HEADER OXIDOREDUCTASE 07-FEB-17 5PH0
TITLE PANDDA ANALYSIS GROUP DEPOSITION -- CRYSTAL STRUCTURE OF JMJD2D IN
TITLE 2 COMPLEX WITH N09484A
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4D;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3D,
COMPND 5 JUMONJI DOMAIN-CONTAINING PROTEIN 2D;
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 GENE: KDM4D, JHDM3D, JMJD2D;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PANDDA, SGC - DIAMOND I04-1 FRAGMENT SCREENING, JMJ DOMAIN,
KEYWDS 2 EPIGENETICS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.M.PEARCE,T.KROJER,R.TALON,A.R.BRADLEY,M.FAIRHEAD,R.SETHI,N.WRIGHT,
AUTHOR 2 E.MACLEAN,P.COLLINS,J.BRANDAO-NETO,A.DOUANGAMATH,Z.RENJIE,A.DIAS,
AUTHOR 3 M.VOLLMAR,J.NG,A.SZYKOWSKA,N.BURGESS-BROWN,P.E.BRENNAN,O.COX,
AUTHOR 4 U.OPPERMANN,C.BOUNTRA,C.H.ARROWSMITH,A.EDWARDS,F.VON DELFT
REVDAT 4 06-MAR-24 5PH0 1 LINK
REVDAT 3 04-OCT-17 5PH0 1 REMARK
REVDAT 2 27-SEP-17 5PH0 1 JRNL REMARK
REVDAT 1 15-MAR-17 5PH0 0
JRNL AUTH N.M.PEARCE,T.KROJER,A.R.BRADLEY,P.COLLINS,R.P.NOWAK,R.TALON,
JRNL AUTH 2 B.D.MARSDEN,S.KELM,J.SHI,C.M.DEANE,F.VON DELFT
JRNL TITL A MULTI-CRYSTAL METHOD FOR EXTRACTING OBSCURED
JRNL TITL 2 CRYSTALLOGRAPHIC STATES FROM CONVENTIONALLY UNINTERPRETABLE
JRNL TITL 3 ELECTRON DENSITY.
JRNL REF NAT COMMUN V. 8 15123 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 28436492
JRNL DOI 10.1038/NCOMMS15123
REMARK 2
REMARK 2 RESOLUTION. 1.34 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1682
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) : 1.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.41
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 87409
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.130
REMARK 3 R VALUE (WORKING SET) : 0.128
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.920
REMARK 3 FREE R VALUE TEST SET COUNT : 4300
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 29.4176 - 4.1624 1.00 3090 142 0.1510 0.1676
REMARK 3 2 4.1624 - 3.3052 1.00 2913 144 0.1275 0.1508
REMARK 3 3 3.3052 - 2.8878 1.00 2838 158 0.1329 0.1876
REMARK 3 4 2.8878 - 2.6240 1.00 2837 152 0.1416 0.1724
REMARK 3 5 2.6240 - 2.4360 1.00 2836 143 0.1322 0.1812
REMARK 3 6 2.4360 - 2.2924 1.00 2796 147 0.1318 0.1695
REMARK 3 7 2.2924 - 2.1777 1.00 2824 124 0.1265 0.1574
REMARK 3 8 2.1777 - 2.0829 1.00 2821 126 0.1200 0.1592
REMARK 3 9 2.0829 - 2.0027 1.00 2797 132 0.1141 0.1505
REMARK 3 10 2.0027 - 1.9336 1.00 2751 159 0.1166 0.1504
REMARK 3 11 1.9336 - 1.8732 1.00 2776 153 0.1115 0.1396
REMARK 3 12 1.8732 - 1.8197 1.00 2773 144 0.1104 0.1437
REMARK 3 13 1.8197 - 1.7718 1.00 2764 153 0.1096 0.1444
REMARK 3 14 1.7718 - 1.7285 1.00 2772 143 0.1068 0.1340
REMARK 3 15 1.7285 - 1.6892 1.00 2746 145 0.1050 0.1250
REMARK 3 16 1.6892 - 1.6533 1.00 2777 137 0.1075 0.1567
REMARK 3 17 1.6533 - 1.6202 1.00 2765 132 0.1066 0.1494
REMARK 3 18 1.6202 - 1.5897 1.00 2727 155 0.1015 0.1529
REMARK 3 19 1.5897 - 1.5613 1.00 2785 133 0.1093 0.1503
REMARK 3 20 1.5613 - 1.5348 1.00 2744 133 0.1087 0.1436
REMARK 3 21 1.5348 - 1.5100 1.00 2754 159 0.1112 0.1484
REMARK 3 22 1.5100 - 1.4868 1.00 2733 138 0.1157 0.1523
REMARK 3 23 1.4868 - 1.4649 1.00 2755 156 0.1213 0.1833
REMARK 3 24 1.4649 - 1.4443 1.00 2719 145 0.1263 0.1519
REMARK 3 25 1.4443 - 1.4248 1.00 2740 147 0.1335 0.1628
REMARK 3 26 1.4248 - 1.4063 1.00 2735 151 0.1463 0.2041
REMARK 3 27 1.4063 - 1.3887 1.00 2727 164 0.1585 0.2023
REMARK 3 28 1.3887 - 1.3720 0.99 2714 126 0.1729 0.2117
REMARK 3 29 1.3720 - 1.3560 0.97 2647 141 0.1750 0.2266
REMARK 3 30 1.3560 - 1.3408 0.89 2453 118 0.1887 0.1958
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.090
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 13.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.88
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 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 : 0.006 3123
REMARK 3 ANGLE : 1.092 4275
REMARK 3 CHIRALITY : 0.049 422
REMARK 3 PLANARITY : 0.006 567
REMARK 3 DIHEDRAL : 12.715 1199
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 5PH0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1001400648.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-12
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 : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97630
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : AIMLESS 0.1.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 87517
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.340
REMARK 200 RESOLUTION RANGE LOW (A) : 29.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.09700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.36
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 0.67400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: 4D6R
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG3350 -- 0.1M HEPES PH 7.0 --
REMARK 280 0.25M AMMONIUM SULFATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.13200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 35.73350
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 35.73350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 112.69800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 35.73350
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 35.73350
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 37.56600
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 35.73350
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 35.73350
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 112.69800
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 35.73350
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 35.73350
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 37.56600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.13200
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: MONOMERIC
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 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 832 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 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 GLU A 2
REMARK 465 THR A 3
REMARK 465 MET A 4
REMARK 465 LYS A 5
REMARK 465 SER A 6
REMARK 465 LYS A 7
REMARK 465 ALA A 8
REMARK 465 ASN A 9
REMARK 465 CYS A 10
REMARK 465 ARG A 342
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 61 CG CD OE1 OE2
REMARK 470 LYS A 92 NZ
REMARK 470 ARG A 225 NE CZ NH1 NH2
REMARK 470 LYS A 255 CD CE NZ
REMARK 470 ARG A 316 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 338 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 341 CG OD1 OD2
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 569 O HOH A 851 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 LYS A 186 -5.33 75.26
REMARK 500 MET A 196 19.46 58.59
REMARK 500 ARG A 316 94.87 46.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 954 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH A 955 DISTANCE = 6.56 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 <JMJD2DA-X336> <USED_FOR_STATISTICAL_MAP>YES</USED_FOR_STATISTICAL_
REMARK 600 MAP> <SMILES_OF_COMPOUND_ADDED>C1CC2C(CC1N)NC(C(F)(F)F)[NH]2</
REMARK 600 SMILES_OF_COMPOUND_ADDED> <SITE12> <LABEL>NONE</LABEL> <COORDINATE>-
REMARK 600 10.78 -7.18 -7.18</COORDINATE> <SMILES>C1CC2C(CC1N)NC(C(F)(F)F)[NH]
REMARK 600 2</SMILES> <CONFIDENCE>4 - HIGH CONFIDENCE</CONFIDENCE> <COMMENT>
REMARK 600 NONE</COMMENT> <OCCUPANCY>0.22</OCCUPANCY> <B_AVERAGE>16.785</B_
REMARK 600 AVERAGE> <B_RATIO>1.2954969316716323</B_RATIO> <RSCC>0.875</RSCC> <
REMARK 600 RSR>0.157</RSR> <RSZD>1.8</RSZD> <RMSD>0.1456880228433346</RMSD> </
REMARK 600 SITE12> </JMJD2DA-X336>
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 MG A 403 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 65 O
REMARK 620 2 VAL A 171 O 101.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NI A 402 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 192 NE2
REMARK 620 2 GLU A 194 OE1 98.7
REMARK 620 3 HIS A 280 NE2 85.8 90.0
REMARK 620 4 OGA A 404 O1 168.2 93.0 95.3
REMARK 620 5 OGA A 404 O2' 91.0 169.3 95.2 77.2
REMARK 620 6 HOH A 598 O 90.3 87.1 174.7 89.2 88.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 238 SG
REMARK 620 2 HIS A 244 NE2 108.4
REMARK 620 3 CYS A 310 SG 116.9 110.3
REMARK 620 4 CYS A 312 SG 114.2 98.8 106.6
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 ZN A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OGA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 71N A 417
DBREF 5PH0 A 1 342 UNP Q6B0I6 KDM4D_HUMAN 1 342
SEQADV 5PH0 MET A -21 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 HIS A -20 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 HIS A -19 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 HIS A -18 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 HIS A -17 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 HIS A -16 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 HIS A -15 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 SER A -14 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 SER A -13 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 GLY A -12 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 VAL A -11 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 ASP A -10 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 LEU A -9 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 GLY A -8 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 THR A -7 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 GLU A -6 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 ASN A -5 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 LEU A -4 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 TYR A -3 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 PHE A -2 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 GLN A -1 UNP Q6B0I6 EXPRESSION TAG
SEQADV 5PH0 SER A 0 UNP Q6B0I6 EXPRESSION TAG
SEQRES 1 A 364 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 364 GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU THR MET
SEQRES 3 A 364 LYS SER LYS ALA ASN CYS ALA GLN ASN PRO ASN CYS ASN
SEQRES 4 A 364 ILE MET ILE PHE HIS PRO THR LYS GLU GLU PHE ASN ASP
SEQRES 5 A 364 PHE ASP LYS TYR ILE ALA TYR MET GLU SER GLN GLY ALA
SEQRES 6 A 364 HIS ARG ALA GLY LEU ALA LYS ILE ILE PRO PRO LYS GLU
SEQRES 7 A 364 TRP LYS ALA ARG GLU THR TYR ASP ASN ILE SER GLU ILE
SEQRES 8 A 364 LEU ILE ALA THR PRO LEU GLN GLN VAL ALA SER GLY ARG
SEQRES 9 A 364 ALA GLY VAL PHE THR GLN TYR HIS LYS LYS LYS LYS ALA
SEQRES 10 A 364 MET THR VAL GLY GLU TYR ARG HIS LEU ALA ASN SER LYS
SEQRES 11 A 364 LYS TYR GLN THR PRO PRO HIS GLN ASN PHE GLU ASP LEU
SEQRES 12 A 364 GLU ARG LYS TYR TRP LYS ASN ARG ILE TYR ASN SER PRO
SEQRES 13 A 364 ILE TYR GLY ALA ASP ILE SER GLY SER LEU PHE ASP GLU
SEQRES 14 A 364 ASN THR LYS GLN TRP ASN LEU GLY HIS LEU GLY THR ILE
SEQRES 15 A 364 GLN ASP LEU LEU GLU LYS GLU CYS GLY VAL VAL ILE GLU
SEQRES 16 A 364 GLY VAL ASN THR PRO TYR LEU TYR PHE GLY MET TRP LYS
SEQRES 17 A 364 THR THR PHE ALA TRP HIS THR GLU ASP MET ASP LEU TYR
SEQRES 18 A 364 SER ILE ASN TYR LEU HIS LEU GLY GLU PRO LYS THR TRP
SEQRES 19 A 364 TYR VAL VAL PRO PRO GLU HIS GLY GLN ARG LEU GLU ARG
SEQRES 20 A 364 LEU ALA ARG GLU LEU PHE PRO GLY SER SER ARG GLY CYS
SEQRES 21 A 364 GLY ALA PHE LEU ARG HIS LYS VAL ALA LEU ILE SER PRO
SEQRES 22 A 364 THR VAL LEU LYS GLU ASN GLY ILE PRO PHE ASN ARG ILE
SEQRES 23 A 364 THR GLN GLU ALA GLY GLU PHE MET VAL THR PHE PRO TYR
SEQRES 24 A 364 GLY TYR HIS ALA GLY PHE ASN HIS GLY PHE ASN CYS ALA
SEQRES 25 A 364 GLU ALA ILE ASN PHE ALA THR PRO ARG TRP ILE ASP TYR
SEQRES 26 A 364 GLY LYS MET ALA SER GLN CYS SER CYS GLY GLU ALA ARG
SEQRES 27 A 364 VAL THR PHE SER MET ASP ALA PHE VAL ARG ILE LEU GLN
SEQRES 28 A 364 PRO GLU ARG TYR ASP LEU TRP LYS ARG GLY GLN ASP ARG
HET ZN A 401 1
HET NI A 402 1
HET MG A 403 1
HET OGA A 404 10
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET EDO A 412 4
HET SO4 A 413 5
HET SO4 A 414 5
HET SO4 A 415 5
HET SO4 A 416 5
HET 71N A 417 14
HETNAM ZN ZINC ION
HETNAM NI NICKEL (II) ION
HETNAM MG MAGNESIUM ION
HETNAM OGA N-OXALYLGLYCINE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM SO4 SULFATE ION
HETNAM 71N 2-(TRIFLUOROMETHYL)-1H-BENZIMIDAZOL-5-AMINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ZN ZN 2+
FORMUL 3 NI NI 2+
FORMUL 4 MG MG 2+
FORMUL 5 OGA C4 H5 N O5
FORMUL 6 EDO 8(C2 H6 O2)
FORMUL 14 SO4 4(O4 S 2-)
FORMUL 18 71N C8 H6 F3 N3
FORMUL 19 HOH *455(H2 O)
HELIX 1 AA1 ASP A 30 GLN A 41 1 12
HELIX 2 AA2 GLY A 42 ALA A 46 5 5
HELIX 3 AA3 VAL A 98 ASN A 106 1 9
HELIX 4 AA4 ASN A 117 ARG A 129 1 13
HELIX 5 AA5 ILE A 130 ASN A 132 5 3
HELIX 6 AA6 THR A 159 GLY A 169 1 11
HELIX 7 AA7 GLU A 194 LEU A 198 5 5
HELIX 8 AA8 PRO A 216 GLU A 218 5 3
HELIX 9 AA9 HIS A 219 PHE A 231 1 13
HELIX 10 AB1 PHE A 231 CYS A 238 1 8
HELIX 11 AB2 ALA A 240 LYS A 245 5 6
HELIX 12 AB3 SER A 250 ASN A 257 1 8
HELIX 13 AB4 ARG A 299 ALA A 307 1 9
HELIX 14 AB5 PHE A 319 GLN A 329 1 11
HELIX 15 AB6 GLN A 329 ASP A 341 1 13
SHEET 1 AA110 MET A 19 PHE A 21 0
SHEET 2 AA110 LEU A 48 ILE A 51 1 O LYS A 50 N PHE A 21
SHEET 3 AA110 PHE A 271 THR A 274 -1 O PHE A 271 N ILE A 51
SHEET 4 AA110 TYR A 199 GLY A 207 -1 N ASN A 202 O MET A 272
SHEET 5 AA110 ASN A 288 PHE A 295 -1 O GLU A 291 N TYR A 203
SHEET 6 AA110 TYR A 179 GLY A 183 -1 N TYR A 181 O ALA A 290
SHEET 7 AA110 ILE A 135 SER A 141 -1 N ILE A 140 O LEU A 180
SHEET 8 AA110 LEU A 75 GLY A 81 -1 N LEU A 75 O TYR A 136
SHEET 9 AA110 VAL A 85 LYS A 92 -1 O LYS A 91 N GLN A 76
SHEET 10 AA110 ALA A 247 ILE A 249 -1 O LEU A 248 N PHE A 86
SHEET 1 AA2 2 LEU A 70 ILE A 71 0
SHEET 2 AA2 2 MET A 96 THR A 97 -1 O MET A 96 N ILE A 71
SHEET 1 AA3 4 THR A 188 HIS A 192 0
SHEET 2 AA3 4 TYR A 279 ASN A 284 -1 O GLY A 282 N PHE A 189
SHEET 3 AA3 4 LYS A 210 VAL A 215 -1 N TYR A 213 O ALA A 281
SHEET 4 AA3 4 ASN A 262 GLN A 266 -1 O GLN A 266 N LYS A 210
LINK O ASN A 65 MG MG A 403 1555 1555 2.78
LINK O VAL A 171 MG MG A 403 1555 8555 2.74
LINK NE2 HIS A 192 NI NI A 402 1555 1555 2.19
LINK OE1 GLU A 194 NI NI A 402 1555 1555 2.03
LINK SG CYS A 238 ZN ZN A 401 1555 1555 2.30
LINK NE2 HIS A 244 ZN ZN A 401 1555 1555 2.08
LINK NE2 HIS A 280 NI NI A 402 1555 1555 2.15
LINK SG CYS A 310 ZN ZN A 401 1555 1555 2.28
LINK SG CYS A 312 ZN ZN A 401 1555 1555 2.31
LINK NI NI A 402 O1 OGA A 404 1555 1555 2.12
LINK NI NI A 402 O2' OGA A 404 1555 1555 2.08
LINK NI NI A 402 O HOH A 598 1555 1555 2.13
SITE 1 AC1 4 CYS A 238 HIS A 244 CYS A 310 CYS A 312
SITE 1 AC2 5 HIS A 192 GLU A 194 HIS A 280 OGA A 404
SITE 2 AC2 5 HOH A 598
SITE 1 AC3 7 ASN A 65 ILE A 66 SER A 67 GLU A 68
SITE 2 AC3 7 ILE A 69 VAL A 170 VAL A 171
SITE 1 AC4 12 TYR A 136 PHE A 189 HIS A 192 GLU A 194
SITE 2 AC4 12 SER A 200 ASN A 202 LYS A 210 HIS A 280
SITE 3 AC4 12 NI A 402 EDO A 412 HOH A 598 HOH A 763
SITE 1 AC5 7 LYS A 150 GLN A 151 TRP A 152 ASN A 153
SITE 2 AC5 7 HIS A 156 HOH A 579 HOH A 704
SITE 1 AC6 4 PRO A 251 THR A 252 ARG A 263 HOH A 684
SITE 1 AC7 8 GLU A 224 ALA A 240 PHE A 241 LEU A 242
SITE 2 AC7 8 TYR A 279 SER A 308 HOH A 506 HOH A 634
SITE 1 AC8 7 ASP A 64 ASN A 65 ILE A 66 SER A 67
SITE 2 AC8 7 GLU A 68 ARG A 82 HOH A 556
SITE 1 AC9 4 PHE A 118 ILE A 264 THR A 265 HOH A 548
SITE 1 AD1 8 TRP A 57 LYS A 58 ALA A 59 TYR A 203
SITE 2 AD1 8 HOH A 503 HOH A 504 HOH A 593 HOH A 697
SITE 1 AD2 6 SER A 80 THR A 87 CYS A 168 LYS A 305
SITE 2 AD2 6 HOH A 537 HOH A 545
SITE 1 AD3 6 TYR A 179 TYR A 181 SER A 200 ASN A 294
SITE 2 AD3 6 OGA A 404 HOH A 598
SITE 1 AD4 6 ARG A 102 HIS A 103 ASN A 106 HOH A 510
SITE 2 AD4 6 HOH A 554 HOH A 646
SITE 1 AD5 8 ARG A 60 GLU A 61 THR A 62 ASP A 64
SITE 2 AD5 8 HOH A 507 HOH A 546 HOH A 565 HOH A 670
SITE 1 AD6 4 ARG A 123 LYS A 124 LYS A 127 ASN A 128
SITE 1 AD7 6 PRO A 113 LYS A 124 ASN A 128 TRP A 185
SITE 2 AD7 6 LYS A 186 HOH A 628
SITE 1 AD8 11 GLU A 39 HIS A 44 TYR A 199 PHE A 275
SITE 2 AD8 11 PRO A 276 ARG A 299 TYR A 303 HOH A 703
SITE 3 AD8 11 HOH A 750 HOH A 794 HOH A 894
CRYST1 71.467 71.467 150.264 90.00 90.00 90.00 P 43 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 0.013992 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013992 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006655 0.00000
(ATOM LINES ARE NOT SHOWN.)
END