HEADER OXIDOREDUCTASE 29-NOV-06 2O23
TITLE THE STRUCTURE OF WILD-TYPE HUMAN HADH2 (17BETA-HYDROXYSTEROID
TITLE 2 DEHYDROGENASE TYPE 10) BOUND TO NAD+ AT 1.2 A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HADH2 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: HYDROXYACYL-COENZYME A DEHYDROGENASE, TYPE II;
COMPND 5 EC: 1.1.1.178;
COMPND 6 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: HADH2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11-DERIVATIVE
KEYWDS HSD17B10, SCHAD, ERAB, TYPE II HADH, 2-METHYL-3-HYDROXYBUTYRYL-COA
KEYWDS 2 DEHYDROGENASE, MHBD, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, SGC, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.L.KAVANAGH,N.SHAFQAT,K.SCHOLER,J.DEBRECZENI,J.ZSCHOCKE,F.VON DELFT,
AUTHOR 2 J.WEIGELT,C.ARROWSMITH,M.SUNDSTROM,A.EDWARDS,U.OPPERMANN,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 6 30-AUG-23 2O23 1 REMARK SEQADV
REVDAT 5 31-JAN-18 2O23 1 AUTHOR JRNL
REVDAT 4 18-OCT-17 2O23 1 REMARK
REVDAT 3 13-JUL-11 2O23 1 VERSN
REVDAT 2 24-FEB-09 2O23 1 VERSN
REVDAT 1 12-DEC-06 2O23 0
JRNL AUTH K.L.KAVANAGH,N.SHAFQAT,K.SCHOLER,J.DEBRECZENI,J.ZSCHOCKE,
JRNL AUTH 2 F.VON DELFT,J.WEIGELT,C.ARROWSMITH,M.SUNDSTROM,A.EDWARDS,
JRNL AUTH 3 U.OPPERMANN
JRNL TITL THE STRUCTURE OF WILD-TYPE HUMAN HADH2
JRNL TITL 2 (17BETA-HYDROXYSTEROID DEHYDROGENASE TYPE 10) BOUND TO NAD+
JRNL TITL 3 AT 1.2 A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.20 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) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 166548
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) : 0.123
REMARK 3 R VALUE (WORKING SET) : 0.123
REMARK 3 FREE R VALUE : 0.154
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1996
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12109
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.25
REMARK 3 BIN R VALUE (WORKING SET) : 0.2380
REMARK 3 BIN FREE R VALUE SET COUNT : 157
REMARK 3 BIN FREE R VALUE : 0.2720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3582
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 94
REMARK 3 SOLVENT ATOMS : 614
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.17
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.45000
REMARK 3 B22 (A**2) : -0.45000
REMARK 3 B33 (A**2) : 0.67000
REMARK 3 B12 (A**2) : -0.22000
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): 0.028
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.030
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.020
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.028
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.976
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3917 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2567 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5372 ; 1.550 ; 2.007
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6330 ; 0.961 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 552 ; 5.857 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 144 ;34.888 ;24.653
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 612 ;11.222 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;16.141 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 639 ; 0.091 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4480 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 723 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 736 ; 0.224 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2733 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1932 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1900 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 401 ; 0.161 ; 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): 8 ; 0.257 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 63 ; 0.215 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 54 ; 0.142 ; 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): 2784 ; 4.510 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1084 ; 2.796 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4119 ; 5.149 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1428 ; 7.416 ; 7.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1231 ; 8.854 ;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): 7038 ; 3.737 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 621 ;20.149 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 6404 ; 7.413 ; 3.000
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 : 1.20
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 2O23 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040589.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-SEP-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9687
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 168585
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.26
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: PDB ENTRY 1U7T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.83
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25.5% PEG 3350, 15% GLYCEROL, 0.17 M
REMARK 280 AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K, PH 7
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.05800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 23.02900
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 23.02900
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 46.05800
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 20000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -121.0 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 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 843 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 882 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 903 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1068 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 880 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 980 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 ALA A 3
REMARK 465 ALA A 4
REMARK 465 CYS A 5
REMARK 465 LEU A 205
REMARK 465 LEU A 206
REMARK 465 THR A 207
REMARK 465 SER A 208
REMARK 465 LEU A 209
REMARK 465 PRO A 210
REMARK 465 GLU A 211
REMARK 465 LYS A 212
REMARK 465 VAL A 213
REMARK 465 CYS A 214
REMARK 465 GLY B -1
REMARK 465 HIS B 0
REMARK 465 THR B 207
REMARK 465 SER B 208
REMARK 465 LEU B 209
REMARK 465 PRO B 210
REMARK 465 GLU B 211
REMARK 465 LYS B 212
REMARK 465 VAL B 213
REMARK 465 CYS B 214
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 6 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 44 CG OD1 ND2
REMARK 470 LYS A 52 CD CE NZ
REMARK 470 LYS A 69 NZ
REMARK 470 LYS A 105 CE NZ
REMARK 470 GLN A 143 CG CD OE1 NE2
REMARK 470 ASN A 215 CG OD1 ND2
REMARK 470 PHE A 216 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 260 CD OE1 NE2
REMARK 470 SER A 263 OG
REMARK 470 LYS B 69 CD CE NZ
REMARK 470 LYS B 79 CE NZ
REMARK 470 LYS B 104 CG CD CE NZ
REMARK 470 LYS B 105 CE NZ
REMARK 470 ASN B 215 CG OD1 ND2
REMARK 470 GLN B 220 CG CD OE1 NE2
REMARK 470 SER B 263 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 1028 O HOH B 997 2.17
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 ALA A 63 146.46 -170.60
REMARK 500 ALA A 154 -130.68 -94.97
REMARK 500 GLU A 160 55.20 -140.64
REMARK 500 ASP A 254 10.35 -157.40
REMARK 500 ALA B 63 145.58 -173.29
REMARK 500 LEU B 122 -60.30 -102.14
REMARK 500 ALA B 154 -131.00 -95.23
REMARK 500 ASP B 254 9.04 -155.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 130 0.08 SIDE CHAIN
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 NAD A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAD B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 801
DBREF 2O23 A 1 261 UNP Q6IBS9 Q6IBS9_HUMAN 1 261
DBREF 2O23 B 1 261 UNP Q6IBS9 Q6IBS9_HUMAN 1 261
SEQADV 2O23 GLY A -1 UNP Q6IBS9 CLONING ARTIFACT
SEQADV 2O23 HIS A 0 UNP Q6IBS9 CLONING ARTIFACT
SEQADV 2O23 GLY A 262 UNP Q6IBS9 CLONING ARTIFACT
SEQADV 2O23 SER A 263 UNP Q6IBS9 CLONING ARTIFACT
SEQADV 2O23 GLY B -1 UNP Q6IBS9 CLONING ARTIFACT
SEQADV 2O23 HIS B 0 UNP Q6IBS9 CLONING ARTIFACT
SEQADV 2O23 GLY B 262 UNP Q6IBS9 CLONING ARTIFACT
SEQADV 2O23 SER B 263 UNP Q6IBS9 CLONING ARTIFACT
SEQRES 1 A 265 GLY HIS MET ALA ALA ALA CYS ARG SER VAL LYS GLY LEU
SEQRES 2 A 265 VAL ALA VAL ILE THR GLY GLY ALA SER GLY LEU GLY LEU
SEQRES 3 A 265 ALA THR ALA GLU ARG LEU VAL GLY GLN GLY ALA SER ALA
SEQRES 4 A 265 VAL LEU LEU ASP LEU PRO ASN SER GLY GLY GLU ALA GLN
SEQRES 5 A 265 ALA LYS LYS LEU GLY ASN ASN CYS VAL PHE ALA PRO ALA
SEQRES 6 A 265 ASP VAL THR SER GLU LYS ASP VAL GLN THR ALA LEU ALA
SEQRES 7 A 265 LEU ALA LYS GLY LYS PHE GLY ARG VAL ASP VAL ALA VAL
SEQRES 8 A 265 ASN CYS ALA GLY ILE ALA VAL ALA SER LYS THR TYR ASN
SEQRES 9 A 265 LEU LYS LYS GLY GLN THR HIS THR LEU GLU ASP PHE GLN
SEQRES 10 A 265 ARG VAL LEU ASP VAL ASN LEU MET GLY THR PHE ASN VAL
SEQRES 11 A 265 ILE ARG LEU VAL ALA GLY GLU MET GLY GLN ASN GLU PRO
SEQRES 12 A 265 ASP GLN GLY GLY GLN ARG GLY VAL ILE ILE ASN THR ALA
SEQRES 13 A 265 SER VAL ALA ALA PHE GLU GLY GLN VAL GLY GLN ALA ALA
SEQRES 14 A 265 TYR SER ALA SER LYS GLY GLY ILE VAL GLY MET THR LEU
SEQRES 15 A 265 PRO ILE ALA ARG ASP LEU ALA PRO ILE GLY ILE ARG VAL
SEQRES 16 A 265 MET THR ILE ALA PRO GLY LEU PHE GLY THR PRO LEU LEU
SEQRES 17 A 265 THR SER LEU PRO GLU LYS VAL CYS ASN PHE LEU ALA SER
SEQRES 18 A 265 GLN VAL PRO PHE PRO SER ARG LEU GLY ASP PRO ALA GLU
SEQRES 19 A 265 TYR ALA HIS LEU VAL GLN ALA ILE ILE GLU ASN PRO PHE
SEQRES 20 A 265 LEU ASN GLY GLU VAL ILE ARG LEU ASP GLY ALA ILE ARG
SEQRES 21 A 265 MET GLN PRO GLY SER
SEQRES 1 B 265 GLY HIS MET ALA ALA ALA CYS ARG SER VAL LYS GLY LEU
SEQRES 2 B 265 VAL ALA VAL ILE THR GLY GLY ALA SER GLY LEU GLY LEU
SEQRES 3 B 265 ALA THR ALA GLU ARG LEU VAL GLY GLN GLY ALA SER ALA
SEQRES 4 B 265 VAL LEU LEU ASP LEU PRO ASN SER GLY GLY GLU ALA GLN
SEQRES 5 B 265 ALA LYS LYS LEU GLY ASN ASN CYS VAL PHE ALA PRO ALA
SEQRES 6 B 265 ASP VAL THR SER GLU LYS ASP VAL GLN THR ALA LEU ALA
SEQRES 7 B 265 LEU ALA LYS GLY LYS PHE GLY ARG VAL ASP VAL ALA VAL
SEQRES 8 B 265 ASN CYS ALA GLY ILE ALA VAL ALA SER LYS THR TYR ASN
SEQRES 9 B 265 LEU LYS LYS GLY GLN THR HIS THR LEU GLU ASP PHE GLN
SEQRES 10 B 265 ARG VAL LEU ASP VAL ASN LEU MET GLY THR PHE ASN VAL
SEQRES 11 B 265 ILE ARG LEU VAL ALA GLY GLU MET GLY GLN ASN GLU PRO
SEQRES 12 B 265 ASP GLN GLY GLY GLN ARG GLY VAL ILE ILE ASN THR ALA
SEQRES 13 B 265 SER VAL ALA ALA PHE GLU GLY GLN VAL GLY GLN ALA ALA
SEQRES 14 B 265 TYR SER ALA SER LYS GLY GLY ILE VAL GLY MET THR LEU
SEQRES 15 B 265 PRO ILE ALA ARG ASP LEU ALA PRO ILE GLY ILE ARG VAL
SEQRES 16 B 265 MET THR ILE ALA PRO GLY LEU PHE GLY THR PRO LEU LEU
SEQRES 17 B 265 THR SER LEU PRO GLU LYS VAL CYS ASN PHE LEU ALA SER
SEQRES 18 B 265 GLN VAL PRO PHE PRO SER ARG LEU GLY ASP PRO ALA GLU
SEQRES 19 B 265 TYR ALA HIS LEU VAL GLN ALA ILE ILE GLU ASN PRO PHE
SEQRES 20 B 265 LEU ASN GLY GLU VAL ILE ARG LEU ASP GLY ALA ILE ARG
SEQRES 21 B 265 MET GLN PRO GLY SER
HET NAD A 802 44
HET NAD B 803 44
HET GOL B 801 12
HETNAM NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NAD 2(C21 H27 N7 O14 P2)
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *614(H2 O)
HELIX 1 1 SER A 20 GLN A 33 1 14
HELIX 2 2 GLY A 46 GLY A 55 1 10
HELIX 3 3 SER A 67 GLY A 83 1 17
HELIX 4 4 THR A 110 LEU A 122 1 13
HELIX 5 5 LEU A 122 GLY A 137 1 16
HELIX 6 6 VAL A 156 GLY A 161 1 6
HELIX 7 7 GLN A 165 ALA A 187 1 23
HELIX 8 8 ASN A 215 GLN A 220 1 6
HELIX 9 9 ASP A 229 ASN A 243 1 15
HELIX 10 10 SER B 20 GLN B 33 1 14
HELIX 11 11 GLY B 46 GLY B 55 1 10
HELIX 12 12 SER B 67 GLY B 83 1 17
HELIX 13 13 THR B 110 LEU B 122 1 13
HELIX 14 14 LEU B 122 GLY B 137 1 16
HELIX 15 15 VAL B 156 GLY B 161 1 6
HELIX 16 16 GLN B 165 ALA B 187 1 23
HELIX 17 17 ASN B 215 GLN B 220 1 6
HELIX 18 18 ASP B 229 ASN B 243 1 15
SHEET 1 A 7 CYS A 58 PRO A 62 0
SHEET 2 A 7 SER A 36 ASP A 41 1 N LEU A 39 O ALA A 61
SHEET 3 A 7 VAL A 12 THR A 16 1 N ILE A 15 O VAL A 38
SHEET 4 A 7 VAL A 87 ASN A 90 1 O VAL A 89 N THR A 16
SHEET 5 A 7 GLY A 148 THR A 153 1 O ILE A 151 N ASN A 90
SHEET 6 A 7 ILE A 191 PRO A 198 1 O ARG A 192 N ILE A 150
SHEET 7 A 7 VAL A 250 LEU A 253 1 O ILE A 251 N ALA A 197
SHEET 1 B 2 TYR A 101 ASN A 102 0
SHEET 2 B 2 GLN A 107 THR A 108 -1 O GLN A 107 N ASN A 102
SHEET 1 C 7 CYS B 58 PRO B 62 0
SHEET 2 C 7 SER B 36 ASP B 41 1 N LEU B 39 O ALA B 61
SHEET 3 C 7 VAL B 12 THR B 16 1 N ILE B 15 O VAL B 38
SHEET 4 C 7 VAL B 87 ASN B 90 1 O VAL B 89 N VAL B 14
SHEET 5 C 7 GLY B 148 THR B 153 1 O ILE B 151 N ASN B 90
SHEET 6 C 7 ILE B 191 PRO B 198 1 O ILE B 196 N ASN B 152
SHEET 7 C 7 VAL B 250 LEU B 253 1 O ILE B 251 N ALA B 197
SHEET 1 D 2 TYR B 101 ASN B 102 0
SHEET 2 D 2 GLN B 107 THR B 108 -1 O GLN B 107 N ASN B 102
CISPEP 1 PHE A 223 PRO A 224 0 -4.86
CISPEP 2 PHE B 223 PRO B 224 0 -6.22
SITE 1 AC1 29 GLY A 17 SER A 20 GLY A 21 LEU A 22
SITE 2 AC1 29 ASP A 41 LEU A 42 ALA A 63 ASP A 64
SITE 3 AC1 29 VAL A 65 CYS A 91 ALA A 92 VAL A 120
SITE 4 AC1 29 THR A 153 ALA A 154 TYR A 168 LYS A 172
SITE 5 AC1 29 PRO A 198 GLY A 199 PHE A 201 THR A 203
SITE 6 AC1 29 PRO A 204 HOH A 806 HOH A 844 HOH A 851
SITE 7 AC1 29 HOH A 859 HOH A 928 HOH A 939 HOH A 964
SITE 8 AC1 29 HOH A 995
SITE 1 AC2 31 GLY B 17 SER B 20 GLY B 21 LEU B 22
SITE 2 AC2 31 ASP B 41 LEU B 42 ALA B 63 ASP B 64
SITE 3 AC2 31 VAL B 65 CYS B 91 ALA B 92 GLY B 93
SITE 4 AC2 31 VAL B 120 THR B 153 ALA B 154 TYR B 168
SITE 5 AC2 31 LYS B 172 PRO B 198 GLY B 199 LEU B 200
SITE 6 AC2 31 PHE B 201 THR B 203 PRO B 204 LEU B 205
SITE 7 AC2 31 HOH B 806 HOH B 845 HOH B 848 HOH B 867
SITE 8 AC2 31 HOH B 886 HOH B 913 HOH B1035
SITE 1 AC3 9 GLU A 249 VAL A 250 ARG A 252 GLU B 249
SITE 2 AC3 9 VAL B 250 ARG B 252 HOH B 884 HOH B 900
SITE 3 AC3 9 HOH B1090
CRYST1 117.037 117.037 69.087 90.00 90.00 120.00 P 32 2 1 12
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 0.008544 0.004933 0.000000 0.00000
SCALE2 0.000000 0.009866 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014475 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
