HEADER OXIDOREDUCTASE 25-NOV-04 2BEL
TITLE STRUCTURE OF HUMAN 11-BETA-HYDROXYSTEROID DEHYDROGENASE IN COMPLEX
TITLE 2 WITH NADP AND CARBENOXOLONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORTICOSTEROID 11-BETA-DEHYDROGENASE ISOZYME 1;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: RESIDUES 26-284;
COMPND 5 SYNONYM: HUMAN 11-BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 1,11-DH, 11-
COMPND 6 BETA-HSD1;
COMPND 7 EC: 1.1.1.146;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P11
KEYWDS OXIDOREDUCTASE, GLUCOCORTICOID ACTIVATION, DRUG TARGET, INHIBITOR,
KEYWDS 2 SHORT-CHAIN DEHYDROGENASE/REDUCTASE, HORMONE METABOLISM, MICROSOME,
KEYWDS 3 NADP, STEROID METABOLISM
EXPDTA X-RAY DIFFRACTION
AUTHOR K.KAVANAGH,X.WU,S.SVENSSON,B.ELLEBY,F.VON DELFT,J.E.DEBRECZENI,
AUTHOR 2 S.SHARMA,J.BRAY,A.EDWARDS,C.ARROWSMITH,M.SUNDSTROM,L.ABRAHMSEN,
AUTHOR 3 U.OPPERMANN
REVDAT 4 24-JAN-18 2BEL 1 JRNL
REVDAT 3 13-JUL-11 2BEL 1 VERSN
REVDAT 2 24-FEB-09 2BEL 1 VERSN
REVDAT 1 06-DEC-04 2BEL 0
JRNL AUTH X.WU,K.KAVANAGH,S.SVENSSON,B.ELLEBY,M.HULT,F.VON DELFT,
JRNL AUTH 2 B.MARSDEN,H.JORNVALL,L.ABRAHMSEN,U.OPPERMANN
JRNL TITL THE HIGH RESOLUTION STRUCTURES OF HUMAN, MURINE AND GUINEA
JRNL TITL 2 PIG 11-BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 1 REVEAL
JRNL TITL 3 CRITICAL DIFFERENCES IN ACTIVE SITE ARCHITECTURE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.11 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 2.11
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 56.52
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 66821
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1953
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) : 2.11
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.16
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4333
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2880
REMARK 3 BIN FREE R VALUE SET COUNT : 115
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7439
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 348
REMARK 3 SOLVENT ATOMS : 268
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : 33.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.50
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.43000
REMARK 3 B22 (A**2) : 0.31000
REMARK 3 B33 (A**2) : -1.73000
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): 0.195
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.183
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.184
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.196
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7956 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7400 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10870 ; 1.607 ; 2.017
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17106 ; 0.859 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1000 ; 6.357 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 257 ;36.654 ;24.047
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1307 ;13.838 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 24 ;13.998 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1313 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8546 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1474 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1724 ; 0.210 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7459 ; 0.169 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3917 ; 0.180 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4580 ; 0.087 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 343 ; 0.135 ; 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): 9 ; 0.076 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 37 ; 0.214 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.132 ; 0.200
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): 5158 ; 2.010 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7932 ; 2.969 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3237 ; 4.676 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2936 ; 6.138 ;11.000
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 26 A 268
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4651 18.3629 16.5308
REMARK 3 T TENSOR
REMARK 3 T11: -0.1247 T22: 0.0157
REMARK 3 T33: -0.0483 T12: 0.0523
REMARK 3 T13: 0.0905 T23: 0.1400
REMARK 3 L TENSOR
REMARK 3 L11: 2.3616 L22: 1.4540
REMARK 3 L33: 2.3701 L12: -0.1717
REMARK 3 L13: -0.2123 L23: -0.5538
REMARK 3 S TENSOR
REMARK 3 S11: 0.0328 S12: -0.3304 S13: -0.1705
REMARK 3 S21: 0.3260 S22: 0.1743 S23: 0.2586
REMARK 3 S31: -0.0543 S32: -0.2862 S33: -0.2071
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 27 B 277
REMARK 3 ORIGIN FOR THE GROUP (A): 4.8711 23.5270 -12.8828
REMARK 3 T TENSOR
REMARK 3 T11: -0.2200 T22: -0.0433
REMARK 3 T33: -0.1359 T12: 0.0417
REMARK 3 T13: 0.0147 T23: 0.0271
REMARK 3 L TENSOR
REMARK 3 L11: 1.4279 L22: 1.2343
REMARK 3 L33: 3.2123 L12: -0.3271
REMARK 3 L13: 0.6865 L23: -0.5420
REMARK 3 S TENSOR
REMARK 3 S11: 0.0827 S12: 0.2140 S13: -0.0542
REMARK 3 S21: -0.0866 S22: -0.0055 S23: 0.0593
REMARK 3 S31: -0.0138 S32: 0.1639 S33: -0.0772
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 15 C 271
REMARK 3 ORIGIN FOR THE GROUP (A): 44.6656 -9.3341 -20.5652
REMARK 3 T TENSOR
REMARK 3 T11: 0.2180 T22: -0.1165
REMARK 3 T33: -0.0865 T12: 0.0159
REMARK 3 T13: -0.0336 T23: 0.0506
REMARK 3 L TENSOR
REMARK 3 L11: 0.8367 L22: 3.6680
REMARK 3 L33: 1.0072 L12: -0.6098
REMARK 3 L13: -0.0702 L23: 0.5743
REMARK 3 S TENSOR
REMARK 3 S11: 0.1268 S12: 0.2171 S13: 0.0961
REMARK 3 S21: -1.1445 S22: -0.1036 S23: 0.0161
REMARK 3 S31: -0.2805 S32: 0.0198 S33: -0.0232
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 25 D 277
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3150 5.0606 7.7864
REMARK 3 T TENSOR
REMARK 3 T11: -0.1779 T22: -0.1686
REMARK 3 T33: -0.0860 T12: 0.0026
REMARK 3 T13: -0.0611 T23: 0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 1.0576 L22: 3.0447
REMARK 3 L33: 2.0825 L12: -0.5658
REMARK 3 L13: -0.3827 L23: 1.0301
REMARK 3 S TENSOR
REMARK 3 S11: -0.0422 S12: -0.1194 S13: -0.0361
REMARK 3 S21: 0.2138 S22: 0.1087 S23: -0.1679
REMARK 3 S31: 0.1934 S32: 0.1375 S33: -0.0665
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
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 THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2BEL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1290021771.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : SI 1 1 1
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68824
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 61.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.1
REMARK 200 DATA REDUNDANCY : 4.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.60
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
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: UNPUBLISHED MODEL OF HUMAN 11BETA HSD1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MGCL2, 15% PEG 3350,, PH 5.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 80.08100
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.49200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 80.08100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.49200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 FUNCTION: CATALYZES REVERSIBLY THE CONVERSION OF CORTISOL TO THE
REMARK 400 INACTIVE METABOLITE CORTISONE.
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 GLY A 4
REMARK 465 SER A 5
REMARK 465 SER A 6
REMARK 465 HIS A 7
REMARK 465 HIS A 8
REMARK 465 HIS A 9
REMARK 465 HIS A 10
REMARK 465 HIS A 11
REMARK 465 HIS A 12
REMARK 465 SER A 13
REMARK 465 SER A 14
REMARK 465 GLY A 15
REMARK 465 ARG A 16
REMARK 465 GLU A 17
REMARK 465 ASN A 18
REMARK 465 LEU A 19
REMARK 465 TYR A 20
REMARK 465 PHE A 21
REMARK 465 GLN A 22
REMARK 465 GLY A 23
REMARK 465 HIS A 24
REMARK 465 MET A 25
REMARK 465 ARG A 269
REMARK 465 ASN A 270
REMARK 465 PRO A 271
REMARK 465 CYS A 272
REMARK 465 ARG A 273
REMARK 465 LYS A 274
REMARK 465 ILE A 275
REMARK 465 LEU A 276
REMARK 465 GLU A 277
REMARK 465 PHE A 278
REMARK 465 LEU A 279
REMARK 465 TYR A 280
REMARK 465 SER A 281
REMARK 465 THR A 282
REMARK 465 SER A 283
REMARK 465 TYR A 284
REMARK 465 GLY A 285
REMARK 465 SER A 286
REMARK 465 GLY B 4
REMARK 465 SER B 5
REMARK 465 SER B 6
REMARK 465 HIS B 7
REMARK 465 HIS B 8
REMARK 465 HIS B 9
REMARK 465 HIS B 10
REMARK 465 HIS B 11
REMARK 465 HIS B 12
REMARK 465 SER B 13
REMARK 465 SER B 14
REMARK 465 GLY B 15
REMARK 465 ARG B 16
REMARK 465 GLU B 17
REMARK 465 ASN B 18
REMARK 465 LEU B 19
REMARK 465 TYR B 20
REMARK 465 PHE B 21
REMARK 465 GLN B 22
REMARK 465 GLY B 23
REMARK 465 HIS B 24
REMARK 465 MET B 25
REMARK 465 GLU B 26
REMARK 465 PHE B 278
REMARK 465 LEU B 279
REMARK 465 TYR B 280
REMARK 465 SER B 281
REMARK 465 THR B 282
REMARK 465 SER B 283
REMARK 465 TYR B 284
REMARK 465 GLY B 285
REMARK 465 SER B 286
REMARK 465 GLY C 4
REMARK 465 SER C 5
REMARK 465 SER C 6
REMARK 465 HIS C 7
REMARK 465 HIS C 8
REMARK 465 HIS C 9
REMARK 465 HIS C 10
REMARK 465 HIS C 11
REMARK 465 HIS C 12
REMARK 465 SER C 13
REMARK 465 SER C 14
REMARK 465 ILE C 230
REMARK 465 VAL C 231
REMARK 465 HIS C 232
REMARK 465 CYS C 272
REMARK 465 ARG C 273
REMARK 465 LYS C 274
REMARK 465 ILE C 275
REMARK 465 LEU C 276
REMARK 465 GLU C 277
REMARK 465 PHE C 278
REMARK 465 LEU C 279
REMARK 465 TYR C 280
REMARK 465 SER C 281
REMARK 465 THR C 282
REMARK 465 SER C 283
REMARK 465 TYR C 284
REMARK 465 GLY C 285
REMARK 465 SER C 286
REMARK 465 GLY D 4
REMARK 465 SER D 5
REMARK 465 SER D 6
REMARK 465 HIS D 7
REMARK 465 HIS D 8
REMARK 465 HIS D 9
REMARK 465 HIS D 10
REMARK 465 HIS D 11
REMARK 465 HIS D 12
REMARK 465 SER D 13
REMARK 465 SER D 14
REMARK 465 GLY D 15
REMARK 465 ARG D 16
REMARK 465 GLU D 17
REMARK 465 ASN D 18
REMARK 465 LEU D 19
REMARK 465 TYR D 20
REMARK 465 PHE D 21
REMARK 465 GLN D 22
REMARK 465 GLY D 23
REMARK 465 HIS D 24
REMARK 465 PHE D 278
REMARK 465 LEU D 279
REMARK 465 TYR D 280
REMARK 465 SER D 281
REMARK 465 THR D 282
REMARK 465 SER D 283
REMARK 465 TYR D 284
REMARK 465 GLY D 285
REMARK 465 SER D 286
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 GLU A 26 CG CD OE1 OE2
REMARK 470 LYS A 36 CE NZ
REMARK 470 LYS A 56 CE NZ
REMARK 470 LYS A 68 CD CE NZ
REMARK 470 GLU A 69 CD OE1 OE2
REMARK 470 LYS A 73 CD CE NZ
REMARK 470 GLN A 105 CG CD OE1 NE2
REMARK 470 LEU A 145 CD1 CD2
REMARK 470 ARG A 205 NE CZ NH1 NH2
REMARK 470 GLU A 221 CG CD OE1 OE2
REMARK 470 LYS A 225 CE NZ
REMARK 470 SER A 261 OG
REMARK 470 ILE A 268 CG1 CG2 CD1
REMARK 470 ARG B 28 NE CZ NH1 NH2
REMARK 470 LYS B 68 CD CE NZ
REMARK 470 GLU B 69 CG CD OE1 OE2
REMARK 470 ARG B 205 NE CZ NH1 NH2
REMARK 470 GLU B 221 CG CD OE1 OE2
REMARK 470 LYS B 225 CD CE NZ
REMARK 470 VAL B 231 CG1 CG2
REMARK 470 MET B 233 CG SD CE
REMARK 470 GLU B 239 CD OE1 OE2
REMARK 470 SER B 261 OG
REMARK 470 ILE B 268 CG1 CG2 CD1
REMARK 470 ARG B 269 NE CZ NH1 NH2
REMARK 470 ARG B 273 CD NE CZ NH1 NH2
REMARK 470 LYS B 274 CD CE NZ
REMARK 470 GLU B 277 CD OE1 OE2
REMARK 470 HIS C 24 ND1 CD2 CE1 NE2
REMARK 470 MET C 25 CG SD CE
REMARK 470 GLU C 26 CG CD OE1 OE2
REMARK 470 ARG C 28 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 56 CG CD CE NZ
REMARK 470 LYS C 68 CD CE NZ
REMARK 470 GLU C 69 CG CD OE1 OE2
REMARK 470 GLN C 72 CG CD OE1 NE2
REMARK 470 LYS C 73 CG CD CE NZ
REMARK 470 GLU C 80 CG CD OE1 OE2
REMARK 470 LYS C 108 CD CE NZ
REMARK 470 LYS C 138 CE NZ
REMARK 470 ARG C 205 CZ NH1 NH2
REMARK 470 ASN C 207 OD1 ND2
REMARK 470 GLU C 221 CG CD OE1 OE2
REMARK 470 MET C 233 CG SD CE
REMARK 470 GLN C 234 CD OE1 NE2
REMARK 470 GLU C 239 CG CD OE1 OE2
REMARK 470 ARG C 269 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 270 CG OD1 ND2
REMARK 470 GLU D 26 CD OE1 OE2
REMARK 470 LYS D 56 CG CD CE NZ
REMARK 470 LYS D 68 NZ
REMARK 470 ARG D 205 CD NE CZ NH1 NH2
REMARK 470 GLU D 221 CD OE1 OE2
REMARK 470 LYS D 225 CE NZ
REMARK 470 ILE D 230 CG1 CD1
REMARK 470 VAL D 231 CG1 CG2
REMARK 470 ILE D 268 CG1 CG2 CD1
REMARK 470 ARG D 273 CD NE CZ NH1 NH2
REMARK 470 GLU D 277 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 ALA A 65 -173.96 -178.83
REMARK 500 HIS A 130 -71.04 -125.63
REMARK 500 ASP A 131 21.02 -143.61
REMARK 500 PHE A 144 -59.49 -128.82
REMARK 500 SER A 169 -152.60 -125.26
REMARK 500 VAL A 180 38.15 -141.62
REMARK 500 ASN A 207 59.62 -95.22
REMARK 500 ASP A 219 39.56 -77.82
REMARK 500 SER A 261 -6.38 -55.76
REMARK 500 LEU A 267 46.07 -108.19
REMARK 500 ALA B 65 179.07 173.68
REMARK 500 HIS B 130 -65.86 -125.50
REMARK 500 ASP B 131 28.53 -154.91
REMARK 500 PHE B 144 -65.35 -122.28
REMARK 500 ASN B 162 56.07 36.64
REMARK 500 SER B 169 -149.34 -116.35
REMARK 500 MET B 179 -2.92 81.88
REMARK 500 ASP B 219 39.31 -70.96
REMARK 500 ILE B 268 -72.95 -120.42
REMARK 500 ALA C 65 -176.47 170.21
REMARK 500 HIS C 130 -66.68 -127.68
REMARK 500 ASP C 131 24.45 -157.06
REMARK 500 PHE C 144 -66.38 -123.88
REMARK 500 SER C 169 -156.93 -126.31
REMARK 500 LYS C 174 -32.77 -132.70
REMARK 500 VAL C 180 36.29 -143.12
REMARK 500 ASP C 219 43.83 -80.46
REMARK 500 SER C 261 -5.60 -55.34
REMARK 500 ILE C 268 -55.86 -134.36
REMARK 500 ARG C 269 -79.40 -62.12
REMARK 500 ALA D 65 -177.42 -178.55
REMARK 500 HIS D 130 -74.31 -116.78
REMARK 500 ASP D 131 31.32 -150.92
REMARK 500 PHE D 144 -58.18 -122.45
REMARK 500 SER D 169 -152.12 -120.27
REMARK 500 LYS D 174 -33.18 -131.00
REMARK 500 VAL D 180 35.63 -150.00
REMARK 500 ARG D 205 53.22 35.18
REMARK 500 ASP D 219 45.81 -83.90
REMARK 500 SER D 261 4.79 -66.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 CBO B 1279
REMARK 610 CBO C 1273
REMARK 610 CBO D 1279
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C1274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D1280
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBO A1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP B1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBO B1279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP C1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBO C1273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP D1278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBO D1279
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XU7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE INTERFACE OPEN CONFORMATION OFTETRAMERIC
REMARK 900 11B-HSD1
REMARK 900 RELATED ID: 1XU9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE INTERFACE CLOSED CONFORMATION OF11B-
REMARK 900 HYDROXYSTEROID DEHYDROGENASE ISOZYME 1
DBREF 2BEL A 4 25 PDB 2BEL 2BEL 4 25
DBREF 2BEL A 26 284 UNP P28845 DHI1_HUMAN 26 284
DBREF 2BEL A 285 286 PDB 2BEL 2BEL 285 286
DBREF 2BEL B 4 25 PDB 2BEL 2BEL 4 25
DBREF 2BEL B 26 284 UNP P28845 DHI1_HUMAN 26 284
DBREF 2BEL B 285 286 PDB 2BEL 2BEL 285 286
DBREF 2BEL C 4 25 PDB 2BEL 2BEL 4 25
DBREF 2BEL C 26 284 UNP P28845 DHI1_HUMAN 26 284
DBREF 2BEL C 285 286 PDB 2BEL 2BEL 285 286
DBREF 2BEL D 4 25 PDB 2BEL 2BEL 4 25
DBREF 2BEL D 26 284 UNP P28845 DHI1_HUMAN 26 284
DBREF 2BEL D 285 286 PDB 2BEL 2BEL 285 286
SEQRES 1 A 283 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY ARG
SEQRES 2 A 283 GLU ASN LEU TYR PHE GLN GLY HIS MET GLU PHE ARG PRO
SEQRES 3 A 283 GLU MET LEU GLN GLY LYS LYS VAL ILE VAL THR GLY ALA
SEQRES 4 A 283 SER LYS GLY ILE GLY ARG GLU MET ALA TYR HIS LEU ALA
SEQRES 5 A 283 LYS MET GLY ALA HIS VAL VAL VAL THR ALA ARG SER LYS
SEQRES 6 A 283 GLU THR LEU GLN LYS VAL VAL SER HIS CYS LEU GLU LEU
SEQRES 7 A 283 GLY ALA ALA SER ALA HIS TYR ILE ALA GLY THR MET GLU
SEQRES 8 A 283 ASP MET THR PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY
SEQRES 9 A 283 LYS LEU MET GLY GLY LEU ASP MET LEU ILE LEU ASN HIS
SEQRES 10 A 283 ILE THR ASN THR SER LEU ASN LEU PHE HIS ASP ASP ILE
SEQRES 11 A 283 HIS HIS VAL ARG LYS SER MET GLU VAL ASN PHE LEU SER
SEQRES 12 A 283 TYR VAL VAL LEU THR VAL ALA ALA LEU PRO MET LEU LYS
SEQRES 13 A 283 GLN SER ASN GLY SER ILE VAL VAL VAL SER SER LEU ALA
SEQRES 14 A 283 GLY LYS VAL ALA TYR PRO MET VAL ALA ALA TYR SER ALA
SEQRES 15 A 283 SER LYS PHE ALA LEU ASP GLY PHE PHE SER SER ILE ARG
SEQRES 16 A 283 LYS GLU TYR SER VAL SER ARG VAL ASN VAL SER ILE THR
SEQRES 17 A 283 LEU CYS VAL LEU GLY LEU ILE ASP THR GLU THR ALA MET
SEQRES 18 A 283 LYS ALA VAL SER GLY ILE VAL HIS MET GLN ALA ALA PRO
SEQRES 19 A 283 LYS GLU GLU CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA
SEQRES 20 A 283 LEU ARG GLN GLU GLU VAL TYR TYR ASP SER SER LEU TRP
SEQRES 21 A 283 THR THR LEU LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU
SEQRES 22 A 283 GLU PHE LEU TYR SER THR SER TYR GLY SER
SEQRES 1 B 283 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY ARG
SEQRES 2 B 283 GLU ASN LEU TYR PHE GLN GLY HIS MET GLU PHE ARG PRO
SEQRES 3 B 283 GLU MET LEU GLN GLY LYS LYS VAL ILE VAL THR GLY ALA
SEQRES 4 B 283 SER LYS GLY ILE GLY ARG GLU MET ALA TYR HIS LEU ALA
SEQRES 5 B 283 LYS MET GLY ALA HIS VAL VAL VAL THR ALA ARG SER LYS
SEQRES 6 B 283 GLU THR LEU GLN LYS VAL VAL SER HIS CYS LEU GLU LEU
SEQRES 7 B 283 GLY ALA ALA SER ALA HIS TYR ILE ALA GLY THR MET GLU
SEQRES 8 B 283 ASP MET THR PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY
SEQRES 9 B 283 LYS LEU MET GLY GLY LEU ASP MET LEU ILE LEU ASN HIS
SEQRES 10 B 283 ILE THR ASN THR SER LEU ASN LEU PHE HIS ASP ASP ILE
SEQRES 11 B 283 HIS HIS VAL ARG LYS SER MET GLU VAL ASN PHE LEU SER
SEQRES 12 B 283 TYR VAL VAL LEU THR VAL ALA ALA LEU PRO MET LEU LYS
SEQRES 13 B 283 GLN SER ASN GLY SER ILE VAL VAL VAL SER SER LEU ALA
SEQRES 14 B 283 GLY LYS VAL ALA TYR PRO MET VAL ALA ALA TYR SER ALA
SEQRES 15 B 283 SER LYS PHE ALA LEU ASP GLY PHE PHE SER SER ILE ARG
SEQRES 16 B 283 LYS GLU TYR SER VAL SER ARG VAL ASN VAL SER ILE THR
SEQRES 17 B 283 LEU CYS VAL LEU GLY LEU ILE ASP THR GLU THR ALA MET
SEQRES 18 B 283 LYS ALA VAL SER GLY ILE VAL HIS MET GLN ALA ALA PRO
SEQRES 19 B 283 LYS GLU GLU CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA
SEQRES 20 B 283 LEU ARG GLN GLU GLU VAL TYR TYR ASP SER SER LEU TRP
SEQRES 21 B 283 THR THR LEU LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU
SEQRES 22 B 283 GLU PHE LEU TYR SER THR SER TYR GLY SER
SEQRES 1 C 283 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY ARG
SEQRES 2 C 283 GLU ASN LEU TYR PHE GLN GLY HIS MET GLU PHE ARG PRO
SEQRES 3 C 283 GLU MET LEU GLN GLY LYS LYS VAL ILE VAL THR GLY ALA
SEQRES 4 C 283 SER LYS GLY ILE GLY ARG GLU MET ALA TYR HIS LEU ALA
SEQRES 5 C 283 LYS MET GLY ALA HIS VAL VAL VAL THR ALA ARG SER LYS
SEQRES 6 C 283 GLU THR LEU GLN LYS VAL VAL SER HIS CYS LEU GLU LEU
SEQRES 7 C 283 GLY ALA ALA SER ALA HIS TYR ILE ALA GLY THR MET GLU
SEQRES 8 C 283 ASP MET THR PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY
SEQRES 9 C 283 LYS LEU MET GLY GLY LEU ASP MET LEU ILE LEU ASN HIS
SEQRES 10 C 283 ILE THR ASN THR SER LEU ASN LEU PHE HIS ASP ASP ILE
SEQRES 11 C 283 HIS HIS VAL ARG LYS SER MET GLU VAL ASN PHE LEU SER
SEQRES 12 C 283 TYR VAL VAL LEU THR VAL ALA ALA LEU PRO MET LEU LYS
SEQRES 13 C 283 GLN SER ASN GLY SER ILE VAL VAL VAL SER SER LEU ALA
SEQRES 14 C 283 GLY LYS VAL ALA TYR PRO MET VAL ALA ALA TYR SER ALA
SEQRES 15 C 283 SER LYS PHE ALA LEU ASP GLY PHE PHE SER SER ILE ARG
SEQRES 16 C 283 LYS GLU TYR SER VAL SER ARG VAL ASN VAL SER ILE THR
SEQRES 17 C 283 LEU CYS VAL LEU GLY LEU ILE ASP THR GLU THR ALA MET
SEQRES 18 C 283 LYS ALA VAL SER GLY ILE VAL HIS MET GLN ALA ALA PRO
SEQRES 19 C 283 LYS GLU GLU CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA
SEQRES 20 C 283 LEU ARG GLN GLU GLU VAL TYR TYR ASP SER SER LEU TRP
SEQRES 21 C 283 THR THR LEU LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU
SEQRES 22 C 283 GLU PHE LEU TYR SER THR SER TYR GLY SER
SEQRES 1 D 283 GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY ARG
SEQRES 2 D 283 GLU ASN LEU TYR PHE GLN GLY HIS MET GLU PHE ARG PRO
SEQRES 3 D 283 GLU MET LEU GLN GLY LYS LYS VAL ILE VAL THR GLY ALA
SEQRES 4 D 283 SER LYS GLY ILE GLY ARG GLU MET ALA TYR HIS LEU ALA
SEQRES 5 D 283 LYS MET GLY ALA HIS VAL VAL VAL THR ALA ARG SER LYS
SEQRES 6 D 283 GLU THR LEU GLN LYS VAL VAL SER HIS CYS LEU GLU LEU
SEQRES 7 D 283 GLY ALA ALA SER ALA HIS TYR ILE ALA GLY THR MET GLU
SEQRES 8 D 283 ASP MET THR PHE ALA GLU GLN PHE VAL ALA GLN ALA GLY
SEQRES 9 D 283 LYS LEU MET GLY GLY LEU ASP MET LEU ILE LEU ASN HIS
SEQRES 10 D 283 ILE THR ASN THR SER LEU ASN LEU PHE HIS ASP ASP ILE
SEQRES 11 D 283 HIS HIS VAL ARG LYS SER MET GLU VAL ASN PHE LEU SER
SEQRES 12 D 283 TYR VAL VAL LEU THR VAL ALA ALA LEU PRO MET LEU LYS
SEQRES 13 D 283 GLN SER ASN GLY SER ILE VAL VAL VAL SER SER LEU ALA
SEQRES 14 D 283 GLY LYS VAL ALA TYR PRO MET VAL ALA ALA TYR SER ALA
SEQRES 15 D 283 SER LYS PHE ALA LEU ASP GLY PHE PHE SER SER ILE ARG
SEQRES 16 D 283 LYS GLU TYR SER VAL SER ARG VAL ASN VAL SER ILE THR
SEQRES 17 D 283 LEU CYS VAL LEU GLY LEU ILE ASP THR GLU THR ALA MET
SEQRES 18 D 283 LYS ALA VAL SER GLY ILE VAL HIS MET GLN ALA ALA PRO
SEQRES 19 D 283 LYS GLU GLU CYS ALA LEU GLU ILE ILE LYS GLY GLY ALA
SEQRES 20 D 283 LEU ARG GLN GLU GLU VAL TYR TYR ASP SER SER LEU TRP
SEQRES 21 D 283 THR THR LEU LEU ILE ARG ASN PRO CYS ARG LYS ILE LEU
SEQRES 22 D 283 GLU PHE LEU TYR SER THR SER TYR GLY SER
HET NAP A1269 48
HET CBO A1270 41
HET CL A1271 1
HET NAP B1278 48
HET CBO B1279 37
HET CL B1280 1
HET NAP C1272 48
HET CBO C1273 37
HET CL C1274 1
HET NAP D1278 48
HET CBO D1279 37
HET CL D1280 1
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM CBO CARBENOXOLONE
HETNAM CL CHLORIDE ION
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 5 NAP 4(C21 H28 N7 O17 P3)
FORMUL 6 CBO 4(C34 H50 O7)
FORMUL 7 CL 4(CL 1-)
FORMUL 17 HOH *268(H2 O)
HELIX 1 1 ARG A 28 GLN A 33 5 6
HELIX 2 2 LYS A 44 GLY A 58 1 15
HELIX 3 3 SER A 67 GLY A 82 1 16
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 SER A 204 1 25
HELIX 9 9 THR A 220 SER A 228 1 9
HELIX 10 10 PRO A 237 LEU A 251 1 15
HELIX 11 11 SER A 261 LEU A 267 1 7
HELIX 12 12 ARG B 28 GLN B 33 5 6
HELIX 13 13 LYS B 44 GLY B 58 1 15
HELIX 14 14 SER B 67 GLY B 82 1 16
HELIX 15 15 ASP B 95 GLY B 111 1 17
HELIX 16 16 ASP B 132 PHE B 144 1 13
HELIX 17 17 PHE B 144 SER B 161 1 18
HELIX 18 18 SER B 170 LYS B 174 5 5
HELIX 19 19 VAL B 180 ARG B 205 1 26
HELIX 20 20 THR B 220 VAL B 227 1 8
HELIX 21 21 PRO B 237 LEU B 251 1 15
HELIX 22 22 SER B 261 ILE B 268 1 8
HELIX 23 23 ILE B 268 GLU B 277 1 10
HELIX 24 24 GLY C 15 GLN C 22 1 8
HELIX 25 25 ARG C 28 LEU C 32 5 5
HELIX 26 26 LYS C 44 MET C 57 1 14
HELIX 27 27 SER C 67 LEU C 81 1 15
HELIX 28 28 ASP C 95 GLY C 111 1 17
HELIX 29 29 ASP C 132 PHE C 144 1 13
HELIX 30 30 PHE C 144 ASN C 162 1 19
HELIX 31 31 ALA C 172 LYS C 174 5 3
HELIX 32 32 VAL C 180 SER C 204 1 25
HELIX 33 33 THR C 220 VAL C 227 1 8
HELIX 34 34 PRO C 237 LEU C 251 1 15
HELIX 35 35 SER C 261 ILE C 268 1 8
HELIX 36 36 ARG D 28 GLN D 33 5 6
HELIX 37 37 LYS D 44 MET D 57 1 14
HELIX 38 38 SER D 67 GLY D 82 1 16
HELIX 39 39 ASP D 95 GLY D 111 1 17
HELIX 40 40 ASP D 132 PHE D 144 1 13
HELIX 41 41 PHE D 144 ASN D 162 1 19
HELIX 42 42 SER D 170 LYS D 174 5 5
HELIX 43 43 VAL D 180 SER D 204 1 25
HELIX 44 44 THR D 220 SER D 228 1 9
HELIX 45 45 PRO D 237 LEU D 251 1 15
HELIX 46 46 ASP D 259 SER D 261 5 3
HELIX 47 47 LEU D 262 ILE D 268 1 7
HELIX 48 48 ILE D 268 GLU D 277 1 10
SHEET 1 AA 7 SER A 85 TYR A 88 0
SHEET 2 AA 7 HIS A 60 VAL A 63 1 O VAL A 61 N HIS A 87
SHEET 3 AA 7 LYS A 36 VAL A 39 1 O VAL A 37 N VAL A 62
SHEET 4 AA 7 MET A 115 LEU A 118 1 O MET A 115 N ILE A 38
SHEET 5 AA 7 SER A 164 SER A 170 1 O SER A 164 N LEU A 116
SHEET 6 AA 7 SER A 209 LEU A 215 1 O SER A 209 N ILE A 165
SHEET 7 AA 7 GLU A 255 TYR A 258 1 O VAL A 256 N VAL A 214
SHEET 1 BA 7 SER B 85 ALA B 90 0
SHEET 2 BA 7 HIS B 60 ALA B 65 1 O VAL B 61 N HIS B 87
SHEET 3 BA 7 LYS B 36 VAL B 39 1 O VAL B 37 N VAL B 62
SHEET 4 BA 7 MET B 115 LEU B 118 1 O MET B 115 N ILE B 38
SHEET 5 BA 7 SER B 164 VAL B 168 1 O SER B 164 N LEU B 116
SHEET 6 BA 7 SER B 209 LEU B 215 1 O SER B 209 N ILE B 165
SHEET 7 BA 7 GLU B 255 TYR B 258 1 O VAL B 256 N VAL B 214
SHEET 1 CA 7 SER C 85 ALA C 90 0
SHEET 2 CA 7 HIS C 60 ALA C 65 1 O VAL C 61 N HIS C 87
SHEET 3 CA 7 LYS C 36 VAL C 39 1 O VAL C 37 N VAL C 62
SHEET 4 CA 7 MET C 115 LEU C 118 1 O MET C 115 N ILE C 38
SHEET 5 CA 7 SER C 164 SER C 170 1 O SER C 164 N LEU C 116
SHEET 6 CA 7 SER C 209 LEU C 215 1 O SER C 209 N ILE C 165
SHEET 7 CA 7 GLU C 255 TYR C 258 1 O VAL C 256 N VAL C 214
SHEET 1 DA 7 SER D 85 ALA D 90 0
SHEET 2 DA 7 HIS D 60 ALA D 65 1 O VAL D 61 N HIS D 87
SHEET 3 DA 7 LYS D 36 VAL D 39 1 O VAL D 37 N VAL D 62
SHEET 4 DA 7 MET D 115 LEU D 118 1 O MET D 115 N ILE D 38
SHEET 5 DA 7 SER D 164 VAL D 168 1 O SER D 164 N LEU D 116
SHEET 6 DA 7 SER D 209 LEU D 215 1 O SER D 209 N ILE D 165
SHEET 7 DA 7 GLU D 255 TYR D 258 1 O VAL D 256 N VAL D 214
CISPEP 1 TYR A 258 ASP A 259 0 3.25
CISPEP 2 TYR B 258 ASP B 259 0 10.62
CISPEP 3 TYR C 258 ASP C 259 0 8.63
CISPEP 4 TYR D 258 ASP D 259 0 18.99
SITE 1 AC1 4 GLY A 45 GLU A 221 LYS A 238 HOH A2049
SITE 1 AC2 4 GLY B 45 ARG B 48 GLU B 221 LYS B 238
SITE 1 AC3 3 GLY C 45 GLU C 221 LYS C 238
SITE 1 AC4 3 GLY D 45 GLU D 221 LYS D 238
SITE 1 AC5 30 GLY A 41 ALA A 42 SER A 43 LYS A 44
SITE 2 AC5 30 GLY A 45 ILE A 46 ALA A 65 ARG A 66
SITE 3 AC5 30 SER A 67 THR A 92 MET A 93 ASN A 119
SITE 4 AC5 30 ILE A 121 VAL A 168 SER A 169 SER A 170
SITE 5 AC5 30 TYR A 183 LYS A 187 GLY A 216 LEU A 217
SITE 6 AC5 30 ILE A 218 THR A 220 THR A 222 ALA A 223
SITE 7 AC5 30 CBO A1270 HOH A2001 HOH A2002 HOH A2049
SITE 8 AC5 30 HOH A2050 HOH A2051
SITE 1 AC6 10 ILE A 121 SER A 170 TYR A 177 VAL A 180
SITE 2 AC6 10 TYR A 183 GLY A 216 LEU A 217 MET A 233
SITE 3 AC6 10 NAP A1269 HOH A2043
SITE 1 AC7 35 GLY B 41 ALA B 42 SER B 43 LYS B 44
SITE 2 AC7 35 GLY B 45 ILE B 46 ALA B 65 ARG B 66
SITE 3 AC7 35 SER B 67 THR B 92 MET B 93 ASN B 119
SITE 4 AC7 35 HIS B 120 ILE B 121 VAL B 168 SER B 169
SITE 5 AC7 35 SER B 170 TYR B 183 LYS B 187 LEU B 215
SITE 6 AC7 35 GLY B 216 LEU B 217 ILE B 218 THR B 220
SITE 7 AC7 35 THR B 222 ALA B 223 CBO B1279 HOH B2025
SITE 8 AC7 35 HOH B2074 HOH B2075 HOH B2076 HOH B2077
SITE 9 AC7 35 HOH B2078 HOH B2079 HOH B2080
SITE 1 AC8 7 ILE B 121 SER B 170 TYR B 177 VAL B 180
SITE 2 AC8 7 TYR B 183 LEU B 217 NAP B1278
SITE 1 AC9 30 GLY C 41 ALA C 42 SER C 43 LYS C 44
SITE 2 AC9 30 GLY C 45 ILE C 46 ALA C 65 ARG C 66
SITE 3 AC9 30 SER C 67 GLY C 91 THR C 92 MET C 93
SITE 4 AC9 30 ASN C 119 ILE C 121 VAL C 168 SER C 169
SITE 5 AC9 30 SER C 170 TYR C 183 LYS C 187 LEU C 215
SITE 6 AC9 30 GLY C 216 LEU C 217 ILE C 218 THR C 220
SITE 7 AC9 30 THR C 222 ALA C 223 CBO C1273 HOH C2015
SITE 8 AC9 30 HOH C2052 HOH C2053
SITE 1 BC1 9 ILE C 121 SER C 170 LEU C 171 TYR C 183
SITE 2 BC1 9 GLY C 216 LEU C 217 ALA C 226 NAP C1272
SITE 3 BC1 9 HOH C2054
SITE 1 BC2 31 GLY D 41 ALA D 42 SER D 43 LYS D 44
SITE 2 BC2 31 GLY D 45 ILE D 46 ALA D 65 ARG D 66
SITE 3 BC2 31 SER D 67 THR D 92 MET D 93 ASN D 119
SITE 4 BC2 31 ILE D 121 VAL D 168 SER D 169 TYR D 183
SITE 5 BC2 31 LYS D 187 LEU D 215 GLY D 216 LEU D 217
SITE 6 BC2 31 ILE D 218 THR D 220 THR D 222 ALA D 223
SITE 7 BC2 31 CBO D1279 HOH D2036 HOH D2037 HOH D2078
SITE 8 BC2 31 HOH D2079 HOH D2080 HOH D2081
SITE 1 BC3 10 ILE D 121 THR D 124 SER D 170 TYR D 177
SITE 2 BC3 10 TYR D 183 GLY D 216 LEU D 217 ALA D 226
SITE 3 BC3 10 NAP D1278 HOH D2082
CRYST1 160.162 112.984 66.326 90.00 90.00 90.00 P 21 21 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 0.006244 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008851 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015077 0.00000
MTRIX1 1 -0.938010 0.337520 0.078850 -8.42495 1
MTRIX2 1 0.338140 0.841120 0.422120 2.91119 1
MTRIX3 1 0.076150 0.422610 -0.903110 -5.86785 1
MTRIX1 2 0.231140 0.923610 0.305820 23.52363 1
MTRIX2 2 0.971820 -0.204190 -0.117820 3.88708 1
MTRIX3 2 -0.046370 0.324430 -0.944770 -11.89135 1
MTRIX1 3 0.094580 0.989320 0.110880 22.28565 1
MTRIX2 3 -0.992780 0.085480 0.084140 -3.96804 1
MTRIX3 3 0.073760 -0.118040 0.990270 -5.53188 1
(ATOM LINES ARE NOT SHOWN.)
END
