HEADER OXIDOREDUCTASE 10-MAR-16 5FYZ
TITLE CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN COMPLEX
TITLE 2 WITH 3D FRAGMENT 2-(2-OXO-2,3-DIHYDRO-1H-INDOL-3-YL)ACETONITRILE
TITLE 3 (N10063A)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 5B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: JMJC DOMAIN, RESIDUES 26-101,374-770;
COMPND 5 SYNONYM: CANCER/TESTIS ANTIGEN 31, CT31, HISTONE DEMETHYLASE JARID1B,
COMPND 6 JUMONJI/ARID DOMAIN-CONTAINING PROTEIN 1B, PLU-1, RETINOBLASTOMA-
COMPND 7 BINDING PROTEIN 2 HOMOLOG 1, RBP2-H1;
COMPND 8 EC: 1.14.11.-;
COMPND 9 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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFB-LIC-BSE
KEYWDS OXIDOREDUCTASE, JARID1B, PLU1, PANDDA, FRAGMENT SOAKING, X-RAY
KEYWDS 2 FRAGMENT SCREENING, STRUCTURAL GENOMICS CONSORTIUM, SGC
EXPDTA X-RAY DIFFRACTION
AUTHOR R.NOWAK,T.KROJER,C.JOHANSSON,C.GILEADI,K.KUPINSKA,C.STRAIN-DAMERELL,
AUTHOR 2 A.SZYKOWSKA,N.A.BURGESS-BROWN,C.H.ARROWSMITH,C.BOUNTRA,A.M.EDWARDS,
AUTHOR 3 F.VON DELFT,P.E.BRENNAN,U.OPPERMANN
REVDAT 3 10-JAN-24 5FYZ 1 REMARK LINK
REVDAT 2 24-JAN-18 5FYZ 1 AUTHOR JRNL
REVDAT 1 23-MAR-16 5FYZ 0
JRNL AUTH R.NOWAK,T.KROJER,C.JOHANSSON,C.GILEADI,K.KUPINSKA,
JRNL AUTH 2 C.STRAIN-DAMERELL,A.SZYKOWSKA,F.VON DELFT,N.A.BURGESS-BROWN,
JRNL AUTH 3 C.H.ARROWSMITH,C.BOUNTRA,A.M.EDWARDS,U.OPPERMANN
JRNL TITL CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B
JRNL TITL 2 IN COMPLEX WITH N10063A
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 95.58
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 90821
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4639
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 95.7181 - 5.4374 1.00 3177 157 0.1814 0.1967
REMARK 3 2 5.4374 - 4.3158 1.00 2997 157 0.1501 0.1645
REMARK 3 3 4.3158 - 3.7703 1.00 2942 172 0.1576 0.1997
REMARK 3 4 3.7703 - 3.4255 1.00 2941 138 0.1776 0.2058
REMARK 3 5 3.4255 - 3.1800 1.00 2932 142 0.1951 0.2365
REMARK 3 6 3.1800 - 2.9925 1.00 2900 159 0.2025 0.2256
REMARK 3 7 2.9925 - 2.8426 1.00 2867 164 0.2017 0.2293
REMARK 3 8 2.8426 - 2.7189 1.00 2877 163 0.2088 0.2323
REMARK 3 9 2.7189 - 2.6142 1.00 2883 158 0.2133 0.2650
REMARK 3 10 2.6142 - 2.5240 1.00 2886 143 0.2145 0.2522
REMARK 3 11 2.5240 - 2.4450 1.00 2838 166 0.2156 0.2595
REMARK 3 12 2.4450 - 2.3751 1.00 2884 148 0.2210 0.2631
REMARK 3 13 2.3751 - 2.3126 1.00 2828 172 0.2229 0.2539
REMARK 3 14 2.3126 - 2.2562 1.00 2852 163 0.2274 0.2627
REMARK 3 15 2.2562 - 2.2049 1.00 2859 140 0.2385 0.2471
REMARK 3 16 2.2049 - 2.1580 1.00 2849 156 0.2324 0.2524
REMARK 3 17 2.1580 - 2.1148 1.00 2872 127 0.2351 0.2664
REMARK 3 18 2.1148 - 2.0749 1.00 2864 139 0.2400 0.2700
REMARK 3 19 2.0749 - 2.0378 1.00 2835 150 0.2412 0.3047
REMARK 3 20 2.0378 - 2.0033 1.00 2861 146 0.2444 0.2501
REMARK 3 21 2.0033 - 1.9710 1.00 2824 159 0.2556 0.2818
REMARK 3 22 1.9710 - 1.9406 1.00 2812 161 0.2710 0.2660
REMARK 3 23 1.9406 - 1.9121 1.00 2863 155 0.2688 0.3473
REMARK 3 24 1.9121 - 1.8852 1.00 2796 174 0.2638 0.2853
REMARK 3 25 1.8852 - 1.8597 1.00 2818 168 0.2792 0.3115
REMARK 3 26 1.8597 - 1.8355 1.00 2860 145 0.2866 0.3105
REMARK 3 27 1.8355 - 1.8126 1.00 2807 163 0.2996 0.3788
REMARK 3 28 1.8126 - 1.7907 1.00 2821 166 0.3106 0.3186
REMARK 3 29 1.7907 - 1.7699 1.00 2830 140 0.3236 0.3199
REMARK 3 30 1.7699 - 1.7500 1.00 2807 148 0.3442 0.3655
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.220
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.180
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.44
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 : 0.007 3920
REMARK 3 ANGLE : 1.100 5315
REMARK 3 CHIRALITY : 0.045 561
REMARK 3 PLANARITY : 0.006 682
REMARK 3 DIHEDRAL : 14.730 1435
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: GLYCINE LINKER UNOBSERVED
REMARK 4
REMARK 4 5FYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAR-16.
REMARK 100 THE DEPOSITION ID IS D_1290066412.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91732
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90897
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 122.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.300
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 19.90
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 20.20
REMARK 200 R MERGE FOR SHELL (I) : 1.50000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.300
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 5A3P
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5 -- 0.8M POTASSIUM
REMARK 280 PHOSPHATE DIBASIC -- 0.8M SODIUM PHOSPHATE MONOBASIC
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.38667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 50.69333
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 76.04000
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 25.34667
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 126.73333
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 101.38667
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 50.69333
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 25.34667
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 76.04000
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 126.73333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2299 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 GLY A 102
REMARK 465 GLY A 103
REMARK 465 GLY A 104
REMARK 465 GLY A 105
REMARK 465 ALA A 374
REMARK 465 ARG A 375
REMARK 465 GLY A 443
REMARK 465 LYS A 444
REMARK 465 SER A 754
REMARK 465 TYR A 755
REMARK 465 ASN A 756
REMARK 465 GLU A 757
REMARK 465 TRP A 758
REMARK 465 ALA A 759
REMARK 465 LEU A 760
REMARK 465 ASN A 761
REMARK 465 VAL A 762
REMARK 465 ASN A 763
REMARK 465 GLU A 764
REMARK 465 ALA A 765
REMARK 465 LEU A 766
REMARK 465 GLU A 767
REMARK 465 ALA A 768
REMARK 465 LYS A 769
REMARK 465 ILE A 770
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 40 CG CD OE1 OE2
REMARK 470 LYS A 100 CG CD CE NZ
REMARK 470 LYS A 432 CG CD CE NZ
REMARK 470 GLU A 433 CG CD OE1 OE2
REMARK 470 GLU A 450 CG CD OE1 OE2
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 OD1 ASN A 509 O HOH A 2193 1.85
REMARK 500 O HOH A 2093 O HOH A 2132 2.03
REMARK 500 O HOH A 2246 O HOH A 2311 2.07
REMARK 500 OG SER A 470 O HOH A 2158 2.12
REMARK 500 O MET A 0 O HOH A 2001 2.19
REMARK 500 N ASP A 376 O HOH A 2076 2.19
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 2110 O HOH A 2110 9765 1.97
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 MET A 0 -76.69 54.32
REMARK 500 LEU A 90 78.01 -116.58
REMARK 500 ILE A 479 61.02 -111.50
REMARK 500 PHE A 493 -9.59 78.46
REMARK 500 PHE A 700 -52.24 -152.20
REMARK 500 LYS A 709 77.95 -118.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2208 DISTANCE = 6.15 ANGSTROMS
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 NA A1773 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 91 OD1
REMARK 620 2 LEU A 413 O 131.7
REMARK 620 3 THR A 416 O 139.7 88.6
REMARK 620 4 GLU A 419 O 88.7 107.8 76.6
REMARK 620 5 HOH A2062 O 66.4 82.9 130.3 60.1
REMARK 620 6 HOH A2064 O 72.6 128.5 81.9 118.6 138.9
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN A1757 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 499 NE2
REMARK 620 2 GLU A 501 OE2 94.4
REMARK 620 3 HIS A 587 NE2 89.2 88.5
REMARK 620 4 NYK A1756 N03 95.8 169.5 94.5
REMARK 620 5 HOH A2180 O 89.4 90.4 178.1 86.9
REMARK 620 6 HOH A2187 O 176.9 86.5 93.9 83.2 87.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1754 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 692 SG
REMARK 620 2 CYS A 695 SG 107.7
REMARK 620 3 CYS A 715 SG 116.0 112.4
REMARK 620 4 HIS A 718 ND1 110.7 109.1 100.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A1755 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 706 SG
REMARK 620 2 CYS A 708 SG 126.9
REMARK 620 3 CYS A 723 SG 102.8 115.1
REMARK 620 4 CYS A 725 SG 104.9 91.7 115.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1754
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1755
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NYK A 1756
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 1757
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1758
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1759
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1760
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1761
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1762
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1763
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1764
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1765
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1766
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1767
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1768
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1769
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1770
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1771
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 1772
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1773
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1774
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: 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
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
REMARK 900 RELATED ID: 5FYY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH N05798A
REMARK 900 RELATED ID: 5FZ0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH N11213A
REMARK 900 RELATED ID: 5FZ1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH E48115B
REMARK 900 RELATED ID: 5FZ3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH N08776B
REMARK 900 RELATED ID: 5FZ4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH N10057A
REMARK 900 RELATED ID: 5FZ6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH MAYBRIDGE FRAGMENT N05859B ( LIGAND MODELLED BASED ON
REMARK 900 PANDDA EVENT MAP, SGC - DIAMOND I04-1 FRAGMENT SCREENING)
REMARK 900 RELATED ID: 5FZ7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH MAYBRIDGE FRAGMENT ETHYL 2- AMINO-4-THIOPHEN-2-
REMARK 900 YLTHIOPHENE-3-CARBOXYLATE (N06131B ) (LIGAND MODELLED BASED ON
REMARK 900 PANDDA EVENT MAP, SGC - DIAMOND I04-1 FRAGMENT SCREENING)
REMARK 900 RELATED ID: 5FZ8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH MALATE
REMARK 900 RELATED ID: 5FZ9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH MAYBRIDGE FRAGMENT THIENO(3,2 -B)THIOPHENE-5-
REMARK 900 CARBOXYLIC ACID (N06263B) (LIGAND MODELLED BASED ON PANDDA EVENT
REMARK 900 MAP, SGC - DIAMOND I04 -1 FRAGMENT SCREENING)
REMARK 900 RELATED ID: 5FZA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH 3D FRAGMENT 2-PIPERIDIN-4- YLOXY-5-(TRIFLUOROMETHYL)
REMARK 900 PYRIDINE (N10072A) (LIGAND MODELLED BASED ON PANDDA EVENT MAP)
REMARK 900 RELATED ID: 5FZB RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH MAYBRIDGE FRAGMENT 4- PYRIDYLTHIOUREA (N06275B)
REMARK 900 (LIGAND MODELLED BASED ON PANDDA EVENT MAP, SGC - DIAMOND I04-1
REMARK 900 FRAGMENT SCREENING)
REMARK 900 RELATED ID: 5FZC RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH MAYBRIDGE FRAGMENT 4,5- DIHYDRONAPHTHO(1,2-B)THIOPHENE-
REMARK 900 2-CARBOXYLICACID (N11181A ) (LIGAND MODELLED BASED ON PANDDA EVENT
REMARK 900 MAP, SGC - DIAMOND I04-1 FRAGMENT SCREENING)
REMARK 900 RELATED ID: 5FZD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH L-2-HYDROXYGLUTARATE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES S AND M COME FROM THE EXPRESSION VECTOR. RESIDUES
REMARK 999 102-373 WERE DELETED FROM THE ORIGINAL SEQUENCE Q9UGL1.
REMARK 999 DELETED RESIDUES WERE LINKED WITH 4 GLYCINE LINKER (GGGG).
DBREF 5FYZ A 26 101 UNP Q9UGL1 KDM5B_HUMAN 26 101
DBREF 5FYZ A 374 770 UNP Q9UGL1 KDM5B_HUMAN 374 770
SEQADV 5FYZ SER A -1 UNP Q9UGL1 EXPRESSION TAG
SEQADV 5FYZ MET A 0 UNP Q9UGL1 EXPRESSION TAG
SEQADV 5FYZ GLY A 102 UNP Q9UGL1 LINKER
SEQADV 5FYZ GLY A 103 UNP Q9UGL1 LINKER
SEQADV 5FYZ GLY A 104 UNP Q9UGL1 LINKER
SEQADV 5FYZ GLY A 105 UNP Q9UGL1 LINKER
SEQRES 1 A 479 SER MET PHE LEU PRO PRO PRO GLU CYS PRO VAL PHE GLU
SEQRES 2 A 479 PRO SER TRP GLU GLU PHE ALA ASP PRO PHE ALA PHE ILE
SEQRES 3 A 479 HIS LYS ILE ARG PRO ILE ALA GLU GLN THR GLY ILE CYS
SEQRES 4 A 479 LYS VAL ARG PRO PRO PRO ASP TRP GLN PRO PRO PHE ALA
SEQRES 5 A 479 CYS ASP VAL ASP LYS LEU HIS PHE THR PRO ARG ILE GLN
SEQRES 6 A 479 ARG LEU ASN GLU LEU GLU ALA GLN THR ARG VAL LYS LEU
SEQRES 7 A 479 GLY GLY GLY GLY ALA ARG ASP TYR THR LEU ARG THR PHE
SEQRES 8 A 479 GLY GLU MET ALA ASP ALA PHE LYS SER ASP TYR PHE ASN
SEQRES 9 A 479 MET PRO VAL HIS MET VAL PRO THR GLU LEU VAL GLU LYS
SEQRES 10 A 479 GLU PHE TRP ARG LEU VAL SER THR ILE GLU GLU ASP VAL
SEQRES 11 A 479 THR VAL GLU TYR GLY ALA ASP ILE ALA SER LYS GLU PHE
SEQRES 12 A 479 GLY SER GLY PHE PRO VAL ARG ASP GLY LYS ILE LYS LEU
SEQRES 13 A 479 SER PRO GLU GLU GLU GLU TYR LEU ASP SER GLY TRP ASN
SEQRES 14 A 479 LEU ASN ASN MET PRO VAL MET GLU GLN SER VAL LEU ALA
SEQRES 15 A 479 HIS ILE THR ALA ASP ILE CYS GLY MET LYS LEU PRO TRP
SEQRES 16 A 479 LEU TYR VAL GLY MET CYS PHE SER SER PHE CYS TRP HIS
SEQRES 17 A 479 ILE GLU ASP HIS TRP SER TYR SER ILE ASN TYR LEU HIS
SEQRES 18 A 479 TRP GLY GLU PRO LYS THR TRP TYR GLY VAL PRO GLY TYR
SEQRES 19 A 479 ALA ALA GLU GLN LEU GLU ASN VAL MET LYS LYS LEU ALA
SEQRES 20 A 479 PRO GLU LEU PHE VAL SER GLN PRO ASP LEU LEU HIS GLN
SEQRES 21 A 479 LEU VAL THR ILE MET ASN PRO ASN THR LEU MET THR HIS
SEQRES 22 A 479 GLU VAL PRO VAL TYR ARG THR ASN GLN CYS ALA GLY GLU
SEQRES 23 A 479 PHE VAL ILE THR PHE PRO ARG ALA TYR HIS SER GLY PHE
SEQRES 24 A 479 ASN GLN GLY PHE ASN PHE ALA GLU ALA VAL ASN PHE CYS
SEQRES 25 A 479 THR VAL ASP TRP LEU PRO LEU GLY ARG GLN CYS VAL GLU
SEQRES 26 A 479 HIS TYR ARG LEU LEU HIS ARG TYR CYS VAL PHE SER HIS
SEQRES 27 A 479 ASP GLU MET ILE CYS LYS MET ALA SER LYS ALA ASP VAL
SEQRES 28 A 479 LEU ASP VAL VAL VAL ALA SER THR VAL GLN LYS ASP MET
SEQRES 29 A 479 ALA ILE MET ILE GLU ASP GLU LYS ALA LEU ARG GLU THR
SEQRES 30 A 479 VAL ARG LYS LEU GLY VAL ILE ASP SER GLU ARG MET ASP
SEQRES 31 A 479 PHE GLU LEU LEU PRO ASP ASP GLU ARG GLN CYS VAL LYS
SEQRES 32 A 479 CYS LYS THR THR CYS PHE MET SER ALA ILE SER CYS SER
SEQRES 33 A 479 CYS LYS PRO GLY LEU LEU VAL CYS LEU HIS HIS VAL LYS
SEQRES 34 A 479 GLU LEU CYS SER CYS PRO PRO TYR LYS TYR LYS LEU ARG
SEQRES 35 A 479 TYR ARG TYR THR LEU ASP ASP LEU TYR PRO MET MET ASN
SEQRES 36 A 479 ALA LEU LYS LEU ARG ALA GLU SER TYR ASN GLU TRP ALA
SEQRES 37 A 479 LEU ASN VAL ASN GLU ALA LEU GLU ALA LYS ILE
HET ZN A1754 1
HET ZN A1755 1
HET NYK A1756 13
HET MN A1757 1
HET PO4 A1758 5
HET EDO A1759 4
HET EDO A1760 4
HET EDO A1761 4
HET EDO A1762 4
HET EDO A1763 4
HET EDO A1764 4
HET EDO A1765 4
HET EDO A1766 4
HET EDO A1767 4
HET EDO A1768 4
HET EDO A1769 4
HET DMS A1770 4
HET DMS A1771 4
HET DMS A1772 4
HET NA A1773 1
HET EDO A1774 4
HETNAM ZN ZINC ION
HETNAM NYK [(3S)-2-OXO-2,3-DIHYDRO-1H-INDOL-3-YL]ACETONITRILE
HETNAM MN MANGANESE (II) ION
HETNAM PO4 PHOSPHATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM DMS DIMETHYL SULFOXIDE
HETNAM NA SODIUM ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 ZN 2(ZN 2+)
FORMUL 4 NYK C10 H8 N2 O
FORMUL 5 MN MN 2+
FORMUL 6 PO4 O4 P 3-
FORMUL 7 EDO 12(C2 H6 O2)
FORMUL 18 DMS 3(C2 H6 O S)
FORMUL 21 NA NA 1+
FORMUL 23 HOH *344(H2 O)
HELIX 1 1 SER A 38 ALA A 43 1 6
HELIX 2 2 ASP A 44 GLU A 57 1 14
HELIX 3 3 LEU A 379 ASN A 395 1 17
HELIX 4 4 PRO A 397 VAL A 401 5 5
HELIX 5 5 PRO A 402 THR A 416 1 15
HELIX 6 6 SER A 448 LEU A 455 1 8
HELIX 7 7 VAL A 471 ILE A 475 5 5
HELIX 8 8 ILE A 479 LEU A 484 1 6
HELIX 9 9 GLU A 501 SER A 505 5 5
HELIX 10 10 PRO A 523 TYR A 525 5 3
HELIX 11 11 ALA A 526 ALA A 538 1 13
HELIX 12 12 PRO A 539 VAL A 543 5 5
HELIX 13 13 ASP A 547 HIS A 550 5 4
HELIX 14 14 ASN A 557 HIS A 564 1 8
HELIX 15 15 THR A 604 ASP A 606 5 3
HELIX 16 16 TRP A 607 HIS A 622 1 16
HELIX 17 17 SER A 628 SER A 638 1 11
HELIX 18 18 LYS A 639 LEU A 643 5 5
HELIX 19 19 ASP A 644 LEU A 672 1 29
HELIX 20 20 ASP A 681 LEU A 685 5 5
HELIX 21 21 PRO A 686 ARG A 690 5 5
HELIX 22 22 HIS A 718 LEU A 722 5 5
HELIX 23 23 PRO A 726 TYR A 728 5 3
HELIX 24 24 THR A 737 GLU A 753 1 17
SHEET 1 AA 8 VAL A 34 PHE A 35 0
SHEET 2 AA 8 ILE A 61 VAL A 64 1 O LYS A 63 N PHE A 35
SHEET 3 AA 8 PHE A 578 THR A 581 -1 O PHE A 578 N VAL A 64
SHEET 4 AA 8 TYR A 506 GLY A 514 -1 O SER A 507 N THR A 581
SHEET 5 AA 8 ASN A 595 PHE A 602 -1 O PHE A 596 N HIS A 512
SHEET 6 AA 8 TRP A 486 GLY A 490 -1 O TRP A 486 N ALA A 599
SHEET 7 AA 8 THR A 422 ILE A 429 -1 O GLY A 426 N VAL A 489
SHEET 8 AA 8 ARG A 86 ARG A 89 -1 O ARG A 86 N TYR A 425
SHEET 1 AB 2 HIS A 82 PHE A 83 0
SHEET 2 AB 2 TYR A 377 THR A 378 -1 O TYR A 377 N PHE A 83
SHEET 1 AC 2 GLN A 96 THR A 97 0
SHEET 2 AC 2 LEU A 552 VAL A 553 -1 O VAL A 553 N GLN A 96
SHEET 1 AD 4 SER A 495 HIS A 499 0
SHEET 2 AD 4 HIS A 587 ASN A 591 -1 O HIS A 587 N HIS A 499
SHEET 3 AD 4 LYS A 517 GLY A 521 -1 O THR A 518 N PHE A 590
SHEET 4 AD 4 TYR A 569 GLN A 573 -1 O TYR A 569 N GLY A 521
SHEET 1 AE 3 ASP A 676 ARG A 679 0
SHEET 2 AE 3 TYR A 730 TYR A 734 1 O TYR A 730 N ASP A 676
SHEET 3 AE 3 SER A 702 CYS A 706 -1 O ALA A 703 N ARG A 733
LINK OD1 ASN A 91 NA NA A1773 1555 1555 2.65
LINK O LEU A 413 NA NA A1773 1555 1555 2.75
LINK O THR A 416 NA NA A1773 1555 1555 2.41
LINK O GLU A 419 NA NA A1773 1555 1555 3.12
LINK NE2 HIS A 499 MN MN A1757 1555 1555 2.09
LINK OE2 GLU A 501 MN MN A1757 1555 1555 2.08
LINK NE2 HIS A 587 MN MN A1757 1555 1555 2.17
LINK SG CYS A 692 ZN ZN A1754 1555 1555 2.13
LINK SG CYS A 695 ZN ZN A1754 1555 1555 2.36
LINK SG CYS A 706 ZN ZN A1755 1555 1555 2.61
LINK SG CYS A 708 ZN ZN A1755 1555 1555 2.65
LINK SG CYS A 715 ZN ZN A1754 1555 1555 2.28
LINK ND1 HIS A 718 ZN ZN A1754 1555 1555 2.13
LINK SG CYS A 723 ZN ZN A1755 1555 1555 2.37
LINK SG CYS A 725 ZN ZN A1755 1555 1555 2.74
LINK N03 NYK A1756 MN MN A1757 1555 1555 2.21
LINK MN MN A1757 O HOH A2180 1555 1555 2.05
LINK MN MN A1757 O HOH A2187 1555 1555 2.24
LINK NA NA A1773 O HOH A2062 1555 1555 2.14
LINK NA NA A1773 O HOH A2064 1555 1555 2.82
SITE 1 AC1 4 CYS A 692 CYS A 695 CYS A 715 HIS A 718
SITE 1 AC2 4 CYS A 706 CYS A 708 CYS A 723 CYS A 725
SITE 1 AC3 11 TYR A 488 PHE A 496 HIS A 499 LYS A 517
SITE 2 AC3 11 HIS A 587 MN A1757 DMS A1770 HOH A2180
SITE 3 AC3 11 HOH A2187 HOH A2193 HOH A2203
SITE 1 AC4 6 HIS A 499 GLU A 501 HIS A 587 NYK A1756
SITE 2 AC4 6 HOH A2180 HOH A2187
SITE 1 AC5 5 HIS A 622 LYS A 694 HIS A 718 HOH A2245
SITE 2 AC5 5 HOH A2250
SITE 1 AC6 6 ASP A 630 CYS A 699 PHE A 700 MET A 701
SITE 2 AC6 6 SER A 702 HOH A2262
SITE 1 AC7 7 PHE A 83 GLY A 426 ALA A 427 LEU A 487
SITE 2 AC7 7 TYR A 488 VAL A 489 HOH A2128
SITE 1 AC8 3 ARG A 666 THR A 737 HOH A2340
SITE 1 AC9 6 ARG A 612 ASP A 630 MET A 658 GLU A 662
SITE 2 AC9 6 LEU A 665 HOH A2239
SITE 1 BC1 2 PRO A 30 VAL A 568
SITE 1 BC2 9 ASP A 688 GLU A 689 ARG A 690 GLN A 691
SITE 2 BC2 9 VAL A 693 GLY A 711 LEU A 712 LEU A 713
SITE 3 BC2 9 HOH A2342
SITE 1 BC3 4 GLY A 524 ARG A 584 HOH A2206 HOH A2343
SITE 1 BC4 5 ARG A 670 VAL A 674 ILE A 675 HOH A2121
SITE 2 BC4 5 HOH A2281
SITE 1 BC5 2 HIS A 564 GLU A 565
SITE 1 BC6 4 LYS A 80 LYS A 720 CYS A 723 HOH A2325
SITE 1 BC7 5 CYS A 634 LYS A 635 GLU A 683 ARG A 735
SITE 2 BC7 5 TYR A 736
SITE 1 BC8 8 GLN A 88 GLN A 96 THR A 97 TYR A 425
SITE 2 BC8 8 SER A 495 PHE A 496 CYS A 497 NYK A1756
SITE 1 BC9 6 TRP A 486 TYR A 488 SER A 507 VAL A 600
SITE 2 BC9 6 ASN A 601 HOH A2193
SITE 1 CC1 6 ILE A 500 TRP A 504 HIS A 617 LEU A 621
SITE 2 CC1 6 ARG A 623 HOH A2186
SITE 1 CC2 7 LEU A 90 ASN A 91 LEU A 413 THR A 416
SITE 2 CC2 7 GLU A 419 HOH A2062 HOH A2064
SITE 1 CC3 1 HOH A2344
CRYST1 141.880 141.880 152.080 90.00 90.00 120.00 P 65 2 2 12
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 0.007048 0.004069 0.000000 0.00000
SCALE2 0.000000 0.008139 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006575 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
