HEADER OXIDOREDUCTASE 07-MAR-16 5FYI
TITLE CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH PYRUVATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 4A;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 4-354;
COMPND 5 SYNONYM: JMJC DOMAIN-CONTAINING HISTONE DEMETHYLATION PROTEIN 3A, JU
COMPND 6 MONJI 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, TCA INTERMEDIATE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.NOWAK,J.KOPEC,C.JOHANSSON,A.SZYKOWSKA,F.VON DELFT,C.H.ARROWSMITH,
AUTHOR 2 C.BOUNTRA,A.EDWARDS,U.OPPERMANN
REVDAT 4 10-JAN-24 5FYI 1 REMARK
REVDAT 3 15-NOV-23 5FYI 1 REMARK LINK ATOM
REVDAT 2 24-JAN-18 5FYI 1 AUTHOR JRNL
REVDAT 1 16-MAR-16 5FYI 0
JRNL AUTH R.NOWAK,J.KOPEC,C.JOHANSSON,A.SZYKOWSKA,F.VON DELFT,
JRNL AUTH 2 C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,U.OPPERMANN
JRNL TITL CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH PYRUVATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 50981
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.197
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 2457
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 29.7702 - 5.4832 1.00 2895 150 0.1680 0.2088
REMARK 3 2 5.4832 - 4.3565 1.00 2785 118 0.1431 0.1543
REMARK 3 3 4.3565 - 3.8071 1.00 2726 147 0.1627 0.1928
REMARK 3 4 3.8071 - 3.4596 1.00 2717 156 0.1853 0.2096
REMARK 3 5 3.4596 - 3.2119 1.00 2706 137 0.2066 0.2428
REMARK 3 6 3.2119 - 3.0228 1.00 2686 139 0.2115 0.2783
REMARK 3 7 3.0228 - 2.8715 1.00 2703 125 0.2234 0.2558
REMARK 3 8 2.8715 - 2.7466 1.00 2707 125 0.2405 0.2838
REMARK 3 9 2.7466 - 2.6409 1.00 2671 133 0.2329 0.3033
REMARK 3 10 2.6409 - 2.5498 1.00 2686 148 0.2434 0.3238
REMARK 3 11 2.5498 - 2.4702 1.00 2666 125 0.2346 0.2703
REMARK 3 12 2.4702 - 2.3996 1.00 2662 131 0.2359 0.2991
REMARK 3 13 2.3996 - 2.3364 1.00 2679 128 0.2477 0.3396
REMARK 3 14 2.3364 - 2.2795 1.00 2653 143 0.2493 0.3144
REMARK 3 15 2.2795 - 2.2277 1.00 2683 129 0.2599 0.2860
REMARK 3 16 2.2277 - 2.1803 1.00 2624 142 0.2618 0.3331
REMARK 3 17 2.1803 - 2.1367 1.00 2660 142 0.2741 0.3142
REMARK 3 18 2.1367 - 2.0963 0.99 2615 139 0.2865 0.3264
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: DISORDERED SIDE-CHAINS WERE REMOVED.
REMARK 4
REMARK 4 5FYI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1290066387.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
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 : 51046
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.15
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.68000
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: DIMPLE
REMARK 200 STARTING MODEL: PDB ENTRY 5A7O
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.0 -- 0.2M AMMONIUM
REMARK 280 SULFATE -- 28% PEG3350
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 50.22500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.41500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.22500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.41500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 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 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 ASN B 9
REMARK 465 LEU B 354
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 ARG A 13 NE CZ NH1 NH2
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 ARG A 25 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 29 CZ NH1 NH2
REMARK 470 GLU A 52 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 CG CD NE CZ NH1 NH2
REMARK 470 SER A 112 OG
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 CD NE CZ NH1 NH2
REMARK 470 LYS A 162 CG CD CE NZ
REMARK 470 GLN A 232 CG CD OE1 NE2
REMARK 470 LYS A 310 CG CD CE NZ
REMARK 470 LYS A 330 CD CE NZ
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 GLU B 22 CG CD OE1 OE2
REMARK 470 ARG B 29 CZ NH1 NH2
REMARK 470 LYS B 51 CD CE NZ
REMARK 470 GLU B 52 CG CD OE1 OE2
REMARK 470 LYS B 54 CE NZ
REMARK 470 LYS B 90 CG CD CE NZ
REMARK 470 LYS B 99 CD CE NZ
REMARK 470 ARG B 110 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 113 OE1 OE2
REMARK 470 GLU B 115 CG CD OE1 OE2
REMARK 470 GLU B 142 CG CD OE1 OE2
REMARK 470 LYS B 143 CG CD CE NZ
REMARK 470 ARG B 154 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 161 CD OE1 OE2
REMARK 470 LYS B 162 CD CE NZ
REMARK 470 GLU B 163 CG CD OE1 OE2
REMARK 470 LYS B 224 CG CD CE NZ
REMARK 470 GLN B 232 CD OE1 NE2
REMARK 470 LYS B 310 CG CD CE NZ
REMARK 470 LYS B 323 NZ
REMARK 470 ARG B 328 CZ NH1 NH2
REMARK 470 LYS B 333 CD CE NZ
REMARK 470 LYS B 336 CG CD CE NZ
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 OG1 THR A 93 O HOH A 2020 2.01
REMARK 500 O GLY A 203 O HOH A 2093 2.12
REMARK 500 OH TYR B 111 O HOH B 2062 2.12
REMARK 500 OG SER A 58 OD2 ASP A 60 2.14
REMARK 500 O PRO B 49 O HOH B 2020 2.16
REMARK 500 N GLU A 96 O HOH A 2020 2.16
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 52.72 -109.25
REMARK 500 SER A 103 157.08 -49.56
REMARK 500 SER A 112 -83.87 -95.82
REMARK 500 ARG A 152 69.15 -157.60
REMARK 500 MET A 192 18.54 56.00
REMARK 500 ALA A 236 57.77 -148.25
REMARK 500 PHE A 353 -68.09 -100.89
REMARK 500 SER B 103 156.28 -47.04
REMARK 500 SER B 112 -82.99 -97.99
REMARK 500 ARG B 152 68.36 -157.86
REMARK 500 MET B 192 19.90 55.83
REMARK 500 ALA B 236 57.75 -145.41
REMARK 500 LYS B 310 -98.80 -62.22
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 103.9
REMARK 620 3 HIS A 276 NE2 93.5 81.4
REMARK 620 4 PYR A1355 O 163.3 91.2 95.7
REMARK 620 5 PYR A1355 O3 87.5 167.1 104.2 76.7
REMARK 620 6 HOH A2083 O 84.2 87.2 167.4 89.6 88.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A3000 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 234 SG
REMARK 620 2 HIS A 240 NE2 107.7
REMARK 620 3 CYS A 306 SG 112.9 118.2
REMARK 620 4 CYS A 308 SG 112.2 96.6 108.2
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 111.5
REMARK 620 3 HIS B 276 NE2 90.4 82.2
REMARK 620 4 PYR B1354 O 164.4 84.0 90.6
REMARK 620 5 PYR B1354 O3 88.0 160.5 97.3 76.4
REMARK 620 6 HOH B2090 O 89.0 90.6 172.0 92.1 90.7
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 109.4
REMARK 620 3 CYS B 306 SG 112.7 113.3
REMARK 620 4 CYS B 308 SG 115.4 93.0 111.6
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 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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR B 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYR A 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1357
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1359
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1360
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1361
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1361
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1362
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1363
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1362
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1363
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1364
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1364
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1365
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KA B 1365
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FXV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH N05859B
REMARK 900 RELATED ID: 5FXW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH FUMARATE
REMARK 900 RELATED ID: 5FXX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH OXALOACETATE
REMARK 900 RELATED ID: 5FXZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH CITRATE
REMARK 900 RELATED ID: 5FY0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH L-MALATE
REMARK 900 RELATED ID: 5FY1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH N08619B
REMARK 900 RELATED ID: 5FY4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH SUCCINATE
REMARK 900 RELATED ID: 5FY5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH FUMARATE
REMARK 900 RELATED ID: 5FY7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH SUCCINATE
REMARK 900 RELATED ID: 5FY8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH D- THREO-
REMARK 900 ISOCITRATE
REMARK 900 RELATED ID: 5FY9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH PYRUVATE
REMARK 900 RELATED ID: 5FYB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH MC1648
REMARK 900 RELATED ID: 5FYC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH SUCCINATE
REMARK 900 RELATED ID: 5FYH RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH FUMARATE
REMARK 900 RELATED ID: 5FYM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY
REMARK 900 IN COMPLEX WITH D-2-HYDROXYGLUTARATE
REMARK 900 RELATED ID: 5FYS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH D-2-HYDROXYGLUTARATE
REMARK 900 RELATED ID: 5FYT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH N09996A
REMARK 900 RELATED ID: 5FYU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH N10042A
REMARK 900 RELATED ID: 5FYV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH OXALOACETATE
DBREF 5FYI A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FYI B 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 5FYI MET A -21 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS A -20 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS A -19 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS A -18 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS A -17 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS A -16 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS A -15 UNP O75164 EXPRESSION TAG
SEQADV 5FYI SER A -14 UNP O75164 EXPRESSION TAG
SEQADV 5FYI SER A -13 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLY A -12 UNP O75164 EXPRESSION TAG
SEQADV 5FYI VAL A -11 UNP O75164 EXPRESSION TAG
SEQADV 5FYI ASP A -10 UNP O75164 EXPRESSION TAG
SEQADV 5FYI LEU A -9 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLY A -8 UNP O75164 EXPRESSION TAG
SEQADV 5FYI THR A -7 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLU A -6 UNP O75164 EXPRESSION TAG
SEQADV 5FYI ASN A -5 UNP O75164 EXPRESSION TAG
SEQADV 5FYI LEU A -4 UNP O75164 EXPRESSION TAG
SEQADV 5FYI TYR A -3 UNP O75164 EXPRESSION TAG
SEQADV 5FYI PHE A -2 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLN A -1 UNP O75164 EXPRESSION TAG
SEQADV 5FYI SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 5FYI MET B -21 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS B -20 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS B -19 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS B -18 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS B -17 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS B -16 UNP O75164 EXPRESSION TAG
SEQADV 5FYI HIS B -15 UNP O75164 EXPRESSION TAG
SEQADV 5FYI SER B -14 UNP O75164 EXPRESSION TAG
SEQADV 5FYI SER B -13 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLY B -12 UNP O75164 EXPRESSION TAG
SEQADV 5FYI VAL B -11 UNP O75164 EXPRESSION TAG
SEQADV 5FYI ASP B -10 UNP O75164 EXPRESSION TAG
SEQADV 5FYI LEU B -9 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLY B -8 UNP O75164 EXPRESSION TAG
SEQADV 5FYI THR B -7 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLU B -6 UNP O75164 EXPRESSION TAG
SEQADV 5FYI ASN B -5 UNP O75164 EXPRESSION TAG
SEQADV 5FYI LEU B -4 UNP O75164 EXPRESSION TAG
SEQADV 5FYI TYR B -3 UNP O75164 EXPRESSION TAG
SEQADV 5FYI PHE B -2 UNP O75164 EXPRESSION TAG
SEQADV 5FYI GLN B -1 UNP O75164 EXPRESSION TAG
SEQADV 5FYI 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 PYR A1355 6
HET PYR A1356 6
HET DMS A1357 4
HET EDO A1358 4
HET EDO A1359 4
HET EDO A1360 4
HET EDO A1361 4
HET EDO A1362 4
HET EDO A1363 4
HET EDO A1364 4
HET EDO A1365 4
HET ZN A3000 1
HET EDO A3001 4
HET NI B 501 1
HET ZN B 502 1
HET PYR B1354 6
HET PYR B1355 6
HET DMS B1356 4
HET EDO B1357 4
HET EDO B1358 4
HET EDO B1359 4
HET EDO B1360 4
HET EDO B1361 4
HET EDO B1362 4
HET EDO B1363 4
HET EDO B1364 4
HET 1KA B1365 7
HETNAM NI NICKEL (II) ION
HETNAM PYR PYRUVIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ZN ZINC ION
HETNAM 1KA (2-HYDROXYETHOXY)ACETALDEHYDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NI 2(NI 2+)
FORMUL 4 PYR 4(C3 H4 O3)
FORMUL 6 DMS 2(C2 H6 O S)
FORMUL 7 EDO 17(C2 H6 O2)
FORMUL 15 ZN 2(ZN 2+)
FORMUL 30 1KA C4 H8 O3
FORMUL 31 HOH *325(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 ARG A 328 ALA A 334 1 7
HELIX 18 18 THR A 347 PHE A 353 5 7
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 SER B 103 1 10
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 ALA B 334 1 10
HELIX 35 35 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 NI NI A 501 1555 1555 2.29
LINK OE2 GLU A 190 NI NI A 501 1555 1555 2.10
LINK SG CYS A 234 ZN ZN A3000 1555 1555 2.31
LINK NE2 HIS A 240 ZN ZN A3000 1555 1555 2.06
LINK NE2 HIS A 276 NI NI A 501 1555 1555 2.25
LINK SG CYS A 306 ZN ZN A3000 1555 1555 2.14
LINK SG CYS A 308 ZN ZN A3000 1555 1555 2.37
LINK NI NI A 501 O PYR A1355 1555 1555 2.16
LINK NI NI A 501 O3 PYR A1355 1555 1555 2.36
LINK NI NI A 501 O HOH A2083 1555 1555 2.26
LINK NE2 HIS B 188 NI NI B 501 1555 1555 2.29
LINK OE2 GLU B 190 NI NI B 501 1555 1555 2.17
LINK SG CYS B 234 ZN ZN B 502 1555 1555 2.26
LINK NE2 HIS B 240 ZN ZN B 502 1555 1555 2.11
LINK NE2 HIS B 276 NI NI B 501 1555 1555 2.27
LINK SG CYS B 306 ZN ZN B 502 1555 1555 2.17
LINK SG CYS B 308 ZN ZN B 502 1555 1555 2.33
LINK NI NI B 501 O PYR B1354 1555 1555 2.25
LINK NI NI B 501 O3 PYR B1354 1555 1555 2.26
LINK NI NI B 501 O HOH B2090 1555 1555 2.35
SITE 1 AC1 5 HIS A 188 GLU A 190 HIS A 276 PYR A1355
SITE 2 AC1 5 HOH A2083
SITE 1 AC2 5 HIS B 188 GLU B 190 HIS B 276 PYR B1354
SITE 2 AC2 5 HOH B2090
SITE 1 AC3 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC4 9 PHE A 185 HIS A 188 GLU A 190 SER A 196
SITE 2 AC4 9 ASN A 198 TRP A 208 HIS A 276 NI A 501
SITE 3 AC4 9 PYR A1356
SITE 1 AC5 9 PHE B 185 HIS B 188 GLU B 190 SER B 196
SITE 2 AC5 9 ASN B 198 TRP B 208 HIS B 276 NI B 501
SITE 3 AC5 9 PYR B1355
SITE 1 AC6 8 TYR B 132 TYR B 177 PHE B 185 ASN B 198
SITE 2 AC6 8 LYS B 206 SER B 288 PYR B1354 EDO B1364
SITE 1 AC7 7 TYR A 132 TYR A 177 ASN A 198 LYS A 206
SITE 2 AC7 7 SER A 288 PYR A1355 EDO A1365
SITE 1 AC8 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC9 5 PHE A 227 PRO A 228 GLY A 229 SER A 230
SITE 2 AC9 5 LYS B 105
SITE 1 BC1 4 PHE B 227 PRO B 228 GLY B 229 SER B 230
SITE 1 BC2 6 HIS A 188 THR A 189 LEU A 238 ARG A 239
SITE 2 BC2 6 TYR A 275 HOH A2105
SITE 1 BC3 8 TYR B 121 TRP B 122 PHE B 185 TRP B 187
SITE 2 BC3 8 LEU B 244 ILE B 245 ALA B 277 GLY B 278
SITE 1 BC4 4 GLY B 80 SER B 246 LEU B 248 HOH B2067
SITE 1 BC5 6 GLU B 235 ALA B 236 PHE B 237 LEU B 238
SITE 2 BC5 6 HOH B2112 HOH B2132
SITE 1 BC6 6 HOH A2062 THR B 76 LEU B 81 PHE B 82
SITE 2 BC6 6 THR B 83 PHE B 227
SITE 1 BC7 5 GLY A 80 PHE A 82 TRP A 122 SER A 246
SITE 2 BC7 5 HOH A2034
SITE 1 BC8 3 GLU A 163 LYS B 330 HOH B2152
SITE 1 BC9 6 THR A 83 PHE A 227 SER A 230 PHE A 237
SITE 2 BC9 6 THR A 243 HOH A2116
SITE 1 CC1 2 ARG B 98 ASN B 102
SITE 1 CC2 5 TYR B 106 ASN B 128 PRO B 130 TRP B 181
SITE 2 CC2 5 LYS B 182
SITE 1 CC3 5 TYR B 18 LYS B 46 GLU B 263 GLU B 266
SITE 2 CC3 5 HOH B2006
SITE 1 CC4 4 PHE A 114 THR A 261 GLU A 263 HIS A 281
SITE 1 CC5 4 ASP A 158 GLU A 161 LYS A 162 HOH A2075
SITE 1 CC6 2 GLU A 214 HIS A 215
SITE 1 CC7 4 PHE B 185 HIS B 188 LYS B 241 PYR B1355
SITE 1 CC8 3 TYR A 132 PHE A 185 PYR A1356
SITE 1 CC9 5 ALA B 12 GLU B 214 HIS B 215 PRO B 256
SITE 2 CC9 5 HOH B2122
CRYST1 100.450 148.830 57.060 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 0.009955 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006719 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017525 0.00000
(ATOM LINES ARE NOT SHOWN.)
END