HEADER OXIDOREDUCTASE 10-JUN-07 2Q8E
TITLE SPECIFICITY AND MECHANISM OF JMJD2A, A TRIMETHYLLYSINE-SPECIFIC
TITLE 2 HISTONE DEMETHYLASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: JUMONJI DOMAIN;
COMPND 5 SYNONYM: JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
COMPND 6 EC: 1.14.11.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: HISTONE 3 PEPTIDE;
COMPND 10 CHAIN: F, G;
COMPND 11 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: JMJD2A, JHDM3A, JMJD2, KIAA0677;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: SYNTHETIC PEPTIDE
KEYWDS HISTONE DEMETHYLASE, HYDROXYLASE, N-OXALYLGLYCINE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-F.COUTURE,E.COLLAZO,P.ORTIZ-TELLO,J.S.BRUNZELLE,R.C.TRIEVEL
REVDAT 5 30-AUG-23 2Q8E 1 REMARK SEQADV LINK
REVDAT 4 24-JAN-18 2Q8E 1 AUTHOR
REVDAT 3 24-FEB-09 2Q8E 1 VERSN
REVDAT 2 29-JAN-08 2Q8E 1 JRNL
REVDAT 1 03-JUL-07 2Q8E 0
JRNL AUTH J.F.COUTURE,E.COLLAZO,P.A.ORTIZ-TELLO,J.S.BRUNZELLE,
JRNL AUTH 2 R.C.TRIEVEL
JRNL TITL SPECIFICITY AND MECHANISM OF JMJD2A, A
JRNL TITL 2 TRIMETHYLLYSINE-SPECIFIC HISTONE DEMETHYLASE.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 14 689 2007
JRNL REFN ISSN 1545-9993
JRNL PMID 17589523
JRNL DOI 10.1038/NSMB1273
REMARK 2
REMARK 2 RESOLUTION. 2.05 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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 54030
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2753
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3732
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE SET COUNT : 229
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5599
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 47.43
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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): 0.206
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.878
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5802 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7858 ; 1.561 ; 1.946
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 688 ; 6.446 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 275 ;32.602 ;23.309
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 943 ;16.516 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 34 ;18.279 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 805 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4492 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2672 ; 0.208 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3948 ; 0.311 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 306 ; 0.239 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 3 ; 0.258 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 32 ; 0.201 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.151 ; 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): 3553 ; 0.860 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5570 ; 1.362 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2639 ; 2.201 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2288 ; 3.139 ; 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 : 1.20
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 2Q8E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-07.
REMARK 100 THE DEPOSITION ID IS D_1000043278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-FEB-07
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 : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54092
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 37.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.46300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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: 2GP5
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 50.14700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.48200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.14700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.48200
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 300 REMARK: JMJD2A IS A MONOMER WITH TWO MOLECULES IN THE ASYMMETRIC
REMARK 300 UNIT.
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: 1340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G
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 -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 347
REMARK 465 PRO A 348
REMARK 465 GLU A 349
REMARK 465 ALA A 350
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 SER B 3
REMARK 465 GLU B 4
REMARK 465 SER B 5
REMARK 465 GLU B 6
REMARK 465 THR B 7
REMARK 465 LEU B 8
REMARK 465 PRO B 346
REMARK 465 THR B 347
REMARK 465 PRO B 348
REMARK 465 GLU B 349
REMARK 465 ALA B 350
REMARK 465 ARG F 26
REMARK 465 LYS F 27
REMARK 465 SER F 28
REMARK 465 ALA F 29
REMARK 465 PRO F 30
REMARK 465 ALA F 31
REMARK 465 THR F 32
REMARK 465 LYS F 37
REMARK 465 PRO F 38
REMARK 465 HIS F 39
REMARK 465 ARG F 40
REMARK 465 TYR F 41
REMARK 465 ARG G 26
REMARK 465 LYS G 27
REMARK 465 SER G 28
REMARK 465 ALA G 29
REMARK 465 PRO G 30
REMARK 465 ALA G 31
REMARK 465 THR G 32
REMARK 465 ARG G 40
REMARK 465 TYR G 41
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 4 CG CD OE1 OE2
REMARK 470 ARG A 25 CD NE CZ NH1 NH2
REMARK 470 ARG A 29 CD NE CZ NH1 NH2
REMARK 470 LYS A 54 CD CE NZ
REMARK 470 ARG A 95 CD NE CZ NH1 NH2
REMARK 470 LYS A 143 CD CE NZ
REMARK 470 LYS A 162 CD CE NZ
REMARK 470 GLN A 232 CG CD OE1 NE2
REMARK 470 LYS A 310 CB CG CD CE NZ
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 PRO A 346 O
REMARK 470 GLU B 22 CD OE1 OE2
REMARK 470 LYS B 51 CD CE NZ
REMARK 470 LYS B 54 CD CE NZ
REMARK 470 LYS B 99 CE NZ
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 163 CG CD OE1 OE2
REMARK 470 GLU B 235 CG CD OE1 OE2
REMARK 470 LYS B 310 CB CG CD CE NZ
REMARK 470 LYS B 314 CG CD CE NZ
REMARK 470 LYS B 323 CD CE NZ
REMARK 470 LEU B 345 O
REMARK 470 VAL F 35 CG1 CG2
REMARK 470 HIS G 39 CG ND1 CD2 CE1 NE2
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 512 O HOH A 651 1.44
REMARK 500 O HOH A 525 O HOH A 636 1.61
REMARK 500 O HOH A 511 O HOH A 651 1.86
REMARK 500 OH TYR B 111 O HOH B 596 1.93
REMARK 500 O HOH B 577 O HOH B 598 1.93
REMARK 500 O HOH A 510 O HOH A 535 2.04
REMARK 500 O HOH A 545 O HOH A 623 2.04
REMARK 500 O VAL B 66 O HOH B 579 2.09
REMARK 500 O HOH A 547 O HOH A 646 2.19
REMARK 500
REMARK 500 REMARK: NULL
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 LEU B 74 CA - CB - CG ANGL. DEV. = -13.9 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 SER A 112 -80.14 -84.63
REMARK 500 ARG A 152 72.78 -162.96
REMARK 500 VAL A 171 -63.03 -99.61
REMARK 500 LYS A 182 3.63 83.64
REMARK 500 GLN A 325 49.50 -140.34
REMARK 500 ARG B 152 69.28 -159.61
REMARK 500 VAL B 171 -62.41 -100.69
REMARK 500 LYS B 182 2.00 82.52
REMARK 500 ALA B 236 56.96 -149.85
REMARK 500 LYS G 37 104.41 162.45
REMARK 500 PRO G 38 -177.37 -47.14
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 501 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 188 NE2
REMARK 620 2 GLU A 190 OE1 91.2
REMARK 620 3 HIS A 276 NE2 92.8 92.0
REMARK 620 4 OGA A 503 O2' 93.1 162.5 104.7
REMARK 620 5 OGA A 503 O2 163.3 95.6 102.1 76.0
REMARK 620 6 HOH A 563 O 78.9 75.2 164.4 89.1 88.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 113.3
REMARK 620 3 CYS A 306 SG 119.0 107.5
REMARK 620 4 CYS A 308 SG 109.6 97.4 107.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 502 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 188 NE2
REMARK 620 2 GLU B 190 OE1 96.8
REMARK 620 3 HIS B 276 NE2 89.9 89.3
REMARK 620 4 OGA B 504 O2 167.7 95.5 90.0
REMARK 620 5 OGA B 504 O2' 90.9 169.4 98.0 77.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 506 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 HIS B 240 NE2 116.8
REMARK 620 3 CYS B 306 SG 109.7 105.5
REMARK 620 4 CYS B 308 SG 116.6 98.7 108.5
REMARK 620 N 1 2 3
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OGA B 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2Q8C RELATED DB: PDB
REMARK 900 JMJD2A IN TERNARY COMPLEX WITH HISTONE H3-K9ME3 AND ALPHA-
REMARK 900 KETOGLUTARATE
REMARK 900 RELATED ID: 2Q8D RELATED DB: PDB
REMARK 900 JMJD2A IN TERNARY COMPLEX WITH HISTONE H3-K36ME2 AND SUCCINATE
DBREF 2Q8E A 1 350 UNP O75164 JHD3A_HUMAN 1 350
DBREF 2Q8E B 1 350 UNP O75164 JHD3A_HUMAN 1 350
DBREF 2Q8E F 26 41 PDB 2Q8E 2Q8E 26 41
DBREF 2Q8E G 26 41 PDB 2Q8E 2Q8E 26 41
SEQADV 2Q8E GLY A -1 UNP O75164 CLONING ARTIFACT
SEQADV 2Q8E SER A 0 UNP O75164 CLONING ARTIFACT
SEQADV 2Q8E GLY B -1 UNP O75164 CLONING ARTIFACT
SEQADV 2Q8E SER B 0 UNP O75164 CLONING ARTIFACT
SEQRES 1 A 352 GLY SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER
SEQRES 2 A 352 ALA ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE
SEQRES 3 A 352 ARG ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN
SEQRES 4 A 352 GLY ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO
SEQRES 5 A 352 LYS GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP
SEQRES 6 A 352 ASP LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR
SEQRES 7 A 352 GLY GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS
SEQRES 8 A 352 LYS ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN
SEQRES 9 A 352 SER ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU
SEQRES 10 A 352 GLU LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN
SEQRES 11 A 352 PRO PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR
SEQRES 12 A 352 GLU LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG
SEQRES 13 A 352 THR ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR
SEQRES 14 A 352 ILE GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET
SEQRES 15 A 352 TRP LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP
SEQRES 16 A 352 LEU TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS
SEQRES 17 A 352 SER TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU
SEQRES 18 A 352 GLU ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN
SEQRES 19 A 352 SER CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE
SEQRES 20 A 352 SER PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP
SEQRES 21 A 352 LYS VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE
SEQRES 22 A 352 PRO TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN
SEQRES 23 A 352 CYS ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE
SEQRES 24 A 352 GLU TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS
SEQRES 25 A 352 ASP MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS
SEQRES 26 A 352 PHE GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS
SEQRES 27 A 352 ASP ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU
SEQRES 28 A 352 ALA
SEQRES 1 B 352 GLY SER MET ALA SER GLU SER GLU THR LEU ASN PRO SER
SEQRES 2 B 352 ALA ARG ILE MET THR PHE TYR PRO THR MET GLU GLU PHE
SEQRES 3 B 352 ARG ASN PHE SER ARG TYR ILE ALA TYR ILE GLU SER GLN
SEQRES 4 B 352 GLY ALA HIS ARG ALA GLY LEU ALA LYS VAL VAL PRO PRO
SEQRES 5 B 352 LYS GLU TRP LYS PRO ARG ALA SER TYR ASP ASP ILE ASP
SEQRES 6 B 352 ASP LEU VAL ILE PRO ALA PRO ILE GLN GLN LEU VAL THR
SEQRES 7 B 352 GLY GLN SER GLY LEU PHE THR GLN TYR ASN ILE GLN LYS
SEQRES 8 B 352 LYS ALA MET THR VAL ARG GLU PHE ARG LYS ILE ALA ASN
SEQRES 9 B 352 SER ASP LYS TYR CYS THR PRO ARG TYR SER GLU PHE GLU
SEQRES 10 B 352 GLU LEU GLU ARG LYS TYR TRP LYS ASN LEU THR PHE ASN
SEQRES 11 B 352 PRO PRO ILE TYR GLY ALA ASP VAL ASN GLY THR LEU TYR
SEQRES 12 B 352 GLU LYS HIS VAL ASP GLU TRP ASN ILE GLY ARG LEU ARG
SEQRES 13 B 352 THR ILE LEU ASP LEU VAL GLU LYS GLU SER GLY ILE THR
SEQRES 14 B 352 ILE GLU GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET
SEQRES 15 B 352 TRP LYS THR SER PHE ALA TRP HIS THR GLU ASP MET ASP
SEQRES 16 B 352 LEU TYR SER ILE ASN TYR LEU HIS PHE GLY GLU PRO LYS
SEQRES 17 B 352 SER TRP TYR SER VAL PRO PRO GLU HIS GLY LYS ARG LEU
SEQRES 18 B 352 GLU ARG LEU ALA LYS GLY PHE PHE PRO GLY SER ALA GLN
SEQRES 19 B 352 SER CYS GLU ALA PHE LEU ARG HIS LYS MET THR LEU ILE
SEQRES 20 B 352 SER PRO LEU MET LEU LYS LYS TYR GLY ILE PRO PHE ASP
SEQRES 21 B 352 LYS VAL THR GLN GLU ALA GLY GLU PHE MET ILE THR PHE
SEQRES 22 B 352 PRO TYR GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN
SEQRES 23 B 352 CYS ALA GLU SER THR ASN PHE ALA THR ARG ARG TRP ILE
SEQRES 24 B 352 GLU TYR GLY LYS GLN ALA VAL LEU CYS SER CYS ARG LYS
SEQRES 25 B 352 ASP MET VAL LYS ILE SER MET ASP VAL PHE VAL ARG LYS
SEQRES 26 B 352 PHE GLN PRO GLU ARG TYR LYS LEU TRP LYS ALA GLY LYS
SEQRES 27 B 352 ASP ASN THR VAL ILE ASP HIS THR LEU PRO THR PRO GLU
SEQRES 28 B 352 ALA
SEQRES 1 F 16 ARG LYS SER ALA PRO ALA THR GLY GLY VAL M3L LYS PRO
SEQRES 2 F 16 HIS ARG TYR
SEQRES 1 G 16 ARG LYS SER ALA PRO ALA THR GLY GLY VAL M3L LYS PRO
SEQRES 2 G 16 HIS ARG TYR
MODRES 2Q8E M3L F 36 LYS N-TRIMETHYLLYSINE
MODRES 2Q8E M3L G 36 LYS N-TRIMETHYLLYSINE
HET M3L F 36 12
HET M3L G 36 12
HET NI A 501 1
HET ZN A 505 1
HET OGA A 503 10
HET NI B 502 1
HET ZN B 506 1
HET OGA B 504 10
HETNAM M3L N-TRIMETHYLLYSINE
HETNAM NI NICKEL (II) ION
HETNAM ZN ZINC ION
HETNAM OGA N-OXALYLGLYCINE
FORMUL 3 M3L 2(C9 H21 N2 O2 1+)
FORMUL 5 NI 2(NI 2+)
FORMUL 6 ZN 2(ZN 2+)
FORMUL 7 OGA 2(C4 H5 N O5)
FORMUL 11 HOH *290(H2 O)
HELIX 1 1 SER A 3 LEU A 8 1 6
HELIX 2 2 THR A 20 ASN A 26 1 7
HELIX 3 3 ASN A 26 GLN A 37 1 12
HELIX 4 4 GLY A 38 ALA A 42 5 5
HELIX 5 5 VAL A 94 SER A 103 1 10
HELIX 6 6 GLU A 113 LEU A 125 1 13
HELIX 7 7 THR A 155 LEU A 157 5 3
HELIX 8 8 ASP A 158 GLY A 165 1 8
HELIX 9 9 GLU A 190 LEU A 194 5 5
HELIX 10 10 PRO A 212 GLU A 214 5 3
HELIX 11 11 HIS A 215 PHE A 227 1 13
HELIX 12 12 PHE A 227 CYS A 234 1 8
HELIX 13 13 ALA A 236 LYS A 241 5 6
HELIX 14 14 SER A 246 TYR A 253 1 8
HELIX 15 15 ARG A 295 ALA A 303 1 9
HELIX 16 16 MET A 317 GLN A 325 1 9
HELIX 17 17 ARG A 328 ALA A 334 1 7
HELIX 18 18 ASN B 9 ARG B 13 5 5
HELIX 19 19 GLU B 22 ARG B 25 5 4
HELIX 20 20 ASN B 26 GLN B 37 1 12
HELIX 21 21 GLY B 38 ALA B 42 5 5
HELIX 22 22 VAL B 94 SER B 103 1 10
HELIX 23 23 GLU B 113 LEU B 125 1 13
HELIX 24 24 LEU B 157 GLY B 165 1 9
HELIX 25 25 GLU B 190 LEU B 194 5 5
HELIX 26 26 PRO B 212 GLU B 214 5 3
HELIX 27 27 HIS B 215 PHE B 227 1 13
HELIX 28 28 PHE B 227 CYS B 234 1 8
HELIX 29 29 ALA B 236 LYS B 241 5 6
HELIX 30 30 SER B 246 TYR B 253 1 8
HELIX 31 31 ARG B 295 ALA B 303 1 9
HELIX 32 32 MET B 317 GLN B 325 1 9
HELIX 33 33 GLN B 325 GLY B 335 1 11
SHEET 1 A10 MET A 15 PHE A 17 0
SHEET 2 A10 LEU A 44 VAL A 47 1 O LYS A 46 N PHE A 17
SHEET 3 A10 PHE A 267 THR A 270 -1 O PHE A 267 N VAL A 47
SHEET 4 A10 TYR A 195 GLY A 203 -1 N ASN A 198 O MET A 268
SHEET 5 A10 ASN A 284 PHE A 291 -1 O GLU A 287 N TYR A 199
SHEET 6 A10 TYR A 175 GLY A 179 -1 N TYR A 177 O ALA A 286
SHEET 7 A10 ILE A 131 ASN A 137 -1 N VAL A 136 O LEU A 176
SHEET 8 A10 ILE A 71 GLN A 78 -1 N ILE A 71 O TYR A 132
SHEET 9 A10 LEU A 81 GLN A 88 -1 O TYR A 85 N LEU A 74
SHEET 10 A10 THR A 243 ILE A 245 -1 O LEU A 244 N PHE A 82
SHEET 1 B 2 VAL A 66 ILE A 67 0
SHEET 2 B 2 MET A 92 THR A 93 -1 O MET A 92 N ILE A 67
SHEET 1 C 4 SER A 184 HIS A 188 0
SHEET 2 C 4 TYR A 275 ASN A 280 -1 O GLY A 278 N PHE A 185
SHEET 3 C 4 LYS A 206 VAL A 211 -1 N SER A 207 O PHE A 279
SHEET 4 C 4 ASP A 258 GLN A 262 -1 O GLN A 262 N LYS A 206
SHEET 1 D10 MET B 15 PHE B 17 0
SHEET 2 D10 LEU B 44 VAL B 47 1 O LYS B 46 N MET B 15
SHEET 3 D10 PHE B 267 THR B 270 -1 O PHE B 267 N VAL B 47
SHEET 4 D10 TYR B 195 GLY B 203 -1 N SER B 196 O THR B 270
SHEET 5 D10 ASN B 284 PHE B 291 -1 O GLU B 287 N TYR B 199
SHEET 6 D10 TYR B 175 GLY B 179 -1 N TYR B 175 O SER B 288
SHEET 7 D10 ILE B 131 ASN B 137 -1 N VAL B 136 O LEU B 176
SHEET 8 D10 ILE B 71 GLN B 78 -1 N ILE B 71 O TYR B 132
SHEET 9 D10 LEU B 81 GLN B 88 -1 O TYR B 85 N LEU B 74
SHEET 10 D10 THR B 243 ILE B 245 -1 O LEU B 244 N PHE B 82
SHEET 1 E 2 VAL B 66 ILE B 67 0
SHEET 2 E 2 MET B 92 THR B 93 -1 O MET B 92 N ILE B 67
SHEET 1 F 4 SER B 184 HIS B 188 0
SHEET 2 F 4 TYR B 275 ASN B 280 -1 O GLY B 278 N PHE B 185
SHEET 3 F 4 LYS B 206 VAL B 211 -1 N SER B 207 O PHE B 279
SHEET 4 F 4 ASP B 258 GLN B 262 -1 O GLN B 262 N LYS B 206
LINK C VAL F 35 N M3L F 36 1555 1555 1.34
LINK C VAL G 35 N M3L G 36 1555 1555 1.33
LINK C M3L G 36 N LYS G 37 1555 1555 1.33
LINK NE2 HIS A 188 NI NI A 501 1555 1555 2.14
LINK OE1 GLU A 190 NI NI A 501 1555 1555 2.13
LINK SG CYS A 234 ZN ZN A 505 1555 1555 2.10
LINK NE2 HIS A 240 ZN ZN A 505 1555 1555 2.06
LINK NE2 HIS A 276 NI NI A 501 1555 1555 1.92
LINK SG CYS A 306 ZN ZN A 505 1555 1555 1.74
LINK SG CYS A 308 ZN ZN A 505 1555 1555 2.34
LINK NI NI A 501 O2' OGA A 503 1555 1555 2.31
LINK NI NI A 501 O2 OGA A 503 1555 1555 1.98
LINK NI NI A 501 O HOH A 563 1555 1555 1.47
LINK NE2 HIS B 188 NI NI B 502 1555 1555 2.08
LINK OE1 GLU B 190 NI NI B 502 1555 1555 2.20
LINK SG CYS B 234 ZN ZN B 506 1555 1555 2.13
LINK NE2 HIS B 240 ZN ZN B 506 1555 1555 2.03
LINK NE2 HIS B 276 NI NI B 502 1555 1555 2.11
LINK SG CYS B 306 ZN ZN B 506 1555 1555 1.59
LINK SG CYS B 308 ZN ZN B 506 1555 1555 2.27
LINK NI NI B 502 O2 OGA B 504 1555 1555 1.82
LINK NI NI B 502 O2' OGA B 504 1555 1555 2.33
CISPEP 1 PRO G 38 HIS G 39 0 24.50
SITE 1 AC1 5 HIS A 188 GLU A 190 HIS A 276 OGA A 503
SITE 2 AC1 5 HOH A 563
SITE 1 AC2 4 HIS B 188 GLU B 190 HIS B 276 OGA B 504
SITE 1 AC3 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC4 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC5 12 TYR A 132 PHE A 185 HIS A 188 GLU A 190
SITE 2 AC5 12 SER A 196 ASN A 198 LYS A 206 HIS A 276
SITE 3 AC5 12 SER A 288 NI A 501 HOH A 563 M3L F 36
SITE 1 AC6 13 TYR B 132 TYR B 177 PHE B 185 HIS B 188
SITE 2 AC6 13 GLU B 190 SER B 196 ASN B 198 LYS B 206
SITE 3 AC6 13 TRP B 208 HIS B 276 SER B 288 NI B 502
SITE 4 AC6 13 HOH B 583
CRYST1 100.294 148.964 56.810 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009971 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006713 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017602 0.00000
(ATOM LINES ARE NOT SHOWN.)
END