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HEADER HYDROLASE 18-SEP-09 3JW8
TITLE CRYSTAL STRUCTURE OF HUMAN MONO-GLYCERIDE LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MGLL PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MONOGLYCERIDE LIPASE, ISOFORM CRA_B, CDNA,
COMPND 5 FLJ96595, HOMO SAPIENS MONOGLYCERIDE LIPASE (MGLL), MRNA;
COMPND 6 EC: 3.1.1.23;
COMPND 7 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: MGLL, HCG_40840;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS ALPHA-BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.BERTRAND,F.AUGE,J.HOUTMANN,A.RAK,F.VALLEE,V.MIKOL,
AUTHOR 2 P.F.BERNE,N.MICHOT,D.CHEURET,C.HOORNAERT,M.MATHIEU
REVDAT 1 26-JAN-10 3JW8 0
JRNL AUTH T.BERTRAND,F.AUGE,J.HOUTMANN,A.RAK,F.VALLEE,
JRNL AUTH 2 V.MIKOL,P.F.BERNE,N.MICHOT,D.CHEURET,C.HOORNAERT,
JRNL AUTH 3 M.MATHIEU
JRNL TITL STRUCTURAL BASIS FOR HUMAN MONOGLYCERIDE LIPASE
JRNL TITL 2 INHIBITION.
JRNL REF J.MOL.BIOL. 2009
JRNL REFN ESSN 1089-8638
JRNL PMID 19962385
JRNL DOI 10.1016/J.JMB.2009.11.060
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.3
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 17.21
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) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 44314
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) : 0.157
REMARK 3 FREE R VALUE : 0.189
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 2230
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.04
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3037
REMARK 3 BIN R VALUE (WORKING SET) : 0.1522
REMARK 3 BIN FREE R VALUE : 0.2088
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.39
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 173
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4404
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 532
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.56
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.24510
REMARK 3 B22 (A**2) : 0.79650
REMARK 3 B33 (A**2) : -0.55140
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) : 0.17
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.020
REMARK 3 BOND ANGLES (DEGREES) : 1.32
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
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 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 3JW8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB055237.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-08
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797, 0.9799, 1.000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44315
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 73.900
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 FOR THE DATA SET : 18.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.14900
REMARK 200 FOR SHELL : 6.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES, 40% MPD, PH 6.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+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 0.00000
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 0.00000
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 43.29400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.15550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 70.28350
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.29400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.15550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.28350
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.29400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.15550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.28350
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.29400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.15550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.28350
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -280.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7670 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 44390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -221.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 126.31100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 126.31100
REMARK 350 BIOMT3 4 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 MSE A -6
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 465 MSE A 1
REMARK 465 GLU A 2
REMARK 465 THR A 3
REMARK 465 GLY A 4
REMARK 465 PRO A 5
REMARK 465 GLU A 6
REMARK 465 ASP A 7
REMARK 465 PRO A 8
REMARK 465 SER A 9
REMARK 465 SER A 10
REMARK 465 MSE A 11
REMARK 465 PRO A 12
REMARK 465 GLU A 13
REMARK 465 GLU A 14
REMARK 465 SER A 15
REMARK 465 THR A 306
REMARK 465 ALA A 307
REMARK 465 GLY A 308
REMARK 465 THR A 309
REMARK 465 ALA A 310
REMARK 465 SER A 311
REMARK 465 PRO A 312
REMARK 465 PRO A 313
REMARK 465 MSE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MSE B 1
REMARK 465 GLU B 2
REMARK 465 THR B 3
REMARK 465 GLY B 4
REMARK 465 PRO B 5
REMARK 465 GLU B 6
REMARK 465 ASP B 7
REMARK 465 PRO B 8
REMARK 465 SER B 9
REMARK 465 SER B 10
REMARK 465 MSE B 11
REMARK 465 PRO B 12
REMARK 465 GLU B 13
REMARK 465 GLU B 14
REMARK 465 SER B 15
REMARK 465 SER B 16
REMARK 465 PRO B 17
REMARK 465 ARG B 18
REMARK 465 ARG B 19
REMARK 465 THR B 20
REMARK 465 PRO B 21
REMARK 465 GLN B 22
REMARK 465 SER B 23
REMARK 465 ILE B 24
REMARK 465 PRO B 25
REMARK 465 TYR B 26
REMARK 465 GLN B 27
REMARK 465 THR B 306
REMARK 465 ALA B 307
REMARK 465 GLY B 308
REMARK 465 THR B 309
REMARK 465 ALA B 310
REMARK 465 SER B 311
REMARK 465 PRO B 312
REMARK 465 PRO B 313
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 B 97 CD - NE - CZ ANGL. DEV. = 8.4 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 GLU A 63 -153.88 -103.94
REMARK 500 SER A 132 -129.83 62.56
REMARK 500 SER A 156 62.94 38.62
REMARK 500 VAL A 159 -33.58 -132.07
REMARK 500 TYR A 278 -152.83 -89.36
REMARK 500 GLU A 284 -164.31 -102.72
REMARK 500 GLU B 63 -154.16 -106.27
REMARK 500 SER B 132 -128.56 60.29
REMARK 500 SER B 156 65.56 29.20
REMARK 500 TYR B 278 -153.91 -88.97
REMARK 500 GLU B 284 -166.15 -100.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 LEU B 160 23.7 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 549 DISTANCE = 7.15 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 707
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 831
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 866
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD A 886
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 812
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 830
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 865
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3JWE RELATED DB: PDB
DBREF 3JW8 A 1 313 UNP Q6IBG9 Q6IBG9_HUMAN 1 313
DBREF 3JW8 B 1 313 UNP Q6IBG9 Q6IBG9_HUMAN 1 313
SEQADV 3JW8 MSE A -6 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS A -5 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS A -4 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS A -3 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS A -2 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS A -1 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS A 0 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 MSE B -6 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS B -5 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS B -4 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS B -3 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS B -2 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS B -1 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JW8 HIS B 0 UNP Q6IBG9 EXPRESSION TAG
SEQRES 1 A 320 MSE HIS HIS HIS HIS HIS HIS MSE GLU THR GLY PRO GLU
SEQRES 2 A 320 ASP PRO SER SER MSE PRO GLU GLU SER SER PRO ARG ARG
SEQRES 3 A 320 THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU
SEQRES 4 A 320 VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP
SEQRES 5 A 320 LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER
SEQRES 6 A 320 HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU
SEQRES 7 A 320 ALA ARG MSE LEU MSE GLY LEU ASP LEU LEU VAL PHE ALA
SEQRES 8 A 320 HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG
SEQRES 9 A 320 MSE VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 A 320 LEU GLN HIS VAL ASP SER MSE GLN LYS ASP TYR PRO GLY
SEQRES 11 A 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MSE GLY GLY ALA
SEQRES 12 A 320 ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE
SEQRES 13 A 320 ALA GLY MSE VAL LEU ILE SER PRO LEU VAL LEU ALA ASN
SEQRES 14 A 320 PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS
SEQRES 15 A 320 VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY PRO
SEQRES 16 A 320 ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL
SEQRES 17 A 320 ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY
SEQRES 18 A 320 LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL
SEQRES 19 A 320 SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO
SEQRES 20 A 320 PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP
SEQRES 21 A 320 SER LYS GLY ALA TYR LEU LEU MSE GLU LEU ALA LYS SER
SEQRES 22 A 320 GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS
SEQRES 23 A 320 VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL
SEQRES 24 A 320 PHE HIS GLU ILE ASN MSE TRP VAL SER GLN ARG THR ALA
SEQRES 25 A 320 THR ALA GLY THR ALA SER PRO PRO
SEQRES 1 B 320 MSE HIS HIS HIS HIS HIS HIS MSE GLU THR GLY PRO GLU
SEQRES 2 B 320 ASP PRO SER SER MSE PRO GLU GLU SER SER PRO ARG ARG
SEQRES 3 B 320 THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU
SEQRES 4 B 320 VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP
SEQRES 5 B 320 LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER
SEQRES 6 B 320 HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU
SEQRES 7 B 320 ALA ARG MSE LEU MSE GLY LEU ASP LEU LEU VAL PHE ALA
SEQRES 8 B 320 HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG
SEQRES 9 B 320 MSE VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 B 320 LEU GLN HIS VAL ASP SER MSE GLN LYS ASP TYR PRO GLY
SEQRES 11 B 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MSE GLY GLY ALA
SEQRES 12 B 320 ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE
SEQRES 13 B 320 ALA GLY MSE VAL LEU ILE SER PRO LEU VAL LEU ALA ASN
SEQRES 14 B 320 PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS
SEQRES 15 B 320 VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY PRO
SEQRES 16 B 320 ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL
SEQRES 17 B 320 ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY
SEQRES 18 B 320 LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL
SEQRES 19 B 320 SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO
SEQRES 20 B 320 PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP
SEQRES 21 B 320 SER LYS GLY ALA TYR LEU LEU MSE GLU LEU ALA LYS SER
SEQRES 22 B 320 GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS
SEQRES 23 B 320 VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL
SEQRES 24 B 320 PHE HIS GLU ILE ASN MSE TRP VAL SER GLN ARG THR ALA
SEQRES 25 B 320 THR ALA GLY THR ALA SER PRO PRO
MODRES 3JW8 MSE A 74 MET SELENOMETHIONINE
MODRES 3JW8 MSE A 76 MET SELENOMETHIONINE
MODRES 3JW8 MSE A 98 MET SELENOMETHIONINE
MODRES 3JW8 MSE A 117 MET SELENOMETHIONINE
MODRES 3JW8 MSE A 133 MET SELENOMETHIONINE
MODRES 3JW8 MSE A 152 MET SELENOMETHIONINE
MODRES 3JW8 MSE A 261 MET SELENOMETHIONINE
MODRES 3JW8 MSE A 298 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 74 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 76 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 98 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 117 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 133 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 152 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 261 MET SELENOMETHIONINE
MODRES 3JW8 MSE B 298 MET SELENOMETHIONINE
HET MSE A 74 8
HET MSE A 76 8
HET MSE A 98 8
HET MSE A 117 8
HET MSE A 133 8
HET MSE A 152 8
HET MSE A 261 8
HET MSE A 298 8
HET MSE B 74 8
HET MSE B 76 8
HET MSE B 98 8
HET MSE B 117 8
HET MSE B 133 8
HET MSE B 152 8
HET MSE B 261 8
HET MSE B 298 8
HET MPD A 707 8
HET MRD A 831 8
HET MRD A 866 8
HET MRD A 886 8
HET MPD B 812 8
HET MRD B 830 8
HET MRD B 865 8
HETNAM MSE SELENOMETHIONINE
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 1 MSE 16(C5 H11 N O2 SE)
FORMUL 3 MPD 2(C6 H14 O2)
FORMUL 4 MRD 5(C6 H14 O2)
FORMUL 10 HOH *532(H2 O)
HELIX 1 1 PRO A 25 LEU A 29 5 5
HELIX 2 2 HIS A 64 ARG A 67 5 4
HELIX 3 3 TYR A 68 LEU A 78 1 11
HELIX 4 4 PHE A 103 TYR A 121 1 19
HELIX 5 5 MSE A 133 ARG A 145 1 13
HELIX 6 6 THR A 167 LEU A 181 1 15
HELIX 7 7 ASP A 190 LEU A 194 5 5
HELIX 8 8 ASN A 197 ASP A 207 1 11
HELIX 9 9 LYS A 216 LEU A 234 1 19
HELIX 10 10 PRO A 235 LEU A 237 5 3
HELIX 11 11 ASP A 253 ALA A 264 1 12
HELIX 12 12 VAL A 280 GLU A 284 5 5
HELIX 13 13 LEU A 285 ARG A 303 1 19
HELIX 14 14 HIS B 64 ARG B 67 5 4
HELIX 15 15 TYR B 68 GLY B 77 1 10
HELIX 16 16 PHE B 103 TYR B 121 1 19
HELIX 17 17 MSE B 133 ARG B 145 1 13
HELIX 18 18 THR B 167 LEU B 181 1 15
HELIX 19 19 ASP B 190 LEU B 194 5 5
HELIX 20 20 ASN B 197 ASP B 207 1 11
HELIX 21 21 LYS B 216 LEU B 234 1 19
HELIX 22 22 PRO B 235 LEU B 237 5 3
HELIX 23 23 ASP B 253 ALA B 264 1 12
HELIX 24 24 VAL B 280 GLU B 284 5 5
HELIX 25 25 LEU B 285 ARG B 303 1 19
SHEET 1 A16 HIS A 31 VAL A 33 0
SHEET 2 A16 TYR A 39 TRP A 45 -1 O LEU A 40 N LEU A 32
SHEET 3 A16 LEU A 80 HIS A 85 -1 O VAL A 82 N TRP A 45
SHEET 4 A16 ALA A 53 SER A 58 1 N VAL A 57 O PHE A 83
SHEET 5 A16 VAL A 126 HIS A 131 1 O LEU A 129 N SER A 58
SHEET 6 A16 GLY A 151 ILE A 155 1 O ILE A 155 N GLY A 130
SHEET 7 A16 PHE A 241 GLY A 246 1 O LEU A 242 N LEU A 154
SHEET 8 A16 LYS A 269 TYR A 274 1 O THR A 270 N LEU A 243
SHEET 9 A16 LYS B 269 TYR B 274 -1 O LEU B 271 N LEU A 271
SHEET 10 A16 PHE B 241 GLY B 246 1 N LEU B 243 O THR B 270
SHEET 11 A16 GLY B 151 ILE B 155 1 N LEU B 154 O LEU B 242
SHEET 12 A16 VAL B 126 HIS B 131 1 N GLY B 130 O ILE B 155
SHEET 13 A16 ALA B 53 SER B 58 1 N SER B 58 O LEU B 129
SHEET 14 A16 LEU B 80 HIS B 85 1 O LEU B 81 N ALA B 53
SHEET 15 A16 TYR B 39 TRP B 45 -1 N TRP B 45 O VAL B 82
SHEET 16 A16 HIS B 31 VAL B 33 -1 N LEU B 32 O LEU B 40
LINK C MSE A 74 N LEU A 75 1555 1555 1.33
LINK C MSE A 76 N GLY A 77 1555 1555 1.35
LINK C MSE A 98 N VAL A 99 1555 1555 1.32
LINK C MSE A 117 N GLN A 118 1555 1555 1.33
LINK C MSE A 133 N GLY A 134 1555 1555 1.32
LINK C MSE A 152 N VAL A 153 1555 1555 1.35
LINK C MSE A 261 N GLU A 262 1555 1555 1.32
LINK C MSE A 298 N TRP A 299 1555 1555 1.35
LINK C MSE B 74 N LEU B 75 1555 1555 1.34
LINK C MSE B 76 N GLY B 77 1555 1555 1.34
LINK C MSE B 98 N VAL B 99 1555 1555 1.33
LINK C MSE B 117 N GLN B 118 1555 1555 1.36
LINK C MSE B 133 N GLY B 134 1555 1555 1.34
LINK C MSE B 152 N VAL B 153 1555 1555 1.33
LINK C MSE B 261 N GLU B 262 1555 1555 1.32
LINK C MSE B 298 N TRP B 299 1555 1555 1.35
LINK C ARG A 73 N MSE A 74 1555 1555 1.36
LINK C LEU A 75 N MSE A 76 1555 1555 1.35
LINK C ARG A 97 N MSE A 98 1555 1555 1.36
LINK C SER A 116 N MSE A 117 1555 1555 1.38
LINK C SER A 132 N MSE A 133 1555 1555 1.35
LINK C GLY A 151 N MSE A 152 1555 1555 1.33
LINK C LEU A 260 N MSE A 261 1555 1555 1.34
LINK C ASN A 297 N MSE A 298 1555 1555 1.33
LINK C ARG B 73 N MSE B 74 1555 1555 1.38
LINK C LEU B 75 N MSE B 76 1555 1555 1.32
LINK C ARG B 97 N MSE B 98 1555 1555 1.34
LINK C SER B 116 N MSE B 117 1555 1555 1.37
LINK C SER B 132 N MSE B 133 1555 1555 1.32
LINK C GLY B 151 N MSE B 152 1555 1555 1.35
LINK C LEU B 260 N MSE B 261 1555 1555 1.35
LINK C ASN B 297 N MSE B 298 1555 1555 1.34
SITE 1 AC1 8 LEU A 158 ALA A 161 ASN A 162 SER A 165
SITE 2 AC1 8 ALA A 166 GLY A 220 MRD A 831 MRD A 886
SITE 1 AC2 4 SER A 132 HOH A 445 HOH A 513 MPD A 707
SITE 1 AC3 8 ALA A 61 HIS A 131 ILE A 189 LEU A 251
SITE 2 AC3 8 HIS A 279 VAL A 280 HOH A 445 HOH A 529
SITE 1 AC4 4 SER A 165 LYS A 170 LEU A 186 MPD A 707
SITE 1 AC5 7 ALA B 161 ASN B 162 SER B 165 LEU B 215
SITE 2 AC5 7 LEU B 223 HOH B 456 MRD B 830
SITE 1 AC6 4 SER B 132 HOH B 444 HOH B 516 MPD B 812
SITE 1 AC7 12 GLY B 60 ALA B 61 GLU B 63 HIS B 131
SITE 2 AC7 12 LEU B 194 TYR B 204 LEU B 251 HIS B 279
SITE 3 AC7 12 VAL B 280 HOH B 444 HOH B 447 HOH B 516
CRYST1 86.588 126.311 140.567 90.00 90.00 90.00 I 2 2 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 0.011549 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007917 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007114 0.00000
TER 2253 ALA A 305
TER 4406 ALA B 305
MASTER 445 0 23 25 16 0 12 6 4992 2 216 50
END |