HEADER OXIDOREDUCTASE 20-DEC-13 4O61
TITLE STRUCTURE OF HUMAN ALKBH5 CRYSTALLIZED IN THE PRESENCE OF CITRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA DEMETHYLASE ALKBH5;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 74-294;
COMPND 5 SYNONYM: ALKYLATED DNA REPAIR PROTEIN ALKB HOMOLOG 5, ALPHA-
COMPND 6 KETOGLUTARATE-DEPENDENT DIOXYGENASE ALKB HOMOLOG 5;
COMPND 7 EC: 1.14.11.-;
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 GENE: ALKBH5, ABH5, OFOXD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-V2R-PRARE2;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28-MHL
KEYWDS DIOXYGENASE, RNA DEMETHYLASE, STRUCTURAL GENOMICS CONSORTIUM, SGC,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.TEMPEL,X.CHAO,K.LIU,A.DONG,T.CEROVINA,H.HE,C.BOUNTRA,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,J.MIN,STRUCTURAL GENOMICS CONSORTIUM
AUTHOR 3 (SGC)
REVDAT 5 20-SEP-23 4O61 1 REMARK SEQADV
REVDAT 4 01-JUL-15 4O61 1 JRNL
REVDAT 3 04-JUN-14 4O61 1 JRNL
REVDAT 2 07-MAY-14 4O61 1 JRNL
REVDAT 1 26-FEB-14 4O61 0
JRNL AUTH C.XU,K.LIU,W.TEMPEL,M.DEMETRIADES,W.AIK,C.J.SCHOFIELD,J.MIN
JRNL TITL STRUCTURES OF HUMAN ALKBH5 DEMETHYLASE REVEAL A UNIQUE
JRNL TITL 2 BINDING MODE FOR SPECIFIC SINGLE-STRANDED N6-METHYLADENOSINE
JRNL TITL 3 RNA DEMETHYLATION.
JRNL REF J.BIOL.CHEM. V. 289 17299 2014
JRNL REFN ISSN 0021-9258
JRNL PMID 24778178
JRNL DOI 10.1074/JBC.M114.550350
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 34660
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : THIN SHELLS (SFTOOLS)
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1810
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2338
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.88
REMARK 3 BIN R VALUE (WORKING SET) : 0.2440
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 76
REMARK 3 SOLVENT ATOMS : 272
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.08000
REMARK 3 B22 (A**2) : -0.12000
REMARK 3 B33 (A**2) : -1.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.07000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.152
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.150
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.130
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.681
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3475 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3299 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4729 ; 1.457 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7590 ; 0.806 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 438 ; 5.951 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 163 ;32.370 ;23.067
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 577 ;13.116 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;20.388 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 525 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3928 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 789 ; 0.001 ; 0.020
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): 1702 ; 2.111 ; 2.133
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1701 ; 2.112 ; 2.131
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2127 ; 3.098 ; 3.177
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: PHASER, PARROT, ARP/WARP, BUCCANEER
REMARK 3 WERE ALSO USED DURING PHASING AND REFINEMENT. COOT WAS USED FOR
REMARK 3 INTERACTIVE MODEL BUILDING. MOLPROBITY WAS USED FOR GEOMETRY
REMARK 3 VALIDATION.
REMARK 4
REMARK 4 4O61 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-DEC-13.
REMARK 100 THE DEPOSITION ID IS D_1000084086.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-E DW
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AIMLESS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.2.14, XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34700
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 38.430
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.12900
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.94
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.98300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: BALBES
REMARK 200 STARTING MODEL: PDB ENTRY 3H8R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2 M DIAMMONIUM CITRATE,
REMARK 280 TEMPERATURE 291K
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 28.58600
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
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: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 73
REMARK 465 GLN A 74
REMARK 465 GLN A 75
REMARK 465 GLY A 142
REMARK 465 ALA A 143
REMARK 465 GLN A 144
REMARK 465 LEU A 145
REMARK 465 GLN A 146
REMARK 465 LYS A 147
REMARK 465 ARG A 148
REMARK 465 GLY B 73
REMARK 465 GLN B 74
REMARK 465 GLN B 75
REMARK 465 LEU B 76
REMARK 465 TYR B 141
REMARK 465 GLY B 142
REMARK 465 ALA B 143
REMARK 465 GLN B 144
REMARK 465 LEU B 145
REMARK 465 GLN B 146
REMARK 465 LYS B 147
REMARK 465 ARG B 148
REMARK 465 THR B 294
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 LEU A 76 CG CD1 CD2
REMARK 470 GLN A 77 CG CD OE1 NE2
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 GLU A 79 CG CD OE1 OE2
REMARK 470 GLU A 80 CG CD OE1 OE2
REMARK 470 ARG A 83 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 86 NZ
REMARK 470 ARG A 93 CD NE CZ NH1 NH2
REMARK 470 GLN A 97 CD OE1 NE2
REMARK 470 LYS A 102 NZ
REMARK 470 LYS A 231 CE NZ
REMARK 470 ARG A 238 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 241 CD OE1 OE2
REMARK 470 LYS A 274 CD CE NZ
REMARK 470 THR A 294 CA C O CB OG1 CG2
REMARK 470 GLN B 77 CG CD OE1 NE2
REMARK 470 LYS B 78 CG CD CE NZ
REMARK 470 GLU B 80 CD OE1 OE2
REMARK 470 LYS B 84 NZ
REMARK 470 LYS B 86 CD CE NZ
REMARK 470 ARG B 93 NE CZ NH1 NH2
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 ARG B 180 CD NE CZ NH1 NH2
REMARK 470 LYS B 231 CE NZ
REMARK 470 ARG B 238 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 274 CE NZ
REMARK 470 GLU B 293 CG CD OE1 OE2
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 GLU B 137 UNK UNX B 311 2.12
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 SER A 203 120.59 -27.69
REMARK 500 PHE A 221 -47.10 78.15
REMARK 500 SER B 203 122.44 -33.88
REMARK 500 PRO B 207 107.05 -56.79
REMARK 500 PHE B 221 -43.90 75.89
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 GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 302
DBREF 4O61 A 74 294 UNP Q6P6C2 ALKB5_HUMAN 74 294
DBREF 4O61 B 74 294 UNP Q6P6C2 ALKB5_HUMAN 74 294
SEQADV 4O61 GLY A 73 UNP Q6P6C2 EXPRESSION TAG
SEQADV 4O61 GLY B 73 UNP Q6P6C2 EXPRESSION TAG
SEQRES 1 A 222 GLY GLN GLN LEU GLN LYS GLU GLU GLU ALA ARG LYS VAL
SEQRES 2 A 222 LYS SER GLY ILE ARG GLN MET ARG LEU PHE SER GLN ASP
SEQRES 3 A 222 GLU CYS ALA LYS ILE GLU ALA ARG ILE ASP GLU VAL VAL
SEQRES 4 A 222 SER ARG ALA GLU LYS GLY LEU TYR ASN GLU HIS THR VAL
SEQRES 5 A 222 ASP ARG ALA PRO LEU ARG ASN LYS TYR PHE PHE GLY GLU
SEQRES 6 A 222 GLY TYR THR TYR GLY ALA GLN LEU GLN LYS ARG GLY PRO
SEQRES 7 A 222 GLY GLN GLU ARG LEU TYR PRO PRO GLY ASP VAL ASP GLU
SEQRES 8 A 222 ILE PRO GLU TRP VAL HIS GLN LEU VAL ILE GLN LYS LEU
SEQRES 9 A 222 VAL GLU HIS ARG VAL ILE PRO GLU GLY PHE VAL ASN SER
SEQRES 10 A 222 ALA VAL ILE ASN ASP TYR GLN PRO GLY GLY CYS ILE VAL
SEQRES 11 A 222 SER HIS VAL ASP PRO ILE HIS ILE PHE GLU ARG PRO ILE
SEQRES 12 A 222 VAL SER VAL SER PHE PHE SER ASP SER ALA LEU CYS PHE
SEQRES 13 A 222 GLY CYS LYS PHE GLN PHE LYS PRO ILE ARG VAL SER GLU
SEQRES 14 A 222 PRO VAL LEU SER LEU PRO VAL ARG ARG GLY SER VAL THR
SEQRES 15 A 222 VAL LEU SER GLY TYR ALA ALA ASP GLU ILE THR HIS CYS
SEQRES 16 A 222 ILE ARG PRO GLN ASP ILE LYS GLU ARG ARG ALA VAL ILE
SEQRES 17 A 222 ILE LEU ARG LYS THR ARG LEU ASP ALA PRO ARG LEU GLU
SEQRES 18 A 222 THR
SEQRES 1 B 222 GLY GLN GLN LEU GLN LYS GLU GLU GLU ALA ARG LYS VAL
SEQRES 2 B 222 LYS SER GLY ILE ARG GLN MET ARG LEU PHE SER GLN ASP
SEQRES 3 B 222 GLU CYS ALA LYS ILE GLU ALA ARG ILE ASP GLU VAL VAL
SEQRES 4 B 222 SER ARG ALA GLU LYS GLY LEU TYR ASN GLU HIS THR VAL
SEQRES 5 B 222 ASP ARG ALA PRO LEU ARG ASN LYS TYR PHE PHE GLY GLU
SEQRES 6 B 222 GLY TYR THR TYR GLY ALA GLN LEU GLN LYS ARG GLY PRO
SEQRES 7 B 222 GLY GLN GLU ARG LEU TYR PRO PRO GLY ASP VAL ASP GLU
SEQRES 8 B 222 ILE PRO GLU TRP VAL HIS GLN LEU VAL ILE GLN LYS LEU
SEQRES 9 B 222 VAL GLU HIS ARG VAL ILE PRO GLU GLY PHE VAL ASN SER
SEQRES 10 B 222 ALA VAL ILE ASN ASP TYR GLN PRO GLY GLY CYS ILE VAL
SEQRES 11 B 222 SER HIS VAL ASP PRO ILE HIS ILE PHE GLU ARG PRO ILE
SEQRES 12 B 222 VAL SER VAL SER PHE PHE SER ASP SER ALA LEU CYS PHE
SEQRES 13 B 222 GLY CYS LYS PHE GLN PHE LYS PRO ILE ARG VAL SER GLU
SEQRES 14 B 222 PRO VAL LEU SER LEU PRO VAL ARG ARG GLY SER VAL THR
SEQRES 15 B 222 VAL LEU SER GLY TYR ALA ALA ASP GLU ILE THR HIS CYS
SEQRES 16 B 222 ILE ARG PRO GLN ASP ILE LYS GLU ARG ARG ALA VAL ILE
SEQRES 17 B 222 ILE LEU ARG LYS THR ARG LEU ASP ALA PRO ARG LEU GLU
SEQRES 18 B 222 THR
HET GOL A 301 6
HET CIT A 302 13
HET UNL A 303 4
HET UNX A 304 1
HET UNX A 305 1
HET UNX A 306 1
HET UNX A 307 1
HET UNX A 308 1
HET UNX A 309 1
HET UNX A 310 1
HET UNX A 311 1
HET UNX A 312 1
HET UNX A 313 1
HET UNX A 314 1
HET UNX A 315 1
HET UNX A 316 1
HET UNX A 317 1
HET UNX A 318 1
HET GOL B 301 6
HET CIT B 302 13
HET UNL B 303 4
HET UNX B 304 1
HET UNX B 305 1
HET UNX B 306 1
HET UNX B 307 1
HET UNX B 308 1
HET UNX B 309 1
HET UNX B 310 1
HET UNX B 311 1
HET UNX B 312 1
HET UNX B 313 1
HET UNX B 314 1
HET UNX B 315 1
HET UNX B 316 1
HET UNX B 317 1
HET UNX B 318 1
HETNAM GOL GLYCEROL
HETNAM CIT CITRIC ACID
HETNAM UNL UNKNOWN LIGAND
HETNAM UNX UNKNOWN ATOM OR ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 CIT 2(C6 H8 O7)
FORMUL 6 UNX 30(X)
FORMUL 39 HOH *272(H2 O)
HELIX 1 1 LEU A 76 GLY A 88 1 13
HELIX 2 2 SER A 96 LYS A 116 1 21
HELIX 3 3 ASN A 120 HIS A 122 5 3
HELIX 4 4 PRO A 165 VAL A 172 1 8
HELIX 5 5 VAL A 172 HIS A 179 1 8
HELIX 6 6 CYS A 230 PHE A 234 5 5
HELIX 7 7 SER A 257 GLU A 263 1 7
HELIX 8 8 ARG A 269 ILE A 273 5 5
HELIX 9 9 LYS B 78 GLY B 88 1 11
HELIX 10 10 SER B 96 LYS B 116 1 21
HELIX 11 11 ASN B 120 HIS B 122 5 3
HELIX 12 12 PRO B 165 VAL B 172 1 8
HELIX 13 13 VAL B 172 HIS B 179 1 8
HELIX 14 14 CYS B 230 PHE B 234 5 5
HELIX 15 15 SER B 257 GLU B 263 1 7
HELIX 16 16 ARG B 269 ILE B 273 5 5
SHEET 1 A 7 ILE A 89 ARG A 93 0
SHEET 2 A 7 SER A 252 LEU A 256 -1 O VAL A 255 N ARG A 90
SHEET 3 A 7 ILE A 215 PHE A 220 -1 N SER A 217 O THR A 254
SHEET 4 A 7 ARG A 277 ARG A 283 -1 O LEU A 282 N VAL A 216
SHEET 5 A 7 SER A 189 TYR A 195 -1 N TYR A 195 O ARG A 277
SHEET 6 A 7 ARG A 130 PHE A 135 -1 N ASN A 131 O ASP A 194
SHEET 7 A 7 VAL A 124 ALA A 127 -1 N ASP A 125 O LYS A 132
SHEET 1 B 4 ILE A 201 HIS A 204 0
SHEET 2 B 4 HIS A 266 ILE A 268 -1 O HIS A 266 N HIS A 204
SHEET 3 B 4 SER A 224 PHE A 228 -1 N CYS A 227 O CYS A 267
SHEET 4 B 4 LEU A 244 VAL A 248 -1 O LEU A 244 N PHE A 228
SHEET 1 C 7 ILE B 89 ARG B 93 0
SHEET 2 C 7 SER B 252 LEU B 256 -1 O VAL B 255 N ARG B 90
SHEET 3 C 7 ILE B 215 PHE B 220 -1 N SER B 217 O THR B 254
SHEET 4 C 7 ARG B 277 ARG B 283 -1 O ALA B 278 N PHE B 220
SHEET 5 C 7 SER B 189 TYR B 195 -1 N VAL B 191 O ILE B 281
SHEET 6 C 7 ARG B 130 PHE B 135 -1 N ASN B 131 O ASP B 194
SHEET 7 C 7 VAL B 124 ALA B 127 -1 N ASP B 125 O LYS B 132
SHEET 1 D 4 ILE B 201 HIS B 204 0
SHEET 2 D 4 HIS B 266 ILE B 268 -1 O HIS B 266 N HIS B 204
SHEET 3 D 4 SER B 224 PHE B 228 -1 N CYS B 227 O CYS B 267
SHEET 4 D 4 LEU B 244 VAL B 248 -1 O LEU B 244 N PHE B 228
SSBOND 1 CYS A 230 CYS A 267 1555 1555 2.14
SSBOND 2 CYS B 230 CYS B 267 1555 1555 2.07
CISPEP 1 ARG A 213 PRO A 214 0 3.96
CISPEP 2 ARG B 213 PRO B 214 0 7.53
SITE 1 AC1 4 GLU A 263 THR A 265 HOH A 411 HOH A 487
SITE 1 AC2 11 LYS A 132 ASN A 193 ILE A 201 HIS A 204
SITE 2 AC2 11 ASP A 206 ILE A 215 SER A 217 HIS A 266
SITE 3 AC2 11 ILE A 281 ARG A 283 HOH A 416
SITE 1 AC3 8 ALA B 114 GLY B 117 LEU B 118 TYR B 119
SITE 2 AC3 8 VAL B 124 ARG B 126 HOH B 404 HOH B 486
SITE 1 AC4 11 LYS B 132 ASN B 193 ILE B 201 HIS B 204
SITE 2 AC4 11 ASP B 206 ILE B 215 SER B 217 HIS B 266
SITE 3 AC4 11 ILE B 281 ARG B 283 HOH B 406
CRYST1 50.471 57.172 78.644 90.00 102.23 90.00 P 1 21 1 4
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 0.019813 0.000000 0.004295 0.00000
SCALE2 0.000000 0.017491 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013011 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
