HEADER OXIDOREDUCTASE 04-MAR-16 5FY8
TITLE CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH D-THREO-ISOCITRATE
CAVEAT 5FY8 N81 B 1354 HAS WRONG CHIRALITY AT ATOM C02
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,
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, 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 3 10-JAN-24 5FY8 1 CAVEAT REMARK LINK
REVDAT 2 24-JAN-18 5FY8 1 AUTHOR JRNL
REVDAT 1 16-MAR-16 5FY8 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
JRNL TITL 2 D-THREO-ISOCITRATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.34 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) : 2.34
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 36843
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1758
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 28.9818 - 5.4972 1.00 2888 149 0.1610 0.1980
REMARK 3 2 5.4972 - 4.3681 1.00 2766 121 0.1389 0.1691
REMARK 3 3 4.3681 - 3.8173 1.00 2729 144 0.1549 0.1830
REMARK 3 4 3.8173 - 3.4689 1.00 2698 158 0.1862 0.2272
REMARK 3 5 3.4689 - 3.2206 1.00 2696 135 0.1997 0.2550
REMARK 3 6 3.2206 - 3.0310 1.00 2695 138 0.2113 0.2701
REMARK 3 7 3.0310 - 2.8793 1.00 2683 125 0.2212 0.2716
REMARK 3 8 2.8793 - 2.7541 1.00 2706 124 0.2266 0.3120
REMARK 3 9 2.7541 - 2.6481 1.00 2666 130 0.2272 0.2867
REMARK 3 10 2.6481 - 2.5568 1.00 2668 151 0.2485 0.3005
REMARK 3 11 2.5568 - 2.4769 1.00 2635 126 0.2456 0.2904
REMARK 3 12 2.4769 - 2.4061 1.00 2682 134 0.2527 0.3417
REMARK 3 13 2.4061 - 2.3428 0.97 2573 123 0.2717 0.3618
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: SOME RESIDUE SIDECHAINS ARE IN DUAL
REMARK 3 CONFORMATION. SOME RESIDUES DO NOT HAVE SIDECHAINS.
REMARK 4
REMARK 4 5FY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1290066375.
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 : 36894
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.340
REMARK 200 RESOLUTION RANGE LOW (A) : 28.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.70
REMARK 200 R MERGE FOR SHELL (I) : 0.77000
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: DIMPLE
REMARK 200 STARTING MODEL: PDB NETRY 5A7W
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH 6.0 -- 0.15M 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 50.46500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 74.45500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.46500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 74.45500
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 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 NH2 ARG A 322 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 ALA A 2
REMARK 465 SER A 3
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 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 GLU A 4 CG CD OE1 OE2
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 LYS A 54 CG CD CE NZ
REMARK 470 LYS A 90 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 ARG A 221 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 309 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 330 CD CE NZ
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 THR B 7 OG1 CG2
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 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 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 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 OE2 GLU B 349 O HOH B 2087 2.06
REMARK 500 O DMS A 1355 O HOH A 2068 2.09
REMARK 500 O VAL B 66 O HOH B 2013 2.11
REMARK 500 OE1 GLU A 142 O HOH A 2037 2.12
REMARK 500 O ASP B 60 O HOH B 2011 2.13
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 CZ ARG A 322 NH2 ARG A 322 2455 1.33
REMARK 500 NH1 ARG A 322 NH2 ARG A 322 2455 1.91
REMARK 500 NE ARG A 322 NH2 ARG A 322 2455 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 322 NH1 - CZ - NH2 ANGL. DEV. = -28.2 DEGREES
REMARK 500 ARG A 322 NE - CZ - NH2 ANGL. DEV. = -12.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 59 48.37 -102.75
REMARK 500 SER A 112 -85.29 -96.22
REMARK 500 ARG A 152 70.27 -155.58
REMARK 500 ALA A 236 56.75 -146.18
REMARK 500 ARG A 309 -0.12 77.23
REMARK 500 ASN A 338 44.90 -103.78
REMARK 500 TYR B 59 46.04 -104.06
REMARK 500 SER B 112 -83.86 -99.23
REMARK 500 ARG B 152 68.00 -153.01
REMARK 500 ALA B 236 54.69 -146.29
REMARK 500 ASP B 311 45.64 -102.27
REMARK 500 ASN B 338 46.00 -104.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 322 0.36 SIDE CHAIN
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 103.4
REMARK 620 3 HIS A 276 NE2 94.9 82.3
REMARK 620 4 N81 A1354 O12 156.0 93.5 104.3
REMARK 620 5 N81 A1354 O01 94.9 157.7 83.6 73.4
REMARK 620 6 HOH A2050 O 76.1 91.9 168.0 86.5 104.9
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 105.3
REMARK 620 3 CYS A 306 SG 113.6 114.3
REMARK 620 4 CYS A 308 SG 117.7 98.3 106.7
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 110.8
REMARK 620 3 HIS B 276 NE2 87.8 79.5
REMARK 620 4 N81 B1354 O01 95.6 152.0 92.7
REMARK 620 5 N81 B1354 O12 161.1 84.1 83.4 68.2
REMARK 620 6 HOH B2048 O 93.8 95.4 174.9 91.9 96.3
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 105.4
REMARK 620 3 CYS B 306 SG 115.3 116.9
REMARK 620 4 CYS B 308 SG 113.8 92.6 110.8
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 NI B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N81 A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE N81 B 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS B 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1357
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 A 1358
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1359
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: 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: 5FYI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD2A IN COMPLEX WITH PYRUVATE
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
DBREF 5FY8 A 1 359 UNP O75164 KDM4A_HUMAN 1 359
DBREF 5FY8 B 1 359 UNP O75164 KDM4A_HUMAN 1 359
SEQADV 5FY8 MET A -21 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS A -20 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS A -19 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS A -18 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS A -17 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS A -16 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS A -15 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 SER A -14 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 SER A -13 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLY A -12 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 VAL A -11 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 ASP A -10 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 LEU A -9 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLY A -8 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 THR A -7 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLU A -6 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 ASN A -5 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 LEU A -4 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 TYR A -3 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 PHE A -2 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLN A -1 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 SER A 0 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 MET B -21 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS B -20 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS B -19 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS B -18 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS B -17 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS B -16 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 HIS B -15 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 SER B -14 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 SER B -13 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLY B -12 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 VAL B -11 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 ASP B -10 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 LEU B -9 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLY B -8 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 THR B -7 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLU B -6 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 ASN B -5 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 LEU B -4 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 TYR B -3 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 PHE B -2 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 GLN B -1 UNP O75164 EXPRESSION TAG
SEQADV 5FY8 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 N81 A1354 13
HET DMS A1355 4
HET EDO A1356 4
HET EDO A1357 4
HET EDO A1358 4
HET NI B 501 1
HET ZN B 502 1
HET N81 B1354 13
HET DMS B1355 4
HET EDO B1356 4
HET EDO B1357 4
HET EDO B1358 4
HET EDO B1359 4
HETNAM NI NICKEL (II) ION
HETNAM ZN ZINC ION
HETNAM N81 3-CARBOXY-2,3-DIDEOXY-D-ERYTHRO-PENTARIC ACID
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 NI 2(NI 2+)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 5 N81 2(C6 H8 O7)
FORMUL 6 DMS 2(C2 H6 O S)
FORMUL 7 EDO 7(C2 H6 O2)
FORMUL 18 HOH *196(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 VAL A 94 SER A 103 1 10
HELIX 5 5 GLU A 113 LEU A 125 1 13
HELIX 6 6 THR A 155 LEU A 157 5 3
HELIX 7 7 ASP A 158 GLY A 165 1 8
HELIX 8 8 GLU A 190 LEU A 194 5 5
HELIX 9 9 PRO A 212 GLU A 214 5 3
HELIX 10 10 HIS A 215 PHE A 227 1 13
HELIX 11 11 PHE A 227 CYS A 234 1 8
HELIX 12 12 ALA A 236 LYS A 241 5 6
HELIX 13 13 SER A 246 TYR A 253 1 8
HELIX 14 14 ARG A 295 ALA A 303 1 9
HELIX 15 15 MET A 317 GLN A 325 1 9
HELIX 16 16 ARG A 328 ALA A 334 1 7
HELIX 17 17 THR A 347 PHE A 353 5 7
HELIX 18 18 THR B 20 ASN B 26 1 7
HELIX 19 19 ASN B 26 GLN B 37 1 12
HELIX 20 20 GLY B 38 ALA B 42 5 5
HELIX 21 21 VAL B 94 SER B 103 1 10
HELIX 22 22 GLU B 113 LEU B 125 1 13
HELIX 23 23 THR B 155 LEU B 159 5 5
HELIX 24 24 VAL B 160 GLY B 165 1 6
HELIX 25 25 GLU B 190 LEU B 194 5 5
HELIX 26 26 PRO B 212 GLU B 214 5 3
HELIX 27 27 HIS B 215 PHE B 227 1 13
HELIX 28 28 PHE B 227 CYS B 234 1 8
HELIX 29 29 ALA B 236 LYS B 241 5 6
HELIX 30 30 SER B 246 TYR B 253 1 8
HELIX 31 31 ARG B 295 ALA B 303 1 9
HELIX 32 32 MET B 317 GLN B 325 1 9
HELIX 33 33 ARG B 328 ALA B 334 1 7
HELIX 34 34 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 2.42
LINK OE2 GLU A 190 NI NI A 501 1555 1555 2.01
LINK SG CYS A 234 ZN ZN A 502 1555 1555 2.25
LINK NE2 HIS A 240 ZN ZN A 502 1555 1555 2.08
LINK NE2 HIS A 276 NI NI A 501 1555 1555 2.30
LINK SG CYS A 306 ZN ZN A 502 1555 1555 2.13
LINK SG CYS A 308 ZN ZN A 502 1555 1555 2.39
LINK NI NI A 501 O12 N81 A1354 1555 1555 2.78
LINK NI NI A 501 O01 N81 A1354 1555 1555 2.38
LINK NI NI A 501 O HOH A2050 1555 1555 2.41
LINK NE2 HIS B 188 NI NI B 501 1555 1555 2.20
LINK OE2 GLU B 190 NI NI B 501 1555 1555 2.22
LINK SG CYS B 234 ZN ZN B 502 1555 1555 2.22
LINK NE2 HIS B 240 ZN ZN B 502 1555 1555 2.09
LINK NE2 HIS B 276 NI NI B 501 1555 1555 2.42
LINK SG CYS B 306 ZN ZN B 502 1555 1555 2.16
LINK SG CYS B 308 ZN ZN B 502 1555 1555 2.28
LINK NI NI B 501 O01 N81 B1354 1555 1555 2.28
LINK NI NI B 501 O12 N81 B1354 1555 1555 2.53
LINK NI NI B 501 O HOH B2048 1555 1555 2.43
SITE 1 AC1 5 HIS A 188 GLU A 190 HIS A 276 N81 A1354
SITE 2 AC1 5 HOH A2050
SITE 1 AC2 4 CYS A 234 HIS A 240 CYS A 306 CYS A 308
SITE 1 AC3 5 HIS B 188 GLU B 190 HIS B 276 N81 B1354
SITE 2 AC3 5 HOH B2048
SITE 1 AC4 4 CYS B 234 HIS B 240 CYS B 306 CYS B 308
SITE 1 AC5 13 TYR A 132 TYR A 177 PHE A 185 HIS A 188
SITE 2 AC5 13 GLU A 190 SER A 196 ASN A 198 TRP A 208
SITE 3 AC5 13 LYS A 241 HIS A 276 SER A 288 NI A 501
SITE 4 AC5 13 HOH A2050
SITE 1 AC6 13 TYR B 132 TYR B 177 PHE B 185 HIS B 188
SITE 2 AC6 13 GLU B 190 SER B 196 ASN B 198 LYS B 206
SITE 3 AC6 13 TRP B 208 HIS B 276 SER B 288 NI B 501
SITE 4 AC6 13 HOH B2048
SITE 1 AC7 6 PHE A 227 PRO A 228 GLY A 229 SER A 230
SITE 2 AC7 6 HOH A2068 LYS B 105
SITE 1 AC8 6 LYS A 105 PHE B 226 PHE B 227 PRO B 228
SITE 2 AC8 6 GLY B 229 SER B 230
SITE 1 AC9 6 GLU B 235 ALA B 236 PHE B 237 LEU B 238
SITE 2 AC9 6 HOH B2059 HOH B2071
SITE 1 BC1 6 CYS A 234 GLU A 235 ALA A 236 PHE A 237
SITE 2 BC1 6 LEU A 238 HOH A2085
SITE 1 BC2 3 LEU A 65 GLY A 138 THR A 139
SITE 1 BC3 4 ARG B 295 ASP B 342 LEU B 345 HOH B2073
SITE 1 BC4 8 ASP B 191 MET B 192 ARG B 239 LEU B 305
SITE 2 BC4 8 CYS B 306 MET B 312 VAL B 313 HOH B2076
SITE 1 BC5 6 TYR A 253 GLY A 254 HOH A2077 HOH A2108
SITE 2 BC5 6 LYS B 259 VAL B 260
SITE 1 BC6 6 ILE B 67 PRO B 68 ALA B 69 ALA B 134
SITE 2 BC6 6 ASP B 135 VAL B 136
CRYST1 100.930 148.910 57.050 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 0.009908 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006715 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017528 0.00000
(ATOM LINES ARE NOT SHOWN.)
END