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HEADER HYDROLASE/INHIBITOR 21-DEC-20 7L50
TITLE CRYSTAL STRUCTURE OF HUMAN MONOACYLGLYCEROL LIPASE IN COMPLEX WITH
TITLE 2 COMPOUND 1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MONOGLYCERIDE LIPASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 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
KEYWDS INHIBITOR, SERINE HYDROLASE, HYDROLASE, HYDROLASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.QIN,W.LANE,R.J.SKENE
REVDAT 1 11-AUG-21 7L50 0
JRNL AUTH S.IKEDA,H.SUGIYAMA,H.TOKUHARA,M.MURAKAMI,M.NAKAMURA,Y.OGURO,
JRNL AUTH 2 J.AIDA,N.MORISHITA,S.SOGABE,D.R.DOUGAN,S.C.GAY,L.QIN,
JRNL AUTH 3 N.ARIMURA,Y.TAKAHASHI,M.SASAKI,Y.KAMADA,K.AOYAMA,K.KIMOTO,
JRNL AUTH 4 M.KAMATA
JRNL TITL DESIGN AND SYNTHESIS OF NOVEL SPIRO DERIVATIVES AS POTENT
JRNL TITL 2 AND REVERSIBLE MONOACYLGLYCEROL LIPASE (MAGL) INHIBITORS:
JRNL TITL 3 BIOISOSTERIC TRANSFORMATION FROM 3-OXO-3,4-DIHYDRO-2 H
JRNL TITL 4 -BENZO[ B ][1,4]OXAZIN-6-YL MOIETY.
JRNL REF J.MED.CHEM. 2021
JRNL REFN ISSN 0022-2623
JRNL PMID 34328319
JRNL DOI 10.1021/ACS.JMEDCHEM.1C00432
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0257
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.19
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 78322
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.895
REMARK 3 FREE R VALUE TEST SET COUNT : 3834
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5379
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.86
REMARK 3 BIN R VALUE (WORKING SET) : 0.4420
REMARK 3 BIN FREE R VALUE SET COUNT : 291
REMARK 3 BIN FREE R VALUE : 0.4060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8864
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 157
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 82.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.25700
REMARK 3 B22 (A**2) : -8.10900
REMARK 3 B33 (A**2) : 7.50100
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.69400
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.277
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.304
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 31.945
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9209 ; 0.004 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12504 ; 1.127 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1138 ; 5.960 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 436 ;30.528 ;21.743
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1506 ;15.327 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 55 ;15.903 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1150 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7046 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 4378 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 6274 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 307 ; 0.128 ; 0.200
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): 4584 ; 2.564 ; 4.322
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5706 ; 4.275 ; 6.456
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4625 ; 2.918 ; 4.346
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6782 ; 4.708 ; 6.463
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 701
REMARK 3 ORIGIN FOR THE GROUP (A): 97.6509 -33.2935 167.5382
REMARK 3 T TENSOR
REMARK 3 T11: 0.1933 T22: 0.4465
REMARK 3 T33: 0.6496 T12: 0.0067
REMARK 3 T13: 0.0649 T23: 0.0169
REMARK 3 L TENSOR
REMARK 3 L11: 0.5447 L22: 2.3501
REMARK 3 L33: 0.1320 L12: 0.0606
REMARK 3 L13: 0.1750 L23: 0.3806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0227 S12: -0.0338 S13: 0.2427
REMARK 3 S21: -0.1200 S22: -0.0688 S23: 0.0303
REMARK 3 S31: 0.0438 S32: -0.0031 S33: 0.0461
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 701
REMARK 3 ORIGIN FOR THE GROUP (A): 129.0034 -11.2513 177.2518
REMARK 3 T TENSOR
REMARK 3 T11: 0.1814 T22: 0.4245
REMARK 3 T33: 0.6677 T12: -0.0032
REMARK 3 T13: 0.0622 T23: 0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 0.5693 L22: 2.7596
REMARK 3 L33: 0.0604 L12: 0.1347
REMARK 3 L13: -0.0861 L23: 0.3114
REMARK 3 S TENSOR
REMARK 3 S11: 0.0897 S12: 0.0574 S13: -0.1842
REMARK 3 S21: 0.1766 S22: -0.0694 S23: -0.1183
REMARK 3 S31: -0.0268 S32: -0.0127 S33: -0.0204
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 701
REMARK 3 ORIGIN FOR THE GROUP (A): 112.2235 27.7195 119.7576
REMARK 3 T TENSOR
REMARK 3 T11: 0.7744 T22: 0.0385
REMARK 3 T33: 0.4616 T12: -0.0192
REMARK 3 T13: 0.4844 T23: -0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 0.7863 L22: 2.1775
REMARK 3 L33: 0.0994 L12: -0.2595
REMARK 3 L13: 0.2212 L23: -0.2797
REMARK 3 S TENSOR
REMARK 3 S11: 0.1012 S12: -0.0202 S13: 0.2342
REMARK 3 S21: 0.0490 S22: -0.1207 S23: 0.0063
REMARK 3 S31: 0.0478 S32: 0.0115 S33: 0.0195
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 701
REMARK 3 ORIGIN FOR THE GROUP (A): 112.3432 -13.7347 119.5722
REMARK 3 T TENSOR
REMARK 3 T11: 0.8088 T22: 0.0175
REMARK 3 T33: 0.4391 T12: -0.0079
REMARK 3 T13: 0.5147 T23: 0.0067
REMARK 3 L TENSOR
REMARK 3 L11: 0.8644 L22: 2.7054
REMARK 3 L33: 0.0120 L12: 0.1649
REMARK 3 L13: -0.0753 L23: 0.0611
REMARK 3 S TENSOR
REMARK 3 S11: 0.0870 S12: -0.0265 S13: -0.1880
REMARK 3 S21: 0.0934 S22: -0.0984 S23: -0.0162
REMARK 3 S31: -0.0375 S32: 0.0002 S33: 0.0114
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 7L50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-20.
REMARK 100 THE DEPOSITION ID IS D_1000253721.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 79270
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 49.060
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 4.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.72800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5ZUN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAOAC PH 5.5, 32-38% MPD, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
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 63.58400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 GLY A -9
REMARK 465 SER A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 LEU A 167
REMARK 465 ASN A 168
REMARK 465 SER A 169
REMARK 465 VAL A 170
REMARK 465 LEU A 171
REMARK 465 PRO A 172
REMARK 465 ASN A 173
REMARK 465 LEU A 174
REMARK 465 SER A 175
REMARK 465 SER A 176
REMARK 465 THR A 296
REMARK 465 ALA A 297
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 MET B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 GLY B -9
REMARK 465 SER B -8
REMARK 465 GLU B -7
REMARK 465 ASN B -6
REMARK 465 LEU B -5
REMARK 465 TYR B -4
REMARK 465 PHE B -3
REMARK 465 GLN B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 LEU B 167
REMARK 465 ASN B 168
REMARK 465 SER B 169
REMARK 465 VAL B 170
REMARK 465 LEU B 171
REMARK 465 THR B 296
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 MET C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 GLY C -9
REMARK 465 SER C -8
REMARK 465 GLU C -7
REMARK 465 ASN C -6
REMARK 465 LEU C -5
REMARK 465 TYR C -4
REMARK 465 PHE C -3
REMARK 465 GLN C -2
REMARK 465 GLY C -1
REMARK 465 SER C 0
REMARK 465 LEU C 167
REMARK 465 ASN C 168
REMARK 465 SER C 169
REMARK 465 VAL C 170
REMARK 465 LEU C 171
REMARK 465 PRO C 172
REMARK 465 ASN C 173
REMARK 465 LEU C 174
REMARK 465 SER C 175
REMARK 465 THR C 296
REMARK 465 ALA C 297
REMARK 465 GLY C 298
REMARK 465 THR C 299
REMARK 465 ALA C 300
REMARK 465 SER C 301
REMARK 465 PRO C 302
REMARK 465 PRO C 303
REMARK 465 MET D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 GLY D -9
REMARK 465 SER D -8
REMARK 465 GLU D -7
REMARK 465 ASN D -6
REMARK 465 LEU D -5
REMARK 465 TYR D -4
REMARK 465 PHE D -3
REMARK 465 GLN D -2
REMARK 465 GLY D -1
REMARK 465 SER D 0
REMARK 465 LEU D 167
REMARK 465 ASN D 168
REMARK 465 SER D 169
REMARK 465 VAL D 170
REMARK 465 LEU D 171
REMARK 465 PRO D 172
REMARK 465 ASN D 173
REMARK 465 LEU D 174
REMARK 465 SER D 175
REMARK 465 ALA D 295
REMARK 465 THR D 296
REMARK 465 ALA D 297
REMARK 465 GLY D 298
REMARK 465 THR D 299
REMARK 465 ALA D 300
REMARK 465 SER D 301
REMARK 465 PRO D 302
REMARK 465 PRO D 303
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 ARG A 202 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 154 CG CD OE1 OE2
REMARK 470 LYS B 165 CG CD CE NZ
REMARK 470 GLU C 154 CG CD OE1 OE2
REMARK 470 GLU D 154 CG CD OE1 OE2
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 7 150.33 -42.19
REMARK 500 GLU A 53 -152.87 -94.72
REMARK 500 ASP A 69 25.63 81.39
REMARK 500 HIS A 77 159.52 -47.12
REMARK 500 SER A 122 -129.08 54.34
REMARK 500 PRO A 225 -9.08 -55.58
REMARK 500 LEU A 241 -60.38 -108.58
REMARK 500 TYR A 268 -146.69 -86.69
REMARK 500 GLU A 274 -159.97 -109.08
REMARK 500 THR A 294 -16.56 -146.20
REMARK 500 GLU B 53 -154.35 -100.06
REMARK 500 ASP B 69 30.57 73.48
REMARK 500 ARG B 87 118.71 -39.08
REMARK 500 SER B 122 -122.53 58.66
REMARK 500 LEU B 174 -154.39 -109.06
REMARK 500 ASP B 180 105.99 -49.19
REMARK 500 TYR B 268 -140.38 -83.49
REMARK 500 GLU B 274 -159.53 -100.63
REMARK 500 THR B 294 -6.29 -149.44
REMARK 500 GLU C 53 -149.58 -105.67
REMARK 500 SER C 122 -134.44 63.27
REMARK 500 SER C 146 66.99 35.95
REMARK 500 PRO C 225 -7.19 -58.40
REMARK 500 LEU C 241 -61.54 -109.24
REMARK 500 TYR C 268 -146.17 -97.00
REMARK 500 PRO D 11 -8.56 -58.32
REMARK 500 GLU D 53 -157.61 -105.16
REMARK 500 ASP D 69 32.45 71.40
REMARK 500 SER D 122 -116.86 53.20
REMARK 500 ARG D 135 74.18 -118.64
REMARK 500 SER D 196 13.75 -140.30
REMARK 500 PRO D 225 3.11 -58.45
REMARK 500 TYR D 268 -136.66 -88.24
REMARK 500 GLU D 274 -156.53 -96.60
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 7L50 A 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L50 A A0A0C4DFN3 10 313
DBREF1 7L50 B 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L50 B A0A0C4DFN3 10 313
DBREF1 7L50 C 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L50 C A0A0C4DFN3 10 313
DBREF1 7L50 D 0 303 UNP A0A0C4DFN3_HUMAN
DBREF2 7L50 D A0A0C4DFN3 10 313
SEQADV 7L50 MET A -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L50 HIS A -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS A -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS A -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS A -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS A -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS A -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY A -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 SER A -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLU A -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ASN A -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 LEU A -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 TYR A -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 PHE A -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLN A -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY A -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ALA A 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L50 SER A 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L50 SER A 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQADV 7L50 MET B -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L50 HIS B -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS B -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS B -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS B -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS B -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS B -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY B -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 SER B -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLU B -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ASN B -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 LEU B -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 TYR B -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 PHE B -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLN B -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY B -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ALA B 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L50 SER B 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L50 SER B 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQADV 7L50 MET C -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L50 HIS C -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS C -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS C -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS C -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS C -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS C -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY C -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 SER C -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLU C -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ASN C -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 LEU C -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 TYR C -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 PHE C -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLN C -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY C -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ALA C 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L50 SER C 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L50 SER C 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQADV 7L50 MET D -16 UNP A0A0C4DFN INITIATING METHIONINE
SEQADV 7L50 HIS D -15 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS D -14 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS D -13 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS D -12 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS D -11 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 HIS D -10 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY D -9 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 SER D -8 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLU D -7 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ASN D -6 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 LEU D -5 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 TYR D -4 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 PHE D -3 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLN D -2 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 GLY D -1 UNP A0A0C4DFN EXPRESSION TAG
SEQADV 7L50 ALA D 36 UNP A0A0C4DFN LYS 46 CONFLICT
SEQADV 7L50 SER D 169 UNP A0A0C4DFN LEU 179 CONFLICT
SEQADV 7L50 SER D 176 UNP A0A0C4DFN LEU 186 CONFLICT
SEQRES 1 A 320 MET HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU TYR
SEQRES 2 A 320 PHE GLN GLY 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 ALA 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 SER VAL LEU PRO ASN LEU SER SER 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 GLY SER GLU ASN LEU TYR
SEQRES 2 B 320 PHE GLN GLY 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 ALA 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 SER VAL LEU PRO ASN LEU SER SER 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
SEQRES 1 C 320 MET HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU TYR
SEQRES 2 C 320 PHE GLN GLY SER MET PRO GLU GLU SER SER PRO ARG ARG
SEQRES 3 C 320 THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU
SEQRES 4 C 320 VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP
SEQRES 5 C 320 ALA PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER
SEQRES 6 C 320 HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU
SEQRES 7 C 320 ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE ALA
SEQRES 8 C 320 HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG
SEQRES 9 C 320 MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 C 320 LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO GLY
SEQRES 11 C 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY ALA
SEQRES 12 C 320 ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE
SEQRES 13 C 320 ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA ASN
SEQRES 14 C 320 PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS
SEQRES 15 C 320 VAL LEU ASN SER VAL LEU PRO ASN LEU SER SER GLY PRO
SEQRES 16 C 320 ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL
SEQRES 17 C 320 ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY
SEQRES 18 C 320 LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL
SEQRES 19 C 320 SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO
SEQRES 20 C 320 PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP
SEQRES 21 C 320 SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS SER
SEQRES 22 C 320 GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS
SEQRES 23 C 320 VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL
SEQRES 24 C 320 PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR ALA
SEQRES 25 C 320 THR ALA GLY THR ALA SER PRO PRO
SEQRES 1 D 320 MET HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU TYR
SEQRES 2 D 320 PHE GLN GLY SER MET PRO GLU GLU SER SER PRO ARG ARG
SEQRES 3 D 320 THR PRO GLN SER ILE PRO TYR GLN ASP LEU PRO HIS LEU
SEQRES 4 D 320 VAL ASN ALA ASP GLY GLN TYR LEU PHE CYS ARG TYR TRP
SEQRES 5 D 320 ALA PRO THR GLY THR PRO LYS ALA LEU ILE PHE VAL SER
SEQRES 6 D 320 HIS GLY ALA GLY GLU HIS SER GLY ARG TYR GLU GLU LEU
SEQRES 7 D 320 ALA ARG MET LEU MET GLY LEU ASP LEU LEU VAL PHE ALA
SEQRES 8 D 320 HIS ASP HIS VAL GLY HIS GLY GLN SER GLU GLY GLU ARG
SEQRES 9 D 320 MET VAL VAL SER ASP PHE HIS VAL PHE VAL ARG ASP VAL
SEQRES 10 D 320 LEU GLN HIS VAL ASP SER MET GLN LYS ASP TYR PRO GLY
SEQRES 11 D 320 LEU PRO VAL PHE LEU LEU GLY HIS SER MET GLY GLY ALA
SEQRES 12 D 320 ILE ALA ILE LEU THR ALA ALA GLU ARG PRO GLY HIS PHE
SEQRES 13 D 320 ALA GLY MET VAL LEU ILE SER PRO LEU VAL LEU ALA ASN
SEQRES 14 D 320 PRO GLU SER ALA THR THR PHE LYS VAL LEU ALA ALA LYS
SEQRES 15 D 320 VAL LEU ASN SER VAL LEU PRO ASN LEU SER SER GLY PRO
SEQRES 16 D 320 ILE ASP SER SER VAL LEU SER ARG ASN LYS THR GLU VAL
SEQRES 17 D 320 ASP ILE TYR ASN SER ASP PRO LEU ILE CYS ARG ALA GLY
SEQRES 18 D 320 LEU LYS VAL CYS PHE GLY ILE GLN LEU LEU ASN ALA VAL
SEQRES 19 D 320 SER ARG VAL GLU ARG ALA LEU PRO LYS LEU THR VAL PRO
SEQRES 20 D 320 PHE LEU LEU LEU GLN GLY SER ALA ASP ARG LEU CYS ASP
SEQRES 21 D 320 SER LYS GLY ALA TYR LEU LEU MET GLU LEU ALA LYS SER
SEQRES 22 D 320 GLN ASP LYS THR LEU LYS ILE TYR GLU GLY ALA TYR HIS
SEQRES 23 D 320 VAL LEU HIS LYS GLU LEU PRO GLU VAL THR ASN SER VAL
SEQRES 24 D 320 PHE HIS GLU ILE ASN MET TRP VAL SER GLN ARG THR ALA
SEQRES 25 D 320 THR ALA GLY THR ALA SER PRO PRO
HET ACT A 601 4
HET ACT A 602 4
HET XOM A 603 25
HET ACT B 601 4
HET ACT B 602 4
HET XOM B 603 25
HET ACT C 601 4
HET ACT C 602 4
HET XOM C 603 25
HET ACT D 601 4
HET ACT D 602 4
HET XOM D 603 25
HETNAM ACT ACETATE ION
HETNAM XOM (2S,4R)-2-{3-[(3-CHLORO-4-METHYLPHENYL)
HETNAM 2 XOM METHOXY]AZETIDINE-1-CARBONYL}-7-OXA-5-
HETNAM 3 XOM AZASPIRO[3.4]OCTAN-6-ONE
FORMUL 5 ACT 8(C2 H3 O2 1-)
FORMUL 7 XOM 4(C18 H21 CL N2 O4)
FORMUL 17 HOH *157(H2 O)
HELIX 1 AA1 PRO A 15 LEU A 19 5 5
HELIX 2 AA2 HIS A 54 ARG A 57 5 4
HELIX 3 AA3 TYR A 58 LEU A 68 1 11
HELIX 4 AA4 PHE A 93 TYR A 111 1 19
HELIX 5 AA5 SER A 122 GLU A 134 1 13
HELIX 6 AA6 ASN A 152 LYS A 165 1 14
HELIX 7 AA7 ASP A 180 SER A 185 5 6
HELIX 8 AA8 ASN A 187 ASP A 197 1 11
HELIX 9 AA9 LYS A 206 LEU A 224 1 19
HELIX 10 AB1 PRO A 225 LEU A 227 5 3
HELIX 11 AB2 ASP A 243 ALA A 254 1 12
HELIX 12 AB3 VAL A 270 GLU A 274 5 5
HELIX 13 AB4 LEU A 275 ARG A 293 1 19
HELIX 14 AB5 PRO B 15 LEU B 19 5 5
HELIX 15 AB6 HIS B 54 ARG B 57 5 4
HELIX 16 AB7 TYR B 58 LEU B 68 1 11
HELIX 17 AB8 PHE B 93 TYR B 111 1 19
HELIX 18 AB9 SER B 122 ARG B 135 1 14
HELIX 19 AC1 ASN B 152 VAL B 166 1 15
HELIX 20 AC2 ASP B 180 LEU B 184 5 5
HELIX 21 AC3 ASN B 187 ASP B 197 1 11
HELIX 22 AC4 LYS B 206 LEU B 224 1 19
HELIX 23 AC5 PRO B 225 LEU B 227 5 3
HELIX 24 AC6 SER B 244 ALA B 254 1 11
HELIX 25 AC7 VAL B 270 GLU B 274 5 5
HELIX 26 AC8 LEU B 275 GLN B 292 1 18
HELIX 27 AC9 PRO C 15 LEU C 19 5 5
HELIX 28 AD1 HIS C 54 ARG C 57 5 4
HELIX 29 AD2 TYR C 58 GLY C 67 1 10
HELIX 30 AD3 PHE C 93 TYR C 111 1 19
HELIX 31 AD4 SER C 122 ARG C 135 1 14
HELIX 32 AD5 ASN C 152 LYS C 165 1 14
HELIX 33 AD6 ASP C 180 SER C 185 5 6
HELIX 34 AD7 ASN C 187 ASN C 195 1 9
HELIX 35 AD8 LYS C 206 LEU C 224 1 19
HELIX 36 AD9 PRO C 225 LEU C 227 5 3
HELIX 37 AE1 SER C 244 ALA C 254 1 11
HELIX 38 AE2 VAL C 270 GLU C 274 5 5
HELIX 39 AE3 LEU C 275 ARG C 293 1 19
HELIX 40 AE4 PRO D 15 LEU D 19 5 5
HELIX 41 AE5 HIS D 54 ARG D 57 5 4
HELIX 42 AE6 TYR D 58 GLY D 67 1 10
HELIX 43 AE7 PHE D 93 TYR D 111 1 19
HELIX 44 AE8 SER D 122 ARG D 135 1 14
HELIX 45 AE9 ASN D 152 VAL D 166 1 15
HELIX 46 AF1 ASP D 180 LEU D 184 5 5
HELIX 47 AF2 ASN D 187 ASN D 195 1 9
HELIX 48 AF3 LYS D 206 LEU D 224 1 19
HELIX 49 AF4 PRO D 225 LEU D 227 5 3
HELIX 50 AF5 ASP D 243 ALA D 254 1 12
HELIX 51 AF6 VAL D 270 GLU D 274 5 5
HELIX 52 AF7 LEU D 275 ARG D 293 1 19
SHEET 1 AA1 8 HIS A 21 VAL A 23 0
SHEET 2 AA1 8 TYR A 29 TRP A 35 -1 O LEU A 30 N LEU A 22
SHEET 3 AA1 8 LEU A 71 HIS A 75 -1 O VAL A 72 N TRP A 35
SHEET 4 AA1 8 LEU A 44 SER A 48 1 N ILE A 45 O LEU A 71
SHEET 5 AA1 8 VAL A 116 HIS A 121 1 O LEU A 119 N SER A 48
SHEET 6 AA1 8 GLY A 141 PRO A 147 1 O VAL A 143 N LEU A 118
SHEET 7 AA1 8 PHE A 231 GLY A 236 1 O LEU A 234 N SER A 146
SHEET 8 AA1 8 LYS A 259 TYR A 264 1 O LYS A 262 N LEU A 233
SHEET 1 AA2 8 HIS B 21 VAL B 23 0
SHEET 2 AA2 8 TYR B 29 TRP B 35 -1 O LEU B 30 N LEU B 22
SHEET 3 AA2 8 LEU B 70 HIS B 75 -1 O ALA B 74 N ARG B 33
SHEET 4 AA2 8 ALA B 43 SER B 48 1 N ALA B 43 O LEU B 71
SHEET 5 AA2 8 VAL B 116 HIS B 121 1 O LEU B 119 N SER B 48
SHEET 6 AA2 8 GLY B 141 ILE B 145 1 O VAL B 143 N LEU B 118
SHEET 7 AA2 8 PHE B 231 GLY B 236 1 O LEU B 232 N LEU B 144
SHEET 8 AA2 8 LYS B 259 TYR B 264 1 O TYR B 264 N GLN B 235
SHEET 1 AA316 HIS C 21 VAL C 23 0
SHEET 2 AA316 TYR C 29 TRP C 35 -1 O LEU C 30 N LEU C 22
SHEET 3 AA316 LEU C 70 HIS C 75 -1 O VAL C 72 N TRP C 35
SHEET 4 AA316 ALA C 43 SER C 48 1 N ALA C 43 O LEU C 71
SHEET 5 AA316 VAL C 116 HIS C 121 1 O PHE C 117 N PHE C 46
SHEET 6 AA316 GLY C 141 ILE C 145 1 O VAL C 143 N LEU C 118
SHEET 7 AA316 PHE C 231 GLY C 236 1 O LEU C 234 N LEU C 144
SHEET 8 AA316 LYS C 259 TYR C 264 1 O TYR C 264 N GLN C 235
SHEET 9 AA316 LYS D 259 TYR D 264 -1 O LEU D 261 N LEU C 261
SHEET 10 AA316 PHE D 231 GLY D 236 1 N GLN D 235 O TYR D 264
SHEET 11 AA316 GLY D 141 PRO D 147 1 N SER D 146 O LEU D 234
SHEET 12 AA316 VAL D 116 HIS D 121 1 N LEU D 118 O VAL D 143
SHEET 13 AA316 ALA D 43 SER D 48 1 N PHE D 46 O LEU D 119
SHEET 14 AA316 LEU D 70 HIS D 75 1 O LEU D 71 N ALA D 43
SHEET 15 AA316 TYR D 29 TRP D 35 -1 N TRP D 35 O VAL D 72
SHEET 16 AA316 HIS D 21 VAL D 23 -1 N LEU D 22 O LEU D 30
CRYST1 62.894 127.168 119.675 90.00 73.67 90.00 P 1 21 1 8
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 0.015900 0.000000 -0.004658 0.00000
SCALE2 0.000000 0.007864 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008707 0.00000
TER 2206 ALA A 295
TER 4445 ALA B 295
TER 6659 ALA C 295
TER 8868 THR D 294
MASTER 530 0 12 52 32 0 0 6 9153 4 132 100
END |