HEADER OXIDOREDUCTASE 16-MAY-08 3D5Q
TITLE CRYSTAL STRUCTURE OF 11B-HSD1 IN COMPLEX WITH TRIAZOLE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORTICOSTEROID 11-BETA-DEHYDROGENASE ISOZYME 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 11-DH, 11-BETA-HYDROXYSTEROID DEHYDROGENASE 1, 11-BETA-HSD1;
COMPND 5 EC: 1.1.1.146;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSD11B1, HSD11, HSD11L;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH10A;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15
KEYWDS OXIDOREDUCTASE, 11BETA, HYDROXYSTEROID, DEHYDROGENASE, ENDOPLASMIC
KEYWDS 2 RETICULUM, GLYCOPROTEIN, LIPID METABOLISM, MEMBRANE, MICROSOME,
KEYWDS 3 NADP, POLYMORPHISM, SIGNAL-ANCHOR, STEROID METABOLISM, TRANSMEMBRANE
EXPDTA X-RAY DIFFRACTION
AUTHOR Z.WANG,J.LIU,A.SUDOM,N.P.C.WALKER
REVDAT 5 21-FEB-24 3D5Q 1 REMARK
REVDAT 4 20-OCT-21 3D5Q 1 REMARK SEQADV
REVDAT 3 24-FEB-09 3D5Q 1 VERSN
REVDAT 2 11-NOV-08 3D5Q 1 JRNL
REVDAT 1 07-OCT-08 3D5Q 0
JRNL AUTH H.TU,J.P.POWERS,J.LIU,S.URSU,A.SUDOM,X.YAN,H.XU,D.MEININGER,
JRNL AUTH 2 M.DEGRAFFENREID,X.HE,J.C.JAEN,D.SUN,M.LABELLE,H.YAMAMOTO,
JRNL AUTH 3 B.SHAN,N.P.WALKER,Z.WANG
JRNL TITL DISTINCTIVE MOLECULAR INHIBITION MECHANISMS FOR SELECTIVE
JRNL TITL 2 INHIBITORS OF HUMAN 11BETA-HYDROXYSTEROID DEHYDROGENASE TYPE
JRNL TITL 3 1.
JRNL REF BIOORG.MED.CHEM. V. 16 8922 2008
JRNL REFN ISSN 0968-0896
JRNL PMID 18789704
JRNL DOI 10.1016/J.BMC.2008.08.065
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 40744
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) : 0.232
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2012
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) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2851
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2910
REMARK 3 BIN FREE R VALUE SET COUNT : 141
REMARK 3 BIN FREE R VALUE : 0.2970
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7977
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 308
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 69.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.24000
REMARK 3 B22 (A**2) : -1.85000
REMARK 3 B33 (A**2) : -1.60000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.81000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.736
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.319
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.258
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.598
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.938
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8473 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11500 ; 1.500 ; 2.012
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1031 ; 5.612 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 312 ;38.483 ;24.038
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1490 ;18.934 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;17.904 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1347 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6042 ; 0.004 ; 0.020
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): 5148 ; 0.564 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8286 ; 1.055 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3325 ; 1.234 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3202 ; 2.130 ; 4.500
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 : 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: NULL
REMARK 4
REMARK 4 3D5Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-08.
REMARK 100 THE DEPOSITION ID IS D_1000047625.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUN-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.980
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL, SI (111)
REMARK 200 OPTICS : 3X3 CCD ARRAY
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.2.5
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40780
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 76.696
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.44200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 19% PEG 3350, 0.1 M MES 6.4, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 289K, PH 6.4
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 76.65950
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
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 16210 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 40220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -129.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -49.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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 SER A 228
REMARK 465 GLY A 229
REMARK 465 ILE A 230
REMARK 465 VAL A 231
REMARK 465 HIS A 232
REMARK 465 ILE A 290
REMARK 465 ASN A 291
REMARK 465 LYS A 292
REMARK 465 ASN B 285
REMARK 465 MET B 286
REMARK 465 ASP B 287
REMARK 465 ARG B 288
REMARK 465 PHE B 289
REMARK 465 ILE B 290
REMARK 465 ASN B 291
REMARK 465 LYS B 292
REMARK 465 GLN C 21
REMARK 465 PRO C 22
REMARK 465 SER C 228
REMARK 465 GLY C 229
REMARK 465 ILE C 230
REMARK 465 VAL C 231
REMARK 465 HIS C 232
REMARK 465 MET C 233
REMARK 465 THR C 282
REMARK 465 SER C 283
REMARK 465 TYR C 284
REMARK 465 ASN C 285
REMARK 465 MET C 286
REMARK 465 ASP C 287
REMARK 465 ARG C 288
REMARK 465 PHE C 289
REMARK 465 ILE C 290
REMARK 465 ASN C 291
REMARK 465 LYS C 292
REMARK 465 GLY D 229
REMARK 465 ILE D 230
REMARK 465 VAL D 231
REMARK 465 HIS D 232
REMARK 465 THR D 282
REMARK 465 SER D 283
REMARK 465 TYR D 284
REMARK 465 ASN D 285
REMARK 465 MET D 286
REMARK 465 ASP D 287
REMARK 465 ARG D 288
REMARK 465 PHE D 289
REMARK 465 ILE D 290
REMARK 465 ASN D 291
REMARK 465 LYS D 292
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 22 -170.01 -58.34
REMARK 500 GLU A 25 158.33 175.46
REMARK 500 ALA A 65 -177.01 171.80
REMARK 500 ALA A 86 114.04 -163.19
REMARK 500 ASN A 119 -27.73 -146.27
REMARK 500 HIS A 130 -84.01 -124.43
REMARK 500 PHE A 144 -53.33 -125.91
REMARK 500 ALA A 172 0.91 -61.18
REMARK 500 MET A 179 -1.74 81.93
REMARK 500 VAL A 180 34.26 -140.03
REMARK 500 ASN A 207 46.97 -96.21
REMARK 500 GLN A 234 74.85 -179.27
REMARK 500 SER A 261 89.98 -172.45
REMARK 500 LEU A 262 -39.33 -37.58
REMARK 500 TYR A 280 -3.05 -59.81
REMARK 500 SER A 281 2.85 -63.85
REMARK 500 SER A 283 23.02 -74.80
REMARK 500 MET A 286 56.45 -106.58
REMARK 500 ARG A 288 11.04 -59.38
REMARK 500 LEU B 23 98.30 -63.79
REMARK 500 ASN B 24 109.08 -52.65
REMARK 500 GLU B 25 168.19 137.96
REMARK 500 ALA B 65 -169.25 167.18
REMARK 500 SER B 85 148.97 173.58
REMARK 500 ALA B 86 119.63 -164.67
REMARK 500 ASN B 119 -32.35 -143.08
REMARK 500 HIS B 130 -67.27 -132.66
REMARK 500 ASP B 131 27.61 -159.54
REMARK 500 PHE B 144 -69.57 -123.54
REMARK 500 MET B 179 -2.68 84.71
REMARK 500 ASN B 207 67.13 -108.95
REMARK 500 TRP B 263 -84.80 -58.88
REMARK 500 THR B 264 -62.97 -19.94
REMARK 500 LEU B 279 -71.79 -49.05
REMARK 500 SER B 281 -100.21 -76.12
REMARK 500 SER B 283 49.39 -102.49
REMARK 500 GLU C 49 -47.79 -29.72
REMARK 500 ALA C 65 -176.41 165.95
REMARK 500 SER C 85 158.20 167.25
REMARK 500 ASP C 131 38.96 -161.89
REMARK 500 PHE C 144 -50.84 -137.72
REMARK 500 SER C 169 -155.11 -125.49
REMARK 500 ALA C 172 2.91 -66.32
REMARK 500 MET C 179 -0.61 82.68
REMARK 500 VAL C 180 45.60 -144.86
REMARK 500 SER C 202 18.95 -67.80
REMARK 500 VAL C 203 -43.43 -154.77
REMARK 500 SER C 204 5.41 -57.73
REMARK 500 ASN C 207 53.88 -106.06
REMARK 500 LEU C 217 125.09 -38.89
REMARK 500
REMARK 500 THIS ENTRY HAS 82 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T30 A 293
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T30 B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T30 C 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE T30 D 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3CZR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 11BETA-HSD1 IN COMPLEX WITH
REMARK 900 ARYLSULFONYLPIPERAZINE INHIBITOR
REMARK 900 RELATED ID: 3D3E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 11BETA-HSD1 IN COMPLEX WITH BENZAMIDE INHIBITOR
REMARK 900 RELATED ID: 3D4N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF 11B-HSD1 IN COMPLEX WITH SULFONAMIDE INHIBITOR
DBREF 3D5Q A 24 292 UNP P28845 DHI1_HUMAN 24 292
DBREF 3D5Q B 24 292 UNP P28845 DHI1_HUMAN 24 292
DBREF 3D5Q C 24 292 UNP P28845 DHI1_HUMAN 24 292
DBREF 3D5Q D 24 292 UNP P28845 DHI1_HUMAN 24 292
SEQADV 3D5Q GLN A 21 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q PRO A 22 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q LEU A 23 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q SER A 272 UNP P28845 CYS 272 ENGINEERED MUTATION
SEQADV 3D5Q GLN B 21 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q PRO B 22 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q LEU B 23 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q SER B 272 UNP P28845 CYS 272 ENGINEERED MUTATION
SEQADV 3D5Q GLN C 21 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q PRO C 22 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q LEU C 23 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q SER C 272 UNP P28845 CYS 272 ENGINEERED MUTATION
SEQADV 3D5Q GLN D 21 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q PRO D 22 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q LEU D 23 UNP P28845 EXPRESSION TAG
SEQADV 3D5Q SER D 272 UNP P28845 CYS 272 ENGINEERED MUTATION
SEQRES 1 A 272 GLN PRO LEU ASN GLU GLU PHE ARG PRO GLU MET LEU GLN
SEQRES 2 A 272 GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY ILE
SEQRES 3 A 272 GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY ALA
SEQRES 4 A 272 HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU GLN
SEQRES 5 A 272 LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA SER
SEQRES 6 A 272 ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR PHE
SEQRES 7 A 272 ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET GLY
SEQRES 8 A 272 GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN THR
SEQRES 9 A 272 SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL ARG
SEQRES 10 A 272 LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL LEU
SEQRES 11 A 272 THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN GLY
SEQRES 12 A 272 SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL ALA
SEQRES 13 A 272 TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE ALA
SEQRES 14 A 272 LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR SER
SEQRES 15 A 272 VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL LEU
SEQRES 16 A 272 GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL SER
SEQRES 17 A 272 GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU CYS
SEQRES 18 A 272 ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN GLU
SEQRES 19 A 272 GLU VAL TYR TYR ASP SER SER LEU TRP THR THR LEU LEU
SEQRES 20 A 272 ILE ARG ASN PRO SER ARG LYS ILE LEU GLU PHE LEU TYR
SEQRES 21 A 272 SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
SEQRES 1 B 272 GLN PRO LEU ASN GLU GLU PHE ARG PRO GLU MET LEU GLN
SEQRES 2 B 272 GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY ILE
SEQRES 3 B 272 GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY ALA
SEQRES 4 B 272 HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU GLN
SEQRES 5 B 272 LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA SER
SEQRES 6 B 272 ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR PHE
SEQRES 7 B 272 ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET GLY
SEQRES 8 B 272 GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN THR
SEQRES 9 B 272 SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL ARG
SEQRES 10 B 272 LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL LEU
SEQRES 11 B 272 THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN GLY
SEQRES 12 B 272 SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL ALA
SEQRES 13 B 272 TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE ALA
SEQRES 14 B 272 LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR SER
SEQRES 15 B 272 VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL LEU
SEQRES 16 B 272 GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL SER
SEQRES 17 B 272 GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU CYS
SEQRES 18 B 272 ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN GLU
SEQRES 19 B 272 GLU VAL TYR TYR ASP SER SER LEU TRP THR THR LEU LEU
SEQRES 20 B 272 ILE ARG ASN PRO SER ARG LYS ILE LEU GLU PHE LEU TYR
SEQRES 21 B 272 SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
SEQRES 1 C 272 GLN PRO LEU ASN GLU GLU PHE ARG PRO GLU MET LEU GLN
SEQRES 2 C 272 GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY ILE
SEQRES 3 C 272 GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY ALA
SEQRES 4 C 272 HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU GLN
SEQRES 5 C 272 LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA SER
SEQRES 6 C 272 ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR PHE
SEQRES 7 C 272 ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET GLY
SEQRES 8 C 272 GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN THR
SEQRES 9 C 272 SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL ARG
SEQRES 10 C 272 LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL LEU
SEQRES 11 C 272 THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN GLY
SEQRES 12 C 272 SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL ALA
SEQRES 13 C 272 TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE ALA
SEQRES 14 C 272 LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR SER
SEQRES 15 C 272 VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL LEU
SEQRES 16 C 272 GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL SER
SEQRES 17 C 272 GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU CYS
SEQRES 18 C 272 ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN GLU
SEQRES 19 C 272 GLU VAL TYR TYR ASP SER SER LEU TRP THR THR LEU LEU
SEQRES 20 C 272 ILE ARG ASN PRO SER ARG LYS ILE LEU GLU PHE LEU TYR
SEQRES 21 C 272 SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
SEQRES 1 D 272 GLN PRO LEU ASN GLU GLU PHE ARG PRO GLU MET LEU GLN
SEQRES 2 D 272 GLY LYS LYS VAL ILE VAL THR GLY ALA SER LYS GLY ILE
SEQRES 3 D 272 GLY ARG GLU MET ALA TYR HIS LEU ALA LYS MET GLY ALA
SEQRES 4 D 272 HIS VAL VAL VAL THR ALA ARG SER LYS GLU THR LEU GLN
SEQRES 5 D 272 LYS VAL VAL SER HIS CYS LEU GLU LEU GLY ALA ALA SER
SEQRES 6 D 272 ALA HIS TYR ILE ALA GLY THR MET GLU ASP MET THR PHE
SEQRES 7 D 272 ALA GLU GLN PHE VAL ALA GLN ALA GLY LYS LEU MET GLY
SEQRES 8 D 272 GLY LEU ASP MET LEU ILE LEU ASN HIS ILE THR ASN THR
SEQRES 9 D 272 SER LEU ASN LEU PHE HIS ASP ASP ILE HIS HIS VAL ARG
SEQRES 10 D 272 LYS SER MET GLU VAL ASN PHE LEU SER TYR VAL VAL LEU
SEQRES 11 D 272 THR VAL ALA ALA LEU PRO MET LEU LYS GLN SER ASN GLY
SEQRES 12 D 272 SER ILE VAL VAL VAL SER SER LEU ALA GLY LYS VAL ALA
SEQRES 13 D 272 TYR PRO MET VAL ALA ALA TYR SER ALA SER LYS PHE ALA
SEQRES 14 D 272 LEU ASP GLY PHE PHE SER SER ILE ARG LYS GLU TYR SER
SEQRES 15 D 272 VAL SER ARG VAL ASN VAL SER ILE THR LEU CYS VAL LEU
SEQRES 16 D 272 GLY LEU ILE ASP THR GLU THR ALA MET LYS ALA VAL SER
SEQRES 17 D 272 GLY ILE VAL HIS MET GLN ALA ALA PRO LYS GLU GLU CYS
SEQRES 18 D 272 ALA LEU GLU ILE ILE LYS GLY GLY ALA LEU ARG GLN GLU
SEQRES 19 D 272 GLU VAL TYR TYR ASP SER SER LEU TRP THR THR LEU LEU
SEQRES 20 D 272 ILE ARG ASN PRO SER ARG LYS ILE LEU GLU PHE LEU TYR
SEQRES 21 D 272 SER THR SER TYR ASN MET ASP ARG PHE ILE ASN LYS
HET NAP A 1 48
HET T30 A 293 29
HET NAP B 2 48
HET T30 B 1 29
HET NAP C 3 48
HET T30 C 1 29
HET NAP D 4 48
HET T30 D 1 29
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM T30 3-[1-(4-FLUOROPHENYL)CYCLOPROPYL]-4-(1-METHYLETHYL)-5-
HETNAM 2 T30 [4-(TRIFLUOROMETHOXY)PHENYL]-4H-1,2,4-TRIAZOLE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 5 NAP 4(C21 H28 N7 O17 P3)
FORMUL 6 T30 4(C21 H19 F4 N3 O)
HELIX 1 1 ARG A 28 GLN A 33 5 6
HELIX 2 2 LYS A 44 LYS A 56 1 13
HELIX 3 3 SER A 67 GLU A 80 1 14
HELIX 4 4 ASP A 95 GLY A 111 1 17
HELIX 5 5 ASP A 132 PHE A 144 1 13
HELIX 6 6 PHE A 144 ASN A 162 1 19
HELIX 7 7 ALA A 172 LYS A 174 5 3
HELIX 8 8 VAL A 180 ARG A 205 1 26
HELIX 9 9 THR A 220 VAL A 227 1 8
HELIX 10 10 PRO A 237 LEU A 251 1 15
HELIX 11 11 SER A 261 ILE A 268 1 8
HELIX 12 12 ASN A 270 TYR A 280 1 11
HELIX 13 13 SER A 281 SER A 283 5 3
HELIX 14 14 ARG B 28 GLN B 33 5 6
HELIX 15 15 LYS B 44 MET B 57 1 14
HELIX 16 16 SER B 67 GLY B 82 1 16
HELIX 17 17 ASP B 95 GLY B 111 1 17
HELIX 18 18 ASP B 132 PHE B 144 1 13
HELIX 19 19 PHE B 144 SER B 161 1 18
HELIX 20 20 ALA B 172 LYS B 174 5 3
HELIX 21 21 VAL B 180 SER B 204 1 25
HELIX 22 22 THR B 220 SER B 228 1 9
HELIX 23 23 PRO B 237 LEU B 251 1 15
HELIX 24 24 TRP B 263 ILE B 268 1 6
HELIX 25 25 ASN B 270 SER B 283 1 14
HELIX 26 26 ARG C 28 GLN C 33 5 6
HELIX 27 27 LYS C 44 MET C 57 1 14
HELIX 28 28 SER C 67 GLY C 82 1 16
HELIX 29 29 ASP C 95 GLY C 111 1 17
HELIX 30 30 ASP C 132 ASN C 143 1 12
HELIX 31 31 PHE C 144 SER C 161 1 18
HELIX 32 32 ALA C 172 LYS C 174 5 3
HELIX 33 33 VAL C 180 SER C 202 1 23
HELIX 34 34 THR C 220 LYS C 225 1 6
HELIX 35 35 PRO C 237 LEU C 251 1 15
HELIX 36 36 SER C 261 ARG C 269 1 9
HELIX 37 37 ASN C 270 TYR C 280 1 11
HELIX 38 38 ARG D 28 GLN D 33 5 6
HELIX 39 39 LYS D 44 LYS D 56 1 13
HELIX 40 40 SER D 67 GLU D 80 1 14
HELIX 41 41 ASP D 95 GLY D 111 1 17
HELIX 42 42 ASP D 132 ASN D 143 1 12
HELIX 43 43 PHE D 144 ASN D 162 1 19
HELIX 44 44 SER D 170 LYS D 174 5 5
HELIX 45 45 VAL D 180 VAL D 203 1 24
HELIX 46 46 THR D 220 ALA D 226 1 7
HELIX 47 47 PRO D 237 LEU D 251 1 15
HELIX 48 48 SER D 261 LEU D 266 1 6
HELIX 49 49 ASN D 270 SER D 281 1 12
SHEET 1 A 7 HIS A 87 ALA A 90 0
SHEET 2 A 7 HIS A 60 ALA A 65 1 N VAL A 61 O HIS A 87
SHEET 3 A 7 LYS A 36 VAL A 39 1 N VAL A 37 O VAL A 62
SHEET 4 A 7 MET A 115 LEU A 118 1 O MET A 115 N ILE A 38
SHEET 5 A 7 SER A 164 SER A 170 1 O VAL A 166 N LEU A 118
SHEET 6 A 7 SER A 209 LEU A 215 1 O THR A 211 N VAL A 167
SHEET 7 A 7 GLU A 255 TYR A 258 1 O VAL A 256 N VAL A 214
SHEET 1 B 7 SER B 85 ALA B 90 0
SHEET 2 B 7 HIS B 60 ALA B 65 1 N VAL B 61 O HIS B 87
SHEET 3 B 7 LYS B 36 VAL B 39 1 N VAL B 37 O HIS B 60
SHEET 4 B 7 MET B 115 LEU B 118 1 O MET B 115 N ILE B 38
SHEET 5 B 7 SER B 164 SER B 170 1 O VAL B 166 N LEU B 118
SHEET 6 B 7 SER B 209 LEU B 215 1 O THR B 211 N ILE B 165
SHEET 7 B 7 GLU B 255 TYR B 258 1 O VAL B 256 N VAL B 214
SHEET 1 C 7 SER C 85 ALA C 90 0
SHEET 2 C 7 HIS C 60 ALA C 65 1 N VAL C 63 O HIS C 87
SHEET 3 C 7 LYS C 36 VAL C 39 1 N VAL C 37 O HIS C 60
SHEET 4 C 7 MET C 115 LEU C 118 1 O MET C 115 N ILE C 38
SHEET 5 C 7 SER C 164 SER C 170 1 O VAL C 166 N LEU C 116
SHEET 6 C 7 SER C 209 LEU C 215 1 O THR C 211 N VAL C 167
SHEET 7 C 7 GLU C 255 TYR C 258 1 O VAL C 256 N VAL C 214
SHEET 1 D 7 ALA D 86 ALA D 90 0
SHEET 2 D 7 HIS D 60 ALA D 65 1 N VAL D 63 O ILE D 89
SHEET 3 D 7 LYS D 36 VAL D 39 1 N VAL D 37 O HIS D 60
SHEET 4 D 7 MET D 115 LEU D 118 1 O MET D 115 N ILE D 38
SHEET 5 D 7 SER D 164 VAL D 168 1 O VAL D 166 N LEU D 116
SHEET 6 D 7 SER D 209 LEU D 215 1 O THR D 211 N VAL D 167
SHEET 7 D 7 GLU D 255 TYR D 258 1 O VAL D 256 N VAL D 214
SITE 1 AC1 26 GLY A 41 SER A 43 LYS A 44 GLY A 45
SITE 2 AC1 26 ILE A 46 ALA A 65 ARG A 66 SER A 67
SITE 3 AC1 26 THR A 92 MET A 93 ASN A 119 HIS A 120
SITE 4 AC1 26 ILE A 121 VAL A 168 SER A 169 SER A 170
SITE 5 AC1 26 TYR A 183 LYS A 187 LEU A 215 GLY A 216
SITE 6 AC1 26 LEU A 217 ILE A 218 THR A 220 THR A 222
SITE 7 AC1 26 ALA A 223 T30 A 293
SITE 1 AC2 11 NAP A 1 THR A 124 SER A 125 LEU A 126
SITE 2 AC2 11 SER A 170 LEU A 171 ALA A 172 VAL A 175
SITE 3 AC2 11 TYR A 177 TYR A 183 TYR B 280
SITE 1 AC3 25 T30 B 1 GLY B 41 ALA B 42 SER B 43
SITE 2 AC3 25 LYS B 44 GLY B 45 ILE B 46 ARG B 66
SITE 3 AC3 25 SER B 67 THR B 92 MET B 93 ASN B 119
SITE 4 AC3 25 ILE B 121 VAL B 168 SER B 169 SER B 170
SITE 5 AC3 25 TYR B 183 LYS B 187 LEU B 215 GLY B 216
SITE 6 AC3 25 LEU B 217 ILE B 218 THR B 220 THR B 222
SITE 7 AC3 25 ALA B 223
SITE 1 AC4 13 TYR A 280 NAP B 2 THR B 124 SER B 125
SITE 2 AC4 13 LEU B 126 SER B 170 LEU B 171 VAL B 175
SITE 3 AC4 13 TYR B 177 VAL B 180 TYR B 183 LEU B 217
SITE 4 AC4 13 ALA B 223
SITE 1 AC5 23 T30 C 1 GLY C 41 SER C 43 LYS C 44
SITE 2 AC5 23 GLY C 45 ILE C 46 ARG C 66 SER C 67
SITE 3 AC5 23 THR C 92 MET C 93 ASN C 119 ILE C 121
SITE 4 AC5 23 SER C 169 SER C 170 TYR C 183 LYS C 187
SITE 5 AC5 23 LEU C 215 GLY C 216 LEU C 217 ILE C 218
SITE 6 AC5 23 THR C 220 THR C 222 ALA C 223
SITE 1 AC6 13 NAP C 3 THR C 124 SER C 125 LEU C 126
SITE 2 AC6 13 SER C 170 LEU C 171 ALA C 172 VAL C 175
SITE 3 AC6 13 TYR C 177 VAL C 180 TYR C 183 ALA C 223
SITE 4 AC6 13 TYR D 280
SITE 1 AC7 24 T30 D 1 GLY D 41 SER D 43 LYS D 44
SITE 2 AC7 24 GLY D 45 ILE D 46 ARG D 66 SER D 67
SITE 3 AC7 24 THR D 92 MET D 93 ASN D 119 HIS D 120
SITE 4 AC7 24 ILE D 121 SER D 169 SER D 170 TYR D 183
SITE 5 AC7 24 LYS D 187 LEU D 215 GLY D 216 LEU D 217
SITE 6 AC7 24 ILE D 218 THR D 220 THR D 222 ALA D 223
SITE 1 AC8 12 TYR C 280 NAP D 4 THR D 124 SER D 125
SITE 2 AC8 12 LEU D 126 SER D 170 LEU D 171 VAL D 175
SITE 3 AC8 12 TYR D 177 VAL D 180 TYR D 183 ALA D 223
CRYST1 56.675 153.319 73.601 90.00 92.20 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 0.017644 0.000000 0.000678 0.00000
SCALE2 0.000000 0.006522 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013597 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
