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HEADER HYDROLASE 22-MAY-09 3HJU
TITLE CRYSTAL STRUCTURE OF HUMAN MONOGLYCERIDE LIPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MONOACYLGLYCEROL LIPASE, MAGL, MGL,
COMPND 5 LYSOPHOSPHOLIPASE HOMOLOG, LYSOPHOSPHOLIPASE-LIKE, HU-K5;
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;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PASK43
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE, SERINE ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.LABAR,C.BAUVOIS,F.BOREL,J.-L.FERRER,J.WOUTERS,D.M.LAMBERT
REVDAT 1 08-DEC-09 3HJU 0
JRNL AUTH G.LABAR,C.BAUVOIS,F.BOREL,J.-L.FERRER,J.WOUTERS,
JRNL AUTH 2 D.M.LAMBERT
JRNL TITL CRYSTAL STRUCTURE OF THE HUMAN MONOACYLGLYCEROL
JRNL TITL 2 LIPASE, A KEY ACTOR IN ENDOCANNABINOID SIGNALING
JRNL REF CHEMBIOCHEM 2009
JRNL REFN ESSN 1439-7633
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0066
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 35779
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) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.192
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1896
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) : 2.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2558
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.50
REMARK 3 BIN R VALUE (WORKING SET) : 0.2270
REMARK 3 BIN FREE R VALUE SET COUNT : 142
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4516
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 12
REMARK 3 SOLVENT ATOMS : 177
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.20
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.87000
REMARK 3 B22 (A**2) : -1.35000
REMARK 3 B33 (A**2) : 0.48000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.228
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.187
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.946
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4622 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6277 ; 1.839 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 580 ; 6.066 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 192 ;28.037 ;23.438
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 776 ;15.030 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;13.805 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 718 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3462 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2900 ; 1.065 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4677 ; 1.930 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1722 ; 3.179 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1600 ; 4.774 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3HJU COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB053221.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4-6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976180
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37674
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200
REMARK 200 RESOLUTION RANGE LOW (A) : 43.020
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11900
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 86.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40000
REMARK 200 FOR SHELL : 3.860
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: A PARTIAL/INCOMPLETE MODEL OF PDB ENTRIES
REMARK 200 OBTAINED BY OTHER METHODS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% V/V MPD, 70MM SODIUM
REMARK 280 CACODYLATE, PH 4-6, UNDER OIL, 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 42.93000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 63.61500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.57000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 42.93000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 63.61500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.57000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 42.93000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 63.61500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.57000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 42.93000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 63.61500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.57000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 395 LIES ON A SPECIAL POSITION.
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 -17
REMARK 465 ARG A -16
REMARK 465 GLY A -15
REMARK 465 SER A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 GLY A -7
REMARK 465 ALA A -6
REMARK 465 GLY A -5
REMARK 465 ASP A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 PRO A -1
REMARK 465 GLU A 0
REMARK 465 PHE A 1
REMARK 465 PRO A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 GLY A 298
REMARK 465 THR A 299
REMARK 465 ALA A 300
REMARK 465 SER A 301
REMARK 465 PRO A 302
REMARK 465 PRO A 303
REMARK 465 LEU A 304
REMARK 465 GLU A 305
REMARK 465 VAL A 306
REMARK 465 ASP A 307
REMARK 465 LEU A 308
REMARK 465 GLN A 309
REMARK 465 GLY A 310
REMARK 465 ASP A 311
REMARK 465 HIS A 312
REMARK 465 GLY A 313
REMARK 465 LEU A 314
REMARK 465 SER A 315
REMARK 465 ALA A 316
REMARK 465 TRP A 317
REMARK 465 SER A 318
REMARK 465 HIS A 319
REMARK 465 PRO A 320
REMARK 465 GLN A 321
REMARK 465 PHE A 322
REMARK 465 GLU A 323
REMARK 465 LYS A 324
REMARK 465 MET B -17
REMARK 465 ARG B -16
REMARK 465 GLY B -15
REMARK 465 SER B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 GLY B -7
REMARK 465 ALA B -6
REMARK 465 GLY B -5
REMARK 465 ASP B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 PRO B -1
REMARK 465 GLU B 0
REMARK 465 PHE B 1
REMARK 465 PRO B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 SER B 5
REMARK 465 ALA B 297
REMARK 465 GLY B 298
REMARK 465 THR B 299
REMARK 465 ALA B 300
REMARK 465 SER B 301
REMARK 465 PRO B 302
REMARK 465 PRO B 303
REMARK 465 LEU B 304
REMARK 465 GLU B 305
REMARK 465 VAL B 306
REMARK 465 ASP B 307
REMARK 465 LEU B 308
REMARK 465 GLN B 309
REMARK 465 GLY B 310
REMARK 465 ASP B 311
REMARK 465 HIS B 312
REMARK 465 GLY B 313
REMARK 465 LEU B 314
REMARK 465 SER B 315
REMARK 465 ALA B 316
REMARK 465 TRP B 317
REMARK 465 SER B 318
REMARK 465 HIS B 319
REMARK 465 PRO B 320
REMARK 465 GLN B 321
REMARK 465 PHE B 322
REMARK 465 GLU B 323
REMARK 465 LYS B 324
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER B 6 OG
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 OD1 ASN B 168 O PRO B 172 1.46
REMARK 500 OE1 GLU A 60 O HOH A 390 1.56
REMARK 500 OD1 ASN B 168 C PRO B 172 1.85
REMARK 500 O THR B 158 CG1 VAL B 161 1.87
REMARK 500 O LEU B 167 N LEU B 171 1.94
REMARK 500 OD1 ASN B 168 CA PRO B 172 1.96
REMARK 500 CA LEU B 167 CG1 VAL B 170 2.13
REMARK 500 OH TYR A 16 O HOH A 386 2.14
REMARK 500 O LEU B 167 CG1 VAL B 170 2.15
REMARK 500 OE1 GLN B 292 O HOH B 337 2.15
REMARK 500 CG PRO A 15 OD2 ASP A 18 2.18
REMARK 500 O ALA B 164 N ASN B 168 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NZ LYS B 160 O VAL B 166 2545 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 274 CD GLU A 274 OE2 -0.077
REMARK 500
REMARK 500 REMARK: NULL
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 A 87 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP A 99 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP A 243 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 87 NE - CZ - NH1 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PRO B 153 C - N - CD ANGL. DEV. = -18.3 DEGREES
REMARK 500 PRO B 172 CA - N - CD ANGL. DEV. = -12.6 DEGREES
REMARK 500 PRO B 172 C - N - CD ANGL. DEV. = -15.9 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 ARG A 8 169.48 81.19
REMARK 500 SER A 13 -3.05 92.28
REMARK 500 GLU A 53 -154.53 -109.60
REMARK 500 SER A 122 -118.30 60.44
REMARK 500 LEU A 176 7.11 -68.57
REMARK 500 TYR A 268 -146.77 -90.79
REMARK 500 GLU A 274 -164.16 -102.32
REMARK 500 GLU B 53 -149.66 -102.81
REMARK 500 SER B 122 -122.30 60.48
REMARK 500 SER B 146 60.27 38.00
REMARK 500 PRO B 153 53.11 13.05
REMARK 500 SER B 155 164.91 -46.36
REMARK 500 TYR B 268 -149.63 -83.29
REMARK 500 GLU B 274 -160.66 -102.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 154 SER A 155 -143.86
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 B 382 DISTANCE = 6.40 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 417
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 410
DBREF 3HJU A 2 303 UNP Q99685 MGLL_HUMAN 2 303
DBREF 3HJU B 2 303 UNP Q99685 MGLL_HUMAN 2 303
SEQADV 3HJU MET A -17 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ARG A -16 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY A -15 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU SER A -14 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A -13 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A -12 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A -11 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A -10 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A -9 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A -8 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY A -7 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ALA A -6 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY A -5 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ASP A -4 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ARG A -3 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY A -2 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PRO A -1 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLU A 0 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PHE A 1 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LEU A 304 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLU A 305 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU VAL A 306 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ASP A 307 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LEU A 308 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLN A 309 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY A 310 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ASP A 311 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A 312 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY A 313 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LEU A 314 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU SER A 315 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ALA A 316 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU TRP A 317 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU SER A 318 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS A 319 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PRO A 320 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLN A 321 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PHE A 322 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLU A 323 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LYS A 324 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU MET B -17 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ARG B -16 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY B -15 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU SER B -14 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B -13 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B -12 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B -11 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B -10 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B -9 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B -8 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY B -7 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ALA B -6 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY B -5 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ASP B -4 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ARG B -3 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY B -2 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PRO B -1 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLU B 0 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PHE B 1 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LEU B 304 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLU B 305 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU VAL B 306 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ASP B 307 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LEU B 308 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLN B 309 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY B 310 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ASP B 311 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B 312 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLY B 313 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LEU B 314 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU SER B 315 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU ALA B 316 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU TRP B 317 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU SER B 318 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU HIS B 319 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PRO B 320 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLN B 321 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU PHE B 322 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU GLU B 323 UNP Q99685 EXPRESSION TAG
SEQADV 3HJU LYS B 324 UNP Q99685 EXPRESSION TAG
SEQRES 1 A 342 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY ALA GLY
SEQRES 2 A 342 ASP ARG GLY PRO GLU PHE PRO GLU GLU SER SER PRO ARG
SEQRES 3 A 342 ARG THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS
SEQRES 4 A 342 LEU VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR
SEQRES 5 A 342 TRP LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL
SEQRES 6 A 342 SER HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU
SEQRES 7 A 342 LEU ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE
SEQRES 8 A 342 ALA HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU
SEQRES 9 A 342 ARG MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP
SEQRES 10 A 342 VAL LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO
SEQRES 11 A 342 GLY LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY
SEQRES 12 A 342 ALA ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS
SEQRES 13 A 342 PHE ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA
SEQRES 14 A 342 ASN PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA
SEQRES 15 A 342 LYS VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY
SEQRES 16 A 342 PRO ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU
SEQRES 17 A 342 VAL ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA
SEQRES 18 A 342 GLY LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA
SEQRES 19 A 342 VAL SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL
SEQRES 20 A 342 PRO PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS
SEQRES 21 A 342 ASP SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS
SEQRES 22 A 342 SER GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR
SEQRES 23 A 342 HIS VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER
SEQRES 24 A 342 VAL PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR
SEQRES 25 A 342 ALA THR ALA GLY THR ALA SER PRO PRO LEU GLU VAL ASP
SEQRES 26 A 342 LEU GLN GLY ASP HIS GLY LEU SER ALA TRP SER HIS PRO
SEQRES 27 A 342 GLN PHE GLU LYS
SEQRES 1 B 342 MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY ALA GLY
SEQRES 2 B 342 ASP ARG GLY PRO GLU PHE PRO GLU GLU SER SER PRO ARG
SEQRES 3 B 342 ARG THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS
SEQRES 4 B 342 LEU VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR
SEQRES 5 B 342 TRP LYS PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL
SEQRES 6 B 342 SER HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU
SEQRES 7 B 342 LEU ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE
SEQRES 8 B 342 ALA HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU
SEQRES 9 B 342 ARG MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP
SEQRES 10 B 342 VAL LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO
SEQRES 11 B 342 GLY LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY
SEQRES 12 B 342 ALA ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS
SEQRES 13 B 342 PHE ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA
SEQRES 14 B 342 ASN PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA
SEQRES 15 B 342 LYS VAL LEU ASN LEU VAL LEU PRO ASN LEU SER LEU GLY
SEQRES 16 B 342 PRO ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU
SEQRES 17 B 342 VAL ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA
SEQRES 18 B 342 GLY LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA
SEQRES 19 B 342 VAL SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL
SEQRES 20 B 342 PRO PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS
SEQRES 21 B 342 ASP SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS
SEQRES 22 B 342 SER GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR
SEQRES 23 B 342 HIS VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER
SEQRES 24 B 342 VAL PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR
SEQRES 25 B 342 ALA THR ALA GLY THR ALA SER PRO PRO LEU GLU VAL ASP
SEQRES 26 B 342 LEU GLN GLY ASP HIS GLY LEU SER ALA TRP SER HIS PRO
SEQRES 27 B 342 GLN PHE GLU LYS
HET GOL A 417 6
HET GOL B 410 6
HETNAM GOL GLYCEROL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *177(H2 O)
HELIX 1 1 HIS A 54 ARG A 57 5 4
HELIX 2 2 TYR A 58 GLY A 67 1 10
HELIX 3 3 PHE A 93 TYR A 111 1 19
HELIX 4 4 SER A 122 ARG A 135 1 14
HELIX 5 5 THR A 157 LEU A 171 1 15
HELIX 6 6 ASP A 180 LEU A 184 5 5
HELIX 7 7 ASN A 187 SER A 196 1 10
HELIX 8 8 LYS A 206 LEU A 224 1 19
HELIX 9 9 PRO A 225 LEU A 227 5 3
HELIX 10 10 ASP A 243 ALA A 254 1 12
HELIX 11 11 VAL A 270 GLU A 274 5 5
HELIX 12 12 LEU A 275 THR A 296 1 22
HELIX 13 13 PRO B 15 LEU B 19 5 5
HELIX 14 14 HIS B 54 ARG B 57 5 4
HELIX 15 15 TYR B 58 LEU B 68 1 11
HELIX 16 16 PHE B 93 TYR B 111 1 19
HELIX 17 17 SER B 122 ARG B 135 1 14
HELIX 18 18 SER B 155 LYS B 160 1 6
HELIX 19 19 VAL B 161 VAL B 166 1 6
HELIX 20 20 ASP B 180 LEU B 184 5 5
HELIX 21 21 ASN B 187 ASP B 197 1 11
HELIX 22 22 LYS B 206 LEU B 224 1 19
HELIX 23 23 PRO B 225 LEU B 227 5 3
HELIX 24 24 ASP B 243 ALA B 254 1 12
HELIX 25 25 VAL B 270 GLU B 274 5 5
HELIX 26 26 LEU B 275 ARG B 293 1 19
SHEET 1 A16 HIS A 21 VAL A 23 0
SHEET 2 A16 TYR A 29 TRP A 35 -1 O LEU A 30 N LEU A 22
SHEET 3 A16 LEU A 70 HIS A 75 -1 O VAL A 72 N TRP A 35
SHEET 4 A16 ALA A 43 SER A 48 1 N ALA A 43 O LEU A 71
SHEET 5 A16 VAL A 116 HIS A 121 1 O PHE A 117 N LEU A 44
SHEET 6 A16 GLY A 141 ILE A 145 1 O ILE A 145 N GLY A 120
SHEET 7 A16 PHE A 231 GLY A 236 1 O LEU A 232 N LEU A 144
SHEET 8 A16 LYS A 259 TYR A 264 1 O TYR A 264 N GLN A 235
SHEET 9 A16 LYS B 259 TYR B 264 -1 O LEU B 261 N LEU A 261
SHEET 10 A16 PHE B 231 GLY B 236 1 N LEU B 233 O LYS B 262
SHEET 11 A16 GLY B 141 ILE B 145 1 N LEU B 144 O LEU B 232
SHEET 12 A16 VAL B 116 HIS B 121 1 N GLY B 120 O ILE B 145
SHEET 13 A16 ALA B 43 SER B 48 1 N SER B 48 O LEU B 119
SHEET 14 A16 LEU B 70 HIS B 75 1 O LEU B 71 N ALA B 43
SHEET 15 A16 TYR B 29 TRP B 35 -1 N TRP B 35 O VAL B 72
SHEET 16 A16 HIS B 21 VAL B 23 -1 N LEU B 22 O LEU B 30
SITE 1 AC1 6 ALA A 51 GLU A 53 ARG A 57 HIS A 121
SITE 2 AC1 6 TYR A 194 VAL A 270
SITE 1 AC2 5 GLY B 50 ALA B 51 GLU B 53 HIS B 121
SITE 2 AC2 5 VAL B 270
CRYST1 85.860 127.230 137.140 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 0.011647 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007860 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007292 0.00000
TER 2259 ALA A 297
TER 4518 THR B 296
MASTER 518 0 2 26 16 0 4 6 4705 2 12 54
END |