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HEADER HYDROLASE 30-JUL-14 4UUQ
TITLE CRYSTAL STRUCTURE OF HUMAN MONO-GLYCERIDE LIPASE IN COMPLEX
TITLE 2 WITH SAR127303
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MGL, HU-K5, LYSOPHOSPHOLIPASE HOMOLOG,
COMPND 5 LYSOPHOSPHOLIPASE-LIKE, MONOACYLGLYCEROL LIPASE, MAGL, MGLL;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.GRIEBEL,P.PICHAT,S.BEESKE,T.LEROY,N.REDON,D.FRANCON,L.BERT,L.EVEN,
AUTHOR 2 M.LOPEZ-GRANCHA,T.TOLSTYKH,F.SUN,Q.YU,S.BRITTAIN,H.ARLT,T.HE,
AUTHOR 3 B.ZHANG,D.WIEDERSCHAIN,T.BERTRAND,J.HOUTMAN,A.RAK,F.VALLEE,N.MICHOT,
AUTHOR 4 F.AUGE,V.MENET,O.E.BERGIS,P.GEORGE,P.AVENET,V.MIKOL,M.DIDIER,
AUTHOR 5 J.ESCOUBET
REVDAT 1 21-JAN-15 4UUQ 0
JRNL AUTH G.GRIEBEL,P.PICHAT,S.BEESKE,T.LEROY,N.REDON,A.JACQUET,
JRNL AUTH 2 D.FRANCON,L.BERT,L.EVEN,M.LOPEZ-GRANCHA,T.TOLSTYKH,F.SUN,
JRNL AUTH 3 Q.YU,S.BRITTAIN,H.ARLT,T.HE,B.ZHANG,D.WIEDERSCHAIN,
JRNL AUTH 4 T.BERTRAND,J.HOUTMANN,A.RAK,F.VALLEE,N.MICHOT,F.AUGE,
JRNL AUTH 5 V.MENET,O.E.BERGIS,P.GEORGE,P.AVENET,V.MIKOL,M.DIDIER,
JRNL AUTH 6 J.ESCOUBET
JRNL TITL SELECTIVE BLOCKADE OF THE HYDROLYSIS OF THE ENDOCANNABINOID
JRNL TITL 2 2-ARACHIDONOYLGLYCEROL IMPAIRS LEARNING AND MEMORY
JRNL TITL 3 PERFORMANCE WHILE PRODUCING ANTINOCICEPTIVE ACTIVITY IN
JRNL TITL 4 RODENTS.
JRNL REF SCI.REP. V. 5 7642 2015
JRNL REFN ISSN 2045-2322
JRNL PMID 25560837
JRNL DOI 10.1038/SREP07642
REMARK 2
REMARK 2 RESOLUTION. 2.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.5.1
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 73.32
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.14
REMARK 3 NUMBER OF REFLECTIONS : 29604
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) : 0.2150
REMARK 3 R VALUE (WORKING SET) : 0.2099
REMARK 3 FREE R VALUE : 0.2591
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.09
REMARK 3 FREE R VALUE TEST SET COUNT : 2986
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 : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.50
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.14
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4790
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2228
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4326
REMARK 3 BIN R VALUE (WORKING SET) : 0.2185
REMARK 3 BIN FREE R VALUE : 0.2628
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 9.69
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 464
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 : 40
REMARK 3 SOLVENT ATOMS : 241
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.356
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 7.53157145
REMARK 3 B22 (A**2) : 3.22051862
REMARK 3 B33 (A**2) : -10.75209006
REMARK 3 B12 (A**2) : 0.00000000
REMARK 3 B13 (A**2) : 0.00000000
REMARK 3 B23 (A**2) : 0.00000000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : NULL ; NULL ; NULL
REMARK 3 BOND ANGLES : NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : NULL ; NULL ; NULL
REMARK 3 ISOTROPIC THERMAL FACTORS : NULL ; NULL ; NULL
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : NULL ; NULL ; NULL
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : NULL ; NULL ; NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : NULL
REMARK 3 OTHER TORSION ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: COVALENT BONDING BETWEEN CLEAVED LIGAND
REMARK 3 AND SERINE 132
REMARK 4
REMARK 4 4UUQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JUL-14.
REMARK 100 THE PDBE ID CODE IS EBI-61400.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-OCT-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98140
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : TOROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (QUANTUM 4)
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20609
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.36
REMARK 200 RESOLUTION RANGE LOW (A) : 73.32
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 95.2
REMARK 200 DATA REDUNDANCY : 4.6
REMARK 200 R MERGE (I) : 0.01
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 17.70
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.7
REMARK 200 R MERGE FOR SHELL (I) : 0.45
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.60
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 3JW8
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MES BUFFER 50MM PH6.0, MPD
REMARK 280 40%(V/V) AT 4C
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 43.12500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.13000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 69.31000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.12500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.13000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.31000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.12500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.13000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.31000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.12500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.13000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.31000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 46120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.7 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 86.25000
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 86.25000
REMARK 350 BIOMT2 3 0.000000 -1.000000 0.000000 126.26000
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 126.26000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 45240 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.6 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 86.25000
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 86.25000
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 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 -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 MET 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 MET 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 MET 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 MET 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 MET 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 PRO B 188 C - N - CD ANGL. DEV. = -15.7 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 -162.18 -71.11
REMARK 500 ALA A 84 -179.87 -171.81
REMARK 500 SER A 132 -126.98 54.59
REMARK 500 ASN A 162 104.81 -52.02
REMARK 500 LEU A 181 67.74 -117.39
REMARK 500 LEU A 186 -158.97 -114.28
REMARK 500 ILE A 189 117.72 58.27
REMARK 500 ALA A 248 31.52 -97.94
REMARK 500 TYR A 278 -149.09 -96.51
REMARK 500 GLU A 284 -156.33 -100.72
REMARK 500 THR B 50 98.40 21.67
REMARK 500 TYR B 121 59.02 -145.74
REMARK 500 SER B 132 -126.14 58.42
REMARK 500 ARG B 145 69.87 -153.06
REMARK 500 GLU B 164 56.53 -108.89
REMARK 500 TYR B 278 -148.43 -86.61
REMARK 500 GLU B 284 -152.63 -96.03
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 A2057 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH A2069 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A2134 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH B2019 DISTANCE = 6.79 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LIGAND
REMARK 800 64D A1306 BOUND TO SER A 132
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR LIGAND
REMARK 800 64D B1306 BOUND TO SER B 132
DBREF 4UUQ A 11 313 UNP Q99685 MGLL_HUMAN 1 303
DBREF 4UUQ B 11 313 UNP Q99685 MGLL_HUMAN 1 303
SEQADV 4UUQ MET A -6 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS A -5 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS A -4 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS A -3 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS A -2 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS A -1 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS A 0 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ MET A 1 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ GLU A 2 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ THR A 3 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ GLY A 4 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ PRO A 5 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ GLU A 6 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ ASP A 7 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ PRO A 8 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ SER A 9 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ SER A 10 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ MET B -6 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS B -5 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS B -4 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS B -3 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS B -2 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS B -1 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ HIS B 0 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ MET B 1 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ GLU B 2 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ THR B 3 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ GLY B 4 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ PRO B 5 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ GLU B 6 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ ASP B 7 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ PRO B 8 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ SER B 9 UNP Q99685 EXPRESSION TAG
SEQADV 4UUQ SER B 10 UNP Q99685 EXPRESSION TAG
SEQRES 1 A 320 MET HIS HIS HIS HIS HIS HIS MET GLU THR GLY PRO GLU
SEQRES 2 A 320 ASP PRO SER SER MET 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 MET LEU MET 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 MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 A 320 LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO GLY
SEQRES 11 A 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MET 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 MET 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 MET 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 MET TRP VAL SER GLN ARG THR ALA
SEQRES 25 A 320 THR ALA GLY THR ALA SER PRO PRO
SEQRES 1 B 320 MET HIS HIS HIS HIS HIS HIS MET GLU THR GLY PRO GLU
SEQRES 2 B 320 ASP PRO SER SER MET 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 MET LEU MET 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 MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 B 320 LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO GLY
SEQRES 11 B 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MET 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 MET 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 MET 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 MET TRP VAL SER GLN ARG THR ALA
SEQRES 25 B 320 THR ALA GLY THR ALA SER PRO PRO
HET 64D A1306 20
HET 64D B1306 20
HETNAM 64D 4-({[(4-CHLOROPHENYL)SULFONYL]AMINO}METHYL)
HETNAM 2 64D PIPERIDINE-1-CARBOXYLIC ACID
FORMUL 3 64D 2(C13 H17 CL N2 O4 S)
FORMUL 4 HOH *241(H2 O)
HELIX 1 1 TYR A 26 LEU A 29 5 4
HELIX 2 2 HIS A 64 ARG A 67 5 4
HELIX 3 3 TYR A 68 GLY A 77 1 10
HELIX 4 4 PHE A 103 TYR A 121 1 19
HELIX 5 5 MET 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 MET B 133 GLU B 144 1 12
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 AA16 HIS A 31 VAL A 33 0
SHEET 2 AA16 TYR A 39 TRP A 45 -1 O LEU A 40 N LEU A 32
SHEET 3 AA16 LEU A 80 HIS A 85 -1 O VAL A 82 N TRP A 45
SHEET 4 AA16 ALA A 53 SER A 58 1 O ALA A 53 N LEU A 81
SHEET 5 AA16 VAL A 126 HIS A 131 1 O PHE A 127 N PHE A 56
SHEET 6 AA16 GLY A 151 ILE A 155 1 O GLY A 151 N LEU A 128
SHEET 7 AA16 PHE A 241 GLY A 246 1 O LEU A 242 N LEU A 154
SHEET 8 AA16 LYS A 269 TYR A 274 1 O THR A 270 N LEU A 243
SHEET 9 AA16 LYS B 269 TYR B 274 -1 O LYS B 269 N ILE A 273
SHEET 10 AA16 PHE B 241 GLY B 246 1 O PHE B 241 N THR B 270
SHEET 11 AA16 GLY B 151 ILE B 155 1 O MET B 152 N LEU B 242
SHEET 12 AA16 VAL B 126 HIS B 131 1 O LEU B 128 N VAL B 153
SHEET 13 AA16 ALA B 53 SER B 58 1 O LEU B 54 N PHE B 127
SHEET 14 AA16 LEU B 80 HIS B 85 1 O LEU B 81 N ILE B 55
SHEET 15 AA16 TYR B 39 TRP B 45 -1 O ARG B 43 N ALA B 84
SHEET 16 AA16 HIS B 31 VAL B 33 -1 O LEU B 32 N LEU B 40
LINK OG SER A 132 C19 64D A1306 1555 1555 1.41
LINK OG SER B 132 C19 64D B1306 1555 1555 1.61
CISPEP 1 GLY A 187 PRO A 188 0 0.45
CISPEP 2 PRO B 163 GLU B 164 0 0.35
SITE 1 AC1 11 GLY A 60 ALA A 61 SER A 132 MET A 133
SITE 2 AC1 11 LEU A 158 ASN A 162 SER A 165 GLY A 220
SITE 3 AC1 11 LEU A 223 CYS A 252 HOH A2096
SITE 1 AC2 9 GLY B 60 ALA B 61 SER B 132 MET B 133
SITE 2 AC2 9 LEU B 158 ASN B 162 LEU B 223 LEU B 224
SITE 3 AC2 9 HOH B2107
CRYST1 86.250 126.260 138.620 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 0.011594 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007920 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007214 0.00000
TER 2253 ALA A 305
TER 4406 ALA B 305
MASTER 422 0 2 25 16 0 6 6 4685 2 42 50
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