HEADER OXIDOREDUCTASE 09-JUL-15 5A7Q
TITLE CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH COMPOUND 30
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-359;
COMPND 5 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A,
COMPND 6 JUMONJI DOMAIN-CONTAINING PROTEIN 2A;
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 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_PLASMID: PNIC28-BSA4
KEYWDS OXIDOREDUCTASE, JMJD2A, KDM4A
EXPDTA X-RAY DIFFRACTION
AUTHOR S.VELUPILLAI,T.KROJER,C.GILEADI,C.JOHANSSON,M.KORCZYNSKA,D.D.LE,
AUTHOR 2 N.YOUNGER,E.GREGORI-PUIGJANE,A.TUMBER,E.IWASA,S.B.POLLOCK,I.ORTIZ
AUTHOR 3 TORRES,J.KOPEC,S.DIXON-CLARKE,A.MACKENZIE,R.NOWAK,F.VON DELFT,
AUTHOR 4 C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,B.K.SHOICHET,D.G.FUJIMORI,
AUTHOR 5 U.OPPERMANN
REVDAT 4 10-JAN-24 5A7Q 1 REMARK LINK
REVDAT 3 24-JAN-18 5A7Q 1 AUTHOR
REVDAT 2 09-MAR-16 5A7Q 1 JRNL
REVDAT 1 13-JAN-16 5A7Q 0
JRNL AUTH M.KORCZYNSKA,D.D.LE,N.YOUNGER,E.GREGORI-PUIGJANE,A.TUMBER,
JRNL AUTH 2 T.KROJER,S.VELUPILLAI,C.GILEADI,R.P.NOWAK,E.IWASA,
JRNL AUTH 3 S.B.POLLOCK,I.ORTIZ TORRES,U.OPPERMANN,B.K.SHOICHET,
JRNL AUTH 4 D.G.FUJIMORI
JRNL TITL DOCKING AND LINKING OF FRAGMENTS TO DISCOVER JUMONJI HISTONE
JRNL TITL 2 DEMETHYLASE INHIBITORS.
JRNL REF J.MED.CHEM. V. 59 1580 2016
JRNL REFN ISSN 0022-2623
JRNL PMID 26699912
JRNL DOI 10.1021/ACS.JMEDCHEM.5B01527
REMARK 2
REMARK 2 RESOLUTION. 2.00 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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 83.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 1.0
REMARK 3 NUMBER OF REFLECTIONS : 56771
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 2947
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 5A7Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1290064324.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
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 : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59779
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 149.080
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2OQ7
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG3350 -- 0.1M BIS-TRIS PH 6.5 --
REMARK 280 0.15M AMMONIUM SULFATE
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 50.59700
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.54000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.59700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.54000
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 LEU A 354
REMARK 465 LYS A 355
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 LEU B 8
REMARK 465 LYS B 355
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 GLU A 4 CG CD OE1 OE2
REMARK 470 THR A 7 OG1 CG2
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 LYS A 54 CG CD CE NZ
REMARK 470 LYS A 90 CE NZ
REMARK 470 ARG A 95 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 99 CG CD CE NZ
REMARK 470 SER A 112 OG
REMARK 470 GLU A 113 CG CD OE1 OE2
REMARK 470 GLU A 115 CG CD OE1 OE2
REMARK 470 LYS A 143 CG CD CE NZ
REMARK 470 LYS A 162 CG CD CE NZ
REMARK 470 LYS A 224 CE NZ
REMARK 470 GLU A 235 CG CD OE1 OE2
REMARK 470 LYS A 310 CE NZ
REMARK 470 ASP A 311 CG OD1 OD2
REMARK 470 LYS A 314 CE NZ
REMARK 470 LYS A 330 CE NZ
REMARK 470 LYS A 336 CD CE NZ
REMARK 470 LYS B 51 CD CE NZ
REMARK 470 LYS B 54 CD CE NZ
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 LYS B 99 CD CE NZ
REMARK 470 SER B 112 OG
REMARK 470 LYS B 162 CG CD CE NZ
REMARK 470 LYS B 224 CD CE NZ
REMARK 470 LYS B 310 CG CD CE NZ
REMARK 470 ASP B 311 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 OG SER B 58 OD2 ASP B 60 2.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2045 O HOH A 2045 2545 1.36
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 TYR A 59 43.22 -108.47
REMARK 500 SER A 112 -93.42 -92.01
REMARK 500 ARG A 152 73.10 -157.63
REMARK 500 MET A 192 17.35 58.10
REMARK 500 ALA A 236 59.53 -152.90
REMARK 500 SER B 112 -80.57 -99.73
REMARK 500 ARG B 152 60.07 -150.86
REMARK 500 VAL B 171 -61.82 -97.55
REMARK 500 MET B 192 19.87 56.10
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 MN A1354 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 188 NE2
REMARK 620 2 GLU A 190 OE2 99.3
REMARK 620 3 HIS A 276 NE2 88.2 83.2
REMARK 620 4 KCH A1356 N13 89.0 164.9 109.9
REMARK 620 5 KCH A1356 O17 97.7 82.8 165.5 83.6
REMARK 620 6 HOH A2093 O 172.3 88.4 93.0 83.5 82.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1357 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 108.0
REMARK 620 3 CYS A 306 SG 114.1 116.2
REMARK 620 4 CYS A 308 SG 110.8 95.0 111.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B1355 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 188 NE2
REMARK 620 2 GLU B 190 OE2 103.4
REMARK 620 3 HIS B 276 NE2 86.8 87.7
REMARK 620 4 KCH B1357 O17 101.2 80.0 166.5
REMARK 620 5 KCH B1357 N13 90.0 160.8 107.0 84.0
REMARK 620 6 HOH B2101 O 170.0 85.6 89.0 84.7 82.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1358 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 234 SG
REMARK 620 2 HIS B 240 NE2 108.9
REMARK 620 3 CYS B 306 SG 114.8 117.6
REMARK 620 4 CYS B 308 SG 113.7 89.7 109.7
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 MN A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KCH B 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KCH A 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1360
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5A7N RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH COMPOUND 43
REMARK 900 RELATED ID: 5A7O RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH COMPOUND 42
REMARK 900 RELATED ID: 5A7P RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH COMPOUND 36
REMARK 900 RELATED ID: 5A7S RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH COMPOUND 44
DBREF 5A7Q A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5A7Q B 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 5A7Q MET A -21 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS A -20 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS A -19 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS A -18 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS A -17 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS A -16 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS A -15 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q SER A -14 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q SER A -13 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLY A -12 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q VAL A -11 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q ASP A -10 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q LEU A -9 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLY A -8 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q THR A -7 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLU A -6 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q ASN A -5 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q LEU A -4 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q TYR A -3 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q PHE A -2 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLN A -1 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q MET B -21 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS B -20 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS B -19 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS B -18 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS B -17 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS B -16 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q HIS B -15 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q SER B -14 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q SER B -13 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLY B -12 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q VAL B -11 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q ASP B -10 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q LEU B -9 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLY B -8 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q THR B -7 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLU B -6 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q ASN B -5 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q LEU B -4 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q TYR B -3 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q PHE B -2 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q GLN B -1 UNP O75164 EXPRESSION TAG
SEQADV 5A7Q 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 MN A1354 1
HET MN A1355 1
HET KCH A1356 17
HET ZN A1357 1
HET CL A1358 1
HET CL A1359 1
HET MN B1355 1
HET MN B1356 1
HET KCH B1357 17
HET ZN B1358 1
HET CL B1359 1
HET EDO B1360 4
HETNAM MN MANGANESE (II) ION
HETNAM KCH 2-(5-AZANYL-2-OXIDANYL-PHENYL)PYRIDINE-4-CARBOXYLIC
HETNAM 2 KCH ACID
HETNAM ZN ZINC ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 MN 4(MN 2+)
FORMUL 5 KCH 2(C12 H10 N2 O3)
FORMUL 6 ZN 2(ZN 2+)
FORMUL 7 CL 3(CL 1-)
FORMUL 14 EDO C2 H6 O2
FORMUL 15 HOH *329(H2 O)
HELIX 1 1 THR A 20 ASN A 26 1 7
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 ARG A 328 ALA A 334 1 7
HELIX 18 18 THR A 347 PHE A 353 5 7
HELIX 19 19 ASN B 9 ARG B 13 5 5
HELIX 20 20 THR B 20 ASN B 26 1 7
HELIX 21 21 ASN B 26 GLN B 37 1 12
HELIX 22 22 GLY B 38 ALA B 42 5 5
HELIX 23 23 VAL B 94 SER B 103 1 10
HELIX 24 24 GLU B 113 LEU B 125 1 13
HELIX 25 25 ASN B 149 LEU B 153 5 5
HELIX 26 26 THR B 155 LEU B 157 5 3
HELIX 27 27 ASP B 158 GLY B 165 1 8
HELIX 28 28 GLU B 190 LEU B 194 5 5
HELIX 29 29 PRO B 212 GLU B 214 5 3
HELIX 30 30 HIS B 215 PHE B 227 1 13
HELIX 31 31 PHE B 227 CYS B 234 1 8
HELIX 32 32 ALA B 236 LYS B 241 5 6
HELIX 33 33 SER B 246 TYR B 253 1 8
HELIX 34 34 ARG B 295 ALA B 303 1 9
HELIX 35 35 MET B 317 GLN B 325 1 9
HELIX 36 36 GLN B 325 ALA B 334 1 10
HELIX 37 37 THR B 347 PHE B 353 5 7
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 MN MN A1354 1555 1555 2.26
LINK OE2 GLU A 190 MN MN A1354 1555 1555 2.07
LINK SG CYS A 234 ZN ZN A1357 1555 1555 2.28
LINK NE2 HIS A 240 ZN ZN A1357 1555 1555 2.11
LINK NE2 HIS A 276 MN MN A1354 1555 1555 2.22
LINK SG CYS A 306 ZN ZN A1357 1555 1555 2.25
LINK SG CYS A 308 ZN ZN A1357 1555 1555 2.36
LINK MN MN A1354 N13 KCH A1356 1555 1555 2.16
LINK MN MN A1354 O17 KCH A1356 1555 1555 2.04
LINK MN MN A1354 O HOH A2093 1555 1555 2.19
LINK NE2 HIS B 188 MN MN B1355 1555 1555 2.22
LINK OE2 GLU B 190 MN MN B1355 1555 1555 2.16
LINK SG CYS B 234 ZN ZN B1358 1555 1555 2.18
LINK NE2 HIS B 240 ZN ZN B1358 1555 1555 2.22
LINK NE2 HIS B 276 MN MN B1355 1555 1555 2.17
LINK SG CYS B 306 ZN ZN B1358 1555 1555 2.34
LINK SG CYS B 308 ZN ZN B1358 1555 1555 2.34
LINK MN MN B1355 O17 KCH B1357 1555 1555 2.05
LINK MN MN B1355 N13 KCH B1357 1555 1555 2.08
LINK MN MN B1355 O HOH B2101 1555 1555 2.32
SITE 1 AC1 5 HIS A 188 GLU A 190 HIS A 276 KCH A1356
SITE 2 AC1 5 HOH A2093
SITE 1 AC2 5 HIS B 188 GLU B 190 HIS B 276 KCH B1357
SITE 2 AC2 5 HOH B2101
SITE 1 AC3 2 GLY A 229 SER A 230
SITE 1 AC4 2 GLY B 229 SER B 230
SITE 1 AC5 12 TYR B 132 PHE B 185 HIS B 188 GLU B 190
SITE 2 AC5 12 ASN B 198 LYS B 206 TRP B 208 LYS B 241
SITE 3 AC5 12 HIS B 276 MN B1355 HOH B2101 HOH B2169
SITE 1 AC6 12 TYR A 132 PHE A 185 HIS A 188 GLU A 190
SITE 2 AC6 12 ASN A 198 LYS A 206 TRP A 208 LYS A 241
SITE 3 AC6 12 HIS A 276 MN A1354 HOH A2061 HOH A2093
SITE 1 AC7 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC8 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC9 3 ALA A 236 PHE A 237 LEU A 238
SITE 1 BC1 3 GLY A 170 TYR A 177 SER A 288
SITE 1 BC2 3 GLY B 170 TYR B 177 SER B 288
SITE 1 BC3 4 TYR B 18 GLU B 263 GLU B 266 HOH B2008
CRYST1 101.194 149.080 57.627 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 0.009882 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006708 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017353 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
