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HEADER HYDROLASE 18-SEP-09 3JWE
TITLE CRYSTAL STRUCTURE OF HUMAN MONO-GLYCERIDE LIPASE IN COMPLEX
TITLE 2 WITH SAR629
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: 562
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 3JWE 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. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.2
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 63.63
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) (%) : 87.2
REMARK 3 NUMBER OF REFLECTIONS : 18830
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) : 0.196
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 968
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 (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.86
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3155
REMARK 3 BIN R VALUE (WORKING SET) : 0.2141
REMARK 3 BIN FREE R VALUE : 0.2478
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.48
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 183
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 : 4263
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 52.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.41300
REMARK 3 B22 (A**2) : -12.32520
REMARK 3 B33 (A**2) : 17.73830
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) : 0.34
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) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.06
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 3JWE COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-09.
REMARK 100 THE RCSB ID CODE IS RCSB055243.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9330
REMARK 200 MONOCHROMATOR : DIAMONDS 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18831
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 63.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 87.2
REMARK 200 DATA REDUNDANCY : 3.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10400
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35600
REMARK 200 FOR SHELL : 2.700
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: 3JW8
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74
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 43.91050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 69.25300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.69050
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.91050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 69.25300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.69050
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.91050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 69.25300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.69050
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.91050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 69.25300
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.69050
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: 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 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 ASN A 162
REMARK 465 PRO A 163
REMARK 465 GLU A 164
REMARK 465 SER A 165
REMARK 465 ALA A 166
REMARK 465 THR A 167
REMARK 465 THR A 168
REMARK 465 PHE A 169
REMARK 465 LYS A 170
REMARK 465 VAL A 171
REMARK 465 LEU A 172
REMARK 465 ALA A 173
REMARK 465 ALA A 174
REMARK 465 LYS A 175
REMARK 465 VAL A 176
REMARK 465 LEU A 177
REMARK 465 ASN A 178
REMARK 465 LEU A 179
REMARK 465 VAL A 180
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER A 132 N24 F4P A 314 2.16
REMARK 500 OG SER B 132 N24 F4P B 314 2.17
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 PRO A 21 -7.62 -57.69
REMARK 500 SER A 132 -122.85 61.75
REMARK 500 SER A 156 72.03 38.48
REMARK 500 TYR A 278 -152.28 -89.68
REMARK 500 SER B 132 -122.98 61.48
REMARK 500 SER B 156 72.16 38.53
REMARK 500 TYR B 278 -151.59 -90.02
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 VAL B 153 24.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 F4P 315 B IS AN UNCLEAVED FORM OF THE MOLECULE. F4P 314 A AND B
REMARK 600 IS THE RESULT OF THE CATALYTIC REACTION OCCURING IN THE CRYSTAL.
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 F4P A 314
REMARK 610 F4P B 314
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F4P A 314
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F4P B 314
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F4P B 315
DBREF 3JWE A 1 313 UNP Q6IBG9 Q6IBG9_HUMAN 1 313
DBREF 3JWE B 1 313 UNP Q6IBG9 Q6IBG9_HUMAN 1 313
SEQADV 3JWE MET A -6 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS A -5 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS A -4 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS A -3 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS A -2 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS A -1 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS A 0 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE MET B -6 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS B -5 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS B -4 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS B -3 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS B -2 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS B -1 UNP Q6IBG9 EXPRESSION TAG
SEQADV 3JWE HIS B 0 UNP Q6IBG9 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 F4P A 314 23
HET F4P B 314 23
HET F4P B 315 28
HETNAM F4P 1-[BIS(4-FLUOROPHENYL)METHYL]-4-(1H-1,2,4-TRIAZOL-1-
HETNAM 2 F4P YLCARBONYL)PIPERAZINE
FORMUL 3 F4P 3(C20 H19 F2 N5 O)
FORMUL 6 HOH *71(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 MET A 133 ARG A 145 1 13
HELIX 6 6 ASP A 190 LEU A 194 5 5
HELIX 7 7 ASN A 197 ASP A 207 1 11
HELIX 8 8 LYS A 216 LEU A 234 1 19
HELIX 9 9 PRO A 235 LEU A 237 5 3
HELIX 10 10 SER A 254 ALA A 264 1 11
HELIX 11 11 VAL A 280 GLU A 284 5 5
HELIX 12 12 LEU A 285 ARG A 303 1 19
HELIX 13 13 HIS B 64 ARG B 67 5 4
HELIX 14 14 TYR B 68 LEU B 78 1 11
HELIX 15 15 PHE B 103 TYR B 121 1 19
HELIX 16 16 MET B 133 ARG B 145 1 13
HELIX 17 17 ASN B 162 ALA B 166 5 5
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 SER B 254 ALA B 264 1 11
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 ALA A 53 O LEU A 81
SHEET 5 A16 VAL A 126 SER A 132 1 O LEU A 129 N SER A 58
SHEET 6 A16 GLY A 151 PRO A 157 1 O VAL A 153 N LEU A 128
SHEET 7 A16 PHE A 241 GLY A 246 1 O LEU A 244 N SER A 156
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 PRO B 157 1 N LEU B 154 O LEU B 242
SHEET 12 A16 VAL B 126 SER B 132 1 N LEU B 128 O VAL B 153
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 OG SER A 132 C1 F4P A 314 1555 1555 1.28
LINK OG SER B 132 C1 F4P B 314 1555 1555 1.30
SITE 1 AC1 12 ALA A 61 SER A 132 MET A 133 LEU A 158
SITE 2 AC1 12 LEU A 160 ALA A 161 LEU A 186 LEU A 224
SITE 3 AC1 12 VAL A 227 LEU A 251 CYS A 252 HIS A 279
SITE 1 AC2 15 ALA B 61 SER B 132 MET B 133 LEU B 158
SITE 2 AC2 15 LEU B 160 ALA B 161 LEU B 186 ILE B 189
SITE 3 AC2 15 LEU B 224 VAL B 227 LEU B 251 CYS B 252
SITE 4 AC2 15 HIS B 279 F4P B 315 HOH B 324
SITE 1 AC3 13 ALA B 161 ASN B 162 SER B 165 LYS B 170
SITE 2 AC3 13 VAL B 171 ALA B 174 LEU B 186 LEU B 215
SITE 3 AC3 13 VAL B 217 GLY B 220 ILE B 221 LEU B 224
SITE 4 AC3 13 F4P B 314
CRYST1 87.821 138.506 127.381 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 0.011387 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007220 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007850 0.00000
TER 2112 ALA A 305
TER 4265 ALA B 305
MASTER 396 0 3 25 16 0 11 6 4408 2 76 50
END |