HEADER OXIDOREDUCTASE 12-APR-13 4BIS
TITLE JMJD2A COMPLEXED WITH 8-HYDROXYQUINOLINE-4-CARBOXYLIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A,
COMPND 5 JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
COMPND 6 EC: 1.14.11.-;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PNIC28 BSA4
KEYWDS OXIDOREDUCTASE, NON-HEME, 2-OXOGLUTARATE, DIOXYGENASE, OXYGENASE,
KEYWDS 2 FACIAL TRIAD, METAL BINDING PROTEIN, EPIGENETIC AND TRANSCRIPTION
KEYWDS 3 REGULATION, CHROMATIN REGULATOR, HYDROXYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR R.CHOWDHURY,C.THINNES,C.J.SCHOFIELD
REVDAT 5 20-DEC-23 4BIS 1 REMARK LINK
REVDAT 4 08-MAY-19 4BIS 1 REMARK
REVDAT 3 06-MAR-19 4BIS 1 REMARK
REVDAT 2 28-MAR-18 4BIS 1 JRNL
REVDAT 1 05-FEB-14 4BIS 0
JRNL AUTH R.J.HOPKINSON,A.TUMBER,C.YAPP,R.CHOWDHURY,W.AIK,K.H.CHE,
JRNL AUTH 2 X.S.LI,J.B.L.KRISTENSEN,O.N.F.KING,M.C.CHAN,K.K.YEOH,H.CHOI,
JRNL AUTH 3 L.J.WALPORT,C.C.THINNES,J.T.BUSH,C.LEJEUNE,A.M.RYDZIK,
JRNL AUTH 4 N.R.ROSE,E.A.BAGG,M.A.MCDONOUGH,T.KROJER,W.W.YUE,S.S.NG,
JRNL AUTH 5 L.OLSEN,P.E.BRENNAN,U.OPPERMANN,S.MULLER-KNAPP,R.J.KLOSE,
JRNL AUTH 6 P.J.RATCLIFFE,C.J.SCHOFIELD,A.KAWAMURA
JRNL TITL 5-CARBOXY-8-HYDROXYQUINOLINE IS A BROAD SPECTRUM
JRNL TITL 2 2-OXOGLUTARATE OXYGENASE INHIBITOR WHICH CAUSES IRON
JRNL TITL 3 TRANSLOCATION.
JRNL REF CHEM SCI V. 4 3110 2013
JRNL REFN ISSN 2041-6520
JRNL PMID 26682036
JRNL DOI 10.1039/C3SC51122G
REMARK 2
REMARK 2 RESOLUTION. 2.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 60.19
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 31126
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.194
REMARK 3 R VALUE (WORKING SET) : 0.193
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1568
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 60.2042 - 5.5438 0.99 2860 143 0.1755 0.1928
REMARK 3 2 5.5438 - 4.4007 1.00 2721 153 0.1422 0.1685
REMARK 3 3 4.4007 - 3.8445 1.00 2688 156 0.1545 0.1879
REMARK 3 4 3.8445 - 3.4931 1.00 2688 149 0.1901 0.2349
REMARK 3 5 3.4931 - 3.2427 1.00 2691 128 0.2043 0.2508
REMARK 3 6 3.2427 - 3.0515 1.00 2655 141 0.2173 0.2299
REMARK 3 7 3.0515 - 2.8987 1.00 2627 163 0.2403 0.2904
REMARK 3 8 2.8987 - 2.7725 0.99 2643 148 0.2442 0.2960
REMARK 3 9 2.7725 - 2.6658 1.00 2669 130 0.2450 0.2697
REMARK 3 10 2.6658 - 2.5738 1.00 2630 125 0.2676 0.3068
REMARK 3 11 2.5738 - 2.4933 1.00 2635 132 0.2788 0.3125
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 36.62
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.920
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.85000
REMARK 3 B22 (A**2) : 1.18000
REMARK 3 B33 (A**2) : 0.66000
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 5816
REMARK 3 ANGLE : 1.260 7901
REMARK 3 CHIRALITY : 0.056 815
REMARK 3 PLANARITY : 0.004 1010
REMARK 3 DIHEDRAL : 15.222 2085
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4BIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-APR-13.
REMARK 100 THE DEPOSITION ID IS D_1290056481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91630
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31126
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.490
REMARK 200 RESOLUTION RANGE LOW (A) : 60.190
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.79000
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: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2OX0
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PROPANE PH 7.5, 0.02M
REMARK 280 NA/K PHOSPHATE, 20% W/V PEG 3350, SITTING DROP, 277K, VAPOR
REMARK 280 DIFFUSION, SITTING DROP
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 50.34500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 75.07500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.34500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 75.07500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 MET A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 SER A -14
REMARK 465 SER A -13
REMARK 465 GLY A -12
REMARK 465 VAL A -11
REMARK 465 ASP A -10
REMARK 465 LEU A -9
REMARK 465 GLY A -8
REMARK 465 THR A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 PHE A -2
REMARK 465 GLN A -1
REMARK 465 SER A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 SER A 3
REMARK 465 GLU A 4
REMARK 465 SER A 5
REMARK 465 GLU A 6
REMARK 465 THR A 7
REMARK 465 GLU A 356
REMARK 465 SER A 357
REMARK 465 GLU A 358
REMARK 465 LEU A 359
REMARK 465 MET B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 SER B -14
REMARK 465 SER B -13
REMARK 465 GLY B -12
REMARK 465 VAL B -11
REMARK 465 ASP B -10
REMARK 465 LEU B -9
REMARK 465 GLY B -8
REMARK 465 THR B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLN 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 GLU B 356
REMARK 465 SER B 357
REMARK 465 GLU B 358
REMARK 465 LEU B 359
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 8 CG CD1 CD2
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 ARG A 95 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 ARG A 110 CD NE CZ NH1 NH2
REMARK 470 GLU A 113 CD OE1 OE2
REMARK 470 GLU A 115 CD OE1 OE2
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 ARG A 154 NE CZ NH1 NH2
REMARK 470 LYS A 162 CG CD CE NZ
REMARK 470 ARG A 221 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 224 CD CE NZ
REMARK 470 GLN A 232 CG CD OE1 NE2
REMARK 470 LYS A 252 CE NZ
REMARK 470 ARG A 294 CZ NH1 NH2
REMARK 470 LYS A 310 CD CE NZ
REMARK 470 MET A 312 CG SD CE
REMARK 470 LYS A 330 CD CE NZ
REMARK 470 LYS A 336 CE NZ
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 LYS B 54 CG CD CE NZ
REMARK 470 LYS B 99 CG CD CE NZ
REMARK 470 ARG B 110 CD NE CZ NH1 NH2
REMARK 470 GLU B 113 CD OE1 OE2
REMARK 470 GLU B 115 CD OE1 OE2
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 ARG B 154 NE CZ NH1 NH2
REMARK 470 LYS B 162 CG CD CE NZ
REMARK 470 LYS B 224 CD CE NZ
REMARK 470 GLN B 232 CG CD OE1 NE2
REMARK 470 LYS B 252 CE NZ
REMARK 470 ARG B 294 CZ NH1 NH2
REMARK 470 LYS B 310 CD CE NZ
REMARK 470 ASP B 311 CG OD1 OD2
REMARK 470 LYS B 336 CE NZ
REMARK 470 LYS B 355 CG CD CE NZ
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 103 173.69 -54.58
REMARK 500 SER A 112 -85.80 -107.02
REMARK 500 LYS A 143 -14.31 -42.27
REMARK 500 MET A 192 15.83 59.66
REMARK 500 ALA A 236 56.79 -156.52
REMARK 500 ASN A 338 37.52 -96.50
REMARK 500 ASN B 9 62.09 62.99
REMARK 500 TYR B 59 50.36 -110.68
REMARK 500 ALA B 91 152.53 -48.88
REMARK 500 SER B 112 -62.67 -102.13
REMARK 500 ILE B 150 -7.41 -58.27
REMARK 500 ARG B 152 73.22 -156.76
REMARK 500 ARG B 154 39.08 72.04
REMARK 500 ILE B 156 1.26 -61.79
REMARK 500 PHE B 227 64.93 -117.08
REMARK 500 ALA B 236 56.17 -104.35
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 OE2 104.7
REMARK 620 3 HIS A 276 NE2 93.8 81.7
REMARK 620 4 8HQ A 601 NAI 103.8 148.5 109.5
REMARK 620 5 8HQ A 601 OAC 77.2 99.4 171.0 74.2
REMARK 620 6 HOH A2077 O 161.9 71.6 102.9 77.2 85.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 116.4
REMARK 620 3 CYS A 306 SG 114.6 111.3
REMARK 620 4 CYS A 308 SG 105.1 93.5 113.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI B 501 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 188 NE2
REMARK 620 2 GLU B 190 OE2 99.6
REMARK 620 3 HIS B 276 NE2 89.9 79.4
REMARK 620 4 8HQ B 601 NAI 114.7 144.3 109.0
REMARK 620 5 8HQ B 601 OAC 83.2 102.2 173.1 73.7
REMARK 620 6 HOH B2085 O 163.1 75.9 73.3 73.8 113.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 HIS B 240 NE2 102.0
REMARK 620 3 CYS B 306 SG 118.1 115.3
REMARK 620 4 CYS B 308 SG 109.0 84.8 121.4
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 ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8HQ A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8HQ B 601
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NJY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJD2A COMPLEXED WITH 5-CARBOXY- 8-
REMARK 900 HYDROXYQUINOLINE
REMARK 900 RELATED ID: 4BIO RELATED DB: PDB
REMARK 900 FACTOR INHIBITING HIF-1 ALPHA IN COMPLEX WITH 8- HYDROXYQUINOLINE-5-
REMARK 900 CARBOXYLIC ACID
DBREF 4BIS A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 4BIS B 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 4BIS MET A -21 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS A -20 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS A -19 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS A -18 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS A -17 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS A -16 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS A -15 UNP O75164 EXPRESSION TAG
SEQADV 4BIS SER A -14 UNP O75164 EXPRESSION TAG
SEQADV 4BIS SER A -13 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLY A -12 UNP O75164 EXPRESSION TAG
SEQADV 4BIS VAL A -11 UNP O75164 EXPRESSION TAG
SEQADV 4BIS ASP A -10 UNP O75164 EXPRESSION TAG
SEQADV 4BIS LEU A -9 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLY A -8 UNP O75164 EXPRESSION TAG
SEQADV 4BIS THR A -7 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLU A -6 UNP O75164 EXPRESSION TAG
SEQADV 4BIS ASN A -5 UNP O75164 EXPRESSION TAG
SEQADV 4BIS LEU A -4 UNP O75164 EXPRESSION TAG
SEQADV 4BIS TYR A -3 UNP O75164 EXPRESSION TAG
SEQADV 4BIS PHE A -2 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLN A -1 UNP O75164 EXPRESSION TAG
SEQADV 4BIS SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 4BIS MET B -21 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS B -20 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS B -19 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS B -18 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS B -17 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS B -16 UNP O75164 EXPRESSION TAG
SEQADV 4BIS HIS B -15 UNP O75164 EXPRESSION TAG
SEQADV 4BIS SER B -14 UNP O75164 EXPRESSION TAG
SEQADV 4BIS SER B -13 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLY B -12 UNP O75164 EXPRESSION TAG
SEQADV 4BIS VAL B -11 UNP O75164 EXPRESSION TAG
SEQADV 4BIS ASP B -10 UNP O75164 EXPRESSION TAG
SEQADV 4BIS LEU B -9 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLY B -8 UNP O75164 EXPRESSION TAG
SEQADV 4BIS THR B -7 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLU B -6 UNP O75164 EXPRESSION TAG
SEQADV 4BIS ASN B -5 UNP O75164 EXPRESSION TAG
SEQADV 4BIS LEU B -4 UNP O75164 EXPRESSION TAG
SEQADV 4BIS TYR B -3 UNP O75164 EXPRESSION TAG
SEQADV 4BIS PHE B -2 UNP O75164 EXPRESSION TAG
SEQADV 4BIS GLN B -1 UNP O75164 EXPRESSION TAG
SEQADV 4BIS SER B 0 UNP O75164 EXPRESSION TAG
SEQRES 1 A 381 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 381 GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER GLU
SEQRES 3 A 381 SER GLU THR LEU ASN PRO SER ALA ARG ILE MET THR PHE
SEQRES 4 A 381 TYR PRO THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR
SEQRES 5 A 381 ILE ALA TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY
SEQRES 6 A 381 LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG
SEQRES 7 A 381 ALA SER TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA
SEQRES 8 A 381 PRO ILE GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE
SEQRES 9 A 381 THR GLN TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG
SEQRES 10 A 381 GLU PHE ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR
SEQRES 11 A 381 PRO ARG TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR
SEQRES 12 A 381 TRP LYS ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA
SEQRES 13 A 381 ASP VAL ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU
SEQRES 14 A 381 TRP ASN ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL
SEQRES 15 A 381 GLU LYS GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR
SEQRES 16 A 381 PRO TYR LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA
SEQRES 17 A 381 TRP HIS THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR
SEQRES 18 A 381 LEU HIS PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO
SEQRES 19 A 381 PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY
SEQRES 20 A 381 PHE PHE PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU
SEQRES 21 A 381 ARG HIS LYS MET THR LEU ILE SER PRO LEU MET LEU LYS
SEQRES 22 A 381 LYS TYR GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA
SEQRES 23 A 381 GLY GLU PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA
SEQRES 24 A 381 GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN
SEQRES 25 A 381 PHE ALA THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA
SEQRES 26 A 381 VAL LEU CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER
SEQRES 27 A 381 MET ASP VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR
SEQRES 28 A 381 LYS LEU TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP
SEQRES 29 A 381 HIS THR LEU PRO THR PRO GLU ALA ALA GLU PHE LEU LYS
SEQRES 30 A 381 GLU SER GLU LEU
SEQRES 1 B 381 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 381 GLY THR GLU ASN LEU TYR PHE GLN SER MET ALA SER GLU
SEQRES 3 B 381 SER GLU THR LEU ASN PRO SER ALA ARG ILE MET THR PHE
SEQRES 4 B 381 TYR PRO THR MET GLU GLU PHE ARG ASN PHE SER ARG TYR
SEQRES 5 B 381 ILE ALA TYR ILE GLU SER GLN GLY ALA HIS ARG ALA GLY
SEQRES 6 B 381 LEU ALA LYS VAL VAL PRO PRO LYS GLU TRP LYS PRO ARG
SEQRES 7 B 381 ALA SER TYR ASP ASP ILE ASP ASP LEU VAL ILE PRO ALA
SEQRES 8 B 381 PRO ILE GLN GLN LEU VAL THR GLY GLN SER GLY LEU PHE
SEQRES 9 B 381 THR GLN TYR ASN ILE GLN LYS LYS ALA MET THR VAL ARG
SEQRES 10 B 381 GLU PHE ARG LYS ILE ALA ASN SER ASP LYS TYR CYS THR
SEQRES 11 B 381 PRO ARG TYR SER GLU PHE GLU GLU LEU GLU ARG LYS TYR
SEQRES 12 B 381 TRP LYS ASN LEU THR PHE ASN PRO PRO ILE TYR GLY ALA
SEQRES 13 B 381 ASP VAL ASN GLY THR LEU TYR GLU LYS HIS VAL ASP GLU
SEQRES 14 B 381 TRP ASN ILE GLY ARG LEU ARG THR ILE LEU ASP LEU VAL
SEQRES 15 B 381 GLU LYS GLU SER GLY ILE THR ILE GLU GLY VAL ASN THR
SEQRES 16 B 381 PRO TYR LEU TYR PHE GLY MET TRP LYS THR SER PHE ALA
SEQRES 17 B 381 TRP HIS THR GLU ASP MET ASP LEU TYR SER ILE ASN TYR
SEQRES 18 B 381 LEU HIS PHE GLY GLU PRO LYS SER TRP TYR SER VAL PRO
SEQRES 19 B 381 PRO GLU HIS GLY LYS ARG LEU GLU ARG LEU ALA LYS GLY
SEQRES 20 B 381 PHE PHE PRO GLY SER ALA GLN SER CYS GLU ALA PHE LEU
SEQRES 21 B 381 ARG HIS LYS MET THR LEU ILE SER PRO LEU MET LEU LYS
SEQRES 22 B 381 LYS TYR GLY ILE PRO PHE ASP LYS VAL THR GLN GLU ALA
SEQRES 23 B 381 GLY GLU PHE MET ILE THR PHE PRO TYR GLY TYR HIS ALA
SEQRES 24 B 381 GLY PHE ASN HIS GLY PHE ASN CYS ALA GLU SER THR ASN
SEQRES 25 B 381 PHE ALA THR ARG ARG TRP ILE GLU TYR GLY LYS GLN ALA
SEQRES 26 B 381 VAL LEU CYS SER CYS ARG LYS ASP MET VAL LYS ILE SER
SEQRES 27 B 381 MET ASP VAL PHE VAL ARG LYS PHE GLN PRO GLU ARG TYR
SEQRES 28 B 381 LYS LEU TRP LYS ALA GLY LYS ASP ASN THR VAL ILE ASP
SEQRES 29 B 381 HIS THR LEU PRO THR PRO GLU ALA ALA GLU PHE LEU LYS
SEQRES 30 B 381 GLU SER GLU LEU
HET NI A 501 1
HET ZN A 502 1
HET CL A 503 1
HET 8HQ A 601 14
HET GOL A 701 6
HET NI B 501 1
HET ZN B 502 1
HET CL B 503 1
HET 8HQ B 601 14
HETNAM NI NICKEL (II) ION
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM 8HQ 8-HYDROXYQUINOLINE-4-CARBOXYLIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 NI 2(NI 2+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 5 CL 2(CL 1-)
FORMUL 6 8HQ 2(C10 H7 N O3)
FORMUL 7 GOL C3 H8 O3
FORMUL 12 HOH *263(H2 O)
HELIX 1 1 THR A 20 ARG A 25 1 6
HELIX 2 2 ASN A 26 GLN A 37 1 12
HELIX 3 3 GLY A 38 ALA A 42 5 5
HELIX 4 4 ASP A 61 ASP A 64 5 4
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 GLN A 325 ALA A 334 1 10
HELIX 18 18 THR A 347 LYS A 355 5 9
HELIX 19 19 THR B 20 ARG B 25 1 6
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 ASN B 102 1 9
HELIX 23 23 GLU B 113 LEU B 125 1 13
HELIX 24 24 THR B 155 LEU B 157 5 3
HELIX 25 25 ASP B 158 GLU B 163 1 6
HELIX 26 26 GLU B 190 LEU B 194 5 5
HELIX 27 27 PRO B 212 GLU B 214 5 3
HELIX 28 28 HIS B 215 PHE B 227 1 13
HELIX 29 29 PHE B 227 CYS B 234 1 8
HELIX 30 30 ALA B 236 LYS B 241 5 6
HELIX 31 31 SER B 246 TYR B 253 1 8
HELIX 32 32 ARG B 295 ALA B 303 1 9
HELIX 33 33 MET B 317 GLN B 325 1 9
HELIX 34 34 GLN B 325 GLY B 335 1 11
HELIX 35 35 THR B 347 GLU B 349 5 3
HELIX 36 36 ALA B 350 LYS B 355 1 6
SHEET 1 AA10 MET A 15 PHE A 17 0
SHEET 2 AA10 LEU A 44 VAL A 47 1 O LEU A 44 N MET A 15
SHEET 3 AA10 PHE A 267 THR A 270 -1 O PHE A 267 N VAL A 47
SHEET 4 AA10 TYR A 195 GLY A 203 -1 O SER A 196 N THR A 270
SHEET 5 AA10 ASN A 284 PHE A 291 -1 O CYS A 285 N HIS A 201
SHEET 6 AA10 TYR A 175 GLY A 179 -1 O TYR A 175 N SER A 288
SHEET 7 AA10 ILE A 131 ASN A 137 -1 O GLY A 133 N PHE A 178
SHEET 8 AA10 ILE A 71 GLN A 78 -1 O ILE A 71 N TYR A 132
SHEET 9 AA10 LEU A 81 GLN A 88 -1 O LEU A 81 N GLN A 78
SHEET 10 AA10 THR A 243 ILE A 245 -1 O LEU A 244 N PHE A 82
SHEET 1 AB 2 VAL A 66 ILE A 67 0
SHEET 2 AB 2 MET A 92 THR A 93 -1 O MET A 92 N ILE A 67
SHEET 1 AC 4 SER A 184 HIS A 188 0
SHEET 2 AC 4 TYR A 275 ASN A 280 -1 O HIS A 276 N HIS A 188
SHEET 3 AC 4 LYS A 206 VAL A 211 -1 O SER A 207 N PHE A 279
SHEET 4 AC 4 ASP A 258 GLN A 262 -1 O ASP A 258 N SER A 210
SHEET 1 BA10 MET B 15 PHE B 17 0
SHEET 2 BA10 LEU B 44 VAL B 47 1 O LEU B 44 N MET B 15
SHEET 3 BA10 PHE B 267 THR B 270 -1 O PHE B 267 N VAL B 47
SHEET 4 BA10 TYR B 195 GLY B 203 -1 O SER B 196 N THR B 270
SHEET 5 BA10 ASN B 284 PHE B 291 -1 O CYS B 285 N HIS B 201
SHEET 6 BA10 TYR B 175 GLY B 179 -1 O TYR B 175 N SER B 288
SHEET 7 BA10 ILE B 131 ASN B 137 -1 O GLY B 133 N PHE B 178
SHEET 8 BA10 ILE B 71 GLN B 78 -1 O ILE B 71 N TYR B 132
SHEET 9 BA10 LEU B 81 GLN B 88 -1 O LEU B 81 N GLN B 78
SHEET 10 BA10 THR B 243 ILE B 245 -1 O LEU B 244 N PHE B 82
SHEET 1 BB 2 VAL B 66 ILE B 67 0
SHEET 2 BB 2 MET B 92 THR B 93 -1 O MET B 92 N ILE B 67
SHEET 1 BC 4 SER B 184 HIS B 188 0
SHEET 2 BC 4 TYR B 275 ASN B 280 -1 O HIS B 276 N HIS B 188
SHEET 3 BC 4 LYS B 206 VAL B 211 -1 O SER B 207 N PHE B 279
SHEET 4 BC 4 ASP B 258 GLN B 262 -1 O ASP B 258 N SER B 210
LINK NE2 HIS A 188 NI NI A 501 1555 1555 2.29
LINK OE2 GLU A 190 NI NI A 501 1555 1555 2.09
LINK SG CYS A 234 ZN ZN A 502 1555 1555 2.34
LINK NE2 HIS A 240 ZN ZN A 502 1555 1555 2.22
LINK NE2 HIS A 276 NI NI A 501 1555 1555 2.23
LINK SG CYS A 306 ZN ZN A 502 1555 1555 2.25
LINK SG CYS A 308 ZN ZN A 502 1555 1555 2.41
LINK NI NI A 501 NAI 8HQ A 601 1555 1555 2.31
LINK NI NI A 501 OAC 8HQ A 601 1555 1555 2.11
LINK NI NI A 501 O HOH A2077 1555 1555 2.04
LINK NE2 HIS B 188 NI NI B 501 1555 1555 2.21
LINK OE2 GLU B 190 NI NI B 501 1555 1555 2.19
LINK SG CYS B 234 ZN ZN B 502 1555 1555 2.35
LINK NE2 HIS B 240 ZN ZN B 502 1555 1555 2.30
LINK NE2 HIS B 276 NI NI B 501 1555 1555 2.33
LINK SG CYS B 306 ZN ZN B 502 1555 1555 2.36
LINK SG CYS B 308 ZN ZN B 502 1555 1555 2.35
LINK NI NI B 501 NAI 8HQ B 601 1555 1555 2.29
LINK NI NI B 501 OAC 8HQ B 601 1555 1555 2.16
LINK NI NI B 501 O HOH B2085 1555 1555 2.18
SITE 1 AC1 5 HIS A 188 GLU A 190 HIS A 276 8HQ A 601
SITE 2 AC1 5 HOH A2077
SITE 1 AC2 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC3 3 PHE A 227 GLY A 229 SER A 230
SITE 1 AC4 11 TYR A 132 TYR A 177 PHE A 185 HIS A 188
SITE 2 AC4 11 GLU A 190 LYS A 206 TRP A 208 LYS A 241
SITE 3 AC4 11 NI A 501 HOH A2075 HOH A2077
SITE 1 AC5 1 ARG A 98
SITE 1 AC6 5 HIS B 188 GLU B 190 HIS B 276 8HQ B 601
SITE 2 AC6 5 HOH B2085
SITE 1 AC7 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC8 3 PHE B 227 GLY B 229 SER B 230
SITE 1 AC9 10 TYR B 132 TYR B 177 HIS B 188 GLU B 190
SITE 2 AC9 10 LYS B 206 TRP B 208 LYS B 241 NI B 501
SITE 3 AC9 10 HOH B2085 HOH B2089
CRYST1 100.690 150.150 57.450 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 0.009931 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006660 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017406 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
