
FORMUL 6 SO4 3(O4 S 2-)
FORMUL 11 HOH *485(H2 O)
HELIX 1 1 PHE A 33 ILE A 36 5 4
HELIX 2 2 TRP A 37 SER A 45 1 9
HELIX 3 3 GLY A 66 TYR A 70 5 5
HELIX 4 4 GLU A 71 LEU A 86 1 16
HELIX 5 5 ASP A 97 TYR A 110 1 14
HELIX 6 6 HIS A 124 ASN A 135 1 12
HELIX 7 7 ASN A 135 SER A 142 1 8
HELIX 8 8 GLU A 143 PHE A 148 1 6
HELIX 9 9 GLU A 152 LYS A 176 1 25
HELIX 10 10 THR A 180 GLY A 194 1 15
HELIX 11 11 SER A 195 TYR A 202 1 8
HELIX 12 12 TYR A 203 LEU A 206 5 4
HELIX 13 13 THR A 210 ARG A 215 1 6
HELIX 14 14 MET A 243 ASP A 248 5 6
HELIX 15 15 GLY A 249 TYR A 253 5 5
HELIX 16 16 ALA A 268 LYS A 273 1 6
HELIX 17 17 LYS A 273 LYS A 287 1 15
HELIX 18 18 PHE B 33 ILE B 36 5 4
HELIX 19 19 TRP B 37 SER B 45 1 9
HELIX 20 20 GLY B 66 TYR B 70 5 5
HELIX 21 21 GLU B 71 LEU B 86 1 16
HELIX 22 22 ASP B 97 TYR B 110 1 14
HELIX 23 23 HIS B 124 ASN B 135 1 12
HELIX 24 24 ASN B 135 SER B 142 1 8
HELIX 25 25 GLU B 143 PHE B 148 1 6
HELIX 26 26 GLN B 149 GLN B 151 5 3
HELIX 27 27 GLU B 152 LYS B 176 1 25
HELIX 28 28 THR B 180 GLY B 194 1 15
HELIX 29 29 SER B 195 ARG B 204 1 10
HELIX 30 30 GLU B 212 ARG B 216 5 5
HELIX 31 31 MET B 243 ASP B 248 5 6
HELIX 32 32 GLY B 249 TYR B 253 5 5
HELIX 33 33 ALA B 268 LYS B 273 1 6
HELIX 34 34 LYS B 273 ASN B 286 1 14
SHEET 1 A 8 SER A 2 VAL A 8 0
SHEET 2 A 8 VAL A 11 LYS A 18 -1 O SER A 17 N SER A 2
SHEET 3 A 8 HIS A 49 LEU A 53 -1 O THR A 50 N LYS A 18
SHEET 4 A 8 LEU A 23 LEU A 27 1 N PHE A 26 O VAL A 51
SHEET 5 A 8 CYS A 91 VAL A 95 1 O VAL A 94 N LEU A 25
SHEET 6 A 8 VAL A 114 PHE A 120 1 O PHE A 120 N VAL A 95
SHEET 7 A 8 VAL A 231 GLY A 236 1 O GLN A 232 N ALA A 119
SHEET 8 A 8 ILE A 257 LEU A 262 1 O LEU A 262 N TRP A 235
SHEET 1 B 8 TYR B 5 VAL B 8 0
SHEET 2 B 8 VAL B 11 LYS B 18 -1 O LEU B 13 N ILE B 6
SHEET 3 B 8 HIS B 49 LEU B 53 -1 O ALA B 52 N ILE B 16
SHEET 4 B 8 LEU B 23 LEU B 27 1 N PHE B 26 O VAL B 51
SHEET 5 B 8 CYS B 91 VAL B 95 1 O VAL B 94 N LEU B 27
SHEET 6 B 8 VAL B 114 ALA B 119 1 O ILE B 118 N LEU B 93
SHEET 7 B 8 VAL B 231 GLY B 236 1 O GLN B 232 N ALA B 119
SHEET 8 B 8 ILE B 257 LEU B 262 1 O LEU B 262 N TRP B 235
CISPEP 1 PHE A 30 PRO A 31 0 -3.52
CISPEP 2 PHE B 30 PRO B 31 0 -4.88
SITE 1 AC1 9 PHE A 30 ASP A 97 TRP A 98 PRO A 123
SITE 2 AC1 9 TYR A 144 MET A 145 TYR A 203 PO6 A 303
SITE 3 AC1 9 HOH A 591
SITE 1 AC2 5 GLN A 139 SER A 142 LYS A 146 ILE A 208
SITE 2 AC2 5 LEU A 214
SITE 1 AC3 8 PHE A 30 PRO A 31 VAL A 169 TYR A 178
SITE 2 AC3 8 SER A 266 HIS A 267 PO6 A 301 HOH A 591
SITE 1 AC4 6 LYS A 273 PRO A 274 GLN A 275 GLU A 276
SITE 2 AC4 6 HOH A 514 ASN B 161
SITE 1 AC5 2 ARG A 133 THR A 134
SITE 1 AC6 9 PHE B 30 PRO B 31 LEU B 168 VAL B 169
SITE 2 AC6 9 TYR B 178 SER B 266 HIS B 267 PO6 B 302
SITE 3 AC6 9 HOH B 544
SITE 1 AC7 8 PHE B 30 ASP B 97 TRP B 98 PRO B 123
SITE 2 AC7 8 TYR B 144 MET B 145 TYR B 203 PO6 B 301
SITE 1 AC8 5 LYS B 273 PRO B 274 GLN B 275 GLU B 276
SITE 2 AC8 5 HOH B 582
CRYST1 108.541 108.541 116.843 90.00 90.00 90.00 P 41 21 2 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 0.009213 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009213 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008558 0.00000
TER 2419 LYS A 287
TER 4788 LYS B 287
MASTER 408 0 8 34 16 0 17 6 5280 2 70 50
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