HEADER OXIDOREDUCTASE 03-OCT-06 2ILT
TITLE HUMAN 11-BETA-HYDROXYSTEROID DEHYDROGENASE (HSD1) WITH NADP AND
TITLE 2 ADAMANTANE SULFONE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CORTICOSTEROID 11-BETA-DEHYDROGENASE ISOZYME 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DEHYDROGENASE DOMAIN (RESIDUES 23-284);
COMPND 5 SYNONYM: 11-DH, 11-BETA-HYDROXYSTEROID DEHYDROGENASE 1, 11-BETA-HSD1;
COMPND 6 EC: 1.1.1.146;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: HSD11B1
KEYWDS HSD1, NADP, INHIBITOR, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.LONGENECKER,B.SORENSEN,R.JUDGE,W.QIN,J.T.LINK
REVDAT 5 21-FEB-24 2ILT 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2ILT 1 REMARK
REVDAT 3 13-JUL-11 2ILT 1 VERSN
REVDAT 2 24-FEB-09 2ILT 1 VERSN
REVDAT 1 03-APR-07 2ILT 0
JRNL AUTH B.SORENSEN,M.WINN,J.ROHDE,Q.SHUAI,J.WANG,S.FUNG,K.MONZON,
JRNL AUTH 2 W.CHIOU,D.STOLARIK,H.IMADE,L.PAN,X.DENG,L.CHOVAN,
JRNL AUTH 3 K.LONGENECKER,R.JUDGE,W.QIN,M.BRUNE,H.CAMP,E.U.FREVERT,
JRNL AUTH 4 P.JACOBSON,J.T.LINK
JRNL TITL ADAMANTANE SULFONE AND SULFONAMIDE 11-BETA-HSD1 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 17 527 2007
JRNL REFN ISSN 0960-894X
JRNL PMID 17070044
JRNL DOI 10.1016/J.BMCL.2006.10.008
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 87.71
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 14220
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.209
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 713
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 983
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2100
REMARK 3 BIN FREE R VALUE SET COUNT : 56
REMARK 3 BIN FREE R VALUE : 0.2270
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2130
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 79
REMARK 3 SOLVENT ATOMS : 173
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.378
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.271
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.171
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.826
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.900
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2254 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3063 ; 1.313 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 274 ; 7.064 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;35.748 ;24.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 389 ;15.136 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;14.878 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 349 ; 0.093 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1640 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1084 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1537 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 153 ; 0.150 ; 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): 106 ; 0.186 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.286 ; 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): 1413 ; 0.619 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2192 ; 1.044 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 961 ; 1.442 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 871 ; 2.239 ; 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2ILT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.
REMARK 100 THE DEPOSITION ID IS D_1000039727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 200
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 : 17-BM
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 : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14223
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 87.710
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.7000
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) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 61.93550
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 61.93550
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 61.93550
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 61.93550
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 61.93550
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 61.93550
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 61.93550
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 61.93550
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 61.93550
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 61.93550
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 61.93550
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 61.93550
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 61.93550
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 61.93550
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 61.93550
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 61.93550
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 61.93550
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 61.93550
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 61.93550
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 61.93550
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 61.93550
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 61.93550
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 61.93550
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 61.93550
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 61.93550
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 61.93550
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 300 REMARK: THE MONOMER OF THE ASYMMETRIC UNIT CONSTITUTES HALF OF A
REMARK 300 BIOLOGICALLY RELEVANT DIMER FORMED BY THE SYMMETRY OPERATOR 1-X, Y,
REMARK 300 1-Z
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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 123.87100
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 123.87100
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 79560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 123740 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -517.0 KCAL/MOL
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 BIOMT1 2 -1.000000 0.000000 0.000000 123.87100
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 123.87100
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 123.87100
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 123.87100
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 123.87100
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 123.87100
REMARK 350 BIOMT1 5 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 5 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 6 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT2 6 -1.000000 0.000000 0.000000 123.87100
REMARK 350 BIOMT3 6 0.000000 -1.000000 0.000000 123.87100
REMARK 350 BIOMT1 7 0.000000 0.000000 -1.000000 123.87100
REMARK 350 BIOMT2 7 -1.000000 0.000000 0.000000 123.87100
REMARK 350 BIOMT3 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT1 8 0.000000 0.000000 -1.000000 123.87100
REMARK 350 BIOMT2 8 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 8 0.000000 -1.000000 0.000000 123.87100
REMARK 350 BIOMT1 9 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 9 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 9 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT1 10 0.000000 -1.000000 0.000000 123.87100
REMARK 350 BIOMT2 10 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT3 10 -1.000000 0.000000 0.000000 123.87100
REMARK 350 BIOMT1 11 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 11 0.000000 0.000000 -1.000000 123.87100
REMARK 350 BIOMT3 11 -1.000000 0.000000 0.000000 123.87100
REMARK 350 BIOMT1 12 0.000000 -1.000000 0.000000 123.87100
REMARK 350 BIOMT2 12 0.000000 0.000000 -1.000000 123.87100
REMARK 350 BIOMT3 12 1.000000 0.000000 0.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NI NI A 801 LIES ON A SPECIAL POSITION.
REMARK 375 NI NI A 802 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 903 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 990 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 991 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1012 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1030 LIES ON A SPECIAL POSITION.
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 23 C - N - CA ANGL. DEV. = 9.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 23 47.60 -96.11
REMARK 500 ASN A 24 -122.83 154.99
REMARK 500 ALA A 65 179.36 169.51
REMARK 500 ASP A 131 -9.01 67.37
REMARK 500 PHE A 144 -53.16 -121.97
REMARK 500 SER A 169 -147.92 -123.08
REMARK 500 LYS A 174 -32.86 -132.78
REMARK 500 MET A 179 -9.51 83.84
REMARK 500 ASN A 207 53.64 -92.41
REMARK 500 ASP A 219 37.52 -76.59
REMARK 500 HIS A 232 79.73 -116.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 22 PRO A 23 121.82
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 802 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 12 NE2
REMARK 620 2 HIS A 12 NE2 83.5
REMARK 620 3 HIS A 12 NE2 83.5 83.5
REMARK 620 4 HIS A 14 NE2 96.6 175.1 91.6
REMARK 620 5 HIS A 14 NE2 91.6 96.5 175.1 88.4
REMARK 620 6 HIS A 14 NE2 175.0 91.5 96.6 88.4 88.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 801 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 18 NE2
REMARK 620 2 HIS A 18 NE2 89.5
REMARK 620 3 HIS A 18 NE2 89.4 89.5
REMARK 620 4 HIS A 20 NE2 93.0 90.5 177.5
REMARK 620 5 HIS A 20 NE2 90.4 177.4 93.1 86.9
REMARK 620 6 HIS A 20 NE2 177.4 93.2 90.6 87.0 86.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAP A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NN1 A 902
DBREF 2ILT A 24 285 UNP P28845 DHI1_HUMAN 23 284
SEQADV 2ILT GLN A 11 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT HIS A 12 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT GLN A 13 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT HIS A 14 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT GLN A 15 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT HIS A 16 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT GLN A 17 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT HIS A 18 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT GLN A 19 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT HIS A 20 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT GLN A 21 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT GLN A 22 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT PRO A 23 UNP P28845 CLONING ARTIFACT
SEQADV 2ILT SER A 272 UNP P28845 CYS 271 CONFLICT
SEQRES 1 A 275 GLN HIS GLN HIS GLN HIS GLN HIS GLN HIS GLN GLN PRO
SEQRES 2 A 275 ASN GLU GLU PHE ARG PRO GLU MET LEU GLN GLY LYS LYS
SEQRES 3 A 275 VAL ILE VAL THR GLY ALA SER LYS GLY ILE GLY ARG GLU
SEQRES 4 A 275 MET ALA TYR HIS LEU ALA LYS MET GLY ALA HIS VAL VAL
SEQRES 5 A 275 VAL THR ALA ARG SER LYS GLU THR LEU GLN LYS VAL VAL
SEQRES 6 A 275 SER HIS CYS LEU GLU LEU GLY ALA ALA SER ALA HIS TYR
SEQRES 7 A 275 ILE ALA GLY THR MET GLU ASP MET THR PHE ALA GLU GLN
SEQRES 8 A 275 PHE VAL ALA GLN ALA GLY LYS LEU MET GLY GLY LEU ASP
SEQRES 9 A 275 MET LEU ILE LEU ASN HIS ILE THR ASN THR SER LEU ASN
SEQRES 10 A 275 LEU PHE HIS ASP ASP ILE HIS HIS VAL ARG LYS SER MET
SEQRES 11 A 275 GLU VAL ASN PHE LEU SER TYR VAL VAL LEU THR VAL ALA
SEQRES 12 A 275 ALA LEU PRO MET LEU LYS GLN SER ASN GLY SER ILE VAL
SEQRES 13 A 275 VAL VAL SER SER LEU ALA GLY LYS VAL ALA TYR PRO MET
SEQRES 14 A 275 VAL ALA ALA TYR SER ALA SER LYS PHE ALA LEU ASP GLY
SEQRES 15 A 275 PHE PHE SER SER ILE ARG LYS GLU TYR SER VAL SER ARG
SEQRES 16 A 275 VAL ASN VAL SER ILE THR LEU CYS VAL LEU GLY LEU ILE
SEQRES 17 A 275 ASP THR GLU THR ALA MET LYS ALA VAL SER GLY ILE VAL
SEQRES 18 A 275 HIS MET GLN ALA ALA PRO LYS GLU GLU CYS ALA LEU GLU
SEQRES 19 A 275 ILE ILE LYS GLY GLY ALA LEU ARG GLN GLU GLU VAL TYR
SEQRES 20 A 275 TYR ASP SER SER LEU TRP THR THR LEU LEU ILE ARG ASN
SEQRES 21 A 275 PRO SER ARG LYS ILE LEU GLU PHE LEU TYR SER THR SER
SEQRES 22 A 275 TYR ASN
HET NI A 801 1
HET NI A 802 1
HET NAP A 901 48
HET NN1 A 902 29
HETNAM NI NICKEL (II) ION
HETNAM NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
HETNAM NN1 2-(2-CHLORO-4-FLUOROPHENOXY)-2-METHYL-N-[(1R,2S,3S,5S,
HETNAM 2 NN1 7S)-5-(METHYLSULFONYL)-2-ADAMANTYL]PROPANAMIDE
HETSYN NAP 2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE
FORMUL 2 NI 2(NI 2+)
FORMUL 4 NAP C21 H28 N7 O17 P3
FORMUL 5 NN1 C21 H27 CL F N O4 S
FORMUL 6 HOH *173(H2 O)
HELIX 1 1 ARG A 28 LEU A 32 5 5
HELIX 2 2 LYS A 44 MET A 57 1 14
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 SER A 170 LYS A 174 5 5
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 ILE A 268 1 8
HELIX 12 12 ASN A 270 ASN A 285 1 16
SHEET 1 A 7 SER A 85 ALA A 90 0
SHEET 2 A 7 HIS A 60 ALA A 65 1 N VAL A 63 O HIS A 87
SHEET 3 A 7 LYS A 36 VAL A 39 1 N VAL A 37 O HIS A 60
SHEET 4 A 7 MET A 115 LEU A 118 1 O ILE A 117 N ILE A 38
SHEET 5 A 7 SER A 164 VAL A 168 1 O VAL A 166 N LEU A 116
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
LINK NE2 HIS A 12 NI B NI A 802 1555 1555 2.51
LINK NE2 HIS A 12 NI B NI A 802 6566 1555 2.51
LINK NE2 HIS A 12 NI B NI A 802 12665 1555 2.51
LINK NE2 HIS A 14 NI B NI A 802 1555 1555 2.33
LINK NE2 HIS A 14 NI B NI A 802 6566 1555 2.33
LINK NE2 HIS A 14 NI B NI A 802 12665 1555 2.33
LINK NE2 HIS A 18 NI A NI A 801 1555 1555 2.40
LINK NE2 HIS A 18 NI A NI A 801 6566 1555 2.40
LINK NE2 HIS A 18 NI A NI A 801 12665 1555 2.40
LINK NE2 HIS A 20 NI A NI A 801 1555 1555 2.28
LINK NE2 HIS A 20 NI A NI A 801 12665 1555 2.28
LINK NE2 HIS A 20 NI A NI A 801 6566 1555 2.28
SITE 1 AC1 2 HIS A 18 HIS A 20
SITE 1 AC2 2 HIS A 12 HIS A 14
SITE 1 AC3 32 GLY A 41 ALA A 42 SER A 43 LYS A 44
SITE 2 AC3 32 GLY A 45 ILE A 46 ALA A 65 ARG A 66
SITE 3 AC3 32 SER A 67 GLY A 91 THR A 92 MET A 93
SITE 4 AC3 32 ASN A 119 HIS A 120 ILE A 121 VAL A 168
SITE 5 AC3 32 SER A 169 TYR A 183 LYS A 187 LEU A 215
SITE 6 AC3 32 GLY A 216 LEU A 217 ILE A 218 THR A 220
SITE 7 AC3 32 THR A 222 ALA A 223 NN1 A 902 HOH A 925
SITE 8 AC3 32 HOH A 935 HOH A 947 HOH A 960 HOH A 997
SITE 1 AC4 12 ILE A 121 THR A 124 SER A 170 PRO A 178
SITE 2 AC4 12 TYR A 183 GLY A 216 LEU A 217 THR A 222
SITE 3 AC4 12 ALA A 223 ALA A 226 NAP A 901 HOH A1010
CRYST1 123.871 123.871 123.871 90.00 90.00 90.00 I 2 3 24
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 0.008073 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008073 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008073 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
